Browse entries in the PDBbind-CN Database
HEADER RNA BINDING PROTEIN/RNA 01-NOV-12 4HT9 TITLE CRYSTAL STRUCTURE OF E COLI HFQ BOUND TO TWO RNAS COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN HFQ; COMPND 3 CHAIN: A, B, C; COMPND 4 FRAGMENT: SM FOLD; COMPND 5 SYNONYM: HF-1, HOST FACTOR-I PROTEIN; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: RNA (5'-R(*AP*AP*AP*AP*AP*AP*A)-3'); COMPND 9 CHAIN: D; COMPND 10 ENGINEERED: YES; COMPND 11 OTHER_DETAILS: A7 RNA; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: RNA (5'-R(*AP*UP*UP*UP*UP*UP*UP*A)-3'); COMPND 14 CHAIN: E; COMPND 15 ENGINEERED: YES; COMPND 16 OTHER_DETAILS: AU6A RNA SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 469008; SOURCE 4 STRAIN: B / BL21-DE3; SOURCE 5 GENE: B21_04001, ECBD_3862, ECD_04039, HFQ; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A; SOURCE 11 MOL_ID: 2; SOURCE 12 SYNTHETIC: YES; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN E. COLI; SOURCE 16 MOL_ID: 3; SOURCE 17 SYNTHETIC: YES; SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 19 ORGANISM_TAXID: 9606; SOURCE 20 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN E. COLI KEYWDS HFQ, DSRA, RPOS, SM FOLD, RNA CHAPERONE, SINGLE STRANDED RNA, KEYWDS 2 CYTOPLASMIC, RNA BINDING PROTEIN-RNA COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR W.W.WANG,L.J.WANG REVDAT 3 26-JUN-13 4HT9 1 JRNL REVDAT 2 19-JUN-13 4HT9 1 JRNL REVDAT 1 17-APR-13 4HT9 0 JRNL AUTH W.WANG,L.WANG,J.WU,Q.GONG,Y.SHI JRNL TITL HFQ-BRIDGED TERNARY COMPLEX IS IMPORTANT FOR TRANSLATION JRNL TITL 2 ACTIVATION OF RPOS BY DSRA. JRNL REF NUCLEIC ACIDS RES. V. 41 5938 2013 JRNL REFN ISSN 0305-1048 JRNL PMID 23605038 JRNL DOI 10.1093/NAR/GKT276 REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.7.0029 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.31 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3 REMARK 3 NUMBER OF REFLECTIONS : 16985 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) : 0.186 REMARK 3 R VALUE (WORKING SET) : 0.184 REMARK 3 FREE R VALUE : 0.221 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 916 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) : 1247 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.88 REMARK 3 BIN R VALUE (WORKING SET) : 0.2120 REMARK 3 BIN FREE R VALUE SET COUNT : 79 REMARK 3 BIN FREE R VALUE : 0.2700 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1440 REMARK 3 NUCLEIC ACID ATOMS : 191 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 162 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.22 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.94000 REMARK 3 B22 (A**2) : 1.88000 REMARK 3 B33 (A**2) : -0.94000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -1.15000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.148 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.134 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.086 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.921 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1734 ; 0.009 ; 0.018 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2396 ; 1.431 ; 1.878 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 193 ; 6.044 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 66 ;31.904 ;23.636 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 280 ;15.624 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;20.217 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 284 ; 0.095 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1212 ; 0.008 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 937 ; 0.602 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1542 ; 1.135 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 797 ; 1.620 ; 3.000 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 848 ; 2.612 ; 4.500 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 4 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 6 A 65 REMARK 3 ORIGIN FOR THE GROUP (A): 13.6010 0.2599 9.5822 REMARK 3 T TENSOR REMARK 3 T11: 0.0328 T22: 0.0141 REMARK 3 T33: 0.0638 T12: 0.0014 REMARK 3 T13: 0.0131 T23: 0.0186 REMARK 3 L TENSOR REMARK 3 L11: 1.3864 L22: 0.4093 REMARK 3 L33: 2.7118 L12: 0.0814 REMARK 3 L13: -0.2231 L23: -0.2958 REMARK 3 S TENSOR REMARK 3 S11: 0.0612 S12: -0.0008 S13: 0.0174 REMARK 3 S21: -0.0101 S22: 0.0362 S23: 0.0353 REMARK 3 S31: 0.0521 S32: -0.1687 S33: -0.0975 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 4 B 65 REMARK 3 ORIGIN FOR THE GROUP (A): 29.9390 -0.3982 18.7951 REMARK 3 T TENSOR REMARK 3 T11: 0.0462 T22: 0.0107 REMARK 3 T33: 0.0544 T12: 0.0069 REMARK 3 T13: 0.0076 T23: 0.0074 REMARK 3 L TENSOR REMARK 3 L11: 2.0131 L22: 1.1534 REMARK 3 L33: 1.9452 L12: -0.6113 REMARK 3 L13: 0.4406 L23: -0.5373 REMARK 3 S TENSOR REMARK 3 S11: 0.0229 S12: -0.1087 S13: -0.1040 REMARK 3 S21: 0.1015 S22: 0.0207 S23: 0.0018 REMARK 3 S31: 0.0267 S32: 0.0555 S33: -0.0435 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 6 C 65 REMARK 3 ORIGIN FOR THE GROUP (A): 13.9433 0.0980 -9.6228 REMARK 3 T TENSOR REMARK 3 T11: 0.0094 T22: 0.0775 REMARK 3 T33: 0.0360 T12: -0.0186 REMARK 3 T13: -0.0090 T23: 0.0352 REMARK 3 L TENSOR REMARK 3 L11: 2.4295 L22: 0.9631 REMARK 3 L33: 2.1951 L12: 0.2461 REMARK 3 L13: -0.1099 L23: -0.0881 REMARK 3 S TENSOR REMARK 3 S11: -0.0526 S12: 0.2621 S13: 0.0262 REMARK 3 S21: -0.0017 S22: 0.1553 S23: 0.0383 REMARK 3 S31: 0.0751 S32: -0.2138 S33: -0.1027 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : D 1 D 7 REMARK 3 ORIGIN FOR THE GROUP (A): 23.0954 14.2697 9.1037 REMARK 3 T TENSOR REMARK 3 T11: 0.1621 T22: 0.0625 REMARK 3 T33: 0.1861 T12: -0.0023 REMARK 3 T13: 0.0836 T23: 0.0708 REMARK 3 L TENSOR REMARK 3 L11: 4.1979 L22: 0.7739 REMARK 3 L33: 2.6628 L12: -1.0157 REMARK 3 L13: 2.7030 L23: -0.0297 REMARK 3 S TENSOR REMARK 3 S11: -0.1580 S12: 0.1570 S13: 0.4992 REMARK 3 S21: -0.1835 S22: 0.0631 S23: -0.1922 REMARK 3 S31: -0.4661 S32: 0.1345 S33: 0.0949 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN REMARK 3 THE INPUT REMARK 4 REMARK 4 4HT9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-NOV-12. REMARK 100 THE RCSB ID CODE IS RCSB075892. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-MAR-11 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.2 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRF REMARK 200 BEAMLINE : BL17U REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793 REMARK 200 MONOCHROMATOR : PLANE GRATING REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17910 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 REMARK 200 RESOLUTION RANGE LOW (A) : 49.244 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6 REMARK 200 DATA REDUNDANCY : 6.500 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.05700 REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.5000 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) : 1.90 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0 REMARK 200 DATA REDUNDANCY IN SHELL : 6.60 REMARK 200 R MERGE FOR SHELL (I) : 0.26800 REMARK 200 R SYM FOR SHELL (I) : 0.26800 REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRY 1HK9 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 33.02 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.84 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM NACL, 100 MM CACODYLATE, 12% REMARK 280 PEG 8000, PH 6.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 283K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z+1/2 REMARK 290 4555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 30.29500 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 19.14000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 42.26000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 30.29500 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 19.14000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 42.26000 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: DECAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 10150 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 16190 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -85.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 60.59000 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 1 REMARK 465 ALA A 2 REMARK 465 LYS A 3 REMARK 465 GLY A 4 REMARK 465 GLN A 5 REMARK 465 MET B 1 REMARK 465 ALA B 2 REMARK 465 LYS B 3 REMARK 465 MET C 1 REMARK 465 ALA C 2 REMARK 465 LYS C 3 REMARK 465 GLY C 4 REMARK 465 GLN C 5 REMARK 465 A E 3 REMARK 465 U E 6 REMARK 465 U E 7 REMARK 465 U E 8 REMARK 465 U E 9 REMARK 465 A E 10 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 THR A 49 OG1 CG2 REMARK 470 GLN B 5 CB CG CD OE1 NE2 REMARK 470 GLN B 41 CD OE1 NE2 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 ASP A 40 -158.89 -137.63 REMARK 500 ASN A 48 -109.42 -133.30 REMARK 500 THR B 49 -52.73 54.13 REMARK 500 ASP C 40 -158.71 -139.82 REMARK 500 ASN C 48 -120.82 -129.57 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH E 109 DISTANCE = 5.51 ANGSTROMS DBREF 4HT9 A 1 65 UNP C6ECV6 C6ECV6_ECOBD 1 65 DBREF 4HT9 B 1 65 UNP C6ECV6 C6ECV6_ECOBD 1 65 DBREF 4HT9 C 1 65 UNP C6ECV6 C6ECV6_ECOBD 1 65 DBREF 4HT9 D 1 7 PDB 4HT9 4HT9 1 7 DBREF 4HT9 E 3 10 PDB 4HT9 4HT9 3 10 SEQRES 1 A 65 MET ALA LYS GLY GLN SER LEU GLN ASP PRO PHE LEU ASN SEQRES 2 A 65 ALA LEU ARG ARG GLU ARG VAL PRO VAL SER ILE TYR LEU SEQRES 3 A 65 VAL ASN GLY ILE LYS LEU GLN GLY GLN ILE GLU SER PHE SEQRES 4 A 65 ASP GLN PHE VAL ILE LEU LEU LYS ASN THR VAL SER GLN SEQRES 5 A 65 MET VAL TYR LYS HIS ALA ILE SER THR VAL VAL PRO SER SEQRES 1 B 65 MET ALA LYS GLY GLN SER LEU GLN ASP PRO PHE LEU ASN SEQRES 2 B 65 ALA LEU ARG ARG GLU ARG VAL PRO VAL SER ILE TYR LEU SEQRES 3 B 65 VAL ASN GLY ILE LYS LEU GLN GLY GLN ILE GLU SER PHE SEQRES 4 B 65 ASP GLN PHE VAL ILE LEU LEU LYS ASN THR VAL SER GLN SEQRES 5 B 65 MET VAL TYR LYS HIS ALA ILE SER THR VAL VAL PRO SER SEQRES 1 C 65 MET ALA LYS GLY GLN SER LEU GLN ASP PRO PHE LEU ASN SEQRES 2 C 65 ALA LEU ARG ARG GLU ARG VAL PRO VAL SER ILE TYR LEU SEQRES 3 C 65 VAL ASN GLY ILE LYS LEU GLN GLY GLN ILE GLU SER PHE SEQRES 4 C 65 ASP GLN PHE VAL ILE LEU LEU LYS ASN THR VAL SER GLN SEQRES 5 C 65 MET VAL TYR LYS HIS ALA ILE SER THR VAL VAL PRO SER SEQRES 1 D 7 A A A A A A A SEQRES 1 E 8 A U U U U U U A FORMUL 6 HOH *162(H2 O) HELIX 1 1 LEU A 7 GLU A 18 1 12 HELIX 2 2 LEU B 7 GLU B 18 1 12 HELIX 3 3 LEU C 7 GLU C 18 1 12 SHEET 1 A15 ILE B 59 PRO B 64 0 SHEET 2 A15 PRO B 21 LEU B 26 -1 N SER B 23 O VAL B 63 SHEET 3 A15 LYS B 31 PHE B 39 -1 O GLY B 34 N VAL B 22 SHEET 4 A15 VAL B 43 LYS B 47 -1 O LEU B 45 N SER B 38 SHEET 5 A15 SER B 51 TYR B 55 -1 O GLN B 52 N LEU B 46 SHEET 6 A15 ILE A 59 PRO A 64 -1 N SER A 60 O TYR B 55 SHEET 7 A15 PRO A 21 LEU A 26 -1 N TYR A 25 O SER A 60 SHEET 8 A15 LYS A 31 PHE A 39 -1 O GLY A 34 N VAL A 22 SHEET 9 A15 VAL A 43 LYS A 47 -1 O LYS A 47 N GLN A 35 SHEET 10 A15 SER A 51 TYR A 55 -1 O VAL A 54 N ILE A 44 SHEET 11 A15 ILE C 59 PRO C 64 -1 O SER C 60 N TYR A 55 SHEET 12 A15 VAL C 22 LEU C 26 -1 N TYR C 25 O SER C 60 SHEET 13 A15 LYS C 31 PHE C 39 -1 O LEU C 32 N ILE C 24 SHEET 14 A15 VAL C 43 LYS C 47 -1 O LEU C 45 N GLU C 37 SHEET 15 A15 SER C 51 TYR C 55 -1 O VAL C 54 N ILE C 44 CRYST1 60.590 38.280 84.520 90.00 90.00 90.00 I 1 2 1 12 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 0.016504 0.000000 0.000000 0.00000 SCALE2 0.000000 0.026123 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011832 0.00000 ATOM 1 N SER A 6 21.546 -12.311 13.804 1.00 38.59 N ANISOU 1 N SER A 6 5544 4087 5030 524 -35 347 N ATOM 2 CA SER A 6 21.198 -12.742 15.189 1.00 37.02 C ANISOU 2 CA SER A 6 5367 3881 4819 495 -48 431 C ATOM 3 C SER A 6 20.524 -11.655 16.048 1.00 34.63 C ANISOU 3 C SER A 6 4941 3702 4514 381 -51 442 C ATOM 4 O SER A 6 19.558 -11.947 16.764 1.00 33.37 O ANISOU 4 O SER A 6 4814 3514 4352 286 -61 489 O ATOM 5 CB SER A 6 22.422 -13.320 15.893 1.00 39.88 C ANISOU 5 CB SER A 6 5734 4273 5145 655 -48 490 C ATOM 6 OG SER A 6 22.031 -13.940 17.093 1.00 42.75 O ANISOU 6 OG SER A 6 6149 4603 5493 630 -62 580 O ATOM 7 N LEU A 7 21.016 -10.412 15.963 1.00 30.47 N ANISOU 7 N LEU A 7 4283 3311 3985 387 -39 398 N ATOM 8 CA LEU A 7 20.430 -9.284 16.711 1.00 28.05 C ANISOU 8 CA LEU A 7 3874 3111 3675 292 -34 392 C ATOM 9 C LEU A 7 19.589 -8.352 15.847 1.00 24.55 C ANISOU 9 C LEU A 7 3394 2670 3263 207 -22 333 C ATOM 10 O LEU A 7 18.680 -7.698 16.341 1.00 22.66 O ANISOU 10 O LEU A 7 3110 2475 3025 125 -16 334 O ATOM 11 CB LEU A 7 21.511 -8.455 17.408 1.00 28.31 C ANISOU 11 CB LEU A 7 3793 3290 3674 340 -29 385 C ATOM 12 CG LEU A 7 22.387 -9.136 18.445 1.00 30.85 C ANISOU 12 CG LEU A 7 4108 3665 3946 427 -43 452 C ATOM 13 CD1 LEU A 7 23.503 -8.174 18.828 1.00 32.02 C ANISOU 13 CD1 LEU A 7 4128 3982 4055 455 -38 425 C ATOM 14 CD2 LEU A 7 21.591 -9.578 19.661 1.00 31.62 C ANISOU 14 CD2 LEU A 7 4236 3756 4024 372 -54 520 C ATOM 15 N GLN A 8 19.895 -8.306 14.562 1.00 23.83 N ANISOU 15 N GLN A 8 3323 2543 3191 237 -16 285 N ATOM 16 CA GLN A 8 19.230 -7.432 13.611 1.00 22.87 C ANISOU 16 CA GLN A 8 3166 2431 3092 175 -4 238 C ATOM 17 C GLN A 8 17.727 -7.687 13.512 1.00 22.08 C ANISOU 17 C GLN A 8 3101 2285 3001 74 -13 252 C ATOM 18 O GLN A 8 16.919 -6.760 13.614 1.00 20.45 O ANISOU 18 O GLN A 8 2832 2138 2802 15 -2 246 O ATOM 19 CB GLN A 8 19.845 -7.655 12.242 1.00 23.81 C ANISOU 19 CB GLN A 8 3317 2514 3217 232 0 195 C ATOM 20 CG GLN A 8 19.867 -6.448 11.371 1.00 21.97 C ANISOU 20 CG GLN A 8 3013 2341 2995 210 19 153 C ATOM 21 CD GLN A 8 20.378 -6.734 9.980 1.00 21.32 C ANISOU 21 CD GLN A 8 2961 2233 2907 259 24 114 C ATOM 22 OE1 GLN A 8 19.881 -6.151 9.030 1.00 19.54 O ANISOU 22 OE1 GLN A 8 2718 2018 2689 218 31 89 O ATOM 23 NE2 GLN A 8 21.362 -7.629 9.849 1.00 22.25 N ANISOU 23 NE2 GLN A 8 3123 2326 3004 356 22 110 N ATOM 24 N ASP A 9 17.358 -8.942 13.273 1.00 21.27 N ANISOU 24 N ASP A 9 3104 2081 2895 54 -32 271 N ATOM 25 CA ASP A 9 15.968 -9.295 13.059 1.00 21.88 C ANISOU 25 CA ASP A 9 3215 2127 2971 -62 -44 284 C ATOM 26 C ASP A 9 15.116 -9.035 14.300 1.00 20.44 C ANISOU 26 C ASP A 9 2979 2012 2774 -132 -43 336 C ATOM 27 O ASP A 9 14.063 -8.410 14.184 1.00 19.49 O ANISOU 27 O ASP A 9 2795 1959 2650 -204 -38 334 O ATOM 28 CB ASP A 9 15.823 -10.756 12.586 1.00 25.37 C ANISOU 28 CB ASP A 9 3803 2431 3406 -87 -64 289 C ATOM 29 CG ASP A 9 16.415 -10.982 11.216 1.00 28.80 C ANISOU 29 CG ASP A 9 4291 2808 3844 -30 -61 224 C ATOM 30 OD1 ASP A 9 16.859 -10.006 10.582 1.00 28.64 O ANISOU 30 OD1 ASP A 9 4185 2866 3831 17 -46 185 O ATOM 31 OD2 ASP A 9 16.436 -12.141 10.755 1.00 31.94 O ANISOU 31 OD2 ASP A 9 4823 3079 4233 -34 -72 211 O ATOM 32 N PRO A 10 15.556 -9.505 15.485 1.00 20.36 N ANISOU 32 N PRO A 10 2989 1999 2748 -104 -46 387 N ATOM 33 CA PRO A 10 14.707 -9.183 16.646 1.00 19.28 C ANISOU 33 CA PRO A 10 2791 1947 2588 -173 -41 432 C ATOM 34 C PRO A 10 14.588 -7.655 16.920 1.00 17.67 C ANISOU 34 C PRO A 10 2462 1866 2384 -158 -15 395 C ATOM 35 O PRO A 10 13.543 -7.197 17.384 1.00 16.50 O ANISOU 35 O PRO A 10 2257 1794 2219 -219 -4 410 O ATOM 36 CB PRO A 10 15.409 -9.889 17.815 1.00 20.32 C ANISOU 36 CB PRO A 10 2962 2064 2696 -126 -49 492 C ATOM 37 CG PRO A 10 16.281 -10.929 17.214 1.00 20.85 C ANISOU 37 CG PRO A 10 3143 2004 2775 -52 -62 494 C ATOM 38 CD PRO A 10 16.582 -10.525 15.805 1.00 20.86 C ANISOU 38 CD PRO A 10 3141 1980 2804 -19 -56 417 C ATOM 39 N PHE A 11 15.652 -6.895 16.663 1.00 16.00 N ANISOU 39 N PHE A 11 2215 1677 2186 -79 -3 349 N ATOM 40 CA PHE A 11 15.630 -5.438 16.895 1.00 15.46 C ANISOU 40 CA PHE A 11 2059 1697 2120 -70 25 308 C ATOM 41 C PHE A 11 14.578 -4.759 16.007 1.00 14.37 C ANISOU 41 C PHE A 11 1891 1569 1999 -106 39 286 C ATOM 42 O PHE A 11 13.724 -4.020 16.507 1.00 14.35 O ANISOU 42 O PHE A 11 1835 1635 1984 -129 60 288 O ATOM 43 CB PHE A 11 17.023 -4.857 16.635 1.00 14.99 C ANISOU 43 CB PHE A 11 1979 1650 2068 -1 33 266 C ATOM 44 CG PHE A 11 17.114 -3.372 16.863 1.00 15.07 C ANISOU 44 CG PHE A 11 1923 1724 2077 -6 63 220 C ATOM 45 CD1 PHE A 11 16.761 -2.471 15.858 1.00 14.99 C ANISOU 45 CD1 PHE A 11 1901 1698 2096 -10 83 186 C ATOM 46 CD2 PHE A 11 17.564 -2.881 18.100 1.00 15.83 C ANISOU 46 CD2 PHE A 11 1981 1894 2140 -7 73 212 C ATOM 47 CE1 PHE A 11 16.863 -1.074 16.092 1.00 14.84 C ANISOU 47 CE1 PHE A 11 1848 1713 2079 -12 116 145 C ATOM 48 CE2 PHE A 11 17.643 -1.504 18.340 1.00 15.80 C ANISOU 48 CE2 PHE A 11 1940 1930 2132 -21 104 159 C ATOM 49 CZ PHE A 11 17.293 -0.604 17.328 1.00 14.77 C ANISOU 49 CZ PHE A 11 1814 1759 2038 -21 127 126 C ATOM 50 N LEU A 12 14.629 -5.043 14.706 1.00 14.08 N ANISOU 50 N LEU A 12 1890 1476 1984 -103 28 268 N ATOM 51 CA LEU A 12 13.653 -4.533 13.723 1.00 14.66 C ANISOU 51 CA LEU A 12 1935 1571 2064 -134 34 257 C ATOM 52 C LEU A 12 12.216 -5.004 13.988 1.00 15.48 C ANISOU 52 C LEU A 12 2023 1717 2142 -217 24 299 C ATOM 53 O LEU A 12 11.246 -4.227 13.919 1.00 16.08 O ANISOU 53 O LEU A 12 2030 1873 2207 -228 41 306 O ATOM 54 CB LEU A 12 14.099 -4.906 12.301 1.00 14.47 C ANISOU 54 CB LEU A 12 1957 1488 2055 -118 21 228 C ATOM 55 CG LEU A 12 15.404 -4.262 11.799 1.00 13.86 C ANISOU 55 CG LEU A 12 1872 1401 1995 -43 36 190 C ATOM 56 CD1 LEU A 12 15.896 -4.820 10.462 1.00 14.76 C ANISOU 56 CD1 LEU A 12 2033 1465 2110 -21 24 163 C ATOM 57 CD2 LEU A 12 15.271 -2.731 11.718 1.00 13.52 C ANISOU 57 CD2 LEU A 12 1763 1410 1963 -27 69 175 C ATOM 58 N ASN A 13 12.081 -6.289 14.300 1.00 16.03 N ANISOU 58 N ASN A 13 2158 1736 2197 -274 -3 332 N ATOM 59 CA ASN A 13 10.777 -6.840 14.605 1.00 16.55 C ANISOU 59 CA ASN A 13 2210 1849 2229 -378 -15 378 C ATOM 60 C ASN A 13 10.128 -6.214 15.842 1.00 15.89 C ANISOU 60 C ASN A 13 2041 1878 2118 -384 9 410 C ATOM 61 O ASN A 13 8.905 -6.052 15.874 1.00 15.65 O ANISOU 61 O ASN A 13 1945 1946 2056 -443 14 437 O ATOM 62 CB ASN A 13 10.864 -8.352 14.825 1.00 17.72 C ANISOU 62 CB ASN A 13 2468 1898 2367 -445 -44 413 C ATOM 63 CG ASN A 13 9.500 -8.964 14.997 1.00 19.04 C ANISOU 63 CG ASN A 13 2626 2116 2494 -584 -59 461 C ATOM 64 OD1 ASN A 13 9.148 -9.467 16.085 1.00 20.73 O ANISOU 64 OD1 ASN A 13 2845 2351 2679 -640 -61 520 O ATOM 65 ND2 ASN A 13 8.699 -8.889 13.942 1.00 18.90 N ANISOU 65 ND2 ASN A 13 2580 2138 2462 -648 -71 443 N ATOM 66 N ALA A 14 10.930 -5.902 16.869 1.00 15.16 N ANISOU 66 N ALA A 14 1946 1789 2027 -325 25 407 N ATOM 67 CA ALA A 14 10.388 -5.333 18.097 1.00 15.57 C ANISOU 67 CA ALA A 14 1925 1950 2042 -326 50 427 C ATOM 68 C ALA A 14 9.806 -3.970 17.774 1.00 15.39 C ANISOU 68 C ALA A 14 1822 2004 2021 -278 85 391 C ATOM 69 O ALA A 14 8.740 -3.642 18.245 1.00 15.13 O ANISOU 69 O ALA A 14 1720 2078 1952 -297 105 414 O ATOM 70 CB ALA A 14 11.443 -5.224 19.196 1.00 15.78 C ANISOU 70 CB ALA A 14 1963 1972 2059 -275 57 422 C ATOM 71 N LEU A 15 10.491 -3.222 16.913 1.00 14.57 N ANISOU 71 N LEU A 15 1732 1847 1958 -214 95 340 N ATOM 72 CA LEU A 15 10.001 -1.911 16.457 1.00 14.54 C ANISOU 72 CA LEU A 15 1674 1888 1962 -156 130 313 C ATOM 73 C LEU A 15 8.709 -2.044 15.643 1.00 15.15 C ANISOU 73 C LEU A 15 1702 2033 2020 -191 123 348 C ATOM 74 O LEU A 15 7.755 -1.286 15.823 1.00 15.95 O ANISOU 74 O LEU A 15 1733 2232 2096 -157 153 360 O ATOM 75 CB LEU A 15 11.084 -1.220 15.625 1.00 14.10 C ANISOU 75 CB LEU A 15 1655 1751 1949 -99 138 264 C ATOM 76 CG LEU A 15 12.357 -0.840 16.397 1.00 13.92 C ANISOU 76 CG LEU A 15 1660 1695 1935 -70 149 225 C ATOM 77 CD1 LEU A 15 13.421 -0.344 15.414 1.00 14.09 C ANISOU 77 CD1 LEU A 15 1711 1650 1992 -37 150 187 C ATOM 78 CD2 LEU A 15 12.047 0.200 17.471 1.00 14.93 C ANISOU 78 CD2 LEU A 15 1756 1879 2038 -41 190 199 C ATOM 79 N ARG A 16 8.665 -3.031 14.760 1.00 15.67 N ANISOU 79 N ARG A 16 1806 2057 2091 -257 83 362 N ATOM 80 CA ARG A 16 7.444 -3.305 13.978 1.00 16.57 C ANISOU 80 CA ARG A 16 1869 2253 2173 -317 67 396 C ATOM 81 C ARG A 16 6.282 -3.719 14.905 1.00 17.42 C ANISOU 81 C ARG A 16 1910 2483 2224 -391 69 449 C ATOM 82 O ARG A 16 5.156 -3.186 14.830 1.00 17.98 O ANISOU 82 O ARG A 16 1882 2695 2255 -382 86 477 O ATOM 83 CB ARG A 16 7.762 -4.402 12.951 1.00 17.48 C ANISOU 83 CB ARG A 16 2061 2283 2297 -390 23 386 C ATOM 84 CG ARG A 16 6.639 -4.777 11.993 1.00 19.33 C ANISOU 84 CG ARG A 16 2254 2602 2491 -476 -2 409 C ATOM 85 CD ARG A 16 6.807 -6.218 11.510 1.00 20.47 C ANISOU 85 CD ARG A 16 2499 2652 2627 -591 -46 401 C ATOM 86 NE ARG A 16 6.809 -7.135 12.646 1.00 22.37 N ANISOU 86 NE ARG A 16 2792 2852 2858 -662 -55 434 N ATOM 87 CZ ARG A 16 5.729 -7.523 13.336 1.00 23.50 C ANISOU 87 CZ ARG A 16 2882 3097 2951 -766 -60 490 C ATOM 88 NH1 ARG A 16 4.511 -7.091 13.015 1.00 25.37 N ANISOU 88 NH1 ARG A 16 2999 3501 3138 -810 -58 517 N ATOM 89 NH2 ARG A 16 5.863 -8.348 14.362 1.00 24.49 N ANISOU 89 NH2 ARG A 16 3067 3172 3068 -825 -65 527 N ATOM 90 N ARG A 17 6.570 -4.675 15.786 1.00 17.05 N ANISOU 90 N ARG A 17 1916 2394 2168 -458 52 471 N ATOM 91 CA ARG A 17 5.588 -5.255 16.721 1.00 17.72 C ANISOU 91 CA ARG A 17 1951 2587 2194 -552 51 532 C ATOM 92 C ARG A 17 4.887 -4.193 17.569 1.00 18.19 C ANISOU 92 C ARG A 17 1899 2797 2216 -481 98 541 C ATOM 93 O ARG A 17 3.660 -4.237 17.725 1.00 18.32 O ANISOU 93 O ARG A 17 1819 2969 2173 -532 104 587 O ATOM 94 CB ARG A 17 6.297 -6.278 17.613 1.00 17.94 C ANISOU 94 CB ARG A 17 2071 2520 2225 -602 33 556 C ATOM 95 CG ARG A 17 5.364 -7.125 18.477 1.00 19.04 C ANISOU 95 CG ARG A 17 2185 2747 2303 -729 24 631 C ATOM 96 CD ARG A 17 6.178 -7.900 19.483 1.00 19.42 C ANISOU 96 CD ARG A 17 2322 2704 2354 -740 15 662 C ATOM 97 NE ARG A 17 6.740 -7.003 20.490 1.00 18.97 N ANISOU 97 NE ARG A 17 2221 2695 2293 -630 50 639 N ATOM 98 CZ ARG A 17 8.011 -7.005 20.882 1.00 18.89 C ANISOU 98 CZ ARG A 17 2275 2592 2312 -554 47 615 C ATOM 99 NH1 ARG A 17 8.880 -7.877 20.377 1.00 18.69 N ANISOU 99 NH1 ARG A 17 2360 2417 2323 -556 16 617 N ATOM 100 NH2 ARG A 17 8.410 -6.139 21.800 1.00 18.28 N ANISOU 100 NH2 ARG A 17 2149 2581 2217 -476 77 587 N ATOM 101 N GLU A 18 5.658 -3.224 18.084 1.00 17.82 N ANISOU 101 N GLU A 18 1864 2711 2196 -363 133 492 N ATOM 102 CA GLU A 18 5.092 -2.196 18.954 1.00 19.00 C ANISOU 102 CA GLU A 18 1932 2980 2308 -283 185 485 C ATOM 103 C GLU A 18 4.748 -0.896 18.225 1.00 19.43 C ANISOU 103 C GLU A 18 1944 3062 2377 -166 221 453 C ATOM 104 O GLU A 18 4.375 0.097 18.874 1.00 20.27 O ANISOU 104 O GLU A 18 2004 3239 2457 -71 273 434 O ATOM 105 CB GLU A 18 6.037 -1.931 20.135 1.00 19.50 C ANISOU 105 CB GLU A 18 2039 2996 2373 -242 204 449 C ATOM 106 CG GLU A 18 6.367 -3.184 20.932 1.00 18.99 C ANISOU 106 CG GLU A 18 2017 2913 2287 -340 171 496 C ATOM 107 CD GLU A 18 5.134 -3.829 21.542 1.00 20.79 C ANISOU 107 CD GLU A 18 2172 3285 2443 -433 171 570 C ATOM 108 OE1 GLU A 18 4.289 -3.074 22.065 1.00 21.04 O ANISOU 108 OE1 GLU A 18 2108 3462 2425 -385 213 570 O ATOM 109 OE2 GLU A 18 4.995 -5.076 21.488 1.00 20.84 O ANISOU 109 OE2 GLU A 18 2218 3260 2439 -552 131 630 O ATOM 110 N ARG A 19 4.844 -0.925 16.894 1.00 19.13 N ANISOU 110 N ARG A 19 1925 2970 2374 -168 197 451 N ATOM 111 CA AARG A 19 4.557 0.232 16.031 0.50 19.24 C ANISOU 111 CA AARG A 19 1909 2999 2403 -57 226 437 C ATOM 112 CA BARG A 19 4.518 0.235 16.056 0.50 19.32 C ANISOU 112 CA BARG A 19 1915 3014 2410 -57 227 439 C ATOM 113 C ARG A 19 5.275 1.507 16.483 1.00 18.88 C ANISOU 113 C ARG A 19 1911 2872 2389 65 278 378 C ATOM 114 O ARG A 19 4.688 2.591 16.525 1.00 19.51 O ANISOU 114 O ARG A 19 1956 3004 2455 176 326 375 O ATOM 115 CB AARG A 19 3.046 0.465 15.875 0.50 21.07 C ANISOU 115 CB AARG A 19 2015 3422 2570 -36 242 493 C ATOM 116 CB BARG A 19 2.998 0.495 16.049 0.50 21.31 C ANISOU 116 CB BARG A 19 2039 3462 2595 -33 247 493 C ATOM 117 CG AARG A 19 2.384 -0.484 14.890 0.50 21.91 C ANISOU 117 CG AARG A 19 2077 3602 2648 -153 189 541 C ATOM 118 CG BARG A 19 2.150 -0.684 15.589 0.50 22.29 C ANISOU 118 CG BARG A 19 2103 3695 2672 -177 197 553 C ATOM 119 CD AARG A 19 0.873 -0.344 14.940 0.50 23.44 C ANISOU 119 CD AARG A 19 2121 4027 2759 -150 202 604 C ATOM 120 CD BARG A 19 0.722 -0.541 16.091 0.50 24.17 C ANISOU 120 CD BARG A 19 2196 4164 2824 -172 221 611 C ATOM 121 NE AARG A 19 0.317 -1.075 16.072 0.50 23.95 N ANISOU 121 NE AARG A 19 2135 4198 2766 -248 201 639 N ATOM 122 NE BARG A 19 0.553 -1.309 17.317 0.50 25.81 N ANISOU 122 NE BARG A 19 2392 4423 2991 -269 218 633 N ATOM 123 CZ AARG A 19 -0.023 -0.524 17.234 0.50 24.68 C ANISOU 123 CZ AARG A 19 2176 4378 2823 -171 252 640 C ATOM 124 CZ BARG A 19 0.349 -2.619 17.334 0.50 26.24 C ANISOU 124 CZ BARG A 19 2459 4491 3021 -447 169 673 C ATOM 125 NH1AARG A 19 0.110 0.778 17.425 0.50 24.41 N ANISOU 125 NH1AARG A 19 2144 4324 2806 7 309 602 N ATOM 126 NH1BARG A 19 0.287 -3.289 16.188 0.50 26.25 N ANISOU 126 NH1BARG A 19 2485 4456 3031 -546 120 682 N ATOM 127 NH2AARG A 19 -0.511 -1.289 18.204 0.50 25.15 N ANISOU 127 NH2AARG A 19 2189 4542 2824 -278 247 680 N ATOM 128 NH2BARG A 19 0.218 -3.251 18.493 0.50 27.02 N ANISOU 128 NH2BARG A 19 2553 4632 3082 -529 172 704 N ATOM 129 N VAL A 20 6.566 1.363 16.787 1.00 16.97 N ANISOU 129 N VAL A 20 1757 2502 2188 43 267 332 N ATOM 130 CA VAL A 20 7.412 2.458 17.294 1.00 16.36 C ANISOU 130 CA VAL A 20 1738 2343 2135 118 308 267 C ATOM 131 C VAL A 20 7.769 3.387 16.136 1.00 15.94 C ANISOU 131 C VAL A 20 1725 2202 2127 185 324 249 C ATOM 132 O VAL A 20 8.277 2.915 15.103 1.00 15.64 O ANISOU 132 O VAL A 20 1713 2109 2122 145 287 259 O ATOM 133 CB VAL A 20 8.720 1.901 17.930 1.00 15.66 C ANISOU 133 CB VAL A 20 1712 2176 2063 58 283 233 C ATOM 134 CG1 VAL A 20 9.595 3.034 18.492 1.00 15.99 C ANISOU 134 CG1 VAL A 20 1807 2153 2116 108 322 161 C ATOM 135 CG2 VAL A 20 8.418 0.871 19.017 1.00 17.03 C ANISOU 135 CG2 VAL A 20 1854 2427 2189 -12 262 268 C ATOM 136 N PRO A 21 7.521 4.707 16.285 1.00 16.07 N ANISOU 136 N PRO A 21 1758 2202 2144 289 381 223 N ATOM 137 CA PRO A 21 7.995 5.605 15.245 1.00 16.23 C ANISOU 137 CA PRO A 21 1837 2120 2210 343 398 212 C ATOM 138 C PRO A 21 9.509 5.611 15.215 1.00 15.44 C ANISOU 138 C PRO A 21 1817 1900 2149 283 382 161 C ATOM 139 O PRO A 21 10.151 5.758 16.265 1.00 15.03 O ANISOU 139 O PRO A 21 1798 1824 2088 257 394 108 O ATOM 140 CB PRO A 21 7.470 6.974 15.689 1.00 17.01 C ANISOU 140 CB PRO A 21 1961 2205 2296 466 468 189 C ATOM 141 CG PRO A 21 6.354 6.690 16.637 1.00 17.78 C ANISOU 141 CG PRO A 21 1975 2448 2333 494 485 208 C ATOM 142 CD PRO A 21 6.756 5.416 17.327 1.00 17.11 C ANISOU 142 CD PRO A 21 1864 2405 2232 367 435 206 C ATOM 143 N VAL A 22 10.082 5.452 14.021 1.00 15.54 N ANISOU 143 N VAL A 22 1850 1858 2195 260 356 176 N ATOM 144 CA VAL A 22 11.513 5.277 13.916 1.00 15.13 C ANISOU 144 CA VAL A 22 1851 1727 2170 199 336 138 C ATOM 145 C VAL A 22 12.151 6.279 12.967 1.00 14.69 C ANISOU 145 C VAL A 22 1853 1582 2148 223 360 129 C ATOM 146 O VAL A 22 11.482 6.834 12.086 1.00 14.25 O ANISOU 146 O VAL A 22 1793 1522 2098 284 377 170 O ATOM 147 CB VAL A 22 11.933 3.864 13.433 1.00 15.72 C ANISOU 147 CB VAL A 22 1904 1822 2246 130 277 159 C ATOM 148 CG1 VAL A 22 11.389 2.774 14.360 1.00 15.75 C ANISOU 148 CG1 VAL A 22 1870 1897 2218 89 252 178 C ATOM 149 CG2 VAL A 22 11.556 3.630 11.961 1.00 15.97 C ANISOU 149 CG2 VAL A 22 1920 1860 2287 139 257 199 C ATOM 150 N SER A 23 13.439 6.487 13.197 1.00 14.13 N ANISOU 150 N SER A 23 1827 1454 2090 170 359 83 N ATOM 151 CA SER A 23 14.329 7.197 12.286 1.00 14.59 C ANISOU 151 CA SER A 23 1933 1438 2173 155 371 78 C ATOM 152 C SER A 23 15.334 6.216 11.698 1.00 14.39 C ANISOU 152 C SER A 23 1881 1436 2149 98 325 82 C ATOM 153 O SER A 23 15.939 5.433 12.435 1.00 13.98 O ANISOU 153 O SER A 23 1809 1420 2082 57 299 58 O ATOM 154 CB SER A 23 15.063 8.286 13.051 1.00 15.48 C ANISOU 154 CB SER A 23 2116 1480 2286 125 411 18 C ATOM 155 OG SER A 23 14.146 9.289 13.459 1.00 16.34 O ANISOU 155 OG SER A 23 2271 1544 2394 198 463 10 O ATOM 156 N ILE A 24 15.470 6.249 10.374 1.00 13.76 N ANISOU 156 N ILE A 24 1802 1345 2082 107 319 115 N ATOM 157 CA ILE A 24 16.500 5.481 9.699 1.00 13.40 C ANISOU 157 CA ILE A 24 1739 1321 2033 68 286 112 C ATOM 158 C ILE A 24 17.437 6.497 9.113 1.00 13.29 C ANISOU 158 C ILE A 24 1760 1262 2027 40 314 106 C ATOM 159 O ILE A 24 17.019 7.307 8.273 1.00 13.57 O ANISOU 159 O ILE A 24 1822 1259 2073 69 339 141 O ATOM 160 CB ILE A 24 15.910 4.572 8.598 1.00 13.27 C ANISOU 160 CB ILE A 24 1692 1342 2008 89 254 150 C ATOM 161 CG1 ILE A 24 15.011 3.498 9.245 1.00 13.48 C ANISOU 161 CG1 ILE A 24 1691 1410 2021 87 224 157 C ATOM 162 CG2 ILE A 24 17.045 3.907 7.783 1.00 13.35 C ANISOU 162 CG2 ILE A 24 1696 1367 2008 66 231 139 C ATOM 163 CD1 ILE A 24 14.377 2.525 8.267 1.00 13.29 C ANISOU 163 CD1 ILE A 24 1647 1422 1980 81 189 183 C ATOM 164 N TYR A 25 18.697 6.482 9.568 1.00 12.90 N ANISOU 164 N TYR A 25 1707 1228 1966 -18 310 68 N ATOM 165 CA TYR A 25 19.696 7.423 9.051 1.00 13.46 C ANISOU 165 CA TYR A 25 1805 1274 2036 -73 336 63 C ATOM 166 C TYR A 25 20.500 6.694 8.008 1.00 13.31 C ANISOU 166 C TYR A 25 1739 1319 2000 -78 311 82 C ATOM 167 O TYR A 25 21.001 5.584 8.253 1.00 13.76 O ANISOU 167 O TYR A 25 1749 1441 2037 -68 278 67 O ATOM 168 CB TYR A 25 20.637 7.906 10.158 1.00 13.72 C ANISOU 168 CB TYR A 25 1848 1313 2050 -151 346 9 C ATOM 169 CG TYR A 25 19.988 8.813 11.168 1.00 14.41 C ANISOU 169 CG TYR A 25 2001 1329 2146 -153 380 -24 C ATOM 170 CD1 TYR A 25 19.355 8.285 12.301 1.00 14.61 C ANISOU 170 CD1 TYR A 25 2007 1383 2160 -121 368 -47 C ATOM 171 CD2 TYR A 25 20.010 10.193 10.990 1.00 16.07 C ANISOU 171 CD2 TYR A 25 2298 1437 2369 -185 428 -32 C ATOM 172 CE1 TYR A 25 18.765 9.126 13.242 1.00 15.76 C ANISOU 172 CE1 TYR A 25 2211 1473 2303 -115 405 -86 C ATOM 173 CE2 TYR A 25 19.425 11.043 11.919 1.00 16.61 C ANISOU 173 CE2 TYR A 25 2443 1427 2441 -175 466 -74 C ATOM 174 CZ TYR A 25 18.812 10.496 13.031 1.00 16.70 C ANISOU 174 CZ TYR A 25 2424 1484 2436 -136 454 -104 C ATOM 175 OH TYR A 25 18.258 11.348 13.944 1.00 18.01 O ANISOU 175 OH TYR A 25 2665 1582 2596 -119 497 -152 O ATOM 176 N LEU A 26 20.599 7.307 6.845 1.00 13.30 N ANISOU 176 N LEU A 26 1754 1298 2001 -82 330 117 N ATOM 177 CA LEU A 26 21.325 6.722 5.715 1.00 13.44 C ANISOU 177 CA LEU A 26 1728 1386 1994 -81 314 135 C ATOM 178 C LEU A 26 22.791 7.071 5.763 1.00 14.37 C ANISOU 178 C LEU A 26 1820 1558 2084 -157 325 117 C ATOM 179 O LEU A 26 23.181 8.022 6.446 1.00 15.07 O ANISOU 179 O LEU A 26 1939 1610 2174 -230 349 98 O ATOM 180 CB LEU A 26 20.715 7.254 4.418 1.00 13.32 C ANISOU 180 CB LEU A 26 1735 1345 1981 -53 331 190 C ATOM 181 CG LEU A 26 19.243 6.966 4.142 1.00 13.17 C ANISOU 181 CG LEU A 26 1722 1307 1974 19 319 219 C ATOM 182 CD1 LEU A 26 18.860 7.447 2.747 1.00 13.98 C ANISOU 182 CD1 LEU A 26 1830 1418 2063 45 331 281 C ATOM 183 CD2 LEU A 26 18.910 5.461 4.297 1.00 12.58 C ANISOU 183 CD2 LEU A 26 1607 1286 1886 47 274 193 C ATOM 184 N VAL A 27 23.610 6.346 5.002 1.00 14.86 N ANISOU 184 N VAL A 27 1824 1712 2111 -144 310 121 N ATOM 185 CA VAL A 27 25.055 6.615 4.988 1.00 16.69 C ANISOU 185 CA VAL A 27 2004 2034 2301 -214 319 111 C ATOM 186 C VAL A 27 25.445 8.014 4.516 1.00 18.20 C ANISOU 186 C VAL A 27 2231 2196 2490 -312 359 139 C ATOM 187 O VAL A 27 26.536 8.471 4.803 1.00 20.18 O ANISOU 187 O VAL A 27 2449 2511 2708 -406 369 127 O ATOM 188 CB VAL A 27 25.833 5.554 4.191 1.00 16.68 C ANISOU 188 CB VAL A 27 1930 2151 2255 -159 302 111 C ATOM 189 CG1 VAL A 27 25.713 4.215 4.907 1.00 16.09 C ANISOU 189 CG1 VAL A 27 1838 2096 2181 -77 267 81 C ATOM 190 CG2 VAL A 27 25.331 5.467 2.760 1.00 16.76 C ANISOU 190 CG2 VAL A 27 1955 2152 2260 -116 308 145 C ATOM 191 N ASN A 28 24.551 8.677 3.789 1.00 18.44 N ANISOU 191 N ASN A 28 2325 2131 2548 -293 380 183 N ATOM 192 CA ASN A 28 24.822 10.021 3.276 1.00 20.31 C ANISOU 192 CA ASN A 28 2620 2312 2785 -378 421 223 C ATOM 193 C ASN A 28 24.257 11.112 4.203 1.00 20.24 C ANISOU 193 C ASN A 28 2716 2157 2817 -417 450 208 C ATOM 194 O ASN A 28 24.254 12.304 3.865 1.00 21.39 O ANISOU 194 O ASN A 28 2946 2207 2973 -476 490 244 O ATOM 195 CB ASN A 28 24.260 10.136 1.855 1.00 21.09 C ANISOU 195 CB ASN A 28 2731 2402 2880 -323 431 292 C ATOM 196 CG ASN A 28 22.780 9.890 1.805 1.00 22.09 C ANISOU 196 CG ASN A 28 2893 2459 3042 -215 420 309 C ATOM 197 OD1 ASN A 28 22.109 9.840 2.844 1.00 21.26 O ANISOU 197 OD1 ASN A 28 2818 2291 2970 -186 414 275 O ATOM 198 ND2 ASN A 28 22.248 9.714 0.594 1.00 24.58 N ANISOU 198 ND2 ASN A 28 3195 2804 3341 -157 416 362 N ATOM 199 N GLY A 29 23.760 10.691 5.364 1.00 19.02 N ANISOU 199 N GLY A 29 2564 1980 2681 -379 433 156 N ATOM 200 CA GLY A 29 23.324 11.616 6.428 1.00 19.65 C ANISOU 200 CA GLY A 29 2738 1941 2787 -412 461 121 C ATOM 201 C GLY A 29 21.820 11.848 6.489 1.00 19.61 C ANISOU 201 C GLY A 29 2796 1831 2822 -298 476 143 C ATOM 202 O GLY A 29 21.303 12.346 7.495 1.00 19.86 O ANISOU 202 O GLY A 29 2892 1783 2871 -289 496 104 O ATOM 203 N ILE A 30 21.118 11.492 5.416 1.00 18.94 N ANISOU 203 N ILE A 30 2687 1764 2744 -210 467 205 N ATOM 204 CA ILE A 30 19.657 11.711 5.307 1.00 18.65 C ANISOU 204 CA ILE A 30 2689 1664 2734 -96 479 242 C ATOM 205 C ILE A 30 18.887 10.909 6.357 1.00 17.75 C ANISOU 205 C ILE A 30 2536 1582 2625 -39 454 199 C ATOM 206 O ILE A 30 19.172 9.714 6.521 1.00 16.44 O ANISOU 206 O ILE A 30 2291 1511 2443 -46 411 174 O ATOM 207 CB ILE A 30 19.158 11.328 3.870 1.00 18.77 C ANISOU 207 CB ILE A 30 2660 1736 2736 -29 464 317 C ATOM 208 CG1 ILE A 30 19.930 12.081 2.764 1.00 21.63 C ANISOU 208 CG1 ILE A 30 3052 2083 3083 -87 489 372 C ATOM 209 CG2 ILE A 30 17.656 11.489 3.700 1.00 20.47 C ANISOU 209 CG2 ILE A 30 2887 1927 2964 89 471 365 C ATOM 210 CD1 ILE A 30 19.991 13.554 2.960 1.00 23.24 C ANISOU 210 CD1 ILE A 30 3379 2142 3309 -122 544 396 C ATOM 211 N LYS A 31 17.936 11.559 7.051 1.00 17.63 N ANISOU 211 N LYS A 31 2580 1490 2629 20 485 193 N ATOM 212 CA LYS A 31 17.057 10.905 8.034 1.00 17.87 C ANISOU 212 CA LYS A 31 2572 1561 2658 77 469 163 C ATOM 213 C LYS A 31 15.702 10.610 7.430 1.00 17.36 C ANISOU 213 C LYS A 31 2468 1537 2593 186 461 224 C ATOM 214 O LYS A 31 15.013 11.518 7.009 1.00 17.96 O ANISOU 214 O LYS A 31 2593 1554 2677 260 499 272 O ATOM 215 CB LYS A 31 16.856 11.781 9.281 1.00 19.55 C ANISOU 215 CB LYS A 31 2863 1689 2876 78 511 108 C ATOM 216 CG LYS A 31 15.922 11.168 10.343 1.00 20.85 C ANISOU 216 CG LYS A 31 2982 1911 3029 136 500 81 C ATOM 217 CD LYS A 31 15.838 12.016 11.607 1.00 23.70 C ANISOU 217 CD LYS A 31 3422 2200 3384 133 544 13 C ATOM 218 CE LYS A 31 15.127 13.333 11.377 1.00 26.38 C ANISOU 218 CE LYS A 31 3869 2415 3740 221 607 33 C ATOM 219 NZ LYS A 31 15.265 14.229 12.562 1.00 29.48 N ANISOU 219 NZ LYS A 31 4365 2715 4122 200 655 -52 N ATOM 220 N LEU A 32 15.315 9.334 7.407 1.00 16.05 N ANISOU 220 N LEU A 32 2216 1473 2410 193 414 226 N ATOM 221 CA LEU A 32 13.970 8.948 7.009 1.00 15.77 C ANISOU 221 CA LEU A 32 2128 1504 2361 272 400 276 C ATOM 222 C LEU A 32 13.177 8.564 8.249 1.00 16.22 C ANISOU 222 C LEU A 32 2156 1598 2409 296 399 248 C ATOM 223 O LEU A 32 13.727 7.999 9.183 1.00 16.24 O ANISOU 223 O LEU A 32 2152 1608 2410 239 382 196 O ATOM 224 CB LEU A 32 14.008 7.740 6.080 1.00 15.31 C ANISOU 224 CB LEU A 32 2002 1535 2281 244 348 294 C ATOM 225 CG LEU A 32 14.879 7.835 4.827 1.00 15.59 C ANISOU 225 CG LEU A 32 2046 1567 2310 214 343 315 C ATOM 226 CD1 LEU A 32 15.016 6.485 4.121 1.00 15.58 C ANISOU 226 CD1 LEU A 32 1990 1648 2280 184 292 306 C ATOM 227 CD2 LEU A 32 14.355 8.907 3.884 1.00 16.40 C ANISOU 227 CD2 LEU A 32 2175 1646 2409 276 375 388 C ATOM 228 N GLN A 33 11.892 8.861 8.248 1.00 16.45 N ANISOU 228 N GLN A 33 2160 1667 2425 384 416 290 N ATOM 229 CA GLN A 33 11.071 8.577 9.422 1.00 18.22 C ANISOU 229 CA GLN A 33 2347 1944 2631 411 421 270 C ATOM 230 C GLN A 33 9.827 7.825 9.003 1.00 17.79 C ANISOU 230 C GLN A 33 2195 2023 2542 442 391 326 C ATOM 231 O GLN A 33 9.254 8.086 7.947 1.00 18.68 O ANISOU 231 O GLN A 33 2280 2176 2640 495 390 387 O ATOM 232 CB GLN A 33 10.640 9.869 10.143 1.00 19.90 C ANISOU 232 CB GLN A 33 2625 2088 2849 500 487 256 C ATOM 233 CG GLN A 33 11.785 10.666 10.767 1.00 21.00 C ANISOU 233 CG GLN A 33 2871 2096 3012 448 520 187 C ATOM 234 CD GLN A 33 11.296 11.945 11.455 1.00 23.77 C ANISOU 234 CD GLN A 33 3310 2359 3363 540 590 162 C ATOM 235 OE1 GLN A 33 10.651 11.900 12.499 1.00 26.33 O ANISOU 235 OE1 GLN A 33 3614 2728 3662 583 608 130 O ATOM 236 NE2 GLN A 33 11.626 13.077 10.880 1.00 25.43 N ANISOU 236 NE2 GLN A 33 3625 2439 3597 567 632 176 N ATOM 237 N GLY A 34 9.395 6.906 9.853 1.00 17.74 N ANISOU 237 N GLY A 34 2135 2094 2513 401 366 309 N ATOM 238 CA GLY A 34 8.129 6.243 9.631 1.00 18.63 C ANISOU 238 CA GLY A 34 2150 2345 2582 411 342 361 C ATOM 239 C GLY A 34 8.051 5.051 10.547 1.00 18.50 C ANISOU 239 C GLY A 34 2100 2382 2547 321 307 337 C ATOM 240 O GLY A 34 8.679 5.047 11.614 1.00 18.50 O ANISOU 240 O GLY A 34 2139 2329 2560 297 319 288 O ATOM 241 N GLN A 35 7.303 4.039 10.111 1.00 19.38 N ANISOU 241 N GLN A 35 2142 2599 2623 264 264 373 N ATOM 242 CA GLN A 35 7.122 2.780 10.856 1.00 19.89 C ANISOU 242 CA GLN A 35 2182 2709 2664 163 227 366 C ATOM 243 C GLN A 35 7.762 1.637 10.115 1.00 18.80 C ANISOU 243 C GLN A 35 2081 2527 2536 68 175 353 C ATOM 244 O GLN A 35 7.643 1.575 8.891 1.00 17.62 O ANISOU 244 O GLN A 35 1922 2395 2377 63 156 369 O ATOM 245 CB GLN A 35 5.648 2.426 10.918 1.00 23.29 C ANISOU 245 CB GLN A 35 2510 3305 3036 149 218 421 C ATOM 246 CG GLN A 35 4.841 3.348 11.768 1.00 27.11 C ANISOU 246 CG GLN A 35 2941 3865 3494 251 271 438 C ATOM 247 CD GLN A 35 4.209 2.574 12.868 1.00 29.91 C ANISOU 247 CD GLN A 35 3240 4321 3805 182 262 449 C ATOM 248 OE1 GLN A 35 4.846 1.688 13.449 1.00 32.08 O ANISOU 248 OE1 GLN A 35 3561 4535 4092 86 235 424 O ATOM 249 NE2 GLN A 35 2.971 2.885 13.174 1.00 29.76 N ANISOU 249 NE2 GLN A 35 3116 4462 3727 234 287 494 N ATOM 250 N ILE A 36 8.392 0.717 10.847 1.00 17.92 N ANISOU 250 N ILE A 36 2012 2362 2433 -1 153 326 N ATOM 251 CA ILE A 36 8.945 -0.487 10.208 1.00 18.48 C ANISOU 251 CA ILE A 36 2133 2382 2508 -79 107 311 C ATOM 252 C ILE A 36 7.750 -1.372 9.921 1.00 18.92 C ANISOU 252 C ILE A 36 2143 2532 2515 -165 73 348 C ATOM 253 O ILE A 36 7.023 -1.790 10.847 1.00 18.95 O ANISOU 253 O ILE A 36 2110 2599 2489 -214 71 375 O ATOM 254 CB ILE A 36 9.949 -1.265 11.091 1.00 18.82 C ANISOU 254 CB ILE A 36 2240 2341 2569 -111 94 283 C ATOM 255 CG1 ILE A 36 11.137 -0.383 11.563 1.00 19.97 C ANISOU 255 CG1 ILE A 36 2415 2423 2749 -45 126 246 C ATOM 256 CG2 ILE A 36 10.398 -2.565 10.399 1.00 18.83 C ANISOU 256 CG2 ILE A 36 2306 2281 2569 -173 52 271 C ATOM 257 CD1 ILE A 36 11.986 0.214 10.462 1.00 20.00 C ANISOU 257 CD1 ILE A 36 2444 2377 2778 -5 134 223 C ATOM 258 N GLU A 37 7.527 -1.630 8.639 1.00 18.63 N ANISOU 258 N GLU A 37 2102 2517 2459 -194 48 350 N ATOM 259 CA AGLU A 37 6.390 -2.449 8.240 0.50 19.64 C ANISOU 259 CA AGLU A 37 2184 2748 2529 -298 11 379 C ATOM 260 CA BGLU A 37 6.403 -2.439 8.186 0.50 19.96 C ANISOU 260 CA BGLU A 37 2226 2789 2570 -297 11 379 C ATOM 261 C GLU A 37 6.816 -3.909 8.077 1.00 19.80 C ANISOU 261 C GLU A 37 2299 2676 2546 -412 -31 348 C ATOM 262 O GLU A 37 6.101 -4.813 8.518 1.00 19.48 O ANISOU 262 O GLU A 37 2259 2674 2471 -524 -55 369 O ATOM 263 CB AGLU A 37 5.730 -1.870 6.977 0.50 20.30 C ANISOU 263 CB AGLU A 37 2199 2939 2577 -271 6 404 C ATOM 264 CB BGLU A 37 5.918 -1.876 6.843 0.50 21.13 C ANISOU 264 CB BGLU A 37 2317 3024 2688 -267 5 396 C ATOM 265 CG AGLU A 37 4.327 -2.380 6.680 0.50 21.67 C ANISOU 265 CG AGLU A 37 2281 3281 2673 -369 -25 447 C ATOM 266 CG BGLU A 37 4.904 -2.715 6.093 0.50 23.11 C ANISOU 266 CG BGLU A 37 2523 3391 2867 -389 -41 414 C ATOM 267 CD AGLU A 37 3.329 -2.135 7.800 0.50 21.94 C ANISOU 267 CD AGLU A 37 2220 3439 2677 -366 -4 496 C ATOM 268 CD BGLU A 37 4.424 -2.023 4.834 0.50 23.78 C ANISOU 268 CD BGLU A 37 2535 3588 2912 -341 -45 442 C ATOM 269 OE1AGLU A 37 3.524 -1.224 8.636 0.50 21.81 O ANISOU 269 OE1AGLU A 37 2193 3402 2694 -250 43 502 O ATOM 270 OE1BGLU A 37 3.394 -2.450 4.293 0.50 25.87 O ANISOU 270 OE1BGLU A 37 2726 4002 3103 -429 -78 469 O ATOM 271 OE2AGLU A 37 2.340 -2.876 7.849 0.50 23.14 O ANISOU 271 OE2AGLU A 37 2311 3715 2765 -487 -35 527 O ATOM 272 OE2BGLU A 37 5.079 -1.054 4.381 0.50 23.93 O ANISOU 272 OE2BGLU A 37 2570 3555 2966 -223 -15 441 O ATOM 273 N SER A 38 7.995 -4.132 7.482 1.00 19.42 N ANISOU 273 N SER A 38 2339 2507 2532 -378 -35 299 N ATOM 274 CA SER A 38 8.544 -5.454 7.250 1.00 20.33 C ANISOU 274 CA SER A 38 2566 2513 2646 -450 -66 262 C ATOM 275 C SER A 38 10.032 -5.312 6.879 1.00 19.00 C ANISOU 275 C SER A 38 2465 2233 2519 -356 -51 215 C ATOM 276 O SER A 38 10.548 -4.189 6.758 1.00 18.55 O ANISOU 276 O SER A 38 2367 2194 2489 -263 -21 215 O ATOM 277 CB SER A 38 7.764 -6.172 6.144 1.00 21.42 C ANISOU 277 CB SER A 38 2711 2700 2727 -560 -104 250 C ATOM 278 OG SER A 38 7.718 -5.377 4.980 1.00 22.51 O ANISOU 278 OG SER A 38 2794 2910 2848 -507 -99 244 O ATOM 279 N PHE A 39 10.717 -6.448 6.726 1.00 19.08 N ANISOU 279 N PHE A 39 2585 2133 2532 -380 -70 178 N ATOM 280 CA PHE A 39 12.162 -6.478 6.395 1.00 17.82 C ANISOU 280 CA PHE A 39 2484 1887 2400 -285 -56 136 C ATOM 281 C PHE A 39 12.534 -7.875 5.911 1.00 17.79 C ANISOU 281 C PHE A 39 2606 1774 2378 -318 -79 93 C ATOM 282 O PHE A 39 11.843 -8.833 6.235 1.00 17.89 O ANISOU 282 O PHE A 39 2679 1747 2372 -416 -103 103 O ATOM 283 CB PHE A 39 13.037 -6.096 7.615 1.00 18.50 C ANISOU 283 CB PHE A 39 2561 1943 2525 -210 -32 151 C ATOM 284 CG PHE A 39 12.820 -6.985 8.818 1.00 20.60 C ANISOU 284 CG PHE A 39 2874 2162 2790 -254 -45 181 C ATOM 285 CD1 PHE A 39 11.810 -6.692 9.734 1.00 21.09 C ANISOU 285 CD1 PHE A 39 2874 2295 2842 -310 -42 227 C ATOM 286 CD2 PHE A 39 13.587 -8.135 8.998 1.00 21.92 C ANISOU 286 CD2 PHE A 39 3150 2219 2961 -235 -56 168 C ATOM 287 CE1 PHE A 39 11.586 -7.528 10.832 1.00 22.86 C ANISOU 287 CE1 PHE A 39 3140 2487 3059 -360 -53 264 C ATOM 288 CE2 PHE A 39 13.367 -8.971 10.084 1.00 24.30 C ANISOU 288 CE2 PHE A 39 3504 2470 3258 -277 -67 209 C ATOM 289 CZ PHE A 39 12.367 -8.664 11.000 1.00 22.99 C ANISOU 289 CZ PHE A 39 3272 2382 3081 -347 -66 259 C ATOM 290 N ASP A 40 13.600 -7.983 5.112 1.00 16.98 N ANISOU 290 N ASP A 40 2548 1626 2277 -239 -70 45 N ATOM 291 CA ASP A 40 14.160 -9.285 4.762 1.00 17.71 C ANISOU 291 CA ASP A 40 2776 1597 2354 -231 -81 -2 C ATOM 292 C ASP A 40 15.676 -9.181 4.834 1.00 17.86 C ANISOU 292 C ASP A 40 2809 1582 2394 -90 -54 -21 C ATOM 293 O ASP A 40 16.177 -8.261 5.496 1.00 16.69 O ANISOU 293 O ASP A 40 2574 1492 2273 -33 -35 11 O ATOM 294 CB ASP A 40 13.647 -9.811 3.403 1.00 18.50 C ANISOU 294 CB ASP A 40 2929 1696 2403 -303 -101 -57 C ATOM 295 CG ASP A 40 14.090 -8.964 2.216 1.00 17.96 C ANISOU 295 CG ASP A 40 2793 1714 2316 -240 -86 -86 C ATOM 296 OD1 ASP A 40 14.960 -8.072 2.379 1.00 16.78 O ANISOU 296 OD1 ASP A 40 2576 1605 2197 -139 -57 -69 O ATOM 297 OD2 ASP A 40 13.536 -9.192 1.109 1.00 18.78 O ANISOU 297 OD2 ASP A 40 2911 1856 2368 -306 -104 -124 O ATOM 298 N GLN A 41 16.395 -10.082 4.159 1.00 18.32 N ANISOU 298 N GLN A 41 2971 1558 2431 -34 -52 -75 N ATOM 299 CA GLN A 41 17.860 -10.103 4.261 1.00 19.67 C ANISOU 299 CA GLN A 41 3146 1717 2610 111 -27 -88 C ATOM 300 C GLN A 41 18.484 -8.769 3.840 1.00 18.40 C ANISOU 300 C GLN A 41 2854 1684 2453 164 -3 -84 C ATOM 301 O GLN A 41 19.443 -8.302 4.443 1.00 17.59 O ANISOU 301 O GLN A 41 2695 1624 2366 241 16 -62 O ATOM 302 CB GLN A 41 18.441 -11.249 3.428 1.00 21.60 C ANISOU 302 CB GLN A 41 3524 1863 2821 175 -22 -154 C ATOM 303 CG GLN A 41 19.948 -11.443 3.596 1.00 24.77 C ANISOU 303 CG GLN A 41 3929 2262 3219 345 6 -161 C ATOM 304 CD GLN A 41 20.535 -12.545 2.717 1.00 27.66 C ANISOU 304 CD GLN A 41 4430 2536 3545 435 19 -233 C ATOM 305 OE1 GLN A 41 19.890 -13.034 1.784 1.00 29.89 O ANISOU 305 OE1 GLN A 41 4798 2764 3795 363 8 -293 O ATOM 306 NE2 GLN A 41 21.784 -12.927 3.003 1.00 29.20 N ANISOU 306 NE2 GLN A 41 4640 2723 3731 599 44 -229 N ATOM 307 N PHE A 42 17.919 -8.164 2.804 1.00 18.49 N ANISOU 307 N PHE A 42 2821 1762 2444 111 -5 -100 N ATOM 308 CA PHE A 42 18.548 -7.027 2.184 1.00 18.38 C ANISOU 308 CA PHE A 42 2709 1850 2424 157 20 -96 C ATOM 309 C PHE A 42 17.810 -5.707 2.329 1.00 16.34 C ANISOU 309 C PHE A 42 2351 1670 2186 101 24 -47 C ATOM 310 O PHE A 42 18.403 -4.679 2.087 1.00 15.42 O ANISOU 310 O PHE A 42 2166 1618 2075 134 48 -31 O ATOM 311 CB PHE A 42 18.779 -7.311 0.709 1.00 20.12 C ANISOU 311 CB PHE A 42 2959 2094 2592 177 24 -151 C ATOM 312 CG PHE A 42 19.776 -8.405 0.465 1.00 22.76 C ANISOU 312 CG PHE A 42 3384 2364 2900 273 35 -206 C ATOM 313 CD1 PHE A 42 21.094 -8.281 0.924 1.00 23.69 C ANISOU 313 CD1 PHE A 42 3465 2511 3025 387 61 -196 C ATOM 314 CD2 PHE A 42 19.402 -9.556 -0.208 1.00 25.12 C ANISOU 314 CD2 PHE A 42 3806 2578 3160 253 20 -269 C ATOM 315 CE1 PHE A 42 22.023 -9.289 0.687 1.00 25.23 C ANISOU 315 CE1 PHE A 42 3737 2659 3188 503 75 -241 C ATOM 316 CE2 PHE A 42 20.329 -10.583 -0.437 1.00 26.85 C ANISOU 316 CE2 PHE A 42 4127 2723 3353 364 37 -324 C ATOM 317 CZ PHE A 42 21.633 -10.443 0.014 1.00 26.82 C ANISOU 317 CZ PHE A 42 4077 2756 3357 501 66 -306 C ATOM 318 N VAL A 43 16.516 -5.732 2.654 1.00 15.30 N ANISOU 318 N VAL A 43 2216 1536 2060 17 3 -21 N ATOM 319 CA VAL A 43 15.746 -4.482 2.679 1.00 14.60 C ANISOU 319 CA VAL A 43 2037 1526 1983 -13 12 27 C ATOM 320 C VAL A 43 14.868 -4.329 3.920 1.00 14.84 C ANISOU 320 C VAL A 43 2044 1555 2040 -56 6 68 C ATOM 321 O VAL A 43 14.585 -5.312 4.627 1.00 14.81 O ANISOU 321 O VAL A 43 2093 1496 2037 -95 -13 66 O ATOM 322 CB VAL A 43 14.853 -4.259 1.394 1.00 14.84 C ANISOU 322 CB VAL A 43 2041 1630 1969 -58 -1 29 C ATOM 323 CG1 VAL A 43 15.675 -4.350 0.123 1.00 15.32 C ANISOU 323 CG1 VAL A 43 2118 1710 1991 -17 7 -12 C ATOM 324 CG2 VAL A 43 13.658 -5.208 1.352 1.00 15.34 C ANISOU 324 CG2 VAL A 43 2138 1690 2000 -155 -39 20 C ATOM 325 N ILE A 44 14.466 -3.083 4.165 1.00 13.97 N ANISOU 325 N ILE A 44 1859 1502 1946 -44 27 108 N ATOM 326 CA ILE A 44 13.478 -2.700 5.187 1.00 14.46 C ANISOU 326 CA ILE A 44 1880 1592 2021 -72 30 148 C ATOM 327 C ILE A 44 12.376 -1.904 4.494 1.00 15.47 C ANISOU 327 C ILE A 44 1943 1809 2127 -80 33 185 C ATOM 328 O ILE A 44 12.642 -0.956 3.718 1.00 15.47 O ANISOU 328 O ILE A 44 1917 1834 2127 -33 54 198 O ATOM 329 CB ILE A 44 14.101 -1.805 6.293 1.00 14.10 C ANISOU 329 CB ILE A 44 1814 1532 2014 -25 62 156 C ATOM 330 CG1 ILE A 44 15.136 -2.594 7.094 1.00 13.53 C ANISOU 330 CG1 ILE A 44 1787 1401 1952 -12 55 132 C ATOM 331 CG2 ILE A 44 13.028 -1.204 7.218 1.00 14.66 C ANISOU 331 CG2 ILE A 44 1836 1645 2088 -36 75 192 C ATOM 332 CD1 ILE A 44 15.977 -1.727 8.042 1.00 13.09 C ANISOU 332 CD1 ILE A 44 1706 1348 1918 23 83 130 C ATOM 333 N LEU A 45 11.137 -2.273 4.775 1.00 16.25 N ANISOU 333 N LEU A 45 2011 1965 2201 -138 14 211 N ATOM 334 CA LEU A 45 10.016 -1.520 4.267 1.00 17.53 C ANISOU 334 CA LEU A 45 2093 2237 2333 -131 18 258 C ATOM 335 C LEU A 45 9.580 -0.536 5.331 1.00 17.36 C ANISOU 335 C LEU A 45 2021 2240 2334 -76 53 295 C ATOM 336 O LEU A 45 9.224 -0.935 6.447 1.00 17.01 O ANISOU 336 O LEU A 45 1972 2197 2293 -108 51 299 O ATOM 337 CB LEU A 45 8.874 -2.475 3.892 1.00 19.44 C ANISOU 337 CB LEU A 45 2311 2559 2516 -234 -24 266 C ATOM 338 CG LEU A 45 8.910 -3.035 2.460 1.00 22.15 C ANISOU 338 CG LEU A 45 2678 2926 2811 -281 -55 236 C ATOM 339 CD1 LEU A 45 8.435 -1.968 1.483 1.00 23.05 C ANISOU 339 CD1 LEU A 45 2709 3154 2894 -225 -44 282 C ATOM 340 CD2 LEU A 45 10.277 -3.562 2.036 1.00 22.09 C ANISOU 340 CD2 LEU A 45 2768 2800 2825 -257 -53 173 C ATOM 341 N LEU A 46 9.663 0.742 4.985 1.00 16.67 N ANISOU 341 N LEU A 46 1910 2164 2261 8 88 321 N ATOM 342 CA LEU A 46 9.355 1.845 5.886 1.00 17.07 C ANISOU 342 CA LEU A 46 1937 2215 2333 80 131 346 C ATOM 343 C LEU A 46 8.074 2.548 5.458 1.00 18.68 C ANISOU 343 C LEU A 46 2062 2534 2500 135 143 409 C ATOM 344 O LEU A 46 7.995 3.105 4.349 1.00 19.25 O ANISOU 344 O LEU A 46 2120 2636 2557 178 147 442 O ATOM 345 CB LEU A 46 10.516 2.858 5.927 1.00 15.76 C ANISOU 345 CB LEU A 46 1826 1949 2213 138 170 326 C ATOM 346 CG LEU A 46 10.341 4.084 6.846 1.00 16.40 C ANISOU 346 CG LEU A 46 1914 1999 2318 209 222 334 C ATOM 347 CD1 LEU A 46 10.476 3.732 8.326 1.00 16.04 C ANISOU 347 CD1 LEU A 46 1879 1933 2282 182 226 298 C ATOM 348 CD2 LEU A 46 11.375 5.117 6.474 1.00 15.94 C ANISOU 348 CD2 LEU A 46 1916 1848 2292 241 256 324 C ATOM 349 N LYS A 47 7.098 2.561 6.361 1.00 19.78 N ANISOU 349 N LYS A 47 2146 2749 2619 144 153 432 N ATOM 350 CA LYS A 47 5.778 3.058 6.048 1.00 23.36 C ANISOU 350 CA LYS A 47 2504 3348 3023 200 161 498 C ATOM 351 C LYS A 47 5.525 4.422 6.644 1.00 25.66 C ANISOU 351 C LYS A 47 2793 3622 3333 338 223 522 C ATOM 352 O LYS A 47 5.734 4.665 7.836 1.00 24.01 O ANISOU 352 O LYS A 47 2616 3358 3149 358 254 489 O ATOM 353 CB LYS A 47 4.710 2.062 6.525 1.00 24.80 C ANISOU 353 CB LYS A 47 2607 3665 3151 109 128 515 C ATOM 354 CG LYS A 47 3.386 2.228 5.801 1.00 28.79 C ANISOU 354 CG LYS A 47 2991 4366 3582 128 115 584 C ATOM 355 CD LYS A 47 2.287 2.664 6.742 1.00 31.86 C ANISOU 355 CD LYS A 47 3284 4886 3934 193 147 629 C ATOM 356 CE LYS A 47 1.287 1.545 6.993 1.00 34.59 C ANISOU 356 CE LYS A 47 3537 5396 4208 54 104 650 C ATOM 357 NZ LYS A 47 0.624 1.102 5.724 1.00 34.73 N ANISOU 357 NZ LYS A 47 3479 5561 4156 -19 55 686 N ATOM 358 N ASN A 48 5.061 5.318 5.792 1.00 29.07 N ANISOU 358 N ASN A 48 3196 4102 3746 439 244 580 N ATOM 359 CA ASN A 48 4.625 6.611 6.243 1.00 34.71 C ANISOU 359 CA ASN A 48 3916 4805 4469 590 307 613 C ATOM 360 C ASN A 48 3.274 6.865 5.564 1.00 38.31 C ANISOU 360 C ASN A 48 4252 5451 4853 672 304 703 C ATOM 361 O ASN A 48 2.294 6.196 5.895 1.00 42.07 O ANISOU 361 O ASN A 48 4619 6093 5272 630 280 724 O ATOM 362 CB ASN A 48 5.694 7.641 5.918 1.00 35.31 C ANISOU 362 CB ASN A 48 4110 4704 4603 646 346 598 C ATOM 363 CG ASN A 48 5.646 8.834 6.832 1.00 39.44 C ANISOU 363 CG ASN A 48 4697 5135 5153 764 416 587 C ATOM 364 OD1 ASN A 48 6.500 8.987 7.703 1.00 37.67 O ANISOU 364 OD1 ASN A 48 4557 4785 4971 725 436 516 O ATOM 365 ND2 ASN A 48 4.632 9.691 6.650 1.00 40.67 N ANISOU 365 ND2 ASN A 48 4817 5359 5278 915 455 656 N ATOM 366 N THR A 49 3.203 7.783 4.610 1.00 41.57 N ANISOU 366 N THR A 49 4676 5856 5261 782 326 764 N ATOM 367 CA THR A 49 2.016 7.837 3.756 1.00 42.55 C ANISOU 367 CA THR A 49 4673 6190 5305 843 308 857 C ATOM 368 C THR A 49 2.021 6.560 2.892 1.00 43.34 C ANISOU 368 C THR A 49 4714 6392 5359 674 230 843 C ATOM 369 O THR A 49 1.075 5.759 2.930 1.00 44.61 O ANISOU 369 O THR A 49 4759 6741 5451 599 190 861 O ATOM 370 CB THR A 49 1.977 9.108 2.893 1.00 44.77 C ANISOU 370 CB THR A 49 4988 6435 5586 1007 349 937 C ATOM 371 N VAL A 50 3.119 6.342 2.170 1.00 39.08 N ANISOU 371 N VAL A 50 4264 5729 4856 604 210 804 N ATOM 372 CA VAL A 50 3.298 5.116 1.390 1.00 36.41 C ANISOU 372 CA VAL A 50 3904 5449 4480 447 143 769 C ATOM 373 C VAL A 50 4.437 4.259 1.986 1.00 32.49 C ANISOU 373 C VAL A 50 3510 4789 4045 328 128 668 C ATOM 374 O VAL A 50 5.204 4.742 2.831 1.00 30.80 O ANISOU 374 O VAL A 50 3378 4425 3900 368 168 633 O ATOM 375 CB VAL A 50 3.533 5.443 -0.106 1.00 37.87 C ANISOU 375 CB VAL A 50 4088 5669 4631 471 128 813 C ATOM 376 CG1 VAL A 50 4.910 6.063 -0.337 1.00 37.13 C ANISOU 376 CG1 VAL A 50 4122 5374 4610 503 162 785 C ATOM 377 CG2 VAL A 50 3.315 4.210 -0.982 1.00 39.50 C ANISOU 377 CG2 VAL A 50 4245 5996 4766 321 59 784 C ATOM 378 N SER A 51 4.501 2.990 1.579 1.00 28.57 N ANISOU 378 N SER A 51 3010 4330 3515 185 73 624 N ATOM 379 CA SER A 51 5.607 2.112 1.931 1.00 25.66 C ANISOU 379 CA SER A 51 2743 3813 3195 92 57 538 C ATOM 380 C SER A 51 6.722 2.310 0.908 1.00 22.67 C ANISOU 380 C SER A 51 2433 3348 2834 106 59 515 C ATOM 381 O SER A 51 6.491 2.209 -0.299 1.00 21.73 O ANISOU 381 O SER A 51 2281 3318 2659 90 34 535 O ATOM 382 CB SER A 51 5.156 0.653 1.902 1.00 27.97 C ANISOU 382 CB SER A 51 3021 4167 3440 -61 1 502 C ATOM 383 OG SER A 51 4.039 0.458 2.759 1.00 33.41 O ANISOU 383 OG SER A 51 3629 4967 4097 -91 -2 535 O ATOM 384 N GLN A 52 7.920 2.606 1.393 1.00 19.48 N ANISOU 384 N GLN A 52 2113 2791 2497 132 88 474 N ATOM 385 CA GLN A 52 9.092 2.671 0.517 1.00 18.11 C ANISOU 385 CA GLN A 52 1999 2546 2335 131 91 447 C ATOM 386 C GLN A 52 10.067 1.575 0.929 1.00 16.57 C ANISOU 386 C GLN A 52 1872 2258 2165 58 72 365 C ATOM 387 O GLN A 52 10.076 1.167 2.087 1.00 15.91 O ANISOU 387 O GLN A 52 1807 2127 2112 35 73 340 O ATOM 388 CB GLN A 52 9.759 4.047 0.583 1.00 18.50 C ANISOU 388 CB GLN A 52 2085 2512 2431 222 145 478 C ATOM 389 CG GLN A 52 10.372 4.401 1.935 1.00 18.89 C ANISOU 389 CG GLN A 52 2187 2446 2545 235 178 442 C ATOM 390 CD GLN A 52 10.993 5.781 1.930 1.00 20.49 C ANISOU 390 CD GLN A 52 2440 2560 2785 301 231 469 C ATOM 391 OE1 GLN A 52 11.971 6.031 1.214 1.00 21.89 O ANISOU 391 OE1 GLN A 52 2653 2696 2967 286 239 465 O ATOM 392 NE2 GLN A 52 10.441 6.682 2.730 1.00 21.51 N ANISOU 392 NE2 GLN A 52 2578 2658 2935 371 270 494 N ATOM 393 N MET A 53 10.879 1.101 -0.013 1.00 15.37 N ANISOU 393 N MET A 53 1757 2089 1995 34 58 327 N ATOM 394 CA MET A 53 11.808 0.019 0.275 1.00 14.84 C ANISOU 394 CA MET A 53 1757 1938 1942 -10 43 253 C ATOM 395 C MET A 53 13.188 0.664 0.446 1.00 14.54 C ANISOU 395 C MET A 53 1754 1824 1949 42 80 240 C ATOM 396 O MET A 53 13.664 1.371 -0.459 1.00 14.31 O ANISOU 396 O MET A 53 1715 1816 1906 74 99 262 O ATOM 397 CB MET A 53 11.809 -1.000 -0.887 1.00 15.34 C ANISOU 397 CB MET A 53 1843 2040 1944 -65 7 210 C ATOM 398 CG MET A 53 12.730 -2.208 -0.675 1.00 15.46 C ANISOU 398 CG MET A 53 1944 1960 1968 -91 -5 132 C ATOM 399 SD MET A 53 12.760 -3.299 -2.111 1.00 15.95 S ANISOU 399 SD MET A 53 2054 2054 1950 -143 -37 67 S ATOM 400 CE MET A 53 13.803 -2.351 -3.228 1.00 16.22 C ANISOU 400 CE MET A 53 2060 2134 1967 -62 -3 79 C ATOM 401 N VAL A 54 13.791 0.455 1.616 1.00 13.79 N ANISOU 401 N VAL A 54 1689 1654 1897 43 89 212 N ATOM 402 CA VAL A 54 15.114 0.970 1.926 1.00 12.80 C ANISOU 402 CA VAL A 54 1585 1476 1803 73 119 195 C ATOM 403 C VAL A 54 16.131 -0.165 1.854 1.00 12.71 C ANISOU 403 C VAL A 54 1613 1436 1781 68 102 138 C ATOM 404 O VAL A 54 15.959 -1.207 2.513 1.00 13.04 O ANISOU 404 O VAL A 54 1687 1443 1826 47 79 112 O ATOM 405 CB VAL A 54 15.149 1.638 3.329 1.00 12.90 C ANISOU 405 CB VAL A 54 1597 1443 1861 83 143 203 C ATOM 406 CG1 VAL A 54 16.488 2.337 3.550 1.00 12.45 C ANISOU 406 CG1 VAL A 54 1554 1352 1825 93 173 189 C ATOM 407 CG2 VAL A 54 14.016 2.660 3.458 1.00 13.08 C ANISOU 407 CG2 VAL A 54 1592 1490 1890 110 163 256 C ATOM 408 N TYR A 55 17.198 0.005 1.063 1.00 12.49 N ANISOU 408 N TYR A 55 1585 1426 1736 92 117 123 N ATOM 409 CA TYR A 55 18.267 -1.005 1.065 1.00 12.40 C ANISOU 409 CA TYR A 55 1605 1397 1710 116 110 71 C ATOM 410 C TYR A 55 19.115 -0.873 2.325 1.00 12.13 C ANISOU 410 C TYR A 55 1566 1334 1710 131 123 67 C ATOM 411 O TYR A 55 19.575 0.206 2.648 1.00 11.67 O ANISOU 411 O TYR A 55 1475 1290 1670 125 149 88 O ATOM 412 CB TYR A 55 19.176 -0.954 -0.197 1.00 12.20 C ANISOU 412 CB TYR A 55 1568 1427 1641 145 125 55 C ATOM 413 CG TYR A 55 18.543 -1.584 -1.415 1.00 12.65 C ANISOU 413 CG TYR A 55 1645 1515 1645 133 104 33 C ATOM 414 CD1 TYR A 55 18.570 -2.956 -1.591 1.00 12.83 C ANISOU 414 CD1 TYR A 55 1732 1502 1640 140 81 -28 C ATOM 415 CD2 TYR A 55 17.882 -0.799 -2.364 1.00 12.61 C ANISOU 415 CD2 TYR A 55 1604 1574 1613 113 107 76 C ATOM 416 CE1 TYR A 55 17.963 -3.548 -2.694 1.00 13.60 C ANISOU 416 CE1 TYR A 55 1858 1627 1680 111 61 -60 C ATOM 417 CE2 TYR A 55 17.262 -1.378 -3.471 1.00 13.29 C ANISOU 417 CE2 TYR A 55 1700 1710 1637 92 84 54 C ATOM 418 CZ TYR A 55 17.323 -2.761 -3.622 1.00 13.81 C ANISOU 418 CZ TYR A 55 1833 1741 1674 83 60 -21 C ATOM 419 OH TYR A 55 16.716 -3.363 -4.670 1.00 14.48 O ANISOU 419 OH TYR A 55 1939 1871 1691 46 36 -56 O ATOM 420 N LYS A 56 19.327 -1.994 3.015 1.00 12.42 N ANISOU 420 N LYS A 56 1640 1330 1748 148 104 39 N ATOM 421 CA LYS A 56 20.185 -2.026 4.194 1.00 12.58 C ANISOU 421 CA LYS A 56 1650 1344 1787 171 110 38 C ATOM 422 C LYS A 56 21.595 -1.516 3.943 1.00 12.94 C ANISOU 422 C LYS A 56 1648 1454 1813 202 135 31 C ATOM 423 O LYS A 56 22.176 -0.868 4.809 1.00 13.14 O ANISOU 423 O LYS A 56 1637 1506 1851 187 147 40 O ATOM 424 CB LYS A 56 20.241 -3.422 4.827 1.00 13.29 C ANISOU 424 CB LYS A 56 1798 1380 1873 200 86 21 C ATOM 425 CG LYS A 56 18.979 -3.884 5.519 1.00 13.54 C ANISOU 425 CG LYS A 56 1866 1357 1921 147 64 38 C ATOM 426 CD LYS A 56 19.140 -5.333 5.984 1.00 14.63 C ANISOU 426 CD LYS A 56 2083 1425 2051 172 43 27 C ATOM 427 CE LYS A 56 17.931 -5.810 6.746 1.00 14.83 C ANISOU 427 CE LYS A 56 2141 1405 2087 102 21 53 C ATOM 428 NZ LYS A 56 18.148 -7.231 7.230 1.00 16.53 N ANISOU 428 NZ LYS A 56 2454 1531 2295 123 4 53 N ATOM 429 N HIS A 57 22.141 -1.773 2.757 1.00 13.27 N ANISOU 429 N HIS A 57 1687 1537 1818 237 142 12 N ATOM 430 CA HIS A 57 23.495 -1.316 2.447 1.00 13.65 C ANISOU 430 CA HIS A 57 1675 1673 1836 261 167 11 C ATOM 431 C HIS A 57 23.616 0.196 2.505 1.00 13.10 C ANISOU 431 C HIS A 57 1560 1635 1782 190 192 45 C ATOM 432 O HIS A 57 24.718 0.709 2.684 1.00 13.69 O ANISOU 432 O HIS A 57 1581 1784 1838 177 211 50 O ATOM 433 CB HIS A 57 24.010 -1.822 1.092 1.00 14.89 C ANISOU 433 CB HIS A 57 1833 1884 1940 313 176 -15 C ATOM 434 CG HIS A 57 23.198 -1.381 -0.085 1.00 14.88 C ANISOU 434 CG HIS A 57 1842 1886 1927 275 179 -5 C ATOM 435 ND1 HIS A 57 22.627 -2.282 -0.958 1.00 15.76 N ANISOU 435 ND1 HIS A 57 2007 1975 2007 297 162 -40 N ATOM 436 CD2 HIS A 57 22.889 -0.143 -0.562 1.00 14.75 C ANISOU 436 CD2 HIS A 57 1794 1896 1917 218 196 40 C ATOM 437 CE1 HIS A 57 21.964 -1.623 -1.891 1.00 15.37 C ANISOU 437 CE1 HIS A 57 1942 1956 1941 254 164 -15 C ATOM 438 NE2 HIS A 57 22.118 -0.321 -1.682 1.00 14.62 N ANISOU 438 NE2 HIS A 57 1797 1887 1870 215 186 39 N ATOM 439 N ALA A 58 22.480 0.895 2.385 1.00 12.14 N ANISOU 439 N ALA A 58 1463 1461 1691 146 194 71 N ATOM 440 CA ALA A 58 22.441 2.362 2.431 1.00 12.28 C ANISOU 440 CA ALA A 58 1466 1472 1727 88 222 107 C ATOM 441 C ALA A 58 22.208 2.953 3.828 1.00 11.86 C ANISOU 441 C ALA A 58 1425 1369 1712 52 227 106 C ATOM 442 O ALA A 58 22.256 4.168 4.014 1.00 11.74 O ANISOU 442 O ALA A 58 1418 1330 1712 3 255 125 O ATOM 443 CB ALA A 58 21.399 2.886 1.451 1.00 12.39 C ANISOU 443 CB ALA A 58 1500 1465 1743 84 227 144 C ATOM 444 N ILE A 59 21.982 2.091 4.814 1.00 11.17 N ANISOU 444 N ILE A 59 1346 1262 1634 74 203 84 N ATOM 445 CA ILE A 59 21.589 2.572 6.130 1.00 11.05 C ANISOU 445 CA ILE A 59 1342 1209 1646 45 207 82 C ATOM 446 C ILE A 59 22.794 2.612 7.045 1.00 11.35 C ANISOU 446 C ILE A 59 1345 1301 1665 23 209 60 C ATOM 447 O ILE A 59 23.625 1.682 7.031 1.00 11.72 O ANISOU 447 O ILE A 59 1363 1406 1683 64 192 49 O ATOM 448 CB ILE A 59 20.514 1.650 6.736 1.00 10.30 C ANISOU 448 CB ILE A 59 1273 1076 1565 69 180 81 C ATOM 449 CG1 ILE A 59 19.272 1.622 5.827 1.00 10.45 C ANISOU 449 CG1 ILE A 59 1309 1071 1589 77 175 105 C ATOM 450 CG2 ILE A 59 20.179 2.019 8.190 1.00 9.96 C ANISOU 450 CG2 ILE A 59 1233 1015 1537 46 185 76 C ATOM 451 CD1 ILE A 59 18.226 0.617 6.301 1.00 10.64 C ANISOU 451 CD1 ILE A 59 1351 1075 1615 79 146 107 C ATOM 452 N SER A 60 22.905 3.685 7.821 1.00 11.76 N ANISOU 452 N SER A 60 1403 1340 1727 -38 230 52 N ATOM 453 CA ASER A 60 23.872 3.694 8.923 0.50 11.89 C ANISOU 453 CA ASER A 60 1381 1420 1716 -72 224 27 C ATOM 454 CA BSER A 60 23.856 3.724 8.940 0.50 11.86 C ANISOU 454 CA BSER A 60 1379 1414 1713 -74 225 27 C ATOM 455 C SER A 60 23.232 3.170 10.211 1.00 11.60 C ANISOU 455 C SER A 60 1359 1362 1686 -54 206 17 C ATOM 456 O SER A 60 23.763 2.225 10.811 1.00 12.15 O ANISOU 456 O SER A 60 1396 1490 1730 -19 181 17 O ATOM 457 CB ASER A 60 24.506 5.076 9.123 0.50 12.55 C ANISOU 457 CB ASER A 60 1467 1512 1790 -171 255 12 C ATOM 458 CB BSER A 60 24.358 5.145 9.184 0.50 12.44 C ANISOU 458 CB BSER A 60 1462 1485 1781 -172 257 11 C ATOM 459 OG ASER A 60 23.517 6.055 9.331 0.50 12.59 O ANISOU 459 OG ASER A 60 1542 1410 1831 -196 281 10 O ATOM 460 OG BSER A 60 25.100 5.571 8.071 0.50 12.70 O ANISOU 460 OG BSER A 60 1473 1556 1797 -202 273 29 O ATOM 461 N THR A 61 22.097 3.744 10.608 1.00 11.34 N ANISOU 461 N THR A 61 1371 1255 1683 -66 220 16 N ATOM 462 CA THR A 61 21.457 3.416 11.902 1.00 11.53 C ANISOU 462 CA THR A 61 1402 1274 1704 -59 210 8 C ATOM 463 C THR A 61 19.954 3.331 11.823 1.00 11.38 C ANISOU 463 C THR A 61 1415 1195 1713 -28 214 28 C ATOM 464 O THR A 61 19.327 3.960 10.949 1.00 12.02 O ANISOU 464 O THR A 61 1519 1232 1817 -17 234 43 O ATOM 465 CB THR A 61 21.808 4.444 13.004 1.00 11.90 C ANISOU 465 CB THR A 61 1455 1332 1733 -125 232 -33 C ATOM 466 OG1 THR A 61 21.303 5.734 12.629 1.00 12.18 O ANISOU 466 OG1 THR A 61 1545 1288 1794 -151 272 -44 O ATOM 467 CG2 THR A 61 23.348 4.549 13.172 1.00 12.46 C ANISOU 467 CG2 THR A 61 1475 1497 1762 -177 224 -52 C ATOM 468 N VAL A 62 19.374 2.612 12.781 1.00 11.29 N ANISOU 468 N VAL A 62 1398 1198 1692 -15 196 35 N ATOM 469 CA VAL A 62 17.915 2.559 12.978 1.00 11.61 C ANISOU 469 CA VAL A 62 1452 1216 1745 3 202 55 C ATOM 470 C VAL A 62 17.677 2.843 14.473 1.00 11.96 C ANISOU 470 C VAL A 62 1491 1287 1767 -14 213 35 C ATOM 471 O VAL A 62 18.299 2.222 15.331 1.00 11.82 O ANISOU 471 O VAL A 62 1456 1315 1722 -27 192 31 O ATOM 472 CB VAL A 62 17.330 1.201 12.560 1.00 11.13 C ANISOU 472 CB VAL A 62 1390 1156 1684 20 166 91 C ATOM 473 CG1 VAL A 62 15.829 1.156 12.817 1.00 10.71 C ANISOU 473 CG1 VAL A 62 1330 1110 1629 19 170 117 C ATOM 474 CG2 VAL A 62 17.622 0.902 11.091 1.00 11.30 C ANISOU 474 CG2 VAL A 62 1421 1158 1715 35 156 98 C ATOM 475 N VAL A 63 16.853 3.845 14.782 1.00 13.27 N ANISOU 475 N VAL A 63 1673 1431 1937 -4 250 21 N ATOM 476 CA VAL A 63 16.670 4.271 16.186 1.00 13.60 C ANISOU 476 CA VAL A 63 1717 1502 1948 -18 269 -13 C ATOM 477 C VAL A 63 15.230 4.767 16.405 1.00 13.26 C ANISOU 477 C VAL A 63 1677 1455 1905 29 302 -3 C ATOM 478 O VAL A 63 14.644 5.374 15.499 1.00 13.36 O ANISOU 478 O VAL A 63 1707 1426 1945 69 324 14 O ATOM 479 CB VAL A 63 17.738 5.338 16.605 1.00 14.53 C ANISOU 479 CB VAL A 63 1864 1603 2052 -66 293 -75 C ATOM 480 CG1 VAL A 63 17.605 6.617 15.791 1.00 14.89 C ANISOU 480 CG1 VAL A 63 1968 1561 2130 -59 336 -91 C ATOM 481 CG2 VAL A 63 17.704 5.629 18.100 1.00 15.87 C ANISOU 481 CG2 VAL A 63 2035 1818 2175 -90 307 -121 C ATOM 482 N PRO A 64 14.642 4.497 17.590 1.00 13.44 N ANISOU 482 N PRO A 64 1677 1538 1891 30 306 -6 N ATOM 483 CA PRO A 64 13.350 5.111 17.794 1.00 13.54 C ANISOU 483 CA PRO A 64 1686 1565 1895 87 345 -2 C ATOM 484 C PRO A 64 13.460 6.629 17.698 1.00 13.72 C ANISOU 484 C PRO A 64 1774 1509 1931 122 400 -54 C ATOM 485 O PRO A 64 14.440 7.207 18.153 1.00 13.80 O ANISOU 485 O PRO A 64 1830 1481 1933 75 411 -114 O ATOM 486 CB PRO A 64 12.988 4.691 19.224 1.00 14.46 C ANISOU 486 CB PRO A 64 1769 1768 1958 73 346 -9 C ATOM 487 CG PRO A 64 13.596 3.315 19.335 1.00 13.75 C ANISOU 487 CG PRO A 64 1653 1711 1861 18 290 30 C ATOM 488 CD PRO A 64 14.947 3.492 18.638 1.00 13.68 C ANISOU 488 CD PRO A 64 1675 1639 1882 -5 274 5 C ATOM 489 N ASER A 65 12.457 7.259 17.090 0.38 13.43 N ANISOU 489 N ASER A 65 1746 1449 1909 201 433 -29 N ATOM 490 N CSER A 65 12.466 7.246 17.066 0.62 14.66 N ANISOU 490 N CSER A 65 1901 1604 2065 200 432 -28 N ATOM 491 CA ASER A 65 12.410 8.713 16.962 0.38 13.73 C ANISOU 491 CA ASER A 65 1866 1390 1960 255 493 -67 C ATOM 492 CA CSER A 65 12.398 8.690 16.955 0.62 16.03 C ANISOU 492 CA CSER A 65 2155 1683 2251 255 492 -66 C ATOM 493 C ASER A 65 12.307 9.405 18.329 0.38 14.43 C ANISOU 493 C ASER A 65 1997 1477 2007 268 537 -143 C ATOM 494 C CSER A 65 11.793 9.318 18.216 0.62 16.83 C ANISOU 494 C CSER A 65 2279 1805 2309 304 541 -119 C ATOM 495 O ASER A 65 12.592 10.601 18.458 0.38 14.40 O ANISOU 495 O ASER A 65 2093 1369 2008 283 586 -201 O ATOM 496 O CSER A 65 11.631 8.679 19.239 0.62 15.72 O ANISOU 496 O CSER A 65 2088 1759 2125 278 527 -132 O ATOM 497 CB ASER A 65 11.233 9.115 16.065 0.38 13.96 C ANISOU 497 CB ASER A 65 1881 1419 2003 363 518 -7 C ATOM 498 CB CSER A 65 11.541 9.061 15.750 0.62 17.20 C ANISOU 498 CB CSER A 65 2299 1810 2426 342 507 -2 C ATOM 499 OG ASER A 65 11.503 8.767 14.711 0.38 13.38 O ANISOU 499 OG ASER A 65 1793 1327 1964 344 484 47 O ATOM 500 OG CSER A 65 11.082 10.396 15.840 0.62 20.55 O ANISOU 500 OG CSER A 65 2801 2155 2853 435 574 -24 O TER 501 SER A 65 ATOM 502 N GLY B 4 40.840 -14.038 10.590 1.00 44.66 N ANISOU 502 N GLY B 4 5859 5219 5892 1558 -178 -463 N ATOM 503 CA GLY B 4 39.441 -14.209 11.066 1.00 44.88 C ANISOU 503 CA GLY B 4 5977 5067 6008 1402 -237 -457 C ATOM 504 C GLY B 4 38.968 -12.966 11.789 1.00 42.87 C ANISOU 504 C GLY B 4 5649 4891 5748 1221 -200 -357 C ATOM 505 O GLY B 4 39.321 -11.857 11.402 1.00 42.32 O ANISOU 505 O GLY B 4 5489 4986 5603 1193 -140 -338 O ATOM 506 N GLN B 5 38.171 -13.157 12.841 1.00 41.34 N ANISOU 506 N GLN B 5 5495 4578 5634 1104 -235 -289 N ATOM 507 CA GLN B 5 37.686 -12.053 13.675 1.00 37.69 C ANISOU 507 CA GLN B 5 4976 4180 5164 949 -204 -200 C ATOM 508 C GLN B 5 38.479 -11.966 14.984 1.00 36.35 C ANISOU 508 C GLN B 5 4751 4065 4996 947 -196 -94 C ATOM 509 O GLN B 5 37.976 -11.457 15.997 1.00 33.71 O ANISOU 509 O GLN B 5 4405 3733 4672 834 -193 -18 O ATOM 510 N SER B 6 39.720 -12.455 14.934 1.00 35.83 N ANISOU 510 N SER B 6 4650 4056 4910 1084 -194 -94 N ATOM 511 CA SER B 6 40.616 -12.534 16.091 1.00 35.23 C ANISOU 511 CA SER B 6 4516 4040 4830 1110 -200 1 C ATOM 512 C SER B 6 40.990 -11.191 16.723 1.00 32.65 C ANISOU 512 C SER B 6 4086 3872 4446 1008 -168 63 C ATOM 513 O SER B 6 41.541 -11.162 17.825 1.00 32.87 O ANISOU 513 O SER B 6 4072 3949 4466 1002 -186 140 O ATOM 514 CB SER B 6 41.894 -13.285 15.710 1.00 36.80 C ANISOU 514 CB SER B 6 4682 4287 5012 1295 -201 -19 C ATOM 515 OG SER B 6 42.610 -12.599 14.693 1.00 37.40 O ANISOU 515 OG SER B 6 4670 4526 5015 1347 -148 -66 O ATOM 516 N LEU B 7 40.728 -10.089 16.020 1.00 30.06 N ANISOU 516 N LEU B 7 3719 3622 4078 933 -128 28 N ATOM 517 CA LEU B 7 40.912 -8.755 16.600 1.00 28.12 C ANISOU 517 CA LEU B 7 3399 3490 3796 818 -109 76 C ATOM 518 C LEU B 7 39.558 -8.127 16.945 1.00 25.46 C ANISOU 518 C LEU B 7 3120 3079 3472 685 -107 76 C ATOM 519 O LEU B 7 39.333 -7.674 18.073 1.00 24.45 O ANISOU 519 O LEU B 7 2991 2960 3337 608 -120 127 O ATOM 520 CB LEU B 7 41.703 -7.842 15.646 1.00 29.21 C ANISOU 520 CB LEU B 7 3438 3774 3885 827 -64 60 C ATOM 521 CG LEU B 7 42.663 -6.748 16.159 1.00 30.61 C ANISOU 521 CG LEU B 7 3498 4098 4034 760 -59 120 C ATOM 522 CD1 LEU B 7 42.814 -5.634 15.131 1.00 30.04 C ANISOU 522 CD1 LEU B 7 3362 4118 3935 709 -10 114 C ATOM 523 CD2 LEU B 7 42.345 -6.167 17.533 1.00 28.63 C ANISOU 523 CD2 LEU B 7 3262 3828 3789 646 -97 162 C ATOM 524 N GLN B 8 38.656 -8.118 15.967 1.00 24.68 N ANISOU 524 N GLN B 8 3072 2920 3387 669 -93 18 N ATOM 525 CA GLN B 8 37.376 -7.426 16.075 1.00 23.00 C ANISOU 525 CA GLN B 8 2897 2660 3182 555 -83 15 C ATOM 526 C GLN B 8 36.497 -7.914 17.241 1.00 22.55 C ANISOU 526 C GLN B 8 2895 2509 3163 502 -109 66 C ATOM 527 O GLN B 8 35.977 -7.120 18.023 1.00 22.72 O ANISOU 527 O GLN B 8 2912 2555 3166 419 -97 102 O ATOM 528 CB GLN B 8 36.608 -7.530 14.746 1.00 22.51 C ANISOU 528 CB GLN B 8 2874 2554 3125 566 -75 -57 C ATOM 529 CG GLN B 8 35.448 -6.550 14.704 1.00 20.95 C ANISOU 529 CG GLN B 8 2688 2349 2924 458 -57 -53 C ATOM 530 CD GLN B 8 34.453 -6.728 13.566 1.00 20.04 C ANISOU 530 CD GLN B 8 2613 2183 2817 457 -65 -115 C ATOM 531 OE1 GLN B 8 33.346 -6.215 13.655 1.00 19.36 O ANISOU 531 OE1 GLN B 8 2541 2072 2744 379 -61 -105 O ATOM 532 NE2 GLN B 8 34.833 -7.416 12.504 1.00 20.61 N ANISOU 532 NE2 GLN B 8 2702 2253 2876 549 -78 -182 N ATOM 533 N ASP B 9 36.315 -9.222 17.362 1.00 22.28 N ANISOU 533 N ASP B 9 2916 2367 3184 554 -144 74 N ATOM 534 CA ASP B 9 35.456 -9.734 18.425 1.00 22.08 C ANISOU 534 CA ASP B 9 2934 2256 3198 499 -162 146 C ATOM 535 C ASP B 9 36.014 -9.495 19.850 1.00 21.33 C ANISOU 535 C ASP B 9 2807 2233 3062 491 -162 231 C ATOM 536 O ASP B 9 35.275 -9.086 20.739 1.00 21.04 O ANISOU 536 O ASP B 9 2778 2209 3007 419 -149 283 O ATOM 537 CB ASP B 9 35.116 -11.220 18.200 1.00 24.93 C ANISOU 537 CB ASP B 9 3366 2461 3645 544 -208 145 C ATOM 538 CG ASP B 9 34.182 -11.442 17.008 1.00 26.96 C ANISOU 538 CG ASP B 9 3666 2634 3945 519 -225 63 C ATOM 539 OD1 ASP B 9 33.665 -10.470 16.456 1.00 27.87 O ANISOU 539 OD1 ASP B 9 3754 2813 4022 463 -195 25 O ATOM 540 OD2 ASP B 9 33.974 -12.609 16.615 1.00 29.89 O ANISOU 540 OD2 ASP B 9 4101 2867 4388 558 -276 35 O ATOM 541 N PRO B 10 37.315 -9.741 20.078 1.00 20.83 N ANISOU 541 N PRO B 10 2706 2233 2976 573 -178 244 N ATOM 542 CA PRO B 10 37.760 -9.473 21.460 1.00 20.57 C ANISOU 542 CA PRO B 10 2644 2279 2893 560 -189 321 C ATOM 543 C PRO B 10 37.762 -7.972 21.788 1.00 19.16 C ANISOU 543 C PRO B 10 2421 2212 2646 477 -169 300 C ATOM 544 O PRO B 10 37.467 -7.599 22.919 1.00 18.77 O ANISOU 544 O PRO B 10 2380 2201 2551 434 -174 345 O ATOM 545 CB PRO B 10 39.186 -10.046 21.501 1.00 21.52 C ANISOU 545 CB PRO B 10 2719 2453 3007 671 -217 336 C ATOM 546 CG PRO B 10 39.231 -11.032 20.380 1.00 22.56 C ANISOU 546 CG PRO B 10 2889 2482 3201 758 -222 285 C ATOM 547 CD PRO B 10 38.295 -10.538 19.319 1.00 21.40 C ANISOU 547 CD PRO B 10 2769 2293 3068 694 -194 207 C ATOM 548 N PHE B 11 38.062 -7.136 20.800 1.00 18.74 N ANISOU 548 N PHE B 11 2329 2207 2584 458 -149 234 N ATOM 549 CA PHE B 11 38.045 -5.666 20.993 1.00 18.50 C ANISOU 549 CA PHE B 11 2267 2254 2507 374 -136 211 C ATOM 550 C PHE B 11 36.663 -5.184 21.409 1.00 17.63 C ANISOU 550 C PHE B 11 2214 2095 2389 304 -114 212 C ATOM 551 O PHE B 11 36.516 -4.470 22.387 1.00 17.61 O ANISOU 551 O PHE B 11 2217 2137 2336 262 -121 223 O ATOM 552 CB PHE B 11 38.511 -4.944 19.727 1.00 18.99 C ANISOU 552 CB PHE B 11 2280 2359 2575 366 -112 160 C ATOM 553 CG PHE B 11 38.649 -3.442 19.875 1.00 19.12 C ANISOU 553 CG PHE B 11 2265 2436 2562 278 -109 145 C ATOM 554 CD1 PHE B 11 37.578 -2.602 19.590 1.00 18.73 C ANISOU 554 CD1 PHE B 11 2260 2342 2515 214 -82 117 C ATOM 555 CD2 PHE B 11 39.859 -2.873 20.274 1.00 20.30 C ANISOU 555 CD2 PHE B 11 2340 2683 2690 259 -141 160 C ATOM 556 CE1 PHE B 11 37.712 -1.222 19.699 1.00 19.36 C ANISOU 556 CE1 PHE B 11 2324 2453 2579 140 -85 101 C ATOM 557 CE2 PHE B 11 39.995 -1.486 20.383 1.00 19.86 C ANISOU 557 CE2 PHE B 11 2264 2659 2624 167 -151 142 C ATOM 558 CZ PHE B 11 38.916 -0.672 20.109 1.00 19.99 C ANISOU 558 CZ PHE B 11 2339 2610 2645 111 -123 111 C ATOM 559 N LEU B 12 35.643 -5.572 20.656 1.00 17.23 N ANISOU 559 N LEU B 12 2202 1961 2384 296 -91 195 N ATOM 560 CA LEU B 12 34.279 -5.159 20.951 1.00 16.71 C ANISOU 560 CA LEU B 12 2173 1861 2315 237 -66 203 C ATOM 561 C LEU B 12 33.746 -5.777 22.254 1.00 18.26 C ANISOU 561 C LEU B 12 2396 2044 2497 235 -70 282 C ATOM 562 O LEU B 12 33.065 -5.100 23.049 1.00 18.48 O ANISOU 562 O LEU B 12 2435 2111 2477 200 -48 300 O ATOM 563 CB LEU B 12 33.354 -5.478 19.761 1.00 16.14 C ANISOU 563 CB LEU B 12 2121 1713 2298 226 -52 169 C ATOM 564 CG LEU B 12 33.562 -4.601 18.515 1.00 15.88 C ANISOU 564 CG LEU B 12 2064 1712 2256 220 -34 104 C ATOM 565 CD1 LEU B 12 32.640 -5.057 17.380 1.00 15.58 C ANISOU 565 CD1 LEU B 12 2050 1609 2261 221 -34 68 C ATOM 566 CD2 LEU B 12 33.281 -3.143 18.854 1.00 15.12 C ANISOU 566 CD2 LEU B 12 1960 1666 2119 165 -10 96 C ATOM 567 N ASN B 13 34.044 -7.063 22.470 1.00 19.02 N ANISOU 567 N ASN B 13 2505 2088 2633 281 -95 334 N ATOM 568 CA ASN B 13 33.615 -7.755 23.688 1.00 21.14 C ANISOU 568 CA ASN B 13 2794 2346 2891 283 -97 434 C ATOM 569 C ASN B 13 34.137 -7.121 24.948 1.00 21.23 C ANISOU 569 C ASN B 13 2791 2472 2803 291 -103 463 C ATOM 570 O ASN B 13 33.393 -6.999 25.919 1.00 21.91 O ANISOU 570 O ASN B 13 2892 2594 2840 273 -79 521 O ATOM 571 CB ASN B 13 33.996 -9.249 23.678 1.00 22.55 C ANISOU 571 CB ASN B 13 2996 2433 3139 339 -132 492 C ATOM 572 CG ASN B 13 32.921 -10.116 23.036 1.00 24.37 C ANISOU 572 CG ASN B 13 3263 2527 3469 305 -135 507 C ATOM 573 OD1 ASN B 13 31.732 -9.951 23.319 1.00 25.54 O ANISOU 573 OD1 ASN B 13 3412 2665 3626 236 -108 549 O ATOM 574 ND2 ASN B 13 33.329 -11.014 22.137 1.00 24.56 N ANISOU 574 ND2 ASN B 13 3314 2450 3569 354 -172 465 N ATOM 575 N ALA B 14 35.406 -6.709 24.925 1.00 21.15 N ANISOU 575 N ALA B 14 2747 2531 2758 321 -135 421 N ATOM 576 CA ALA B 14 36.022 -6.034 26.068 1.00 22.08 C ANISOU 576 CA ALA B 14 2849 2762 2778 323 -160 428 C ATOM 577 C ALA B 14 35.321 -4.709 26.376 1.00 22.22 C ANISOU 577 C ALA B 14 2884 2822 2735 267 -136 374 C ATOM 578 O ALA B 14 34.969 -4.453 27.539 1.00 22.77 O ANISOU 578 O ALA B 14 2977 2954 2719 272 -135 403 O ATOM 579 CB ALA B 14 37.527 -5.833 25.861 1.00 22.28 C ANISOU 579 CB ALA B 14 2817 2854 2795 352 -208 395 C ATOM 580 N LEU B 15 35.073 -3.898 25.341 1.00 21.03 N ANISOU 580 N LEU B 15 2729 2638 2623 225 -116 299 N ATOM 581 CA LEU B 15 34.296 -2.657 25.509 1.00 20.45 C ANISOU 581 CA LEU B 15 2682 2579 2507 183 -91 246 C ATOM 582 C LEU B 15 32.919 -2.941 26.098 1.00 21.20 C ANISOU 582 C LEU B 15 2812 2665 2579 188 -42 299 C ATOM 583 O LEU B 15 32.455 -2.237 26.993 1.00 21.52 O ANISOU 583 O LEU B 15 2877 2762 2536 194 -29 288 O ATOM 584 CB LEU B 15 34.131 -1.916 24.179 1.00 20.16 C ANISOU 584 CB LEU B 15 2636 2495 2529 145 -71 182 C ATOM 585 CG LEU B 15 35.465 -1.400 23.604 1.00 19.68 C ANISOU 585 CG LEU B 15 2529 2464 2486 129 -109 141 C ATOM 586 CD1 LEU B 15 35.262 -0.935 22.167 1.00 19.62 C ANISOU 586 CD1 LEU B 15 2507 2412 2535 104 -79 106 C ATOM 587 CD2 LEU B 15 36.072 -0.292 24.469 1.00 20.75 C ANISOU 587 CD2 LEU B 15 2667 2658 2561 94 -154 100 C ATOM 588 N ARG B 16 32.278 -3.986 25.589 1.00 21.25 N ANISOU 588 N ARG B 16 2814 2602 2658 189 -19 357 N ATOM 589 CA ARG B 16 30.952 -4.366 26.066 1.00 22.91 C ANISOU 589 CA ARG B 16 3033 2805 2865 181 28 429 C ATOM 590 C ARG B 16 30.976 -4.799 27.522 1.00 24.60 C ANISOU 590 C ARG B 16 3256 3095 2996 216 31 519 C ATOM 591 O ARG B 16 30.220 -4.268 28.339 1.00 24.24 O ANISOU 591 O ARG B 16 3220 3122 2868 226 70 538 O ATOM 592 CB ARG B 16 30.370 -5.462 25.177 1.00 24.73 C ANISOU 592 CB ARG B 16 3256 2933 3209 159 31 472 C ATOM 593 CG ARG B 16 29.005 -5.953 25.625 1.00 27.51 C ANISOU 593 CG ARG B 16 3599 3277 3578 131 73 567 C ATOM 594 CD ARG B 16 28.589 -7.037 24.657 1.00 29.66 C ANISOU 594 CD ARG B 16 3866 3426 3976 96 51 590 C ATOM 595 NE ARG B 16 28.195 -8.239 25.365 1.00 36.43 N ANISOU 595 NE ARG B 16 4722 4243 4875 83 49 722 N ATOM 596 CZ ARG B 16 29.035 -9.102 25.945 1.00 37.73 C ANISOU 596 CZ ARG B 16 4908 4383 5044 122 17 785 C ATOM 597 NH1 ARG B 16 30.360 -8.934 25.917 1.00 38.86 N ANISOU 597 NH1 ARG B 16 5066 4551 5149 180 -17 723 N ATOM 598 NH2 ARG B 16 28.535 -10.160 26.550 1.00 39.82 N ANISOU 598 NH2 ARG B 16 5172 4600 5358 101 19 922 N ATOM 599 N ARG B 17 31.866 -5.745 27.839 1.00 25.07 N ANISOU 599 N ARG B 17 3312 3145 3068 246 -10 574 N ATOM 600 CA AARG B 17 32.022 -6.313 29.191 0.50 26.78 C ANISOU 600 CA AARG B 17 3534 3435 3205 288 -15 679 C ATOM 601 CA BARG B 17 31.923 -6.285 29.192 0.50 26.62 C ANISOU 601 CA BARG B 17 3514 3415 3184 286 -10 680 C ATOM 602 C ARG B 17 32.324 -5.239 30.228 1.00 27.29 C ANISOU 602 C ARG B 17 3613 3633 3122 316 -24 629 C ATOM 603 O ARG B 17 31.787 -5.246 31.338 1.00 28.73 O ANISOU 603 O ARG B 17 3808 3905 3205 346 6 696 O ATOM 604 CB AARG B 17 33.191 -7.300 29.225 0.50 27.11 C ANISOU 604 CB AARG B 17 3569 3449 3282 330 -71 723 C ATOM 605 CB BARG B 17 32.823 -7.524 29.253 0.50 26.73 C ANISOU 605 CB BARG B 17 3525 3383 3250 323 -56 754 C ATOM 606 CG AARG B 17 32.990 -8.649 28.569 0.50 27.40 C ANISOU 606 CG AARG B 17 3612 3350 3450 329 -75 794 C ATOM 607 CG BARG B 17 32.141 -8.786 28.747 0.50 27.18 C ANISOU 607 CG BARG B 17 3588 3308 3431 303 -43 843 C ATOM 608 CD AARG B 17 34.295 -9.414 28.711 0.50 28.11 C ANISOU 608 CD AARG B 17 3696 3432 3552 398 -133 822 C ATOM 609 CD BARG B 17 33.142 -9.727 28.097 0.50 27.08 C ANISOU 609 CD BARG B 17 3581 3200 3506 344 -97 837 C ATOM 610 NE AARG B 17 35.070 -8.823 29.798 0.50 28.43 N ANISOU 610 NE AARG B 17 3721 3619 3461 435 -159 824 N ATOM 611 NE BARG B 17 32.502 -10.850 27.421 0.50 27.15 N ANISOU 611 NE BARG B 17 3613 3054 3649 319 -100 887 N ATOM 612 CZ AARG B 17 36.278 -8.285 29.663 0.50 27.80 C ANISOU 612 CZ AARG B 17 3610 3606 3349 459 -208 746 C ATOM 613 CZ BARG B 17 33.114 -11.614 26.522 0.50 27.55 C ANISOU 613 CZ BARG B 17 3683 2993 3794 355 -143 846 C ATOM 614 NH1AARG B 17 36.895 -8.306 28.489 0.50 26.83 N ANISOU 614 NH1AARG B 17 3462 3424 3308 462 -224 672 N ATOM 615 NH1BARG B 17 34.377 -11.367 26.209 0.50 27.52 N ANISOU 615 NH1BARG B 17 3662 3035 3760 421 -173 771 N ATOM 616 NH2AARG B 17 36.883 -7.757 30.719 0.50 28.01 N ANISOU 616 NH2AARG B 17 3623 3766 3255 482 -245 746 N ATOM 617 NH2BARG B 17 32.476 -12.631 25.948 0.50 28.12 N ANISOU 617 NH2BARG B 17 3787 2908 3988 329 -159 879 N ATOM 618 N GLU B 18 33.228 -4.335 29.866 1.00 28.03 N ANISOU 618 N GLU B 18 3705 3743 3204 305 -71 513 N ATOM 619 CA GLU B 18 33.702 -3.302 30.785 1.00 29.82 C ANISOU 619 CA GLU B 18 3951 4076 3304 322 -108 443 C ATOM 620 C GLU B 18 32.853 -2.022 30.761 1.00 29.37 C ANISOU 620 C GLU B 18 3930 4026 3203 305 -73 351 C ATOM 621 O GLU B 18 33.162 -1.072 31.478 1.00 29.15 O ANISOU 621 O GLU B 18 3935 4066 3075 320 -110 271 O ATOM 622 CB GLU B 18 35.196 -3.000 30.544 1.00 31.60 C ANISOU 622 CB GLU B 18 4147 4318 3542 310 -190 377 C ATOM 623 CG GLU B 18 36.141 -4.163 30.872 1.00 35.73 C ANISOU 623 CG GLU B 18 4634 4868 4073 356 -233 466 C ATOM 624 CD GLU B 18 37.440 -4.153 30.066 1.00 38.07 C ANISOU 624 CD GLU B 18 4873 5151 4440 344 -288 422 C ATOM 625 OE1 GLU B 18 37.676 -3.210 29.262 1.00 39.05 O ANISOU 625 OE1 GLU B 18 4981 5250 4606 289 -295 329 O ATOM 626 OE2 GLU B 18 38.238 -5.108 30.230 1.00 40.99 O ANISOU 626 OE2 GLU B 18 5209 5540 4825 396 -321 492 O ATOM 627 N ARG B 19 31.778 -2.007 29.959 1.00 28.75 N ANISOU 627 N ARG B 19 3848 3877 3199 281 -9 360 N ATOM 628 CA ARG B 19 30.850 -0.859 29.885 1.00 29.00 C ANISOU 628 CA ARG B 19 3910 3912 3197 282 32 287 C ATOM 629 C ARG B 19 31.590 0.444 29.592 1.00 26.94 C ANISOU 629 C ARG B 19 3678 3629 2929 256 -23 153 C ATOM 630 O ARG B 19 31.289 1.482 30.168 1.00 26.66 O ANISOU 630 O ARG B 19 3692 3626 2811 282 -25 76 O ATOM 631 CB ARG B 19 30.030 -0.704 31.182 1.00 32.37 C ANISOU 631 CB ARG B 19 4363 4449 3488 347 78 325 C ATOM 632 CG ARG B 19 29.595 -2.016 31.808 1.00 36.50 C ANISOU 632 CG ARG B 19 4854 5019 3995 369 118 483 C ATOM 633 CD ARG B 19 28.231 -2.455 31.317 1.00 39.86 C ANISOU 633 CD ARG B 19 5241 5410 4494 348 198 567 C ATOM 634 NE ARG B 19 27.204 -2.188 32.321 1.00 44.13 N ANISOU 634 NE ARG B 19 5781 6073 4915 408 271 620 N ATOM 635 CZ ARG B 19 26.004 -2.768 32.362 1.00 47.53 C ANISOU 635 CZ ARG B 19 6157 6527 5374 400 347 744 C ATOM 636 NH1 ARG B 19 25.646 -3.668 31.449 1.00 46.78 N ANISOU 636 NH1 ARG B 19 6016 6326 5433 324 349 818 N ATOM 637 NH2 ARG B 19 25.154 -2.447 33.334 1.00 49.32 N ANISOU 637 NH2 ARG B 19 6374 6892 5472 470 420 793 N ATOM 638 N VAL B 20 32.569 0.372 28.694 1.00 24.37 N ANISOU 638 N VAL B 20 3320 3247 2692 208 -68 128 N ATOM 639 CA VAL B 20 33.396 1.528 28.366 1.00 23.94 C ANISOU 639 CA VAL B 20 3276 3169 2650 164 -126 26 C ATOM 640 C VAL B 20 32.571 2.448 27.465 1.00 21.79 C ANISOU 640 C VAL B 20 3028 2820 2433 142 -84 -25 C ATOM 641 O VAL B 20 31.999 1.985 26.484 1.00 20.78 O ANISOU 641 O VAL B 20 2872 2642 2382 132 -36 17 O ATOM 642 CB VAL B 20 34.678 1.096 27.618 1.00 23.91 C ANISOU 642 CB VAL B 20 3209 3151 2725 125 -174 40 C ATOM 643 CG1 VAL B 20 35.504 2.305 27.225 1.00 24.76 C ANISOU 643 CG1 VAL B 20 3312 3237 2861 63 -230 -43 C ATOM 644 CG2 VAL B 20 35.519 0.154 28.483 1.00 24.40 C ANISOU 644 CG2 VAL B 20 3243 3291 2737 161 -219 98 C ATOM 645 N PRO B 21 32.477 3.749 27.809 1.00 21.58 N ANISOU 645 N PRO B 21 3057 2778 2364 139 -108 -117 N ATOM 646 CA PRO B 21 31.851 4.659 26.845 1.00 21.23 C ANISOU 646 CA PRO B 21 3033 2647 2385 119 -77 -157 C ATOM 647 C PRO B 21 32.684 4.692 25.557 1.00 20.43 C ANISOU 647 C PRO B 21 2879 2490 2393 48 -98 -145 C ATOM 648 O PRO B 21 33.917 4.790 25.623 1.00 20.83 O ANISOU 648 O PRO B 21 2901 2556 2457 2 -164 -159 O ATOM 649 CB PRO B 21 31.911 6.016 27.553 1.00 21.87 C ANISOU 649 CB PRO B 21 3194 2709 2407 128 -123 -264 C ATOM 650 CG PRO B 21 32.005 5.683 29.015 1.00 23.26 C ANISOU 650 CG PRO B 21 3398 2985 2452 185 -147 -276 C ATOM 651 CD PRO B 21 32.835 4.429 29.064 1.00 22.83 C ANISOU 651 CD PRO B 21 3273 2991 2413 163 -167 -190 C ATOM 652 N VAL B 22 32.030 4.566 24.404 1.00 18.37 N ANISOU 652 N VAL B 22 2596 2181 2201 44 -45 -113 N ATOM 653 CA VAL B 22 32.735 4.557 23.131 1.00 17.81 C ANISOU 653 CA VAL B 22 2474 2077 2214 -6 -53 -96 C ATOM 654 C VAL B 22 32.282 5.692 22.197 1.00 16.66 C ANISOU 654 C VAL B 22 2351 1861 2118 -29 -34 -120 C ATOM 655 O VAL B 22 31.156 6.218 22.323 1.00 16.09 O ANISOU 655 O VAL B 22 2326 1759 2028 9 2 -139 O ATOM 656 CB VAL B 22 32.633 3.191 22.394 1.00 18.10 C ANISOU 656 CB VAL B 22 2458 2130 2290 14 -20 -31 C ATOM 657 CG1 VAL B 22 33.234 2.076 23.233 1.00 18.99 C ANISOU 657 CG1 VAL B 22 2549 2296 2369 38 -46 5 C ATOM 658 CG2 VAL B 22 31.194 2.837 22.017 1.00 18.04 C ANISOU 658 CG2 VAL B 22 2462 2099 2294 45 38 -6 C ATOM 659 N SER B 23 33.163 6.048 21.264 1.00 16.25 N ANISOU 659 N SER B 23 2258 1790 2126 -83 -53 -107 N ATOM 660 CA SER B 23 32.798 6.832 20.095 1.00 15.99 C ANISOU 660 CA SER B 23 2227 1701 2146 -101 -25 -95 C ATOM 661 C SER B 23 32.798 5.904 18.877 1.00 15.65 C ANISOU 661 C SER B 23 2123 1693 2132 -85 14 -42 C ATOM 662 O SER B 23 33.769 5.179 18.633 1.00 16.63 O ANISOU 662 O SER B 23 2188 1866 2263 -94 0 -18 O ATOM 663 CB SER B 23 33.762 8.013 19.842 1.00 16.38 C ANISOU 663 CB SER B 23 2275 1705 2243 -178 -72 -104 C ATOM 664 OG SER B 23 33.760 8.899 20.944 1.00 17.53 O ANISOU 664 OG SER B 23 2493 1803 2365 -193 -123 -172 O ATOM 665 N ILE B 24 31.715 5.944 18.114 1.00 14.41 N ANISOU 665 N ILE B 24 1977 1513 1985 -54 58 -30 N ATOM 666 CA ILE B 24 31.663 5.246 16.844 1.00 13.74 C ANISOU 666 CA ILE B 24 1845 1455 1919 -37 84 4 C ATOM 667 C ILE B 24 31.591 6.271 15.713 1.00 13.89 C ANISOU 667 C ILE B 24 1862 1451 1965 -54 101 28 C ATOM 668 O ILE B 24 30.595 6.973 15.551 1.00 14.03 O ANISOU 668 O ILE B 24 1917 1427 1986 -36 120 26 O ATOM 669 CB ILE B 24 30.471 4.267 16.758 1.00 13.29 C ANISOU 669 CB ILE B 24 1792 1404 1852 9 108 7 C ATOM 670 CG1 ILE B 24 30.615 3.170 17.819 1.00 13.61 C ANISOU 670 CG1 ILE B 24 1833 1465 1874 22 93 8 C ATOM 671 CG2 ILE B 24 30.390 3.661 15.353 1.00 12.87 C ANISOU 671 CG2 ILE B 24 1704 1371 1813 28 120 21 C ATOM 672 CD1 ILE B 24 29.464 2.186 17.850 1.00 13.46 C ANISOU 672 CD1 ILE B 24 1812 1440 1861 47 110 26 C ATOM 673 N TYR B 25 32.662 6.362 14.928 1.00 13.62 N ANISOU 673 N TYR B 25 1775 1452 1947 -81 99 62 N ATOM 674 CA TYR B 25 32.681 7.302 13.820 1.00 13.64 C ANISOU 674 CA TYR B 25 1767 1444 1971 -99 120 108 C ATOM 675 C TYR B 25 32.133 6.558 12.622 1.00 13.10 C ANISOU 675 C TYR B 25 1673 1428 1875 -41 153 122 C ATOM 676 O TYR B 25 32.591 5.445 12.299 1.00 12.59 O ANISOU 676 O TYR B 25 1570 1425 1788 -9 155 113 O ATOM 677 CB TYR B 25 34.102 7.790 13.482 1.00 15.02 C ANISOU 677 CB TYR B 25 1881 1651 2173 -160 108 158 C ATOM 678 CG TYR B 25 34.719 8.708 14.490 1.00 16.64 C ANISOU 678 CG TYR B 25 2109 1797 2418 -238 58 144 C ATOM 679 CD1 TYR B 25 35.416 8.209 15.599 1.00 17.64 C ANISOU 679 CD1 TYR B 25 2223 1948 2533 -256 14 105 C ATOM 680 CD2 TYR B 25 34.617 10.091 14.335 1.00 18.32 C ANISOU 680 CD2 TYR B 25 2361 1922 2680 -291 46 169 C ATOM 681 CE1 TYR B 25 35.985 9.077 16.529 1.00 19.88 C ANISOU 681 CE1 TYR B 25 2530 2180 2845 -330 -48 79 C ATOM 682 CE2 TYR B 25 35.183 10.966 15.252 1.00 20.28 C ANISOU 682 CE2 TYR B 25 2639 2095 2970 -369 -17 142 C ATOM 683 CZ TYR B 25 35.865 10.459 16.336 1.00 20.94 C ANISOU 683 CZ TYR B 25 2708 2215 3034 -390 -67 92 C ATOM 684 OH TYR B 25 36.403 11.368 17.233 1.00 23.28 O ANISOU 684 OH TYR B 25 3040 2437 3366 -469 -143 52 O ATOM 685 N LEU B 26 31.161 7.177 11.963 1.00 12.63 N ANISOU 685 N LEU B 26 1639 1344 1815 -20 174 140 N ATOM 686 CA LEU B 26 30.582 6.593 10.769 1.00 12.40 C ANISOU 686 CA LEU B 26 1588 1370 1751 34 193 149 C ATOM 687 C LEU B 26 31.446 6.962 9.582 1.00 13.21 C ANISOU 687 C LEU B 26 1645 1538 1838 32 216 211 C ATOM 688 O LEU B 26 32.300 7.840 9.694 1.00 13.36 O ANISOU 688 O LEU B 26 1647 1542 1888 -23 219 261 O ATOM 689 CB LEU B 26 29.144 7.043 10.571 1.00 12.46 C ANISOU 689 CB LEU B 26 1631 1344 1758 65 200 149 C ATOM 690 CG LEU B 26 28.245 6.673 11.747 1.00 12.09 C ANISOU 690 CG LEU B 26 1615 1258 1722 72 189 103 C ATOM 691 CD1 LEU B 26 26.838 7.243 11.517 1.00 12.68 C ANISOU 691 CD1 LEU B 26 1706 1315 1796 111 202 115 C ATOM 692 CD2 LEU B 26 28.236 5.147 11.995 1.00 12.59 C ANISOU 692 CD2 LEU B 26 1657 1352 1774 82 172 66 C ATOM 693 N VAL B 27 31.213 6.300 8.448 1.00 13.43 N ANISOU 693 N VAL B 27 1649 1641 1813 91 229 208 N ATOM 694 CA VAL B 27 32.032 6.551 7.238 1.00 14.79 C ANISOU 694 CA VAL B 27 1768 1907 1944 110 262 273 C ATOM 695 C VAL B 27 31.841 7.952 6.653 1.00 15.92 C ANISOU 695 C VAL B 27 1915 2032 2101 84 286 366 C ATOM 696 O VAL B 27 32.655 8.388 5.834 1.00 16.80 O ANISOU 696 O VAL B 27 1976 2217 2192 78 319 450 O ATOM 697 CB VAL B 27 31.804 5.487 6.133 1.00 15.34 C ANISOU 697 CB VAL B 27 1823 2070 1935 198 264 233 C ATOM 698 CG1 VAL B 27 32.318 4.113 6.602 1.00 14.83 C ANISOU 698 CG1 VAL B 27 1753 2016 1865 228 242 155 C ATOM 699 CG2 VAL B 27 30.332 5.430 5.741 1.00 14.95 C ANISOU 699 CG2 VAL B 27 1815 1997 1868 229 243 202 C ATOM 700 N ASN B 28 30.769 8.640 7.062 1.00 15.78 N ANISOU 700 N ASN B 28 1954 1924 2118 75 272 360 N ATOM 701 CA ASN B 28 30.505 10.012 6.627 1.00 16.99 C ANISOU 701 CA ASN B 28 2127 2030 2298 58 288 447 C ATOM 702 C ASN B 28 31.027 11.057 7.614 1.00 16.84 C ANISOU 702 C ASN B 28 2140 1893 2366 -26 271 468 C ATOM 703 O ASN B 28 30.812 12.249 7.417 1.00 17.84 O ANISOU 703 O ASN B 28 2299 1943 2535 -46 274 535 O ATOM 704 CB ASN B 28 29.002 10.218 6.423 1.00 17.77 C ANISOU 704 CB ASN B 28 2268 2100 2384 115 281 430 C ATOM 705 CG ASN B 28 28.184 9.840 7.661 1.00 17.90 C ANISOU 705 CG ASN B 28 2325 2046 2429 118 255 341 C ATOM 706 OD1 ASN B 28 28.707 9.693 8.746 1.00 18.47 O ANISOU 706 OD1 ASN B 28 2411 2070 2535 75 241 299 O ATOM 707 ND2 ASN B 28 26.891 9.706 7.488 1.00 20.63 N ANISOU 707 ND2 ASN B 28 2681 2399 2757 172 249 322 N ATOM 708 N GLY B 29 31.671 10.594 8.678 1.00 15.67 N ANISOU 708 N GLY B 29 1988 1725 2242 -68 245 407 N ATOM 709 CA GLY B 29 32.331 11.484 9.641 1.00 16.46 C ANISOU 709 CA GLY B 29 2114 1725 2415 -154 212 411 C ATOM 710 C GLY B 29 31.499 11.788 10.878 1.00 16.22 C ANISOU 710 C GLY B 29 2169 1586 2408 -144 180 326 C ATOM 711 O GLY B 29 32.003 12.419 11.796 1.00 17.08 O ANISOU 711 O GLY B 29 2313 1612 2565 -205 140 300 O ATOM 712 N ILE B 30 30.240 11.355 10.895 1.00 15.62 N ANISOU 712 N ILE B 30 2122 1519 2294 -66 194 283 N ATOM 713 CA ILE B 30 29.356 11.566 12.058 1.00 15.79 C ANISOU 713 CA ILE B 30 2212 1466 2319 -36 178 209 C ATOM 714 C ILE B 30 29.832 10.696 13.236 1.00 15.62 C ANISOU 714 C ILE B 30 2186 1470 2280 -56 154 139 C ATOM 715 O ILE B 30 30.109 9.485 13.058 1.00 15.10 O ANISOU 715 O ILE B 30 2067 1489 2182 -47 161 132 O ATOM 716 CB ILE B 30 27.889 11.240 11.687 1.00 16.14 C ANISOU 716 CB ILE B 30 2261 1543 2329 50 205 202 C ATOM 717 CG1 ILE B 30 27.353 12.184 10.587 1.00 17.36 C ANISOU 717 CG1 ILE B 30 2424 1675 2496 83 224 276 C ATOM 718 CG2 ILE B 30 26.969 11.266 12.902 1.00 16.13 C ANISOU 718 CG2 ILE B 30 2307 1503 2318 93 203 136 C ATOM 719 CD1 ILE B 30 27.486 13.647 10.913 1.00 19.06 C ANISOU 719 CD1 ILE B 30 2710 1759 2772 64 210 298 C ATOM 720 N LYS B 31 29.915 11.290 14.424 1.00 15.46 N ANISOU 720 N LYS B 31 2225 1375 2274 -74 122 86 N ATOM 721 CA LYS B 31 30.375 10.597 15.620 1.00 15.39 C ANISOU 721 CA LYS B 31 2217 1394 2237 -88 94 26 C ATOM 722 C LYS B 31 29.213 10.268 16.558 1.00 15.57 C ANISOU 722 C LYS B 31 2281 1422 2212 -16 110 -27 C ATOM 723 O LYS B 31 28.543 11.181 17.071 1.00 15.74 O ANISOU 723 O LYS B 31 2371 1377 2232 22 110 -62 O ATOM 724 CB LYS B 31 31.421 11.448 16.359 1.00 17.15 C ANISOU 724 CB LYS B 31 2471 1550 2494 -164 36 -1 C ATOM 725 CG LYS B 31 31.980 10.766 17.605 1.00 18.19 C ANISOU 725 CG LYS B 31 2600 1726 2586 -175 -2 -59 C ATOM 726 CD LYS B 31 33.058 11.584 18.296 1.00 20.75 C ANISOU 726 CD LYS B 31 2947 1994 2943 -259 -78 -92 C ATOM 727 CE LYS B 31 32.457 12.628 19.223 1.00 23.46 C ANISOU 727 CE LYS B 31 3404 2232 3278 -234 -113 -175 C ATOM 728 NZ LYS B 31 33.549 13.460 19.802 1.00 25.89 N ANISOU 728 NZ LYS B 31 3737 2470 3629 -331 -205 -215 N ATOM 729 N LEU B 32 28.955 8.982 16.763 1.00 14.75 N ANISOU 729 N LEU B 32 2136 1397 2073 8 127 -27 N ATOM 730 CA LEU B 32 27.954 8.573 17.738 1.00 15.27 C ANISOU 730 CA LEU B 32 2223 1485 2093 65 146 -56 C ATOM 731 C LEU B 32 28.621 8.191 19.042 1.00 16.27 C ANISOU 731 C LEU B 32 2366 1634 2181 50 116 -94 C ATOM 732 O LEU B 32 29.732 7.701 19.034 1.00 17.13 O ANISOU 732 O LEU B 32 2443 1766 2299 2 85 -87 O ATOM 733 CB LEU B 32 27.146 7.382 17.217 1.00 14.49 C ANISOU 733 CB LEU B 32 2068 1450 1988 91 177 -20 C ATOM 734 CG LEU B 32 26.503 7.494 15.828 1.00 14.85 C ANISOU 734 CG LEU B 32 2083 1501 2059 107 196 16 C ATOM 735 CD1 LEU B 32 25.835 6.172 15.462 1.00 15.14 C ANISOU 735 CD1 LEU B 32 2067 1594 2093 116 203 35 C ATOM 736 CD2 LEU B 32 25.501 8.622 15.763 1.00 15.93 C ANISOU 736 CD2 LEU B 32 2254 1602 2197 158 218 19 C ATOM 737 N GLN B 33 27.947 8.429 20.169 1.00 17.46 N ANISOU 737 N GLN B 33 2564 1790 2279 102 125 -133 N ATOM 738 CA GLN B 33 28.514 8.038 21.471 1.00 18.72 C ANISOU 738 CA GLN B 33 2742 1990 2380 101 95 -166 C ATOM 739 C GLN B 33 27.561 7.161 22.269 1.00 17.75 C ANISOU 739 C GLN B 33 2604 1945 2197 161 140 -140 C ATOM 740 O GLN B 33 26.336 7.336 22.213 1.00 18.34 O ANISOU 740 O GLN B 33 2678 2033 2259 218 190 -126 O ATOM 741 CB GLN B 33 28.847 9.254 22.305 1.00 21.51 C ANISOU 741 CB GLN B 33 3178 2288 2706 106 51 -246 C ATOM 742 CG GLN B 33 30.047 10.040 21.812 1.00 25.07 C ANISOU 742 CG GLN B 33 3638 2665 3223 19 -12 -263 C ATOM 743 CD GLN B 33 30.374 11.166 22.764 1.00 28.66 C ANISOU 743 CD GLN B 33 4184 3050 3655 16 -76 -356 C ATOM 744 OE1 GLN B 33 31.175 10.995 23.682 1.00 30.91 O ANISOU 744 OE1 GLN B 33 4479 3370 3898 -12 -134 -399 O ATOM 745 NE2 GLN B 33 29.702 12.299 22.597 1.00 31.47 N ANISOU 745 NE2 GLN B 33 4615 3311 4033 54 -70 -394 N ATOM 746 N GLY B 34 28.116 6.229 23.020 1.00 17.90 N ANISOU 746 N GLY B 34 2602 2019 2178 150 122 -123 N ATOM 747 CA GLY B 34 27.301 5.394 23.886 1.00 18.40 C ANISOU 747 CA GLY B 34 2649 2160 2183 199 164 -79 C ATOM 748 C GLY B 34 28.078 4.197 24.376 1.00 19.62 C ANISOU 748 C GLY B 34 2772 2359 2325 174 138 -35 C ATOM 749 O GLY B 34 29.304 4.188 24.352 1.00 20.06 O ANISOU 749 O GLY B 34 2827 2401 2392 134 84 -58 O ATOM 750 N GLN B 35 27.357 3.176 24.812 1.00 20.60 N ANISOU 750 N GLN B 35 2862 2535 2430 196 178 40 N ATOM 751 CA GLN B 35 28.005 1.957 25.263 1.00 21.42 C ANISOU 751 CA GLN B 35 2939 2668 2530 180 155 98 C ATOM 752 C GLN B 35 27.680 0.818 24.290 1.00 20.34 C ANISOU 752 C GLN B 35 2752 2490 2487 146 166 163 C ATOM 753 O GLN B 35 26.601 0.792 23.707 1.00 20.01 O ANISOU 753 O GLN B 35 2685 2435 2484 143 202 186 O ATOM 754 CB GLN B 35 27.565 1.654 26.695 1.00 25.13 C ANISOU 754 CB GLN B 35 3421 3229 2900 233 182 143 C ATOM 755 CG GLN B 35 28.360 2.442 27.735 1.00 29.52 C ANISOU 755 CG GLN B 35 4034 3828 3353 263 139 69 C ATOM 756 CD GLN B 35 27.912 2.182 29.160 1.00 34.06 C ANISOU 756 CD GLN B 35 4624 4515 3802 332 169 111 C ATOM 757 OE1 GLN B 35 27.593 1.055 29.526 1.00 37.27 O ANISOU 757 OE1 GLN B 35 4989 4967 4204 337 200 223 O ATOM 758 NE2 GLN B 35 27.898 3.229 29.976 1.00 36.02 N ANISOU 758 NE2 GLN B 35 4937 4807 3944 388 157 22 N ATOM 759 N ILE B 36 28.615 -0.107 24.108 1.00 20.41 N ANISOU 759 N ILE B 36 2744 2478 2532 126 127 186 N ATOM 760 CA ILE B 36 28.349 -1.279 23.277 1.00 20.06 C ANISOU 760 CA ILE B 36 2668 2381 2573 104 124 233 C ATOM 761 C ILE B 36 27.479 -2.227 24.112 1.00 19.63 C ANISOU 761 C ILE B 36 2598 2348 2513 108 152 333 C ATOM 762 O ILE B 36 27.915 -2.754 25.128 1.00 19.53 O ANISOU 762 O ILE B 36 2592 2372 2456 127 144 385 O ATOM 763 CB ILE B 36 29.639 -1.988 22.826 1.00 20.58 C ANISOU 763 CB ILE B 36 2728 2414 2676 102 76 223 C ATOM 764 CG1 ILE B 36 30.650 -0.996 22.211 1.00 22.10 C ANISOU 764 CG1 ILE B 36 2920 2613 2863 94 53 148 C ATOM 765 CG2 ILE B 36 29.303 -3.170 21.903 1.00 20.65 C ANISOU 765 CG2 ILE B 36 2721 2352 2772 91 66 250 C ATOM 766 CD1 ILE B 36 30.584 -0.868 20.711 1.00 22.34 C ANISOU 766 CD1 ILE B 36 2934 2602 2951 81 57 114 C ATOM 767 N GLU B 37 26.241 -2.418 23.673 1.00 19.15 N ANISOU 767 N GLU B 37 2506 2273 2497 86 184 369 N ATOM 768 CA GLU B 37 25.293 -3.278 24.367 1.00 20.07 C ANISOU 768 CA GLU B 37 2588 2412 2624 72 214 482 C ATOM 769 C GLU B 37 25.498 -4.708 23.906 1.00 19.33 C ANISOU 769 C GLU B 37 2486 2226 2631 31 171 534 C ATOM 770 O GLU B 37 25.547 -5.625 24.722 1.00 19.51 O ANISOU 770 O GLU B 37 2507 2249 2659 27 170 631 O ATOM 771 CB GLU B 37 23.878 -2.816 24.027 1.00 21.18 C ANISOU 771 CB GLU B 37 2684 2584 2780 61 260 499 C ATOM 772 CG GLU B 37 22.767 -3.619 24.638 1.00 23.75 C ANISOU 772 CG GLU B 37 2950 2948 3127 35 298 630 C ATOM 773 CD GLU B 37 21.405 -3.020 24.317 1.00 25.51 C ANISOU 773 CD GLU B 37 3112 3225 3355 34 345 645 C ATOM 774 OE1 GLU B 37 21.306 -2.124 23.449 1.00 26.16 O ANISOU 774 OE1 GLU B 37 3204 3292 3441 51 338 554 O ATOM 775 OE2 GLU B 37 20.435 -3.462 24.931 1.00 27.25 O ANISOU 775 OE2 GLU B 37 3266 3510 3576 20 390 761 O ATOM 776 N SER B 38 25.638 -4.877 22.588 1.00 18.17 N ANISOU 776 N SER B 38 2343 2000 2560 7 132 467 N ATOM 777 CA SER B 38 25.879 -6.187 21.970 1.00 17.87 C ANISOU 777 CA SER B 38 2314 1855 2620 -19 78 482 C ATOM 778 C SER B 38 26.210 -5.977 20.498 1.00 16.73 C ANISOU 778 C SER B 38 2183 1662 2511 -15 42 373 C ATOM 779 O SER B 38 26.122 -4.849 19.988 1.00 15.56 O ANISOU 779 O SER B 38 2027 1562 2321 -4 64 311 O ATOM 780 CB SER B 38 24.638 -7.075 22.135 1.00 19.40 C ANISOU 780 CB SER B 38 2470 2011 2891 -82 80 584 C ATOM 781 OG SER B 38 23.473 -6.407 21.705 1.00 21.03 O ANISOU 781 OG SER B 38 2628 2262 3099 -111 108 576 O ATOM 782 N PHE B 39 26.629 -7.038 19.827 1.00 16.16 N ANISOU 782 N PHE B 39 2135 1495 2510 -14 -12 352 N ATOM 783 CA PHE B 39 26.980 -6.988 18.416 1.00 16.51 C ANISOU 783 CA PHE B 39 2194 1504 2573 5 -47 248 C ATOM 784 C PHE B 39 26.890 -8.379 17.827 1.00 17.44 C ANISOU 784 C PHE B 39 2343 1499 2784 -4 -113 237 C ATOM 785 O PHE B 39 26.932 -9.363 18.558 1.00 18.49 O ANISOU 785 O PHE B 39 2492 1563 2968 -16 -133 310 O ATOM 786 CB PHE B 39 28.395 -6.413 18.194 1.00 16.13 C ANISOU 786 CB PHE B 39 2160 1504 2464 69 -40 187 C ATOM 787 CG PHE B 39 29.490 -7.209 18.850 1.00 17.27 C ANISOU 787 CG PHE B 39 2325 1625 2612 114 -61 216 C ATOM 788 CD1 PHE B 39 29.761 -7.054 20.203 1.00 17.73 C ANISOU 788 CD1 PHE B 39 2377 1734 2626 117 -41 287 C ATOM 789 CD2 PHE B 39 30.263 -8.104 18.107 1.00 18.16 C ANISOU 789 CD2 PHE B 39 2463 1674 2762 169 -104 169 C ATOM 790 CE1 PHE B 39 30.750 -7.795 20.821 1.00 18.60 C ANISOU 790 CE1 PHE B 39 2499 1831 2735 164 -65 324 C ATOM 791 CE2 PHE B 39 31.273 -8.845 18.718 1.00 19.42 C ANISOU 791 CE2 PHE B 39 2637 1815 2926 225 -124 202 C ATOM 792 CZ PHE B 39 31.512 -8.689 20.077 1.00 19.46 C ANISOU 792 CZ PHE B 39 2630 1872 2892 219 -106 285 C ATOM 793 N ASP B 40 26.745 -8.445 16.508 1.00 17.62 N ANISOU 793 N ASP B 40 2377 1490 2826 3 -150 146 N ATOM 794 CA ASP B 40 26.792 -9.724 15.787 1.00 19.46 C ANISOU 794 CA ASP B 40 2658 1597 3139 11 -228 98 C ATOM 795 C ASP B 40 27.626 -9.489 14.526 1.00 19.48 C ANISOU 795 C ASP B 40 2686 1627 3089 93 -242 -25 C ATOM 796 O ASP B 40 28.336 -8.487 14.440 1.00 18.73 O ANISOU 796 O ASP B 40 2568 1638 2912 136 -190 -41 O ATOM 797 CB ASP B 40 25.373 -10.254 15.494 1.00 20.39 C ANISOU 797 CB ASP B 40 2759 1645 3343 -83 -276 119 C ATOM 798 CG ASP B 40 24.560 -9.346 14.551 1.00 20.53 C ANISOU 798 CG ASP B 40 2736 1742 3323 -106 -271 64 C ATOM 799 OD1 ASP B 40 25.136 -8.452 13.856 1.00 19.03 O ANISOU 799 OD1 ASP B 40 2548 1635 3048 -43 -242 -7 O ATOM 800 OD2 ASP B 40 23.321 -9.548 14.502 1.00 21.96 O ANISOU 800 OD2 ASP B 40 2875 1903 3564 -190 -299 103 O ATOM 801 N GLN B 41 27.521 -10.384 13.545 1.00 20.45 N ANISOU 801 N GLN B 41 2856 1658 3257 114 -314 -108 N ATOM 802 CA GLN B 41 28.238 -10.253 12.279 1.00 20.55 C ANISOU 802 CA GLN B 41 2893 1710 3206 207 -326 -225 C ATOM 803 C GLN B 41 28.060 -8.901 11.546 1.00 20.20 C ANISOU 803 C GLN B 41 2800 1803 3070 209 -277 -251 C ATOM 804 O GLN B 41 29.004 -8.411 10.942 1.00 19.79 O ANISOU 804 O GLN B 41 2742 1835 2941 288 -244 -294 O ATOM 805 CB GLN B 41 27.900 -11.443 11.350 1.00 23.85 C ANISOU 805 CB GLN B 41 3379 2000 3684 225 -425 -324 C ATOM 806 CG GLN B 41 28.443 -11.321 9.933 1.00 25.26 C ANISOU 806 CG GLN B 41 3585 2236 3777 329 -441 -456 C ATOM 807 N PHE B 42 26.865 -8.321 11.612 1.00 18.44 N ANISOU 807 N PHE B 42 2539 1607 2861 126 -271 -214 N ATOM 808 CA PHE B 42 26.525 -7.197 10.758 1.00 18.33 C ANISOU 808 CA PHE B 42 2491 1698 2774 133 -243 -241 C ATOM 809 C PHE B 42 26.286 -5.904 11.497 1.00 16.51 C ANISOU 809 C PHE B 42 2211 1551 2512 98 -167 -160 C ATOM 810 O PHE B 42 26.434 -4.827 10.896 1.00 14.85 O ANISOU 810 O PHE B 42 1980 1428 2235 124 -130 -171 O ATOM 811 CB PHE B 42 25.279 -7.510 9.926 1.00 20.33 C ANISOU 811 CB PHE B 42 2741 1924 3059 87 -311 -284 C ATOM 812 CG PHE B 42 25.443 -8.696 9.024 1.00 23.50 C ANISOU 812 CG PHE B 42 3206 2240 3484 126 -402 -391 C ATOM 813 CD1 PHE B 42 26.423 -8.702 8.032 1.00 24.80 C ANISOU 813 CD1 PHE B 42 3407 2453 3563 238 -401 -484 C ATOM 814 CD2 PHE B 42 24.614 -9.801 9.157 1.00 25.58 C ANISOU 814 CD2 PHE B 42 3492 2375 3854 53 -491 -401 C ATOM 815 CE1 PHE B 42 26.573 -9.801 7.182 1.00 27.41 C ANISOU 815 CE1 PHE B 42 3807 2704 3901 295 -488 -602 C ATOM 816 CE2 PHE B 42 24.755 -10.908 8.312 1.00 28.19 C ANISOU 816 CE2 PHE B 42 3897 2604 4211 91 -591 -519 C ATOM 817 CZ PHE B 42 25.737 -10.904 7.326 1.00 28.95 C ANISOU 817 CZ PHE B 42 4041 2750 4209 222 -589 -628 C ATOM 818 N VAL B 43 25.884 -5.991 12.768 1.00 15.34 N ANISOU 818 N VAL B 43 2046 1377 2406 45 -147 -79 N ATOM 819 CA VAL B 43 25.483 -4.752 13.489 1.00 14.26 C ANISOU 819 CA VAL B 43 1870 1315 2232 22 -80 -17 C ATOM 820 C VAL B 43 26.076 -4.642 14.890 1.00 13.82 C ANISOU 820 C VAL B 43 1819 1267 2166 22 -41 44 C ATOM 821 O VAL B 43 26.464 -5.642 15.486 1.00 13.96 O ANISOU 821 O VAL B 43 1856 1226 2220 22 -64 69 O ATOM 822 CB VAL B 43 23.944 -4.547 13.578 1.00 14.51 C ANISOU 822 CB VAL B 43 1857 1362 2296 -36 -82 26 C ATOM 823 CG1 VAL B 43 23.308 -4.532 12.198 1.00 14.71 C ANISOU 823 CG1 VAL B 43 1870 1398 2320 -36 -129 -33 C ATOM 824 CG2 VAL B 43 23.253 -5.584 14.461 1.00 15.17 C ANISOU 824 CG2 VAL B 43 1925 1384 2457 -98 -104 97 C ATOM 825 N ILE B 44 26.147 -3.408 15.384 1.00 13.15 N ANISOU 825 N ILE B 44 1721 1249 2028 28 12 63 N ATOM 826 CA ILE B 44 26.478 -3.142 16.764 1.00 13.28 C ANISOU 826 CA ILE B 44 1740 1288 2017 28 44 113 C ATOM 827 C ILE B 44 25.256 -2.439 17.371 1.00 12.83 C ANISOU 827 C ILE B 44 1657 1272 1945 8 85 158 C ATOM 828 O ILE B 44 24.702 -1.508 16.740 1.00 12.05 O ANISOU 828 O ILE B 44 1545 1203 1829 15 102 135 O ATOM 829 CB ILE B 44 27.740 -2.239 16.865 1.00 13.51 C ANISOU 829 CB ILE B 44 1783 1359 1992 58 60 82 C ATOM 830 CG1 ILE B 44 28.954 -2.968 16.259 1.00 13.99 C ANISOU 830 CG1 ILE B 44 1851 1402 2063 92 29 48 C ATOM 831 CG2 ILE B 44 27.937 -1.825 18.323 1.00 13.79 C ANISOU 831 CG2 ILE B 44 1826 1426 1987 57 83 119 C ATOM 832 CD1 ILE B 44 30.233 -2.125 16.221 1.00 14.58 C ANISOU 832 CD1 ILE B 44 1914 1530 2095 111 41 30 C ATOM 833 N LEU B 45 24.786 -2.904 18.531 1.00 12.90 N ANISOU 833 N LEU B 45 1654 1290 1957 -8 103 229 N ATOM 834 CA LEU B 45 23.755 -2.138 19.282 1.00 13.62 C ANISOU 834 CA LEU B 45 1717 1448 2010 -3 156 273 C ATOM 835 C LEU B 45 24.437 -1.143 20.202 1.00 14.01 C ANISOU 835 C LEU B 45 1804 1544 1977 41 187 251 C ATOM 836 O LEU B 45 25.197 -1.534 21.081 1.00 14.26 O ANISOU 836 O LEU B 45 1857 1582 1981 49 180 270 O ATOM 837 CB LEU B 45 22.827 -3.077 20.073 1.00 14.33 C ANISOU 837 CB LEU B 45 1765 1547 2134 -38 169 374 C ATOM 838 CG LEU B 45 22.068 -4.116 19.242 1.00 14.85 C ANISOU 838 CG LEU B 45 1793 1552 2299 -101 121 398 C ATOM 839 CD1 LEU B 45 21.001 -4.764 20.095 1.00 16.34 C ANISOU 839 CD1 LEU B 45 1919 1768 2521 -148 146 520 C ATOM 840 CD2 LEU B 45 21.448 -3.518 17.982 1.00 15.08 C ANISOU 840 CD2 LEU B 45 1797 1591 2341 -104 105 339 C ATOM 841 N LEU B 46 24.144 0.151 20.010 1.00 14.29 N ANISOU 841 N LEU B 46 1848 1606 1974 70 214 210 N ATOM 842 CA LEU B 46 24.826 1.212 20.745 1.00 15.11 C ANISOU 842 CA LEU B 46 1999 1731 2010 105 225 167 C ATOM 843 C LEU B 46 23.774 1.796 21.654 1.00 16.49 C ANISOU 843 C LEU B 46 2170 1968 2130 151 277 192 C ATOM 844 O LEU B 46 22.737 2.276 21.186 1.00 17.18 O ANISOU 844 O LEU B 46 2229 2070 2229 170 306 199 O ATOM 845 CB LEU B 46 25.366 2.286 19.784 1.00 14.47 C ANISOU 845 CB LEU B 46 1944 1615 1939 107 210 102 C ATOM 846 CG LEU B 46 26.045 3.455 20.493 1.00 14.63 C ANISOU 846 CG LEU B 46 2018 1633 1907 127 206 52 C ATOM 847 CD1 LEU B 46 27.387 2.994 21.072 1.00 15.08 C ANISOU 847 CD1 LEU B 46 2087 1694 1948 104 166 42 C ATOM 848 CD2 LEU B 46 26.190 4.652 19.543 1.00 15.15 C ANISOU 848 CD2 LEU B 46 2105 1655 1997 125 201 13 C ATOM 849 N LYS B 47 24.014 1.697 22.953 1.00 18.03 N ANISOU 849 N LYS B 47 2384 2210 2255 177 291 209 N ATOM 850 CA LYS B 47 23.023 2.123 23.911 1.00 19.89 C ANISOU 850 CA LYS B 47 2612 2526 2419 238 350 238 C ATOM 851 C LYS B 47 23.463 3.408 24.600 1.00 20.08 C ANISOU 851 C LYS B 47 2711 2560 2357 300 348 150 C ATOM 852 O LYS B 47 24.578 3.513 25.098 1.00 20.59 O ANISOU 852 O LYS B 47 2824 2611 2386 290 305 105 O ATOM 853 CB LYS B 47 22.763 1.032 24.947 1.00 22.63 C ANISOU 853 CB LYS B 47 2924 2941 2735 235 374 338 C ATOM 854 CG LYS B 47 21.560 1.354 25.804 1.00 25.86 C ANISOU 854 CG LYS B 47 3298 3459 3070 301 450 391 C ATOM 855 CD LYS B 47 21.211 0.228 26.757 1.00 29.27 C ANISOU 855 CD LYS B 47 3679 3966 3475 290 484 521 C ATOM 856 CE LYS B 47 19.752 0.320 27.162 1.00 32.12 C ANISOU 856 CE LYS B 47 3960 4440 3804 333 567 608 C ATOM 857 NZ LYS B 47 19.397 1.603 27.827 1.00 34.91 N ANISOU 857 NZ LYS B 47 4352 4879 4034 454 619 538 N ATOM 858 N ASN B 48 22.567 4.384 24.617 1.00 20.83 N ANISOU 858 N ASN B 48 2816 2677 2421 366 390 122 N ATOM 859 CA ASN B 48 22.771 5.631 25.341 1.00 21.37 C ANISOU 859 CA ASN B 48 2968 2745 2407 440 388 30 C ATOM 860 C ASN B 48 21.370 6.044 25.756 1.00 22.54 C ANISOU 860 C ASN B 48 3089 2974 2499 539 465 56 C ATOM 861 O ASN B 48 20.702 6.799 25.040 1.00 22.19 O ANISOU 861 O ASN B 48 3041 2898 2492 575 483 37 O ATOM 862 CB ASN B 48 23.460 6.674 24.441 1.00 20.28 C ANISOU 862 CB ASN B 48 2888 2491 2328 412 337 -55 C ATOM 863 CG ASN B 48 24.028 7.850 25.227 1.00 20.85 C ANISOU 863 CG ASN B 48 3063 2527 2334 458 302 -162 C ATOM 864 OD1 ASN B 48 23.516 8.205 26.287 1.00 21.49 O ANISOU 864 OD1 ASN B 48 3180 2670 2314 550 332 -194 O ATOM 865 ND2 ASN B 48 25.113 8.431 24.729 1.00 19.65 N ANISOU 865 ND2 ASN B 48 2954 2277 2235 394 234 -219 N ATOM 866 N THR B 49 20.946 5.524 26.914 1.00 24.24 N ANISOU 866 N THR B 49 3278 3307 2623 589 514 112 N ATOM 867 CA THR B 49 19.523 5.369 27.358 1.00 26.49 C ANISOU 867 CA THR B 49 3485 3719 2859 666 605 197 C ATOM 868 C THR B 49 18.646 4.605 26.351 1.00 26.78 C ANISOU 868 C THR B 49 3405 3759 3010 597 625 303 C ATOM 869 O THR B 49 18.010 3.622 26.721 1.00 26.34 O ANISOU 869 O THR B 49 3259 3792 2959 570 666 424 O ATOM 870 CB THR B 49 18.786 6.659 27.855 1.00 29.27 C ANISOU 870 CB THR B 49 3883 4120 3118 816 656 124 C ATOM 871 OG1 THR B 49 18.156 7.313 26.752 1.00 32.28 O ANISOU 871 OG1 THR B 49 4244 4440 3582 828 661 108 O ATOM 872 CG2 THR B 49 19.711 7.597 28.606 1.00 28.39 C ANISOU 872 CG2 THR B 49 3910 3962 2916 873 607 -18 C ATOM 873 N VAL B 50 18.648 5.049 25.088 1.00 25.70 N ANISOU 873 N VAL B 50 3273 3527 2965 562 588 260 N ATOM 874 CA VAL B 50 17.961 4.361 23.980 1.00 25.79 C ANISOU 874 CA VAL B 50 3185 3528 3084 488 580 335 C ATOM 875 C VAL B 50 18.918 3.366 23.317 1.00 23.10 C ANISOU 875 C VAL B 50 2852 3097 2826 368 509 340 C ATOM 876 O VAL B 50 20.115 3.620 23.264 1.00 23.53 O ANISOU 876 O VAL B 50 2987 3078 2875 350 462 266 O ATOM 877 CB VAL B 50 17.507 5.370 22.891 1.00 25.79 C ANISOU 877 CB VAL B 50 3191 3481 3126 525 572 285 C ATOM 878 CG1 VAL B 50 16.788 4.662 21.747 1.00 26.13 C ANISOU 878 CG1 VAL B 50 3133 3529 3268 452 552 353 C ATOM 879 CG2 VAL B 50 16.592 6.436 23.473 1.00 27.79 C ANISOU 879 CG2 VAL B 50 3448 3809 3302 665 640 268 C ATOM 880 N SER B 51 18.386 2.236 22.843 1.00 22.99 N ANISOU 880 N SER B 51 2752 3091 2892 290 497 426 N ATOM 881 CA SER B 51 19.167 1.266 22.054 1.00 21.83 C ANISOU 881 CA SER B 51 2614 2850 2829 192 426 420 C ATOM 882 C SER B 51 19.017 1.548 20.573 1.00 19.00 C ANISOU 882 C SER B 51 2246 2436 2538 167 384 373 C ATOM 883 O SER B 51 17.896 1.573 20.053 1.00 18.37 O ANISOU 883 O SER B 51 2092 2398 2492 165 395 413 O ATOM 884 CB SER B 51 18.712 -0.162 22.335 1.00 23.25 C ANISOU 884 CB SER B 51 2723 3045 3067 118 421 531 C ATOM 885 OG SER B 51 19.075 -0.554 23.649 1.00 26.79 O ANISOU 885 OG SER B 51 3189 3540 3451 137 452 585 O ATOM 886 N GLN B 52 20.145 1.738 19.884 1.00 17.43 N ANISOU 886 N GLN B 52 2113 2156 2353 149 336 297 N ATOM 887 CA GLN B 52 20.110 1.997 18.467 1.00 16.28 C ANISOU 887 CA GLN B 52 1962 1971 2252 133 299 258 C ATOM 888 C GLN B 52 20.998 0.992 17.739 1.00 15.20 C ANISOU 888 C GLN B 52 1842 1769 2165 73 237 234 C ATOM 889 O GLN B 52 22.041 0.568 18.280 1.00 14.66 O ANISOU 889 O GLN B 52 1815 1670 2086 61 225 222 O ATOM 890 CB GLN B 52 20.522 3.456 18.190 1.00 16.87 C ANISOU 890 CB GLN B 52 2097 2025 2289 191 311 196 C ATOM 891 CG GLN B 52 21.561 3.661 17.131 1.00 18.15 C ANISOU 891 CG GLN B 52 2300 2126 2472 166 268 145 C ATOM 892 CD GLN B 52 21.987 5.117 16.993 1.00 18.17 C ANISOU 892 CD GLN B 52 2360 2095 2448 208 279 105 C ATOM 893 OE1 GLN B 52 21.754 5.719 15.970 1.00 20.15 O ANISOU 893 OE1 GLN B 52 2607 2334 2714 223 274 104 O ATOM 894 NE2 GLN B 52 22.572 5.691 18.048 1.00 20.05 N ANISOU 894 NE2 GLN B 52 2655 2316 2648 228 290 74 N ATOM 895 N MET B 53 20.555 0.581 16.552 1.00 13.92 N ANISOU 895 N MET B 53 1646 1593 2052 43 197 226 N ATOM 896 CA MET B 53 21.270 -0.428 15.768 1.00 13.30 C ANISOU 896 CA MET B 53 1586 1453 2014 3 135 191 C ATOM 897 C MET B 53 22.130 0.253 14.694 1.00 12.71 C ANISOU 897 C MET B 53 1551 1367 1911 33 121 124 C ATOM 898 O MET B 53 21.624 1.070 13.927 1.00 13.04 O ANISOU 898 O MET B 53 1580 1439 1938 59 127 116 O ATOM 899 CB MET B 53 20.267 -1.425 15.153 1.00 13.99 C ANISOU 899 CB MET B 53 1616 1531 2168 -52 86 214 C ATOM 900 CG MET B 53 20.928 -2.405 14.214 1.00 14.23 C ANISOU 900 CG MET B 53 1681 1492 2235 -75 14 154 C ATOM 901 SD MET B 53 19.770 -3.620 13.604 1.00 15.29 S ANISOU 901 SD MET B 53 1760 1590 2458 -153 -67 167 S ATOM 902 CE MET B 53 18.977 -2.699 12.280 1.00 16.00 C ANISOU 902 CE MET B 53 1811 1757 2512 -124 -86 128 C ATOM 903 N VAL B 54 23.427 -0.023 14.705 1.00 12.37 N ANISOU 903 N VAL B 54 1551 1291 1858 37 108 92 N ATOM 904 CA VAL B 54 24.413 0.586 13.773 1.00 11.79 C ANISOU 904 CA VAL B 54 1503 1220 1755 63 103 47 C ATOM 905 C VAL B 54 24.930 -0.525 12.889 1.00 12.13 C ANISOU 905 C VAL B 54 1552 1242 1815 63 55 8 C ATOM 906 O VAL B 54 25.447 -1.544 13.395 1.00 12.94 O ANISOU 906 O VAL B 54 1668 1305 1943 54 34 5 O ATOM 907 CB VAL B 54 25.618 1.187 14.550 1.00 11.87 C ANISOU 907 CB VAL B 54 1546 1227 1738 70 126 44 C ATOM 908 CG1 VAL B 54 26.548 1.978 13.617 1.00 12.10 C ANISOU 908 CG1 VAL B 54 1584 1270 1745 85 129 24 C ATOM 909 CG2 VAL B 54 25.092 2.064 15.694 1.00 11.94 C ANISOU 909 CG2 VAL B 54 1566 1245 1725 78 162 67 C ATOM 910 N TYR B 55 24.779 -0.353 11.572 1.00 11.49 N ANISOU 910 N TYR B 55 1464 1187 1715 84 36 -24 N ATOM 911 CA TYR B 55 25.358 -1.293 10.622 1.00 11.58 C ANISOU 911 CA TYR B 55 1492 1189 1721 108 -9 -81 C ATOM 912 C TYR B 55 26.861 -1.128 10.557 1.00 11.34 C ANISOU 912 C TYR B 55 1477 1178 1656 145 15 -93 C ATOM 913 O TYR B 55 27.346 -0.019 10.381 1.00 11.29 O ANISOU 913 O TYR B 55 1461 1214 1614 154 54 -68 O ATOM 914 CB TYR B 55 24.751 -1.144 9.227 1.00 11.62 C ANISOU 914 CB TYR B 55 1485 1238 1694 132 -39 -114 C ATOM 915 CG TYR B 55 23.395 -1.780 9.129 1.00 12.09 C ANISOU 915 CG TYR B 55 1520 1275 1798 90 -92 -119 C ATOM 916 CD1 TYR B 55 23.258 -3.160 8.914 1.00 12.67 C ANISOU 916 CD1 TYR B 55 1612 1285 1918 69 -164 -171 C ATOM 917 CD2 TYR B 55 22.241 -1.018 9.293 1.00 11.91 C ANISOU 917 CD2 TYR B 55 1453 1289 1782 71 -74 -69 C ATOM 918 CE1 TYR B 55 21.997 -3.760 8.847 1.00 13.58 C ANISOU 918 CE1 TYR B 55 1695 1374 2091 10 -224 -167 C ATOM 919 CE2 TYR B 55 20.985 -1.606 9.248 1.00 12.65 C ANISOU 919 CE2 TYR B 55 1503 1378 1926 24 -124 -60 C ATOM 920 CZ TYR B 55 20.860 -2.981 9.011 1.00 13.49 C ANISOU 920 CZ TYR B 55 1621 1420 2085 -17 -203 -107 C ATOM 921 OH TYR B 55 19.581 -3.520 8.962 1.00 14.54 O ANISOU 921 OH TYR B 55 1698 1546 2279 -82 -261 -88 O ATOM 922 N LYS B 56 27.581 -2.238 10.725 1.00 11.52 N ANISOU 922 N LYS B 56 1518 1163 1696 163 -12 -123 N ATOM 923 CA LYS B 56 29.062 -2.226 10.640 1.00 11.85 C ANISOU 923 CA LYS B 56 1557 1239 1705 208 8 -131 C ATOM 924 C LYS B 56 29.552 -1.679 9.299 1.00 12.04 C ANISOU 924 C LYS B 56 1565 1345 1665 259 26 -150 C ATOM 925 O LYS B 56 30.606 -1.006 9.245 1.00 12.06 O ANISOU 925 O LYS B 56 1540 1406 1637 272 66 -119 O ATOM 926 CB LYS B 56 29.626 -3.628 10.891 1.00 12.80 C ANISOU 926 CB LYS B 56 1703 1304 1855 242 -30 -164 C ATOM 927 CG LYS B 56 29.635 -4.042 12.360 1.00 13.21 C ANISOU 927 CG LYS B 56 1763 1301 1957 204 -33 -116 C ATOM 928 CD LYS B 56 30.227 -5.447 12.437 1.00 14.88 C ANISOU 928 CD LYS B 56 2005 1448 2202 252 -75 -144 C ATOM 929 CE LYS B 56 30.200 -5.968 13.872 1.00 15.21 C ANISOU 929 CE LYS B 56 2056 1435 2289 219 -81 -80 C ATOM 930 NZ LYS B 56 30.913 -7.279 13.852 1.00 16.80 N ANISOU 930 NZ LYS B 56 2290 1568 2523 281 -122 -103 N ATOM 931 N HIS B 57 28.777 -1.894 8.229 1.00 12.10 N ANISOU 931 N HIS B 57 1582 1367 1647 281 -2 -192 N ATOM 932 CA HIS B 57 29.175 -1.362 6.926 1.00 12.32 C ANISOU 932 CA HIS B 57 1594 1490 1596 338 19 -200 C ATOM 933 C HIS B 57 29.274 0.167 6.927 1.00 11.57 C ANISOU 933 C HIS B 57 1467 1445 1482 308 76 -118 C ATOM 934 O HIS B 57 29.987 0.725 6.101 1.00 12.61 O ANISOU 934 O HIS B 57 1574 1661 1556 345 111 -90 O ATOM 935 CB HIS B 57 28.297 -1.839 5.744 1.00 13.08 C ANISOU 935 CB HIS B 57 1710 1608 1653 374 -33 -265 C ATOM 936 CG HIS B 57 26.845 -1.475 5.861 1.00 13.19 C ANISOU 936 CG HIS B 57 1717 1594 1701 315 -59 -245 C ATOM 937 ND1 HIS B 57 25.844 -2.422 5.842 1.00 13.86 N ANISOU 937 ND1 HIS B 57 1817 1618 1830 286 -133 -298 N ATOM 938 CD2 HIS B 57 26.220 -0.272 5.949 1.00 13.14 C ANISOU 938 CD2 HIS B 57 1683 1616 1692 285 -25 -177 C ATOM 939 CE1 HIS B 57 24.668 -1.824 5.945 1.00 13.79 C ANISOU 939 CE1 HIS B 57 1778 1618 1843 240 -138 -256 C ATOM 940 NE2 HIS B 57 24.865 -0.516 5.981 1.00 12.98 N ANISOU 940 NE2 HIS B 57 1654 1570 1707 249 -72 -187 N ATOM 941 N ALA B 58 28.575 0.821 7.839 1.00 10.89 N ANISOU 941 N ALA B 58 1385 1308 1446 246 84 -78 N ATOM 942 CA ALA B 58 28.567 2.287 7.891 1.00 10.52 C ANISOU 942 CA ALA B 58 1326 1277 1395 220 126 -10 C ATOM 943 C ALA B 58 29.591 2.848 8.863 1.00 10.50 C ANISOU 943 C ALA B 58 1317 1253 1421 181 152 26 C ATOM 944 O ALA B 58 29.698 4.066 9.054 1.00 10.58 O ANISOU 944 O ALA B 58 1327 1251 1443 149 177 76 O ATOM 945 CB ALA B 58 27.163 2.768 8.286 1.00 10.12 C ANISOU 945 CB ALA B 58 1285 1186 1373 195 119 5 C ATOM 946 N ILE B 59 30.288 1.967 9.551 1.00 10.70 N ANISOU 946 N ILE B 59 1341 1263 1462 181 138 -1 N ATOM 947 CA ILE B 59 31.258 2.393 10.576 1.00 11.40 C ANISOU 947 CA ILE B 59 1418 1339 1575 142 147 26 C ATOM 948 C ILE B 59 32.663 2.545 10.002 1.00 11.99 C ANISOU 948 C ILE B 59 1442 1489 1625 158 167 54 C ATOM 949 O ILE B 59 33.150 1.670 9.276 1.00 12.37 O ANISOU 949 O ILE B 59 1470 1592 1639 221 168 29 O ATOM 950 CB ILE B 59 31.290 1.333 11.699 1.00 11.21 C ANISOU 950 CB ILE B 59 1412 1272 1576 140 119 -3 C ATOM 951 CG1 ILE B 59 29.868 1.209 12.302 1.00 11.06 C ANISOU 951 CG1 ILE B 59 1425 1196 1580 120 108 -11 C ATOM 952 CG2 ILE B 59 32.335 1.698 12.765 1.00 11.13 C ANISOU 952 CG2 ILE B 59 1386 1265 1577 107 116 18 C ATOM 953 CD1 ILE B 59 29.793 0.292 13.514 1.00 10.94 C ANISOU 953 CD1 ILE B 59 1425 1141 1589 110 89 -13 C ATOM 954 N SER B 60 33.305 3.666 10.317 1.00 12.65 N ANISOU 954 N SER B 60 1502 1576 1728 102 181 107 N ATOM 955 CA SER B 60 34.734 3.812 10.089 1.00 13.27 C ANISOU 955 CA SER B 60 1513 1730 1800 95 195 150 C ATOM 956 C SER B 60 35.552 3.279 11.278 1.00 13.35 C ANISOU 956 C SER B 60 1506 1733 1834 77 165 132 C ATOM 957 O SER B 60 36.377 2.381 11.105 1.00 13.72 O ANISOU 957 O SER B 60 1509 1842 1860 131 166 125 O ATOM 958 CB SER B 60 35.083 5.287 9.789 1.00 14.40 C ANISOU 958 CB SER B 60 1630 1875 1966 26 215 228 C ATOM 959 OG SER B 60 36.424 5.556 10.148 1.00 16.40 O ANISOU 959 OG SER B 60 1815 2174 2244 -22 210 272 O ATOM 960 N ATHR B 61 35.326 3.821 12.468 0.50 12.88 N ANISOU 960 N ATHR B 61 1482 1605 1808 15 136 124 N ATOM 961 N BTHR B 61 35.297 3.816 12.482 0.50 12.32 N ANISOU 961 N BTHR B 61 1412 1532 1737 16 136 123 N ATOM 962 CA ATHR B 61 36.152 3.437 13.591 0.50 13.38 C ANISOU 962 CA ATHR B 61 1525 1678 1882 -2 101 115 C ATOM 963 CA BTHR B 61 36.216 3.688 13.628 0.50 12.42 C ANISOU 963 CA BTHR B 61 1400 1553 1764 -17 99 121 C ATOM 964 C ATHR B 61 35.310 3.327 14.850 0.50 12.80 C ANISOU 964 C ATHR B 61 1521 1530 1811 -15 73 75 C ATOM 965 C BTHR B 61 35.499 3.574 14.985 0.50 12.34 C ANISOU 965 C BTHR B 61 1459 1473 1758 -32 68 80 C ATOM 966 O ATHR B 61 34.225 3.901 14.947 0.50 11.99 O ANISOU 966 O ATHR B 61 1475 1370 1713 -28 82 62 O ATOM 967 O BTHR B 61 34.654 4.404 15.284 0.50 11.96 O ANISOU 967 O BTHR B 61 1464 1363 1717 -61 69 67 O ATOM 968 CB ATHR B 61 37.294 4.443 13.813 0.50 14.40 C ANISOU 968 CB ATHR B 61 1594 1839 2037 -79 84 162 C ATOM 969 CB BTHR B 61 37.145 4.916 13.685 0.50 12.71 C ANISOU 969 CB BTHR B 61 1389 1607 1833 -101 88 171 C ATOM 970 OG1ATHR B 61 38.195 3.950 14.818 0.50 15.65 O ANISOU 970 OG1ATHR B 61 1718 2031 2196 -86 42 154 O ATOM 971 OG1BTHR B 61 38.071 4.864 12.593 0.50 12.55 O ANISOU 971 OG1BTHR B 61 1280 1686 1804 -85 122 230 O ATOM 972 CG2ATHR B 61 36.731 5.724 14.279 0.50 14.28 C ANISOU 972 CG2ATHR B 61 1636 1736 2052 -152 66 158 C ATOM 973 CG2BTHR B 61 37.921 4.971 14.994 0.50 13.11 C ANISOU 973 CG2BTHR B 61 1425 1658 1897 -149 31 157 C ATOM 974 N VAL B 62 35.835 2.556 15.788 1.00 12.62 N ANISOU 974 N VAL B 62 1491 1524 1782 0 43 65 N ATOM 975 CA VAL B 62 35.308 2.450 17.155 1.00 12.57 C ANISOU 975 CA VAL B 62 1537 1477 1762 -10 17 43 C ATOM 976 C VAL B 62 36.479 2.722 18.112 1.00 13.82 C ANISOU 976 C VAL B 62 1662 1677 1913 -46 -31 48 C ATOM 977 O VAL B 62 37.537 2.080 18.013 1.00 13.66 O ANISOU 977 O VAL B 62 1577 1720 1893 -23 -45 70 O ATOM 978 CB VAL B 62 34.740 1.056 17.445 1.00 12.22 C ANISOU 978 CB VAL B 62 1516 1417 1711 48 20 39 C ATOM 979 CG1 VAL B 62 34.200 0.995 18.872 1.00 12.18 C ANISOU 979 CG1 VAL B 62 1555 1391 1680 40 3 38 C ATOM 980 CG2 VAL B 62 33.614 0.724 16.450 1.00 11.76 C ANISOU 980 CG2 VAL B 62 1481 1320 1666 73 50 29 C ATOM 981 N VAL B 63 36.285 3.668 19.026 1.00 15.39 N ANISOU 981 N VAL B 63 1903 1843 2100 -95 -61 22 N ATOM 982 CA VAL B 63 37.368 4.090 19.964 1.00 18.03 C ANISOU 982 CA VAL B 63 2210 2215 2425 -143 -125 14 C ATOM 983 C VAL B 63 36.765 4.328 21.337 1.00 18.18 C ANISOU 983 C VAL B 63 2306 2208 2392 -137 -155 -32 C ATOM 984 O VAL B 63 35.680 4.916 21.415 1.00 18.77 O ANISOU 984 O VAL B 63 2451 2223 2459 -131 -130 -62 O ATOM 985 CB VAL B 63 37.941 5.494 19.605 1.00 20.22 C ANISOU 985 CB VAL B 63 2468 2467 2747 -233 -153 14 C ATOM 986 CG1 VAL B 63 39.370 5.653 20.120 1.00 22.61 C ANISOU 986 CG1 VAL B 63 2694 2836 3060 -291 -222 27 C ATOM 987 CG2 VAL B 63 37.796 5.860 18.141 1.00 23.19 C ANISOU 987 CG2 VAL B 63 2815 2830 3166 -242 -98 57 C ATOM 988 N PRO B 64 37.477 3.975 22.438 1.00 19.06 N ANISOU 988 N PRO B 64 2404 2377 2462 -134 -211 -39 N ATOM 989 CA PRO B 64 36.952 4.452 23.730 1.00 20.09 C ANISOU 989 CA PRO B 64 2612 2495 2525 -128 -244 -92 C ATOM 990 C PRO B 64 36.873 5.977 23.722 1.00 20.99 C ANISOU 990 C PRO B 64 2775 2540 2660 -193 -277 -153 C ATOM 991 O PRO B 64 37.780 6.640 23.188 1.00 20.99 O ANISOU 991 O PRO B 64 2727 2528 2721 -270 -315 -147 O ATOM 992 CB PRO B 64 38.004 3.976 24.752 1.00 20.60 C ANISOU 992 CB PRO B 64 2639 2647 2541 -125 -315 -87 C ATOM 993 CG PRO B 64 38.679 2.822 24.084 1.00 20.21 C ANISOU 993 CG PRO B 64 2504 2646 2528 -91 -294 -17 C ATOM 994 CD PRO B 64 38.636 3.077 22.601 1.00 19.68 C ANISOU 994 CD PRO B 64 2402 2540 2537 -114 -243 1 C ATOM 995 N SER B 65 35.786 6.532 24.270 1.00 22.34 N ANISOU 995 N SER B 65 3038 2661 2787 -159 -259 -206 N ATOM 996 CA ASER B 65 35.583 7.982 24.382 0.50 23.85 C ANISOU 996 CA ASER B 65 3301 2764 2995 -199 -295 -277 C ATOM 997 CA BSER B 65 35.657 7.985 24.311 0.50 23.50 C ANISOU 997 CA BSER B 65 3251 2720 2958 -205 -296 -273 C ATOM 998 C SER B 65 36.506 8.574 25.437 1.00 25.64 C ANISOU 998 C SER B 65 3550 3004 3188 -248 -403 -346 C ATOM 999 O SER B 65 36.837 7.891 26.414 1.00 26.38 O ANISOU 999 O SER B 65 3633 3187 3201 -214 -436 -353 O ATOM 1000 CB ASER B 65 34.136 8.294 24.778 0.50 24.29 C ANISOU 1000 CB ASER B 65 3448 2783 2998 -119 -242 -317 C ATOM 1001 CB BSER B 65 34.193 8.418 24.435 0.50 23.49 C ANISOU 1001 CB BSER B 65 3337 2664 2924 -134 -238 -308 C ATOM 1002 OG ASER B 65 33.245 8.122 23.692 0.50 23.61 O ANISOU 1002 OG ASER B 65 3346 2664 2960 -93 -160 -266 O ATOM 1003 OG BSER B 65 33.525 7.718 25.470 0.50 22.83 O ANISOU 1003 OG BSER B 65 3284 2651 2741 -51 -212 -316 O TER 1004 SER B 65 ATOM 1005 N SER C 6 11.456 -13.452 0.662 1.00 33.55 N ANISOU 1005 N SER C 6 4713 3633 4402 -602 -117 800 N ATOM 1006 CA SER C 6 11.744 -12.096 0.133 1.00 29.91 C ANISOU 1006 CA SER C 6 4159 3311 3894 -521 -116 705 C ATOM 1007 C SER C 6 10.557 -11.146 0.319 1.00 28.52 C ANISOU 1007 C SER C 6 3879 3324 3635 -571 -76 737 C ATOM 1008 O SER C 6 9.393 -11.509 0.112 1.00 28.30 O ANISOU 1008 O SER C 6 3816 3339 3598 -700 -52 772 O ATOM 1009 CB SER C 6 12.130 -12.164 -1.350 1.00 30.25 C ANISOU 1009 CB SER C 6 4195 3305 3994 -529 -130 568 C ATOM 1010 OG SER C 6 12.668 -10.937 -1.806 1.00 28.60 O ANISOU 1010 OG SER C 6 3916 3201 3751 -439 -133 496 O ATOM 1011 N LEU C 7 10.884 -9.938 0.755 1.00 25.34 N ANISOU 1011 N LEU C 7 3422 3030 3174 -467 -69 722 N ATOM 1012 CA LEU C 7 10.008 -8.779 0.678 1.00 23.89 C ANISOU 1012 CA LEU C 7 3134 3012 2932 -467 -33 715 C ATOM 1013 C LEU C 7 10.447 -7.971 -0.532 1.00 21.28 C ANISOU 1013 C LEU C 7 2760 2698 2630 -421 -48 612 C ATOM 1014 O LEU C 7 9.616 -7.413 -1.249 1.00 21.31 O ANISOU 1014 O LEU C 7 2680 2797 2618 -458 -32 597 O ATOM 1015 CB LEU C 7 10.134 -7.931 1.949 1.00 24.90 C ANISOU 1015 CB LEU C 7 3245 3232 2985 -378 -11 752 C ATOM 1016 CG LEU C 7 9.279 -8.282 3.172 1.00 28.18 C ANISOU 1016 CG LEU C 7 3654 3725 3326 -428 29 862 C ATOM 1017 CD1 LEU C 7 7.808 -8.017 2.860 1.00 29.86 C ANISOU 1017 CD1 LEU C 7 3765 4067 3514 -512 78 886 C ATOM 1018 CD2 LEU C 7 9.471 -9.722 3.627 1.00 29.96 C ANISOU 1018 CD2 LEU C 7 3974 3830 3577 -496 8 953 C ATOM 1019 N GLN C 8 11.759 -7.921 -0.770 1.00 19.57 N ANISOU 1019 N GLN C 8 2590 2396 2449 -340 -81 549 N ATOM 1020 CA GLN C 8 12.300 -7.159 -1.912 1.00 18.06 C ANISOU 1020 CA GLN C 8 2359 2225 2279 -301 -93 460 C ATOM 1021 C GLN C 8 11.702 -7.582 -3.249 1.00 18.42 C ANISOU 1021 C GLN C 8 2376 2281 2342 -396 -95 420 C ATOM 1022 O GLN C 8 11.252 -6.753 -4.019 1.00 17.11 O ANISOU 1022 O GLN C 8 2135 2213 2154 -404 -87 403 O ATOM 1023 CB GLN C 8 13.828 -7.263 -2.006 1.00 17.71 C ANISOU 1023 CB GLN C 8 2363 2094 2272 -216 -125 400 C ATOM 1024 CG GLN C 8 14.394 -6.520 -3.227 1.00 17.31 C ANISOU 1024 CG GLN C 8 2266 2075 2235 -192 -130 316 C ATOM 1025 CD GLN C 8 15.900 -6.642 -3.399 1.00 17.19 C ANISOU 1025 CD GLN C 8 2279 1997 2257 -116 -155 252 C ATOM 1026 OE1 GLN C 8 16.465 -6.022 -4.305 1.00 17.09 O ANISOU 1026 OE1 GLN C 8 2226 2020 2248 -99 -154 192 O ATOM 1027 NE2 GLN C 8 16.569 -7.422 -2.526 1.00 17.68 N ANISOU 1027 NE2 GLN C 8 2400 1977 2341 -68 -178 275 N ATOM 1028 N ASP C 9 11.732 -8.884 -3.544 1.00 20.01 N ANISOU 1028 N ASP C 9 2640 2377 2585 -468 -108 402 N ATOM 1029 CA ASP C 9 11.347 -9.326 -4.886 1.00 21.59 C ANISOU 1029 CA ASP C 9 2822 2586 2797 -562 -116 331 C ATOM 1030 C ASP C 9 9.862 -9.087 -5.173 1.00 21.77 C ANISOU 1030 C ASP C 9 2757 2743 2773 -668 -101 376 C ATOM 1031 O ASP C 9 9.527 -8.521 -6.210 1.00 21.36 O ANISOU 1031 O ASP C 9 2631 2797 2689 -691 -107 340 O ATOM 1032 CB ASP C 9 11.816 -10.766 -5.169 1.00 24.04 C ANISOU 1032 CB ASP C 9 3230 2730 3174 -608 -131 275 C ATOM 1033 CG ASP C 9 13.334 -10.843 -5.347 1.00 25.47 C ANISOU 1033 CG ASP C 9 3460 2818 3398 -489 -146 202 C ATOM 1034 OD1 ASP C 9 13.999 -9.783 -5.254 1.00 24.73 O ANISOU 1034 OD1 ASP C 9 3321 2797 3277 -392 -147 197 O ATOM 1035 OD2 ASP C 9 13.868 -11.948 -5.574 1.00 27.37 O ANISOU 1035 OD2 ASP C 9 3782 2914 3706 -492 -156 146 O ATOM 1036 N PRO C 10 8.966 -9.486 -4.253 1.00 22.42 N ANISOU 1036 N PRO C 10 2836 2839 2842 -730 -82 465 N ATOM 1037 CA PRO C 10 7.556 -9.161 -4.513 1.00 22.78 C ANISOU 1037 CA PRO C 10 2772 3042 2840 -820 -66 510 C ATOM 1038 C PRO C 10 7.279 -7.661 -4.661 1.00 21.96 C ANISOU 1038 C PRO C 10 2563 3090 2691 -725 -52 529 C ATOM 1039 O PRO C 10 6.473 -7.262 -5.506 1.00 22.00 O ANISOU 1039 O PRO C 10 2470 3223 2664 -771 -58 531 O ATOM 1040 CB PRO C 10 6.843 -9.739 -3.292 1.00 23.58 C ANISOU 1040 CB PRO C 10 2888 3138 2933 -881 -37 610 C ATOM 1041 CG PRO C 10 7.684 -10.914 -2.930 1.00 24.19 C ANISOU 1041 CG PRO C 10 3103 3016 3073 -895 -54 601 C ATOM 1042 CD PRO C 10 9.104 -10.482 -3.171 1.00 23.39 C ANISOU 1042 CD PRO C 10 3051 2839 2997 -752 -77 527 C ATOM 1043 N PHE C 11 7.960 -6.836 -3.865 1.00 21.28 N ANISOU 1043 N PHE C 11 2497 2984 2603 -594 -38 543 N ATOM 1044 CA PHE C 11 7.821 -5.376 -3.944 1.00 19.84 C ANISOU 1044 CA PHE C 11 2237 2903 2398 -493 -22 554 C ATOM 1045 C PHE C 11 8.212 -4.864 -5.339 1.00 19.92 C ANISOU 1045 C PHE C 11 2217 2938 2416 -481 -50 502 C ATOM 1046 O PHE C 11 7.443 -4.132 -5.975 1.00 19.93 O ANISOU 1046 O PHE C 11 2121 3060 2391 -479 -48 533 O ATOM 1047 CB PHE C 11 8.682 -4.721 -2.858 1.00 19.11 C ANISOU 1047 CB PHE C 11 2196 2756 2309 -373 -8 551 C ATOM 1048 CG PHE C 11 8.494 -3.233 -2.723 1.00 19.61 C ANISOU 1048 CG PHE C 11 2196 2894 2362 -271 17 557 C ATOM 1049 CD1 PHE C 11 7.515 -2.716 -1.870 1.00 19.89 C ANISOU 1049 CD1 PHE C 11 2170 3023 2363 -239 63 606 C ATOM 1050 CD2 PHE C 11 9.309 -2.359 -3.427 1.00 18.94 C ANISOU 1050 CD2 PHE C 11 2114 2777 2305 -206 0 513 C ATOM 1051 CE1 PHE C 11 7.354 -1.340 -1.738 1.00 20.86 C ANISOU 1051 CE1 PHE C 11 2245 3189 2491 -132 90 600 C ATOM 1052 CE2 PHE C 11 9.158 -0.982 -3.304 1.00 19.42 C ANISOU 1052 CE2 PHE C 11 2131 2873 2373 -114 24 521 C ATOM 1053 CZ PHE C 11 8.183 -0.479 -2.449 1.00 19.79 C ANISOU 1053 CZ PHE C 11 2126 2994 2397 -71 69 560 C ATOM 1054 N LEU C 12 9.386 -5.282 -5.825 1.00 19.29 N ANISOU 1054 N LEU C 12 2211 2755 2363 -472 -74 429 N ATOM 1055 CA LEU C 12 9.859 -4.836 -7.134 1.00 19.22 C ANISOU 1055 CA LEU C 12 2174 2781 2347 -466 -94 380 C ATOM 1056 C LEU C 12 9.002 -5.401 -8.260 1.00 20.80 C ANISOU 1056 C LEU C 12 2320 3071 2510 -585 -113 365 C ATOM 1057 O LEU C 12 8.670 -4.687 -9.205 1.00 21.47 O ANISOU 1057 O LEU C 12 2328 3273 2557 -586 -125 381 O ATOM 1058 CB LEU C 12 11.344 -5.197 -7.332 1.00 18.05 C ANISOU 1058 CB LEU C 12 2107 2519 2232 -425 -108 299 C ATOM 1059 CG LEU C 12 12.343 -4.454 -6.442 1.00 17.94 C ANISOU 1059 CG LEU C 12 2126 2446 2244 -311 -100 303 C ATOM 1060 CD1 LEU C 12 13.743 -4.941 -6.773 1.00 18.39 C ANISOU 1060 CD1 LEU C 12 2239 2418 2332 -281 -116 223 C ATOM 1061 CD2 LEU C 12 12.288 -2.933 -6.648 1.00 16.83 C ANISOU 1061 CD2 LEU C 12 1925 2377 2093 -249 -88 336 C ATOM 1062 N ASN C 13 8.641 -6.679 -8.144 1.00 21.39 N ANISOU 1062 N ASN C 13 2438 3094 2597 -691 -120 338 N ATOM 1063 CA ASN C 13 7.774 -7.311 -9.123 1.00 23.16 C ANISOU 1063 CA ASN C 13 2613 3403 2783 -829 -141 309 C ATOM 1064 C ASN C 13 6.419 -6.654 -9.261 1.00 23.19 C ANISOU 1064 C ASN C 13 2485 3591 2736 -862 -141 395 C ATOM 1065 O ASN C 13 5.929 -6.520 -10.375 1.00 24.69 O ANISOU 1065 O ASN C 13 2598 3912 2872 -924 -169 381 O ATOM 1066 CB ASN C 13 7.643 -8.812 -8.884 1.00 24.17 C ANISOU 1066 CB ASN C 13 2823 3411 2949 -947 -145 262 C ATOM 1067 CG ASN C 13 8.733 -9.583 -9.586 1.00 25.58 C ANISOU 1067 CG ASN C 13 3096 3463 3160 -951 -158 136 C ATOM 1068 OD1 ASN C 13 9.072 -9.282 -10.744 1.00 25.75 O ANISOU 1068 OD1 ASN C 13 3085 3559 3138 -952 -172 65 O ATOM 1069 ND2 ASN C 13 9.301 -10.572 -8.898 1.00 25.79 N ANISOU 1069 ND2 ASN C 13 3236 3305 3260 -947 -151 114 N ATOM 1070 N ALA C 14 5.843 -6.222 -8.141 1.00 22.72 N ANISOU 1070 N ALA C 14 2392 3555 2686 -812 -110 482 N ATOM 1071 CA ALA C 14 4.546 -5.546 -8.178 1.00 23.74 C ANISOU 1071 CA ALA C 14 2381 3866 2774 -817 -102 566 C ATOM 1072 C ALA C 14 4.692 -4.212 -8.906 1.00 23.11 C ANISOU 1072 C ALA C 14 2233 3874 2675 -706 -113 596 C ATOM 1073 O ALA C 14 3.898 -3.887 -9.775 1.00 23.40 O ANISOU 1073 O ALA C 14 2158 4067 2664 -740 -138 633 O ATOM 1074 CB ALA C 14 3.990 -5.351 -6.779 1.00 24.08 C ANISOU 1074 CB ALA C 14 2405 3916 2828 -773 -55 640 C ATOM 1075 N LEU C 15 5.747 -3.468 -8.570 1.00 22.01 N ANISOU 1075 N LEU C 15 2161 3630 2573 -581 -98 583 N ATOM 1076 CA LEU C 15 6.013 -2.207 -9.220 1.00 22.17 C ANISOU 1076 CA LEU C 15 2138 3697 2589 -483 -104 617 C ATOM 1077 C LEU C 15 6.219 -2.375 -10.721 1.00 22.47 C ANISOU 1077 C LEU C 15 2151 3811 2578 -551 -147 588 C ATOM 1078 O LEU C 15 5.771 -1.537 -11.508 1.00 22.40 O ANISOU 1078 O LEU C 15 2053 3925 2535 -520 -165 656 O ATOM 1079 CB LEU C 15 7.270 -1.582 -8.624 1.00 20.48 C ANISOU 1079 CB LEU C 15 2016 3340 2427 -373 -84 587 C ATOM 1080 CG LEU C 15 7.154 -1.044 -7.195 1.00 20.10 C ANISOU 1080 CG LEU C 15 1986 3239 2413 -280 -41 612 C ATOM 1081 CD1 LEU C 15 8.541 -0.566 -6.759 1.00 18.42 C ANISOU 1081 CD1 LEU C 15 1866 2892 2240 -203 -35 561 C ATOM 1082 CD2 LEU C 15 6.142 0.099 -7.106 1.00 20.90 C ANISOU 1082 CD2 LEU C 15 1984 3441 2516 -196 -18 693 C ATOM 1083 N ARG C 16 6.902 -3.458 -11.100 1.00 22.80 N ANISOU 1083 N ARG C 16 2272 3780 2613 -638 -162 487 N ATOM 1084 CA AARG C 16 7.218 -3.719 -12.500 0.50 23.88 C ANISOU 1084 CA AARG C 16 2395 3989 2689 -708 -195 430 C ATOM 1085 CA BARG C 16 7.224 -3.742 -12.498 0.50 24.05 C ANISOU 1085 CA BARG C 16 2419 4009 2711 -709 -195 428 C ATOM 1086 C ARG C 16 5.960 -4.134 -13.275 1.00 25.43 C ANISOU 1086 C ARG C 16 2488 4363 2811 -830 -231 448 C ATOM 1087 O ARG C 16 5.692 -3.620 -14.365 1.00 25.40 O ANISOU 1087 O ARG C 16 2404 4514 2734 -843 -262 482 O ATOM 1088 CB AARG C 16 8.321 -4.781 -12.611 0.50 23.72 C ANISOU 1088 CB AARG C 16 2490 3830 2692 -750 -192 300 C ATOM 1089 CB BARG C 16 8.280 -4.860 -12.577 0.50 24.23 C ANISOU 1089 CB BARG C 16 2556 3891 2757 -756 -192 297 C ATOM 1090 CG AARG C 16 8.643 -5.231 -14.035 0.50 24.77 C ANISOU 1090 CG AARG C 16 2616 4042 2753 -832 -217 209 C ATOM 1091 CG BARG C 16 8.704 -5.269 -13.988 0.50 25.51 C ANISOU 1091 CG BARG C 16 2717 4124 2851 -830 -215 204 C ATOM 1092 CD AARG C 16 9.505 -6.480 -14.014 0.50 25.06 C ANISOU 1092 CD AARG C 16 2765 3930 2828 -874 -207 67 C ATOM 1093 CD BARG C 16 9.706 -6.417 -13.947 0.50 26.05 C ANISOU 1093 CD BARG C 16 2900 4036 2961 -855 -203 65 C ATOM 1094 NE AARG C 16 9.518 -7.181 -15.292 0.50 26.95 N ANISOU 1094 NE AARG C 16 2998 4249 2993 -981 -226 -48 N ATOM 1095 NE BARG C 16 9.106 -7.724 -14.205 0.50 27.82 N ANISOU 1095 NE BARG C 16 3151 4241 3177 -994 -218 -22 N ATOM 1096 CZ AARG C 16 8.532 -7.968 -15.717 0.50 27.49 C ANISOU 1096 CZ AARG C 16 3038 4387 3019 -1124 -253 -91 C ATOM 1097 CZ BARG C 16 8.147 -8.269 -13.477 0.50 28.46 C ANISOU 1097 CZ BARG C 16 3229 4295 3290 -1066 -222 19 C ATOM 1098 NH1AARG C 16 7.450 -8.126 -14.979 0.50 27.73 N ANISOU 1098 NH1AARG C 16 3033 4428 3076 -1175 -260 -14 N ATOM 1099 NH1BARG C 16 7.661 -9.465 -13.790 0.50 29.36 N ANISOU 1099 NH1BARG C 16 3374 4378 3402 -1212 -236 -68 N ATOM 1100 NH2AARG C 16 8.625 -8.579 -16.889 0.50 29.74 N ANISOU 1100 NH2AARG C 16 3323 4747 3228 -1223 -269 -218 N ATOM 1101 NH2BARG C 16 7.662 -7.607 -12.441 0.50 29.34 N ANISOU 1101 NH2BARG C 16 3304 4411 3431 -1000 -207 142 N ATOM 1102 N ARG C 17 5.184 -5.052 -12.710 1.00 27.56 N ANISOU 1102 N ARG C 17 2755 4623 3094 -926 -229 433 N ATOM 1103 CA ARG C 17 3.983 -5.538 -13.394 1.00 30.32 C ANISOU 1103 CA ARG C 17 2999 5147 3374 -1067 -266 439 C ATOM 1104 C ARG C 17 2.901 -4.471 -13.531 1.00 31.04 C ANISOU 1104 C ARG C 17 2933 5437 3425 -1009 -279 574 C ATOM 1105 O ARG C 17 2.196 -4.412 -14.551 1.00 31.03 O ANISOU 1105 O ARG C 17 2820 5630 3338 -1083 -326 595 O ATOM 1106 CB ARG C 17 3.454 -6.802 -12.720 1.00 33.86 C ANISOU 1106 CB ARG C 17 3487 5522 3856 -1200 -257 394 C ATOM 1107 CG ARG C 17 4.216 -8.041 -13.155 1.00 36.97 C ANISOU 1107 CG ARG C 17 4006 5774 4266 -1303 -266 246 C ATOM 1108 CD ARG C 17 3.360 -9.296 -13.025 1.00 43.80 C ANISOU 1108 CD ARG C 17 4875 6627 5140 -1493 -277 202 C ATOM 1109 NE ARG C 17 3.711 -10.053 -11.828 1.00 46.47 N ANISOU 1109 NE ARG C 17 5333 6748 5575 -1491 -239 203 N ATOM 1110 CZ ARG C 17 4.652 -10.994 -11.784 1.00 48.96 C ANISOU 1110 CZ ARG C 17 5796 6852 5953 -1506 -232 99 C ATOM 1111 NH1 ARG C 17 5.339 -11.305 -12.874 1.00 49.57 N ANISOU 1111 NH1 ARG C 17 5918 6909 6006 -1526 -251 -34 N ATOM 1112 NH2 ARG C 17 4.907 -11.627 -10.646 1.00 50.27 N ANISOU 1112 NH2 ARG C 17 6062 6835 6203 -1495 -203 132 N ATOM 1113 N GLU C 18 2.795 -3.610 -12.524 1.00 30.98 N ANISOU 1113 N GLU C 18 2912 5384 3476 -871 -238 662 N ATOM 1114 CA GLU C 18 1.770 -2.571 -12.499 1.00 31.97 C ANISOU 1114 CA GLU C 18 2890 5670 3585 -785 -239 790 C ATOM 1115 C GLU C 18 2.246 -1.273 -13.127 1.00 30.55 C ANISOU 1115 C GLU C 18 2692 5511 3404 -647 -249 859 C ATOM 1116 O GLU C 18 1.498 -0.296 -13.170 1.00 30.38 O ANISOU 1116 O GLU C 18 2559 5601 3385 -547 -251 973 O ATOM 1117 CB GLU C 18 1.283 -2.331 -11.074 1.00 34.34 C ANISOU 1117 CB GLU C 18 3177 5924 3946 -709 -182 838 C ATOM 1118 CG GLU C 18 0.373 -3.428 -10.537 1.00 38.50 C ANISOU 1118 CG GLU C 18 3663 6506 4459 -854 -174 825 C ATOM 1119 CD GLU C 18 0.373 -3.484 -9.023 1.00 42.19 C ANISOU 1119 CD GLU C 18 4182 6870 4979 -798 -108 839 C ATOM 1120 OE1 GLU C 18 0.638 -2.437 -8.379 1.00 43.91 O ANISOU 1120 OE1 GLU C 18 4409 7042 5235 -631 -69 877 O ATOM 1121 OE2 GLU C 18 0.118 -4.580 -8.477 1.00 42.55 O ANISOU 1121 OE2 GLU C 18 4262 6877 5026 -928 -95 813 O ATOM 1122 N ARG C 19 3.481 -1.291 -13.640 1.00 29.46 N ANISOU 1122 N ARG C 19 2661 5267 3265 -643 -254 793 N ATOM 1123 CA ARG C 19 4.094 -0.153 -14.330 1.00 29.30 C ANISOU 1123 CA ARG C 19 2639 5254 3240 -541 -262 857 C ATOM 1124 C ARG C 19 3.955 1.119 -13.507 1.00 28.42 C ANISOU 1124 C ARG C 19 2512 5074 3212 -372 -224 955 C ATOM 1125 O ARG C 19 3.614 2.192 -14.022 1.00 28.09 O ANISOU 1125 O ARG C 19 2396 5109 3169 -282 -237 1071 O ATOM 1126 CB ARG C 19 3.481 0.024 -15.721 1.00 32.29 C ANISOU 1126 CB ARG C 19 2902 5856 3512 -597 -322 921 C ATOM 1127 CG ARG C 19 3.304 -1.290 -16.456 1.00 35.47 C ANISOU 1127 CG ARG C 19 3299 6355 3823 -782 -360 809 C ATOM 1128 CD ARG C 19 4.363 -1.461 -17.515 1.00 39.38 C ANISOU 1128 CD ARG C 19 3858 6851 4252 -827 -375 733 C ATOM 1129 NE ARG C 19 3.894 -0.935 -18.791 1.00 43.37 N ANISOU 1129 NE ARG C 19 4251 7588 4639 -849 -429 822 N ATOM 1130 CZ ARG C 19 3.230 -1.645 -19.699 1.00 45.43 C ANISOU 1130 CZ ARG C 19 4434 8048 4779 -993 -483 776 C ATOM 1131 NH1 ARG C 19 2.940 -2.924 -19.475 1.00 47.56 N ANISOU 1131 NH1 ARG C 19 4734 8291 5046 -1135 -487 637 N ATOM 1132 NH2 ARG C 19 2.854 -1.070 -20.831 1.00 45.63 N ANISOU 1132 NH2 ARG C 19 4352 8300 4685 -1000 -536 874 N ATOM 1133 N VAL C 20 4.228 0.975 -12.213 1.00 27.09 N ANISOU 1133 N VAL C 20 2419 4757 3116 -329 -176 905 N ATOM 1134 CA VAL C 20 4.074 2.049 -11.252 1.00 26.40 C ANISOU 1134 CA VAL C 20 2328 4595 3106 -178 -130 961 C ATOM 1135 C VAL C 20 5.225 3.039 -11.433 1.00 25.01 C ANISOU 1135 C VAL C 20 2234 4286 2981 -90 -119 968 C ATOM 1136 O VAL C 20 6.387 2.634 -11.409 1.00 23.30 O ANISOU 1136 O VAL C 20 2121 3960 2771 -132 -118 882 O ATOM 1137 CB VAL C 20 4.123 1.494 -9.807 1.00 25.75 C ANISOU 1137 CB VAL C 20 2311 4412 3062 -178 -83 893 C ATOM 1138 CG1 VAL C 20 3.811 2.590 -8.802 1.00 26.23 C ANISOU 1138 CG1 VAL C 20 2355 4424 3186 -26 -31 933 C ATOM 1139 CG2 VAL C 20 3.174 0.306 -9.651 1.00 27.56 C ANISOU 1139 CG2 VAL C 20 2481 4749 3242 -306 -92 879 C ATOM 1140 N PRO C 21 4.913 4.338 -11.631 1.00 24.71 N ANISOU 1140 N PRO C 21 2148 4256 2986 32 -112 1073 N ATOM 1141 CA PRO C 21 5.997 5.326 -11.601 1.00 24.28 C ANISOU 1141 CA PRO C 21 2181 4045 2998 107 -93 1077 C ATOM 1142 C PRO C 21 6.714 5.302 -10.253 1.00 22.34 C ANISOU 1142 C PRO C 21 2041 3630 2817 142 -48 973 C ATOM 1143 O PRO C 21 6.077 5.332 -9.195 1.00 21.84 O ANISOU 1143 O PRO C 21 1963 3557 2780 197 -12 955 O ATOM 1144 CB PRO C 21 5.273 6.663 -11.807 1.00 25.33 C ANISOU 1144 CB PRO C 21 2242 4196 3185 243 -86 1212 C ATOM 1145 CG PRO C 21 4.041 6.288 -12.549 1.00 26.75 C ANISOU 1145 CG PRO C 21 2281 4596 3288 211 -128 1297 C ATOM 1146 CD PRO C 21 3.631 4.935 -12.039 1.00 26.60 C ANISOU 1146 CD PRO C 21 2247 4648 3213 98 -128 1199 C ATOM 1147 N VAL C 22 8.035 5.240 -10.309 1.00 21.28 N ANISOU 1147 N VAL C 22 2003 3385 2696 106 -49 905 N ATOM 1148 CA VAL C 22 8.847 5.172 -9.089 1.00 20.55 C ANISOU 1148 CA VAL C 22 2006 3151 2651 128 -18 805 C ATOM 1149 C VAL C 22 9.914 6.250 -9.061 1.00 20.14 C ANISOU 1149 C VAL C 22 2020 2965 2666 176 -5 798 C ATOM 1150 O VAL C 22 10.311 6.787 -10.103 1.00 20.61 O ANISOU 1150 O VAL C 22 2069 3033 2728 161 -22 860 O ATOM 1151 CB VAL C 22 9.502 3.782 -8.878 1.00 20.67 C ANISOU 1151 CB VAL C 22 2075 3157 2621 29 -33 705 C ATOM 1152 CG1 VAL C 22 8.423 2.728 -8.658 1.00 21.87 C ANISOU 1152 CG1 VAL C 22 2177 3408 2723 -28 -38 707 C ATOM 1153 CG2 VAL C 22 10.454 3.413 -10.019 1.00 20.85 C ANISOU 1153 CG2 VAL C 22 2118 3193 2609 -45 -63 680 C ATOM 1154 N SER C 23 10.324 6.594 -7.849 1.00 19.95 N ANISOU 1154 N SER C 23 2059 2828 2693 226 25 725 N ATOM 1155 CA SER C 23 11.476 7.417 -7.620 1.00 19.50 C ANISOU 1155 CA SER C 23 2075 2639 2697 242 35 684 C ATOM 1156 C SER C 23 12.537 6.493 -7.021 1.00 18.68 C ANISOU 1156 C SER C 23 2029 2505 2561 179 22 574 C ATOM 1157 O SER C 23 12.257 5.779 -6.057 1.00 19.11 O ANISOU 1157 O SER C 23 2098 2575 2587 183 29 521 O ATOM 1158 CB SER C 23 11.143 8.543 -6.640 1.00 20.10 C ANISOU 1158 CB SER C 23 2176 2612 2849 346 77 668 C ATOM 1159 OG SER C 23 10.211 9.456 -7.208 1.00 21.97 O ANISOU 1159 OG SER C 23 2357 2858 3132 426 89 779 O ATOM 1160 N ILE C 24 13.722 6.462 -7.623 1.00 17.37 N ANISOU 1160 N ILE C 24 1890 2313 2397 123 4 550 N ATOM 1161 CA ILE C 24 14.852 5.744 -7.045 1.00 17.17 C ANISOU 1161 CA ILE C 24 1912 2255 2358 85 -10 450 C ATOM 1162 C ILE C 24 15.862 6.774 -6.516 1.00 17.46 C ANISOU 1162 C ILE C 24 1994 2187 2456 100 -1 404 C ATOM 1163 O ILE C 24 16.400 7.579 -7.281 1.00 18.17 O ANISOU 1163 O ILE C 24 2078 2244 2582 76 2 443 O ATOM 1164 CB ILE C 24 15.504 4.761 -8.056 1.00 17.23 C ANISOU 1164 CB ILE C 24 1904 2328 2316 12 -35 434 C ATOM 1165 CG1 ILE C 24 14.462 3.699 -8.490 1.00 18.30 C ANISOU 1165 CG1 ILE C 24 2004 2557 2392 -19 -46 458 C ATOM 1166 CG2 ILE C 24 16.733 4.119 -7.423 1.00 17.20 C ANISOU 1166 CG2 ILE C 24 1941 2284 2311 -3 -48 338 C ATOM 1167 CD1 ILE C 24 14.928 2.626 -9.467 1.00 19.72 C ANISOU 1167 CD1 ILE C 24 2174 2798 2520 -90 -65 419 C ATOM 1168 N TYR C 25 16.071 6.798 -5.206 1.00 17.31 N ANISOU 1168 N TYR C 25 2015 2119 2443 130 5 327 N ATOM 1169 CA TYR C 25 17.062 7.712 -4.628 1.00 17.88 C ANISOU 1169 CA TYR C 25 2128 2101 2565 126 7 262 C ATOM 1170 C TYR C 25 18.400 6.993 -4.553 1.00 17.33 C ANISOU 1170 C TYR C 25 2061 2056 2466 71 -27 197 C ATOM 1171 O TYR C 25 18.476 5.847 -4.082 1.00 16.52 O ANISOU 1171 O TYR C 25 1961 2005 2311 74 -47 165 O ATOM 1172 CB TYR C 25 16.636 8.190 -3.249 1.00 19.49 C ANISOU 1172 CB TYR C 25 2369 2258 2777 184 29 198 C ATOM 1173 CG TYR C 25 15.441 9.118 -3.275 1.00 20.39 C ANISOU 1173 CG TYR C 25 2476 2331 2940 258 70 248 C ATOM 1174 CD1 TYR C 25 14.145 8.612 -3.231 1.00 20.90 C ANISOU 1174 CD1 TYR C 25 2498 2476 2966 306 88 301 C ATOM 1175 CD2 TYR C 25 15.611 10.492 -3.350 1.00 21.69 C ANISOU 1175 CD2 TYR C 25 2671 2374 3195 281 93 244 C ATOM 1176 CE1 TYR C 25 13.038 9.454 -3.249 1.00 21.91 C ANISOU 1176 CE1 TYR C 25 2602 2582 3141 390 127 349 C ATOM 1177 CE2 TYR C 25 14.512 11.341 -3.373 1.00 23.11 C ANISOU 1177 CE2 TYR C 25 2844 2505 3433 371 133 293 C ATOM 1178 CZ TYR C 25 13.232 10.811 -3.318 1.00 23.32 C ANISOU 1178 CZ TYR C 25 2814 2631 3414 433 150 345 C ATOM 1179 OH TYR C 25 12.131 11.646 -3.332 1.00 23.90 O ANISOU 1179 OH TYR C 25 2863 2671 3547 538 191 395 O ATOM 1180 N LEU C 26 19.441 7.648 -5.051 1.00 17.09 N ANISOU 1180 N LEU C 26 2026 1992 2476 22 -32 187 N ATOM 1181 CA LEU C 26 20.776 7.056 -5.058 1.00 17.17 C ANISOU 1181 CA LEU C 26 2018 2042 2464 -24 -61 127 C ATOM 1182 C LEU C 26 21.570 7.499 -3.852 1.00 18.24 C ANISOU 1182 C LEU C 26 2179 2139 2613 -29 -78 34 C ATOM 1183 O LEU C 26 21.168 8.419 -3.157 1.00 18.70 O ANISOU 1183 O LEU C 26 2276 2124 2705 -10 -62 8 O ATOM 1184 CB LEU C 26 21.514 7.441 -6.336 1.00 17.34 C ANISOU 1184 CB LEU C 26 1999 2084 2504 -88 -53 169 C ATOM 1185 CG LEU C 26 20.781 7.128 -7.628 1.00 17.38 C ANISOU 1185 CG LEU C 26 1974 2150 2480 -94 -39 259 C ATOM 1186 CD1 LEU C 26 21.639 7.596 -8.795 1.00 17.55 C ANISOU 1186 CD1 LEU C 26 1955 2207 2506 -165 -27 300 C ATOM 1187 CD2 LEU C 26 20.487 5.628 -7.757 1.00 16.91 C ANISOU 1187 CD2 LEU C 26 1902 2170 2355 -77 -55 234 C ATOM 1188 N VAL C 27 22.705 6.840 -3.616 1.00 18.60 N ANISOU 1188 N VAL C 27 2198 2240 2630 -51 -113 -21 N ATOM 1189 CA VAL C 27 23.537 7.126 -2.453 1.00 19.21 C ANISOU 1189 CA VAL C 27 2283 2314 2700 -63 -143 -111 C ATOM 1190 C VAL C 27 24.134 8.550 -2.477 1.00 20.25 C ANISOU 1190 C VAL C 27 2422 2375 2899 -132 -133 -146 C ATOM 1191 O VAL C 27 24.457 9.087 -1.429 1.00 20.52 O ANISOU 1191 O VAL C 27 2481 2385 2933 -145 -149 -230 O ATOM 1192 CB VAL C 27 24.643 6.055 -2.215 1.00 19.50 C ANISOU 1192 CB VAL C 27 2274 2442 2693 -58 -190 -149 C ATOM 1193 CG1 VAL C 27 24.039 4.752 -1.699 1.00 21.04 C ANISOU 1193 CG1 VAL C 27 2491 2671 2831 12 -206 -127 C ATOM 1194 CG2 VAL C 27 25.465 5.797 -3.470 1.00 20.13 C ANISOU 1194 CG2 VAL C 27 2289 2569 2791 -97 -184 -127 C ATOM 1195 N ASN C 28 24.261 9.144 -3.659 1.00 19.92 N ANISOU 1195 N ASN C 28 2359 2301 2908 -182 -106 -82 N ATOM 1196 CA ASN C 28 24.763 10.519 -3.784 1.00 21.95 C ANISOU 1196 CA ASN C 28 2630 2465 3243 -260 -90 -94 C ATOM 1197 C ASN C 28 23.669 11.592 -3.702 1.00 22.15 C ANISOU 1197 C ASN C 28 2727 2353 3338 -227 -51 -60 C ATOM 1198 O ASN C 28 23.919 12.783 -3.931 1.00 23.22 O ANISOU 1198 O ASN C 28 2890 2376 3558 -285 -31 -50 O ATOM 1199 CB ASN C 28 25.607 10.676 -5.049 1.00 22.42 C ANISOU 1199 CB ASN C 28 2629 2566 3323 -344 -79 -33 C ATOM 1200 CG ASN C 28 24.787 10.615 -6.323 1.00 22.82 C ANISOU 1200 CG ASN C 28 2675 2623 3372 -324 -45 93 C ATOM 1201 OD1 ASN C 28 23.697 10.021 -6.367 1.00 21.27 O ANISOU 1201 OD1 ASN C 28 2497 2443 3141 -244 -41 130 O ATOM 1202 ND2 ASN C 28 25.320 11.225 -7.387 1.00 23.34 N ANISOU 1202 ND2 ASN C 28 2709 2693 3468 -406 -23 166 N ATOM 1203 N GLY C 29 22.451 11.148 -3.392 1.00 22.81 N ANISOU 1203 N GLY C 29 2835 2444 3389 -131 -37 -36 N ATOM 1204 CA GLY C 29 21.326 12.053 -3.152 1.00 24.75 C ANISOU 1204 CA GLY C 29 3135 2576 3694 -69 2 -15 C ATOM 1205 C GLY C 29 20.513 12.328 -4.397 1.00 25.18 C ANISOU 1205 C GLY C 29 3173 2609 3786 -42 30 129 C ATOM 1206 O GLY C 29 19.477 12.982 -4.328 1.00 26.24 O ANISOU 1206 O GLY C 29 3336 2664 3970 31 61 169 O ATOM 1207 N ILE C 30 21.002 11.854 -5.543 1.00 24.55 N ANISOU 1207 N ILE C 30 3042 2610 3677 -98 18 206 N ATOM 1208 CA ILE C 30 20.319 12.075 -6.820 1.00 25.53 C ANISOU 1208 CA ILE C 30 3141 2747 3813 -86 36 350 C ATOM 1209 C ILE C 30 19.058 11.199 -6.886 1.00 24.71 C ANISOU 1209 C ILE C 30 3012 2731 3645 -5 35 391 C ATOM 1210 O ILE C 30 19.102 10.030 -6.496 1.00 24.51 O ANISOU 1210 O ILE C 30 2970 2798 3546 1 15 332 O ATOM 1211 CB ILE C 30 21.298 11.765 -7.985 1.00 25.24 C ANISOU 1211 CB ILE C 30 3050 2800 3740 -180 27 400 C ATOM 1212 CG1 ILE C 30 22.448 12.791 -7.994 1.00 26.96 C ANISOU 1212 CG1 ILE C 30 3283 2930 4032 -276 34 383 C ATOM 1213 CG2 ILE C 30 20.597 11.681 -9.331 1.00 26.12 C ANISOU 1213 CG2 ILE C 30 3124 2984 3818 -173 36 543 C ATOM 1214 CD1 ILE C 30 22.025 14.247 -7.982 1.00 28.31 C ANISOU 1214 CD1 ILE C 30 3517 2923 4319 -271 62 445 C ATOM 1215 N LYS C 31 17.948 11.775 -7.355 1.00 24.46 N ANISOU 1215 N LYS C 31 2977 2669 3649 57 55 495 N ATOM 1216 CA LYS C 31 16.699 11.049 -7.531 1.00 24.69 C ANISOU 1216 CA LYS C 31 2964 2797 3620 120 53 546 C ATOM 1217 C LYS C 31 16.459 10.711 -8.995 1.00 25.23 C ANISOU 1217 C LYS C 31 2973 2976 3636 84 39 666 C ATOM 1218 O LYS C 31 16.348 11.609 -9.826 1.00 25.78 O ANISOU 1218 O LYS C 31 3035 3011 3747 83 47 780 O ATOM 1219 CB LYS C 31 15.512 11.869 -6.982 1.00 26.49 C ANISOU 1219 CB LYS C 31 3207 2947 3911 229 84 575 C ATOM 1220 CG LYS C 31 14.153 11.193 -7.109 1.00 27.09 C ANISOU 1220 CG LYS C 31 3222 3140 3930 292 84 632 C ATOM 1221 CD LYS C 31 13.005 12.094 -6.649 1.00 29.81 C ANISOU 1221 CD LYS C 31 3563 3420 4344 415 121 667 C ATOM 1222 CE LYS C 31 12.793 13.283 -7.576 1.00 32.53 C ANISOU 1222 CE LYS C 31 3904 3679 4777 455 128 802 C ATOM 1223 NZ LYS C 31 11.714 14.186 -7.090 1.00 35.62 N ANISOU 1223 NZ LYS C 31 4291 3990 5252 597 168 829 N ATOM 1224 N LEU C 32 16.361 9.420 -9.308 1.00 22.76 N ANISOU 1224 N LEU C 32 2622 2796 3229 53 17 641 N ATOM 1225 CA LEU C 32 15.980 8.989 -10.641 1.00 23.27 C ANISOU 1225 CA LEU C 32 2627 2989 3223 17 2 732 C ATOM 1226 C LEU C 32 14.483 8.720 -10.638 1.00 24.08 C ANISOU 1226 C LEU C 32 2688 3161 3300 77 -3 790 C ATOM 1227 O LEU C 32 13.921 8.321 -9.617 1.00 23.09 O ANISOU 1227 O LEU C 32 2574 3019 3179 122 5 729 O ATOM 1228 CB LEU C 32 16.751 7.735 -11.075 1.00 22.92 C ANISOU 1228 CB LEU C 32 2566 3045 3096 -57 -15 656 C ATOM 1229 CG LEU C 32 18.292 7.784 -11.048 1.00 23.21 C ANISOU 1229 CG LEU C 32 2621 3051 3148 -114 -10 585 C ATOM 1230 CD1 LEU C 32 18.905 6.454 -11.465 1.00 21.99 C ANISOU 1230 CD1 LEU C 32 2443 2997 2916 -158 -22 504 C ATOM 1231 CD2 LEU C 32 18.798 8.919 -11.934 1.00 24.07 C ANISOU 1231 CD2 LEU C 32 2718 3143 3286 -158 5 682 C ATOM 1232 N GLN C 33 13.831 8.967 -11.767 1.00 26.09 N ANISOU 1232 N GLN C 33 2886 3508 3520 75 -15 914 N ATOM 1233 CA GLN C 33 12.416 8.618 -11.915 1.00 27.82 C ANISOU 1233 CA GLN C 33 3040 3833 3699 117 -28 973 C ATOM 1234 C GLN C 33 12.162 7.788 -13.158 1.00 27.81 C ANISOU 1234 C GLN C 33 2973 4010 3583 39 -62 1012 C ATOM 1235 O GLN C 33 12.848 7.939 -14.167 1.00 28.68 O ANISOU 1235 O GLN C 33 3077 4170 3651 -20 -71 1051 O ATOM 1236 CB GLN C 33 11.554 9.862 -11.933 1.00 31.03 C ANISOU 1236 CB GLN C 33 3423 4188 4181 221 -16 1097 C ATOM 1237 CG GLN C 33 11.566 10.618 -10.619 1.00 34.27 C ANISOU 1237 CG GLN C 33 3893 4428 4698 309 24 1034 C ATOM 1238 CD GLN C 33 10.588 11.766 -10.622 1.00 38.51 C ANISOU 1238 CD GLN C 33 4404 4910 5319 433 42 1146 C ATOM 1239 OE1 GLN C 33 9.377 11.568 -10.486 1.00 40.89 O ANISOU 1239 OE1 GLN C 33 4632 5304 5601 503 42 1186 O ATOM 1240 NE2 GLN C 33 11.108 12.981 -10.780 1.00 40.14 N ANISOU 1240 NE2 GLN C 33 4665 4960 5624 463 59 1201 N ATOM 1241 N GLY C 34 11.189 6.891 -13.076 1.00 25.69 N ANISOU 1241 N GLY C 34 2655 3848 3257 28 -80 992 N ATOM 1242 CA GLY C 34 10.830 6.049 -14.213 1.00 25.97 C ANISOU 1242 CA GLY C 34 2629 4061 3178 -58 -115 1007 C ATOM 1243 C GLY C 34 10.003 4.842 -13.816 1.00 25.35 C ANISOU 1243 C GLY C 34 2522 4056 3054 -99 -129 936 C ATOM 1244 O GLY C 34 9.393 4.815 -12.749 1.00 25.62 O ANISOU 1244 O GLY C 34 2558 4037 3138 -46 -111 920 O ATOM 1245 N GLN C 35 9.988 3.842 -14.683 1.00 25.21 N ANISOU 1245 N GLN C 35 2478 4161 2939 -201 -157 889 N ATOM 1246 CA GLN C 35 9.351 2.566 -14.375 1.00 25.29 C ANISOU 1246 CA GLN C 35 2477 4220 2912 -270 -169 806 C ATOM 1247 C GLN C 35 10.386 1.468 -14.320 1.00 25.09 C ANISOU 1247 C GLN C 35 2531 4126 2875 -338 -162 662 C ATOM 1248 O GLN C 35 11.347 1.469 -15.101 1.00 24.89 O ANISOU 1248 O GLN C 35 2526 4115 2815 -368 -161 626 O ATOM 1249 CB GLN C 35 8.288 2.224 -15.415 1.00 28.05 C ANISOU 1249 CB GLN C 35 2725 4772 3161 -340 -212 859 C ATOM 1250 CG GLN C 35 7.072 3.133 -15.349 1.00 30.95 C ANISOU 1250 CG GLN C 35 2993 5223 3544 -260 -224 1004 C ATOM 1251 CD GLN C 35 6.096 2.916 -16.500 1.00 34.49 C ANISOU 1251 CD GLN C 35 3321 5903 3879 -329 -278 1074 C ATOM 1252 OE1 GLN C 35 6.107 1.871 -17.167 1.00 35.26 O ANISOU 1252 OE1 GLN C 35 3412 6100 3884 -457 -306 985 O ATOM 1253 NE2 GLN C 35 5.242 3.909 -16.739 1.00 36.13 N ANISOU 1253 NE2 GLN C 35 3432 6201 4094 -240 -295 1229 N ATOM 1254 N ILE C 36 10.189 0.546 -13.384 1.00 23.68 N ANISOU 1254 N ILE C 36 2395 3876 2728 -358 -155 586 N ATOM 1255 CA ILE C 36 11.038 -0.643 -13.248 1.00 23.87 C ANISOU 1255 CA ILE C 36 2496 3821 2754 -411 -151 455 C ATOM 1256 C ILE C 36 10.723 -1.559 -14.411 1.00 24.60 C ANISOU 1256 C ILE C 36 2558 4031 2758 -523 -177 397 C ATOM 1257 O ILE C 36 9.625 -2.153 -14.501 1.00 24.95 O ANISOU 1257 O ILE C 36 2559 4152 2768 -596 -198 402 O ATOM 1258 CB ILE C 36 10.791 -1.383 -11.903 1.00 24.21 C ANISOU 1258 CB ILE C 36 2591 3754 2852 -403 -138 418 C ATOM 1259 CG1 ILE C 36 10.801 -0.418 -10.685 1.00 26.04 C ANISOU 1259 CG1 ILE C 36 2838 3908 3150 -298 -112 475 C ATOM 1260 CG2 ILE C 36 11.683 -2.617 -11.754 1.00 23.92 C ANISOU 1260 CG2 ILE C 36 2639 3616 2832 -442 -138 299 C ATOM 1261 CD1 ILE C 36 12.129 -0.021 -10.086 1.00 26.72 C ANISOU 1261 CD1 ILE C 36 2993 3872 3288 -233 -97 431 C ATOM 1262 N GLU C 37 11.666 -1.659 -15.328 1.00 24.71 N ANISOU 1262 N GLU C 37 2586 4073 2728 -546 -175 336 N ATOM 1263 CA GLU C 37 11.466 -2.468 -16.505 1.00 25.60 C ANISOU 1263 CA GLU C 37 2674 4309 2743 -652 -195 259 C ATOM 1264 C GLU C 37 11.777 -3.928 -16.186 1.00 24.79 C ANISOU 1264 C GLU C 37 2651 4095 2671 -706 -189 109 C ATOM 1265 O GLU C 37 11.082 -4.832 -16.642 1.00 24.14 O ANISOU 1265 O GLU C 37 2559 4070 2542 -810 -210 44 O ATOM 1266 CB GLU C 37 12.357 -1.939 -17.621 1.00 29.07 C ANISOU 1266 CB GLU C 37 3093 4841 3112 -651 -186 255 C ATOM 1267 CG GLU C 37 12.033 -2.432 -19.002 1.00 32.94 C ANISOU 1267 CG GLU C 37 3533 5517 3467 -757 -209 202 C ATOM 1268 CD GLU C 37 12.941 -1.789 -20.036 1.00 36.90 C ANISOU 1268 CD GLU C 37 4008 6124 3888 -751 -192 220 C ATOM 1269 OE1 GLU C 37 13.501 -0.691 -19.757 1.00 38.55 O ANISOU 1269 OE1 GLU C 37 4215 6284 4148 -672 -172 326 O ATOM 1270 OE2 GLU C 37 13.121 -2.390 -21.111 1.00 38.96 O ANISOU 1270 OE2 GLU C 37 4251 6516 4034 -831 -194 123 O ATOM 1271 N SER C 38 12.816 -4.150 -15.387 1.00 22.75 N ANISOU 1271 N SER C 38 2470 3675 2497 -635 -162 57 N ATOM 1272 CA SER C 38 13.260 -5.500 -15.014 1.00 22.57 C ANISOU 1272 CA SER C 38 2533 3518 2524 -658 -154 -70 C ATOM 1273 C SER C 38 14.280 -5.363 -13.896 1.00 20.80 C ANISOU 1273 C SER C 38 2370 3140 2394 -549 -134 -67 C ATOM 1274 O SER C 38 14.743 -4.255 -13.623 1.00 20.85 O ANISOU 1274 O SER C 38 2350 3159 2414 -477 -125 5 O ATOM 1275 CB SER C 38 13.903 -6.209 -16.200 1.00 24.01 C ANISOU 1275 CB SER C 38 2728 3749 2646 -709 -146 -212 C ATOM 1276 OG SER C 38 14.736 -5.316 -16.918 1.00 25.02 O ANISOU 1276 OG SER C 38 2811 3975 2722 -665 -128 -193 O ATOM 1277 N PHE C 39 14.621 -6.475 -13.248 1.00 20.42 N ANISOU 1277 N PHE C 39 2401 2947 2411 -541 -131 -139 N ATOM 1278 CA PHE C 39 15.660 -6.477 -12.199 1.00 20.13 C ANISOU 1278 CA PHE C 39 2416 2779 2453 -436 -121 -138 C ATOM 1279 C PHE C 39 16.190 -7.895 -12.015 1.00 20.28 C ANISOU 1279 C PHE C 39 2518 2658 2531 -431 -119 -242 C ATOM 1280 O PHE C 39 15.531 -8.871 -12.413 1.00 21.73 O ANISOU 1280 O PHE C 39 2734 2812 2710 -519 -124 -300 O ATOM 1281 CB PHE C 39 15.110 -5.933 -10.867 1.00 19.88 C ANISOU 1281 CB PHE C 39 2389 2706 2458 -397 -127 -25 C ATOM 1282 CG PHE C 39 14.045 -6.800 -10.242 1.00 20.97 C ANISOU 1282 CG PHE C 39 2562 2793 2614 -462 -135 3 C ATOM 1283 CD1 PHE C 39 12.713 -6.683 -10.639 1.00 22.02 C ANISOU 1283 CD1 PHE C 39 2638 3030 2698 -551 -142 49 C ATOM 1284 CD2 PHE C 39 14.376 -7.733 -9.270 1.00 21.29 C ANISOU 1284 CD2 PHE C 39 2684 2688 2718 -436 -137 -6 C ATOM 1285 CE1 PHE C 39 11.722 -7.489 -10.061 1.00 23.04 C ANISOU 1285 CE1 PHE C 39 2788 3123 2843 -628 -146 79 C ATOM 1286 CE2 PHE C 39 13.403 -8.547 -8.696 1.00 22.54 C ANISOU 1286 CE2 PHE C 39 2876 2797 2893 -511 -140 34 C ATOM 1287 CZ PHE C 39 12.075 -8.428 -9.100 1.00 22.84 C ANISOU 1287 CZ PHE C 39 2853 2943 2883 -615 -142 72 C ATOM 1288 N ASP C 40 17.376 -8.004 -11.422 1.00 19.35 N ANISOU 1288 N ASP C 40 2432 2450 2470 -328 -113 -265 N ATOM 1289 CA ASP C 40 17.930 -9.286 -11.024 1.00 19.56 C ANISOU 1289 CA ASP C 40 2540 2320 2572 -289 -114 -335 C ATOM 1290 C ASP C 40 18.619 -9.149 -9.651 1.00 19.78 C ANISOU 1290 C ASP C 40 2594 2260 2660 -182 -129 -263 C ATOM 1291 O ASP C 40 18.332 -8.218 -8.895 1.00 18.50 O ANISOU 1291 O ASP C 40 2404 2147 2480 -168 -138 -165 O ATOM 1292 CB ASP C 40 18.837 -9.866 -12.147 1.00 20.32 C ANISOU 1292 CB ASP C 40 2635 2422 2663 -269 -91 -485 C ATOM 1293 CG ASP C 40 20.149 -9.056 -12.387 1.00 19.76 C ANISOU 1293 CG ASP C 40 2497 2433 2577 -176 -74 -504 C ATOM 1294 OD1 ASP C 40 20.485 -8.138 -11.596 1.00 17.98 O ANISOU 1294 OD1 ASP C 40 2241 2230 2362 -124 -86 -411 O ATOM 1295 OD2 ASP C 40 20.882 -9.387 -13.378 1.00 19.93 O ANISOU 1295 OD2 ASP C 40 2496 2499 2576 -161 -45 -625 O ATOM 1296 N GLN C 41 19.528 -10.055 -9.327 1.00 20.62 N ANISOU 1296 N GLN C 41 2753 2246 2837 -101 -133 -314 N ATOM 1297 CA GLN C 41 20.163 -10.041 -8.021 1.00 21.58 C ANISOU 1297 CA GLN C 41 2895 2299 3003 -2 -156 -240 C ATOM 1298 C GLN C 41 20.832 -8.693 -7.683 1.00 20.16 C ANISOU 1298 C GLN C 41 2639 2235 2787 51 -162 -200 C ATOM 1299 O GLN C 41 20.760 -8.250 -6.536 1.00 18.84 O ANISOU 1299 O GLN C 41 2477 2065 2616 80 -183 -113 O ATOM 1300 CB GLN C 41 21.200 -11.150 -7.983 1.00 25.52 C ANISOU 1300 CB GLN C 41 3441 2672 3582 96 -160 -310 C ATOM 1301 CG GLN C 41 22.106 -11.132 -6.780 1.00 28.63 C ANISOU 1301 CG GLN C 41 3837 3027 4015 216 -192 -240 C ATOM 1302 CD GLN C 41 22.828 -12.444 -6.618 1.00 33.01 C ANISOU 1302 CD GLN C 41 4454 3425 4664 315 -201 -278 C ATOM 1303 OE1 GLN C 41 23.294 -13.034 -7.594 1.00 35.49 O ANISOU 1303 OE1 GLN C 41 4769 3701 5013 342 -173 -403 O ATOM 1304 NE2 GLN C 41 22.918 -12.919 -5.382 1.00 35.36 N ANISOU 1304 NE2 GLN C 41 4805 3630 5002 376 -238 -169 N ATOM 1305 N PHE C 42 21.470 -8.069 -8.682 1.00 19.29 N ANISOU 1305 N PHE C 42 2459 2225 2644 53 -141 -267 N ATOM 1306 CA PHE C 42 22.368 -6.920 -8.461 1.00 18.95 C ANISOU 1306 CA PHE C 42 2345 2270 2583 99 -144 -247 C ATOM 1307 C PHE C 42 21.953 -5.623 -9.121 1.00 17.25 C ANISOU 1307 C PHE C 42 2071 2175 2309 30 -125 -216 C ATOM 1308 O PHE C 42 22.446 -4.560 -8.743 1.00 16.55 O ANISOU 1308 O PHE C 42 1940 2133 2215 47 -129 -179 O ATOM 1309 CB PHE C 42 23.777 -7.254 -8.938 1.00 21.56 C ANISOU 1309 CB PHE C 42 2632 2619 2939 176 -133 -338 C ATOM 1310 CG PHE C 42 24.435 -8.326 -8.136 1.00 23.67 C ANISOU 1310 CG PHE C 42 2943 2773 3278 280 -158 -349 C ATOM 1311 CD1 PHE C 42 24.695 -8.130 -6.783 1.00 25.07 C ANISOU 1311 CD1 PHE C 42 3130 2924 3472 336 -200 -265 C ATOM 1312 CD2 PHE C 42 24.816 -9.516 -8.731 1.00 25.64 C ANISOU 1312 CD2 PHE C 42 3222 2946 3575 329 -141 -444 C ATOM 1313 CE1 PHE C 42 25.311 -9.126 -6.028 1.00 26.95 C ANISOU 1313 CE1 PHE C 42 3404 3066 3771 441 -231 -252 C ATOM 1314 CE2 PHE C 42 25.439 -10.505 -7.990 1.00 27.74 C ANISOU 1314 CE2 PHE C 42 3529 3091 3919 442 -166 -440 C ATOM 1315 CZ PHE C 42 25.671 -10.316 -6.636 1.00 27.13 C ANISOU 1315 CZ PHE C 42 3458 2994 3855 498 -215 -332 C ATOM 1316 N VAL C 43 21.078 -5.684 -10.117 1.00 16.36 N ANISOU 1316 N VAL C 43 1953 2109 2152 -51 -107 -228 N ATOM 1317 CA VAL C 43 20.771 -4.448 -10.844 1.00 16.20 C ANISOU 1317 CA VAL C 43 1872 2207 2076 -104 -92 -182 C ATOM 1318 C VAL C 43 19.283 -4.256 -11.087 1.00 16.11 C ANISOU 1318 C VAL C 43 1864 2230 2026 -178 -96 -119 C ATOM 1319 O VAL C 43 18.514 -5.206 -11.016 1.00 16.59 O ANISOU 1319 O VAL C 43 1967 2246 2091 -215 -104 -136 O ATOM 1320 CB VAL C 43 21.495 -4.355 -12.213 1.00 16.50 C ANISOU 1320 CB VAL C 43 1854 2349 2066 -126 -62 -253 C ATOM 1321 CG1 VAL C 43 22.995 -4.609 -12.082 1.00 17.36 C ANISOU 1321 CG1 VAL C 43 1937 2449 2211 -50 -52 -326 C ATOM 1322 CG2 VAL C 43 20.840 -5.274 -13.245 1.00 17.80 C ANISOU 1322 CG2 VAL C 43 2034 2545 2183 -189 -52 -325 C ATOM 1323 N ILE C 44 18.887 -3.017 -11.358 1.00 15.92 N ANISOU 1323 N ILE C 44 1793 2285 1972 -199 -91 -40 N ATOM 1324 CA ILE C 44 17.512 -2.706 -11.743 1.00 16.74 C ANISOU 1324 CA ILE C 44 1874 2452 2034 -257 -96 30 C ATOM 1325 C ILE C 44 17.549 -1.934 -13.053 1.00 17.62 C ANISOU 1325 C ILE C 44 1922 2693 2080 -298 -85 57 C ATOM 1326 O ILE C 44 18.334 -1.004 -13.189 1.00 17.03 O ANISOU 1326 O ILE C 44 1822 2635 2013 -273 -72 86 O ATOM 1327 CB ILE C 44 16.788 -1.866 -10.670 1.00 16.41 C ANISOU 1327 CB ILE C 44 1834 2377 2023 -223 -100 125 C ATOM 1328 CG1 ILE C 44 16.559 -2.684 -9.396 1.00 16.66 C ANISOU 1328 CG1 ILE C 44 1924 2312 2094 -199 -110 115 C ATOM 1329 CG2 ILE C 44 15.454 -1.352 -11.193 1.00 16.62 C ANISOU 1329 CG2 ILE C 44 1812 2494 2009 -265 -103 208 C ATOM 1330 CD1 ILE C 44 16.192 -1.805 -8.199 1.00 16.08 C ANISOU 1330 CD1 ILE C 44 1855 2211 2044 -149 -106 182 C ATOM 1331 N LEU C 45 16.713 -2.319 -14.020 1.00 19.11 N ANISOU 1331 N LEU C 45 2084 2979 2199 -369 -92 53 N ATOM 1332 CA LEU C 45 16.598 -1.547 -15.262 1.00 21.21 C ANISOU 1332 CA LEU C 45 2283 3392 2383 -411 -88 106 C ATOM 1333 C LEU C 45 15.448 -0.550 -15.145 1.00 21.42 C ANISOU 1333 C LEU C 45 2269 3464 2406 -406 -105 248 C ATOM 1334 O LEU C 45 14.276 -0.928 -15.007 1.00 21.69 O ANISOU 1334 O LEU C 45 2290 3528 2426 -436 -125 273 O ATOM 1335 CB LEU C 45 16.423 -2.464 -16.484 1.00 22.42 C ANISOU 1335 CB LEU C 45 2419 3658 2441 -492 -91 15 C ATOM 1336 CG LEU C 45 16.339 -1.770 -17.850 1.00 24.14 C ANISOU 1336 CG LEU C 45 2564 4061 2546 -544 -89 71 C ATOM 1337 CD1 LEU C 45 17.604 -0.989 -18.182 1.00 24.28 C ANISOU 1337 CD1 LEU C 45 2562 4102 2561 -512 -55 89 C ATOM 1338 CD2 LEU C 45 15.974 -2.754 -18.961 1.00 25.36 C ANISOU 1338 CD2 LEU C 45 2703 4342 2591 -635 -97 -35 C ATOM 1339 N LEU C 46 15.805 0.726 -15.169 1.00 21.45 N ANISOU 1339 N LEU C 46 2251 3467 2432 -366 -94 341 N ATOM 1340 CA LEU C 46 14.862 1.793 -14.955 1.00 22.51 C ANISOU 1340 CA LEU C 46 2354 3611 2588 -332 -102 475 C ATOM 1341 C LEU C 46 14.621 2.503 -16.285 1.00 23.76 C ANISOU 1341 C LEU C 46 2447 3914 2667 -367 -111 577 C ATOM 1342 O LEU C 46 15.572 2.922 -16.953 1.00 23.91 O ANISOU 1342 O LEU C 46 2460 3967 2659 -386 -93 585 O ATOM 1343 CB LEU C 46 15.398 2.780 -13.924 1.00 22.38 C ANISOU 1343 CB LEU C 46 2374 3459 2671 -257 -84 509 C ATOM 1344 CG LEU C 46 14.476 3.971 -13.669 1.00 22.35 C ANISOU 1344 CG LEU C 46 2346 3438 2708 -202 -84 637 C ATOM 1345 CD1 LEU C 46 13.213 3.519 -12.942 1.00 22.35 C ANISOU 1345 CD1 LEU C 46 2334 3443 2716 -177 -94 643 C ATOM 1346 CD2 LEU C 46 15.186 5.061 -12.879 1.00 22.08 C ANISOU 1346 CD2 LEU C 46 2354 3267 2768 -145 -62 653 C ATOM 1347 N LYS C 47 13.353 2.628 -16.663 1.00 24.71 N ANISOU 1347 N LYS C 47 2510 4135 2742 -377 -138 662 N ATOM 1348 CA LYS C 47 13.013 3.308 -17.924 1.00 26.30 C ANISOU 1348 CA LYS C 47 2642 4496 2856 -404 -156 783 C ATOM 1349 C LYS C 47 12.238 4.606 -17.738 1.00 26.77 C ANISOU 1349 C LYS C 47 2665 4536 2969 -324 -164 957 C ATOM 1350 O LYS C 47 11.197 4.648 -17.067 1.00 24.71 O ANISOU 1350 O LYS C 47 2382 4255 2753 -274 -176 990 O ATOM 1351 CB LYS C 47 12.244 2.390 -18.877 1.00 29.18 C ANISOU 1351 CB LYS C 47 2949 5046 3091 -494 -192 747 C ATOM 1352 CG LYS C 47 11.968 3.086 -20.209 1.00 32.36 C ANISOU 1352 CG LYS C 47 3274 5640 3380 -524 -216 879 C ATOM 1353 CD LYS C 47 12.358 2.242 -21.412 1.00 35.30 C ANISOU 1353 CD LYS C 47 3625 6185 3602 -633 -222 778 C ATOM 1354 CE LYS C 47 11.180 1.405 -21.890 1.00 36.43 C ANISOU 1354 CE LYS C 47 3708 6488 3646 -711 -271 740 C ATOM 1355 NZ LYS C 47 10.596 0.654 -20.745 1.00 36.93 N ANISOU 1355 NZ LYS C 47 3808 6418 3808 -701 -274 656 N ATOM 1356 N ASN C 48 12.770 5.668 -18.337 1.00 26.84 N ANISOU 1356 N ASN C 48 2669 4549 2981 -309 -154 1069 N ATOM 1357 CA ASN C 48 12.060 6.936 -18.458 1.00 28.64 C ANISOU 1357 CA ASN C 48 2860 4767 3254 -233 -165 1255 C ATOM 1358 C ASN C 48 12.145 7.343 -19.932 1.00 30.04 C ANISOU 1358 C ASN C 48 2980 5120 3315 -286 -185 1383 C ATOM 1359 O ASN C 48 11.692 6.579 -20.793 1.00 29.44 O ANISOU 1359 O ASN C 48 2843 5243 3101 -357 -219 1362 O ATOM 1360 CB ASN C 48 12.537 8.024 -17.451 1.00 28.83 C ANISOU 1360 CB ASN C 48 2954 4567 3435 -146 -128 1285 C ATOM 1361 CG ASN C 48 14.054 8.141 -17.340 1.00 29.22 C ANISOU 1361 CG ASN C 48 3068 4520 3516 -194 -94 1209 C ATOM 1362 OD1 ASN C 48 14.792 8.009 -18.325 1.00 29.35 O ANISOU 1362 OD1 ASN C 48 3066 4639 3447 -272 -90 1217 O ATOM 1363 ND2 ASN C 48 14.531 8.421 -16.118 1.00 29.07 N ANISOU 1363 ND2 ASN C 48 3116 4316 3613 -149 -68 1132 N ATOM 1364 N THR C 49 12.719 8.503 -20.241 1.00 31.20 N ANISOU 1364 N THR C 49 3145 5201 3506 -263 -166 1514 N ATOM 1365 CA THR C 49 13.005 8.812 -21.645 1.00 33.50 C ANISOU 1365 CA THR C 49 3389 5669 3670 -331 -178 1635 C ATOM 1366 C THR C 49 14.169 7.955 -22.152 1.00 33.70 C ANISOU 1366 C THR C 49 3430 5779 3597 -440 -150 1484 C ATOM 1367 O THR C 49 14.334 7.779 -23.364 1.00 34.69 O ANISOU 1367 O THR C 49 3503 6108 3568 -518 -159 1525 O ATOM 1368 CB THR C 49 13.316 10.299 -21.893 1.00 34.06 C ANISOU 1368 CB THR C 49 3480 5643 3819 -289 -163 1837 C ATOM 1369 OG1 THR C 49 14.481 10.678 -21.147 1.00 33.72 O ANISOU 1369 OG1 THR C 49 3522 5395 3896 -297 -112 1760 O ATOM 1370 CG2 THR C 49 12.124 11.180 -21.516 1.00 35.19 C ANISOU 1370 CG2 THR C 49 3601 5708 4060 -161 -189 1995 C ATOM 1371 N VAL C 50 14.977 7.443 -21.221 1.00 33.40 N ANISOU 1371 N VAL C 50 3456 5592 3643 -439 -116 1314 N ATOM 1372 CA VAL C 50 16.041 6.490 -21.540 1.00 33.31 C ANISOU 1372 CA VAL C 50 3455 5645 3558 -516 -87 1146 C ATOM 1373 C VAL C 50 15.915 5.209 -20.688 1.00 32.30 C ANISOU 1373 C VAL C 50 3362 5449 3461 -505 -91 947 C ATOM 1374 O VAL C 50 15.219 5.179 -19.669 1.00 31.22 O ANISOU 1374 O VAL C 50 3251 5191 3419 -443 -106 939 O ATOM 1375 CB VAL C 50 17.480 7.096 -21.393 1.00 33.36 C ANISOU 1375 CB VAL C 50 3494 5555 3625 -536 -36 1140 C ATOM 1376 CG1 VAL C 50 17.665 8.337 -22.267 1.00 35.52 C ANISOU 1376 CG1 VAL C 50 3740 5886 3870 -566 -27 1348 C ATOM 1377 CG2 VAL C 50 17.828 7.399 -19.936 1.00 31.76 C ANISOU 1377 CG2 VAL C 50 3360 5113 3594 -470 -23 1080 C ATOM 1378 N SER C 51 16.598 4.158 -21.124 1.00 31.60 N ANISOU 1378 N SER C 51 3273 5440 3293 -564 -73 792 N ATOM 1379 CA SER C 51 16.607 2.883 -20.443 1.00 30.24 C ANISOU 1379 CA SER C 51 3142 5196 3153 -559 -75 610 C ATOM 1380 C SER C 51 17.988 2.683 -19.804 1.00 28.28 C ANISOU 1380 C SER C 51 2938 4825 2982 -534 -34 499 C ATOM 1381 O SER C 51 18.991 2.566 -20.517 1.00 28.54 O ANISOU 1381 O SER C 51 2947 4944 2953 -572 0 448 O ATOM 1382 CB SER C 51 16.318 1.784 -21.458 1.00 33.58 C ANISOU 1382 CB SER C 51 3533 5793 3433 -639 -86 503 C ATOM 1383 OG SER C 51 15.451 0.801 -20.913 1.00 36.52 O ANISOU 1383 OG SER C 51 3929 6117 3829 -645 -115 414 O ATOM 1384 N GLN C 52 18.041 2.648 -18.476 1.00 25.24 N ANISOU 1384 N GLN C 52 2606 4260 2723 -470 -37 466 N ATOM 1385 CA GLN C 52 19.326 2.716 -17.735 1.00 23.51 C ANISOU 1385 CA GLN C 52 2418 3928 2587 -437 -9 394 C ATOM 1386 C GLN C 52 19.476 1.612 -16.687 1.00 21.90 C ANISOU 1386 C GLN C 52 2266 3608 2446 -393 -17 260 C ATOM 1387 O GLN C 52 18.533 1.337 -15.940 1.00 21.44 O ANISOU 1387 O GLN C 52 2240 3479 2426 -366 -42 271 O ATOM 1388 CB GLN C 52 19.513 4.110 -17.105 1.00 23.90 C ANISOU 1388 CB GLN C 52 2481 3869 2730 -405 -4 511 C ATOM 1389 CG GLN C 52 18.454 4.479 -16.062 1.00 24.25 C ANISOU 1389 CG GLN C 52 2562 3795 2856 -343 -28 565 C ATOM 1390 CD GLN C 52 17.788 5.806 -16.352 1.00 26.40 C ANISOU 1390 CD GLN C 52 2818 4060 3152 -328 -32 732 C ATOM 1391 OE1 GLN C 52 18.338 6.867 -16.048 1.00 28.16 O ANISOU 1391 OE1 GLN C 52 3061 4188 3451 -317 -15 789 O ATOM 1392 NE2 GLN C 52 16.598 5.757 -16.961 1.00 25.39 N ANISOU 1392 NE2 GLN C 52 2652 4033 2963 -328 -56 814 N ATOM 1393 N MET C 53 20.647 0.964 -16.647 1.00 19.78 N ANISOU 1393 N MET C 53 2000 3330 2185 -382 5 142 N ATOM 1394 CA MET C 53 20.891 -0.108 -15.672 1.00 18.53 C ANISOU 1394 CA MET C 53 1893 3057 2091 -329 -6 30 C ATOM 1395 C MET C 53 21.502 0.494 -14.404 1.00 17.07 C ANISOU 1395 C MET C 53 1730 2752 2004 -272 -12 53 C ATOM 1396 O MET C 53 22.574 1.069 -14.451 1.00 16.10 O ANISOU 1396 O MET C 53 1575 2646 1898 -273 6 51 O ATOM 1397 CB MET C 53 21.803 -1.196 -16.258 1.00 19.44 C ANISOU 1397 CB MET C 53 1997 3219 2172 -326 19 -113 C ATOM 1398 CG MET C 53 22.128 -2.356 -15.312 1.00 19.11 C ANISOU 1398 CG MET C 53 2010 3047 2205 -259 7 -216 C ATOM 1399 SD MET C 53 23.358 -3.546 -15.915 1.00 20.58 S ANISOU 1399 SD MET C 53 2179 3262 2379 -219 44 -389 S ATOM 1400 CE MET C 53 24.882 -2.623 -15.780 1.00 21.53 C ANISOU 1400 CE MET C 53 2221 3440 2521 -185 69 -369 C ATOM 1401 N VAL C 54 20.783 0.379 -13.288 1.00 16.05 N ANISOU 1401 N VAL C 54 1651 2518 1928 -235 -38 74 N ATOM 1402 CA VAL C 54 21.202 0.949 -12.019 1.00 14.82 C ANISOU 1402 CA VAL C 54 1520 2262 1848 -186 -48 89 C ATOM 1403 C VAL C 54 21.662 -0.176 -11.100 1.00 14.20 C ANISOU 1403 C VAL C 54 1480 2111 1803 -133 -66 4 C ATOM 1404 O VAL C 54 20.903 -1.140 -10.857 1.00 15.03 O ANISOU 1404 O VAL C 54 1626 2181 1905 -127 -78 -14 O ATOM 1405 CB VAL C 54 20.047 1.747 -11.336 1.00 14.67 C ANISOU 1405 CB VAL C 54 1527 2190 1858 -172 -58 180 C ATOM 1406 CG1 VAL C 54 20.525 2.434 -10.056 1.00 14.05 C ANISOU 1406 CG1 VAL C 54 1475 2018 1844 -130 -65 176 C ATOM 1407 CG2 VAL C 54 19.453 2.785 -12.303 1.00 15.14 C ANISOU 1407 CG2 VAL C 54 1550 2314 1890 -209 -46 284 C ATOM 1408 N TYR C 55 22.889 -0.068 -10.566 1.00 13.25 N ANISOU 1408 N TYR C 55 1344 1972 1719 -98 -70 -40 N ATOM 1409 CA TYR C 55 23.342 -1.067 -9.577 1.00 13.03 C ANISOU 1409 CA TYR C 55 1349 1876 1725 -32 -95 -97 C ATOM 1410 C TYR C 55 22.643 -0.835 -8.232 1.00 12.68 C ANISOU 1410 C TYR C 55 1357 1756 1704 -6 -120 -47 C ATOM 1411 O TYR C 55 22.572 0.309 -7.750 1.00 12.57 O ANISOU 1411 O TYR C 55 1338 1734 1703 -16 -121 -7 O ATOM 1412 CB TYR C 55 24.864 -1.025 -9.401 1.00 12.84 C ANISOU 1412 CB TYR C 55 1274 1882 1724 5 -99 -152 C ATOM 1413 CG TYR C 55 25.608 -1.708 -10.539 1.00 13.42 C ANISOU 1413 CG TYR C 55 1298 2028 1773 9 -69 -228 C ATOM 1414 CD1 TYR C 55 25.889 -3.093 -10.497 1.00 13.44 C ANISOU 1414 CD1 TYR C 55 1323 1989 1795 76 -74 -305 C ATOM 1415 CD2 TYR C 55 26.012 -0.995 -11.663 1.00 13.62 C ANISOU 1415 CD2 TYR C 55 1257 2161 1757 -52 -32 -224 C ATOM 1416 CE1 TYR C 55 26.546 -3.717 -11.548 1.00 14.54 C ANISOU 1416 CE1 TYR C 55 1418 2195 1913 90 -38 -395 C ATOM 1417 CE2 TYR C 55 26.693 -1.621 -12.711 1.00 14.26 C ANISOU 1417 CE2 TYR C 55 1286 2331 1800 -47 4 -304 C ATOM 1418 CZ TYR C 55 26.956 -2.980 -12.645 1.00 14.67 C ANISOU 1418 CZ TYR C 55 1360 2342 1873 28 3 -400 C ATOM 1419 OH TYR C 55 27.602 -3.601 -13.687 1.00 15.01 O ANISOU 1419 OH TYR C 55 1352 2471 1879 43 47 -500 O ATOM 1420 N LYS C 56 22.159 -1.916 -7.614 1.00 13.51 N ANISOU 1420 N LYS C 56 1515 1803 1817 24 -137 -53 N ATOM 1421 CA LYS C 56 21.441 -1.797 -6.356 1.00 13.41 C ANISOU 1421 CA LYS C 56 1546 1740 1808 43 -154 -3 C ATOM 1422 C LYS C 56 22.339 -1.244 -5.275 1.00 13.05 C ANISOU 1422 C LYS C 56 1494 1690 1776 85 -178 -14 C ATOM 1423 O LYS C 56 21.866 -0.548 -4.378 1.00 13.85 O ANISOU 1423 O LYS C 56 1614 1780 1868 88 -181 16 O ATOM 1424 CB LYS C 56 20.867 -3.150 -5.888 1.00 13.35 C ANISOU 1424 CB LYS C 56 1597 1672 1805 56 -167 4 C ATOM 1425 CG LYS C 56 19.664 -3.664 -6.675 1.00 14.22 C ANISOU 1425 CG LYS C 56 1720 1787 1897 -8 -149 20 C ATOM 1426 CD LYS C 56 19.376 -5.088 -6.183 1.00 14.24 C ANISOU 1426 CD LYS C 56 1786 1705 1920 -3 -162 18 C ATOM 1427 CE LYS C 56 18.234 -5.749 -6.921 1.00 14.94 C ANISOU 1427 CE LYS C 56 1888 1793 1995 -85 -149 18 C ATOM 1428 NZ LYS C 56 18.047 -7.097 -6.268 1.00 16.02 N ANISOU 1428 NZ LYS C 56 2100 1820 2169 -86 -163 26 N ATOM 1429 N HIS C 57 23.639 -1.500 -5.367 1.00 13.59 N ANISOU 1429 N HIS C 57 1526 1778 1860 117 -194 -65 N ATOM 1430 CA HIS C 57 24.534 -0.972 -4.367 1.00 13.75 C ANISOU 1430 CA HIS C 57 1526 1816 1884 146 -225 -81 C ATOM 1431 C HIS C 57 24.594 0.556 -4.368 1.00 13.52 C ANISOU 1431 C HIS C 57 1471 1808 1857 92 -211 -78 C ATOM 1432 O HIS C 57 25.045 1.157 -3.392 1.00 14.43 O ANISOU 1432 O HIS C 57 1583 1930 1969 97 -237 -96 O ATOM 1433 CB HIS C 57 25.919 -1.602 -4.498 1.00 14.15 C ANISOU 1433 CB HIS C 57 1523 1902 1953 196 -247 -133 C ATOM 1434 CG HIS C 57 26.625 -1.289 -5.782 1.00 13.96 C ANISOU 1434 CG HIS C 57 1428 1941 1936 163 -214 -175 C ATOM 1435 ND1 HIS C 57 27.084 -2.272 -6.626 1.00 14.35 N ANISOU 1435 ND1 HIS C 57 1452 2005 1995 200 -197 -223 N ATOM 1436 CD2 HIS C 57 26.983 -0.109 -6.350 1.00 14.11 C ANISOU 1436 CD2 HIS C 57 1395 2014 1953 95 -191 -176 C ATOM 1437 CE1 HIS C 57 27.691 -1.722 -7.666 1.00 14.67 C ANISOU 1437 CE1 HIS C 57 1421 2129 2025 156 -163 -254 C ATOM 1438 NE2 HIS C 57 27.647 -0.407 -7.522 1.00 14.46 N ANISOU 1438 NE2 HIS C 57 1376 2124 1992 87 -160 -216 N ATOM 1439 N ALA C 58 24.122 1.177 -5.441 1.00 13.38 N ANISOU 1439 N ALA C 58 1439 1798 1845 40 -174 -53 N ATOM 1440 CA ALA C 58 24.078 2.653 -5.531 1.00 13.49 C ANISOU 1440 CA ALA C 58 1444 1804 1880 -10 -156 -34 C ATOM 1441 C ALA C 58 22.746 3.236 -5.105 1.00 13.72 C ANISOU 1441 C ALA C 58 1523 1781 1910 -5 -140 15 C ATOM 1442 O ALA C 58 22.592 4.464 -5.033 1.00 14.18 O ANISOU 1442 O ALA C 58 1586 1802 1998 -29 -124 30 O ATOM 1443 CB ALA C 58 24.426 3.132 -6.935 1.00 13.92 C ANISOU 1443 CB ALA C 58 1449 1903 1939 -66 -124 -14 C ATOM 1444 N ILE C 59 21.791 2.367 -4.785 1.00 13.81 N ANISOU 1444 N ILE C 59 1568 1785 1895 27 -142 38 N ATOM 1445 CA ILE C 59 20.440 2.802 -4.419 1.00 13.28 C ANISOU 1445 CA ILE C 59 1530 1693 1824 37 -121 86 C ATOM 1446 C ILE C 59 20.261 2.852 -2.908 1.00 13.32 C ANISOU 1446 C ILE C 59 1572 1680 1809 76 -132 63 C ATOM 1447 O ILE C 59 20.642 1.916 -2.198 1.00 12.65 O ANISOU 1447 O ILE C 59 1503 1607 1695 98 -160 45 O ATOM 1448 CB ILE C 59 19.375 1.871 -5.026 1.00 13.52 C ANISOU 1448 CB ILE C 59 1561 1748 1828 28 -111 131 C ATOM 1449 CG1 ILE C 59 19.543 1.825 -6.559 1.00 13.82 C ANISOU 1449 CG1 ILE C 59 1559 1829 1862 -15 -101 144 C ATOM 1450 CG2 ILE C 59 17.941 2.234 -4.560 1.00 13.18 C ANISOU 1450 CG2 ILE C 59 1528 1705 1776 44 -88 183 C ATOM 1451 CD1 ILE C 59 18.661 0.766 -7.199 1.00 14.91 C ANISOU 1451 CD1 ILE C 59 1697 2002 1968 -40 -100 161 C ATOM 1452 N SER C 60 19.669 3.944 -2.425 1.00 13.58 N ANISOU 1452 N SER C 60 1620 1685 1857 87 -108 65 N ATOM 1453 CA SER C 60 19.194 3.988 -1.046 1.00 14.06 C ANISOU 1453 CA SER C 60 1714 1749 1880 124 -105 42 C ATOM 1454 C SER C 60 17.724 3.514 -0.953 1.00 14.19 C ANISOU 1454 C SER C 60 1732 1792 1868 144 -75 103 C ATOM 1455 O SER C 60 17.412 2.619 -0.174 1.00 14.14 O ANISOU 1455 O SER C 60 1744 1819 1810 154 -82 117 O ATOM 1456 CB SER C 60 19.417 5.369 -0.413 1.00 15.32 C ANISOU 1456 CB SER C 60 1890 1865 2065 130 -91 -19 C ATOM 1457 OG SER C 60 18.661 6.355 -1.092 1.00 17.62 O ANISOU 1457 OG SER C 60 2177 2105 2413 138 -50 18 O ATOM 1458 N THR C 61 16.833 4.087 -1.747 1.00 14.02 N ANISOU 1458 N THR C 61 1686 1765 1879 146 -43 151 N ATOM 1459 CA THR C 61 15.410 3.759 -1.626 1.00 14.12 C ANISOU 1459 CA THR C 61 1679 1823 1864 163 -14 208 C ATOM 1460 C THR C 61 14.685 3.664 -2.956 1.00 13.91 C ANISOU 1460 C THR C 61 1605 1826 1855 138 -7 278 C ATOM 1461 O THR C 61 15.090 4.289 -3.949 1.00 13.67 O ANISOU 1461 O THR C 61 1558 1774 1862 125 -12 294 O ATOM 1462 CB THR C 61 14.645 4.768 -0.728 1.00 14.89 C ANISOU 1462 CB THR C 61 1779 1914 1963 223 30 190 C ATOM 1463 OG1 THR C 61 14.690 6.069 -1.321 1.00 15.62 O ANISOU 1463 OG1 THR C 61 1864 1942 2128 248 48 190 O ATOM 1464 CG2 THR C 61 15.226 4.839 0.679 1.00 14.79 C ANISOU 1464 CG2 THR C 61 1810 1901 1907 241 24 111 C ATOM 1465 N VAL C 62 13.608 2.872 -2.960 1.00 13.57 N ANISOU 1465 N VAL C 62 1536 1846 1776 122 2 325 N ATOM 1466 CA VAL C 62 12.709 2.783 -4.089 1.00 14.26 C ANISOU 1466 CA VAL C 62 1565 1991 1862 95 5 392 C ATOM 1467 C VAL C 62 11.346 3.170 -3.526 1.00 16.34 C ANISOU 1467 C VAL C 62 1783 2311 2115 139 43 436 C ATOM 1468 O VAL C 62 10.835 2.509 -2.606 1.00 15.36 O ANISOU 1468 O VAL C 62 1663 2223 1950 131 58 434 O ATOM 1469 CB VAL C 62 12.735 1.357 -4.713 1.00 14.07 C ANISOU 1469 CB VAL C 62 1542 2000 1805 15 -24 392 C ATOM 1470 CG1 VAL C 62 11.754 1.253 -5.863 1.00 14.92 C ANISOU 1470 CG1 VAL C 62 1581 2192 1894 -28 -27 450 C ATOM 1471 CG2 VAL C 62 14.147 1.038 -5.240 1.00 13.62 C ANISOU 1471 CG2 VAL C 62 1521 1891 1762 -7 -52 336 C ATOM 1472 N VAL C 63 10.789 4.262 -4.060 1.00 18.36 N ANISOU 1472 N VAL C 63 1992 2576 2408 191 61 482 N ATOM 1473 CA VAL C 63 9.562 4.911 -3.523 1.00 22.17 C ANISOU 1473 CA VAL C 63 2420 3106 2898 268 105 516 C ATOM 1474 C VAL C 63 8.539 4.975 -4.675 1.00 23.82 C ANISOU 1474 C VAL C 63 2534 3411 3105 262 96 614 C ATOM 1475 O VAL C 63 8.865 5.506 -5.737 1.00 23.47 O ANISOU 1475 O VAL C 63 2480 3348 3089 261 73 656 O ATOM 1476 CB VAL C 63 9.854 6.376 -3.053 1.00 22.59 C ANISOU 1476 CB VAL C 63 2505 3059 3018 366 137 481 C ATOM 1477 CG1 VAL C 63 8.642 7.016 -2.398 1.00 26.76 C ANISOU 1477 CG1 VAL C 63 2981 3631 3558 464 193 495 C ATOM 1478 CG2 VAL C 63 11.034 6.447 -2.083 1.00 25.19 C ANISOU 1478 CG2 VAL C 63 2923 3303 3346 357 134 377 C ATOM 1479 N PRO C 64 7.311 4.441 -4.490 1.00 25.92 N ANISOU 1479 N PRO C 64 2722 3796 3329 250 111 657 N ATOM 1480 CA PRO C 64 6.273 4.770 -5.475 1.00 29.06 C ANISOU 1480 CA PRO C 64 3010 4302 3728 267 101 753 C ATOM 1481 C PRO C 64 6.098 6.293 -5.541 1.00 30.91 C ANISOU 1481 C PRO C 64 3227 4479 4038 403 128 792 C ATOM 1482 O PRO C 64 5.860 6.908 -4.503 1.00 33.27 O ANISOU 1482 O PRO C 64 3539 4734 4369 496 179 751 O ATOM 1483 CB PRO C 64 5.006 4.112 -4.885 1.00 29.72 C ANISOU 1483 CB PRO C 64 3009 4520 3763 247 128 777 C ATOM 1484 CG PRO C 64 5.538 3.029 -3.996 1.00 29.09 C ANISOU 1484 CG PRO C 64 3010 4400 3644 166 131 709 C ATOM 1485 CD PRO C 64 6.788 3.594 -3.401 1.00 27.53 C ANISOU 1485 CD PRO C 64 2922 4055 3482 219 138 633 C ATOM 1486 N SER C 65 6.258 6.876 -6.734 1.00 33.06 N ANISOU 1486 N SER C 65 3478 4747 4337 412 95 867 N ATOM 1487 CA SER C 65 6.177 8.332 -6.957 1.00 35.25 C ANISOU 1487 CA SER C 65 3750 4941 4702 537 115 926 C ATOM 1488 C SER C 65 4.828 8.904 -6.535 1.00 36.41 C ANISOU 1488 C SER C 65 3799 5157 4877 663 155 978 C ATOM 1489 O SER C 65 3.789 8.434 -6.987 1.00 38.10 O ANISOU 1489 O SER C 65 3895 5539 5040 648 138 1052 O ATOM 1490 CB SER C 65 6.431 8.682 -8.429 1.00 34.63 C ANISOU 1490 CB SER C 65 3648 4886 4624 508 67 1032 C ATOM 1491 OG SER C 65 7.773 8.430 -8.793 1.00 37.63 O ANISOU 1491 OG SER C 65 4117 5187 4993 416 44 980 O TER 1492 SER C 65 ATOM 1493 O5' A D 1 37.848 15.907 12.764 0.83 31.48 O ANISOU 1493 O5' A D 1 3126 3583 5251 -1230 943 491 O ATOM 1494 C5' A D 1 37.411 16.321 11.454 0.83 32.09 C ANISOU 1494 C5' A D 1 3218 3712 5263 -1329 994 733 C ATOM 1495 C4' A D 1 36.393 15.344 10.901 0.83 30.27 C ANISOU 1495 C4' A D 1 3068 3603 4831 -1153 1081 690 C ATOM 1496 O4' A D 1 36.938 13.995 10.907 0.83 28.62 O ANISOU 1496 O4' A D 1 2760 3651 4462 -1038 1173 535 O ATOM 1497 C3' A D 1 35.059 15.241 11.644 0.83 28.51 C ANISOU 1497 C3' A D 1 3023 3174 4637 -978 1003 563 C ATOM 1498 O3' A D 1 34.086 14.898 10.659 0.83 28.86 O ANISOU 1498 O3' A D 1 3135 3287 4542 -914 1061 653 O ATOM 1499 C2' A D 1 35.252 13.979 12.471 0.83 26.13 C ANISOU 1499 C2' A D 1 2688 2984 4257 -823 1031 344 C ATOM 1500 O2' A D 1 34.070 13.386 12.975 0.83 24.33 O ANISOU 1500 O2' A D 1 2570 2696 3977 -653 1001 251 O ATOM 1501 C1' A D 1 35.972 13.114 11.444 0.83 26.40 C ANISOU 1501 C1' A D 1 2594 3308 4127 -840 1149 378 C ATOM 1502 N9 A D 1 36.665 11.957 11.995 0.83 25.02 N ANISOU 1502 N9 A D 1 2339 3275 3894 -739 1163 190 N ATOM 1503 C8 A D 1 37.602 11.934 12.998 0.83 25.20 C ANISOU 1503 C8 A D 1 2290 3283 4003 -756 1126 67 C ATOM 1504 N7 A D 1 38.054 10.735 13.268 0.83 24.20 N ANISOU 1504 N7 A D 1 2104 3295 3794 -641 1132 -88 N ATOM 1505 C5 A D 1 37.394 9.917 12.362 0.83 23.17 C ANISOU 1505 C5 A D 1 2006 3271 3527 -542 1160 -73 C ATOM 1506 C6 A D 1 37.430 8.532 12.144 0.83 22.44 C ANISOU 1506 C6 A D 1 1888 3308 3329 -389 1134 -205 C ATOM 1507 N6 A D 1 38.218 7.701 12.826 0.83 22.17 N ANISOU 1507 N6 A D 1 1788 3332 3303 -313 1082 -371 N ATOM 1508 N1 A D 1 36.634 8.027 11.174 0.83 22.33 N ANISOU 1508 N1 A D 1 1920 3351 3212 -308 1136 -169 N ATOM 1509 C2 A D 1 35.858 8.869 10.478 0.83 22.60 C ANISOU 1509 C2 A D 1 2021 3333 3234 -379 1185 -1 C ATOM 1510 N3 A D 1 35.732 10.189 10.597 0.83 23.16 N ANISOU 1510 N3 A D 1 2128 3277 3395 -524 1213 146 N ATOM 1511 C4 A D 1 36.541 10.657 11.566 0.83 23.80 C ANISOU 1511 C4 A D 1 2162 3288 3594 -600 1190 97 C ATOM 1512 P A D 2 33.354 16.041 9.824 0.83 31.33 P ANISOU 1512 P A D 2 3540 3456 4909 -1007 1013 871 P ATOM 1513 OP1 A D 2 32.550 15.392 8.761 0.83 30.53 O ANISOU 1513 OP1 A D 2 3474 3505 4621 -920 1098 931 O ATOM 1514 OP2 A D 2 34.346 17.085 9.478 0.83 32.87 O ANISOU 1514 OP2 A D 2 3645 3617 5227 -1238 978 1061 O ATOM 1515 O5' A D 2 32.388 16.678 10.911 0.83 30.43 O ANISOU 1515 O5' A D 2 3572 3048 4940 -903 864 753 O ATOM 1516 C5' A D 2 31.320 15.913 11.440 0.83 28.52 C ANISOU 1516 C5' A D 2 3408 2819 4611 -703 868 604 C ATOM 1517 C4' A D 2 30.643 16.676 12.544 0.83 28.86 C ANISOU 1517 C4' A D 2 3539 2647 4778 -606 720 485 C ATOM 1518 O4' A D 2 30.529 18.081 12.190 0.83 31.34 O ANISOU 1518 O4' A D 2 3922 2733 5252 -704 590 602 O ATOM 1519 C3' A D 2 29.215 16.224 12.794 0.83 26.72 C ANISOU 1519 C3' A D 2 3349 2398 4405 -422 714 414 C ATOM 1520 O3' A D 2 28.909 16.463 14.155 0.83 24.69 O ANISOU 1520 O3' A D 2 3101 2083 4198 -288 612 236 O ATOM 1521 C2' A D 2 28.437 17.045 11.773 0.83 28.74 C ANISOU 1521 C2' A D 2 3702 2537 4680 -458 674 567 C ATOM 1522 O2' A D 2 27.059 17.128 12.061 0.83 28.56 O ANISOU 1522 O2' A D 2 3763 2473 4615 -295 615 501 O ATOM 1523 C1' A D 2 29.193 18.374 11.805 0.83 32.26 C ANISOU 1523 C1' A D 2 4157 2773 5329 -602 545 636 C ATOM 1524 N9 A D 2 29.228 19.020 10.492 0.83 35.92 N ANISOU 1524 N9 A D 2 4651 3183 5815 -757 547 884 N ATOM 1525 C8 A D 2 30.066 18.726 9.444 0.83 37.22 C ANISOU 1525 C8 A D 2 4719 3523 5899 -921 675 1073 C ATOM 1526 N7 A D 2 29.860 19.462 8.380 0.83 40.80 N ANISOU 1526 N7 A D 2 5211 3921 6369 -1037 646 1307 N ATOM 1527 C5 A D 2 28.803 20.285 8.743 0.83 40.96 C ANISOU 1527 C5 A D 2 5380 3676 6507 -938 476 1256 C ATOM 1528 C6 A D 2 28.102 21.287 8.048 0.83 42.86 C ANISOU 1528 C6 A D 2 5732 3724 6827 -978 349 1423 C ATOM 1529 N6 A D 2 28.378 21.648 6.792 0.83 45.11 N ANISOU 1529 N6 A D 2 5994 4069 7078 -1154 387 1720 N ATOM 1530 N1 A D 2 27.097 21.917 8.698 0.83 43.26 N ANISOU 1530 N1 A D 2 5912 3541 6984 -817 169 1273 N ATOM 1531 C2 A D 2 26.817 21.548 9.956 0.83 41.23 C ANISOU 1531 C2 A D 2 5650 3290 6724 -630 140 989 C ATOM 1532 N3 A D 2 27.402 20.620 10.713 0.83 39.46 N ANISOU 1532 N3 A D 2 5324 3246 6423 -591 257 840 N ATOM 1533 C4 A D 2 28.397 20.016 10.039 0.83 38.50 C ANISOU 1533 C4 A D 2 5096 3309 6224 -754 418 983 C ATOM 1534 P A D 3 28.824 15.237 15.161 0.83 21.88 P ANISOU 1534 P A D 3 2674 1914 3725 -164 665 105 P ATOM 1535 OP1 A D 3 28.974 15.763 16.544 0.83 22.85 O ANISOU 1535 OP1 A D 3 2773 1996 3915 -62 552 -69 O ATOM 1536 OP2 A D 3 29.719 14.149 14.683 0.83 21.14 O ANISOU 1536 OP2 A D 3 2503 1961 3568 -250 781 147 O ATOM 1537 O5' A D 3 27.336 14.731 14.951 0.83 20.20 O ANISOU 1537 O5' A D 3 2507 1782 3386 -43 687 141 O ATOM 1538 C5' A D 3 26.845 13.596 15.673 0.83 17.84 C ANISOU 1538 C5' A D 3 2150 1656 2973 57 718 99 C ATOM 1539 C4' A D 3 25.345 13.535 15.531 0.83 16.85 C ANISOU 1539 C4' A D 3 2061 1580 2763 160 701 143 C ATOM 1540 O4' A D 3 24.879 12.280 16.087 0.83 15.49 O ANISOU 1540 O4' A D 3 1811 1587 2487 212 728 165 O ATOM 1541 C3' A D 3 24.554 14.620 16.266 0.83 17.61 C ANISOU 1541 C3' A D 3 2181 1642 2869 301 594 42 C ATOM 1542 O3' A D 3 23.325 14.728 15.552 0.83 17.51 O ANISOU 1542 O3' A D 3 2222 1630 2799 348 592 119 O ATOM 1543 C2' A D 3 24.320 13.966 17.626 0.83 17.04 C ANISOU 1543 C2' A D 3 1998 1785 2693 419 585 -38 C ATOM 1544 O2' A D 3 23.245 14.521 18.366 0.83 17.93 O ANISOU 1544 O2' A D 3 2081 2008 2725 601 508 -125 O ATOM 1545 C1' A D 3 24.034 12.529 17.193 0.83 15.76 C ANISOU 1545 C1' A D 3 1795 1744 2451 353 672 104 C ATOM 1546 N9 A D 3 24.319 11.489 18.172 0.83 15.36 N ANISOU 1546 N9 A D 3 1636 1863 2337 366 682 109 N ATOM 1547 C8 A D 3 25.514 11.156 18.758 0.83 15.14 C ANISOU 1547 C8 A D 3 1565 1841 2348 326 686 46 C ATOM 1548 N7 A D 3 25.451 10.088 19.515 0.83 14.84 N ANISOU 1548 N7 A D 3 1436 1965 2239 340 681 100 N ATOM 1549 C5 A D 3 24.130 9.678 19.402 0.83 14.83 C ANISOU 1549 C5 A D 3 1406 2078 2152 374 674 223 C ATOM 1550 C6 A D 3 23.418 8.606 19.967 0.83 15.04 C ANISOU 1550 C6 A D 3 1328 2294 2091 376 650 369 C ATOM 1551 N6 A D 3 23.957 7.717 20.806 0.83 15.33 N ANISOU 1551 N6 A D 3 1281 2433 2111 350 621 417 N ATOM 1552 N1 A D 3 22.105 8.494 19.664 0.83 15.14 N ANISOU 1552 N1 A D 3 1316 2395 2041 398 643 484 N ATOM 1553 C2 A D 3 21.563 9.383 18.822 0.83 15.13 C ANISOU 1553 C2 A D 3 1405 2287 2058 433 661 434 C ATOM 1554 N3 A D 3 22.129 10.430 18.227 0.83 15.02 N ANISOU 1554 N3 A D 3 1504 2079 2123 438 676 308 N ATOM 1555 C4 A D 3 23.426 10.524 18.566 0.83 14.92 C ANISOU 1555 C4 A D 3 1499 1991 2178 398 681 216 C ATOM 1556 P A D 4 22.902 16.092 14.817 0.83 19.28 P ANISOU 1556 P A D 4 2565 1647 3114 360 501 126 P ATOM 1557 OP1 A D 4 23.839 17.156 15.252 0.83 20.57 O ANISOU 1557 OP1 A D 4 2753 1632 3432 331 392 32 O ATOM 1558 OP2 A D 4 21.452 16.276 15.033 0.83 19.08 O ANISOU 1558 OP2 A D 4 2543 1712 2995 527 449 88 O ATOM 1559 O5' A D 4 23.011 15.734 13.269 0.83 19.07 O ANISOU 1559 O5' A D 4 2597 1565 3082 215 593 307 O ATOM 1560 C5' A D 4 24.245 15.830 12.538 0.83 19.96 C ANISOU 1560 C5' A D 4 2717 1600 3269 45 643 392 C ATOM 1561 C4' A D 4 24.269 14.812 11.418 0.83 19.59 C ANISOU 1561 C4' A D 4 2654 1666 3123 -20 759 509 C ATOM 1562 O4' A D 4 24.279 13.469 11.982 0.83 17.90 O ANISOU 1562 O4' A D 4 2358 1611 2834 25 807 453 O ATOM 1563 C3' A D 4 23.098 14.844 10.434 0.83 20.09 C ANISOU 1563 C3' A D 4 2789 1727 3118 26 761 598 C ATOM 1564 O3' A D 4 23.549 14.492 9.122 0.83 22.29 O ANISOU 1564 O3' A D 4 3067 2058 3343 -65 840 716 O ATOM 1565 C2' A D 4 22.171 13.771 10.990 0.83 18.10 C ANISOU 1565 C2' A D 4 2486 1616 2776 136 770 546 C ATOM 1566 O2' A D 4 21.263 13.269 10.032 0.83 17.33 O ANISOU 1566 O2' A D 4 2417 1563 2604 166 789 622 O ATOM 1567 C1' A D 4 23.183 12.733 11.481 0.83 17.04 C ANISOU 1567 C1' A D 4 2260 1577 2638 86 818 504 C ATOM 1568 N9 A D 4 22.686 11.902 12.569 0.83 15.70 N ANISOU 1568 N9 A D 4 2014 1523 2427 161 794 456 N ATOM 1569 C8 A D 4 22.046 12.319 13.710 0.83 15.84 C ANISOU 1569 C8 A D 4 1998 1594 2425 261 742 394 C ATOM 1570 N7 A D 4 21.717 11.343 14.518 0.83 15.24 N ANISOU 1570 N7 A D 4 1828 1671 2292 295 735 408 N ATOM 1571 C5 A D 4 22.212 10.209 13.889 0.83 14.36 C ANISOU 1571 C5 A D 4 1704 1556 2195 211 760 466 C ATOM 1572 C6 A D 4 22.163 8.849 14.227 0.83 13.84 C ANISOU 1572 C6 A D 4 1562 1578 2119 190 728 520 C ATOM 1573 N6 A D 4 21.611 8.390 15.355 0.83 13.78 N ANISOU 1573 N6 A D 4 1458 1711 2066 225 688 565 N ATOM 1574 N1 A D 4 22.720 7.966 13.369 0.83 13.23 N ANISOU 1574 N1 A D 4 1499 1451 2077 136 719 530 N ATOM 1575 C2 A D 4 23.280 8.431 12.243 0.83 13.49 C ANISOU 1575 C2 A D 4 1598 1410 2117 108 769 499 C ATOM 1576 N3 A D 4 23.356 9.688 11.796 0.83 14.26 N ANISOU 1576 N3 A D 4 1761 1444 2214 98 820 495 N ATOM 1577 C4 A D 4 22.801 10.537 12.681 0.83 14.62 C ANISOU 1577 C4 A D 4 1811 1482 2261 147 800 475 C ATOM 1578 P A D 5 23.939 15.628 8.067 0.83 26.45 P ANISOU 1578 P A D 5 3653 2483 3914 -181 829 870 P ATOM 1579 OP1 A D 5 24.512 14.972 6.858 0.83 26.68 O ANISOU 1579 OP1 A D 5 3627 2680 3828 -247 934 969 O ATOM 1580 OP2 A D 5 24.749 16.666 8.770 0.83 27.96 O ANISOU 1580 OP2 A D 5 3844 2519 4259 -265 751 857 O ATOM 1581 O5' A D 5 22.530 16.277 7.716 0.83 27.27 O ANISOU 1581 O5' A D 5 3867 2482 4011 -86 750 905 O ATOM 1582 C5' A D 5 21.610 15.670 6.793 0.83 28.37 C ANISOU 1582 C5' A D 5 4031 2718 4029 -18 790 953 C ATOM 1583 C4' A D 5 20.520 16.657 6.460 0.83 31.03 C ANISOU 1583 C4' A D 5 4478 2918 4393 47 694 999 C ATOM 1584 O4' A D 5 21.125 17.850 5.891 0.83 33.35 O ANISOU 1584 O4' A D 5 4830 3063 4777 -77 638 1145 O ATOM 1585 C3' A D 5 19.470 16.188 5.449 0.83 31.08 C ANISOU 1585 C3' A D 5 4521 3008 4281 125 719 1051 C ATOM 1586 O3' A D 5 18.165 16.580 5.860 0.83 30.03 O ANISOU 1586 O3' A D 5 4442 2810 4159 260 627 981 O ATOM 1587 C2' A D 5 19.915 16.864 4.157 0.83 33.32 C ANISOU 1587 C2' A D 5 4853 3266 4542 19 734 1241 C ATOM 1588 O2' A D 5 18.892 17.068 3.204 0.83 35.08 O ANISOU 1588 O2' A D 5 5151 3486 4690 91 705 1315 O ATOM 1589 C1' A D 5 20.457 18.186 4.691 0.83 35.66 C ANISOU 1589 C1' A D 5 5198 3347 5005 -70 627 1286 C ATOM 1590 N9 A D 5 21.411 18.833 3.791 0.83 38.64 N ANISOU 1590 N9 A D 5 5569 3708 5403 -249 642 1506 N ATOM 1591 C8 A D 5 22.248 18.243 2.877 0.83 39.49 C ANISOU 1591 C8 A D 5 5583 4043 5381 -345 777 1627 C ATOM 1592 N7 A D 5 22.976 19.097 2.199 0.83 42.54 N ANISOU 1592 N7 A D 5 5956 4406 5800 -515 760 1860 N ATOM 1593 C5 A D 5 22.597 20.333 2.703 0.83 43.61 C ANISOU 1593 C5 A D 5 6207 4227 6138 -540 577 1891 C ATOM 1594 C6 A D 5 23.010 21.644 2.406 0.83 46.66 C ANISOU 1594 C6 A D 5 6640 4405 6684 -710 436 2118 C ATOM 1595 N6 A D 5 23.934 21.940 1.489 0.83 49.98 N ANISOU 1595 N6 A D 5 6976 4950 7063 -918 490 2406 N ATOM 1596 N1 A D 5 22.432 22.655 3.092 0.83 47.44 N ANISOU 1596 N1 A D 5 6864 4170 6991 -656 214 2044 N ATOM 1597 C2 A D 5 21.506 22.357 4.013 0.83 45.68 C ANISOU 1597 C2 A D 5 6692 3893 6771 -435 170 1760 C ATOM 1598 N3 A D 5 21.037 21.168 4.383 0.83 42.52 N ANISOU 1598 N3 A D 5 6237 3705 6214 -285 311 1567 N ATOM 1599 C4 A D 5 21.630 20.186 3.682 0.83 41.67 C ANISOU 1599 C4 A D 5 6027 3864 5941 -355 503 1649 C ATOM 1600 P A D 6 17.093 15.465 6.301 0.83 29.56 P ANISOU 1600 P A D 6 4314 2902 4015 382 645 887 P ATOM 1601 OP1 A D 6 16.033 16.118 7.098 0.83 28.50 O ANISOU 1601 OP1 A D 6 4195 2735 3898 517 547 795 O ATOM 1602 OP2 A D 6 17.820 14.316 6.883 0.83 26.69 O ANISOU 1602 OP2 A D 6 3844 2657 3641 335 712 839 O ATOM 1603 O5' A D 6 16.394 15.044 4.933 0.83 29.18 O ANISOU 1603 O5' A D 6 4304 2910 3872 410 667 972 O ATOM 1604 C5' A D 6 15.341 14.064 4.983 0.83 28.50 C ANISOU 1604 C5' A D 6 4163 2936 3728 497 657 927 C ATOM 1605 C4' A D 6 14.679 13.917 3.637 0.83 29.52 C ANISOU 1605 C4' A D 6 4345 3088 3781 539 650 992 C ATOM 1606 O4' A D 6 13.966 12.649 3.632 0.83 27.57 O ANISOU 1606 O4' A D 6 4019 2950 3505 588 631 951 O ATOM 1607 C3' A D 6 13.630 14.979 3.295 0.83 30.38 C ANISOU 1607 C3' A D 6 4550 3110 3884 626 576 1016 C ATOM 1608 O3' A D 6 13.569 15.107 1.870 0.83 32.27 O ANISOU 1608 O3' A D 6 4857 3354 4050 624 588 1115 O ATOM 1609 C2' A D 6 12.358 14.335 3.843 0.83 29.87 C ANISOU 1609 C2' A D 6 4410 3144 3795 729 534 943 C ATOM 1610 O2' A D 6 11.151 14.857 3.328 0.83 30.82 O ANISOU 1610 O2' A D 6 4585 3246 3877 838 467 946 O ATOM 1611 C1' A D 6 12.585 12.882 3.425 0.83 28.26 C ANISOU 1611 C1' A D 6 4128 3044 3565 686 569 951 C ATOM 1612 N9 A D 6 11.829 11.867 4.162 0.83 27.27 N ANISOU 1612 N9 A D 6 3883 3022 3457 708 529 920 N ATOM 1613 C8 A D 6 11.945 11.508 5.483 0.83 26.82 C ANISOU 1613 C8 A D 6 3721 3034 3436 679 531 898 C ATOM 1614 N7 A D 6 11.141 10.535 5.839 0.83 25.41 N ANISOU 1614 N7 A D 6 3429 2961 3265 679 479 928 N ATOM 1615 C5 A D 6 10.468 10.213 4.669 0.83 26.41 C ANISOU 1615 C5 A D 6 3594 3064 3376 717 432 946 C ATOM 1616 C6 A D 6 9.477 9.256 4.378 0.83 26.86 C ANISOU 1616 C6 A D 6 3571 3177 3457 725 341 984 C ATOM 1617 N6 A D 6 8.968 8.415 5.283 0.83 25.61 N ANISOU 1617 N6 A D 6 3262 3121 3346 670 284 1048 N ATOM 1618 N1 A D 6 9.010 9.201 3.110 0.83 27.99 N ANISOU 1618 N1 A D 6 3784 3276 3576 785 299 969 N ATOM 1619 C2 A D 6 9.514 10.051 2.203 0.83 28.21 C ANISOU 1619 C2 A D 6 3946 3235 3539 828 356 944 C ATOM 1620 N3 A D 6 10.447 10.991 2.354 0.83 28.18 N ANISOU 1620 N3 A D 6 4018 3175 3512 802 440 945 N ATOM 1621 C4 A D 6 10.887 11.021 3.625 0.83 27.32 C ANISOU 1621 C4 A D 6 3845 3085 3449 747 469 934 C ATOM 1622 P A D 7 14.101 16.430 1.122 0.83 33.61 P ANISOU 1622 P A D 7 5138 3398 4234 556 568 1258 P ATOM 1623 OP1 A D 7 14.393 17.475 2.143 0.83 34.31 O ANISOU 1623 OP1 A D 7 5264 3317 4455 528 493 1229 O ATOM 1624 OP2 A D 7 13.169 16.741 -0.002 0.83 34.10 O ANISOU 1624 OP2 A D 7 5279 3461 4216 637 523 1329 O ATOM 1625 O5' A D 7 15.438 15.942 0.402 0.83 33.63 O ANISOU 1625 O5' A D 7 5085 3524 4169 437 675 1349 O ATOM 1626 C5' A D 7 16.743 16.100 0.992 0.83 31.77 C ANISOU 1626 C5' A D 7 4799 3272 4001 309 722 1368 C ATOM 1627 C4' A D 7 17.658 15.011 0.482 0.83 30.45 C ANISOU 1627 C4' A D 7 4525 3314 3730 275 823 1355 C ATOM 1628 O4' A D 7 17.089 13.717 0.833 0.83 28.53 O ANISOU 1628 O4' A D 7 4225 3145 3471 377 811 1199 O ATOM 1629 C3' A D 7 17.869 14.976 -1.033 0.83 31.38 C ANISOU 1629 C3' A D 7 4635 3603 3686 279 871 1481 C ATOM 1630 O3' A D 7 19.178 14.483 -1.309 0.83 32.38 O ANISOU 1630 O3' A D 7 4648 3920 3736 209 961 1496 O ATOM 1631 C2' A D 7 16.822 13.964 -1.492 0.83 29.80 C ANISOU 1631 C2' A D 7 4430 3485 3406 438 836 1360 C ATOM 1632 O2' A D 7 17.126 13.421 -2.769 0.83 30.17 O ANISOU 1632 O2' A D 7 4425 3761 3279 496 876 1383 O ATOM 1633 C1' A D 7 16.861 12.958 -0.341 0.83 27.86 C ANISOU 1633 C1' A D 7 4116 3213 3255 457 819 1191 C ATOM 1634 N9 A D 7 15.626 12.195 -0.152 0.83 25.70 N ANISOU 1634 N9 A D 7 3842 2916 3006 567 740 1089 N ATOM 1635 C8 A D 7 14.341 12.673 -0.063 0.83 25.51 C ANISOU 1635 C8 A D 7 3882 2803 3008 633 677 1101 C ATOM 1636 N7 A D 7 13.439 11.737 0.116 0.83 24.20 N ANISOU 1636 N7 A D 7 3669 2662 2863 706 610 1018 N ATOM 1637 C5 A D 7 14.180 10.564 0.151 0.83 23.59 C ANISOU 1637 C5 A D 7 3508 2662 2794 690 607 945 C ATOM 1638 C6 A D 7 13.810 9.217 0.301 0.83 22.37 C ANISOU 1638 C6 A D 7 3275 2530 2692 729 512 857 C ATOM 1639 N6 A D 7 12.548 8.811 0.465 0.83 21.94 N ANISOU 1639 N6 A D 7 3201 2448 2690 774 418 852 N ATOM 1640 N1 A D 7 14.796 8.291 0.303 0.83 22.47 N ANISOU 1640 N1 A D 7 3224 2594 2719 717 496 781 N ATOM 1641 C2 A D 7 16.061 8.702 0.146 0.83 22.78 C ANISOU 1641 C2 A D 7 3261 2698 2697 670 595 791 C ATOM 1642 N3 A D 7 16.532 9.937 -0.015 0.83 23.53 N ANISOU 1642 N3 A D 7 3408 2796 2736 607 702 895 N ATOM 1643 C4 A D 7 15.529 10.831 -0.010 0.83 24.36 C ANISOU 1643 C4 A D 7 3593 2810 2852 619 692 971 C TER 1644 A D 7 ATOM 1645 P U E 4 27.100 -5.768 -4.819 1.00 37.20 P ATOM 1646 OP1 U E 4 27.068 -5.098 -6.143 1.00 35.01 O ATOM 1647 OP2 U E 4 27.766 -5.078 -3.681 1.00 38.39 O ATOM 1648 O5' U E 4 25.603 -5.956 -4.302 1.00 38.36 O ATOM 1649 C5' U E 4 25.007 -4.881 -3.565 1.00 41.34 C ATOM 1650 C4' U E 4 23.618 -5.196 -3.068 1.00 42.10 C ATOM 1651 O4' U E 4 22.880 -6.086 -3.941 1.00 40.92 O ATOM 1652 C3' U E 4 23.478 -5.946 -1.757 1.00 44.10 C ATOM 1653 O3' U E 4 23.966 -5.286 -0.605 1.00 47.23 O ATOM 1654 C2' U E 4 21.976 -6.194 -1.750 1.00 41.10 C ATOM 1655 O2' U E 4 21.220 -5.048 -1.417 1.00 42.74 O ATOM 1656 C1' U E 4 21.734 -6.534 -3.224 1.00 41.22 C ATOM 1657 N1 U E 4 21.559 -7.978 -3.419 1.00 40.01 N ATOM 1658 C2 U E 4 20.259 -8.436 -3.510 1.00 39.18 C ATOM 1659 O2 U E 4 19.294 -7.694 -3.476 1.00 34.36 O ATOM 1660 N3 U E 4 20.135 -9.796 -3.647 1.00 40.14 N ATOM 1661 C4 U E 4 21.152 -10.728 -3.685 1.00 40.59 C ATOM 1662 O4 U E 4 20.876 -11.922 -3.821 1.00 44.10 O ATOM 1663 C5 U E 4 22.468 -10.178 -3.558 1.00 40.47 C ATOM 1664 C6 U E 4 22.622 -8.854 -3.422 1.00 40.16 C ATOM 1665 P U E 5 25.064 -6.010 0.312 1.00 55.69 P ATOM 1666 OP1 U E 5 26.083 -4.994 0.685 1.00 54.28 O ATOM 1667 OP2 U E 5 25.497 -7.266 -0.366 1.00 54.96 O ATOM 1668 O5' U E 5 24.224 -6.451 1.594 1.00 53.39 O ATOM 1669 C5' U E 5 23.335 -5.532 2.259 1.00 52.61 C ATOM 1670 C4' U E 5 23.980 -4.987 3.512 1.00 53.22 C ATOM 1671 O4' U E 5 23.234 -5.448 4.664 1.00 52.11 O ATOM 1672 C3' U E 5 25.444 -5.382 3.707 1.00 53.79 C ATOM 1673 O3' U E 5 26.294 -4.252 3.509 1.00 52.38 O ATOM 1674 C2' U E 5 25.528 -5.957 5.126 1.00 52.37 C ATOM 1675 O2' U E 5 26.182 -5.116 6.052 1.00 47.90 O ATOM 1676 C1' U E 5 24.064 -6.228 5.493 1.00 52.68 C ATOM 1677 N1 U E 5 23.652 -7.636 5.382 1.00 52.29 N ATOM 1678 C2 U E 5 22.755 -8.117 6.320 1.00 51.08 C ATOM 1679 O2 U E 5 22.292 -7.425 7.211 1.00 48.43 O ATOM 1680 N3 U E 5 22.422 -9.441 6.172 1.00 50.69 N ATOM 1681 C4 U E 5 22.881 -10.317 5.209 1.00 50.12 C ATOM 1682 O4 U E 5 22.488 -11.484 5.214 1.00 49.80 O ATOM 1683 C5 U E 5 23.803 -9.745 4.275 1.00 49.65 C ATOM 1684 C6 U E 5 24.152 -8.458 4.392 1.00 52.15 C TER 1685 U E 5 HETATM 1686 O HOH A 101 8.183 0.847 13.741 1.00 11.85 O HETATM 1687 O HOH A 102 18.061 -7.786 19.198 1.00 16.38 O HETATM 1688 O HOH A 103 14.071 -2.539 19.026 1.00 17.41 O HETATM 1689 O HOH A 104 20.987 -4.074 1.232 1.00 12.09 O HETATM 1690 O HOH A 105 18.729 14.126 13.762 1.00 26.73 O HETATM 1691 O HOH A 106 9.746 6.989 18.795 1.00 10.82 O HETATM 1692 O HOH A 107 8.011 5.715 3.722 1.00 19.12 O HETATM 1693 O HOH A 108 11.629 -9.222 18.127 1.00 12.18 O HETATM 1694 O HOH A 109 15.124 7.964 20.758 1.00 16.78 O HETATM 1695 O HOH A 110 15.086 -4.377 20.817 1.00 22.61 O HETATM 1696 O HOH A 111 18.794 -12.476 19.419 1.00 14.31 O HETATM 1697 O HOH A 112 9.339 9.184 13.471 1.00 19.11 O HETATM 1698 O HOH A 113 9.656 -2.233 20.791 1.00 18.10 O HETATM 1699 O HOH A 114 9.505 5.676 21.284 1.00 18.94 O HETATM 1700 O HOH A 115 4.754 -1.409 12.537 1.00 19.63 O HETATM 1701 O HOH A 116 15.912 10.807 15.180 1.00 26.52 O HETATM 1702 O HOH A 117 2.563 3.779 16.916 1.00 23.81 O HETATM 1703 O HOH A 118 9.071 -8.834 7.816 1.00 16.60 O HETATM 1704 O HOH A 119 17.864 -3.759 21.863 1.00 30.91 O HETATM 1705 O HOH A 120 15.563 -11.946 1.589 1.00 32.93 O HETATM 1706 O HOH A 121 16.149 9.487 17.636 1.00 27.05 O HETATM 1707 O HOH A 122 9.912 -11.065 9.573 1.00 30.57 O HETATM 1708 O HOH A 123 11.709 -8.208 21.224 1.00 25.82 O HETATM 1709 O HOH A 124 7.137 8.382 12.147 1.00 18.55 O HETATM 1710 O HOH A 125 13.332 13.184 8.330 1.00 20.05 O HETATM 1711 O HOH A 126 12.472 8.928 21.938 1.00 19.09 O HETATM 1712 O HOH A 127 17.584 -9.464 8.254 1.00 28.14 O HETATM 1713 O HOH A 128 15.729 -11.284 7.173 1.00 22.40 O HETATM 1714 O HOH A 129 -2.636 0.952 5.446 1.00 19.27 O HETATM 1715 O HOH A 130 28.783 8.447 3.126 1.00 27.43 O HETATM 1716 O HOH A 131 15.433 -7.015 20.298 1.00 29.94 O HETATM 1717 O HOH A 132 5.417 6.467 12.475 1.00 26.40 O HETATM 1718 O HOH A 133 11.109 2.701 21.944 1.00 29.17 O HETATM 1719 O HOH A 134 1.919 -3.674 14.094 1.00 30.56 O HETATM 1720 O HOH A 135 27.431 -0.290 2.661 1.00 25.91 O HETATM 1721 O HOH A 136 12.849 12.690 16.801 1.00 26.11 O HETATM 1722 O HOH A 137 20.676 -11.072 11.091 1.00 35.82 O HETATM 1723 O HOH A 138 13.982 12.467 14.428 1.00 39.95 O HETATM 1724 O HOH A 139 12.960 -12.022 6.858 1.00 29.10 O HETATM 1725 O HOH A 140 12.126 -1.651 20.524 1.00 27.87 O HETATM 1726 O HOH A 141 0.570 2.826 13.836 1.00 38.28 O HETATM 1727 O HOH A 142 5.060 2.539 20.459 1.00 30.00 O HETATM 1728 O HOH A 143 19.161 -11.057 13.269 1.00 21.78 O HETATM 1729 O HOH A 144 10.290 -11.391 6.626 1.00 29.83 O HETATM 1730 O HOH B 101 28.226 5.896 27.657 1.00 25.39 O HETATM 1731 O HOH B 102 30.726 -0.190 25.809 1.00 16.72 O HETATM 1732 O HOH B 103 24.392 9.246 9.019 1.00 25.17 O HETATM 1733 O HOH B 104 29.016 12.642 19.333 1.00 13.61 O HETATM 1734 O HOH B 105 22.414 5.126 21.136 1.00 14.47 O HETATM 1735 O HOH B 106 26.891 -9.176 21.983 1.00 10.67 O HETATM 1736 O HOH B 107 37.662 -9.350 25.067 1.00 18.58 O HETATM 1737 O HOH B 108 27.024 10.220 26.305 1.00 14.23 O HETATM 1738 O HOH B 109 21.326 -7.341 23.056 1.00 18.29 O HETATM 1739 O HOH B 110 15.323 0.545 20.120 1.00 18.76 O HETATM 1740 O HOH B 111 30.810 8.171 24.874 1.00 17.97 O HETATM 1741 O HOH B 112 22.648 -9.209 12.001 1.00 20.84 O HETATM 1742 O HOH B 113 37.817 -2.160 26.582 1.00 25.32 O HETATM 1743 O HOH B 114 15.791 1.425 23.706 1.00 26.27 O HETATM 1744 O HOH B 115 38.578 -3.198 23.650 1.00 14.06 O HETATM 1745 O HOH B 116 21.228 8.755 22.875 1.00 16.45 O HETATM 1746 O HOH B 117 31.408 -0.077 3.692 1.00 17.17 O HETATM 1747 O HOH B 118 35.742 5.918 27.468 1.00 15.40 O HETATM 1748 O HOH B 119 39.367 -0.372 23.647 1.00 25.49 O HETATM 1749 O HOH B 120 31.442 -9.682 15.075 1.00 22.54 O HETATM 1750 O HOH B 121 26.563 -1.092 28.874 1.00 25.69 O HETATM 1751 O HOH B 122 28.523 2.140 4.116 1.00 20.58 O HETATM 1752 O HOH B 123 30.659 -10.030 7.885 1.00 30.11 O HETATM 1753 O HOH B 124 32.898 -7.576 10.371 1.00 21.63 O HETATM 1754 O HOH B 125 27.841 -12.678 25.576 1.00 33.23 O HETATM 1755 O HOH B 126 22.376 -9.955 23.650 1.00 22.47 O HETATM 1756 O HOH B 127 29.143 4.110 2.267 1.00 29.64 O HETATM 1757 O HOH B 128 25.292 -11.685 18.823 1.00 24.12 O HETATM 1758 O HOH B 129 32.101 -11.201 9.973 1.00 38.71 O HETATM 1759 O HOH B 130 25.557 5.139 27.312 1.00 27.81 O HETATM 1760 O HOH B 131 22.510 -8.659 26.525 1.00 34.36 O HETATM 1761 O HOH B 132 28.547 7.882 26.281 1.00 23.21 O HETATM 1762 O HOH B 133 27.627 12.649 21.384 1.00 21.53 O HETATM 1763 O HOH B 134 35.671 -12.405 21.993 1.00 19.38 O HETATM 1764 O HOH B 135 29.906 1.788 0.409 0.50 18.26 O HETATM 1765 O HOH B 136 38.960 -11.681 24.747 1.00 26.53 O HETATM 1766 O HOH B 137 30.768 15.331 21.315 1.00 35.18 O HETATM 1767 O HOH B 138 18.912 -6.881 21.985 1.00 14.19 O HETATM 1768 O HOH B 139 36.477 -12.310 24.067 1.00 27.20 O HETATM 1769 O HOH B 140 22.551 3.940 28.514 1.00 24.89 O HETATM 1770 O HOH B 141 39.247 -0.026 26.572 1.00 28.39 O HETATM 1771 O HOH B 142 31.795 -12.907 20.591 1.00 28.70 O HETATM 1772 O HOH B 143 29.225 -10.765 22.429 1.00 27.53 O HETATM 1773 O HOH B 144 39.195 2.473 27.821 1.00 24.76 O HETATM 1774 O HOH B 145 24.778 -10.994 22.425 1.00 19.53 O HETATM 1775 O HOH B 146 27.330 -14.050 19.597 1.00 30.18 O HETATM 1776 O HOH B 147 28.254 5.603 0.262 1.00 33.57 O HETATM 1777 O HOH B 148 32.202 8.321 3.086 1.00 32.12 O HETATM 1778 O HOH C 101 13.791 -10.757 -11.328 1.00 21.17 O HETATM 1779 O HOH C 102 24.405 -3.930 -6.900 1.00 10.29 O HETATM 1780 O HOH C 103 12.861 -13.532 2.908 1.00 20.97 O HETATM 1781 O HOH C 104 4.501 -8.836 -6.207 1.00 19.63 O HETATM 1782 O HOH C 105 17.863 14.635 -8.018 1.00 20.60 O HETATM 1783 O HOH C 106 7.632 0.396 -12.055 1.00 17.17 O HETATM 1784 O HOH C 107 12.630 -8.459 -14.033 1.00 17.83 O HETATM 1785 O HOH C 108 19.712 8.822 -0.708 1.00 23.02 O HETATM 1786 O HOH C 109 7.190 -1.846 -15.547 1.00 22.39 O HETATM 1787 O HOH C 110 5.133 -2.751 -4.795 1.00 17.10 O HETATM 1788 O HOH C 111 23.368 -8.774 -11.891 1.00 17.51 O HETATM 1789 O HOH C 112 19.171 0.895 -22.791 1.00 16.86 O HETATM 1790 O HOH C 113 19.673 17.002 -7.063 1.00 34.48 O HETATM 1791 O HOH C 114 8.266 -11.819 -6.512 1.00 15.23 O HETATM 1792 O HOH C 115 16.247 -9.164 -6.548 1.00 20.14 O HETATM 1793 O HOH C 116 21.016 8.216 -15.298 1.00 29.74 O HETATM 1794 O HOH C 117 8.193 8.691 -11.331 1.00 24.84 O HETATM 1795 O HOH C 118 14.145 13.151 -10.675 1.00 34.17 O HETATM 1796 O HOH C 119 14.271 4.234 -23.460 1.00 39.03 O HETATM 1797 O HOH C 120 8.619 -5.758 -17.566 1.00 26.78 O HETATM 1798 O HOH C 121 15.468 10.409 -13.738 1.00 22.33 O HETATM 1799 O HOH C 122 3.543 6.109 -8.580 1.00 24.78 O HETATM 1800 O HOH C 123 6.789 -7.298 -0.615 1.00 17.17 O HETATM 1801 O HOH C 124 16.307 -11.521 -7.907 1.00 25.14 O HETATM 1802 O HOH C 125 5.522 -11.438 -7.030 1.00 23.67 O HETATM 1803 O HOH C 126 15.419 -13.615 3.739 1.00 31.01 O HETATM 1804 O HOH C 127 3.188 -1.963 -6.782 1.00 29.17 O HETATM 1805 O HOH C 128 9.946 -13.759 -4.932 1.00 32.22 O HETATM 1806 O HOH C 129 17.982 2.522 -24.605 1.00 23.98 O HETATM 1807 O HOH C 130 6.061 -9.671 0.268 1.00 27.54 O HETATM 1808 O HOH C 131 4.721 -6.924 -2.422 1.00 23.28 O HETATM 1809 O HOH C 132 4.534 -11.575 -1.558 1.00 27.45 O HETATM 1810 O HOH C 133 10.553 -12.579 2.983 1.00 20.12 O HETATM 1811 O HOH C 134 10.981 -10.058 -12.331 1.00 22.64 O HETATM 1812 O HOH C 135 16.077 -9.120 -0.324 1.00 23.73 O HETATM 1813 O HOH C 136 11.829 5.380 -23.193 1.00 31.35 O HETATM 1814 O HOH C 137 3.515 -9.066 -8.907 1.00 21.91 O HETATM 1815 O HOH C 138 18.252 4.896 -23.475 1.00 22.81 O HETATM 1816 O HOH C 139 3.896 -4.527 -3.026 1.00 18.23 O HETATM 1817 O HOH C 140 16.682 -13.482 -11.623 1.00 31.06 O HETATM 1818 O HOH C 141 17.268 9.604 -15.745 1.00 30.99 O HETATM 1819 O HOH C 142 4.699 -0.038 -3.886 1.00 28.61 O HETATM 1820 O HOH C 143 7.006 -13.089 -0.233 1.00 26.97 O HETATM 1821 O HOH C 144 14.561 -5.969 -19.604 1.00 24.75 O HETATM 1822 O HOH D 101 20.074 11.953 16.752 1.00 11.83 O HETATM 1823 O HOH D 102 32.522 14.547 14.865 1.00 10.40 O HETATM 1824 O HOH D 103 20.761 14.645 17.463 1.00 13.62 O HETATM 1825 O HOH D 104 20.081 6.959 21.045 1.00 13.27 O HETATM 1826 O HOH D 105 17.839 8.306 20.823 1.00 28.37 O HETATM 1827 O HOH D 106 19.046 14.976 9.513 1.00 18.90 O HETATM 1828 O HOH D 107 20.706 17.594 10.186 1.00 25.11 O HETATM 1829 O HOH D 108 28.546 15.250 18.878 1.00 22.45 O HETATM 1830 O HOH D 109 6.637 7.701 1.960 1.00 32.10 O HETATM 1831 O HOH D 110 39.933 15.083 14.303 1.00 22.75 O HETATM 1832 O HOH D 111 23.373 20.022 7.904 1.00 30.53 O HETATM 1833 O HOH D 112 26.667 13.089 5.885 1.00 17.95 O HETATM 1834 O HOH D 113 16.924 18.563 3.611 1.00 28.12 O HETATM 1835 O HOH D 114 26.276 18.070 14.597 1.00 18.49 O HETATM 1836 O HOH D 115 14.333 15.746 9.115 1.00 22.42 O HETATM 1837 O HOH D 116 28.139 15.438 7.925 1.00 26.29 O HETATM 1838 O HOH D 117 24.883 19.107 5.907 1.00 30.74 O HETATM 1839 O HOH E 101 28.382 -5.256 -8.520 1.00 20.22 O HETATM 1840 O HOH E 102 26.995 -4.270 8.205 1.00 16.53 O HETATM 1841 O HOH E 103 29.266 -2.832 -4.126 1.00 31.63 O HETATM 1842 O HOH E 104 28.585 -5.210 3.917 1.00 36.82 O HETATM 1843 O HOH E 105 25.465 -10.654 1.191 1.00 42.98 O HETATM 1844 O HOH E 106 25.700 -9.278 -2.239 1.00 44.81 O HETATM 1845 O HOH E 107 17.811 -10.477 -4.140 1.00 42.11 O HETATM 1846 O HOH E 108 29.485 -6.095 7.835 1.00 32.89 O HETATM 1847 O HOH E 109 27.763 -10.780 3.478 1.00 46.85 O MASTER 383 0 0 3 15 0 0 6 1793 5 0 17 END
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Complexes with the same small molecule ligand
PDB Code
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Ligand Name
No complexes with the same small molecule ligand are found!
Entry Information
PDB ID
4ht9
Complex Type
Protein-Nucleic Acid
PDBbind Subset
general set
Protein Name
E. coli Protein hfq
Ligand Name
7-mer poly(A) A7 and A-U6-A RNA
EC.Number
E.C.-.-.-.-
Resolution
1.8(Å)
Affinity (Kd/Ki/IC50)
Kd=392nM
Release Year
2013
Protein/NA Sequence
Check fasta file
Primary Reference
(2013) Nucleic Acids Res. Vol. 41: pp. 5938-5948
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
A0A140NGK1
Entrez Gene ID
NCBI Entrez Gene ID:
61753826
ASD
Information of known allosteric effects of PDB entries
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