Browse entries in the PDBbind-CN Database
HEADER RNA BINDING PROTEIN/RNA 16-JAN-19 6NOH TITLE CRYSTAL STRUCTURE OF FBF-2 REPEAT 5 MUTANT (C363S, R364Y, Q367S) IN TITLE 2 COMPLEX WITH 8-NT RNA COMPND MOL_ID: 1; COMPND 2 MOLECULE: FEM-3 MRNA-BINDING FACTOR 2; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: FBF-2; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: RNA (5'-R(*UP*GP*UP*AP*AP*AP*UP*A)-3'); COMPND 9 CHAIN: B; COMPND 10 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CAENORHABDITIS ELEGANS; SOURCE 3 ORGANISM_TAXID: 6239; SOURCE 4 GENE: FBF-2, F21H12.5; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 MOL_ID: 2; SOURCE 8 SYNTHETIC: YES; SOURCE 9 ORGANISM_SCIENTIFIC: CAENORHABDITIS ELEGANS; SOURCE 10 ORGANISM_TAXID: 6239 KEYWDS PUM REPEAT PROTEIN, RNA BINDING PROTEIN, RNA BINDING PROTEIN-RNA KEYWDS 2 COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR K.L.MCCANN,Y.WANG,C.QIU,T.M.T.HALL REVDAT 2 07-OCT-20 6NOH 1 JRNL REVDAT 1 30-JAN-19 6NOH 0 JRNL AUTH V.D.BHAT,K.L.MCCANN,Y.WANG,D.R.FONSECA,T.SHUKLA, JRNL AUTH 2 J.C.ALEXANDER,C.QIU,M.WICKENS,T.W.LO,T.M.TANAKA HALL, JRNL AUTH 3 Z.T.CAMPBELL JRNL TITL ENGINEERING A CONSERVED RNA REGULATORY PROTEIN REPURPOSES JRNL TITL 2 ITS BIOLOGICAL FUNCTION IN VIVO . JRNL REF ELIFE V. 8 2019 JRNL REFN ESSN 2050-084X JRNL PMID 30652968 JRNL DOI 10.7554/ELIFE.43788 REMARK 2 REMARK 2 RESOLUTION. 2.25 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.14_3260: ???) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.68 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 25061 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.163 REMARK 3 R VALUE (WORKING SET) : 0.159 REMARK 3 FREE R VALUE : 0.206 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.960 REMARK 3 FREE R VALUE TEST SET COUNT : 1994 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 34.6804 - 5.4142 1.00 1679 146 0.1651 0.2074 REMARK 3 2 5.4142 - 4.3000 1.00 1653 150 0.1440 0.1611 REMARK 3 3 4.3000 - 3.7572 1.00 1645 144 0.1366 0.1745 REMARK 3 4 3.7572 - 3.4140 1.00 1652 139 0.1471 0.1948 REMARK 3 5 3.4140 - 3.1695 1.00 1659 140 0.1647 0.2140 REMARK 3 6 3.1695 - 2.9827 1.00 1651 138 0.1639 0.2088 REMARK 3 7 2.9827 - 2.8334 1.00 1624 133 0.1613 0.2426 REMARK 3 8 2.8334 - 2.7101 1.00 1664 145 0.1717 0.2493 REMARK 3 9 2.7101 - 2.6058 1.00 1628 142 0.1709 0.2185 REMARK 3 10 2.6058 - 2.5159 1.00 1653 146 0.1738 0.2361 REMARK 3 11 2.5159 - 2.4373 1.00 1631 142 0.1789 0.2591 REMARK 3 12 2.4373 - 2.3676 1.00 1653 143 0.1718 0.2611 REMARK 3 13 2.3676 - 2.3053 1.00 1643 143 0.1919 0.2326 REMARK 3 14 2.3053 - 2.2491 1.00 1632 143 0.1976 0.2495 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.970 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 36.64 REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.007 3465 REMARK 3 ANGLE : 0.794 4680 REMARK 3 CHIRALITY : 0.044 539 REMARK 3 PLANARITY : 0.004 569 REMARK 3 DIHEDRAL : 3.668 2876 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 168 THROUGH 383 ) REMARK 3 ORIGIN FOR THE GROUP (A): 74.2098 97.8290 -4.7852 REMARK 3 T TENSOR REMARK 3 T11: 0.2010 T22: 0.2305 REMARK 3 T33: 0.2692 T12: -0.0109 REMARK 3 T13: -0.0125 T23: 0.0501 REMARK 3 L TENSOR REMARK 3 L11: 0.4948 L22: 1.0366 REMARK 3 L33: 1.1383 L12: -0.4294 REMARK 3 L13: 0.4372 L23: -0.6645 REMARK 3 S TENSOR REMARK 3 S11: 0.0761 S12: -0.0423 S13: -0.1456 REMARK 3 S21: -0.0132 S22: 0.1135 S23: 0.2388 REMARK 3 S31: -0.0027 S32: -0.1273 S33: 0.0013 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 384 THROUGH 569 ) REMARK 3 ORIGIN FOR THE GROUP (A): 99.7665 66.8873 15.5892 REMARK 3 T TENSOR REMARK 3 T11: 0.3165 T22: 0.2370 REMARK 3 T33: 0.2319 T12: -0.0122 REMARK 3 T13: -0.0102 T23: 0.0035 REMARK 3 L TENSOR REMARK 3 L11: 0.1314 L22: 2.2057 REMARK 3 L33: 0.0394 L12: -0.5904 REMARK 3 L13: 0.1472 L23: -0.4145 REMARK 3 S TENSOR REMARK 3 S11: -0.0411 S12: 0.0153 S13: 0.0170 REMARK 3 S21: -0.2058 S22: 0.0970 S23: 0.0351 REMARK 3 S31: 0.0150 S32: 0.0063 S33: -0.0001 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 8 ) REMARK 3 ORIGIN FOR THE GROUP (A): 82.9699 73.3646 -0.3374 REMARK 3 T TENSOR REMARK 3 T11: 0.6220 T22: 0.1264 REMARK 3 T33: 0.3343 T12: 0.0979 REMARK 3 T13: -0.3710 T23: 0.0736 REMARK 3 L TENSOR REMARK 3 L11: 0.2929 L22: 0.0351 REMARK 3 L33: 0.2634 L12: 0.0103 REMARK 3 L13: -0.2433 L23: 0.0408 REMARK 3 S TENSOR REMARK 3 S11: 0.5476 S12: 0.2011 S13: -0.2928 REMARK 3 S21: -0.2941 S22: -0.2405 S23: 0.0686 REMARK 3 S31: 0.5626 S32: 0.2701 S33: 0.1310 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 6NOH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JAN-19. REMARK 100 THE DEPOSITION ID IS D_1000239121. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 14-OCT-16 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 22-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300-HS REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25098 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 5.700 REMARK 200 R MERGE (I) : 0.10100 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.29 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 5.70 REMARK 200 R MERGE FOR SHELL (I) : 0.70400 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 3K5Q REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 55.65 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS PH 8.6, 15% [W/V] PEG REMARK 280 8000, 8% [V/V] ETHYLENE GLYCOL, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+5/6 REMARK 290 6555 X-Y,X,Z+1/6 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 33.28433 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 66.56867 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 49.92650 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 83.21083 REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 16.64217 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4890 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19670 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 30.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A 163 REMARK 465 SER A 164 REMARK 465 ASN A 165 REMARK 465 ASN A 166 REMARK 465 VAL A 167 REMARK 465 PRO A 570 REMARK 465 ILE A 571 REMARK 465 TYR A 572 REMARK 465 GLU A 573 REMARK 465 LEU A 574 REMARK 465 GLN A 575 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 A B 8 C5' C4' O4' C3' O3' C2' O2' REMARK 470 A B 8 C1' N9 C8 N7 C5 C6 N6 REMARK 470 A B 8 N1 C2 N3 C4 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 174 -168.52 -107.82 REMARK 500 ARG A 182 10.41 58.80 REMARK 500 ASP A 259 -164.97 -100.81 REMARK 500 ASP A 312 -150.16 -107.48 REMARK 500 CYS A 438 -51.41 -121.44 REMARK 500 ASP A 477 24.66 -159.33 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 601 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 602 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 603 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 604 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 605 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 606 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 607 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 608 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 609 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 610 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 611 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 612 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 101 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6NOF RELATED DB: PDB DBREF 6NOH A 164 575 UNP Q09312 FBF2_CAEEL 164 575 DBREF 6NOH B 1 8 PDB 6NOH 6NOH 1 8 SEQADV 6NOH GLY A 163 UNP Q09312 EXPRESSION TAG SEQADV 6NOH SER A 363 UNP Q09312 CYS 363 ENGINEERED MUTATION SEQADV 6NOH TYR A 364 UNP Q09312 ARG 364 ENGINEERED MUTATION SEQADV 6NOH SER A 367 UNP Q09312 GLN 367 ENGINEERED MUTATION SEQRES 1 A 413 GLY SER ASN ASN VAL LEU PRO THR TRP SER LEU ASP SER SEQRES 2 A 413 ASN GLY GLU MET ARG SER ARG LEU SER LEU SER GLU VAL SEQRES 3 A 413 LEU ASP SER GLY ASP LEU MET LYS PHE ALA VAL ASP LYS SEQRES 4 A 413 THR GLY CYS GLN PHE LEU GLU LYS ALA VAL LYS GLY SER SEQRES 5 A 413 LEU THR SER TYR GLN LYS PHE GLN LEU PHE GLU GLN VAL SEQRES 6 A 413 ILE GLY ARG LYS ASP ASP PHE LEU LYS LEU SER THR ASN SEQRES 7 A 413 ILE PHE GLY ASN TYR LEU VAL GLN SER VAL ILE GLY ILE SEQRES 8 A 413 SER LEU ALA THR ASN ASP ASP GLY TYR THR LYS ARG GLN SEQRES 9 A 413 GLU LYS LEU LYS ASN PHE ILE SER SER GLN MET THR ASP SEQRES 10 A 413 MET CYS LEU ASP LYS PHE ALA CYS ARG VAL ILE GLN SER SEQRES 11 A 413 SER LEU GLN ASN MET ASP LEU SER LEU ALA CYS LYS LEU SEQRES 12 A 413 VAL GLN ALA LEU PRO ARG ASP ALA ARG LEU ILE ALA ILE SEQRES 13 A 413 CYS VAL ASP GLN ASN ALA ASN HIS VAL ILE GLN LYS VAL SEQRES 14 A 413 VAL ALA VAL ILE PRO LEU LYS ASN TRP GLU PHE ILE VAL SEQRES 15 A 413 ASP PHE VAL ALA THR PRO GLU HIS LEU ARG GLN ILE CYS SEQRES 16 A 413 SER ASP LYS TYR GLY SER TYR VAL VAL SER THR ILE ILE SEQRES 17 A 413 GLU LYS LEU THR ALA ASP SER MET ASN VAL ASP LEU THR SEQRES 18 A 413 SER ALA ALA GLN ASN LEU ARG GLU ARG ALA LEU GLN ARG SEQRES 19 A 413 LEU MET THR SER VAL THR ASN ARG CYS GLN GLU LEU ALA SEQRES 20 A 413 THR ASN GLU TYR ALA ASN TYR ILE ILE GLN HIS ILE VAL SEQRES 21 A 413 SER ASN ASP ASP LEU ALA VAL TYR ARG GLU CYS ILE ILE SEQRES 22 A 413 GLU LYS CYS LEU MET ARG ASN LEU LEU SER LEU SER GLN SEQRES 23 A 413 GLU LYS PHE ALA SER HIS VAL VAL GLU LYS ALA PHE LEU SEQRES 24 A 413 HIS ALA PRO LEU GLU LEU LEU ALA GLU MET MET ASP GLU SEQRES 25 A 413 ILE PHE ASP GLY TYR ILE PRO HIS PRO ASP THR GLY LYS SEQRES 26 A 413 ASP ALA LEU ASP ILE MET MET PHE HIS GLN PHE GLY ASN SEQRES 27 A 413 TYR VAL VAL GLN CYS MET LEU THR ILE CYS CYS ASP ALA SEQRES 28 A 413 VAL SER GLY ARG ARG GLN THR LYS GLU GLY GLY TYR ASP SEQRES 29 A 413 HIS ALA ILE SER PHE GLN ASP TRP LEU LYS LYS LEU HIS SEQRES 30 A 413 SER ARG VAL THR LYS GLU ARG HIS ARG LEU SER ARG PHE SEQRES 31 A 413 SER SER GLY LYS LYS MET ILE GLU THR LEU ALA ASN LEU SEQRES 32 A 413 ARG SER THR HIS PRO ILE TYR GLU LEU GLN SEQRES 1 B 8 U G U A A A U A HET EDO A 601 4 HET EDO A 602 4 HET EDO A 603 4 HET EDO A 604 4 HET EDO A 605 4 HET EDO A 606 4 HET EDO A 607 4 HET EDO A 608 4 HET EDO A 609 4 HET EDO A 610 4 HET EDO A 611 4 HET EDO A 612 4 HET EDO B 101 4 HETNAM EDO 1,2-ETHANEDIOL HETSYN EDO ETHYLENE GLYCOL FORMUL 3 EDO 13(C2 H6 O2) FORMUL 16 HOH *129(H2 O) HELIX 1 AA1 PRO A 169 LEU A 173 5 5 HELIX 2 AA2 SER A 184 GLY A 192 1 9 HELIX 3 AA3 ASP A 193 VAL A 199 1 7 HELIX 4 AA4 ASP A 200 VAL A 211 1 12 HELIX 5 AA5 THR A 216 GLY A 229 1 14 HELIX 6 AA6 ARG A 230 THR A 239 1 10 HELIX 7 AA7 PHE A 242 THR A 257 1 16 HELIX 8 AA8 GLY A 261 GLN A 276 1 16 HELIX 9 AA9 GLN A 276 ASP A 283 1 8 HELIX 10 AB1 PHE A 285 MET A 297 1 13 HELIX 11 AB2 ASP A 298 ALA A 308 1 11 HELIX 12 AB3 ASP A 312 VAL A 320 1 9 HELIX 13 AB4 ALA A 324 ILE A 335 1 12 HELIX 14 AB5 PRO A 336 THR A 349 1 14 HELIX 15 AB6 THR A 349 SER A 358 1 10 HELIX 16 AB7 ASP A 359 LEU A 373 1 15 HELIX 17 AB8 ASP A 376 VAL A 380 5 5 HELIX 18 AB9 THR A 383 ARG A 404 1 22 HELIX 19 AC1 ARG A 404 THR A 410 1 7 HELIX 20 AC2 ALA A 414 ASN A 424 1 11 HELIX 21 AC3 LEU A 427 CYS A 438 1 12 HELIX 22 AC4 ASN A 442 GLN A 448 1 7 HELIX 23 AC5 PHE A 451 ALA A 463 1 13 HELIX 24 AC6 PRO A 464 GLY A 478 1 15 HELIX 25 AC7 ASP A 488 PHE A 495 1 8 HELIX 26 AC8 PHE A 498 SER A 515 1 18 HELIX 27 AC9 HIS A 527 GLU A 545 1 19 HELIX 28 AD1 GLU A 545 ARG A 551 1 7 HELIX 29 AD2 PHE A 552 SER A 567 1 16 SSBOND 1 CYS A 405 CYS A 438 1555 1555 2.55 SITE 1 AC1 3 ALA A 375 GLN A 387 EDO A 602 SITE 1 AC2 5 GLN A 387 ASN A 388 ARG A 390 GLU A 391 SITE 2 AC2 5 EDO A 601 SITE 1 AC3 6 ASP A 298 LEU A 299 PHE A 495 ARG A 548 SITE 2 AC3 6 HOH A 711 HOH A 777 SITE 1 AC4 5 SER A 384 ALA A 385 ASP A 477 TYR A 479 SITE 2 AC4 5 SER A 553 SITE 1 AC5 4 LEU A 255 ASN A 258 ARG A 551 HOH A 770 SITE 1 AC6 6 PHE A 224 ILE A 228 GLY A 229 ARG A 265 SITE 2 AC6 6 LYS A 268 HOH A 703 SITE 1 AC7 2 LYS A 220 ALA A 256 SITE 1 AC8 3 ALA A 469 ASP A 533 TRP A 534 SITE 1 AC9 3 GLN A 248 SER A 292 ASN A 296 SITE 1 AD1 4 HIS A 454 GLU A 457 LYS A 458 EDO A 611 SITE 1 AD2 4 GLN A 419 LYS A 458 EDO A 610 U B 3 SITE 1 AD3 6 PHE A 495 GLN A 497 ASN A 500 PHE A 552 SITE 2 AD3 6 SER A 554 U B 1 SITE 1 AD4 2 A B 5 HOH B 202 CRYST1 96.397 96.397 99.853 90.00 90.00 120.00 P 61 6 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.010374 0.005989 0.000000 0.00000 SCALE2 0.000000 0.011979 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010015 0.00000 ATOM 1 N LEU A 168 56.935 95.239 -22.374 1.00 43.88 N ANISOU 1 N LEU A 168 4794 5026 6854 -579 -2137 1184 N ATOM 2 CA LEU A 168 57.559 96.153 -23.331 1.00 58.77 C ANISOU 2 CA LEU A 168 6805 6918 8608 -491 -2090 1070 C ATOM 3 C LEU A 168 56.475 96.955 -24.065 1.00 71.81 C ANISOU 3 C LEU A 168 8390 8596 10297 -484 -2144 1140 C ATOM 4 O LEU A 168 55.434 96.405 -24.421 1.00 75.27 O ANISOU 4 O LEU A 168 8762 8996 10841 -558 -2310 1230 O ATOM 5 CB LEU A 168 58.442 95.376 -24.317 1.00 60.00 C ANISOU 5 CB LEU A 168 7157 6974 8666 -479 -2211 936 C ATOM 6 CG LEU A 168 59.830 95.932 -24.681 1.00 54.52 C ANISOU 6 CG LEU A 168 6608 6295 7810 -380 -2088 793 C ATOM 7 CD1 LEU A 168 60.672 96.251 -23.447 1.00 47.65 C ANISOU 7 CD1 LEU A 168 5697 5493 6914 -351 -1890 779 C ATOM 8 CD2 LEU A 168 60.597 94.979 -25.571 1.00 48.02 C ANISOU 8 CD2 LEU A 168 5968 5376 6903 -365 -2215 681 C ATOM 9 N PRO A 169 56.709 98.252 -24.276 1.00 69.43 N ANISOU 9 N PRO A 169 8105 8359 9916 -398 -2010 1104 N ATOM 10 CA PRO A 169 55.654 99.114 -24.828 1.00 64.92 C ANISOU 10 CA PRO A 169 7456 7826 9384 -382 -2038 1181 C ATOM 11 C PRO A 169 55.617 99.074 -26.348 1.00 63.20 C ANISOU 11 C PRO A 169 7369 7538 9106 -373 -2195 1112 C ATOM 12 O PRO A 169 56.652 99.145 -27.015 1.00 60.32 O ANISOU 12 O PRO A 169 7169 7139 8612 -320 -2181 982 O ATOM 13 CB PRO A 169 56.044 100.506 -24.316 1.00 63.02 C ANISOU 13 CB PRO A 169 7197 7675 9073 -289 -1820 1163 C ATOM 14 CG PRO A 169 57.541 100.458 -24.252 1.00 62.20 C ANISOU 14 CG PRO A 169 7238 7551 8844 -248 -1731 1025 C ATOM 15 CD PRO A 169 57.928 99.013 -23.947 1.00 62.58 C ANISOU 15 CD PRO A 169 7318 7534 8924 -315 -1825 1003 C ATOM 16 N THR A 170 54.396 99.014 -26.896 1.00 65.83 N ANISOU 16 N THR A 170 7623 7858 9531 -419 -2341 1208 N ATOM 17 CA THR A 170 54.221 98.627 -28.298 1.00 66.85 C ANISOU 17 CA THR A 170 7881 7899 9622 -434 -2532 1151 C ATOM 18 C THR A 170 54.975 99.540 -29.273 1.00 64.12 C ANISOU 18 C THR A 170 7684 7556 9121 -333 -2481 1035 C ATOM 19 O THR A 170 55.483 99.058 -30.293 1.00 60.73 O ANISOU 19 O THR A 170 7425 7048 8603 -318 -2597 936 O ATOM 20 CB THR A 170 52.729 98.561 -28.641 1.00 68.57 C ANISOU 20 CB THR A 170 7998 8108 9949 -498 -2608 1258 C ATOM 21 OG1 THR A 170 52.081 99.762 -28.212 1.00 77.86 O ANISOU 21 OG1 THR A 170 9024 9393 11166 -452 -2489 1354 O ATOM 22 CG2 THR A 170 52.083 97.368 -27.939 1.00 64.12 C ANISOU 22 CG2 THR A 170 7349 7503 9512 -609 -2660 1344 C ATOM 23 N TRP A 171 55.099 100.840 -28.971 1.00 63.71 N ANISOU 23 N TRP A 171 7586 7592 9027 -259 -2298 1042 N ATOM 24 CA TRP A 171 55.859 101.740 -29.842 1.00 53.44 C ANISOU 24 CA TRP A 171 6427 6299 7581 -169 -2229 938 C ATOM 25 C TRP A 171 57.295 101.272 -30.081 1.00 60.41 C ANISOU 25 C TRP A 171 7479 7140 8336 -133 -2194 800 C ATOM 26 O TRP A 171 57.913 101.685 -31.069 1.00 60.59 O ANISOU 26 O TRP A 171 7641 7146 8235 -68 -2192 713 O ATOM 27 CB TRP A 171 55.881 103.158 -29.260 1.00 53.25 C ANISOU 27 CB TRP A 171 6328 6370 7536 -102 -2027 968 C ATOM 28 CG TRP A 171 56.754 103.330 -28.026 1.00 61.06 C ANISOU 28 CG TRP A 171 7293 7406 8502 -83 -1839 944 C ATOM 29 CD1 TRP A 171 56.332 103.370 -26.726 1.00 64.46 C ANISOU 29 CD1 TRP A 171 7578 7892 9024 -104 -1744 1033 C ATOM 30 CD2 TRP A 171 58.183 103.506 -27.984 1.00 53.25 C ANISOU 30 CD2 TRP A 171 6429 6415 7390 -36 -1726 828 C ATOM 31 NE1 TRP A 171 57.403 103.545 -25.884 1.00 61.59 N ANISOU 31 NE1 TRP A 171 7250 7553 8599 -75 -1589 973 N ATOM 32 CE2 TRP A 171 58.548 103.631 -26.630 1.00 59.07 C ANISOU 32 CE2 TRP A 171 7089 7200 8153 -38 -1578 850 C ATOM 33 CE3 TRP A 171 59.185 103.563 -28.960 1.00 49.24 C ANISOU 33 CE3 TRP A 171 6085 5872 6750 10 -1737 715 C ATOM 34 CZ2 TRP A 171 59.872 103.809 -26.228 1.00 58.42 C ANISOU 34 CZ2 TRP A 171 7088 7129 7979 -4 -1452 763 C ATOM 35 CZ3 TRP A 171 60.490 103.732 -28.562 1.00 51.02 C ANISOU 35 CZ3 TRP A 171 6380 6117 6888 46 -1603 636 C ATOM 36 CH2 TRP A 171 60.826 103.856 -27.207 1.00 57.35 C ANISOU 36 CH2 TRP A 171 7101 6964 7726 34 -1467 661 C ATOM 37 N SER A 172 57.852 100.442 -29.196 1.00 57.65 N ANISOU 37 N SER A 172 7116 6778 8011 -169 -2159 785 N ATOM 38 CA SER A 172 59.219 99.967 -29.354 1.00 60.69 C ANISOU 38 CA SER A 172 7649 7131 8280 -130 -2120 663 C ATOM 39 C SER A 172 59.312 98.633 -30.086 1.00 67.20 C ANISOU 39 C SER A 172 8594 7849 9089 -161 -2317 611 C ATOM 40 O SER A 172 60.421 98.111 -30.251 1.00 66.13 O ANISOU 40 O SER A 172 8586 7682 8857 -122 -2297 512 O ATOM 41 CB SER A 172 59.909 99.853 -27.982 1.00 57.10 C ANISOU 41 CB SER A 172 7130 6722 7845 -139 -1964 665 C ATOM 42 OG SER A 172 59.390 98.788 -27.196 1.00 51.75 O ANISOU 42 OG SER A 172 6364 6015 7284 -222 -2042 731 O ATOM 43 N LEU A 173 58.196 98.068 -30.531 1.00 72.79 N ANISOU 43 N LEU A 173 9270 8499 9887 -227 -2510 676 N ATOM 44 CA LEU A 173 58.217 96.781 -31.210 1.00 77.50 C ANISOU 44 CA LEU A 173 9994 8981 10474 -261 -2718 628 C ATOM 45 C LEU A 173 58.017 96.938 -32.714 1.00 81.78 C ANISOU 45 C LEU A 173 10679 9467 10928 -216 -2849 573 C ATOM 46 O LEU A 173 57.559 97.972 -33.204 1.00 85.21 O ANISOU 46 O LEU A 173 11080 9949 11347 -183 -2826 603 O ATOM 47 CB LEU A 173 57.156 95.832 -30.640 1.00 77.64 C ANISOU 47 CB LEU A 173 9895 8951 10653 -381 -2831 731 C ATOM 48 CG LEU A 173 57.219 95.345 -29.181 1.00 78.68 C ANISOU 48 CG LEU A 173 9892 9116 10886 -442 -2761 800 C ATOM 49 CD1 LEU A 173 58.567 94.697 -28.875 1.00 82.75 C ANISOU 49 CD1 LEU A 173 10529 9603 11310 -402 -2711 693 C ATOM 50 CD2 LEU A 173 56.894 96.401 -28.154 1.00 80.65 C ANISOU 50 CD2 LEU A 173 9957 9489 11197 -432 -2579 893 C ATOM 51 N ASP A 174 58.372 95.883 -33.445 1.00 84.98 N ANISOU 51 N ASP A 174 11253 9766 11271 -210 -2957 485 N ATOM 52 CA ASP A 174 58.257 95.846 -34.892 1.00 86.79 C ANISOU 52 CA ASP A 174 11644 9925 11405 -162 -3055 415 C ATOM 53 C ASP A 174 57.110 94.918 -35.304 1.00 96.61 C ANISOU 53 C ASP A 174 12890 11060 12756 -258 -3220 460 C ATOM 54 O ASP A 174 56.308 94.474 -34.471 1.00 94.23 O ANISOU 54 O ASP A 174 12443 10753 12606 -362 -3246 561 O ATOM 55 CB ASP A 174 59.604 95.444 -35.513 1.00 79.51 C ANISOU 55 CB ASP A 174 10934 8966 10311 -57 -3041 278 C ATOM 56 CG ASP A 174 59.965 93.978 -35.283 1.00 80.53 C ANISOU 56 CG ASP A 174 11151 8994 10455 -88 -3119 232 C ATOM 57 OD1 ASP A 174 59.235 93.250 -34.577 1.00 80.71 O ANISOU 57 OD1 ASP A 174 11072 8973 10621 -196 -3181 307 O ATOM 58 OD2 ASP A 174 61.010 93.550 -35.818 1.00 82.60 O ANISOU 58 OD2 ASP A 174 11587 9218 10577 5 -3111 124 O ATOM 59 N SER A 175 57.048 94.609 -36.601 1.00105.99 N ANISOU 59 N SER A 175 14250 12159 13862 -219 -3331 388 N ATOM 60 CA SER A 175 55.935 93.858 -37.172 1.00113.92 C ANISOU 60 CA SER A 175 15275 13052 14958 -301 -3500 431 C ATOM 61 C SER A 175 55.746 92.479 -36.546 1.00119.53 C ANISOU 61 C SER A 175 15982 13664 15769 -391 -3587 460 C ATOM 62 O SER A 175 54.702 91.857 -36.772 1.00123.30 O ANISOU 62 O SER A 175 16438 14054 16355 -482 -3723 528 O ATOM 63 CB SER A 175 56.140 93.719 -38.680 1.00117.82 C ANISOU 63 CB SER A 175 15987 13459 15321 -221 -3596 330 C ATOM 64 OG SER A 175 57.261 92.899 -38.961 1.00120.32 O ANISOU 64 OG SER A 175 16491 13705 15518 -145 -3603 215 O ATOM 65 N ASN A 176 56.713 91.988 -35.771 1.00118.43 N ANISOU 65 N ASN A 176 15864 13535 15599 -370 -3516 418 N ATOM 66 CA ASN A 176 56.645 90.660 -35.173 1.00113.87 C ANISOU 66 CA ASN A 176 15299 12861 15106 -445 -3594 441 C ATOM 67 C ASN A 176 56.480 90.694 -33.662 1.00103.32 C ANISOU 67 C ASN A 176 13756 11607 13893 -523 -3496 542 C ATOM 68 O ASN A 176 56.516 89.636 -33.026 1.00 99.57 O ANISOU 68 O ASN A 176 13280 11065 13485 -582 -3541 567 O ATOM 69 CB ASN A 176 57.909 89.858 -35.508 1.00115.07 C ANISOU 69 CB ASN A 176 15660 12939 15122 -353 -3604 308 C ATOM 70 CG ASN A 176 58.299 89.952 -36.967 1.00117.97 C ANISOU 70 CG ASN A 176 16239 13246 15336 -244 -3660 198 C ATOM 71 OD1 ASN A 176 59.472 89.808 -37.308 1.00118.36 O ANISOU 71 OD1 ASN A 176 16438 13293 15239 -129 -3607 88 O ATOM 72 ND2 ASN A 176 57.317 90.153 -37.840 1.00119.60 N ANISOU 72 ND2 ASN A 176 16462 13405 15577 -274 -3768 231 N ATOM 73 N GLY A 177 56.308 91.872 -33.069 1.00 97.65 N ANISOU 73 N GLY A 177 12870 11029 13203 -517 -3363 604 N ATOM 74 CA GLY A 177 56.417 91.967 -31.630 1.00 96.32 C ANISOU 74 CA GLY A 177 12531 10947 13120 -559 -3246 679 C ATOM 75 C GLY A 177 57.838 91.874 -31.119 1.00 90.09 C ANISOU 75 C GLY A 177 11812 10190 12228 -486 -3147 586 C ATOM 76 O GLY A 177 58.044 91.576 -29.941 1.00 82.51 O ANISOU 76 O GLY A 177 10750 9265 11334 -527 -3079 633 O ATOM 77 N GLU A 178 58.823 92.100 -31.987 1.00 91.90 N ANISOU 77 N GLU A 178 12216 10408 12295 -376 -3136 460 N ATOM 78 CA GLU A 178 60.234 92.137 -31.631 1.00 94.21 C ANISOU 78 CA GLU A 178 12583 10743 12472 -291 -3035 370 C ATOM 79 C GLU A 178 60.672 93.580 -31.417 1.00 88.89 C ANISOU 79 C GLU A 178 11833 10202 11737 -222 -2889 376 C ATOM 80 O GLU A 178 60.141 94.501 -32.039 1.00 91.22 O ANISOU 80 O GLU A 178 12105 10534 12020 -201 -2884 401 O ATOM 81 CB GLU A 178 61.090 91.498 -32.726 1.00 98.43 C ANISOU 81 CB GLU A 178 13358 11187 12854 -197 -3100 236 C ATOM 82 CG GLU A 178 61.504 90.066 -32.459 1.00105.26 C ANISOU 82 CG GLU A 178 14320 11946 13728 -216 -3173 195 C ATOM 83 CD GLU A 178 62.632 89.619 -33.369 1.00114.07 C ANISOU 83 CD GLU A 178 15666 13007 14670 -87 -3185 58 C ATOM 84 OE1 GLU A 178 62.939 90.356 -34.330 1.00116.50 O ANISOU 84 OE1 GLU A 178 16061 13348 14857 6 -3153 1 O ATOM 85 OE2 GLU A 178 63.216 88.540 -33.122 1.00116.38 O ANISOU 85 OE2 GLU A 178 16050 13226 14943 -73 -3219 11 O ATOM 86 N MET A 179 61.647 93.773 -30.529 1.00 82.50 N ANISOU 86 N MET A 179 10990 9460 10894 -187 -2698 348 N ATOM 87 CA MET A 179 62.163 95.113 -30.278 1.00 79.82 C ANISOU 87 CA MET A 179 10592 9238 10498 -123 -2478 341 C ATOM 88 C MET A 179 62.854 95.642 -31.530 1.00 75.37 C ANISOU 88 C MET A 179 10188 8676 9774 -15 -2460 246 C ATOM 89 O MET A 179 63.703 94.965 -32.114 1.00 74.45 O ANISOU 89 O MET A 179 10232 8507 9548 49 -2502 153 O ATOM 90 CB MET A 179 63.133 95.111 -29.090 1.00 75.02 C ANISOU 90 CB MET A 179 9930 8689 9883 -112 -2297 326 C ATOM 91 CG MET A 179 63.222 96.454 -28.343 1.00 74.85 C ANISOU 91 CG MET A 179 9780 8784 9875 -96 -2089 370 C ATOM 92 SD MET A 179 64.553 96.592 -27.106 1.00 71.32 S ANISOU 92 SD MET A 179 9303 8406 9389 -67 -1878 334 S ATOM 93 CE MET A 179 66.016 96.509 -28.144 1.00 60.31 C ANISOU 93 CE MET A 179 8101 7000 7816 42 -1848 204 C ATOM 94 N ARG A 180 62.474 96.846 -31.955 1.00 72.46 N ANISOU 94 N ARG A 180 9777 8367 9387 12 -2397 275 N ATOM 95 CA ARG A 180 63.114 97.442 -33.117 1.00 72.62 C ANISOU 95 CA ARG A 180 9938 8397 9255 115 -2365 198 C ATOM 96 C ARG A 180 64.596 97.664 -32.848 1.00 82.68 C ANISOU 96 C ARG A 180 11266 9728 10419 193 -2186 126 C ATOM 97 O ARG A 180 65.015 97.950 -31.722 1.00 88.31 O ANISOU 97 O ARG A 180 11874 10504 11178 169 -2039 152 O ATOM 98 CB ARG A 180 62.442 98.766 -33.485 1.00 74.65 C ANISOU 98 CB ARG A 180 10127 8715 9524 126 -2315 251 C ATOM 99 CG ARG A 180 60.935 98.778 -33.270 1.00 80.14 C ANISOU 99 CG ARG A 180 10690 9393 10368 35 -2433 358 C ATOM 100 CD ARG A 180 60.238 99.823 -34.127 1.00 86.38 C ANISOU 100 CD ARG A 180 11475 10207 11137 65 -2455 389 C ATOM 101 NE ARG A 180 60.274 101.163 -33.544 1.00 90.35 N ANISOU 101 NE ARG A 180 11866 10811 11651 87 -2262 434 N ATOM 102 CZ ARG A 180 61.122 102.119 -33.914 1.00 94.31 C ANISOU 102 CZ ARG A 180 12435 11363 12036 168 -2122 383 C ATOM 103 NH1 ARG A 180 62.015 101.882 -34.867 1.00 97.33 N ANISOU 103 NH1 ARG A 180 12985 11717 12279 240 -2140 290 N ATOM 104 NH2 ARG A 180 61.080 103.311 -33.333 1.00 94.00 N ANISOU 104 NH2 ARG A 180 12297 11401 12016 181 -1964 428 N ATOM 105 N SER A 181 65.400 97.492 -33.888 1.00 81.73 N ANISOU 105 N SER A 181 11315 9586 10153 289 -2203 40 N ATOM 106 CA SER A 181 66.768 97.968 -33.834 1.00 82.21 C ANISOU 106 CA SER A 181 11415 9718 10101 372 -2022 -11 C ATOM 107 C SER A 181 66.755 99.470 -34.083 1.00 84.26 C ANISOU 107 C SER A 181 11625 10061 10330 398 -1893 21 C ATOM 108 O SER A 181 65.697 100.089 -34.219 1.00 90.24 O ANISOU 108 O SER A 181 12313 10820 11155 357 -1939 80 O ATOM 109 CB SER A 181 67.646 97.238 -34.845 1.00 83.17 C ANISOU 109 CB SER A 181 11732 9796 10074 477 -2075 -104 C ATOM 110 OG SER A 181 67.431 95.841 -34.802 1.00 82.54 O ANISOU 110 OG SER A 181 11724 9616 10022 453 -2237 -134 O ATOM 111 N ARG A 182 67.939 100.071 -34.140 1.00 77.03 N ANISOU 111 N ARG A 182 10739 9215 9316 467 -1733 -11 N ATOM 112 CA ARG A 182 68.099 101.498 -34.405 1.00 72.41 C ANISOU 112 CA ARG A 182 10121 8703 8689 496 -1606 17 C ATOM 113 C ARG A 182 67.386 102.384 -33.386 1.00 64.56 C ANISOU 113 C ARG A 182 8964 7751 7817 417 -1532 95 C ATOM 114 O ARG A 182 67.274 103.596 -33.604 1.00 64.03 O ANISOU 114 O ARG A 182 8869 7729 7730 433 -1452 126 O ATOM 115 CB ARG A 182 67.625 101.871 -35.819 1.00 75.70 C ANISOU 115 CB ARG A 182 10644 9094 9025 552 -1695 4 C ATOM 116 CG ARG A 182 68.512 101.363 -36.950 1.00 81.56 C ANISOU 116 CG ARG A 182 11564 9819 9608 662 -1721 -71 C ATOM 117 CD ARG A 182 69.999 101.542 -36.642 1.00 83.79 C ANISOU 117 CD ARG A 182 11853 10174 9809 720 -1546 -96 C ATOM 118 NE ARG A 182 70.633 100.279 -36.275 1.00 81.44 N ANISOU 118 NE ARG A 182 11602 9843 9497 738 -1577 -145 N ATOM 119 CZ ARG A 182 71.055 99.376 -37.156 1.00 79.47 C ANISOU 119 CZ ARG A 182 11513 9547 9136 829 -1660 -211 C ATOM 120 NH1 ARG A 182 70.907 99.606 -38.455 1.00 84.11 N ANISOU 120 NH1 ARG A 182 12228 10118 9614 910 -1719 -235 N ATOM 121 NH2 ARG A 182 71.615 98.241 -36.740 1.00 65.18 N ANISOU 121 NH2 ARG A 182 9743 7704 7320 846 -1687 -254 N ATOM 122 N LEU A 183 66.893 101.825 -32.283 1.00 58.63 N ANISOU 122 N LEU A 183 8108 6983 7185 340 -1557 131 N ATOM 123 CA LEU A 183 66.350 102.657 -31.217 1.00 58.18 C ANISOU 123 CA LEU A 183 7902 6974 7229 284 -1464 204 C ATOM 124 C LEU A 183 67.470 103.451 -30.546 1.00 47.96 C ANISOU 124 C LEU A 183 6583 5749 5890 306 -1278 194 C ATOM 125 O LEU A 183 68.613 102.997 -30.450 1.00 49.50 O ANISOU 125 O LEU A 183 6830 5955 6021 335 -1225 143 O ATOM 126 CB LEU A 183 65.621 101.805 -30.178 1.00 56.85 C ANISOU 126 CB LEU A 183 7632 6777 7192 203 -1528 251 C ATOM 127 CG LEU A 183 64.237 101.267 -30.540 1.00 66.54 C ANISOU 127 CG LEU A 183 8827 7946 8508 152 -1704 301 C ATOM 128 CD1 LEU A 183 63.817 100.201 -29.545 1.00 70.92 C ANISOU 128 CD1 LEU A 183 9299 8470 9178 75 -1765 341 C ATOM 129 CD2 LEU A 183 63.220 102.386 -30.575 1.00 71.11 C ANISOU 129 CD2 LEU A 183 9314 8563 9143 142 -1682 377 C ATOM 130 N SER A 184 67.139 104.652 -30.091 1.00 45.74 N ANISOU 130 N SER A 184 6223 5513 5642 293 -1183 244 N ATOM 131 CA SER A 184 68.103 105.506 -29.415 1.00 47.06 C ANISOU 131 CA SER A 184 6367 5737 5776 303 -1021 242 C ATOM 132 C SER A 184 67.819 105.561 -27.918 1.00 45.80 C ANISOU 132 C SER A 184 6091 5596 5716 248 -958 287 C ATOM 133 O SER A 184 66.687 105.361 -27.467 1.00 48.34 O ANISOU 133 O SER A 184 6332 5902 6133 210 -1015 340 O ATOM 134 CB SER A 184 68.099 106.925 -29.991 1.00 45.21 C ANISOU 134 CB SER A 184 6154 5535 5490 338 -952 262 C ATOM 135 OG SER A 184 67.042 107.700 -29.456 1.00 49.51 O ANISOU 135 OG SER A 184 6610 6086 6115 311 -939 325 O ATOM 136 N LEU A 185 68.877 105.838 -27.161 1.00 45.06 N ANISOU 136 N LEU A 185 5989 5538 5595 248 -840 270 N ATOM 137 CA LEU A 185 68.765 105.997 -25.718 1.00 43.52 C ANISOU 137 CA LEU A 185 5701 5361 5473 207 -767 306 C ATOM 138 C LEU A 185 67.741 107.069 -25.345 1.00 35.47 C ANISOU 138 C LEU A 185 4614 4356 4505 203 -733 370 C ATOM 139 O LEU A 185 66.844 106.821 -24.529 1.00 42.93 O ANISOU 139 O LEU A 185 5472 5299 5539 174 -749 421 O ATOM 140 CB LEU A 185 70.144 106.322 -25.129 1.00 41.54 C ANISOU 140 CB LEU A 185 5469 5146 5170 212 -650 276 C ATOM 141 CG LEU A 185 70.155 106.445 -23.602 1.00 37.88 C ANISOU 141 CG LEU A 185 4927 4698 4768 175 -576 305 C ATOM 142 CD1 LEU A 185 69.745 105.137 -22.962 1.00 27.50 C ANISOU 142 CD1 LEU A 185 3564 3359 3524 141 -642 312 C ATOM 143 CD2 LEU A 185 71.505 106.895 -23.091 1.00 32.25 C ANISOU 143 CD2 LEU A 185 4236 4016 4002 176 -473 279 C ATOM 144 N SER A 186 67.851 108.267 -25.934 1.00 33.57 N ANISOU 144 N SER A 186 4414 4132 4210 236 -684 373 N ATOM 145 CA SER A 186 66.940 109.355 -25.564 1.00 38.60 C ANISOU 145 CA SER A 186 4998 4780 4887 245 -645 431 C ATOM 146 C SER A 186 65.474 109.046 -25.879 1.00 40.78 C ANISOU 146 C SER A 186 5216 5041 5239 240 -746 483 C ATOM 147 O SER A 186 64.579 109.513 -25.160 1.00 39.94 O ANISOU 147 O SER A 186 5028 4949 5198 241 -717 546 O ATOM 148 CB SER A 186 67.353 110.666 -26.235 1.00 41.22 C ANISOU 148 CB SER A 186 5395 5122 5142 282 -585 424 C ATOM 149 OG SER A 186 68.668 111.044 -25.859 1.00 39.53 O ANISOU 149 OG SER A 186 5222 4927 4873 277 -492 392 O ATOM 150 N GLU A 187 65.194 108.266 -26.924 1.00 41.58 N ANISOU 150 N GLU A 187 5356 5112 5332 238 -867 464 N ATOM 151 CA GLU A 187 63.818 107.814 -27.131 1.00 48.74 C ANISOU 151 CA GLU A 187 6195 5999 6324 217 -982 522 C ATOM 152 C GLU A 187 63.307 107.076 -25.902 1.00 40.94 C ANISOU 152 C GLU A 187 5099 5018 5440 170 -983 572 C ATOM 153 O GLU A 187 62.214 107.363 -25.402 1.00 41.92 O ANISOU 153 O GLU A 187 5122 5161 5646 164 -984 653 O ATOM 154 CB GLU A 187 63.715 106.905 -28.354 1.00 56.40 C ANISOU 154 CB GLU A 187 7240 6923 7267 215 -1129 485 C ATOM 155 CG GLU A 187 63.975 107.558 -29.687 1.00 63.73 C ANISOU 155 CG GLU A 187 8273 7845 8097 267 -1148 449 C ATOM 156 CD GLU A 187 63.872 106.549 -30.827 1.00 70.29 C ANISOU 156 CD GLU A 187 9191 8623 8894 271 -1302 408 C ATOM 157 OE1 GLU A 187 62.765 105.996 -31.016 1.00 74.32 O ANISOU 157 OE1 GLU A 187 9656 9099 9481 237 -1434 450 O ATOM 158 OE2 GLU A 187 64.894 106.287 -31.507 1.00 66.12 O ANISOU 158 OE2 GLU A 187 8776 8086 8262 311 -1295 338 O ATOM 159 N VAL A 188 64.092 106.124 -25.391 1.00 41.05 N ANISOU 159 N VAL A 188 5129 5018 5450 142 -979 531 N ATOM 160 CA VAL A 188 63.659 105.383 -24.207 1.00 36.58 C ANISOU 160 CA VAL A 188 4463 4458 4978 96 -979 582 C ATOM 161 C VAL A 188 63.551 106.317 -23.011 1.00 36.25 C ANISOU 161 C VAL A 188 4352 4464 4957 114 -840 627 C ATOM 162 O VAL A 188 62.566 106.279 -22.261 1.00 41.10 O ANISOU 162 O VAL A 188 4859 5099 5658 102 -834 710 O ATOM 163 CB VAL A 188 64.612 104.206 -23.921 1.00 44.23 C ANISOU 163 CB VAL A 188 5477 5400 5929 69 -1000 524 C ATOM 164 CG1 VAL A 188 64.178 103.456 -22.665 1.00 36.52 C ANISOU 164 CG1 VAL A 188 4398 4429 5049 20 -995 581 C ATOM 165 CG2 VAL A 188 64.658 103.261 -25.105 1.00 44.68 C ANISOU 165 CG2 VAL A 188 5617 5400 5958 63 -1145 477 C ATOM 166 N LEU A 189 64.549 107.180 -22.820 1.00 43.64 N ANISOU 166 N LEU A 189 5350 5418 5813 147 -729 579 N ATOM 167 CA LEU A 189 64.510 108.105 -21.692 1.00 43.25 C ANISOU 167 CA LEU A 189 5259 5403 5770 169 -605 613 C ATOM 168 C LEU A 189 63.333 109.065 -21.803 1.00 45.20 C ANISOU 168 C LEU A 189 5455 5669 6050 208 -594 683 C ATOM 169 O LEU A 189 62.660 109.342 -20.805 1.00 42.72 O ANISOU 169 O LEU A 189 5062 5382 5787 224 -536 748 O ATOM 170 CB LEU A 189 65.823 108.878 -21.595 1.00 32.25 C ANISOU 170 CB LEU A 189 3953 4015 4284 189 -510 550 C ATOM 171 CG LEU A 189 67.060 108.078 -21.165 1.00 34.25 C ANISOU 171 CG LEU A 189 4240 4264 4508 159 -491 493 C ATOM 172 CD1 LEU A 189 68.338 108.864 -21.417 1.00 30.08 C ANISOU 172 CD1 LEU A 189 3796 3743 3890 174 -420 440 C ATOM 173 CD2 LEU A 189 66.979 107.629 -19.703 1.00 35.48 C ANISOU 173 CD2 LEU A 189 4329 4433 4719 138 -443 522 C ATOM 174 N ASP A 190 63.066 109.584 -23.004 1.00 42.43 N ANISOU 174 N ASP A 190 5150 5306 5666 230 -645 674 N ATOM 175 CA ASP A 190 61.966 110.534 -23.152 1.00 43.08 C ANISOU 175 CA ASP A 190 5186 5406 5776 273 -635 742 C ATOM 176 C ASP A 190 60.614 109.858 -23.001 1.00 45.17 C ANISOU 176 C ASP A 190 5329 5683 6150 253 -715 831 C ATOM 177 O ASP A 190 59.656 110.494 -22.539 1.00 43.35 O ANISOU 177 O ASP A 190 5020 5487 5965 292 -674 910 O ATOM 178 CB ASP A 190 62.039 111.245 -24.508 1.00 48.30 C ANISOU 178 CB ASP A 190 5930 6050 6372 302 -674 711 C ATOM 179 CG ASP A 190 63.221 112.204 -24.613 1.00 47.02 C ANISOU 179 CG ASP A 190 5871 5884 6109 327 -581 651 C ATOM 180 OD1 ASP A 190 63.679 112.474 -25.747 1.00 48.27 O ANISOU 180 OD1 ASP A 190 6113 6027 6200 338 -613 610 O ATOM 181 OD2 ASP A 190 63.703 112.681 -23.566 1.00 49.77 O ANISOU 181 OD2 ASP A 190 6220 6244 6446 335 -480 647 O ATOM 182 N SER A 191 60.530 108.567 -23.349 1.00 41.19 N ANISOU 182 N SER A 191 4809 5153 5690 195 -830 825 N ATOM 183 CA SER A 191 59.248 107.874 -23.430 1.00 44.47 C ANISOU 183 CA SER A 191 5113 5570 6213 161 -937 914 C ATOM 184 C SER A 191 58.576 107.732 -22.075 1.00 53.51 C ANISOU 184 C SER A 191 6128 6760 7444 158 -869 1008 C ATOM 185 O SER A 191 57.344 107.649 -22.001 1.00 55.47 O ANISOU 185 O SER A 191 6258 7034 7783 153 -915 1113 O ATOM 186 CB SER A 191 59.438 106.484 -24.035 1.00 42.19 C ANISOU 186 CB SER A 191 4856 5229 5945 95 -1081 880 C ATOM 187 OG SER A 191 59.793 105.534 -23.027 1.00 44.25 O ANISOU 187 OG SER A 191 5078 5487 6246 50 -1062 883 O ATOM 188 N GLY A 192 59.357 107.675 -20.999 1.00 49.19 N ANISOU 188 N GLY A 192 5594 6225 6870 161 -764 979 N ATOM 189 CA GLY A 192 58.808 107.312 -19.712 1.00 43.92 C ANISOU 189 CA GLY A 192 4812 5598 6279 155 -708 1064 C ATOM 190 C GLY A 192 58.661 105.827 -19.490 1.00 45.29 C ANISOU 190 C GLY A 192 4928 5748 6531 74 -805 1092 C ATOM 191 O GLY A 192 58.173 105.420 -18.427 1.00 48.57 O ANISOU 191 O GLY A 192 5240 6198 7015 63 -764 1175 O ATOM 192 N ASP A 193 59.079 104.998 -20.445 1.00 41.86 N ANISOU 192 N ASP A 193 4564 5256 6083 23 -931 1028 N ATOM 193 CA ASP A 193 58.935 103.556 -20.333 1.00 44.06 C ANISOU 193 CA ASP A 193 4808 5499 6436 -56 -1043 1051 C ATOM 194 C ASP A 193 60.247 102.850 -19.970 1.00 45.02 C ANISOU 194 C ASP A 193 5019 5587 6498 -76 -1019 955 C ATOM 195 O ASP A 193 60.353 101.629 -20.142 1.00 46.62 O ANISOU 195 O ASP A 193 5235 5740 6736 -136 -1129 943 O ATOM 196 CB ASP A 193 58.363 102.993 -21.635 1.00 45.94 C ANISOU 196 CB ASP A 193 5065 5684 6706 -98 -1224 1054 C ATOM 197 CG ASP A 193 57.009 103.620 -22.004 1.00 56.31 C ANISOU 197 CG ASP A 193 6276 7032 8089 -84 -1262 1159 C ATOM 198 OD1 ASP A 193 56.846 104.040 -23.172 1.00 53.11 O ANISOU 198 OD1 ASP A 193 5932 6603 7645 -65 -1335 1127 O ATOM 199 OD2 ASP A 193 56.115 103.693 -21.127 1.00 57.84 O ANISOU 199 OD2 ASP A 193 6326 7278 8371 -86 -1216 1278 O ATOM 200 N LEU A 194 61.239 103.586 -19.456 1.00 39.90 N ANISOU 200 N LEU A 194 4433 4963 5764 -28 -883 891 N ATOM 201 CA LEU A 194 62.512 102.960 -19.096 1.00 36.17 C ANISOU 201 CA LEU A 194 4038 4467 5237 -44 -857 807 C ATOM 202 C LEU A 194 62.310 101.791 -18.141 1.00 36.43 C ANISOU 202 C LEU A 194 3999 4493 5350 -98 -884 857 C ATOM 203 O LEU A 194 62.987 100.764 -18.266 1.00 38.20 O ANISOU 203 O LEU A 194 4279 4672 5563 -134 -948 803 O ATOM 204 CB LEU A 194 63.467 103.982 -18.475 1.00 38.38 C ANISOU 204 CB LEU A 194 4371 4781 5433 7 -706 756 C ATOM 205 CG LEU A 194 64.803 103.408 -17.959 1.00 40.91 C ANISOU 205 CG LEU A 194 4755 5087 5702 -7 -668 680 C ATOM 206 CD1 LEU A 194 65.959 104.416 -18.127 1.00 29.97 C ANISOU 206 CD1 LEU A 194 3463 3714 4212 35 -575 603 C ATOM 207 CD2 LEU A 194 64.718 102.927 -16.487 1.00 36.37 C ANISOU 207 CD2 LEU A 194 4106 4534 5178 -25 -608 730 C ATOM 208 N MET A 195 61.403 101.934 -17.163 1.00 32.63 N ANISOU 208 N MET A 195 3396 4057 4945 -99 -830 964 N ATOM 209 CA MET A 195 61.196 100.849 -16.203 1.00 36.82 C ANISOU 209 CA MET A 195 3852 4586 5552 -151 -848 1025 C ATOM 210 C MET A 195 60.750 99.576 -16.902 1.00 35.44 C ANISOU 210 C MET A 195 3666 4349 5451 -228 -1024 1046 C ATOM 211 O MET A 195 61.057 98.478 -16.438 1.00 44.03 O ANISOU 211 O MET A 195 4755 5405 6571 -278 -1068 1045 O ATOM 212 CB MET A 195 60.166 101.245 -15.138 1.00 38.36 C ANISOU 212 CB MET A 195 3910 4848 5818 -129 -762 1154 C ATOM 213 CG MET A 195 60.670 102.242 -14.089 1.00 40.09 C ANISOU 213 CG MET A 195 4148 5117 5965 -55 -589 1136 C ATOM 214 SD MET A 195 62.060 101.595 -13.133 1.00 48.68 S ANISOU 214 SD MET A 195 5312 6186 6999 -72 -532 1056 S ATOM 215 CE MET A 195 61.253 100.233 -12.271 1.00 41.46 C ANISOU 215 CE MET A 195 4269 5277 6206 -138 -583 1177 C ATOM 216 N LYS A 196 60.054 99.704 -18.034 1.00 37.68 N ANISOU 216 N LYS A 196 3950 4610 5757 -239 -1134 1061 N ATOM 217 CA LYS A 196 59.617 98.526 -18.780 1.00 45.55 C ANISOU 217 CA LYS A 196 4955 5535 6819 -313 -1322 1077 C ATOM 218 C LYS A 196 60.784 97.868 -19.507 1.00 46.79 C ANISOU 218 C LYS A 196 5271 5620 6888 -314 -1390 943 C ATOM 219 O LYS A 196 60.850 96.637 -19.599 1.00 48.49 O ANISOU 219 O LYS A 196 5514 5770 7141 -372 -1511 937 O ATOM 220 CB LYS A 196 58.517 98.908 -19.777 1.00 42.28 C ANISOU 220 CB LYS A 196 4498 5116 6450 -321 -1425 1134 C ATOM 221 CG LYS A 196 57.153 99.208 -19.159 1.00 50.57 C ANISOU 221 CG LYS A 196 5369 6230 7616 -336 -1403 1294 C ATOM 222 CD LYS A 196 56.104 99.449 -20.263 1.00 61.06 C ANISOU 222 CD LYS A 196 6660 7546 8995 -352 -1533 1349 C ATOM 223 CE LYS A 196 54.698 99.603 -19.706 1.00 65.73 C ANISOU 223 CE LYS A 196 7058 8203 9715 -372 -1529 1524 C ATOM 224 NZ LYS A 196 54.528 100.908 -19.012 1.00 70.30 N ANISOU 224 NZ LYS A 196 7576 8875 10258 -275 -1338 1561 N ATOM 225 N PHE A 197 61.708 98.672 -20.042 1.00 38.59 N ANISOU 225 N PHE A 197 4339 4592 5731 -247 -1316 840 N ATOM 226 CA PHE A 197 62.899 98.105 -20.668 1.00 38.46 C ANISOU 226 CA PHE A 197 4467 4523 5622 -230 -1356 720 C ATOM 227 C PHE A 197 63.832 97.479 -19.638 1.00 44.18 C ANISOU 227 C PHE A 197 5203 5249 6332 -238 -1285 688 C ATOM 228 O PHE A 197 64.506 96.487 -19.933 1.00 38.12 O ANISOU 228 O PHE A 197 4523 4425 5535 -249 -1361 624 O ATOM 229 CB PHE A 197 63.658 99.176 -21.441 1.00 41.65 C ANISOU 229 CB PHE A 197 4966 4951 5907 -157 -1280 636 C ATOM 230 CG PHE A 197 62.995 99.599 -22.719 1.00 43.85 C ANISOU 230 CG PHE A 197 5279 5210 6173 -142 -1374 638 C ATOM 231 CD1 PHE A 197 61.855 100.377 -22.692 1.00 39.32 C ANISOU 231 CD1 PHE A 197 4605 4672 5661 -144 -1366 727 C ATOM 232 CD2 PHE A 197 63.541 99.254 -23.947 1.00 43.72 C ANISOU 232 CD2 PHE A 197 5397 5141 6073 -115 -1464 551 C ATOM 233 CE1 PHE A 197 61.250 100.786 -23.876 1.00 49.89 C ANISOU 233 CE1 PHE A 197 5975 5994 6987 -129 -1455 730 C ATOM 234 CE2 PHE A 197 62.943 99.658 -25.126 1.00 46.98 C ANISOU 234 CE2 PHE A 197 5850 5535 6467 -97 -1552 552 C ATOM 235 CZ PHE A 197 61.795 100.420 -25.090 1.00 47.17 C ANISOU 235 CZ PHE A 197 5769 5592 6559 -108 -1551 641 C ATOM 236 N ALA A 198 63.914 98.063 -18.438 1.00 46.40 N ANISOU 236 N ALA A 198 5408 5595 6627 -225 -1142 729 N ATOM 237 CA ALA A 198 64.951 97.643 -17.499 1.00 43.73 C ANISOU 237 CA ALA A 198 5096 5264 6256 -222 -1063 687 C ATOM 238 C ALA A 198 64.663 96.269 -16.903 1.00 45.14 C ANISOU 238 C ALA A 198 5233 5400 6518 -287 -1148 734 C ATOM 239 O ALA A 198 65.601 95.570 -16.511 1.00 44.41 O ANISOU 239 O ALA A 198 5196 5285 6392 -289 -1138 679 O ATOM 240 CB ALA A 198 65.126 98.686 -16.392 1.00 37.42 C ANISOU 240 CB ALA A 198 4243 4536 5438 -185 -895 714 C ATOM 241 N VAL A 199 63.391 95.855 -16.833 1.00 46.43 N ANISOU 241 N VAL A 199 5298 5552 6792 -343 -1235 840 N ATOM 242 CA VAL A 199 63.052 94.520 -16.329 1.00 48.53 C ANISOU 242 CA VAL A 199 5523 5769 7146 -417 -1331 897 C ATOM 243 C VAL A 199 62.887 93.501 -17.447 1.00 50.16 C ANISOU 243 C VAL A 199 5810 5878 7370 -460 -1528 864 C ATOM 244 O VAL A 199 62.523 92.350 -17.177 1.00 51.37 O ANISOU 244 O VAL A 199 5941 5975 7604 -531 -1638 914 O ATOM 245 CB VAL A 199 61.786 94.532 -15.436 1.00 37.30 C ANISOU 245 CB VAL A 199 3933 4392 5845 -461 -1312 1052 C ATOM 246 CG1 VAL A 199 62.011 95.386 -14.203 1.00 40.32 C ANISOU 246 CG1 VAL A 199 4256 4863 6201 -409 -1120 1081 C ATOM 247 CG2 VAL A 199 60.557 95.007 -16.207 1.00 35.99 C ANISOU 247 CG2 VAL A 199 3696 4237 5741 -476 -1387 1129 C ATOM 248 N ASP A 200 63.149 93.886 -18.691 1.00 54.70 N ANISOU 248 N ASP A 200 6487 6427 7868 -419 -1579 783 N ATOM 249 CA ASP A 200 63.108 92.976 -19.826 1.00 53.72 C ANISOU 249 CA ASP A 200 6471 6204 7734 -442 -1766 734 C ATOM 250 C ASP A 200 64.530 92.620 -20.238 1.00 58.38 C ANISOU 250 C ASP A 200 7219 6762 8202 -380 -1749 598 C ATOM 251 O ASP A 200 65.424 93.474 -20.215 1.00 58.07 O ANISOU 251 O ASP A 200 7216 6782 8068 -309 -1609 534 O ATOM 252 CB ASP A 200 62.366 93.611 -21.006 1.00 54.42 C ANISOU 252 CB ASP A 200 6573 6286 7817 -430 -1845 742 C ATOM 253 CG ASP A 200 62.285 92.687 -22.215 1.00 62.40 C ANISOU 253 CG ASP A 200 7712 7188 8810 -449 -2050 689 C ATOM 254 OD1 ASP A 200 63.064 92.879 -23.180 1.00 56.35 O ANISOU 254 OD1 ASP A 200 7088 6399 7922 -377 -2058 579 O ATOM 255 OD2 ASP A 200 61.441 91.763 -22.197 1.00 67.29 O ANISOU 255 OD2 ASP A 200 8293 7742 9534 -533 -2208 761 O ATOM 256 N LYS A 201 64.733 91.358 -20.628 1.00 52.25 N ANISOU 256 N LYS A 201 6538 5890 7426 -404 -1895 560 N ATOM 257 CA LYS A 201 66.079 90.894 -20.957 1.00 53.09 C ANISOU 257 CA LYS A 201 6790 5966 7417 -336 -1879 439 C ATOM 258 C LYS A 201 66.669 91.681 -22.125 1.00 44.53 C ANISOU 258 C LYS A 201 5812 4901 6207 -246 -1847 349 C ATOM 259 O LYS A 201 67.776 92.219 -22.031 1.00 51.69 O ANISOU 259 O LYS A 201 6756 5864 7018 -176 -1711 285 O ATOM 260 CB LYS A 201 66.056 89.396 -21.265 1.00 57.58 C ANISOU 260 CB LYS A 201 7455 6416 8007 -371 -2062 416 C ATOM 261 CG LYS A 201 67.423 88.819 -21.607 1.00 60.38 C ANISOU 261 CG LYS A 201 7964 6737 8240 -287 -2050 296 C ATOM 262 CD LYS A 201 67.299 87.518 -22.366 1.00 65.96 C ANISOU 262 CD LYS A 201 8810 7311 8940 -297 -2258 255 C ATOM 263 CE LYS A 201 68.470 87.318 -23.305 1.00 71.71 C ANISOU 263 CE LYS A 201 9719 8014 9513 -178 -2257 126 C ATOM 264 NZ LYS A 201 68.167 86.332 -24.379 1.00 75.01 N ANISOU 264 NZ LYS A 201 10299 8300 9903 -168 -2474 79 N ATOM 265 N THR A 202 65.934 91.774 -23.232 1.00 49.77 N ANISOU 265 N THR A 202 6520 5520 6869 -249 -1972 352 N ATOM 266 CA THR A 202 66.450 92.463 -24.413 1.00 50.68 C ANISOU 266 CA THR A 202 6745 5650 6861 -162 -1951 271 C ATOM 267 C THR A 202 66.549 93.971 -24.190 1.00 47.17 C ANISOU 267 C THR A 202 6219 5314 6392 -129 -1778 292 C ATOM 268 O THR A 202 67.530 94.601 -24.602 1.00 52.62 O ANISOU 268 O THR A 202 6977 6047 6969 -51 -1675 224 O ATOM 269 CB THR A 202 65.566 92.149 -25.622 1.00 56.47 C ANISOU 269 CB THR A 202 7550 6303 7602 -177 -2143 273 C ATOM 270 OG1 THR A 202 65.176 90.768 -25.583 1.00 54.85 O ANISOU 270 OG1 THR A 202 7389 5990 7460 -238 -2321 285 O ATOM 271 CG2 THR A 202 66.305 92.438 -26.923 1.00 61.76 C ANISOU 271 CG2 THR A 202 8383 6963 8122 -72 -2150 170 C ATOM 272 N GLY A 203 65.548 94.567 -23.545 1.00 44.99 N ANISOU 272 N GLY A 203 5798 5079 6215 -185 -1743 391 N ATOM 273 CA GLY A 203 65.604 95.996 -23.285 1.00 40.47 C ANISOU 273 CA GLY A 203 5160 4599 5619 -151 -1585 411 C ATOM 274 C GLY A 203 66.729 96.370 -22.340 1.00 37.63 C ANISOU 274 C GLY A 203 4786 4300 5211 -119 -1415 378 C ATOM 275 O GLY A 203 67.391 97.396 -22.523 1.00 40.78 O ANISOU 275 O GLY A 203 5210 4753 5531 -65 -1298 342 O ATOM 276 N CYS A 204 66.957 95.555 -21.310 1.00 40.43 N ANISOU 276 N CYS A 204 5103 4645 5616 -157 -1404 396 N ATOM 277 CA CYS A 204 68.024 95.878 -20.367 1.00 45.35 C ANISOU 277 CA CYS A 204 5714 5322 6196 -131 -1253 368 C ATOM 278 C CYS A 204 69.390 95.712 -21.014 1.00 46.11 C ANISOU 278 C CYS A 204 5934 5414 6174 -64 -1229 265 C ATOM 279 O CYS A 204 70.309 96.491 -20.739 1.00 42.07 O ANISOU 279 O CYS A 204 5426 4961 5597 -24 -1098 236 O ATOM 280 CB CYS A 204 67.918 95.023 -19.106 1.00 49.58 C ANISOU 280 CB CYS A 204 6180 5848 6811 -184 -1250 415 C ATOM 281 SG CYS A 204 68.751 95.776 -17.667 1.00 53.33 S ANISOU 281 SG CYS A 204 6595 6406 7264 -165 -1055 421 S ATOM 282 N GLN A 205 69.534 94.713 -21.891 1.00 46.11 N ANISOU 282 N GLN A 205 6038 5343 6141 -47 -1358 215 N ATOM 283 CA GLN A 205 70.767 94.575 -22.661 1.00 41.43 C ANISOU 283 CA GLN A 205 5567 4750 5424 35 -1336 123 C ATOM 284 C GLN A 205 71.023 95.810 -23.506 1.00 44.47 C ANISOU 284 C GLN A 205 5981 5187 5728 91 -1263 102 C ATOM 285 O GLN A 205 72.161 96.285 -23.598 1.00 48.74 O ANISOU 285 O GLN A 205 6556 5781 6184 147 -1155 61 O ATOM 286 CB GLN A 205 70.696 93.343 -23.561 1.00 43.97 C ANISOU 286 CB GLN A 205 6011 4976 5718 55 -1501 75 C ATOM 287 CG GLN A 205 71.091 92.029 -22.915 1.00 50.68 C ANISOU 287 CG GLN A 205 6887 5773 6595 38 -1554 59 C ATOM 288 CD GLN A 205 71.107 90.886 -23.929 1.00 57.41 C ANISOU 288 CD GLN A 205 7890 6523 7399 74 -1721 0 C ATOM 289 OE1 GLN A 205 70.769 91.077 -25.098 1.00 53.21 O ANISOU 289 OE1 GLN A 205 7441 5962 6816 110 -1801 -27 O ATOM 290 NE2 GLN A 205 71.502 89.701 -23.484 1.00 63.59 N ANISOU 290 NE2 GLN A 205 8719 7248 8193 70 -1779 -22 N ATOM 291 N PHE A 206 69.975 96.333 -24.152 1.00 40.41 N ANISOU 291 N PHE A 206 5452 4661 5243 74 -1324 137 N ATOM 292 CA PHE A 206 70.118 97.571 -24.912 1.00 45.93 C ANISOU 292 CA PHE A 206 6172 5407 5871 122 -1255 127 C ATOM 293 C PHE A 206 70.540 98.725 -24.011 1.00 39.74 C ANISOU 293 C PHE A 206 5303 4704 5091 116 -1088 156 C ATOM 294 O PHE A 206 71.466 99.472 -24.343 1.00 39.82 O ANISOU 294 O PHE A 206 5352 4761 5017 165 -992 124 O ATOM 295 CB PHE A 206 68.809 97.906 -25.631 1.00 48.11 C ANISOU 295 CB PHE A 206 6434 5656 6192 99 -1355 170 C ATOM 296 CG PHE A 206 68.773 99.293 -26.207 1.00 46.67 C ANISOU 296 CG PHE A 206 6250 5525 5957 136 -1276 177 C ATOM 297 CD1 PHE A 206 69.527 99.614 -27.320 1.00 53.15 C ANISOU 297 CD1 PHE A 206 7181 6354 6658 211 -1260 118 C ATOM 298 CD2 PHE A 206 67.974 100.270 -25.642 1.00 48.94 C ANISOU 298 CD2 PHE A 206 6430 5851 6313 102 -1217 247 C ATOM 299 CE1 PHE A 206 69.491 100.898 -27.856 1.00 55.13 C ANISOU 299 CE1 PHE A 206 7434 6651 6864 242 -1190 131 C ATOM 300 CE2 PHE A 206 67.932 101.551 -26.168 1.00 52.71 C ANISOU 300 CE2 PHE A 206 6914 6369 6743 138 -1149 255 C ATOM 301 CZ PHE A 206 68.690 101.867 -27.279 1.00 53.03 C ANISOU 301 CZ PHE A 206 7064 6416 6670 203 -1138 198 C ATOM 302 N LEU A 207 69.864 98.893 -22.865 1.00 38.04 N ANISOU 302 N LEU A 207 4977 4504 4974 57 -1054 222 N ATOM 303 CA LEU A 207 70.193 100.012 -21.977 1.00 43.46 C ANISOU 303 CA LEU A 207 5597 5255 5659 56 -907 247 C ATOM 304 C LEU A 207 71.599 99.859 -21.412 1.00 38.11 C ANISOU 304 C LEU A 207 4946 4607 4927 76 -818 202 C ATOM 305 O LEU A 207 72.370 100.825 -21.379 1.00 37.42 O ANISOU 305 O LEU A 207 4868 4567 4783 101 -714 189 O ATOM 306 CB LEU A 207 69.168 100.126 -20.842 1.00 34.78 C ANISOU 306 CB LEU A 207 4383 4166 4667 4 -890 328 C ATOM 307 CG LEU A 207 67.750 100.585 -21.194 1.00 40.12 C ANISOU 307 CG LEU A 207 5001 4837 5407 -13 -946 395 C ATOM 308 CD1 LEU A 207 66.823 100.574 -19.969 1.00 39.76 C ANISOU 308 CD1 LEU A 207 4832 4811 5463 -55 -916 485 C ATOM 309 CD2 LEU A 207 67.738 101.956 -21.872 1.00 33.09 C ANISOU 309 CD2 LEU A 207 4136 3979 4457 31 -886 389 C ATOM 310 N GLU A 208 71.951 98.643 -20.981 1.00 37.17 N ANISOU 310 N GLU A 208 4838 4457 4827 62 -863 182 N ATOM 311 CA GLU A 208 73.289 98.370 -20.472 1.00 39.41 C ANISOU 311 CA GLU A 208 5145 4768 5062 84 -790 142 C ATOM 312 C GLU A 208 74.350 98.791 -21.473 1.00 42.01 C ANISOU 312 C GLU A 208 5554 5126 5282 150 -749 90 C ATOM 313 O GLU A 208 75.345 99.423 -21.104 1.00 42.01 O ANISOU 313 O GLU A 208 5542 5180 5240 164 -643 83 O ATOM 314 CB GLU A 208 73.438 96.881 -20.153 1.00 48.30 C ANISOU 314 CB GLU A 208 6293 5844 6215 71 -871 123 C ATOM 315 CG GLU A 208 73.134 96.514 -18.712 1.00 64.90 C ANISOU 315 CG GLU A 208 8310 7948 8403 14 -845 170 C ATOM 316 CD GLU A 208 74.247 96.923 -17.766 1.00 74.06 C ANISOU 316 CD GLU A 208 9447 9162 9531 23 -723 158 C ATOM 317 OE1 GLU A 208 75.144 96.089 -17.493 1.00 74.67 O ANISOU 317 OE1 GLU A 208 9555 9232 9584 39 -725 123 O ATOM 318 OE2 GLU A 208 74.223 98.085 -17.306 1.00 73.69 O ANISOU 318 OE2 GLU A 208 9355 9161 9483 16 -630 185 O ATOM 319 N LYS A 209 74.148 98.458 -22.749 1.00 38.23 N ANISOU 319 N LYS A 209 5156 4614 4754 192 -834 58 N ATOM 320 CA LYS A 209 75.113 98.850 -23.768 1.00 38.12 C ANISOU 320 CA LYS A 209 5220 4634 4630 266 -791 17 C ATOM 321 C LYS A 209 75.029 100.344 -24.060 1.00 42.23 C ANISOU 321 C LYS A 209 5715 5203 5128 266 -709 47 C ATOM 322 O LYS A 209 76.060 101.019 -24.167 1.00 42.71 O ANISOU 322 O LYS A 209 5782 5319 5126 295 -612 42 O ATOM 323 CB LYS A 209 74.892 98.034 -25.044 1.00 38.83 C ANISOU 323 CB LYS A 209 5420 4669 4663 321 -910 -26 C ATOM 324 CG LYS A 209 75.910 98.335 -26.142 1.00 49.04 C ANISOU 324 CG LYS A 209 6800 6002 5830 414 -861 -65 C ATOM 325 CD LYS A 209 76.104 97.162 -27.104 1.00 57.17 C ANISOU 325 CD LYS A 209 7957 6977 6787 491 -966 -123 C ATOM 326 CE LYS A 209 76.681 95.935 -26.384 1.00 68.94 C ANISOU 326 CE LYS A 209 9458 8442 8294 495 -988 -151 C ATOM 327 NZ LYS A 209 78.001 96.188 -25.727 1.00 72.34 N ANISOU 327 NZ LYS A 209 9841 8952 8695 517 -851 -147 N ATOM 328 N ALA A 210 73.811 100.879 -24.169 1.00 34.70 N ANISOU 328 N ALA A 210 4728 4229 4228 233 -750 84 N ATOM 329 CA ALA A 210 73.639 102.281 -24.535 1.00 40.57 C ANISOU 329 CA ALA A 210 5460 5008 4948 240 -685 111 C ATOM 330 C ALA A 210 74.277 103.227 -23.517 1.00 40.12 C ANISOU 330 C ALA A 210 5344 5001 4900 214 -559 136 C ATOM 331 O ALA A 210 74.847 104.260 -23.894 1.00 42.66 O ANISOU 331 O ALA A 210 5684 5359 5167 233 -486 141 O ATOM 332 CB ALA A 210 72.152 102.588 -24.693 1.00 40.92 C ANISOU 332 CB ALA A 210 5468 5021 5059 211 -755 153 C ATOM 333 N VAL A 211 74.195 102.908 -22.218 1.00 35.34 N ANISOU 333 N VAL A 211 4674 4394 4362 169 -535 154 N ATOM 334 CA VAL A 211 74.765 103.827 -21.228 1.00 36.92 C ANISOU 334 CA VAL A 211 4831 4631 4565 146 -428 175 C ATOM 335 C VAL A 211 76.276 103.727 -21.135 1.00 36.79 C ANISOU 335 C VAL A 211 4837 4651 4490 161 -367 147 C ATOM 336 O VAL A 211 76.892 104.493 -20.383 1.00 36.30 O ANISOU 336 O VAL A 211 4749 4618 4426 138 -287 163 O ATOM 337 CB VAL A 211 74.170 103.635 -19.822 1.00 35.76 C ANISOU 337 CB VAL A 211 4612 4473 4500 101 -415 208 C ATOM 338 CG1 VAL A 211 72.652 103.713 -19.893 1.00 31.57 C ANISOU 338 CG1 VAL A 211 4043 3917 4035 88 -471 252 C ATOM 339 CG2 VAL A 211 74.665 102.324 -19.198 1.00 32.06 C ANISOU 339 CG2 VAL A 211 4135 3993 4052 88 -442 187 C ATOM 340 N LYS A 212 76.901 102.892 -21.952 1.00 37.95 N ANISOU 340 N LYS A 212 5035 4798 4586 204 -404 108 N ATOM 341 CA LYS A 212 78.380 102.822 -21.959 1.00 43.39 C ANISOU 341 CA LYS A 212 5740 5534 5211 233 -341 92 C ATOM 342 C LYS A 212 78.929 103.821 -22.973 1.00 47.02 C ANISOU 342 C LYS A 212 6231 6035 5600 265 -286 105 C ATOM 343 O LYS A 212 80.129 103.965 -23.066 1.00 42.58 O ANISOU 343 O LYS A 212 5666 5523 4989 282 -221 110 O ATOM 344 CB LYS A 212 78.865 101.446 -22.402 1.00 46.55 C ANISOU 344 CB LYS A 212 6190 5920 5577 284 -397 48 C ATOM 345 CG LYS A 212 78.446 100.283 -21.529 1.00 49.96 C ANISOU 345 CG LYS A 212 6592 6320 6070 254 -434 38 C ATOM 346 CD LYS A 212 79.559 99.320 -21.286 1.00 59.71 C ANISOU 346 CD LYS A 212 7871 7566 7252 312 -443 -1 C ATOM 347 CE LYS A 212 79.156 97.871 -21.456 1.00 70.96 C ANISOU 347 CE LYS A 212 9322 8923 8716 310 -545 -27 C ATOM 348 NZ LYS A 212 78.945 97.185 -20.161 1.00 72.81 N ANISOU 348 NZ LYS A 212 9482 9144 9037 240 -536 -2 N ATOM 349 N GLY A 213 78.053 104.523 -23.673 1.00 46.21 N ANISOU 349 N GLY A 213 6153 5915 5490 272 -312 117 N ATOM 350 CA GLY A 213 78.498 105.486 -24.684 1.00 39.81 C ANISOU 350 CA GLY A 213 5378 5139 4610 303 -267 134 C ATOM 351 C GLY A 213 78.779 106.852 -24.117 1.00 43.88 C ANISOU 351 C GLY A 213 5853 5677 5141 254 -187 177 C ATOM 352 O GLY A 213 78.783 107.015 -22.917 1.00 45.89 O ANISOU 352 O GLY A 213 6059 5928 5449 203 -158 188 O ATOM 353 N SER A 214 79.024 107.808 -24.998 1.00 49.17 N ANISOU 353 N SER A 214 6554 6368 5760 273 -156 201 N ATOM 354 CA SER A 214 79.275 109.214 -24.609 1.00 55.20 C ANISOU 354 CA SER A 214 7300 7143 6532 229 -93 244 C ATOM 355 C SER A 214 77.935 109.886 -24.310 1.00 45.74 C ANISOU 355 C SER A 214 6098 5897 5383 207 -122 256 C ATOM 356 O SER A 214 77.280 110.250 -25.241 1.00 54.85 O ANISOU 356 O SER A 214 7288 7037 6516 236 -153 261 O ATOM 357 CB SER A 214 79.965 109.907 -25.733 1.00 63.34 C ANISOU 357 CB SER A 214 8367 8215 7486 259 -51 273 C ATOM 358 OG SER A 214 79.129 109.963 -26.873 1.00 71.80 O ANISOU 358 OG SER A 214 9455 9331 8494 317 -40 260 O ATOM 359 N LEU A 215 77.572 110.066 -23.056 1.00 35.74 N ANISOU 359 N LEU A 215 4792 4608 4179 163 -110 263 N ATOM 360 CA LEU A 215 76.250 110.657 -22.741 1.00 34.81 C ANISOU 360 CA LEU A 215 4667 4453 4109 156 -130 280 C ATOM 361 C LEU A 215 76.324 112.171 -22.571 1.00 39.02 C ANISOU 361 C LEU A 215 5222 4978 4628 137 -80 314 C ATOM 362 O LEU A 215 77.276 112.649 -21.990 1.00 31.88 O ANISOU 362 O LEU A 215 4317 4084 3711 103 -31 325 O ATOM 363 CB LEU A 215 75.696 110.032 -21.459 1.00 27.82 C ANISOU 363 CB LEU A 215 3731 3547 3293 132 -141 277 C ATOM 364 CG LEU A 215 75.679 108.511 -21.387 1.00 33.94 C ANISOU 364 CG LEU A 215 4482 4323 4089 135 -188 248 C ATOM 365 CD1 LEU A 215 75.626 108.029 -19.958 1.00 30.71 C ANISOU 365 CD1 LEU A 215 4025 3906 3738 103 -174 252 C ATOM 366 CD2 LEU A 215 74.535 107.947 -22.177 1.00 23.56 C ANISOU 366 CD2 LEU A 215 3175 2985 2792 161 -270 243 C ATOM 367 N THR A 216 75.323 112.872 -23.089 1.00 39.18 N ANISOU 367 N THR A 216 5263 4975 4650 160 -99 332 N ATOM 368 CA THR A 216 75.213 114.297 -22.812 1.00 36.21 C ANISOU 368 CA THR A 216 4915 4577 4268 148 -60 363 C ATOM 369 C THR A 216 74.796 114.511 -21.365 1.00 34.80 C ANISOU 369 C THR A 216 4711 4372 4138 130 -39 369 C ATOM 370 O THR A 216 74.329 113.589 -20.683 1.00 34.51 O ANISOU 370 O THR A 216 4629 4337 4146 131 -58 357 O ATOM 371 CB THR A 216 74.192 114.978 -23.724 1.00 35.18 C ANISOU 371 CB THR A 216 4813 4428 4127 185 -87 382 C ATOM 372 OG1 THR A 216 72.881 114.544 -23.357 1.00 36.40 O ANISOU 372 OG1 THR A 216 4928 4566 4337 206 -126 385 O ATOM 373 CG2 THR A 216 74.458 114.668 -25.192 1.00 33.47 C ANISOU 373 CG2 THR A 216 4628 4235 3855 214 -115 375 C ATOM 374 N SER A 217 74.965 115.754 -20.900 1.00 30.29 N ANISOU 374 N SER A 217 4180 3773 3554 116 -3 389 N ATOM 375 CA SER A 217 74.590 116.080 -19.529 1.00 28.08 C ANISOU 375 CA SER A 217 3899 3465 3305 113 19 394 C ATOM 376 C SER A 217 73.114 115.793 -19.277 1.00 32.22 C ANISOU 376 C SER A 217 4386 3982 3873 160 2 406 C ATOM 377 O SER A 217 72.746 115.294 -18.207 1.00 30.15 O ANISOU 377 O SER A 217 4088 3721 3648 164 12 406 O ATOM 378 CB SER A 217 74.920 117.541 -19.233 1.00 29.64 C ANISOU 378 CB SER A 217 4166 3622 3473 100 47 413 C ATOM 379 OG SER A 217 74.104 118.029 -18.190 1.00 37.08 O ANISOU 379 OG SER A 217 5126 4528 4433 131 63 420 O ATOM 380 N TYR A 218 72.253 116.068 -20.261 1.00 31.09 N ANISOU 380 N TYR A 218 4245 3837 3728 196 -26 422 N ATOM 381 CA TYR A 218 70.826 115.837 -20.049 1.00 28.90 C ANISOU 381 CA TYR A 218 3920 3559 3500 238 -46 448 C ATOM 382 C TYR A 218 70.501 114.349 -20.003 1.00 31.76 C ANISOU 382 C TYR A 218 4211 3947 3911 226 -91 440 C ATOM 383 O TYR A 218 69.664 113.923 -19.200 1.00 29.88 O ANISOU 383 O TYR A 218 3915 3713 3726 240 -91 464 O ATOM 384 CB TYR A 218 69.997 116.519 -21.132 1.00 29.99 C ANISOU 384 CB TYR A 218 4079 3690 3628 278 -73 472 C ATOM 385 CG TYR A 218 68.516 116.478 -20.842 1.00 32.61 C ANISOU 385 CG TYR A 218 4354 4024 4013 324 -88 512 C ATOM 386 CD1 TYR A 218 68.007 117.037 -19.684 1.00 34.83 C ANISOU 386 CD1 TYR A 218 4630 4294 4311 358 -38 538 C ATOM 387 CD2 TYR A 218 67.632 115.866 -21.721 1.00 32.67 C ANISOU 387 CD2 TYR A 218 4314 4045 4052 338 -155 529 C ATOM 388 CE1 TYR A 218 66.656 117.000 -19.412 1.00 40.43 C ANISOU 388 CE1 TYR A 218 5277 5017 5069 410 -42 588 C ATOM 389 CE2 TYR A 218 66.277 115.835 -21.467 1.00 40.17 C ANISOU 389 CE2 TYR A 218 5199 5005 5060 377 -172 580 C ATOM 390 CZ TYR A 218 65.796 116.403 -20.307 1.00 43.84 C ANISOU 390 CZ TYR A 218 5647 5469 5543 415 -109 613 C ATOM 391 OH TYR A 218 64.453 116.367 -20.035 1.00 45.18 O ANISOU 391 OH TYR A 218 5740 5658 5769 461 -115 676 O ATOM 392 N GLN A 219 71.149 113.545 -20.856 1.00 29.74 N ANISOU 392 N GLN A 219 3959 3705 3635 205 -130 409 N ATOM 393 CA GLN A 219 70.938 112.097 -20.817 1.00 31.15 C ANISOU 393 CA GLN A 219 4086 3896 3855 192 -182 397 C ATOM 394 C GLN A 219 71.334 111.519 -19.464 1.00 31.45 C ANISOU 394 C GLN A 219 4089 3938 3923 166 -149 391 C ATOM 395 O GLN A 219 70.636 110.652 -18.928 1.00 32.03 O ANISOU 395 O GLN A 219 4102 4013 4054 162 -177 408 O ATOM 396 CB GLN A 219 71.729 111.413 -21.935 1.00 32.59 C ANISOU 396 CB GLN A 219 4302 4088 3993 187 -223 359 C ATOM 397 CG GLN A 219 71.184 111.681 -23.338 1.00 32.07 C ANISOU 397 CG GLN A 219 4270 4016 3898 218 -275 364 C ATOM 398 CD GLN A 219 72.036 111.029 -24.418 1.00 37.33 C ANISOU 398 CD GLN A 219 4984 4695 4504 229 -306 325 C ATOM 399 OE1 GLN A 219 73.270 110.993 -24.324 1.00 35.30 O ANISOU 399 OE1 GLN A 219 4749 4460 4205 219 -259 306 O ATOM 400 NE2 GLN A 219 71.380 110.492 -25.437 1.00 33.23 N ANISOU 400 NE2 GLN A 219 4484 4163 3980 254 -389 318 N ATOM 401 N LYS A 220 72.457 111.982 -18.901 1.00 29.16 N ANISOU 401 N LYS A 220 3834 3650 3596 144 -95 372 N ATOM 402 CA LYS A 220 72.816 111.587 -17.540 1.00 32.13 C ANISOU 402 CA LYS A 220 4186 4028 3995 123 -62 368 C ATOM 403 C LYS A 220 71.751 112.020 -16.550 1.00 31.55 C ANISOU 403 C LYS A 220 4087 3943 3958 152 -34 407 C ATOM 404 O LYS A 220 71.367 111.250 -15.658 1.00 31.24 O ANISOU 404 O LYS A 220 3997 3912 3961 149 -32 421 O ATOM 405 CB LYS A 220 74.164 112.189 -17.140 1.00 29.73 C ANISOU 405 CB LYS A 220 3929 3723 3645 94 -17 349 C ATOM 406 CG LYS A 220 75.337 111.624 -17.907 1.00 28.85 C ANISOU 406 CG LYS A 220 3826 3637 3501 71 -31 321 C ATOM 407 CD LYS A 220 76.651 111.991 -17.230 1.00 26.14 C ANISOU 407 CD LYS A 220 3503 3299 3132 32 8 314 C ATOM 408 CE LYS A 220 77.819 111.366 -17.989 1.00 20.36 C ANISOU 408 CE LYS A 220 2765 2604 2368 21 2 298 C ATOM 409 NZ LYS A 220 79.109 111.788 -17.358 1.00 26.15 N ANISOU 409 NZ LYS A 220 3505 3347 3082 -23 35 304 N ATOM 410 N PHE A 221 71.270 113.257 -16.698 1.00 28.84 N ANISOU 410 N PHE A 221 3782 3584 3594 184 -9 428 N ATOM 411 CA PHE A 221 70.239 113.788 -15.820 1.00 34.46 C ANISOU 411 CA PHE A 221 4478 4288 4328 231 27 468 C ATOM 412 C PHE A 221 69.024 112.868 -15.798 1.00 33.27 C ANISOU 412 C PHE A 221 4235 4161 4246 248 -6 510 C ATOM 413 O PHE A 221 68.530 112.493 -14.729 1.00 26.80 O ANISOU 413 O PHE A 221 3369 3353 3460 264 22 541 O ATOM 414 CB PHE A 221 69.873 115.196 -16.297 1.00 39.49 C ANISOU 414 CB PHE A 221 5175 4900 4928 271 45 483 C ATOM 415 CG PHE A 221 69.004 115.968 -15.356 1.00 34.83 C ANISOU 415 CG PHE A 221 4595 4298 4341 334 93 520 C ATOM 416 CD1 PHE A 221 69.555 116.706 -14.325 1.00 49.71 C ANISOU 416 CD1 PHE A 221 6552 6152 6183 344 140 505 C ATOM 417 CD2 PHE A 221 67.634 115.991 -15.528 1.00 45.50 C ANISOU 417 CD2 PHE A 221 5888 5668 5732 389 89 572 C ATOM 418 CE1 PHE A 221 68.751 117.442 -13.467 1.00 49.90 C ANISOU 418 CE1 PHE A 221 6603 6162 6196 420 187 536 C ATOM 419 CE2 PHE A 221 66.824 116.724 -14.676 1.00 48.75 C ANISOU 419 CE2 PHE A 221 6310 6075 6139 465 142 611 C ATOM 420 CZ PHE A 221 67.389 117.447 -13.645 1.00 50.21 C ANISOU 420 CZ PHE A 221 6579 6227 6271 485 194 590 C ATOM 421 N GLN A 222 68.560 112.454 -16.980 1.00 33.78 N ANISOU 421 N GLN A 222 4274 4232 4331 243 -70 515 N ATOM 422 CA GLN A 222 67.405 111.569 -17.051 1.00 40.58 C ANISOU 422 CA GLN A 222 5044 5109 5265 247 -120 562 C ATOM 423 C GLN A 222 67.720 110.203 -16.456 1.00 40.16 C ANISOU 423 C GLN A 222 4944 5063 5250 203 -144 553 C ATOM 424 O GLN A 222 66.900 109.639 -15.723 1.00 38.67 O ANISOU 424 O GLN A 222 4678 4890 5123 207 -145 606 O ATOM 425 CB GLN A 222 66.954 111.424 -18.500 1.00 40.63 C ANISOU 425 CB GLN A 222 5051 5111 5278 245 -200 562 C ATOM 426 CG GLN A 222 66.418 112.688 -19.109 1.00 38.75 C ANISOU 426 CG GLN A 222 4845 4866 5012 291 -185 583 C ATOM 427 CD GLN A 222 66.231 112.533 -20.592 1.00 41.94 C ANISOU 427 CD GLN A 222 5268 5262 5404 287 -265 570 C ATOM 428 OE1 GLN A 222 67.188 112.283 -21.330 1.00 43.15 O ANISOU 428 OE1 GLN A 222 5480 5407 5508 263 -288 518 O ATOM 429 NE2 GLN A 222 64.999 112.646 -21.038 1.00 33.52 N ANISOU 429 NE2 GLN A 222 4152 4201 4382 313 -311 623 N ATOM 430 N LEU A 223 68.899 109.657 -16.772 1.00 34.01 N ANISOU 430 N LEU A 223 4209 4276 4437 166 -163 494 N ATOM 431 CA LEU A 223 69.308 108.365 -16.216 1.00 41.49 C ANISOU 431 CA LEU A 223 5123 5226 5414 129 -187 480 C ATOM 432 C LEU A 223 69.314 108.392 -14.695 1.00 34.58 C ANISOU 432 C LEU A 223 4223 4362 4556 133 -120 504 C ATOM 433 O LEU A 223 68.736 107.513 -14.044 1.00 34.75 O ANISOU 433 O LEU A 223 4177 4392 4636 122 -135 542 O ATOM 434 CB LEU A 223 70.695 107.983 -16.724 1.00 39.28 C ANISOU 434 CB LEU A 223 4902 4941 5081 104 -199 414 C ATOM 435 CG LEU A 223 70.744 107.017 -17.895 1.00 46.33 C ANISOU 435 CG LEU A 223 5806 5824 5975 94 -287 387 C ATOM 436 CD1 LEU A 223 72.194 106.888 -18.337 1.00 39.00 C ANISOU 436 CD1 LEU A 223 4938 4903 4978 89 -273 329 C ATOM 437 CD2 LEU A 223 70.112 105.645 -17.564 1.00 38.60 C ANISOU 437 CD2 LEU A 223 4768 4832 5067 68 -356 408 C ATOM 438 N PHE A 224 69.990 109.386 -14.111 1.00 30.77 N ANISOU 438 N PHE A 224 3797 3875 4018 148 -50 484 N ATOM 439 CA PHE A 224 70.055 109.480 -12.658 1.00 29.44 C ANISOU 439 CA PHE A 224 3625 3712 3851 161 11 500 C ATOM 440 C PHE A 224 68.649 109.518 -12.064 1.00 37.77 C ANISOU 440 C PHE A 224 4611 4784 4956 205 34 575 C ATOM 441 O PHE A 224 68.349 108.813 -11.098 1.00 34.68 O ANISOU 441 O PHE A 224 4168 4408 4600 204 51 609 O ATOM 442 CB PHE A 224 70.838 110.728 -12.241 1.00 26.89 C ANISOU 442 CB PHE A 224 3389 3370 3460 175 67 472 C ATOM 443 CG PHE A 224 72.286 110.741 -12.693 1.00 36.82 C ANISOU 443 CG PHE A 224 4698 4618 4672 128 53 415 C ATOM 444 CD1 PHE A 224 72.994 109.563 -12.881 1.00 36.74 C ANISOU 444 CD1 PHE A 224 4662 4621 4676 88 17 387 C ATOM 445 CD2 PHE A 224 72.943 111.942 -12.902 1.00 30.21 C ANISOU 445 CD2 PHE A 224 3937 3761 3781 127 76 396 C ATOM 446 CE1 PHE A 224 74.315 109.587 -13.271 1.00 29.00 C ANISOU 446 CE1 PHE A 224 3720 3643 3654 55 13 346 C ATOM 447 CE2 PHE A 224 74.266 111.970 -13.291 1.00 29.15 C ANISOU 447 CE2 PHE A 224 3837 3626 3611 82 67 360 C ATOM 448 CZ PHE A 224 74.951 110.783 -13.486 1.00 30.18 C ANISOU 448 CZ PHE A 224 3931 3781 3756 50 39 337 C ATOM 449 N GLU A 225 67.766 110.330 -12.646 1.00 32.81 N ANISOU 449 N GLU A 225 3978 4158 4331 247 35 608 N ATOM 450 CA GLU A 225 66.458 110.537 -12.041 1.00 37.62 C ANISOU 450 CA GLU A 225 4521 4793 4981 303 71 688 C ATOM 451 C GLU A 225 65.588 109.285 -12.135 1.00 39.86 C ANISOU 451 C GLU A 225 4690 5101 5354 274 15 748 C ATOM 452 O GLU A 225 64.873 108.951 -11.183 1.00 33.00 O ANISOU 452 O GLU A 225 3751 4261 4526 298 52 817 O ATOM 453 CB GLU A 225 65.769 111.731 -12.696 1.00 43.74 C ANISOU 453 CB GLU A 225 5320 5565 5736 359 83 710 C ATOM 454 CG GLU A 225 65.002 112.593 -11.708 1.00 68.99 C ANISOU 454 CG GLU A 225 8517 8777 8918 447 167 764 C ATOM 455 CD GLU A 225 63.820 111.853 -11.084 1.00 87.44 C ANISOU 455 CD GLU A 225 10730 11162 11330 473 180 859 C ATOM 456 OE1 GLU A 225 63.628 111.957 -9.849 1.00 91.75 O ANISOU 456 OE1 GLU A 225 11272 11726 11861 525 256 893 O ATOM 457 OE2 GLU A 225 63.085 111.164 -11.831 1.00 88.95 O ANISOU 457 OE2 GLU A 225 10829 11372 11594 442 113 904 O ATOM 458 N GLN A 226 65.652 108.563 -13.256 1.00 34.17 N ANISOU 458 N GLN A 226 3954 4366 4662 222 -78 727 N ATOM 459 CA GLN A 226 64.773 107.416 -13.457 1.00 32.68 C ANISOU 459 CA GLN A 226 3666 4188 4562 187 -153 787 C ATOM 460 C GLN A 226 65.308 106.118 -12.853 1.00 33.83 C ANISOU 460 C GLN A 226 3791 4326 4737 133 -179 774 C ATOM 461 O GLN A 226 64.536 105.174 -12.654 1.00 42.78 O ANISOU 461 O GLN A 226 4836 5468 5951 103 -228 841 O ATOM 462 CB GLN A 226 64.512 107.212 -14.959 1.00 29.22 C ANISOU 462 CB GLN A 226 3235 3729 4139 161 -256 770 C ATOM 463 CG GLN A 226 63.690 108.335 -15.623 1.00 29.39 C ANISOU 463 CG GLN A 226 3253 3760 4152 213 -248 803 C ATOM 464 CD GLN A 226 63.569 108.150 -17.137 1.00 34.07 C ANISOU 464 CD GLN A 226 3871 4328 4745 189 -354 777 C ATOM 465 OE1 GLN A 226 63.480 107.029 -17.626 1.00 37.95 O ANISOU 465 OE1 GLN A 226 4340 4800 5279 138 -452 773 O ATOM 466 NE2 GLN A 226 63.584 109.246 -17.877 1.00 33.91 N ANISOU 466 NE2 GLN A 226 3908 4303 4673 228 -338 756 N ATOM 467 N VAL A 227 66.599 106.026 -12.558 1.00 33.31 N ANISOU 467 N VAL A 227 3800 4243 4611 116 -153 698 N ATOM 468 CA VAL A 227 67.195 104.783 -12.098 1.00 30.71 C ANISOU 468 CA VAL A 227 3461 3904 4304 68 -185 679 C ATOM 469 C VAL A 227 67.635 104.870 -10.641 1.00 33.72 C ANISOU 469 C VAL A 227 3848 4301 4664 84 -98 685 C ATOM 470 O VAL A 227 67.485 103.901 -9.894 1.00 43.88 O ANISOU 470 O VAL A 227 5084 5593 5996 60 -106 721 O ATOM 471 CB VAL A 227 68.366 104.366 -13.011 1.00 33.65 C ANISOU 471 CB VAL A 227 3909 4246 4630 37 -239 589 C ATOM 472 CG1 VAL A 227 69.023 103.067 -12.517 1.00 26.68 C ANISOU 472 CG1 VAL A 227 3022 3349 3765 -4 -272 567 C ATOM 473 CG2 VAL A 227 67.869 104.201 -14.435 1.00 29.59 C ANISOU 473 CG2 VAL A 227 3398 3713 4131 28 -332 584 C ATOM 474 N ILE A 228 68.158 106.016 -10.207 1.00 31.93 N ANISOU 474 N ILE A 228 3687 4077 4367 125 -20 655 N ATOM 475 CA ILE A 228 68.597 106.141 -8.820 1.00 31.83 C ANISOU 475 CA ILE A 228 3697 4073 4324 144 54 656 C ATOM 476 C ILE A 228 68.007 107.387 -8.182 1.00 30.98 C ANISOU 476 C ILE A 228 3610 3979 4182 219 136 692 C ATOM 477 O ILE A 228 68.528 107.885 -7.178 1.00 42.27 O ANISOU 477 O ILE A 228 5100 5405 5558 247 198 674 O ATOM 478 CB ILE A 228 70.130 106.159 -8.723 1.00 33.01 C ANISOU 478 CB ILE A 228 3928 4202 4413 114 56 572 C ATOM 479 CG1 ILE A 228 70.701 107.342 -9.531 1.00 38.31 C ANISOU 479 CG1 ILE A 228 4677 4857 5023 124 64 522 C ATOM 480 CG2 ILE A 228 70.691 104.828 -9.191 1.00 29.80 C ANISOU 480 CG2 ILE A 228 3502 3786 4037 57 -16 542 C ATOM 481 CD1 ILE A 228 72.193 107.602 -9.317 1.00 36.46 C ANISOU 481 CD1 ILE A 228 4517 4608 4729 97 76 457 C ATOM 482 N GLY A 229 66.926 107.903 -8.757 1.00 36.58 N ANISOU 482 N GLY A 229 4279 4702 4918 255 134 743 N ATOM 483 CA GLY A 229 66.326 109.120 -8.240 1.00 35.70 C ANISOU 483 CA GLY A 229 4194 4601 4767 340 212 777 C ATOM 484 C GLY A 229 65.145 108.899 -7.310 1.00 37.68 C ANISOU 484 C GLY A 229 4357 4897 5060 397 266 879 C ATOM 485 O GLY A 229 64.899 109.715 -6.414 1.00 43.92 O ANISOU 485 O GLY A 229 5188 5698 5801 479 350 902 O ATOM 486 N ARG A 230 64.404 107.809 -7.512 1.00 40.65 N ANISOU 486 N ARG A 230 4618 5301 5528 358 218 947 N ATOM 487 CA ARG A 230 63.197 107.512 -6.747 1.00 48.08 C ANISOU 487 CA ARG A 230 5449 6295 6524 404 264 1066 C ATOM 488 C ARG A 230 63.370 106.181 -6.031 1.00 45.61 C ANISOU 488 C ARG A 230 5077 5991 6260 348 247 1096 C ATOM 489 O ARG A 230 63.760 105.185 -6.650 1.00 35.38 O ANISOU 489 O ARG A 230 3764 4669 5010 260 154 1066 O ATOM 490 CB ARG A 230 61.963 107.481 -7.658 1.00 53.59 C ANISOU 490 CB ARG A 230 6042 7019 7301 405 215 1146 C ATOM 491 CG ARG A 230 61.812 108.754 -8.495 1.00 65.40 C ANISOU 491 CG ARG A 230 7599 8500 8749 456 221 1113 C ATOM 492 CD ARG A 230 60.868 108.580 -9.674 1.00 65.38 C ANISOU 492 CD ARG A 230 7509 8509 8822 430 138 1166 C ATOM 493 NE ARG A 230 61.198 107.409 -10.488 1.00 71.05 N ANISOU 493 NE ARG A 230 8203 9196 9595 324 19 1135 N ATOM 494 CZ ARG A 230 61.450 107.435 -11.797 1.00 70.97 C ANISOU 494 CZ ARG A 230 8234 9150 9581 283 -71 1077 C ATOM 495 NH1 ARG A 230 61.406 108.587 -12.459 1.00 61.93 N ANISOU 495 NH1 ARG A 230 7149 7997 8385 331 -53 1048 N ATOM 496 NH2 ARG A 230 61.743 106.302 -12.447 1.00 67.16 N ANISOU 496 NH2 ARG A 230 7742 8636 9141 198 -179 1050 N ATOM 497 N LYS A 231 63.059 106.164 -4.731 1.00 47.60 N ANISOU 497 N LYS A 231 5307 6281 6499 406 335 1158 N ATOM 498 CA LYS A 231 63.320 104.983 -3.916 1.00 44.40 C ANISOU 498 CA LYS A 231 4861 5882 6127 359 329 1185 C ATOM 499 C LYS A 231 62.629 103.735 -4.469 1.00 44.73 C ANISOU 499 C LYS A 231 4775 5932 6287 277 236 1260 C ATOM 500 O LYS A 231 63.252 102.674 -4.606 1.00 44.59 O ANISOU 500 O LYS A 231 4762 5880 6299 194 163 1223 O ATOM 501 CB LYS A 231 62.893 105.244 -2.473 1.00 47.38 C ANISOU 501 CB LYS A 231 5227 6307 6470 450 446 1259 C ATOM 502 CG LYS A 231 62.982 104.010 -1.573 1.00 55.49 C ANISOU 502 CG LYS A 231 6196 7349 7537 408 447 1311 C ATOM 503 CD LYS A 231 63.954 104.228 -0.425 1.00 67.47 C ANISOU 503 CD LYS A 231 7825 8852 8958 446 513 1249 C ATOM 504 CE LYS A 231 63.406 105.218 0.576 1.00 79.50 C ANISOU 504 CE LYS A 231 9382 10416 10409 579 636 1300 C ATOM 505 NZ LYS A 231 64.444 105.929 1.384 1.00 84.21 N ANISOU 505 NZ LYS A 231 10135 10975 10884 628 683 1206 N ATOM 506 N ASP A 232 61.343 103.844 -4.808 1.00 38.05 N ANISOU 506 N ASP A 232 3818 5127 5511 298 231 1368 N ATOM 507 CA ASP A 232 60.579 102.655 -5.188 1.00 46.24 C ANISOU 507 CA ASP A 232 4727 6172 6670 216 138 1460 C ATOM 508 C ASP A 232 61.100 102.045 -6.487 1.00 39.33 C ANISOU 508 C ASP A 232 3890 5230 5822 120 -4 1376 C ATOM 509 O ASP A 232 61.250 100.821 -6.585 1.00 44.02 O ANISOU 509 O ASP A 232 4455 5794 6478 36 -91 1384 O ATOM 510 CB ASP A 232 59.092 103.000 -5.299 1.00 53.27 C ANISOU 510 CB ASP A 232 5483 7125 7631 261 160 1602 C ATOM 511 CG ASP A 232 58.834 104.187 -6.222 1.00 74.42 C ANISOU 511 CG ASP A 232 8202 9801 10272 315 161 1564 C ATOM 512 OD1 ASP A 232 57.966 104.067 -7.112 1.00 82.89 O ANISOU 512 OD1 ASP A 232 9188 10883 11424 284 83 1626 O ATOM 513 OD2 ASP A 232 59.508 105.233 -6.071 1.00 76.51 O ANISOU 513 OD2 ASP A 232 8588 10050 10431 382 231 1473 O ATOM 514 N ASP A 233 61.386 102.883 -7.486 1.00 33.33 N ANISOU 514 N ASP A 233 3204 4445 5013 137 -27 1295 N ATOM 515 CA ASP A 233 61.937 102.393 -8.746 1.00 40.01 C ANISOU 515 CA ASP A 233 4104 5231 5867 64 -151 1210 C ATOM 516 C ASP A 233 63.362 101.882 -8.561 1.00 32.33 C ANISOU 516 C ASP A 233 3234 4215 4835 29 -162 1098 C ATOM 517 O ASP A 233 63.733 100.841 -9.111 1.00 36.80 O ANISOU 517 O ASP A 233 3813 4738 5433 -41 -264 1063 O ATOM 518 CB ASP A 233 61.883 103.506 -9.792 1.00 38.63 C ANISOU 518 CB ASP A 233 3984 5049 5646 103 -158 1160 C ATOM 519 CG ASP A 233 60.466 103.757 -10.299 1.00 50.20 C ANISOU 519 CG ASP A 233 5341 6548 7187 118 -190 1268 C ATOM 520 OD1 ASP A 233 59.550 102.976 -9.951 1.00 49.24 O ANISOU 520 OD1 ASP A 233 5095 6452 7162 86 -223 1382 O ATOM 521 OD2 ASP A 233 60.266 104.731 -11.051 1.00 51.55 O ANISOU 521 OD2 ASP A 233 5545 6718 7323 160 -186 1244 O ATOM 522 N PHE A 234 64.167 102.594 -7.775 1.00 32.35 N ANISOU 522 N PHE A 234 3314 4227 4751 80 -62 1043 N ATOM 523 CA PHE A 234 65.495 102.109 -7.418 1.00 30.31 C ANISOU 523 CA PHE A 234 3137 3937 4442 50 -63 954 C ATOM 524 C PHE A 234 65.438 100.715 -6.787 1.00 33.77 C ANISOU 524 C PHE A 234 3518 4369 4944 -4 -103 1000 C ATOM 525 O PHE A 234 66.210 99.819 -7.153 1.00 34.82 O ANISOU 525 O PHE A 234 3690 4460 5079 -59 -177 940 O ATOM 526 CB PHE A 234 66.161 103.111 -6.473 1.00 28.47 C ANISOU 526 CB PHE A 234 2981 3719 4119 113 49 915 C ATOM 527 CG PHE A 234 67.430 102.615 -5.867 1.00 30.31 C ANISOU 527 CG PHE A 234 3279 3929 4306 85 55 845 C ATOM 528 CD1 PHE A 234 68.605 102.590 -6.609 1.00 28.93 C ANISOU 528 CD1 PHE A 234 3184 3721 4088 52 10 744 C ATOM 529 CD2 PHE A 234 67.450 102.143 -4.565 1.00 31.77 C ANISOU 529 CD2 PHE A 234 3444 4134 4495 97 106 886 C ATOM 530 CE1 PHE A 234 69.789 102.111 -6.050 1.00 33.21 C ANISOU 530 CE1 PHE A 234 3777 4249 4594 29 14 686 C ATOM 531 CE2 PHE A 234 68.639 101.661 -3.995 1.00 36.81 C ANISOU 531 CE2 PHE A 234 4142 4752 5094 71 106 823 C ATOM 532 CZ PHE A 234 69.807 101.646 -4.741 1.00 31.89 C ANISOU 532 CZ PHE A 234 3591 4095 4431 37 59 723 C ATOM 533 N LEU A 235 64.527 100.516 -5.830 1.00 40.66 N ANISOU 533 N LEU A 235 4299 5284 5866 16 -52 1113 N ATOM 534 CA LEU A 235 64.423 99.224 -5.153 1.00 35.76 C ANISOU 534 CA LEU A 235 3620 4659 5309 -37 -84 1170 C ATOM 535 C LEU A 235 63.951 98.137 -6.105 1.00 37.94 C ANISOU 535 C LEU A 235 3842 4895 5678 -121 -226 1199 C ATOM 536 O LEU A 235 64.499 97.024 -6.110 1.00 42.04 O ANISOU 536 O LEU A 235 4385 5370 6219 -181 -299 1169 O ATOM 537 CB LEU A 235 63.471 99.326 -3.960 1.00 42.50 C ANISOU 537 CB LEU A 235 4379 5575 6193 11 10 1300 C ATOM 538 CG LEU A 235 63.972 100.177 -2.788 1.00 48.97 C ANISOU 538 CG LEU A 235 5266 6426 6915 97 143 1276 C ATOM 539 CD1 LEU A 235 62.963 100.170 -1.660 1.00 43.50 C ANISOU 539 CD1 LEU A 235 4478 5799 6251 153 235 1414 C ATOM 540 CD2 LEU A 235 65.332 99.695 -2.296 1.00 46.03 C ANISOU 540 CD2 LEU A 235 4988 6015 6486 69 137 1179 C ATOM 541 N LYS A 236 62.943 98.447 -6.924 1.00 37.64 N ANISOU 541 N LYS A 236 3741 4867 5694 -125 -272 1256 N ATOM 542 CA LYS A 236 62.444 97.492 -7.911 1.00 38.54 C ANISOU 542 CA LYS A 236 3816 4935 5894 -206 -424 1282 C ATOM 543 C LYS A 236 63.539 97.069 -8.883 1.00 35.37 C ANISOU 543 C LYS A 236 3535 4461 5441 -239 -515 1146 C ATOM 544 O LYS A 236 63.658 95.886 -9.219 1.00 37.98 O ANISOU 544 O LYS A 236 3875 4736 5818 -305 -630 1139 O ATOM 545 CB LYS A 236 61.264 98.102 -8.674 1.00 42.36 C ANISOU 545 CB LYS A 236 4223 5444 6429 -194 -455 1355 C ATOM 546 CG LYS A 236 60.735 97.217 -9.789 1.00 53.58 C ANISOU 546 CG LYS A 236 5617 6809 7934 -278 -627 1376 C ATOM 547 CD LYS A 236 59.356 97.675 -10.250 1.00 68.17 C ANISOU 547 CD LYS A 236 7349 8695 9858 -274 -656 1491 C ATOM 548 CE LYS A 236 58.851 96.847 -11.426 1.00 73.46 C ANISOU 548 CE LYS A 236 8006 9299 10605 -360 -845 1506 C ATOM 549 NZ LYS A 236 57.372 96.941 -11.575 1.00 76.10 N ANISOU 549 NZ LYS A 236 8188 9676 11051 -381 -888 1660 N ATOM 550 N LEU A 237 64.341 98.026 -9.359 1.00 34.93 N ANISOU 550 N LEU A 237 3576 4407 5290 -189 -467 1042 N ATOM 551 CA LEU A 237 65.438 97.677 -10.255 1.00 35.26 C ANISOU 551 CA LEU A 237 3729 4395 5274 -206 -536 920 C ATOM 552 C LEU A 237 66.540 96.915 -9.514 1.00 37.46 C ANISOU 552 C LEU A 237 4059 4654 5520 -220 -518 867 C ATOM 553 O LEU A 237 67.080 95.928 -10.038 1.00 35.88 O ANISOU 553 O LEU A 237 3910 4400 5322 -256 -612 815 O ATOM 554 CB LEU A 237 65.984 98.948 -10.919 1.00 33.82 C ANISOU 554 CB LEU A 237 3623 4226 5001 -151 -481 841 C ATOM 555 CG LEU A 237 65.041 99.566 -11.968 1.00 38.91 C ANISOU 555 CG LEU A 237 4241 4873 5670 -141 -529 872 C ATOM 556 CD1 LEU A 237 65.737 100.634 -12.817 1.00 37.01 C ANISOU 556 CD1 LEU A 237 4094 4633 5337 -96 -497 783 C ATOM 557 CD2 LEU A 237 64.411 98.485 -12.857 1.00 37.69 C ANISOU 557 CD2 LEU A 237 4061 4669 5590 -203 -684 899 C ATOM 558 N SER A 238 66.863 97.338 -8.284 1.00 34.61 N ANISOU 558 N SER A 238 3689 4334 5127 -186 -402 882 N ATOM 559 CA SER A 238 67.949 96.702 -7.534 1.00 32.93 C ANISOU 559 CA SER A 238 3525 4107 4878 -195 -381 832 C ATOM 560 C SER A 238 67.649 95.250 -7.204 1.00 35.28 C ANISOU 560 C SER A 238 3779 4370 5254 -254 -462 885 C ATOM 561 O SER A 238 68.581 94.441 -7.103 1.00 38.05 O ANISOU 561 O SER A 238 4189 4687 5584 -272 -497 825 O ATOM 562 CB SER A 238 68.224 97.464 -6.237 1.00 28.44 C ANISOU 562 CB SER A 238 2958 3586 4261 -146 -249 846 C ATOM 563 OG SER A 238 68.756 98.746 -6.512 1.00 38.12 O ANISOU 563 OG SER A 238 4249 4828 5406 -98 -186 782 O ATOM 564 N THR A 239 66.371 94.904 -7.003 1.00 28.58 N ANISOU 564 N THR A 239 2826 3532 4499 -285 -492 1003 N ATOM 565 CA THR A 239 65.980 93.531 -6.721 1.00 39.00 C ANISOU 565 CA THR A 239 4099 4815 5906 -353 -581 1069 C ATOM 566 C THR A 239 65.548 92.780 -7.971 1.00 48.99 C ANISOU 566 C THR A 239 5374 6013 7229 -411 -743 1065 C ATOM 567 O THR A 239 64.993 91.679 -7.856 1.00 46.57 O ANISOU 567 O THR A 239 5019 5666 7010 -478 -839 1137 O ATOM 568 CB THR A 239 64.844 93.480 -5.684 1.00 38.63 C ANISOU 568 CB THR A 239 3923 4820 5936 -359 -525 1220 C ATOM 569 OG1 THR A 239 63.745 94.286 -6.123 1.00 37.99 O ANISOU 569 OG1 THR A 239 3765 4780 5891 -340 -511 1292 O ATOM 570 CG2 THR A 239 65.327 93.966 -4.329 1.00 39.36 C ANISOU 570 CG2 THR A 239 4024 4966 5965 -301 -380 1224 C ATOM 571 N ASN A 240 65.774 93.340 -9.155 1.00 39.39 N ANISOU 571 N ASN A 240 4222 4779 5964 -389 -780 986 N ATOM 572 CA ASN A 240 65.389 92.668 -10.387 1.00 40.61 C ANISOU 572 CA ASN A 240 4404 4865 6160 -435 -940 973 C ATOM 573 C ASN A 240 66.576 91.911 -10.972 1.00 38.35 C ANISOU 573 C ASN A 240 4249 4512 5810 -431 -1010 852 C ATOM 574 O ASN A 240 67.715 92.391 -10.944 1.00 40.27 O ANISOU 574 O ASN A 240 4568 4776 5957 -377 -930 757 O ATOM 575 CB ASN A 240 64.832 93.665 -11.409 1.00 36.09 C ANISOU 575 CB ASN A 240 3828 4311 5573 -408 -950 966 C ATOM 576 CG ASN A 240 64.453 93.006 -12.729 1.00 37.32 C ANISOU 576 CG ASN A 240 4028 4391 5761 -450 -1123 947 C ATOM 577 OD1 ASN A 240 65.219 93.034 -13.690 1.00 41.19 O ANISOU 577 OD1 ASN A 240 4633 4843 6172 -421 -1166 837 O ATOM 578 ND2 ASN A 240 63.266 92.415 -12.782 1.00 38.76 N ANISOU 578 ND2 ASN A 240 4120 4551 6057 -518 -1227 1058 N ATOM 579 N ILE A 241 66.287 90.736 -11.533 1.00 39.87 N ANISOU 579 N ILE A 241 4468 4623 6056 -487 -1166 860 N ATOM 580 CA ILE A 241 67.311 89.880 -12.120 1.00 38.87 C ANISOU 580 CA ILE A 241 4473 4426 5872 -475 -1246 753 C ATOM 581 C ILE A 241 68.070 90.593 -13.240 1.00 40.69 C ANISOU 581 C ILE A 241 4805 4661 5994 -407 -1231 639 C ATOM 582 O ILE A 241 69.251 90.310 -13.475 1.00 37.13 O ANISOU 582 O ILE A 241 4455 4194 5461 -362 -1220 542 O ATOM 583 CB ILE A 241 66.660 88.568 -12.613 1.00 42.13 C ANISOU 583 CB ILE A 241 4903 4739 6366 -548 -1435 791 C ATOM 584 CG1 ILE A 241 67.719 87.623 -13.187 1.00 44.33 C ANISOU 584 CG1 ILE A 241 5331 4937 6576 -522 -1521 679 C ATOM 585 CG2 ILE A 241 65.549 88.868 -13.644 1.00 34.63 C ANISOU 585 CG2 ILE A 241 3924 3767 5465 -578 -1540 835 C ATOM 586 CD1 ILE A 241 67.227 86.208 -13.428 1.00 51.08 C ANISOU 586 CD1 ILE A 241 6222 5681 7507 -593 -1706 713 C ATOM 587 N PHE A 242 67.417 91.507 -13.957 1.00 40.06 N ANISOU 587 N PHE A 242 4700 4607 5913 -394 -1229 655 N ATOM 588 CA PHE A 242 68.092 92.300 -14.978 1.00 40.63 C ANISOU 588 CA PHE A 242 4860 4693 5882 -328 -1200 560 C ATOM 589 C PHE A 242 68.402 93.722 -14.520 1.00 39.78 C ANISOU 589 C PHE A 242 4717 4674 5725 -281 -1036 557 C ATOM 590 O PHE A 242 69.482 94.239 -14.824 1.00 33.78 O ANISOU 590 O PHE A 242 4028 3936 4870 -228 -969 474 O ATOM 591 CB PHE A 242 67.255 92.353 -16.262 1.00 44.98 C ANISOU 591 CB PHE A 242 5437 5203 6452 -340 -1325 567 C ATOM 592 CG PHE A 242 66.876 90.994 -16.798 1.00 48.26 C ANISOU 592 CG PHE A 242 5903 5517 6917 -390 -1509 570 C ATOM 593 CD1 PHE A 242 67.849 90.044 -17.072 1.00 41.27 C ANISOU 593 CD1 PHE A 242 5138 4571 5972 -365 -1566 484 C ATOM 594 CD2 PHE A 242 65.549 90.672 -17.028 1.00 51.60 C ANISOU 594 CD2 PHE A 242 6256 5903 7445 -461 -1630 664 C ATOM 595 CE1 PHE A 242 67.505 88.793 -17.565 1.00 49.88 C ANISOU 595 CE1 PHE A 242 6295 5556 7102 -407 -1745 483 C ATOM 596 CE2 PHE A 242 65.192 89.417 -17.518 1.00 57.01 C ANISOU 596 CE2 PHE A 242 6997 6484 8179 -516 -1817 670 C ATOM 597 CZ PHE A 242 66.170 88.477 -17.783 1.00 53.84 C ANISOU 597 CZ PHE A 242 6732 6012 7712 -488 -1877 576 C ATOM 598 N GLY A 243 67.479 94.364 -13.793 1.00 40.35 N ANISOU 598 N GLY A 243 4678 4794 5857 -298 -972 650 N ATOM 599 CA GLY A 243 67.665 95.758 -13.427 1.00 38.51 C ANISOU 599 CA GLY A 243 4425 4633 5575 -249 -832 646 C ATOM 600 C GLY A 243 68.868 96.019 -12.532 1.00 35.36 C ANISOU 600 C GLY A 243 4061 4266 5109 -218 -717 595 C ATOM 601 O GLY A 243 69.426 97.121 -12.545 1.00 31.20 O ANISOU 601 O GLY A 243 3564 3779 4513 -174 -624 556 O ATOM 602 N ASN A 244 69.279 95.029 -11.730 1.00 35.30 N ANISOU 602 N ASN A 244 4050 4239 5122 -243 -728 599 N ATOM 603 CA ASN A 244 70.373 95.292 -10.802 1.00 31.53 C ANISOU 603 CA ASN A 244 3598 3795 4587 -216 -623 559 C ATOM 604 C ASN A 244 71.657 95.615 -11.552 1.00 35.18 C ANISOU 604 C ASN A 244 4155 4257 4954 -176 -608 456 C ATOM 605 O ASN A 244 72.502 96.351 -11.037 1.00 35.28 O ANISOU 605 O ASN A 244 4187 4310 4910 -149 -512 424 O ATOM 606 CB ASN A 244 70.570 94.121 -9.835 1.00 30.15 C ANISOU 606 CB ASN A 244 3404 3598 4453 -249 -644 585 C ATOM 607 CG ASN A 244 71.388 92.996 -10.423 1.00 33.20 C ANISOU 607 CG ASN A 244 3871 3928 4817 -254 -735 515 C ATOM 608 OD1 ASN A 244 72.616 93.045 -10.435 1.00 34.35 O ANISOU 608 OD1 ASN A 244 4080 4084 4889 -219 -696 440 O ATOM 609 ND2 ASN A 244 70.701 91.959 -10.919 1.00 34.15 N ANISOU 609 ND2 ASN A 244 3990 3985 5001 -296 -864 544 N ATOM 610 N TYR A 245 71.804 95.112 -12.781 1.00 35.10 N ANISOU 610 N TYR A 245 4206 4205 4924 -170 -702 407 N ATOM 611 CA TYR A 245 72.986 95.450 -13.564 1.00 31.04 C ANISOU 611 CA TYR A 245 3776 3702 4316 -122 -679 321 C ATOM 612 C TYR A 245 72.937 96.897 -14.035 1.00 32.34 C ANISOU 612 C TYR A 245 3942 3910 4437 -94 -609 316 C ATOM 613 O TYR A 245 73.947 97.607 -13.975 1.00 32.89 O ANISOU 613 O TYR A 245 4041 4016 4440 -66 -530 277 O ATOM 614 CB TYR A 245 73.122 94.504 -14.750 1.00 29.67 C ANISOU 614 CB TYR A 245 3679 3471 4122 -108 -797 273 C ATOM 615 CG TYR A 245 73.595 93.124 -14.378 1.00 34.29 C ANISOU 615 CG TYR A 245 4296 4011 4721 -118 -857 253 C ATOM 616 CD1 TYR A 245 74.945 92.863 -14.140 1.00 32.09 C ANISOU 616 CD1 TYR A 245 4064 3752 4378 -78 -808 196 C ATOM 617 CD2 TYR A 245 72.691 92.071 -14.283 1.00 30.95 C ANISOU 617 CD2 TYR A 245 3857 3525 4379 -167 -970 297 C ATOM 618 CE1 TYR A 245 75.372 91.579 -13.799 1.00 35.48 C ANISOU 618 CE1 TYR A 245 4527 4136 4818 -80 -866 178 C ATOM 619 CE2 TYR A 245 73.103 90.807 -13.952 1.00 38.19 C ANISOU 619 CE2 TYR A 245 4810 4390 5308 -177 -1033 281 C ATOM 620 CZ TYR A 245 74.432 90.555 -13.713 1.00 40.68 C ANISOU 620 CZ TYR A 245 5177 4724 5554 -129 -980 218 C ATOM 621 OH TYR A 245 74.796 89.269 -13.392 1.00 51.38 O ANISOU 621 OH TYR A 245 6575 6025 6924 -133 -1047 204 O ATOM 622 N LEU A 246 71.770 97.346 -14.512 1.00 33.75 N ANISOU 622 N LEU A 246 4086 4083 4656 -105 -642 362 N ATOM 623 CA LEU A 246 71.615 98.738 -14.910 1.00 34.71 C ANISOU 623 CA LEU A 246 4208 4240 4740 -77 -578 364 C ATOM 624 C LEU A 246 71.828 99.669 -13.726 1.00 36.45 C ANISOU 624 C LEU A 246 4394 4505 4952 -71 -459 389 C ATOM 625 O LEU A 246 72.391 100.763 -13.880 1.00 30.27 O ANISOU 625 O LEU A 246 3644 3749 4110 -45 -390 362 O ATOM 626 CB LEU A 246 70.231 98.967 -15.530 1.00 29.96 C ANISOU 626 CB LEU A 246 3566 3624 4192 -88 -641 418 C ATOM 627 CG LEU A 246 69.992 100.389 -16.052 1.00 32.24 C ANISOU 627 CG LEU A 246 3863 3944 4443 -55 -585 422 C ATOM 628 CD1 LEU A 246 71.085 100.749 -17.064 1.00 32.69 C ANISOU 628 CD1 LEU A 246 4011 4003 4406 -20 -576 344 C ATOM 629 CD2 LEU A 246 68.599 100.534 -16.667 1.00 29.14 C ANISOU 629 CD2 LEU A 246 3424 3539 4109 -65 -655 480 C ATOM 630 N VAL A 247 71.404 99.246 -12.532 1.00 27.50 N ANISOU 630 N VAL A 247 3200 3376 3872 -93 -438 441 N ATOM 631 CA VAL A 247 71.601 100.075 -11.346 1.00 28.98 C ANISOU 631 CA VAL A 247 3369 3600 4042 -79 -330 461 C ATOM 632 C VAL A 247 73.086 100.252 -11.065 1.00 33.43 C ANISOU 632 C VAL A 247 3992 4175 4536 -69 -282 395 C ATOM 633 O VAL A 247 73.541 101.360 -10.756 1.00 34.99 O ANISOU 633 O VAL A 247 4215 4395 4686 -51 -209 383 O ATOM 634 CB VAL A 247 70.868 99.470 -10.132 1.00 31.21 C ANISOU 634 CB VAL A 247 3580 3888 4392 -98 -317 535 C ATOM 635 CG1 VAL A 247 71.231 100.213 -8.835 1.00 27.83 C ANISOU 635 CG1 VAL A 247 3154 3491 3928 -73 -209 545 C ATOM 636 CG2 VAL A 247 69.388 99.508 -10.341 1.00 28.30 C ANISOU 636 CG2 VAL A 247 3136 3523 4095 -104 -350 617 C ATOM 637 N GLN A 248 73.871 99.170 -11.166 1.00 33.70 N ANISOU 637 N GLN A 248 4050 4191 4563 -82 -327 356 N ATOM 638 CA GLN A 248 75.303 99.295 -10.897 1.00 32.16 C ANISOU 638 CA GLN A 248 3898 4013 4307 -72 -283 304 C ATOM 639 C GLN A 248 75.985 100.174 -11.940 1.00 29.39 C ANISOU 639 C GLN A 248 3595 3680 3891 -49 -264 262 C ATOM 640 O GLN A 248 76.842 100.997 -11.598 1.00 30.91 O ANISOU 640 O GLN A 248 3807 3898 4039 -45 -201 246 O ATOM 641 CB GLN A 248 75.959 97.920 -10.836 1.00 26.53 C ANISOU 641 CB GLN A 248 3199 3280 3600 -80 -335 275 C ATOM 642 CG GLN A 248 75.449 97.073 -9.701 1.00 28.99 C ANISOU 642 CG GLN A 248 3466 3576 3972 -107 -347 320 C ATOM 643 CD GLN A 248 75.958 95.645 -9.760 1.00 31.95 C ANISOU 643 CD GLN A 248 3864 3919 4358 -113 -415 294 C ATOM 644 OE1 GLN A 248 77.160 95.407 -9.636 1.00 29.30 O ANISOU 644 OE1 GLN A 248 3561 3595 3976 -96 -396 248 O ATOM 645 NE2 GLN A 248 75.038 94.678 -9.957 1.00 29.48 N ANISOU 645 NE2 GLN A 248 3530 3561 4108 -139 -500 328 N ATOM 646 N SER A 249 75.591 100.042 -13.213 1.00 30.03 N ANISOU 646 N SER A 249 3698 3745 3967 -35 -322 248 N ATOM 647 CA SER A 249 76.122 100.923 -14.253 1.00 34.81 C ANISOU 647 CA SER A 249 4347 4369 4510 -9 -301 219 C ATOM 648 C SER A 249 75.824 102.389 -13.958 1.00 31.35 C ANISOU 648 C SER A 249 3901 3949 4061 -10 -233 246 C ATOM 649 O SER A 249 76.699 103.247 -14.094 1.00 33.32 O ANISOU 649 O SER A 249 4180 4222 4259 -5 -183 229 O ATOM 650 CB SER A 249 75.549 100.543 -15.613 1.00 34.06 C ANISOU 650 CB SER A 249 4281 4249 4411 11 -380 206 C ATOM 651 OG SER A 249 76.054 99.286 -16.005 1.00 46.39 O ANISOU 651 OG SER A 249 5876 5788 5960 24 -442 169 O ATOM 652 N VAL A 250 74.588 102.696 -13.562 1.00 29.71 N ANISOU 652 N VAL A 250 3655 3731 3902 -14 -233 293 N ATOM 653 CA VAL A 250 74.214 104.093 -13.364 1.00 27.47 C ANISOU 653 CA VAL A 250 3376 3459 3603 -1 -174 317 C ATOM 654 C VAL A 250 74.933 104.668 -12.148 1.00 27.61 C ANISOU 654 C VAL A 250 3406 3488 3596 -8 -103 315 C ATOM 655 O VAL A 250 75.411 105.803 -12.179 1.00 27.37 O ANISOU 655 O VAL A 250 3415 3463 3522 -3 -60 307 O ATOM 656 CB VAL A 250 72.683 104.227 -13.253 1.00 28.78 C ANISOU 656 CB VAL A 250 3492 3617 3825 8 -190 376 C ATOM 657 CG1 VAL A 250 72.287 105.673 -12.901 1.00 26.49 C ANISOU 657 CG1 VAL A 250 3214 3336 3514 35 -122 401 C ATOM 658 CG2 VAL A 250 72.025 103.822 -14.578 1.00 33.92 C ANISOU 658 CG2 VAL A 250 4141 4252 4495 10 -273 376 C ATOM 659 N ILE A 251 75.042 103.883 -11.070 1.00 27.11 N ANISOU 659 N ILE A 251 3316 3424 3559 -22 -97 325 N ATOM 660 CA ILE A 251 75.875 104.273 -9.935 1.00 31.96 C ANISOU 660 CA ILE A 251 3953 4047 4145 -30 -44 315 C ATOM 661 C ILE A 251 77.312 104.543 -10.386 1.00 35.59 C ANISOU 661 C ILE A 251 4452 4518 4552 -44 -38 271 C ATOM 662 O ILE A 251 77.932 105.531 -9.971 1.00 33.91 O ANISOU 662 O ILE A 251 4274 4307 4302 -52 1 267 O ATOM 663 CB ILE A 251 75.809 103.195 -8.837 1.00 31.08 C ANISOU 663 CB ILE A 251 3806 3933 4069 -41 -48 331 C ATOM 664 CG1 ILE A 251 74.404 103.148 -8.225 1.00 34.15 C ANISOU 664 CG1 ILE A 251 4148 4321 4507 -25 -35 394 C ATOM 665 CG2 ILE A 251 76.835 103.492 -7.747 1.00 26.73 C ANISOU 665 CG2 ILE A 251 3287 3389 3481 -51 -6 314 C ATOM 666 CD1 ILE A 251 74.193 101.996 -7.222 1.00 32.26 C ANISOU 666 CD1 ILE A 251 3866 4081 4311 -38 -43 424 C ATOM 667 N GLY A 252 77.852 103.696 -11.270 1.00 31.99 N ANISOU 667 N GLY A 252 3994 4070 4090 -45 -80 244 N ATOM 668 CA GLY A 252 79.168 103.975 -11.835 1.00 31.79 C ANISOU 668 CA GLY A 252 3995 4068 4015 -49 -67 215 C ATOM 669 C GLY A 252 79.245 105.324 -12.538 1.00 32.57 C ANISOU 669 C GLY A 252 4125 4172 4077 -46 -41 222 C ATOM 670 O GLY A 252 80.145 106.128 -12.269 1.00 33.14 O ANISOU 670 O GLY A 252 4217 4256 4120 -67 -8 224 O ATOM 671 N ILE A 253 78.304 105.589 -13.457 1.00 27.94 N ANISOU 671 N ILE A 253 3544 3574 3497 -25 -62 231 N ATOM 672 CA ILE A 253 78.271 106.872 -14.169 1.00 23.85 C ANISOU 672 CA ILE A 253 3060 3057 2945 -20 -39 241 C ATOM 673 C ILE A 253 78.105 108.023 -13.190 1.00 26.52 C ANISOU 673 C ILE A 253 3418 3377 3281 -33 3 261 C ATOM 674 O ILE A 253 78.723 109.090 -13.330 1.00 28.83 O ANISOU 674 O ILE A 253 3747 3668 3538 -48 27 266 O ATOM 675 CB ILE A 253 77.131 106.874 -15.198 1.00 29.22 C ANISOU 675 CB ILE A 253 3741 3725 3638 9 -76 249 C ATOM 676 CG1 ILE A 253 77.389 105.813 -16.262 1.00 26.90 C ANISOU 676 CG1 ILE A 253 3451 3440 3331 28 -127 222 C ATOM 677 CG2 ILE A 253 76.931 108.280 -15.774 1.00 24.19 C ANISOU 677 CG2 ILE A 253 3139 3083 2970 17 -51 265 C ATOM 678 CD1 ILE A 253 76.129 105.314 -16.952 1.00 28.87 C ANISOU 678 CD1 ILE A 253 3692 3664 3612 46 -192 229 C ATOM 679 N SER A 254 77.254 107.828 -12.190 1.00 24.44 N ANISOU 679 N SER A 254 3136 3098 3052 -24 10 278 N ATOM 680 CA SER A 254 77.039 108.866 -11.192 1.00 26.82 C ANISOU 680 CA SER A 254 3471 3378 3341 -19 50 295 C ATOM 681 C SER A 254 78.341 109.216 -10.474 1.00 37.12 C ANISOU 681 C SER A 254 4809 4680 4614 -55 66 279 C ATOM 682 O SER A 254 78.643 110.398 -10.272 1.00 36.24 O ANISOU 682 O SER A 254 4753 4547 4472 -64 83 284 O ATOM 683 CB SER A 254 75.972 108.389 -10.209 1.00 26.26 C ANISOU 683 CB SER A 254 3367 3301 3310 6 61 322 C ATOM 684 OG SER A 254 75.854 109.286 -9.142 1.00 29.17 O ANISOU 684 OG SER A 254 3779 3649 3653 24 103 334 O ATOM 685 N LEU A 255 79.144 108.195 -10.105 1.00 27.49 N ANISOU 685 N LEU A 255 3560 3481 3403 -77 54 263 N ATOM 686 CA LEU A 255 80.414 108.446 -9.421 1.00 28.95 C ANISOU 686 CA LEU A 255 3767 3669 3565 -114 60 254 C ATOM 687 C LEU A 255 81.429 109.135 -10.329 1.00 28.66 C ANISOU 687 C LEU A 255 3744 3647 3498 -143 58 256 C ATOM 688 O LEU A 255 82.321 109.826 -9.836 1.00 35.81 O ANISOU 688 O LEU A 255 4678 4545 4384 -181 59 263 O ATOM 689 CB LEU A 255 80.998 107.129 -8.893 1.00 28.93 C ANISOU 689 CB LEU A 255 3723 3689 3581 -124 46 240 C ATOM 690 CG LEU A 255 80.126 106.479 -7.818 1.00 34.22 C ANISOU 690 CG LEU A 255 4378 4344 4281 -104 51 249 C ATOM 691 CD1 LEU A 255 80.538 105.008 -7.548 1.00 29.19 C ANISOU 691 CD1 LEU A 255 3697 3725 3668 -109 28 237 C ATOM 692 CD2 LEU A 255 80.126 107.322 -6.550 1.00 27.08 C ANISOU 692 CD2 LEU A 255 3524 3413 3353 -104 76 258 C ATOM 693 N ALA A 256 81.326 108.939 -11.643 1.00 28.63 N ANISOU 693 N ALA A 256 3723 3667 3490 -126 50 255 N ATOM 694 CA ALA A 256 82.234 109.553 -12.599 1.00 31.86 C ANISOU 694 CA ALA A 256 4139 4099 3868 -145 56 267 C ATOM 695 C ALA A 256 81.822 110.960 -13.017 1.00 35.68 C ANISOU 695 C ALA A 256 4672 4553 4332 -150 65 287 C ATOM 696 O ALA A 256 82.585 111.603 -13.741 1.00 35.49 O ANISOU 696 O ALA A 256 4657 4545 4284 -173 72 308 O ATOM 697 CB ALA A 256 82.363 108.676 -13.863 1.00 26.13 C ANISOU 697 CB ALA A 256 3384 3413 3132 -112 45 256 C ATOM 698 N THR A 257 80.655 111.463 -12.571 1.00 33.62 N ANISOU 698 N THR A 257 4443 4251 4081 -125 69 288 N ATOM 699 CA THR A 257 80.084 112.727 -13.063 1.00 30.04 C ANISOU 699 CA THR A 257 4040 3765 3609 -115 76 306 C ATOM 700 C THR A 257 80.210 113.774 -11.959 1.00 33.16 C ANISOU 700 C THR A 257 4499 4110 3989 -134 82 312 C ATOM 701 O THR A 257 79.399 113.808 -11.020 1.00 31.72 O ANISOU 701 O THR A 257 4339 3900 3814 -101 92 307 O ATOM 702 CB THR A 257 78.621 112.548 -13.504 1.00 25.92 C ANISOU 702 CB THR A 257 3507 3236 3105 -60 73 307 C ATOM 703 OG1 THR A 257 78.525 111.461 -14.441 1.00 27.98 O ANISOU 703 OG1 THR A 257 3719 3532 3378 -44 52 295 O ATOM 704 CG2 THR A 257 78.091 113.836 -14.185 1.00 21.62 C ANISOU 704 CG2 THR A 257 3014 2663 2538 -43 79 326 C ATOM 705 N ASN A 258 81.209 114.650 -12.094 1.00 29.87 N ANISOU 705 N ASN A 258 4119 3680 3551 -185 74 329 N ATOM 706 CA ASN A 258 81.553 115.604 -11.034 1.00 32.58 C ANISOU 706 CA ASN A 258 4537 3967 3877 -215 61 333 C ATOM 707 C ASN A 258 80.814 116.931 -11.221 1.00 37.37 C ANISOU 707 C ASN A 258 5227 4514 4459 -191 61 344 C ATOM 708 O ASN A 258 81.406 118.002 -11.378 1.00 41.88 O ANISOU 708 O ASN A 258 5856 5046 5011 -235 40 364 O ATOM 709 CB ASN A 258 83.062 115.822 -10.987 1.00 37.23 C ANISOU 709 CB ASN A 258 5118 4567 4462 -294 37 353 C ATOM 710 CG ASN A 258 83.812 114.593 -10.521 1.00 54.66 C ANISOU 710 CG ASN A 258 7255 6824 6690 -310 35 341 C ATOM 711 OD1 ASN A 258 84.217 113.757 -11.330 1.00 61.49 O ANISOU 711 OD1 ASN A 258 8048 7750 7564 -306 46 345 O ATOM 712 ND2 ASN A 258 83.996 114.471 -9.208 1.00 61.92 N ANISOU 712 ND2 ASN A 258 8203 7715 7610 -322 19 326 N ATOM 713 N ASP A 259 79.496 116.854 -11.197 1.00 39.50 N ANISOU 713 N ASP A 259 5500 4776 4733 -120 83 337 N ATOM 714 CA ASP A 259 78.689 118.051 -11.339 1.00 40.15 C ANISOU 714 CA ASP A 259 5660 4805 4791 -80 88 347 C ATOM 715 C ASP A 259 78.196 118.499 -9.960 1.00 49.22 C ANISOU 715 C ASP A 259 6884 5900 5917 -37 96 336 C ATOM 716 O ASP A 259 78.717 118.056 -8.925 1.00 51.10 O ANISOU 716 O ASP A 259 7127 6135 6153 -56 90 321 O ATOM 717 CB ASP A 259 77.559 117.786 -12.334 1.00 38.11 C ANISOU 717 CB ASP A 259 5354 4576 4549 -23 104 356 C ATOM 718 CG ASP A 259 76.642 116.667 -11.887 1.00 48.24 C ANISOU 718 CG ASP A 259 6569 5895 5866 26 122 350 C ATOM 719 OD1 ASP A 259 76.934 116.032 -10.854 1.00 44.63 O ANISOU 719 OD1 ASP A 259 6097 5444 5417 17 127 337 O ATOM 720 OD2 ASP A 259 75.630 116.419 -12.575 1.00 57.44 O ANISOU 720 OD2 ASP A 259 7692 7080 7051 70 126 362 O ATOM 721 N ASP A 260 77.200 119.390 -9.942 1.00 54.64 N ANISOU 721 N ASP A 260 7636 6544 6580 29 111 344 N ATOM 722 CA ASP A 260 76.632 119.881 -8.689 1.00 60.30 C ANISOU 722 CA ASP A 260 8437 7211 7263 93 127 336 C ATOM 723 C ASP A 260 76.207 118.735 -7.786 1.00 52.84 C ANISOU 723 C ASP A 260 7428 6310 6339 130 158 331 C ATOM 724 O ASP A 260 76.581 118.686 -6.609 1.00 55.79 O ANISOU 724 O ASP A 260 7853 6659 6687 132 155 315 O ATOM 725 CB ASP A 260 75.425 120.777 -8.973 1.00 74.68 C ANISOU 725 CB ASP A 260 10310 9001 9063 181 151 352 C ATOM 726 CG ASP A 260 75.788 122.243 -9.070 1.00 84.06 C ANISOU 726 CG ASP A 260 11631 10103 10204 169 118 351 C ATOM 727 OD1 ASP A 260 76.447 122.761 -8.142 1.00 87.60 O ANISOU 727 OD1 ASP A 260 12180 10489 10616 147 89 334 O ATOM 728 OD2 ASP A 260 75.392 122.882 -10.067 1.00 86.66 O ANISOU 728 OD2 ASP A 260 11971 10423 10533 183 116 369 O ATOM 729 N GLY A 261 75.427 117.797 -8.332 1.00 46.31 N ANISOU 729 N GLY A 261 6492 5546 5557 157 182 347 N ATOM 730 CA GLY A 261 74.722 116.742 -7.629 1.00 41.05 C ANISOU 730 CA GLY A 261 5755 4923 4920 200 213 358 C ATOM 731 C GLY A 261 75.537 115.544 -7.214 1.00 42.71 C ANISOU 731 C GLY A 261 5905 5168 5155 143 199 342 C ATOM 732 O GLY A 261 74.966 114.580 -6.703 1.00 53.58 O ANISOU 732 O GLY A 261 7215 6581 6562 171 221 357 O ATOM 733 N TYR A 262 76.858 115.588 -7.384 1.00 39.21 N ANISOU 733 N TYR A 262 5480 4715 4703 65 163 319 N ATOM 734 CA TYR A 262 77.687 114.406 -7.169 1.00 43.38 C ANISOU 734 CA TYR A 262 5942 5282 5257 14 147 306 C ATOM 735 C TYR A 262 77.523 113.841 -5.757 1.00 54.84 C ANISOU 735 C TYR A 262 7400 6733 6704 42 166 303 C ATOM 736 O TYR A 262 77.274 112.642 -5.580 1.00 55.21 O ANISOU 736 O TYR A 262 7367 6822 6788 46 175 310 O ATOM 737 CB TYR A 262 79.140 114.752 -7.447 1.00 34.85 C ANISOU 737 CB TYR A 262 4886 4191 4163 -66 110 293 C ATOM 738 CG TYR A 262 80.120 113.704 -6.998 1.00 41.73 C ANISOU 738 CG TYR A 262 5707 5097 5053 -113 94 280 C ATOM 739 CD1 TYR A 262 80.643 113.716 -5.713 1.00 36.65 C ANISOU 739 CD1 TYR A 262 5109 4428 4388 -126 83 270 C ATOM 740 CD2 TYR A 262 80.529 112.703 -7.865 1.00 42.02 C ANISOU 740 CD2 TYR A 262 5655 5189 5120 -137 87 279 C ATOM 741 CE1 TYR A 262 81.549 112.766 -5.309 1.00 46.07 C ANISOU 741 CE1 TYR A 262 6254 5653 5599 -167 66 261 C ATOM 742 CE2 TYR A 262 81.438 111.750 -7.471 1.00 52.03 C ANISOU 742 CE2 TYR A 262 6879 6488 6403 -171 74 269 C ATOM 743 CZ TYR A 262 81.944 111.784 -6.192 1.00 55.78 C ANISOU 743 CZ TYR A 262 7391 6940 6863 -188 63 262 C ATOM 744 OH TYR A 262 82.852 110.836 -5.796 1.00 55.61 O ANISOU 744 OH TYR A 262 7323 6949 6855 -219 48 254 O ATOM 745 N THR A 263 77.670 114.686 -4.735 1.00 56.74 N ANISOU 745 N THR A 263 7743 6922 6895 63 168 295 N ATOM 746 CA THR A 263 77.530 114.188 -3.369 1.00 61.69 C ANISOU 746 CA THR A 263 8388 7548 7505 98 189 294 C ATOM 747 C THR A 263 76.064 113.939 -3.013 1.00 58.92 C ANISOU 747 C THR A 263 8005 7220 7162 191 246 328 C ATOM 748 O THR A 263 75.745 112.934 -2.363 1.00 58.70 O ANISOU 748 O THR A 263 7919 7228 7157 210 269 345 O ATOM 749 CB THR A 263 78.192 115.149 -2.375 1.00 59.50 C ANISOU 749 CB THR A 263 8243 7202 7163 94 164 272 C ATOM 750 OG1 THR A 263 79.577 115.320 -2.720 1.00 51.18 O ANISOU 750 OG1 THR A 263 7198 6135 6115 -4 105 255 O ATOM 751 CG2 THR A 263 78.094 114.593 -0.945 1.00 50.13 C ANISOU 751 CG2 THR A 263 7081 6015 5949 136 184 270 C ATOM 752 N LYS A 264 75.158 114.823 -3.450 1.00 52.79 N ANISOU 752 N LYS A 264 7261 6427 6372 251 270 347 N ATOM 753 CA LYS A 264 73.731 114.614 -3.205 1.00 50.53 C ANISOU 753 CA LYS A 264 6927 6173 6100 342 327 393 C ATOM 754 C LYS A 264 73.271 113.244 -3.703 1.00 49.99 C ANISOU 754 C LYS A 264 6714 6169 6109 317 327 423 C ATOM 755 O LYS A 264 72.665 112.471 -2.952 1.00 39.88 O ANISOU 755 O LYS A 264 5379 4923 4850 353 361 459 O ATOM 756 CB LYS A 264 72.911 115.732 -3.855 1.00 56.08 C ANISOU 756 CB LYS A 264 7671 6854 6785 402 343 410 C ATOM 757 CG LYS A 264 72.918 117.026 -3.057 1.00 73.74 C ANISOU 757 CG LYS A 264 10058 9021 8937 468 357 395 C ATOM 758 CD LYS A 264 72.490 118.245 -3.861 1.00 82.12 C ANISOU 758 CD LYS A 264 11183 10044 9977 502 352 397 C ATOM 759 CE LYS A 264 73.678 118.871 -4.569 1.00 85.61 C ANISOU 759 CE LYS A 264 11684 10435 10408 405 286 358 C ATOM 760 NZ LYS A 264 74.987 118.679 -3.866 1.00 88.33 N ANISOU 760 NZ LYS A 264 12078 10751 10732 329 243 322 N ATOM 761 N ARG A 265 73.571 112.915 -4.962 1.00 45.52 N ANISOU 761 N ARG A 265 6091 5620 5586 255 285 411 N ATOM 762 CA ARG A 265 73.148 111.627 -5.503 1.00 37.59 C ANISOU 762 CA ARG A 265 4968 4664 4652 230 269 434 C ATOM 763 C ARG A 265 73.664 110.476 -4.661 1.00 49.20 C ANISOU 763 C ARG A 265 6403 6153 6139 199 264 429 C ATOM 764 O ARG A 265 72.948 109.492 -4.437 1.00 47.74 O ANISOU 764 O ARG A 265 6135 6000 6003 210 272 468 O ATOM 765 CB ARG A 265 73.624 111.469 -6.937 1.00 35.23 C ANISOU 765 CB ARG A 265 4640 4371 4375 172 219 409 C ATOM 766 CG ARG A 265 72.931 112.389 -7.912 1.00 29.03 C ANISOU 766 CG ARG A 265 3870 3575 3585 203 219 423 C ATOM 767 CD ARG A 265 73.211 111.921 -9.326 1.00 34.28 C ANISOU 767 CD ARG A 265 4491 4257 4277 156 170 408 C ATOM 768 NE ARG A 265 74.645 111.905 -9.622 1.00 34.53 N ANISOU 768 NE ARG A 265 4556 4281 4281 95 146 365 N ATOM 769 CZ ARG A 265 75.341 112.959 -10.048 1.00 37.44 C ANISOU 769 CZ ARG A 265 4993 4625 4609 75 143 349 C ATOM 770 NH1 ARG A 265 74.734 114.129 -10.213 1.00 31.70 N ANISOU 770 NH1 ARG A 265 4320 3868 3858 114 159 364 N ATOM 771 NH2 ARG A 265 76.650 112.848 -10.292 1.00 33.26 N ANISOU 771 NH2 ARG A 265 4475 4100 4062 17 123 324 N ATOM 772 N GLN A 266 74.906 110.577 -4.190 1.00 44.74 N ANISOU 772 N GLN A 266 5896 5565 5537 157 247 386 N ATOM 773 CA GLN A 266 75.446 109.528 -3.340 1.00 47.50 C ANISOU 773 CA GLN A 266 6220 5931 5899 131 241 380 C ATOM 774 C GLN A 266 74.689 109.448 -2.019 1.00 37.11 C ANISOU 774 C GLN A 266 4916 4618 4566 198 293 418 C ATOM 775 O GLN A 266 74.444 108.349 -1.511 1.00 40.01 O ANISOU 775 O GLN A 266 5219 5015 4969 196 300 444 O ATOM 776 CB GLN A 266 76.940 109.766 -3.104 1.00 52.63 C ANISOU 776 CB GLN A 266 6929 6557 6513 74 208 333 C ATOM 777 CG GLN A 266 77.859 109.126 -4.152 1.00 56.43 C ANISOU 777 CG GLN A 266 7358 7060 7023 7 163 309 C ATOM 778 CD GLN A 266 79.345 109.266 -3.799 1.00 54.94 C ANISOU 778 CD GLN A 266 7207 6860 6806 -49 134 278 C ATOM 779 OE1 GLN A 266 79.943 108.372 -3.194 1.00 42.40 O ANISOU 779 OE1 GLN A 266 5595 5288 5229 -70 122 270 O ATOM 780 NE2 GLN A 266 79.940 110.397 -4.179 1.00 55.94 N ANISOU 780 NE2 GLN A 266 7394 6960 6902 -75 119 267 N ATOM 781 N GLU A 267 74.316 110.596 -1.445 1.00 38.77 N ANISOU 781 N GLU A 267 5213 4799 4717 262 330 423 N ATOM 782 CA GLU A 267 73.623 110.582 -0.158 1.00 47.43 C ANISOU 782 CA GLU A 267 6335 5904 5784 343 388 461 C ATOM 783 C GLU A 267 72.203 110.065 -0.301 1.00 43.18 C ANISOU 783 C GLU A 267 5693 5416 5299 396 431 535 C ATOM 784 O GLU A 267 71.745 109.262 0.519 1.00 50.51 O ANISOU 784 O GLU A 267 6569 6377 6245 422 465 582 O ATOM 785 CB GLU A 267 73.625 111.974 0.470 1.00 55.92 C ANISOU 785 CB GLU A 267 7549 6927 6771 410 411 443 C ATOM 786 CG GLU A 267 74.914 112.265 1.203 1.00 72.24 C ANISOU 786 CG GLU A 267 9721 8945 8781 368 371 388 C ATOM 787 CD GLU A 267 75.333 113.714 1.119 1.00 82.89 C ANISOU 787 CD GLU A 267 11205 10224 10065 377 344 351 C ATOM 788 OE1 GLU A 267 74.439 114.593 1.094 1.00 75.06 O ANISOU 788 OE1 GLU A 267 10266 9215 9039 462 383 369 O ATOM 789 OE2 GLU A 267 76.561 113.964 1.059 1.00 95.20 O ANISOU 789 OE2 GLU A 267 12815 11746 11610 297 282 308 O ATOM 790 N LYS A 268 71.492 110.519 -1.333 1.00 39.88 N ANISOU 790 N LYS A 268 5238 5004 4908 409 429 554 N ATOM 791 CA LYS A 268 70.176 109.972 -1.634 1.00 41.39 C ANISOU 791 CA LYS A 268 5314 5246 5167 443 453 631 C ATOM 792 C LYS A 268 70.262 108.463 -1.838 1.00 43.51 C ANISOU 792 C LYS A 268 5475 5545 5513 370 412 650 C ATOM 793 O LYS A 268 69.475 107.695 -1.272 1.00 41.05 O ANISOU 793 O LYS A 268 5083 5271 5244 393 440 720 O ATOM 794 CB LYS A 268 69.606 110.686 -2.862 1.00 43.64 C ANISOU 794 CB LYS A 268 5584 5527 5470 452 436 637 C ATOM 795 CG LYS A 268 68.407 110.021 -3.481 1.00 52.83 C ANISOU 795 CG LYS A 268 6617 6738 6718 457 429 711 C ATOM 796 CD LYS A 268 67.293 111.019 -3.804 1.00 46.82 C ANISOU 796 CD LYS A 268 5852 5988 5949 542 469 759 C ATOM 797 CE LYS A 268 67.700 111.976 -4.899 1.00 43.45 C ANISOU 797 CE LYS A 268 5495 5521 5494 523 431 702 C ATOM 798 NZ LYS A 268 66.567 112.215 -5.825 1.00 42.53 N ANISOU 798 NZ LYS A 268 5306 5429 5424 554 422 756 N ATOM 799 N LEU A 269 71.261 108.022 -2.597 1.00 44.38 N ANISOU 799 N LEU A 269 5588 5636 5638 286 346 590 N ATOM 800 CA LEU A 269 71.503 106.595 -2.783 1.00 46.97 C ANISOU 800 CA LEU A 269 5838 5980 6029 222 298 594 C ATOM 801 C LEU A 269 71.844 105.910 -1.461 1.00 47.25 C ANISOU 801 C LEU A 269 5878 6022 6051 226 324 606 C ATOM 802 O LEU A 269 71.325 104.828 -1.152 1.00 37.46 O ANISOU 802 O LEU A 269 4559 4808 4869 214 320 659 O ATOM 803 CB LEU A 269 72.622 106.433 -3.809 1.00 52.65 C ANISOU 803 CB LEU A 269 6581 6678 6745 152 234 522 C ATOM 804 CG LEU A 269 73.269 105.111 -4.156 1.00 57.89 C ANISOU 804 CG LEU A 269 7201 7345 7449 89 176 499 C ATOM 805 CD1 LEU A 269 72.239 104.172 -4.729 1.00 58.50 C ANISOU 805 CD1 LEU A 269 7186 7436 7604 77 138 550 C ATOM 806 CD2 LEU A 269 74.342 105.411 -5.181 1.00 62.29 C ANISOU 806 CD2 LEU A 269 7800 7887 7979 49 136 434 C ATOM 807 N LYS A 270 72.704 106.532 -0.656 1.00 42.42 N ANISOU 807 N LYS A 270 5365 5386 5366 240 345 562 N ATOM 808 CA LYS A 270 73.022 105.961 0.645 1.00 41.08 C ANISOU 808 CA LYS A 270 5211 5222 5174 251 370 574 C ATOM 809 C LYS A 270 71.777 105.876 1.526 1.00 39.59 C ANISOU 809 C LYS A 270 4984 5067 4991 331 441 660 C ATOM 810 O LYS A 270 71.580 104.882 2.236 1.00 36.56 O ANISOU 810 O LYS A 270 4547 4707 4636 327 453 705 O ATOM 811 CB LYS A 270 74.120 106.790 1.321 1.00 47.38 C ANISOU 811 CB LYS A 270 6133 5982 5889 255 370 512 C ATOM 812 CG LYS A 270 74.567 106.271 2.677 1.00 46.37 C ANISOU 812 CG LYS A 270 6038 5853 5726 268 386 515 C ATOM 813 CD LYS A 270 73.793 106.936 3.820 1.00 45.49 C ANISOU 813 CD LYS A 270 5988 5743 5551 371 461 556 C ATOM 814 CE LYS A 270 74.039 108.424 3.871 1.00 47.54 C ANISOU 814 CE LYS A 270 6376 5956 5732 412 465 513 C ATOM 815 NZ LYS A 270 73.224 109.088 4.937 1.00 49.81 N ANISOU 815 NZ LYS A 270 6736 6243 5947 532 541 552 N ATOM 816 N ASN A 271 70.928 106.913 1.500 1.00 36.89 N ANISOU 816 N ASN A 271 4666 4730 4619 408 491 690 N ATOM 817 CA ASN A 271 69.707 106.884 2.310 1.00 41.36 C ANISOU 817 CA ASN A 271 5188 5340 5188 498 570 784 C ATOM 818 C ASN A 271 68.733 105.812 1.825 1.00 41.65 C ANISOU 818 C ASN A 271 5071 5424 5331 466 557 870 C ATOM 819 O ASN A 271 68.144 105.093 2.643 1.00 43.38 O ANISOU 819 O ASN A 271 5225 5682 5576 491 598 950 O ATOM 820 CB ASN A 271 69.027 108.251 2.311 1.00 37.98 C ANISOU 820 CB ASN A 271 4822 4907 4701 597 626 797 C ATOM 821 CG ASN A 271 69.846 109.312 3.020 1.00 39.60 C ANISOU 821 CG ASN A 271 5192 5058 4795 641 639 727 C ATOM 822 OD1 ASN A 271 70.763 109.001 3.777 1.00 46.66 O ANISOU 822 OD1 ASN A 271 6147 5929 5651 613 622 685 O ATOM 823 ND2 ASN A 271 69.518 110.578 2.773 1.00 41.87 N ANISOU 823 ND2 ASN A 271 5558 5319 5031 708 661 713 N ATOM 824 N PHE A 272 68.543 105.699 0.504 1.00 37.96 N ANISOU 824 N PHE A 272 4547 4951 4926 410 495 859 N ATOM 825 CA PHE A 272 67.690 104.654 -0.061 1.00 42.89 C ANISOU 825 CA PHE A 272 5036 5606 5656 365 456 934 C ATOM 826 C PHE A 272 68.102 103.277 0.450 1.00 50.41 C ANISOU 826 C PHE A 272 5945 6559 6649 303 423 947 C ATOM 827 O PHE A 272 67.284 102.529 1.000 1.00 47.64 O ANISOU 827 O PHE A 272 5502 6244 6353 310 445 1045 O ATOM 828 CB PHE A 272 67.758 104.671 -1.594 1.00 39.94 C ANISOU 828 CB PHE A 272 4641 5210 5325 304 374 892 C ATOM 829 CG PHE A 272 67.021 105.819 -2.252 1.00 40.32 C ANISOU 829 CG PHE A 272 4695 5264 5360 359 397 908 C ATOM 830 CD1 PHE A 272 66.272 106.722 -1.506 1.00 37.65 C ANISOU 830 CD1 PHE A 272 4373 4953 4979 464 487 962 C ATOM 831 CD2 PHE A 272 67.104 105.994 -3.634 1.00 37.22 C ANISOU 831 CD2 PHE A 272 4300 4851 4992 315 327 867 C ATOM 832 CE1 PHE A 272 65.610 107.779 -2.128 1.00 45.55 C ANISOU 832 CE1 PHE A 272 5383 5958 5966 521 506 976 C ATOM 833 CE2 PHE A 272 66.453 107.044 -4.267 1.00 39.90 C ANISOU 833 CE2 PHE A 272 4648 5195 5319 365 344 881 C ATOM 834 CZ PHE A 272 65.697 107.939 -3.511 1.00 44.96 C ANISOU 834 CZ PHE A 272 5301 5860 5921 467 433 936 C ATOM 835 N ILE A 273 69.377 102.921 0.256 1.00 45.27 N ANISOU 835 N ILE A 273 5356 5869 5976 241 369 855 N ATOM 836 CA ILE A 273 69.847 101.600 0.673 1.00 45.49 C ANISOU 836 CA ILE A 273 5352 5891 6040 184 330 859 C ATOM 837 C ILE A 273 69.749 101.451 2.186 1.00 39.38 C ANISOU 837 C ILE A 273 4592 5141 5230 235 404 909 C ATOM 838 O ILE A 273 69.333 100.406 2.688 1.00 41.62 O ANISOU 838 O ILE A 273 4803 5443 5568 215 401 980 O ATOM 839 CB ILE A 273 71.285 101.347 0.176 1.00 37.41 C ANISOU 839 CB ILE A 273 4396 4828 4990 123 265 752 C ATOM 840 CG1 ILE A 273 71.369 101.521 -1.338 1.00 39.82 C ANISOU 840 CG1 ILE A 273 4695 5115 5321 85 201 707 C ATOM 841 CG2 ILE A 273 71.771 99.941 0.604 1.00 38.66 C ANISOU 841 CG2 ILE A 273 4525 4977 5185 72 223 756 C ATOM 842 CD1 ILE A 273 72.775 101.392 -1.892 1.00 41.27 C ANISOU 842 CD1 ILE A 273 4940 5270 5471 40 150 611 C ATOM 843 N SER A 274 70.129 102.496 2.933 1.00 43.15 N ANISOU 843 N SER A 274 5169 5613 5612 302 465 874 N ATOM 844 CA SER A 274 70.099 102.434 4.393 1.00 50.10 C ANISOU 844 CA SER A 274 6085 6511 6439 363 535 912 C ATOM 845 C SER A 274 68.714 102.057 4.915 1.00 52.50 C ANISOU 845 C SER A 274 6286 6872 6789 417 600 1045 C ATOM 846 O SER A 274 68.588 101.295 5.881 1.00 48.78 O ANISOU 846 O SER A 274 5786 6425 6323 427 632 1104 O ATOM 847 CB SER A 274 70.523 103.781 4.975 1.00 45.00 C ANISOU 847 CB SER A 274 5573 5843 5680 439 584 858 C ATOM 848 OG SER A 274 71.920 103.967 4.866 1.00 46.57 O ANISOU 848 OG SER A 274 5863 5994 5835 385 527 753 O ATOM 849 N SER A 275 67.662 102.577 4.286 1.00 43.72 N ANISOU 849 N SER A 275 5112 5787 5712 452 622 1101 N ATOM 850 CA SER A 275 66.312 102.347 4.788 1.00 48.20 C ANISOU 850 CA SER A 275 5572 6420 6322 511 692 1241 C ATOM 851 C SER A 275 65.835 100.924 4.534 1.00 48.42 C ANISOU 851 C SER A 275 5462 6465 6469 424 636 1324 C ATOM 852 O SER A 275 64.932 100.449 5.231 1.00 42.93 O ANISOU 852 O SER A 275 4675 5824 5813 457 692 1451 O ATOM 853 CB SER A 275 65.340 103.357 4.159 1.00 43.68 C ANISOU 853 CB SER A 275 4970 5873 5754 577 728 1280 C ATOM 854 OG SER A 275 65.181 103.135 2.769 1.00 39.26 O ANISOU 854 OG SER A 275 4346 5294 5276 494 637 1261 O ATOM 855 N GLN A 276 66.421 100.229 3.568 1.00 48.83 N ANISOU 855 N GLN A 276 5503 6471 6579 317 526 1260 N ATOM 856 CA GLN A 276 66.009 98.870 3.248 1.00 47.85 C ANISOU 856 CA GLN A 276 5267 6346 6567 229 452 1329 C ATOM 857 C GLN A 276 67.170 97.898 3.412 1.00 45.45 C ANISOU 857 C GLN A 276 5015 5994 6259 156 386 1255 C ATOM 858 O GLN A 276 67.265 96.896 2.697 1.00 43.48 O ANISOU 858 O GLN A 276 4723 5711 6087 69 286 1250 O ATOM 859 CB GLN A 276 65.436 98.803 1.834 1.00 47.72 C ANISOU 859 CB GLN A 276 5184 6316 6632 173 367 1337 C ATOM 860 CG GLN A 276 64.145 99.572 1.675 1.00 55.86 C ANISOU 860 CG GLN A 276 6136 7401 7688 238 424 1434 C ATOM 861 CD GLN A 276 62.988 98.875 2.352 1.00 66.44 C ANISOU 861 CD GLN A 276 7337 8800 9108 245 460 1601 C ATOM 862 OE1 GLN A 276 62.685 97.715 2.063 1.00 72.93 O ANISOU 862 OE1 GLN A 276 8071 9608 10030 154 376 1660 O ATOM 863 NE2 GLN A 276 62.346 99.573 3.273 1.00 69.05 N ANISOU 863 NE2 GLN A 276 7650 9195 9391 357 586 1681 N ATOM 864 N MET A 277 68.047 98.175 4.375 1.00 41.22 N ANISOU 864 N MET A 277 4576 5453 5633 197 437 1200 N ATOM 865 CA MET A 277 69.350 97.525 4.378 1.00 48.43 C ANISOU 865 CA MET A 277 5556 6318 6526 137 373 1105 C ATOM 866 C MET A 277 69.226 96.012 4.546 1.00 46.15 C ANISOU 866 C MET A 277 5196 6018 6320 68 314 1164 C ATOM 867 O MET A 277 69.813 95.244 3.773 1.00 36.24 O ANISOU 867 O MET A 277 3946 4718 5105 -6 218 1107 O ATOM 868 CB MET A 277 70.243 98.126 5.463 1.00 47.98 C ANISOU 868 CB MET A 277 5612 6258 6359 194 433 1048 C ATOM 869 CG MET A 277 71.591 97.424 5.577 1.00 48.81 C ANISOU 869 CG MET A 277 5775 6323 6447 137 371 963 C ATOM 870 SD MET A 277 72.824 98.035 4.403 1.00 49.73 S ANISOU 870 SD MET A 277 5969 6397 6530 96 303 823 S ATOM 871 CE MET A 277 72.329 97.273 2.892 1.00 53.93 C ANISOU 871 CE MET A 277 6415 6913 7163 26 213 833 C ATOM 872 N THR A 278 68.461 95.565 5.545 1.00 36.29 N ANISOU 872 N THR A 278 3883 4809 5095 94 372 1281 N ATOM 873 CA THR A 278 68.346 94.131 5.795 1.00 41.81 C ANISOU 873 CA THR A 278 4518 5493 5873 25 316 1346 C ATOM 874 C THR A 278 67.800 93.403 4.575 1.00 48.71 C ANISOU 874 C THR A 278 5313 6336 6859 -61 205 1372 C ATOM 875 O THR A 278 68.378 92.412 4.114 1.00 48.96 O ANISOU 875 O THR A 278 5361 6312 6929 -134 105 1327 O ATOM 876 CB THR A 278 67.449 93.872 7.007 1.00 43.68 C ANISOU 876 CB THR A 278 4685 5788 6123 71 405 1490 C ATOM 877 OG1 THR A 278 68.030 94.469 8.172 1.00 50.12 O ANISOU 877 OG1 THR A 278 5594 6624 6824 155 498 1457 O ATOM 878 CG2 THR A 278 67.298 92.379 7.241 1.00 39.62 C ANISOU 878 CG2 THR A 278 4103 5254 5699 -9 340 1567 C ATOM 879 N ASP A 279 66.692 93.894 4.027 1.00 43.18 N ANISOU 879 N ASP A 279 4532 5667 6206 -49 217 1444 N ATOM 880 CA ASP A 279 66.043 93.176 2.942 1.00 41.17 C ANISOU 880 CA ASP A 279 4198 5381 6062 -132 103 1486 C ATOM 881 C ASP A 279 66.855 93.229 1.653 1.00 46.08 C ANISOU 881 C ASP A 279 4898 5941 6669 -173 5 1348 C ATOM 882 O ASP A 279 66.811 92.277 0.862 1.00 42.80 O ANISOU 882 O ASP A 279 4466 5473 6325 -250 -115 1344 O ATOM 883 CB ASP A 279 64.635 93.730 2.741 1.00 59.83 C ANISOU 883 CB ASP A 279 6449 7803 8482 -104 143 1607 C ATOM 884 CG ASP A 279 63.673 93.254 3.823 1.00 78.99 C ANISOU 884 CG ASP A 279 8763 10288 10961 -89 210 1778 C ATOM 885 OD1 ASP A 279 62.985 94.100 4.434 1.00 82.11 O ANISOU 885 OD1 ASP A 279 9119 10758 11323 3 329 1854 O ATOM 886 OD2 ASP A 279 63.628 92.029 4.079 1.00 85.62 O ANISOU 886 OD2 ASP A 279 9558 11101 11872 -164 145 1837 O ATOM 887 N MET A 280 67.616 94.309 1.427 1.00 38.59 N ANISOU 887 N MET A 280 4042 4996 5626 -120 50 1239 N ATOM 888 CA MET A 280 68.469 94.354 0.242 1.00 39.06 C ANISOU 888 CA MET A 280 4174 5003 5662 -152 -32 1115 C ATOM 889 C MET A 280 69.661 93.412 0.372 1.00 39.17 C ANISOU 889 C MET A 280 4255 4971 5657 -189 -88 1039 C ATOM 890 O MET A 280 70.098 92.827 -0.628 1.00 41.36 O ANISOU 890 O MET A 280 4562 5198 5953 -233 -187 976 O ATOM 891 CB MET A 280 68.948 95.784 -0.026 1.00 39.69 C ANISOU 891 CB MET A 280 4327 5100 5651 -91 31 1033 C ATOM 892 CG MET A 280 67.883 96.726 -0.604 1.00 42.33 C ANISOU 892 CG MET A 280 4613 5466 6005 -57 57 1082 C ATOM 893 SD MET A 280 68.603 98.346 -0.995 1.00 46.31 S ANISOU 893 SD MET A 280 5223 5973 6401 4 114 974 S ATOM 894 CE MET A 280 69.472 97.999 -2.538 1.00 34.71 C ANISOU 894 CE MET A 280 3804 4449 4934 -57 0 865 C ATOM 895 N CYS A 281 70.205 93.259 1.578 1.00 38.97 N ANISOU 895 N CYS A 281 4258 4961 5588 -165 -27 1042 N ATOM 896 CA CYS A 281 71.278 92.288 1.772 1.00 40.42 C ANISOU 896 CA CYS A 281 4495 5104 5760 -198 -81 982 C ATOM 897 C CYS A 281 70.794 90.870 1.545 1.00 38.96 C ANISOU 897 C CYS A 281 4258 4876 5670 -266 -178 1044 C ATOM 898 O CYS A 281 71.515 90.056 0.960 1.00 39.79 O ANISOU 898 O CYS A 281 4410 4927 5782 -301 -268 977 O ATOM 899 CB CYS A 281 71.886 92.411 3.166 1.00 45.12 C ANISOU 899 CB CYS A 281 5130 5723 6290 -158 0 983 C ATOM 900 SG CYS A 281 72.634 93.996 3.493 1.00 47.39 S ANISOU 900 SG CYS A 281 5504 6041 6461 -87 90 901 S ATOM 901 N LEU A 282 69.582 90.550 2.001 1.00 33.55 N ANISOU 901 N LEU A 282 3476 4213 5059 -283 -165 1176 N ATOM 902 CA LEU A 282 69.065 89.193 1.874 1.00 40.15 C ANISOU 902 CA LEU A 282 4258 5003 5994 -359 -266 1250 C ATOM 903 C LEU A 282 68.604 88.870 0.464 1.00 45.72 C ANISOU 903 C LEU A 282 4949 5657 6764 -413 -389 1237 C ATOM 904 O LEU A 282 68.342 87.701 0.165 1.00 46.61 O ANISOU 904 O LEU A 282 5046 5711 6954 -481 -501 1274 O ATOM 905 CB LEU A 282 67.912 88.973 2.860 1.00 36.20 C ANISOU 905 CB LEU A 282 3647 4550 5555 -363 -208 1413 C ATOM 906 CG LEU A 282 68.318 89.086 4.327 1.00 45.33 C ANISOU 906 CG LEU A 282 4825 5750 6648 -309 -96 1438 C ATOM 907 CD1 LEU A 282 67.101 89.084 5.229 1.00 42.12 C ANISOU 907 CD1 LEU A 282 4306 5408 6290 -292 -18 1606 C ATOM 908 CD2 LEU A 282 69.262 87.933 4.687 1.00 48.82 C ANISOU 908 CD2 LEU A 282 5326 6135 7087 -347 -159 1394 C ATOM 909 N ASP A 283 68.514 89.865 -0.406 1.00 40.16 N ANISOU 909 N ASP A 283 4261 4970 6029 -383 -377 1183 N ATOM 910 CA ASP A 283 68.020 89.647 -1.752 1.00 42.26 C ANISOU 910 CA ASP A 283 4518 5191 6348 -427 -492 1173 C ATOM 911 C ASP A 283 69.184 89.295 -2.666 1.00 38.73 C ANISOU 911 C ASP A 283 4186 4683 5848 -428 -570 1033 C ATOM 912 O ASP A 283 70.250 89.914 -2.606 1.00 34.19 O ANISOU 912 O ASP A 283 3684 4126 5180 -377 -507 935 O ATOM 913 CB ASP A 283 67.282 90.888 -2.260 1.00 34.65 C ANISOU 913 CB ASP A 283 3512 4277 5377 -390 -441 1193 C ATOM 914 CG ASP A 283 66.643 90.672 -3.602 1.00 36.57 C ANISOU 914 CG ASP A 283 3739 4477 5680 -436 -564 1196 C ATOM 915 OD1 ASP A 283 65.453 90.291 -3.642 1.00 46.93 O ANISOU 915 OD1 ASP A 283 4950 5791 7092 -484 -614 1318 O ATOM 916 OD2 ASP A 283 67.319 90.912 -4.618 1.00 44.10 O ANISOU 916 OD2 ASP A 283 4779 5396 6580 -423 -610 1083 O ATOM 917 N LYS A 284 68.969 88.290 -3.512 1.00 35.90 N ANISOU 917 N LYS A 284 3844 4250 5546 -484 -712 1030 N ATOM 918 CA LYS A 284 70.045 87.792 -4.356 1.00 32.82 C ANISOU 918 CA LYS A 284 3568 3799 5103 -474 -790 906 C ATOM 919 C LYS A 284 70.572 88.873 -5.287 1.00 35.07 C ANISOU 919 C LYS A 284 3909 4108 5306 -420 -754 807 C ATOM 920 O LYS A 284 71.773 88.906 -5.581 1.00 33.27 O ANISOU 920 O LYS A 284 3767 3873 5000 -381 -743 703 O ATOM 921 CB LYS A 284 69.548 86.577 -5.139 1.00 40.06 C ANISOU 921 CB LYS A 284 4502 4624 6095 -539 -957 927 C ATOM 922 CG LYS A 284 70.297 86.264 -6.409 1.00 43.88 C ANISOU 922 CG LYS A 284 5104 5044 6524 -516 -1052 806 C ATOM 923 CD LYS A 284 70.037 84.820 -6.823 1.00 47.33 C ANISOU 923 CD LYS A 284 5585 5375 7024 -575 -1220 822 C ATOM 924 CE LYS A 284 70.997 84.358 -7.919 1.00 49.02 C ANISOU 924 CE LYS A 284 5940 5522 7162 -529 -1304 692 C ATOM 925 NZ LYS A 284 70.719 82.937 -8.298 1.00 47.90 N ANISOU 925 NZ LYS A 284 5859 5263 7076 -581 -1478 705 N ATOM 926 N PHE A 285 69.713 89.789 -5.731 1.00 29.90 N ANISOU 926 N PHE A 285 3203 3489 4670 -415 -730 846 N ATOM 927 CA PHE A 285 70.161 90.784 -6.699 1.00 33.99 C ANISOU 927 CA PHE A 285 3775 4023 5114 -368 -707 759 C ATOM 928 C PHE A 285 70.559 92.107 -6.056 1.00 36.62 C ANISOU 928 C PHE A 285 4104 4430 5379 -313 -562 742 C ATOM 929 O PHE A 285 71.637 92.626 -6.360 1.00 32.01 O ANISOU 929 O PHE A 285 3592 3856 4713 -274 -525 649 O ATOM 930 CB PHE A 285 69.076 90.974 -7.768 1.00 32.07 C ANISOU 930 CB PHE A 285 3499 3761 4923 -393 -788 796 C ATOM 931 CG PHE A 285 68.647 89.664 -8.377 1.00 40.13 C ANISOU 931 CG PHE A 285 4535 4698 6014 -454 -948 817 C ATOM 932 CD1 PHE A 285 69.542 88.931 -9.164 1.00 40.98 C ANISOU 932 CD1 PHE A 285 4757 4740 6073 -442 -1036 716 C ATOM 933 CD2 PHE A 285 67.400 89.116 -8.096 1.00 41.40 C ANISOU 933 CD2 PHE A 285 4600 4844 6287 -520 -1013 941 C ATOM 934 CE1 PHE A 285 69.180 87.692 -9.707 1.00 43.13 C ANISOU 934 CE1 PHE A 285 5065 4921 6402 -493 -1195 728 C ATOM 935 CE2 PHE A 285 67.025 87.871 -8.629 1.00 42.61 C ANISOU 935 CE2 PHE A 285 4775 4906 6508 -586 -1178 963 C ATOM 936 CZ PHE A 285 67.923 87.157 -9.433 1.00 43.59 C ANISOU 936 CZ PHE A 285 5031 4953 6576 -571 -1273 850 C ATOM 937 N ALA A 286 69.752 92.621 -5.122 1.00 34.55 N ANISOU 937 N ALA A 286 3763 4218 5148 -306 -481 833 N ATOM 938 CA ALA A 286 70.089 93.855 -4.415 1.00 27.86 C ANISOU 938 CA ALA A 286 2926 3429 4231 -249 -351 818 C ATOM 939 C ALA A 286 71.397 93.752 -3.630 1.00 37.33 C ANISOU 939 C ALA A 286 4190 4632 5361 -229 -301 752 C ATOM 940 O ALA A 286 72.085 94.764 -3.450 1.00 30.55 O ANISOU 940 O ALA A 286 3379 3801 4427 -188 -228 697 O ATOM 941 CB ALA A 286 68.958 94.234 -3.466 1.00 25.13 C ANISOU 941 CB ALA A 286 2489 3132 3927 -234 -276 936 C ATOM 942 N CYS A 287 71.751 92.560 -3.126 1.00 35.81 N ANISOU 942 N CYS A 287 4001 4409 5195 -259 -345 760 N ATOM 943 CA CYS A 287 73.010 92.454 -2.393 1.00 31.66 C ANISOU 943 CA CYS A 287 3535 3889 4605 -239 -303 699 C ATOM 944 C CYS A 287 74.207 92.750 -3.288 1.00 33.45 C ANISOU 944 C CYS A 287 3839 4106 4765 -220 -323 588 C ATOM 945 O CYS A 287 75.275 93.115 -2.778 1.00 36.12 O ANISOU 945 O CYS A 287 4221 4464 5040 -196 -271 537 O ATOM 946 CB CYS A 287 73.155 91.071 -1.737 1.00 34.86 C ANISOU 946 CB CYS A 287 3931 4261 5052 -273 -352 731 C ATOM 947 SG CYS A 287 73.691 89.721 -2.840 1.00 36.62 S ANISOU 947 SG CYS A 287 4210 4406 5299 -305 -493 669 S ATOM 948 N ARG A 288 74.049 92.624 -4.610 1.00 31.39 N ANISOU 948 N ARG A 288 3596 3816 4515 -228 -396 555 N ATOM 949 CA ARG A 288 75.122 93.016 -5.519 1.00 33.03 C ANISOU 949 CA ARG A 288 3871 4025 4653 -200 -401 461 C ATOM 950 C ARG A 288 75.211 94.532 -5.635 1.00 33.46 C ANISOU 950 C ARG A 288 3932 4125 4658 -171 -320 445 C ATOM 951 O ARG A 288 76.311 95.090 -5.697 1.00 33.08 O ANISOU 951 O ARG A 288 3928 4098 4544 -149 -281 387 O ATOM 952 CB ARG A 288 74.914 92.381 -6.896 1.00 32.83 C ANISOU 952 CB ARG A 288 3876 3953 4645 -207 -506 431 C ATOM 953 CG ARG A 288 74.812 90.881 -6.867 1.00 38.42 C ANISOU 953 CG ARG A 288 4596 4601 5401 -236 -603 442 C ATOM 954 CD ARG A 288 76.111 90.215 -6.429 1.00 38.85 C ANISOU 954 CD ARG A 288 4700 4651 5411 -213 -597 388 C ATOM 955 NE ARG A 288 75.971 88.761 -6.532 1.00 41.28 N ANISOU 955 NE ARG A 288 5033 4888 5762 -236 -702 395 N ATOM 956 CZ ARG A 288 76.925 87.938 -6.948 1.00 38.87 C ANISOU 956 CZ ARG A 288 4800 4550 5418 -205 -753 330 C ATOM 957 NH1 ARG A 288 78.117 88.411 -7.281 1.00 36.36 N ANISOU 957 NH1 ARG A 288 4524 4272 5020 -150 -700 259 N ATOM 958 NH2 ARG A 288 76.681 86.639 -7.024 1.00 44.28 N ANISOU 958 NH2 ARG A 288 5517 5161 6146 -227 -857 341 N ATOM 959 N VAL A 289 74.060 95.211 -5.676 1.00 31.97 N ANISOU 959 N VAL A 289 3698 3950 4500 -171 -297 502 N ATOM 960 CA VAL A 289 74.040 96.672 -5.653 1.00 32.15 C ANISOU 960 CA VAL A 289 3731 4008 4475 -139 -219 495 C ATOM 961 C VAL A 289 74.732 97.189 -4.391 1.00 39.35 C ANISOU 961 C VAL A 289 4666 4946 5339 -121 -137 488 C ATOM 962 O VAL A 289 75.460 98.187 -4.433 1.00 37.63 O ANISOU 962 O VAL A 289 4495 4744 5061 -102 -94 444 O ATOM 963 CB VAL A 289 72.583 97.183 -5.781 1.00 34.92 C ANISOU 963 CB VAL A 289 4023 4370 4874 -134 -209 570 C ATOM 964 CG1 VAL A 289 72.461 98.701 -5.507 1.00 31.90 C ANISOU 964 CG1 VAL A 289 3657 4021 4442 -91 -120 572 C ATOM 965 CG2 VAL A 289 72.002 96.832 -7.171 1.00 23.46 C ANISOU 965 CG2 VAL A 289 2562 2890 3460 -154 -301 567 C ATOM 966 N ILE A 290 74.573 96.483 -3.265 1.00 33.75 N ANISOU 966 N ILE A 290 3930 4237 4655 -129 -124 532 N ATOM 967 CA ILE A 290 75.193 96.935 -2.020 1.00 36.86 C ANISOU 967 CA ILE A 290 4355 4652 5000 -107 -54 527 C ATOM 968 C ILE A 290 76.706 96.761 -2.079 1.00 28.75 C ANISOU 968 C ILE A 290 3382 3619 3924 -115 -70 450 C ATOM 969 O ILE A 290 77.466 97.679 -1.759 1.00 33.27 O ANISOU 969 O ILE A 290 3999 4205 4436 -101 -28 415 O ATOM 970 CB ILE A 290 74.596 96.195 -0.812 1.00 40.32 C ANISOU 970 CB ILE A 290 4751 5095 5474 -109 -33 601 C ATOM 971 CG1 ILE A 290 73.126 96.553 -0.635 1.00 46.52 C ANISOU 971 CG1 ILE A 290 5472 5901 6302 -90 2 691 C ATOM 972 CG2 ILE A 290 75.362 96.536 0.473 1.00 29.95 C ANISOU 972 CG2 ILE A 290 3485 3796 4099 -84 27 586 C ATOM 973 CD1 ILE A 290 72.359 95.452 0.034 1.00 51.39 C ANISOU 973 CD1 ILE A 290 6021 6518 6987 -112 -12 780 C ATOM 974 N GLN A 291 77.168 95.570 -2.456 1.00 28.75 N ANISOU 974 N GLN A 291 3380 3597 3947 -136 -134 428 N ATOM 975 CA GLN A 291 78.606 95.348 -2.535 1.00 37.57 C ANISOU 975 CA GLN A 291 4538 4717 5019 -135 -146 364 C ATOM 976 C GLN A 291 79.248 96.323 -3.512 1.00 40.66 C ANISOU 976 C GLN A 291 4960 5125 5365 -124 -136 314 C ATOM 977 O GLN A 291 80.358 96.813 -3.281 1.00 37.98 O ANISOU 977 O GLN A 291 4648 4805 4977 -121 -111 280 O ATOM 978 CB GLN A 291 78.887 93.907 -2.949 1.00 28.63 C ANISOU 978 CB GLN A 291 3405 3555 3919 -146 -221 348 C ATOM 979 CG GLN A 291 78.470 92.885 -1.908 1.00 35.35 C ANISOU 979 CG GLN A 291 4231 4387 4813 -162 -234 399 C ATOM 980 CD GLN A 291 78.654 91.474 -2.411 1.00 37.42 C ANISOU 980 CD GLN A 291 4504 4606 5109 -173 -321 384 C ATOM 981 OE1 GLN A 291 79.782 90.992 -2.536 1.00 39.55 O ANISOU 981 OE1 GLN A 291 4810 4873 5345 -156 -340 333 O ATOM 982 NE2 GLN A 291 77.545 90.806 -2.723 1.00 29.28 N ANISOU 982 NE2 GLN A 291 3444 3538 4144 -200 -378 433 N ATOM 983 N SER A 292 78.554 96.605 -4.612 1.00 36.50 N ANISOU 983 N SER A 292 4425 4590 4852 -121 -158 315 N ATOM 984 CA SER A 292 79.037 97.552 -5.601 1.00 37.92 C ANISOU 984 CA SER A 292 4632 4786 4989 -109 -146 277 C ATOM 985 C SER A 292 79.226 98.938 -4.994 1.00 32.35 C ANISOU 985 C SER A 292 3946 4100 4245 -106 -80 282 C ATOM 986 O SER A 292 80.282 99.562 -5.160 1.00 37.65 O ANISOU 986 O SER A 292 4647 4789 4872 -109 -64 250 O ATOM 987 CB SER A 292 78.047 97.591 -6.767 1.00 43.20 C ANISOU 987 CB SER A 292 5290 5439 5686 -105 -185 287 C ATOM 988 OG SER A 292 78.658 98.076 -7.935 1.00 52.66 O ANISOU 988 OG SER A 292 6520 6648 6841 -90 -192 245 O ATOM 989 N SER A 293 78.202 99.449 -4.305 1.00 30.94 N ANISOU 989 N SER A 293 3755 3918 4082 -97 -44 327 N ATOM 990 CA SER A 293 78.326 100.762 -3.679 1.00 33.74 C ANISOU 990 CA SER A 293 4148 4281 4392 -84 12 329 C ATOM 991 C SER A 293 79.416 100.772 -2.617 1.00 38.25 C ANISOU 991 C SER A 293 4752 4855 4926 -94 27 310 C ATOM 992 O SER A 293 80.166 101.749 -2.507 1.00 39.04 O ANISOU 992 O SER A 293 4896 4956 4980 -100 43 286 O ATOM 993 CB SER A 293 76.984 101.215 -3.087 1.00 35.42 C ANISOU 993 CB SER A 293 4345 4492 4622 -55 52 385 C ATOM 994 OG SER A 293 75.901 100.959 -3.977 1.00 36.10 O ANISOU 994 OG SER A 293 4383 4576 4757 -52 26 416 O ATOM 995 N LEU A 294 79.541 99.683 -1.845 1.00 34.79 N ANISOU 995 N LEU A 294 4294 4416 4509 -99 15 322 N ATOM 996 CA LEU A 294 80.514 99.657 -0.752 1.00 38.66 C ANISOU 996 CA LEU A 294 4816 4909 4965 -106 25 308 C ATOM 997 C LEU A 294 81.930 99.897 -1.254 1.00 35.07 C ANISOU 997 C LEU A 294 4379 4466 4479 -128 2 262 C ATOM 998 O LEU A 294 82.714 100.609 -0.610 1.00 27.24 O ANISOU 998 O LEU A 294 3426 3475 3448 -140 12 251 O ATOM 999 CB LEU A 294 80.448 98.325 -0.004 1.00 40.14 C ANISOU 999 CB LEU A 294 4976 5093 5184 -108 8 329 C ATOM 1000 CG LEU A 294 79.298 98.209 0.994 1.00 35.22 C ANISOU 1000 CG LEU A 294 4340 4467 4577 -85 45 389 C ATOM 1001 CD1 LEU A 294 79.081 96.757 1.387 1.00 35.72 C ANISOU 1001 CD1 LEU A 294 4362 4523 4688 -97 17 420 C ATOM 1002 CD2 LEU A 294 79.536 99.112 2.219 1.00 27.10 C ANISOU 1002 CD2 LEU A 294 3370 3439 3488 -61 93 392 C ATOM 1003 N GLN A 295 82.281 99.316 -2.401 1.00 29.83 N ANISOU 1003 N GLN A 295 3688 3813 3832 -133 -31 241 N ATOM 1004 CA GLN A 295 83.654 99.427 -2.863 1.00 41.42 C ANISOU 1004 CA GLN A 295 5159 5304 5273 -146 -44 211 C ATOM 1005 C GLN A 295 83.868 100.542 -3.874 1.00 33.10 C ANISOU 1005 C GLN A 295 4118 4262 4195 -152 -33 202 C ATOM 1006 O GLN A 295 85.016 100.925 -4.103 1.00 31.77 O ANISOU 1006 O GLN A 295 3951 4118 4002 -169 -35 192 O ATOM 1007 CB GLN A 295 84.137 98.095 -3.454 1.00 40.17 C ANISOU 1007 CB GLN A 295 4974 5156 5133 -132 -82 193 C ATOM 1008 CG GLN A 295 83.680 97.800 -4.849 1.00 44.74 C ANISOU 1008 CG GLN A 295 5546 5731 5722 -113 -105 180 C ATOM 1009 CD GLN A 295 83.996 96.367 -5.260 1.00 48.95 C ANISOU 1009 CD GLN A 295 6072 6258 6269 -89 -150 162 C ATOM 1010 OE1 GLN A 295 84.603 95.601 -4.496 1.00 48.72 O ANISOU 1010 OE1 GLN A 295 6037 6230 6243 -88 -161 160 O ATOM 1011 NE2 GLN A 295 83.575 95.994 -6.464 1.00 37.31 N ANISOU 1011 NE2 GLN A 295 4606 4771 4799 -66 -183 147 N ATOM 1012 N ASN A 296 82.808 101.088 -4.466 1.00 34.41 N ANISOU 1012 N ASN A 296 4290 4414 4370 -140 -22 212 N ATOM 1013 CA ASN A 296 82.983 102.141 -5.459 1.00 34.38 C ANISOU 1013 CA ASN A 296 4302 4419 4342 -144 -12 206 C ATOM 1014 C ASN A 296 82.600 103.529 -4.971 1.00 34.57 C ANISOU 1014 C ASN A 296 4369 4422 4344 -152 17 220 C ATOM 1015 O ASN A 296 83.199 104.505 -5.430 1.00 39.23 O ANISOU 1015 O ASN A 296 4981 5016 4907 -171 21 217 O ATOM 1016 CB ASN A 296 82.195 101.817 -6.736 1.00 37.10 C ANISOU 1016 CB ASN A 296 4630 4761 4704 -121 -29 203 C ATOM 1017 CG ASN A 296 82.714 100.576 -7.433 1.00 37.94 C ANISOU 1017 CG ASN A 296 4717 4882 4818 -105 -65 181 C ATOM 1018 OD1 ASN A 296 81.975 99.614 -7.653 1.00 46.31 O ANISOU 1018 OD1 ASN A 296 5765 5922 5909 -91 -99 181 O ATOM 1019 ND2 ASN A 296 83.997 100.579 -7.758 1.00 35.20 N ANISOU 1019 ND2 ASN A 296 4367 4568 4440 -106 -61 167 N ATOM 1020 N MET A 297 81.648 103.654 -4.047 1.00 31.64 N ANISOU 1020 N MET A 297 4014 4028 3981 -133 37 239 N ATOM 1021 CA MET A 297 81.256 104.981 -3.576 1.00 28.32 C ANISOU 1021 CA MET A 297 3649 3583 3528 -124 65 249 C ATOM 1022 C MET A 297 82.401 105.648 -2.813 1.00 37.77 C ANISOU 1022 C MET A 297 4897 4768 4686 -156 56 237 C ATOM 1023 O MET A 297 83.359 104.998 -2.382 1.00 31.84 O ANISOU 1023 O MET A 297 4130 4032 3937 -180 35 227 O ATOM 1024 CB MET A 297 80.057 104.902 -2.647 1.00 25.89 C ANISOU 1024 CB MET A 297 3348 3261 3229 -83 96 279 C ATOM 1025 CG MET A 297 78.715 104.646 -3.311 1.00 53.40 C ANISOU 1025 CG MET A 297 6786 6750 6753 -54 105 308 C ATOM 1026 SD MET A 297 77.384 104.762 -2.078 1.00 61.50 S ANISOU 1026 SD MET A 297 7814 7771 7781 2 156 361 S ATOM 1027 CE MET A 297 78.181 104.014 -0.671 1.00 45.45 C ANISOU 1027 CE MET A 297 5798 5738 5731 -9 157 355 C ATOM 1028 N ASP A 298 82.269 106.963 -2.607 1.00 31.35 N ANISOU 1028 N ASP A 298 4151 3922 3837 -154 66 239 N ATOM 1029 CA ASP A 298 83.201 107.664 -1.735 1.00 34.40 C ANISOU 1029 CA ASP A 298 4602 4283 4186 -185 45 231 C ATOM 1030 C ASP A 298 83.258 106.988 -0.370 1.00 35.76 C ANISOU 1030 C ASP A 298 4789 4450 4349 -170 46 230 C ATOM 1031 O ASP A 298 82.236 106.583 0.194 1.00 37.35 O ANISOU 1031 O ASP A 298 4989 4649 4554 -120 79 244 O ATOM 1032 CB ASP A 298 82.806 109.133 -1.598 1.00 35.53 C ANISOU 1032 CB ASP A 298 4835 4376 4289 -172 51 233 C ATOM 1033 CG ASP A 298 83.095 109.914 -2.856 1.00 39.85 C ANISOU 1033 CG ASP A 298 5377 4924 4840 -203 40 236 C ATOM 1034 OD1 ASP A 298 82.632 111.061 -2.978 1.00 46.66 O ANISOU 1034 OD1 ASP A 298 6307 5746 5675 -188 45 240 O ATOM 1035 OD2 ASP A 298 83.802 109.370 -3.729 1.00 45.98 O ANISOU 1035 OD2 ASP A 298 6086 5743 5642 -237 27 237 O ATOM 1036 N LEU A 299 84.475 106.839 0.142 1.00 31.34 N ANISOU 1036 N LEU A 299 4237 3893 3780 -214 9 220 N ATOM 1037 CA LEU A 299 84.674 106.049 1.350 1.00 34.08 C ANISOU 1037 CA LEU A 299 4591 4240 4119 -203 3 219 C ATOM 1038 C LEU A 299 83.786 106.533 2.492 1.00 36.12 C ANISOU 1038 C LEU A 299 4931 4459 4333 -149 31 225 C ATOM 1039 O LEU A 299 83.196 105.719 3.211 1.00 34.88 O ANISOU 1039 O LEU A 299 4758 4313 4181 -110 59 239 O ATOM 1040 CB LEU A 299 86.153 106.081 1.753 1.00 32.05 C ANISOU 1040 CB LEU A 299 4341 3985 3852 -261 -50 211 C ATOM 1041 CG LEU A 299 86.521 105.202 2.952 1.00 40.22 C ANISOU 1041 CG LEU A 299 5379 5024 4879 -254 -64 209 C ATOM 1042 CD1 LEU A 299 85.906 103.787 2.818 1.00 32.67 C ANISOU 1042 CD1 LEU A 299 4349 4101 3962 -218 -33 217 C ATOM 1043 CD2 LEU A 299 88.024 105.145 3.125 1.00 42.02 C ANISOU 1043 CD2 LEU A 299 5591 5266 5109 -314 -121 208 C ATOM 1044 N SER A 300 83.661 107.855 2.659 1.00 33.85 N ANISOU 1044 N SER A 300 4735 4125 4000 -141 26 219 N ATOM 1045 CA SER A 300 82.908 108.393 3.789 1.00 39.70 C ANISOU 1045 CA SER A 300 5573 4826 4684 -75 54 222 C ATOM 1046 C SER A 300 81.429 108.065 3.676 1.00 40.04 C ANISOU 1046 C SER A 300 5578 4892 4743 -1 124 252 C ATOM 1047 O SER A 300 80.767 107.795 4.686 1.00 44.35 O ANISOU 1047 O SER A 300 6152 5439 5262 62 163 272 O ATOM 1048 CB SER A 300 83.107 109.910 3.900 1.00 44.92 C ANISOU 1048 CB SER A 300 6354 5423 5291 -79 24 206 C ATOM 1049 OG SER A 300 84.487 110.250 3.915 1.00 48.95 O ANISOU 1049 OG SER A 300 6887 5913 5799 -162 -50 191 O ATOM 1050 N LEU A 301 80.884 108.087 2.462 1.00 37.70 N ANISOU 1050 N LEU A 301 5216 4618 4491 -5 139 262 N ATOM 1051 CA LEU A 301 79.506 107.642 2.299 1.00 40.86 C ANISOU 1051 CA LEU A 301 5559 5046 4920 55 195 300 C ATOM 1052 C LEU A 301 79.391 106.130 2.485 1.00 40.21 C ANISOU 1052 C LEU A 301 5384 5004 4889 44 198 322 C ATOM 1053 O LEU A 301 78.439 105.647 3.112 1.00 39.87 O ANISOU 1053 O LEU A 301 5317 4978 4855 96 242 364 O ATOM 1054 CB LEU A 301 78.976 108.087 0.940 1.00 43.77 C ANISOU 1054 CB LEU A 301 5888 5422 5320 50 198 305 C ATOM 1055 CG LEU A 301 78.566 109.561 1.015 1.00 58.68 C ANISOU 1055 CG LEU A 301 7874 7267 7155 94 215 302 C ATOM 1056 CD1 LEU A 301 78.970 110.369 -0.220 1.00 59.81 C ANISOU 1056 CD1 LEU A 301 8026 7395 7305 49 184 283 C ATOM 1057 CD2 LEU A 301 77.075 109.639 1.252 1.00 64.66 C ANISOU 1057 CD2 LEU A 301 8615 8039 7913 182 279 347 C ATOM 1058 N ALA A 302 80.374 105.370 1.982 1.00 35.20 N ANISOU 1058 N ALA A 302 4700 4387 4288 -18 153 298 N ATOM 1059 CA ALA A 302 80.363 103.919 2.165 1.00 33.69 C ANISOU 1059 CA ALA A 302 4435 4223 4142 -28 146 314 C ATOM 1060 C ALA A 302 80.366 103.549 3.643 1.00 34.89 C ANISOU 1060 C ALA A 302 4623 4369 4263 0 164 330 C ATOM 1061 O ALA A 302 79.654 102.628 4.060 1.00 35.48 O ANISOU 1061 O ALA A 302 4649 4463 4368 23 188 370 O ATOM 1062 CB ALA A 302 81.564 103.285 1.455 1.00 36.23 C ANISOU 1062 CB ALA A 302 4717 4561 4489 -86 95 282 C ATOM 1063 N CYS A 303 81.164 104.257 4.450 1.00 30.28 N ANISOU 1063 N CYS A 303 4127 3758 3619 -4 148 304 N ATOM 1064 CA CYS A 303 81.164 104.007 5.889 1.00 37.80 C ANISOU 1064 CA CYS A 303 5132 4701 4528 32 164 317 C ATOM 1065 C CYS A 303 79.783 104.210 6.496 1.00 42.61 C ANISOU 1065 C CYS A 303 5759 5316 5116 115 235 365 C ATOM 1066 O CYS A 303 79.385 103.462 7.395 1.00 39.39 O ANISOU 1066 O CYS A 303 5337 4925 4705 150 266 402 O ATOM 1067 CB CYS A 303 82.184 104.895 6.600 1.00 39.51 C ANISOU 1067 CB CYS A 303 5457 4878 4677 16 123 280 C ATOM 1068 SG CYS A 303 83.900 104.604 6.153 1.00 47.14 S ANISOU 1068 SG CYS A 303 6393 5850 5668 -79 42 243 S ATOM 1069 N LYS A 304 79.038 105.217 6.033 1.00 42.86 N ANISOU 1069 N LYS A 304 5817 5336 5131 153 265 372 N ATOM 1070 CA LYS A 304 77.720 105.448 6.624 1.00 47.02 C ANISOU 1070 CA LYS A 304 6355 5876 5635 245 340 426 C ATOM 1071 C LYS A 304 76.768 104.312 6.289 1.00 43.89 C ANISOU 1071 C LYS A 304 5830 5529 5319 247 370 489 C ATOM 1072 O LYS A 304 75.978 103.889 7.134 1.00 48.58 O ANISOU 1072 O LYS A 304 6405 6147 5906 305 425 550 O ATOM 1073 CB LYS A 304 77.148 106.792 6.166 1.00 49.56 C ANISOU 1073 CB LYS A 304 6735 6174 5922 291 363 420 C ATOM 1074 CG LYS A 304 77.906 107.990 6.718 1.00 50.76 C ANISOU 1074 CG LYS A 304 7036 6264 5985 302 333 369 C ATOM 1075 CD LYS A 304 77.436 109.301 6.094 1.00 61.96 C ANISOU 1075 CD LYS A 304 8515 7652 7377 337 343 358 C ATOM 1076 CE LYS A 304 78.224 110.492 6.649 1.00 68.43 C ANISOU 1076 CE LYS A 304 9494 8396 8110 340 297 308 C ATOM 1077 NZ LYS A 304 78.713 111.399 5.563 1.00 73.04 N ANISOU 1077 NZ LYS A 304 10100 8945 8708 279 246 275 N ATOM 1078 N LEU A 305 76.847 103.799 5.061 1.00 42.39 N ANISOU 1078 N LEU A 305 5554 5350 5202 184 330 480 N ATOM 1079 CA LEU A 305 76.071 102.628 4.670 1.00 41.63 C ANISOU 1079 CA LEU A 305 5343 5288 5189 169 332 535 C ATOM 1080 C LEU A 305 76.277 101.462 5.638 1.00 38.74 C ANISOU 1080 C LEU A 305 4953 4933 4834 161 332 563 C ATOM 1081 O LEU A 305 75.328 100.754 5.984 1.00 37.75 O ANISOU 1081 O LEU A 305 4759 4834 4749 183 365 637 O ATOM 1082 CB LEU A 305 76.465 102.227 3.246 1.00 41.67 C ANISOU 1082 CB LEU A 305 5291 5290 5253 100 270 500 C ATOM 1083 CG LEU A 305 75.531 101.257 2.546 1.00 49.52 C ANISOU 1083 CG LEU A 305 6180 6304 6331 83 254 551 C ATOM 1084 CD1 LEU A 305 74.129 101.808 2.627 1.00 50.41 C ANISOU 1084 CD1 LEU A 305 6262 6437 6455 141 311 620 C ATOM 1085 CD2 LEU A 305 75.973 101.064 1.094 1.00 47.48 C ANISOU 1085 CD2 LEU A 305 5896 6036 6109 30 191 505 C ATOM 1086 N VAL A 306 77.509 101.262 6.103 1.00 40.68 N ANISOU 1086 N VAL A 306 5251 5161 5046 129 295 512 N ATOM 1087 CA VAL A 306 77.782 100.167 7.031 1.00 42.14 C ANISOU 1087 CA VAL A 306 5421 5354 5238 123 291 535 C ATOM 1088 C VAL A 306 76.988 100.338 8.319 1.00 40.99 C ANISOU 1088 C VAL A 306 5308 5223 5045 201 363 596 C ATOM 1089 O VAL A 306 76.525 99.356 8.910 1.00 38.14 O ANISOU 1089 O VAL A 306 4895 4883 4713 210 384 658 O ATOM 1090 CB VAL A 306 79.295 100.068 7.310 1.00 38.09 C ANISOU 1090 CB VAL A 306 4962 4821 4691 80 235 469 C ATOM 1091 CG1 VAL A 306 79.569 99.066 8.431 1.00 34.52 C ANISOU 1091 CG1 VAL A 306 4511 4373 4231 86 235 494 C ATOM 1092 CG2 VAL A 306 80.039 99.669 6.028 1.00 34.73 C ANISOU 1092 CG2 VAL A 306 4485 4394 4315 14 173 424 C ATOM 1093 N GLN A 307 76.811 101.583 8.774 1.00 41.48 N ANISOU 1093 N GLN A 307 5461 5271 5027 264 404 584 N ATOM 1094 CA GLN A 307 76.100 101.819 10.030 1.00 40.12 C ANISOU 1094 CA GLN A 307 5338 5113 4792 358 480 639 C ATOM 1095 C GLN A 307 74.641 101.404 9.957 1.00 41.98 C ANISOU 1095 C GLN A 307 5472 5397 5081 402 547 741 C ATOM 1096 O GLN A 307 74.042 101.114 10.997 1.00 47.55 O ANISOU 1096 O GLN A 307 6178 6132 5758 469 612 811 O ATOM 1097 CB GLN A 307 76.187 103.289 10.423 1.00 35.73 C ANISOU 1097 CB GLN A 307 4915 4524 4136 425 501 600 C ATOM 1098 CG GLN A 307 77.594 103.739 10.672 1.00 42.69 C ANISOU 1098 CG GLN A 307 5902 5356 4963 380 429 515 C ATOM 1099 CD GLN A 307 78.389 102.690 11.445 1.00 52.70 C ANISOU 1099 CD GLN A 307 7164 6627 6233 345 397 511 C ATOM 1100 OE1 GLN A 307 78.123 102.448 12.621 1.00 58.15 O ANISOU 1100 OE1 GLN A 307 7900 7326 6869 408 438 547 O ATOM 1101 NE2 GLN A 307 79.360 102.055 10.780 1.00 45.13 N ANISOU 1101 NE2 GLN A 307 6151 5665 5332 251 325 472 N ATOM 1102 N ALA A 308 74.056 101.363 8.763 1.00 35.66 N ANISOU 1102 N ALA A 308 4582 4609 4358 368 532 757 N ATOM 1103 CA ALA A 308 72.663 100.946 8.659 1.00 40.15 C ANISOU 1103 CA ALA A 308 5041 5225 4989 400 584 864 C ATOM 1104 C ALA A 308 72.459 99.447 8.879 1.00 41.37 C ANISOU 1104 C ALA A 308 5096 5400 5222 349 564 929 C ATOM 1105 O ALA A 308 71.308 99.004 8.891 1.00 42.16 O ANISOU 1105 O ALA A 308 5097 5541 5382 366 602 1033 O ATOM 1106 CB ALA A 308 72.099 101.350 7.291 1.00 30.96 C ANISOU 1106 CB ALA A 308 3816 4063 3886 374 560 862 C ATOM 1107 N LEU A 309 73.512 98.650 9.039 1.00 38.64 N ANISOU 1107 N LEU A 309 4771 5028 4882 286 503 879 N ATOM 1108 CA LEU A 309 73.304 97.230 9.288 1.00 37.23 C ANISOU 1108 CA LEU A 309 4510 4861 4776 241 481 943 C ATOM 1109 C LEU A 309 72.588 97.037 10.621 1.00 36.33 C ANISOU 1109 C LEU A 309 4389 4786 4629 315 568 1042 C ATOM 1110 O LEU A 309 72.860 97.766 11.586 1.00 35.61 O ANISOU 1110 O LEU A 309 4398 4697 4435 390 622 1023 O ATOM 1111 CB LEU A 309 74.634 96.470 9.292 1.00 38.98 C ANISOU 1111 CB LEU A 309 4767 5046 4997 176 405 867 C ATOM 1112 CG LEU A 309 75.268 96.132 7.939 1.00 35.97 C ANISOU 1112 CG LEU A 309 4360 4635 4671 98 315 796 C ATOM 1113 CD1 LEU A 309 76.754 95.891 8.128 1.00 37.59 C ANISOU 1113 CD1 LEU A 309 4631 4813 4837 66 263 710 C ATOM 1114 CD2 LEU A 309 74.602 94.926 7.295 1.00 40.54 C ANISOU 1114 CD2 LEU A 309 4838 5212 5356 43 267 854 C ATOM 1115 N PRO A 310 71.679 96.067 10.722 1.00 41.52 N ANISOU 1115 N PRO A 310 4934 5473 5367 296 580 1153 N ATOM 1116 CA PRO A 310 70.961 95.845 11.982 1.00 44.00 C ANISOU 1116 CA PRO A 310 5230 5835 5653 369 672 1265 C ATOM 1117 C PRO A 310 71.897 95.325 13.063 1.00 48.28 C ANISOU 1117 C PRO A 310 5852 6360 6134 373 666 1235 C ATOM 1118 O PRO A 310 72.979 94.806 12.785 1.00 45.51 O ANISOU 1118 O PRO A 310 5535 5964 5794 303 582 1151 O ATOM 1119 CB PRO A 310 69.910 94.795 11.612 1.00 47.24 C ANISOU 1119 CB PRO A 310 5488 6272 6188 315 657 1389 C ATOM 1120 CG PRO A 310 70.559 94.024 10.483 1.00 48.22 C ANISOU 1120 CG PRO A 310 5589 6341 6392 200 531 1316 C ATOM 1121 CD PRO A 310 71.356 95.047 9.706 1.00 41.61 C ANISOU 1121 CD PRO A 310 4838 5471 5500 202 500 1182 C ATOM 1122 N ARG A 311 71.468 95.490 14.318 1.00 50.38 N ANISOU 1122 N ARG A 311 6150 6664 6329 466 760 1308 N ATOM 1123 CA ARG A 311 72.262 95.091 15.477 1.00 49.90 C ANISOU 1123 CA ARG A 311 6174 6590 6194 488 764 1289 C ATOM 1124 C ARG A 311 71.626 93.974 16.290 1.00 47.20 C ANISOU 1124 C ARG A 311 5753 6287 5892 492 807 1422 C ATOM 1125 O ARG A 311 72.173 93.599 17.330 1.00 57.29 O ANISOU 1125 O ARG A 311 7099 7561 7107 518 819 1422 O ATOM 1126 CB ARG A 311 72.510 96.291 16.401 1.00 44.01 C ANISOU 1126 CB ARG A 311 5575 5846 5302 603 831 1246 C ATOM 1127 CG ARG A 311 72.936 97.558 15.688 1.00 48.23 C ANISOU 1127 CG ARG A 311 6189 6344 5792 611 802 1137 C ATOM 1128 CD ARG A 311 74.199 97.328 14.888 1.00 48.48 C ANISOU 1128 CD ARG A 311 6242 6320 5860 501 685 1020 C ATOM 1129 NE ARG A 311 74.515 98.467 14.030 1.00 50.61 N ANISOU 1129 NE ARG A 311 6563 6560 6108 494 655 933 N ATOM 1130 CZ ARG A 311 75.303 99.473 14.394 1.00 51.30 C ANISOU 1130 CZ ARG A 311 6787 6608 6096 526 638 848 C ATOM 1131 NH1 ARG A 311 75.856 99.481 15.601 1.00 51.50 N ANISOU 1131 NH1 ARG A 311 6916 6619 6031 571 646 834 N ATOM 1132 NH2 ARG A 311 75.552 100.464 13.547 1.00 50.14 N ANISOU 1132 NH2 ARG A 311 6678 6433 5942 510 607 780 N ATOM 1133 N ASP A 312 70.478 93.452 15.869 1.00 44.22 N ANISOU 1133 N ASP A 312 5235 5949 5618 467 827 1542 N ATOM 1134 CA ASP A 312 69.759 92.429 16.615 1.00 53.06 C ANISOU 1134 CA ASP A 312 6265 7110 6787 467 871 1691 C ATOM 1135 C ASP A 312 69.896 91.086 15.891 1.00 47.96 C ANISOU 1135 C ASP A 312 5526 6423 6273 331 759 1707 C ATOM 1136 O ASP A 312 70.902 90.854 15.198 1.00 52.04 O ANISOU 1136 O ASP A 312 6091 6877 6805 258 656 1585 O ATOM 1137 CB ASP A 312 68.314 92.884 16.812 1.00 58.82 C ANISOU 1137 CB ASP A 312 6901 7918 7528 549 982 1835 C ATOM 1138 CG ASP A 312 67.672 93.389 15.530 1.00 62.92 C ANISOU 1138 CG ASP A 312 7340 8441 8126 516 953 1831 C ATOM 1139 OD1 ASP A 312 66.954 94.412 15.584 1.00 69.39 O ANISOU 1139 OD1 ASP A 312 8160 9308 8898 614 1041 1865 O ATOM 1140 OD2 ASP A 312 67.882 92.771 14.466 1.00 62.14 O ANISOU 1140 OD2 ASP A 312 7185 8296 8130 398 841 1792 O ATOM 1141 N ALA A 313 68.891 90.221 16.023 1.00 46.82 N ANISOU 1141 N ALA A 313 5253 6313 6224 299 775 1862 N ATOM 1142 CA ALA A 313 68.981 88.886 15.435 1.00 51.07 C ANISOU 1142 CA ALA A 313 5718 6802 6885 172 660 1886 C ATOM 1143 C ALA A 313 69.054 88.931 13.913 1.00 47.72 C ANISOU 1143 C ALA A 313 5262 6328 6540 89 554 1806 C ATOM 1144 O ALA A 313 69.535 87.973 13.290 1.00 46.75 O ANISOU 1144 O ALA A 313 5133 6141 6488 -7 438 1765 O ATOM 1145 CB ALA A 313 67.792 88.026 15.880 1.00 53.92 C ANISOU 1145 CB ALA A 313 5940 7208 7338 150 695 2084 C ATOM 1146 N ARG A 314 68.609 90.028 13.303 1.00 40.36 N ANISOU 1146 N ARG A 314 4322 5423 5591 132 589 1781 N ATOM 1147 CA ARG A 314 68.723 90.161 11.855 1.00 41.92 C ANISOU 1147 CA ARG A 314 4504 5575 5850 63 492 1699 C ATOM 1148 C ARG A 314 70.177 90.077 11.398 1.00 38.41 C ANISOU 1148 C ARG A 314 4170 5062 5361 25 408 1532 C ATOM 1149 O ARG A 314 70.469 89.496 10.349 1.00 44.04 O ANISOU 1149 O ARG A 314 4869 5722 6142 -56 299 1479 O ATOM 1150 CB ARG A 314 68.075 91.473 11.402 1.00 49.55 C ANISOU 1150 CB ARG A 314 5458 6584 6786 129 556 1697 C ATOM 1151 CG ARG A 314 66.535 91.467 11.505 1.00 52.77 C ANISOU 1151 CG ARG A 314 5723 7059 7266 152 619 1872 C ATOM 1152 CD ARG A 314 65.953 92.856 11.252 1.00 49.55 C ANISOU 1152 CD ARG A 314 5320 6699 6808 245 700 1868 C ATOM 1153 NE ARG A 314 66.236 93.776 12.357 1.00 51.94 N ANISOU 1153 NE ARG A 314 5727 7036 6970 373 818 1843 N ATOM 1154 CZ ARG A 314 66.194 95.103 12.260 1.00 53.65 C ANISOU 1154 CZ ARG A 314 6015 7269 7102 464 879 1786 C ATOM 1155 NH1 ARG A 314 65.896 95.679 11.098 1.00 54.97 N ANISOU 1155 NH1 ARG A 314 6152 7423 7309 440 837 1748 N ATOM 1156 NH2 ARG A 314 66.464 95.855 13.322 1.00 49.46 N ANISOU 1156 NH2 ARG A 314 5595 6759 6440 581 974 1764 N ATOM 1157 N LEU A 315 71.111 90.626 12.184 1.00 36.57 N ANISOU 1157 N LEU A 315 4049 4830 5014 86 453 1451 N ATOM 1158 CA LEU A 315 72.519 90.551 11.802 1.00 37.58 C ANISOU 1158 CA LEU A 315 4270 4904 5104 51 376 1306 C ATOM 1159 C LEU A 315 73.036 89.111 11.790 1.00 35.11 C ANISOU 1159 C LEU A 315 3943 4545 4851 -24 287 1308 C ATOM 1160 O LEU A 315 73.909 88.774 10.977 1.00 34.20 O ANISOU 1160 O LEU A 315 3862 4381 4752 -72 198 1209 O ATOM 1161 CB LEU A 315 73.373 91.409 12.736 1.00 43.63 C ANISOU 1161 CB LEU A 315 5155 5680 5742 126 433 1235 C ATOM 1162 CG LEU A 315 74.846 91.565 12.345 1.00 43.82 C ANISOU 1162 CG LEU A 315 5268 5659 5722 96 362 1092 C ATOM 1163 CD1 LEU A 315 74.980 92.186 10.961 1.00 40.94 C ANISOU 1163 CD1 LEU A 315 4895 5276 5383 64 316 1015 C ATOM 1164 CD2 LEU A 315 75.589 92.394 13.387 1.00 44.55 C ANISOU 1164 CD2 LEU A 315 5476 5759 5694 164 410 1040 C ATOM 1165 N ILE A 316 72.540 88.256 12.687 1.00 34.50 N ANISOU 1165 N ILE A 316 3823 4482 4805 -27 312 1421 N ATOM 1166 CA ILE A 316 72.864 86.832 12.599 1.00 41.46 C ANISOU 1166 CA ILE A 316 4685 5311 5756 -103 220 1437 C ATOM 1167 C ILE A 316 72.349 86.264 11.285 1.00 42.44 C ANISOU 1167 C ILE A 316 4740 5394 5993 -184 120 1448 C ATOM 1168 O ILE A 316 73.089 85.619 10.530 1.00 40.05 O ANISOU 1168 O ILE A 316 4472 5028 5715 -235 17 1365 O ATOM 1169 CB ILE A 316 72.280 86.057 13.794 1.00 48.39 C ANISOU 1169 CB ILE A 316 5519 6215 6653 -95 268 1576 C ATOM 1170 CG1 ILE A 316 72.903 86.519 15.103 1.00 44.20 C ANISOU 1170 CG1 ILE A 316 5077 5716 6001 -11 353 1555 C ATOM 1171 CG2 ILE A 316 72.487 84.550 13.601 1.00 45.10 C ANISOU 1171 CG2 ILE A 316 5079 5733 6322 -182 160 1603 C ATOM 1172 CD1 ILE A 316 72.175 85.985 16.315 1.00 47.67 C ANISOU 1172 CD1 ILE A 316 5472 6197 6442 19 427 1705 C ATOM 1173 N ALA A 317 71.063 86.512 10.994 1.00 33.56 N ANISOU 1173 N ALA A 317 3518 4303 4931 -191 148 1553 N ATOM 1174 CA ALA A 317 70.465 86.044 9.750 1.00 31.91 C ANISOU 1174 CA ALA A 317 3242 4053 4828 -269 47 1572 C ATOM 1175 C ALA A 317 71.239 86.535 8.539 1.00 39.04 C ANISOU 1175 C ALA A 317 4212 4918 5703 -276 -16 1421 C ATOM 1176 O ALA A 317 71.329 85.827 7.528 1.00 38.07 O ANISOU 1176 O ALA A 317 4089 4734 5644 -341 -131 1387 O ATOM 1177 CB ALA A 317 69.008 86.503 9.665 1.00 33.86 C ANISOU 1177 CB ALA A 317 3373 4357 5134 -261 101 1705 C ATOM 1178 N ILE A 318 71.816 87.734 8.627 1.00 38.40 N ANISOU 1178 N ILE A 318 4196 4870 5524 -209 54 1333 N ATOM 1179 CA ILE A 318 72.604 88.257 7.521 1.00 39.30 C ANISOU 1179 CA ILE A 318 4371 4955 5607 -213 4 1198 C ATOM 1180 C ILE A 318 73.892 87.457 7.364 1.00 42.99 C ANISOU 1180 C ILE A 318 4911 5369 6055 -239 -73 1102 C ATOM 1181 O ILE A 318 74.281 87.093 6.247 1.00 36.68 O ANISOU 1181 O ILE A 318 4131 4524 5282 -273 -162 1033 O ATOM 1182 CB ILE A 318 72.872 89.756 7.737 1.00 37.73 C ANISOU 1182 CB ILE A 318 4222 4802 5312 -139 96 1142 C ATOM 1183 CG1 ILE A 318 71.683 90.567 7.241 1.00 34.72 C ANISOU 1183 CG1 ILE A 318 3774 4456 4961 -120 137 1202 C ATOM 1184 CG2 ILE A 318 74.139 90.198 7.039 1.00 31.45 C ANISOU 1184 CG2 ILE A 318 3510 3979 4459 -139 56 999 C ATOM 1185 CD1 ILE A 318 71.770 92.019 7.578 1.00 28.74 C ANISOU 1185 CD1 ILE A 318 3069 3739 4110 -40 231 1166 C ATOM 1186 N CYS A 319 74.552 87.138 8.480 1.00 37.94 N ANISOU 1186 N CYS A 319 4313 4736 5367 -216 -41 1102 N ATOM 1187 CA CYS A 319 75.818 86.419 8.409 1.00 40.76 C ANISOU 1187 CA CYS A 319 4736 5049 5701 -230 -107 1015 C ATOM 1188 C CYS A 319 75.643 84.991 7.902 1.00 44.25 C ANISOU 1188 C CYS A 319 5156 5426 6229 -292 -215 1044 C ATOM 1189 O CYS A 319 76.542 84.467 7.233 1.00 38.93 O ANISOU 1189 O CYS A 319 4535 4708 5550 -302 -291 956 O ATOM 1190 CB CYS A 319 76.500 86.424 9.776 1.00 43.46 C ANISOU 1190 CB CYS A 319 5127 5413 5972 -190 -50 1016 C ATOM 1191 SG CYS A 319 77.146 88.080 10.262 1.00 48.10 S ANISOU 1191 SG CYS A 319 5783 6051 6440 -118 41 942 S ATOM 1192 N VAL A 320 74.504 84.350 8.183 1.00 38.45 N ANISOU 1192 N VAL A 320 4350 4686 5576 -331 -226 1168 N ATOM 1193 CA VAL A 320 74.298 82.963 7.779 1.00 37.36 C ANISOU 1193 CA VAL A 320 4199 4474 5523 -398 -341 1203 C ATOM 1194 C VAL A 320 73.532 82.853 6.467 1.00 41.23 C ANISOU 1194 C VAL A 320 4651 4926 6088 -447 -427 1212 C ATOM 1195 O VAL A 320 73.175 81.747 6.057 1.00 46.68 O ANISOU 1195 O VAL A 320 5332 5547 6858 -509 -536 1252 O ATOM 1196 CB VAL A 320 73.598 82.155 8.879 1.00 37.08 C ANISOU 1196 CB VAL A 320 4109 4441 5539 -426 -324 1343 C ATOM 1197 CG1 VAL A 320 74.293 82.379 10.217 1.00 33.68 C ANISOU 1197 CG1 VAL A 320 3721 4053 5022 -367 -232 1338 C ATOM 1198 CG2 VAL A 320 72.120 82.528 8.946 1.00 34.41 C ANISOU 1198 CG2 VAL A 320 3660 4148 5266 -445 -278 1479 C ATOM 1199 N ASP A 321 73.277 83.968 5.793 1.00 40.11 N ANISOU 1199 N ASP A 321 4496 4822 5923 -422 -388 1174 N ATOM 1200 CA ASP A 321 72.492 83.938 4.568 1.00 33.18 C ANISOU 1200 CA ASP A 321 3582 3913 5113 -465 -468 1186 C ATOM 1201 C ASP A 321 73.390 83.679 3.366 1.00 33.41 C ANISOU 1201 C ASP A 321 3697 3883 5115 -464 -561 1055 C ATOM 1202 O ASP A 321 74.510 84.187 3.291 1.00 32.61 O ANISOU 1202 O ASP A 321 3662 3800 4928 -412 -523 948 O ATOM 1203 CB ASP A 321 71.735 85.248 4.374 1.00 34.45 C ANISOU 1203 CB ASP A 321 3686 4141 5261 -434 -384 1214 C ATOM 1204 CG ASP A 321 70.787 85.189 3.186 1.00 45.54 C ANISOU 1204 CG ASP A 321 5042 5518 6745 -482 -469 1247 C ATOM 1205 OD1 ASP A 321 69.737 84.515 3.306 1.00 49.28 O ANISOU 1205 OD1 ASP A 321 5433 5975 7316 -541 -517 1371 O ATOM 1206 OD2 ASP A 321 71.108 85.794 2.136 1.00 39.01 O ANISOU 1206 OD2 ASP A 321 4257 4682 5883 -464 -493 1152 O ATOM 1207 N GLN A 322 72.877 82.892 2.420 1.00 35.15 N ANISOU 1207 N GLN A 322 3916 4032 5409 -519 -687 1070 N ATOM 1208 CA GLN A 322 73.627 82.535 1.218 1.00 40.37 C ANISOU 1208 CA GLN A 322 4667 4630 6041 -509 -784 953 C ATOM 1209 C GLN A 322 74.057 83.760 0.403 1.00 38.80 C ANISOU 1209 C GLN A 322 4495 4478 5771 -456 -731 859 C ATOM 1210 O GLN A 322 75.071 83.713 -0.308 1.00 35.25 O ANISOU 1210 O GLN A 322 4126 4006 5260 -418 -761 749 O ATOM 1211 CB GLN A 322 72.761 81.605 0.365 1.00 43.32 C ANISOU 1211 CB GLN A 322 5035 4918 6508 -579 -931 999 C ATOM 1212 CG GLN A 322 73.346 81.206 -0.977 1.00 47.57 C ANISOU 1212 CG GLN A 322 5675 5383 7016 -562 -1043 886 C ATOM 1213 CD GLN A 322 72.411 80.285 -1.754 1.00 56.34 C ANISOU 1213 CD GLN A 322 6790 6398 8220 -636 -1203 938 C ATOM 1214 OE1 GLN A 322 71.183 80.334 -1.588 1.00 55.34 O ANISOU 1214 OE1 GLN A 322 6565 6278 8182 -701 -1221 1057 O ATOM 1215 NE2 GLN A 322 72.990 79.424 -2.586 1.00 48.66 N ANISOU 1215 NE2 GLN A 322 5930 5333 7225 -623 -1325 854 N ATOM 1216 N ASN A 323 73.301 84.854 0.469 1.00 33.15 N ANISOU 1216 N ASN A 323 3712 3824 5058 -449 -653 904 N ATOM 1217 CA ASN A 323 73.652 86.053 -0.290 1.00 33.12 C ANISOU 1217 CA ASN A 323 3734 3860 4990 -403 -606 824 C ATOM 1218 C ASN A 323 74.263 87.140 0.583 1.00 30.65 C ANISOU 1218 C ASN A 323 3427 3621 4599 -349 -474 799 C ATOM 1219 O ASN A 323 75.304 87.709 0.237 1.00 35.11 O ANISOU 1219 O ASN A 323 4050 4201 5088 -309 -447 702 O ATOM 1220 CB ASN A 323 72.414 86.594 -1.013 1.00 30.42 C ANISOU 1220 CB ASN A 323 3328 3526 4702 -428 -625 881 C ATOM 1221 CG ASN A 323 71.932 85.654 -2.093 1.00 36.32 C ANISOU 1221 CG ASN A 323 4092 4193 5515 -479 -774 884 C ATOM 1222 OD1 ASN A 323 72.686 85.299 -3.009 1.00 41.03 O ANISOU 1222 OD1 ASN A 323 4776 4741 6072 -462 -845 786 O ATOM 1223 ND2 ASN A 323 70.689 85.206 -1.974 1.00 39.22 N ANISOU 1223 ND2 ASN A 323 4377 4542 5981 -541 -826 1002 N ATOM 1224 N ALA A 324 73.634 87.434 1.717 1.00 30.27 N ANISOU 1224 N ALA A 324 3321 3617 4564 -346 -393 889 N ATOM 1225 CA ALA A 324 74.063 88.557 2.536 1.00 31.92 C ANISOU 1225 CA ALA A 324 3546 3889 4695 -290 -275 869 C ATOM 1226 C ALA A 324 75.419 88.326 3.196 1.00 32.56 C ANISOU 1226 C ALA A 324 3695 3968 4709 -266 -258 799 C ATOM 1227 O ALA A 324 76.096 89.302 3.530 1.00 31.95 O ANISOU 1227 O ALA A 324 3656 3927 4556 -225 -190 747 O ATOM 1228 CB ALA A 324 72.991 88.853 3.594 1.00 30.21 C ANISOU 1228 CB ALA A 324 3257 3719 4503 -279 -194 989 C ATOM 1229 N ASN A 325 75.839 87.064 3.389 1.00 29.75 N ANISOU 1229 N ASN A 325 3358 3567 4380 -292 -325 799 N ATOM 1230 CA ASN A 325 77.158 86.823 3.971 1.00 33.45 C ANISOU 1230 CA ASN A 325 3887 4036 4787 -266 -315 735 C ATOM 1231 C ASN A 325 78.266 87.501 3.163 1.00 40.11 C ANISOU 1231 C ASN A 325 4784 4891 5565 -236 -315 624 C ATOM 1232 O ASN A 325 79.313 87.859 3.723 1.00 38.44 O ANISOU 1232 O ASN A 325 4609 4705 5291 -207 -276 577 O ATOM 1233 CB ASN A 325 77.431 85.317 4.091 1.00 25.20 C ANISOU 1233 CB ASN A 325 2860 2932 3784 -294 -400 746 C ATOM 1234 CG ASN A 325 77.933 84.697 2.778 1.00 35.60 C ANISOU 1234 CG ASN A 325 4223 4194 5109 -298 -500 669 C ATOM 1235 OD1 ASN A 325 79.124 84.766 2.460 1.00 34.29 O ANISOU 1235 OD1 ASN A 325 4111 4034 4885 -261 -503 581 O ATOM 1236 ND2 ASN A 325 77.015 84.091 2.005 1.00 31.08 N ANISOU 1236 ND2 ASN A 325 3631 3569 4608 -340 -584 707 N ATOM 1237 N HIS A 326 78.065 87.675 1.850 1.00 33.18 N ANISOU 1237 N HIS A 326 3908 3996 4702 -242 -361 586 N ATOM 1238 CA HIS A 326 79.062 88.357 1.026 1.00 32.99 C ANISOU 1238 CA HIS A 326 3927 3990 4617 -211 -354 494 C ATOM 1239 C HIS A 326 79.042 89.868 1.232 1.00 32.54 C ANISOU 1239 C HIS A 326 3864 3986 4512 -191 -268 487 C ATOM 1240 O HIS A 326 80.058 90.528 0.997 1.00 30.85 O ANISOU 1240 O HIS A 326 3683 3797 4240 -169 -245 424 O ATOM 1241 CB HIS A 326 78.852 88.028 -0.451 1.00 31.18 C ANISOU 1241 CB HIS A 326 3713 3724 4409 -216 -432 458 C ATOM 1242 CG HIS A 326 78.959 86.571 -0.752 1.00 34.74 C ANISOU 1242 CG HIS A 326 4194 4111 4897 -228 -530 453 C ATOM 1243 ND1 HIS A 326 80.166 85.956 -1.018 1.00 33.51 N ANISOU 1243 ND1 HIS A 326 4094 3940 4699 -193 -562 385 N ATOM 1244 CD2 HIS A 326 78.019 85.597 -0.796 1.00 31.78 C ANISOU 1244 CD2 HIS A 326 3802 3678 4596 -270 -606 512 C ATOM 1245 CE1 HIS A 326 79.961 84.667 -1.232 1.00 31.24 C ANISOU 1245 CE1 HIS A 326 3834 3583 4451 -206 -655 394 C ATOM 1246 NE2 HIS A 326 78.669 84.422 -1.100 1.00 32.76 N ANISOU 1246 NE2 HIS A 326 3985 3745 4718 -259 -688 471 N ATOM 1247 N VAL A 327 77.911 90.434 1.658 1.00 26.32 N ANISOU 1247 N VAL A 327 3036 3217 3749 -196 -221 555 N ATOM 1248 CA VAL A 327 77.898 91.844 2.044 1.00 28.65 C ANISOU 1248 CA VAL A 327 3341 3554 3991 -167 -138 550 C ATOM 1249 C VAL A 327 78.850 92.080 3.212 1.00 34.84 C ANISOU 1249 C VAL A 327 4166 4357 4714 -147 -95 530 C ATOM 1250 O VAL A 327 79.666 93.015 3.193 1.00 32.59 O ANISOU 1250 O VAL A 327 3922 4091 4370 -132 -68 477 O ATOM 1251 CB VAL A 327 76.467 92.308 2.380 1.00 33.10 C ANISOU 1251 CB VAL A 327 3852 4135 4587 -161 -92 636 C ATOM 1252 CG1 VAL A 327 76.476 93.780 2.895 1.00 27.64 C ANISOU 1252 CG1 VAL A 327 3191 3481 3829 -118 -5 628 C ATOM 1253 CG2 VAL A 327 75.560 92.168 1.164 1.00 30.78 C ANISOU 1253 CG2 VAL A 327 3516 3824 4354 -185 -145 656 C ATOM 1254 N ILE A 328 78.762 91.231 4.247 1.00 29.31 N ANISOU 1254 N ILE A 328 3458 3650 4029 -151 -93 576 N ATOM 1255 CA ILE A 328 79.632 91.387 5.412 1.00 31.16 C ANISOU 1255 CA ILE A 328 3736 3898 4204 -131 -59 560 C ATOM 1256 C ILE A 328 81.092 91.216 5.011 1.00 27.79 C ANISOU 1256 C ILE A 328 3346 3468 3746 -135 -102 479 C ATOM 1257 O ILE A 328 81.961 91.986 5.431 1.00 30.39 O ANISOU 1257 O ILE A 328 3714 3816 4016 -122 -78 441 O ATOM 1258 CB ILE A 328 79.234 90.401 6.528 1.00 37.36 C ANISOU 1258 CB ILE A 328 4504 4676 5014 -133 -54 631 C ATOM 1259 CG1 ILE A 328 77.785 90.640 6.965 1.00 33.63 C ANISOU 1259 CG1 ILE A 328 3984 4221 4572 -122 1 727 C ATOM 1260 CG2 ILE A 328 80.189 90.542 7.726 1.00 38.04 C ANISOU 1260 CG2 ILE A 328 4645 4775 5034 -109 -27 610 C ATOM 1261 CD1 ILE A 328 77.490 92.116 7.300 1.00 33.05 C ANISOU 1261 CD1 ILE A 328 3937 4183 4437 -75 81 726 C ATOM 1262 N GLN A 329 81.386 90.208 4.188 1.00 29.25 N ANISOU 1262 N GLN A 329 3520 3626 3968 -150 -168 456 N ATOM 1263 CA GLN A 329 82.766 90.008 3.762 1.00 30.89 C ANISOU 1263 CA GLN A 329 3754 3838 4144 -141 -201 387 C ATOM 1264 C GLN A 329 83.251 91.172 2.898 1.00 27.50 C ANISOU 1264 C GLN A 329 3334 3436 3677 -134 -182 339 C ATOM 1265 O GLN A 329 84.418 91.558 2.976 1.00 32.15 O ANISOU 1265 O GLN A 329 3941 4050 4225 -127 -178 300 O ATOM 1266 CB GLN A 329 82.893 88.670 3.030 1.00 23.04 C ANISOU 1266 CB GLN A 329 2759 2807 3190 -143 -275 374 C ATOM 1267 CG GLN A 329 82.813 87.464 3.988 1.00 31.81 C ANISOU 1267 CG GLN A 329 3871 3887 4328 -150 -302 415 C ATOM 1268 CD GLN A 329 82.926 86.123 3.278 1.00 30.87 C ANISOU 1268 CD GLN A 329 3767 3717 4247 -150 -386 399 C ATOM 1269 OE1 GLN A 329 84.029 85.630 3.020 1.00 28.13 O ANISOU 1269 OE1 GLN A 329 3448 3368 3872 -121 -416 349 O ATOM 1270 NE2 GLN A 329 81.777 85.520 2.967 1.00 27.74 N ANISOU 1270 NE2 GLN A 329 3351 3275 3912 -180 -429 447 N ATOM 1271 N LYS A 330 82.369 91.745 2.072 1.00 22.27 N ANISOU 1271 N LYS A 330 2656 2772 3033 -139 -173 347 N ATOM 1272 CA LYS A 330 82.731 92.947 1.322 1.00 26.06 C ANISOU 1272 CA LYS A 330 3148 3276 3477 -134 -150 310 C ATOM 1273 C LYS A 330 83.043 94.115 2.255 1.00 23.75 C ANISOU 1273 C LYS A 330 2882 3005 3136 -132 -97 312 C ATOM 1274 O LYS A 330 84.017 94.848 2.042 1.00 29.28 O ANISOU 1274 O LYS A 330 3602 3726 3798 -136 -93 276 O ATOM 1275 CB LYS A 330 81.607 93.339 0.362 1.00 26.16 C ANISOU 1275 CB LYS A 330 3141 3279 3519 -137 -151 325 C ATOM 1276 CG LYS A 330 81.951 94.581 -0.464 1.00 32.88 C ANISOU 1276 CG LYS A 330 4007 4153 4333 -132 -128 290 C ATOM 1277 CD LYS A 330 83.146 94.279 -1.358 1.00 32.97 C ANISOU 1277 CD LYS A 330 4028 4177 4321 -123 -159 239 C ATOM 1278 CE LYS A 330 82.774 93.242 -2.414 1.00 33.57 C ANISOU 1278 CE LYS A 330 4100 4226 4430 -112 -217 228 C ATOM 1279 NZ LYS A 330 83.927 92.906 -3.281 1.00 34.32 N ANISOU 1279 NZ LYS A 330 4210 4338 4493 -84 -240 181 N ATOM 1280 N VAL A 331 82.196 94.332 3.270 1.00 25.53 N ANISOU 1280 N VAL A 331 3112 3226 3361 -124 -59 359 N ATOM 1281 CA VAL A 331 82.456 95.386 4.254 1.00 28.17 C ANISOU 1281 CA VAL A 331 3494 3571 3639 -112 -16 359 C ATOM 1282 C VAL A 331 83.846 95.222 4.843 1.00 30.85 C ANISOU 1282 C VAL A 331 3861 3917 3943 -122 -41 326 C ATOM 1283 O VAL A 331 84.634 96.172 4.932 1.00 26.98 O ANISOU 1283 O VAL A 331 3407 3435 3410 -131 -40 297 O ATOM 1284 CB VAL A 331 81.400 95.358 5.372 1.00 29.02 C ANISOU 1284 CB VAL A 331 3606 3675 3744 -86 30 420 C ATOM 1285 CG1 VAL A 331 81.872 96.231 6.544 1.00 25.34 C ANISOU 1285 CG1 VAL A 331 3211 3211 3206 -64 62 412 C ATOM 1286 CG2 VAL A 331 80.043 95.820 4.860 1.00 22.77 C ANISOU 1286 CG2 VAL A 331 2783 2887 2981 -71 63 461 C ATOM 1287 N VAL A 332 84.152 94.004 5.279 1.00 30.27 N ANISOU 1287 N VAL A 332 3772 3838 3890 -123 -68 336 N ATOM 1288 CA VAL A 332 85.434 93.738 5.904 1.00 35.75 C ANISOU 1288 CA VAL A 332 4487 4542 4556 -128 -94 312 C ATOM 1289 C VAL A 332 86.577 94.017 4.935 1.00 33.62 C ANISOU 1289 C VAL A 332 4203 4294 4279 -142 -123 267 C ATOM 1290 O VAL A 332 87.645 94.481 5.342 1.00 30.41 O ANISOU 1290 O VAL A 332 3812 3902 3839 -154 -136 251 O ATOM 1291 CB VAL A 332 85.427 92.287 6.432 1.00 40.82 C ANISOU 1291 CB VAL A 332 5112 5170 5227 -122 -120 335 C ATOM 1292 CG1 VAL A 332 86.827 91.786 6.707 1.00 35.50 C ANISOU 1292 CG1 VAL A 332 4443 4508 4536 -123 -158 306 C ATOM 1293 CG2 VAL A 332 84.542 92.195 7.695 1.00 30.63 C ANISOU 1293 CG2 VAL A 332 3841 3868 3927 -107 -82 389 C ATOM 1294 N ALA A 333 86.368 93.782 3.641 1.00 28.73 N ANISOU 1294 N ALA A 333 3551 3676 3688 -139 -134 253 N ATOM 1295 CA ALA A 333 87.458 93.974 2.692 1.00 31.72 C ANISOU 1295 CA ALA A 333 3913 4085 4056 -141 -153 220 C ATOM 1296 C ALA A 333 87.687 95.439 2.321 1.00 31.32 C ANISOU 1296 C ALA A 333 3873 4049 3976 -161 -131 211 C ATOM 1297 O ALA A 333 88.813 95.805 1.990 1.00 36.74 O ANISOU 1297 O ALA A 333 4546 4767 4646 -173 -143 199 O ATOM 1298 CB ALA A 333 87.194 93.157 1.426 1.00 27.72 C ANISOU 1298 CB ALA A 333 3382 3572 3579 -120 -176 205 C ATOM 1299 N VAL A 334 86.665 96.300 2.343 1.00 27.98 N ANISOU 1299 N VAL A 334 3474 3609 3550 -164 -101 223 N ATOM 1300 CA VAL A 334 86.874 97.618 1.736 1.00 34.25 C ANISOU 1300 CA VAL A 334 4282 4412 4320 -181 -87 213 C ATOM 1301 C VAL A 334 86.507 98.787 2.641 1.00 33.74 C ANISOU 1301 C VAL A 334 4275 4325 4221 -189 -65 224 C ATOM 1302 O VAL A 334 86.456 99.933 2.183 1.00 32.93 O ANISOU 1302 O VAL A 334 4195 4217 4100 -202 -55 219 O ATOM 1303 CB VAL A 334 86.108 97.739 0.405 1.00 32.85 C ANISOU 1303 CB VAL A 334 4084 4235 4164 -170 -78 209 C ATOM 1304 CG1 VAL A 334 86.478 96.591 -0.526 1.00 35.37 C ANISOU 1304 CG1 VAL A 334 4365 4567 4505 -151 -106 193 C ATOM 1305 CG2 VAL A 334 84.569 97.807 0.640 1.00 25.58 C ANISOU 1305 CG2 VAL A 334 3171 3285 3262 -154 -53 235 C ATOM 1306 N ILE A 335 86.263 98.529 3.919 1.00 32.68 N ANISOU 1306 N ILE A 335 4173 4173 4071 -177 -59 238 N ATOM 1307 CA ILE A 335 85.887 99.595 4.846 1.00 27.47 C ANISOU 1307 CA ILE A 335 3586 3488 3365 -168 -38 246 C ATOM 1308 C ILE A 335 86.877 99.546 6.004 1.00 27.53 C ANISOU 1308 C ILE A 335 3635 3489 3337 -182 -70 239 C ATOM 1309 O ILE A 335 87.212 98.442 6.462 1.00 27.20 O ANISOU 1309 O ILE A 335 3566 3459 3311 -177 -85 246 O ATOM 1310 CB ILE A 335 84.442 99.417 5.343 1.00 25.93 C ANISOU 1310 CB ILE A 335 3400 3279 3174 -123 10 279 C ATOM 1311 CG1 ILE A 335 83.463 99.360 4.160 1.00 28.41 C ANISOU 1311 CG1 ILE A 335 3663 3600 3531 -115 29 291 C ATOM 1312 CG2 ILE A 335 84.081 100.506 6.381 1.00 23.39 C ANISOU 1312 CG2 ILE A 335 3167 2930 2788 -93 37 286 C ATOM 1313 CD1 ILE A 335 83.264 100.742 3.455 1.00 24.43 C ANISOU 1313 CD1 ILE A 335 3191 3087 3005 -117 43 277 C ATOM 1314 N PRO A 336 87.350 100.679 6.527 1.00 28.30 N ANISOU 1314 N PRO A 336 3803 3563 3387 -199 -89 229 N ATOM 1315 CA PRO A 336 88.266 100.623 7.676 1.00 25.55 C ANISOU 1315 CA PRO A 336 3500 3203 3004 -214 -132 224 C ATOM 1316 C PRO A 336 87.576 100.060 8.908 1.00 29.86 C ANISOU 1316 C PRO A 336 4089 3735 3522 -165 -105 241 C ATOM 1317 O PRO A 336 86.373 100.249 9.111 1.00 28.75 O ANISOU 1317 O PRO A 336 3973 3582 3367 -117 -51 260 O ATOM 1318 CB PRO A 336 88.684 102.082 7.880 1.00 29.48 C ANISOU 1318 CB PRO A 336 4079 3665 3456 -242 -165 211 C ATOM 1319 CG PRO A 336 88.429 102.754 6.516 1.00 27.28 C ANISOU 1319 CG PRO A 336 3765 3395 3205 -260 -147 208 C ATOM 1320 CD PRO A 336 87.199 102.050 5.994 1.00 27.45 C ANISOU 1320 CD PRO A 336 3737 3434 3258 -212 -86 219 C ATOM 1321 N LEU A 337 88.372 99.352 9.728 1.00 25.60 N ANISOU 1321 N LEU A 337 3553 3201 2974 -173 -141 242 N ATOM 1322 CA LEU A 337 87.855 98.579 10.859 1.00 34.92 C ANISOU 1322 CA LEU A 337 4760 4375 4132 -129 -118 265 C ATOM 1323 C LEU A 337 87.034 99.423 11.835 1.00 33.50 C ANISOU 1323 C LEU A 337 4685 4162 3881 -77 -81 275 C ATOM 1324 O LEU A 337 86.073 98.919 12.433 1.00 31.31 O ANISOU 1324 O LEU A 337 4414 3889 3594 -24 -27 310 O ATOM 1325 CB LEU A 337 89.022 97.904 11.609 1.00 25.05 C ANISOU 1325 CB LEU A 337 3512 3132 2874 -150 -175 260 C ATOM 1326 CG LEU A 337 88.698 97.392 13.023 1.00 30.72 C ANISOU 1326 CG LEU A 337 4290 3835 3546 -105 -161 281 C ATOM 1327 CD1 LEU A 337 87.661 96.240 13.014 1.00 28.56 C ANISOU 1327 CD1 LEU A 337 3961 3577 3312 -69 -105 321 C ATOM 1328 CD2 LEU A 337 89.970 96.958 13.764 1.00 20.06 C ANISOU 1328 CD2 LEU A 337 2955 2487 2180 -131 -231 272 C ATOM 1329 N LYS A 338 87.395 100.699 12.013 1.00 32.12 N ANISOU 1329 N LYS A 338 4596 3952 3654 -88 -111 249 N ATOM 1330 CA LYS A 338 86.673 101.553 12.957 1.00 34.05 C ANISOU 1330 CA LYS A 338 4962 4158 3818 -25 -81 253 C ATOM 1331 C LYS A 338 85.172 101.531 12.696 1.00 31.46 C ANISOU 1331 C LYS A 338 4609 3845 3499 39 10 287 C ATOM 1332 O LYS A 338 84.372 101.517 13.634 1.00 38.70 O ANISOU 1332 O LYS A 338 5584 4758 4364 114 63 316 O ATOM 1333 CB LYS A 338 87.199 102.995 12.882 1.00 32.82 C ANISOU 1333 CB LYS A 338 4902 3953 3616 -53 -135 218 C ATOM 1334 CG LYS A 338 86.603 103.944 13.930 1.00 38.81 C ANISOU 1334 CG LYS A 338 5814 4658 4273 21 -118 212 C ATOM 1335 CD LYS A 338 86.886 103.427 15.342 1.00 42.69 C ANISOU 1335 CD LYS A 338 6378 5138 4703 58 -136 217 C ATOM 1336 CE LYS A 338 86.052 104.127 16.408 1.00 44.17 C ANISOU 1336 CE LYS A 338 6713 5285 4782 162 -93 220 C ATOM 1337 NZ LYS A 338 86.431 105.551 16.580 1.00 44.47 N ANISOU 1337 NZ LYS A 338 6896 5249 4750 157 -159 178 N ATOM 1338 N ASN A 339 84.770 101.504 11.426 1.00 30.77 N ANISOU 1338 N ASN A 339 4434 3779 3477 15 30 291 N ATOM 1339 CA ASN A 339 83.355 101.548 11.087 1.00 26.96 C ANISOU 1339 CA ASN A 339 3919 3312 3011 69 107 329 C ATOM 1340 C ASN A 339 82.624 100.220 11.276 1.00 34.23 C ANISOU 1340 C ASN A 339 4755 4269 3981 90 149 382 C ATOM 1341 O ASN A 339 81.393 100.228 11.362 1.00 36.77 O ANISOU 1341 O ASN A 339 5056 4606 4307 144 216 431 O ATOM 1342 CB ASN A 339 83.172 102.007 9.649 1.00 30.94 C ANISOU 1342 CB ASN A 339 4366 3824 3567 35 105 315 C ATOM 1343 CG ASN A 339 83.935 103.273 9.348 1.00 37.13 C ANISOU 1343 CG ASN A 339 5222 4571 4314 1 58 272 C ATOM 1344 OD1 ASN A 339 83.463 104.380 9.620 1.00 38.30 O ANISOU 1344 OD1 ASN A 339 5460 4685 4406 43 76 267 O ATOM 1345 ND2 ASN A 339 85.125 103.120 8.773 1.00 31.95 N ANISOU 1345 ND2 ASN A 339 4527 3922 3689 -72 -5 245 N ATOM 1346 N TRP A 340 83.320 99.080 11.339 1.00 33.38 N ANISOU 1346 N TRP A 340 4595 4176 3913 50 111 380 N ATOM 1347 CA TRP A 340 82.616 97.812 11.542 1.00 34.62 C ANISOU 1347 CA TRP A 340 4678 4357 4118 64 141 435 C ATOM 1348 C TRP A 340 83.084 97.071 12.789 1.00 37.86 C ANISOU 1348 C TRP A 340 5124 4766 4496 78 131 450 C ATOM 1349 O TRP A 340 82.891 95.856 12.889 1.00 34.35 O ANISOU 1349 O TRP A 340 4616 4335 4099 69 131 487 O ATOM 1350 CB TRP A 340 82.721 96.898 10.313 1.00 31.79 C ANISOU 1350 CB TRP A 340 4216 4012 3850 11 108 430 C ATOM 1351 CG TRP A 340 84.096 96.671 9.738 1.00 26.93 C ANISOU 1351 CG TRP A 340 3586 3396 3249 -42 39 376 C ATOM 1352 CD1 TRP A 340 84.732 97.442 8.797 1.00 22.85 C ANISOU 1352 CD1 TRP A 340 3068 2879 2734 -75 11 332 C ATOM 1353 CD2 TRP A 340 84.981 95.581 10.029 1.00 30.57 C ANISOU 1353 CD2 TRP A 340 4025 3863 3729 -64 -5 368 C ATOM 1354 NE1 TRP A 340 85.958 96.898 8.489 1.00 27.99 N ANISOU 1354 NE1 TRP A 340 3691 3541 3402 -113 -43 303 N ATOM 1355 CE2 TRP A 340 86.138 95.759 9.233 1.00 29.12 C ANISOU 1355 CE2 TRP A 340 3822 3687 3555 -104 -55 322 C ATOM 1356 CE3 TRP A 340 84.908 94.467 10.880 1.00 36.09 C ANISOU 1356 CE3 TRP A 340 4715 4561 4435 -50 -6 402 C ATOM 1357 CZ2 TRP A 340 87.218 94.875 9.277 1.00 27.11 C ANISOU 1357 CZ2 TRP A 340 3540 3443 3316 -123 -103 307 C ATOM 1358 CZ3 TRP A 340 85.989 93.573 10.917 1.00 25.38 C ANISOU 1358 CZ3 TRP A 340 3339 3208 3096 -74 -60 381 C ATOM 1359 CH2 TRP A 340 87.128 93.793 10.128 1.00 29.30 C ANISOU 1359 CH2 TRP A 340 3816 3716 3600 -106 -106 334 C ATOM 1360 N GLU A 341 83.687 97.785 13.741 1.00 38.19 N ANISOU 1360 N GLU A 341 5271 4785 4454 100 115 424 N ATOM 1361 CA GLU A 341 84.057 97.183 15.017 1.00 40.69 C ANISOU 1361 CA GLU A 341 5637 5098 4725 124 106 440 C ATOM 1362 C GLU A 341 82.858 96.559 15.733 1.00 36.60 C ANISOU 1362 C GLU A 341 5101 4602 4203 187 185 518 C ATOM 1363 O GLU A 341 83.011 95.541 16.421 1.00 32.98 O ANISOU 1363 O GLU A 341 4628 4153 3751 190 181 550 O ATOM 1364 CB GLU A 341 84.709 98.245 15.905 1.00 40.75 C ANISOU 1364 CB GLU A 341 5779 5070 4633 147 75 400 C ATOM 1365 CG GLU A 341 85.741 97.694 16.865 1.00 56.70 C ANISOU 1365 CG GLU A 341 7843 7080 6619 133 16 387 C ATOM 1366 CD GLU A 341 86.521 98.785 17.585 1.00 65.53 C ANISOU 1366 CD GLU A 341 9096 8153 7647 137 -42 341 C ATOM 1367 OE1 GLU A 341 86.335 99.984 17.253 1.00 60.60 O ANISOU 1367 OE1 GLU A 341 8532 7501 6992 144 -44 315 O ATOM 1368 OE2 GLU A 341 87.316 98.435 18.489 1.00 68.94 O ANISOU 1368 OE2 GLU A 341 9580 8573 8041 132 -95 333 O ATOM 1369 N PHE A 342 81.669 97.161 15.603 1.00 33.30 N ANISOU 1369 N PHE A 342 4681 4196 3775 240 258 557 N ATOM 1370 CA PHE A 342 80.481 96.618 16.259 1.00 34.50 C ANISOU 1370 CA PHE A 342 4802 4379 3928 303 341 648 C ATOM 1371 C PHE A 342 80.136 95.224 15.744 1.00 35.41 C ANISOU 1371 C PHE A 342 4789 4516 4150 251 332 700 C ATOM 1372 O PHE A 342 79.524 94.427 16.465 1.00 40.41 O ANISOU 1372 O PHE A 342 5392 5170 4791 280 374 779 O ATOM 1373 CB PHE A 342 79.289 97.569 16.075 1.00 29.44 C ANISOU 1373 CB PHE A 342 4169 3754 3264 371 419 684 C ATOM 1374 CG PHE A 342 78.728 97.594 14.667 1.00 37.75 C ANISOU 1374 CG PHE A 342 5116 4818 4409 325 416 690 C ATOM 1375 CD1 PHE A 342 77.643 96.793 14.316 1.00 35.79 C ANISOU 1375 CD1 PHE A 342 4751 4605 4243 321 456 776 C ATOM 1376 CD2 PHE A 342 79.279 98.429 13.697 1.00 34.93 C ANISOU 1376 CD2 PHE A 342 4779 4436 4058 284 368 615 C ATOM 1377 CE1 PHE A 342 77.119 96.813 13.017 1.00 33.21 C ANISOU 1377 CE1 PHE A 342 4335 4285 4000 279 441 780 C ATOM 1378 CE2 PHE A 342 78.764 98.459 12.393 1.00 33.48 C ANISOU 1378 CE2 PHE A 342 4506 4262 3952 247 363 619 C ATOM 1379 CZ PHE A 342 77.682 97.654 12.053 1.00 34.76 C ANISOU 1379 CZ PHE A 342 4559 4456 4192 246 397 698 C ATOM 1380 N ILE A 343 80.523 94.907 14.508 1.00 33.33 N ANISOU 1380 N ILE A 343 4455 4244 3965 178 273 661 N ATOM 1381 CA ILE A 343 80.297 93.560 13.995 1.00 30.06 C ANISOU 1381 CA ILE A 343 3940 3835 3646 129 246 699 C ATOM 1382 C ILE A 343 81.166 92.562 14.741 1.00 35.81 C ANISOU 1382 C ILE A 343 4687 4553 4367 112 204 695 C ATOM 1383 O ILE A 343 80.723 91.451 15.066 1.00 41.34 O ANISOU 1383 O ILE A 343 5338 5258 5113 105 209 760 O ATOM 1384 CB ILE A 343 80.554 93.514 12.478 1.00 34.30 C ANISOU 1384 CB ILE A 343 4417 4362 4254 68 191 650 C ATOM 1385 CG1 ILE A 343 79.569 94.414 11.741 1.00 36.48 C ANISOU 1385 CG1 ILE A 343 4668 4649 4543 86 234 666 C ATOM 1386 CG2 ILE A 343 80.438 92.102 11.950 1.00 27.62 C ANISOU 1386 CG2 ILE A 343 3490 3507 3496 21 146 678 C ATOM 1387 CD1 ILE A 343 79.869 94.510 10.270 1.00 43.35 C ANISOU 1387 CD1 ILE A 343 5496 5509 5465 35 181 612 C ATOM 1388 N VAL A 344 82.415 92.938 15.029 1.00 35.11 N ANISOU 1388 N VAL A 344 4667 4448 4224 102 156 623 N ATOM 1389 CA VAL A 344 83.324 92.029 15.727 1.00 36.88 C ANISOU 1389 CA VAL A 344 4910 4664 4439 88 110 615 C ATOM 1390 C VAL A 344 82.818 91.753 17.133 1.00 37.88 C ANISOU 1390 C VAL A 344 5084 4799 4511 145 162 682 C ATOM 1391 O VAL A 344 82.791 90.601 17.589 1.00 40.58 O ANISOU 1391 O VAL A 344 5396 5141 4882 138 154 728 O ATOM 1392 CB VAL A 344 84.755 92.599 15.760 1.00 35.22 C ANISOU 1392 CB VAL A 344 4759 4440 4183 65 45 534 C ATOM 1393 CG1 VAL A 344 85.673 91.601 16.458 1.00 30.56 C ANISOU 1393 CG1 VAL A 344 4178 3844 3588 54 -5 532 C ATOM 1394 CG2 VAL A 344 85.249 92.918 14.348 1.00 27.63 C ANISOU 1394 CG2 VAL A 344 3747 3479 3272 15 4 479 C ATOM 1395 N ASP A 345 82.421 92.810 17.851 1.00 34.20 N ANISOU 1395 N ASP A 345 4699 4338 3959 209 216 689 N ATOM 1396 CA ASP A 345 81.861 92.613 19.183 1.00 41.66 C ANISOU 1396 CA ASP A 345 5694 5297 4839 280 279 758 C ATOM 1397 C ASP A 345 80.551 91.841 19.129 1.00 36.90 C ANISOU 1397 C ASP A 345 4995 4724 4301 293 346 866 C ATOM 1398 O ASP A 345 80.270 91.032 20.017 1.00 38.94 O ANISOU 1398 O ASP A 345 5249 4996 4551 317 375 938 O ATOM 1399 CB ASP A 345 81.677 93.954 19.893 1.00 55.01 C ANISOU 1399 CB ASP A 345 7505 6983 6415 359 323 739 C ATOM 1400 CG ASP A 345 82.993 94.677 20.105 1.00 70.15 C ANISOU 1400 CG ASP A 345 9526 8862 8267 338 242 644 C ATOM 1401 OD1 ASP A 345 83.202 95.738 19.485 1.00 80.51 O ANISOU 1401 OD1 ASP A 345 10870 10155 9566 325 220 587 O ATOM 1402 OD2 ASP A 345 83.844 94.155 20.865 1.00 74.04 O ANISOU 1402 OD2 ASP A 345 10061 9341 8728 330 193 630 O ATOM 1403 N PHE A 346 79.729 92.083 18.104 1.00 36.56 N ANISOU 1403 N PHE A 346 4872 4693 4324 274 369 886 N ATOM 1404 CA PHE A 346 78.531 91.266 17.919 1.00 39.46 C ANISOU 1404 CA PHE A 346 5132 5088 4775 267 412 994 C ATOM 1405 C PHE A 346 78.899 89.799 17.752 1.00 39.43 C ANISOU 1405 C PHE A 346 5067 5063 4851 197 346 1014 C ATOM 1406 O PHE A 346 78.351 88.922 18.435 1.00 39.73 O ANISOU 1406 O PHE A 346 5070 5115 4913 205 375 1109 O ATOM 1407 CB PHE A 346 77.734 91.762 16.706 1.00 37.83 C ANISOU 1407 CB PHE A 346 4850 4890 4633 246 423 1000 C ATOM 1408 CG PHE A 346 76.397 91.076 16.525 1.00 43.25 C ANISOU 1408 CG PHE A 346 5422 5607 5406 238 465 1123 C ATOM 1409 CD1 PHE A 346 75.243 91.613 17.077 1.00 38.78 C ANISOU 1409 CD1 PHE A 346 4838 5088 4809 316 568 1217 C ATOM 1410 CD2 PHE A 346 76.301 89.893 15.803 1.00 40.97 C ANISOU 1410 CD2 PHE A 346 5044 5296 5228 155 398 1149 C ATOM 1411 CE1 PHE A 346 74.021 90.986 16.905 1.00 40.41 C ANISOU 1411 CE1 PHE A 346 4924 5327 5103 302 603 1343 C ATOM 1412 CE2 PHE A 346 75.080 89.263 15.626 1.00 47.71 C ANISOU 1412 CE2 PHE A 346 5790 6171 6169 135 421 1269 C ATOM 1413 CZ PHE A 346 73.939 89.806 16.180 1.00 47.03 C ANISOU 1413 CZ PHE A 346 5670 6138 6060 204 524 1371 C ATOM 1414 N VAL A 347 79.848 89.519 16.855 1.00 39.61 N ANISOU 1414 N VAL A 347 5081 5053 4915 133 258 927 N ATOM 1415 CA VAL A 347 80.197 88.139 16.534 1.00 37.12 C ANISOU 1415 CA VAL A 347 4715 4711 4677 74 188 937 C ATOM 1416 C VAL A 347 80.831 87.468 17.736 1.00 39.99 C ANISOU 1416 C VAL A 347 5131 5068 4994 93 179 954 C ATOM 1417 O VAL A 347 80.600 86.282 17.993 1.00 38.78 O ANISOU 1417 O VAL A 347 4939 4903 4893 69 160 1017 O ATOM 1418 CB VAL A 347 81.120 88.089 15.296 1.00 39.93 C ANISOU 1418 CB VAL A 347 5061 5040 5072 22 104 838 C ATOM 1419 CG1 VAL A 347 81.762 86.723 15.152 1.00 40.64 C ANISOU 1419 CG1 VAL A 347 5132 5097 5212 -18 28 831 C ATOM 1420 CG2 VAL A 347 80.337 88.430 14.033 1.00 32.47 C ANISOU 1420 CG2 VAL A 347 4052 4096 4190 -4 104 839 C ATOM 1421 N ALA A 348 81.619 88.223 18.508 1.00 38.54 N ANISOU 1421 N ALA A 348 5043 4890 4712 135 187 900 N ATOM 1422 CA ALA A 348 82.311 87.648 19.654 1.00 33.52 C ANISOU 1422 CA ALA A 348 4466 4246 4023 155 170 908 C ATOM 1423 C ALA A 348 81.393 87.415 20.841 1.00 34.68 C ANISOU 1423 C ALA A 348 4627 4419 4130 214 252 1015 C ATOM 1424 O ALA A 348 81.833 86.811 21.820 1.00 35.68 O ANISOU 1424 O ALA A 348 4799 4540 4217 232 242 1038 O ATOM 1425 CB ALA A 348 83.473 88.543 20.091 1.00 31.60 C ANISOU 1425 CB ALA A 348 4323 3996 3687 176 137 818 C ATOM 1426 N THR A 349 80.169 87.922 20.810 1.00 36.42 N ANISOU 1426 N THR A 349 4813 4670 4353 250 335 1085 N ATOM 1427 CA THR A 349 79.202 87.587 21.849 1.00 40.64 C ANISOU 1427 CA THR A 349 5339 5240 4863 307 423 1209 C ATOM 1428 C THR A 349 78.968 86.081 21.837 1.00 45.12 C ANISOU 1428 C THR A 349 5825 5795 5525 249 389 1290 C ATOM 1429 O THR A 349 78.611 85.528 20.784 1.00 47.68 O ANISOU 1429 O THR A 349 6057 6100 5959 178 345 1303 O ATOM 1430 CB THR A 349 77.898 88.338 21.619 1.00 47.74 C ANISOU 1430 CB THR A 349 6190 6181 5767 353 515 1278 C ATOM 1431 OG1 THR A 349 78.129 89.733 21.821 1.00 45.16 O ANISOU 1431 OG1 THR A 349 5964 5860 5336 421 547 1207 O ATOM 1432 CG2 THR A 349 76.817 87.856 22.582 1.00 46.75 C ANISOU 1432 CG2 THR A 349 6026 6103 5633 408 611 1429 C ATOM 1433 N PRO A 350 79.174 85.383 22.960 1.00 44.79 N ANISOU 1433 N PRO A 350 5822 5755 5443 275 401 1343 N ATOM 1434 CA PRO A 350 79.224 83.905 22.928 1.00 41.35 C ANISOU 1434 CA PRO A 350 5328 5289 5095 211 345 1401 C ATOM 1435 C PRO A 350 78.066 83.220 22.217 1.00 46.65 C ANISOU 1435 C PRO A 350 5873 5961 5891 153 349 1504 C ATOM 1436 O PRO A 350 78.301 82.280 21.445 1.00 49.07 O ANISOU 1436 O PRO A 350 6134 6219 6293 75 258 1489 O ATOM 1437 CB PRO A 350 79.261 83.542 24.420 1.00 46.90 C ANISOU 1437 CB PRO A 350 6093 6012 5716 273 396 1473 C ATOM 1438 CG PRO A 350 79.991 84.703 25.052 1.00 42.64 C ANISOU 1438 CG PRO A 350 5679 5483 5041 348 415 1382 C ATOM 1439 CD PRO A 350 79.481 85.921 24.299 1.00 46.27 C ANISOU 1439 CD PRO A 350 6124 5961 5494 366 454 1343 C ATOM 1440 N GLU A 351 76.823 83.645 22.446 1.00 50.14 N ANISOU 1440 N GLU A 351 6260 6456 6337 192 446 1613 N ATOM 1441 CA GLU A 351 75.711 82.971 21.780 1.00 55.80 C ANISOU 1441 CA GLU A 351 6847 7173 7181 127 438 1724 C ATOM 1442 C GLU A 351 75.650 83.295 20.287 1.00 51.86 C ANISOU 1442 C GLU A 351 6300 6647 6759 67 373 1647 C ATOM 1443 O GLU A 351 75.267 82.435 19.482 1.00 51.55 O ANISOU 1443 O GLU A 351 6183 6570 6835 -16 300 1685 O ATOM 1444 CB GLU A 351 74.392 83.334 22.463 1.00 58.25 C ANISOU 1444 CB GLU A 351 7098 7559 7478 191 566 1876 C ATOM 1445 CG GLU A 351 73.163 82.602 21.922 1.00 69.08 C ANISOU 1445 CG GLU A 351 8321 8938 8988 120 559 2020 C ATOM 1446 CD GLU A 351 73.350 81.093 21.842 1.00 78.99 C ANISOU 1446 CD GLU A 351 9541 10132 10341 23 460 2069 C ATOM 1447 OE1 GLU A 351 73.934 80.499 22.778 1.00 84.24 O ANISOU 1447 OE1 GLU A 351 10267 10784 10956 42 459 2080 O ATOM 1448 OE2 GLU A 351 72.892 80.495 20.846 1.00 78.68 O ANISOU 1448 OE2 GLU A 351 9417 10052 10426 -70 378 2098 O ATOM 1449 N HIS A 352 76.012 84.516 19.896 1.00 40.42 N ANISOU 1449 N HIS A 352 4902 5211 5244 107 393 1543 N ATOM 1450 CA HIS A 352 76.143 84.825 18.472 1.00 46.87 C ANISOU 1450 CA HIS A 352 5689 5999 6122 53 325 1457 C ATOM 1451 C HIS A 352 77.249 83.994 17.832 1.00 41.79 C ANISOU 1451 C HIS A 352 5071 5290 5516 -12 206 1361 C ATOM 1452 O HIS A 352 77.081 83.458 16.730 1.00 47.00 O ANISOU 1452 O HIS A 352 5678 5911 6268 -78 130 1349 O ATOM 1453 CB HIS A 352 76.418 86.316 18.268 1.00 48.32 C ANISOU 1453 CB HIS A 352 5933 6206 6219 111 369 1364 C ATOM 1454 CG HIS A 352 75.354 87.210 18.820 1.00 55.13 C ANISOU 1454 CG HIS A 352 6782 7130 7035 191 486 1448 C ATOM 1455 ND1 HIS A 352 75.566 88.547 19.074 1.00 57.81 N ANISOU 1455 ND1 HIS A 352 7206 7490 7269 267 541 1382 N ATOM 1456 CD2 HIS A 352 74.076 86.955 19.184 1.00 55.87 C ANISOU 1456 CD2 HIS A 352 6789 7271 7170 211 560 1596 C ATOM 1457 CE1 HIS A 352 74.459 89.082 19.557 1.00 57.32 C ANISOU 1457 CE1 HIS A 352 7117 7484 7180 342 647 1481 C ATOM 1458 NE2 HIS A 352 73.541 88.136 19.638 1.00 56.37 N ANISOU 1458 NE2 HIS A 352 6885 7385 7147 311 665 1616 N ATOM 1459 N LEU A 353 78.390 83.881 18.515 1.00 38.27 N ANISOU 1459 N LEU A 353 4712 4832 4998 13 186 1295 N ATOM 1460 CA LEU A 353 79.540 83.186 17.949 1.00 37.36 C ANISOU 1460 CA LEU A 353 4625 4664 4907 -31 81 1202 C ATOM 1461 C LEU A 353 79.196 81.745 17.589 1.00 43.65 C ANISOU 1461 C LEU A 353 5366 5411 5807 -95 10 1264 C ATOM 1462 O LEU A 353 79.539 81.270 16.494 1.00 41.68 O ANISOU 1462 O LEU A 353 5105 5116 5617 -141 -77 1205 O ATOM 1463 CB LEU A 353 80.709 83.231 18.938 1.00 34.47 C ANISOU 1463 CB LEU A 353 4349 4299 4448 10 76 1147 C ATOM 1464 CG LEU A 353 82.046 82.727 18.397 1.00 41.89 C ANISOU 1464 CG LEU A 353 5321 5199 5397 -18 -21 1044 C ATOM 1465 CD1 LEU A 353 82.662 83.743 17.424 1.00 38.78 C ANISOU 1465 CD1 LEU A 353 4939 4814 4982 -20 -40 934 C ATOM 1466 CD2 LEU A 353 83.016 82.389 19.529 1.00 39.66 C ANISOU 1466 CD2 LEU A 353 5110 4915 5045 14 -34 1029 C ATOM 1467 N ARG A 354 78.503 81.038 18.490 1.00 44.83 N ANISOU 1467 N ARG A 354 5488 5567 5978 -97 43 1389 N ATOM 1468 CA ARG A 354 78.201 79.632 18.232 1.00 48.62 C ANISOU 1468 CA ARG A 354 5926 5990 6558 -164 -36 1456 C ATOM 1469 C ARG A 354 77.312 79.481 17.002 1.00 45.00 C ANISOU 1469 C ARG A 354 5388 5505 6203 -227 -84 1484 C ATOM 1470 O ARG A 354 77.608 78.685 16.107 1.00 40.69 O ANISOU 1470 O ARG A 354 4846 4892 5722 -280 -191 1440 O ATOM 1471 CB ARG A 354 77.549 78.970 19.444 1.00 54.07 C ANISOU 1471 CB ARG A 354 6593 6697 7254 -158 14 1601 C ATOM 1472 CG ARG A 354 77.388 77.472 19.200 1.00 68.16 C ANISOU 1472 CG ARG A 354 8348 8408 9141 -234 -85 1663 C ATOM 1473 CD ARG A 354 76.350 76.794 20.071 1.00 80.79 C ANISOU 1473 CD ARG A 354 9885 10023 10788 -255 -41 1842 C ATOM 1474 NE ARG A 354 74.997 77.009 19.571 1.00 87.35 N ANISOU 1474 NE ARG A 354 10607 10880 11703 -295 -15 1950 N ATOM 1475 CZ ARG A 354 74.099 77.756 20.200 1.00 85.54 C ANISOU 1475 CZ ARG A 354 10322 10735 11444 -246 109 2052 C ATOM 1476 NH1 ARG A 354 74.425 78.331 21.350 1.00 85.97 N ANISOU 1476 NH1 ARG A 354 10436 10849 11381 -154 212 2053 N ATOM 1477 NH2 ARG A 354 72.884 77.920 19.689 1.00 78.93 N ANISOU 1477 NH2 ARG A 354 9375 9924 10690 -283 128 2156 N ATOM 1478 N GLN A 355 76.222 80.252 16.939 1.00 41.91 N ANISOU 1478 N GLN A 355 4931 5167 5826 -216 -8 1556 N ATOM 1479 CA GLN A 355 75.344 80.238 15.769 1.00 43.42 C ANISOU 1479 CA GLN A 355 5044 5339 6113 -274 -54 1583 C ATOM 1480 C GLN A 355 76.096 80.575 14.485 1.00 48.92 C ANISOU 1480 C GLN A 355 5782 5999 6805 -286 -128 1436 C ATOM 1481 O GLN A 355 75.871 79.943 13.447 1.00 48.10 O ANISOU 1481 O GLN A 355 5655 5837 6784 -346 -225 1426 O ATOM 1482 CB GLN A 355 74.198 81.235 15.955 1.00 45.73 C ANISOU 1482 CB GLN A 355 5267 5709 6401 -239 54 1670 C ATOM 1483 CG GLN A 355 73.173 80.864 17.004 1.00 52.89 C ANISOU 1483 CG GLN A 355 6103 6661 7333 -230 130 1847 C ATOM 1484 CD GLN A 355 71.955 81.773 16.930 1.00 63.07 C ANISOU 1484 CD GLN A 355 7305 8023 8635 -197 225 1938 C ATOM 1485 OE1 GLN A 355 71.259 81.819 15.905 1.00 58.32 O ANISOU 1485 OE1 GLN A 355 6629 7410 8120 -250 177 1961 O ATOM 1486 NE2 GLN A 355 71.703 82.515 18.006 1.00 60.94 N ANISOU 1486 NE2 GLN A 355 7051 7830 8274 -103 356 1990 N ATOM 1487 N ILE A 356 76.977 81.581 14.520 1.00 41.49 N ANISOU 1487 N ILE A 356 4905 5090 5769 -228 -86 1323 N ATOM 1488 CA ILE A 356 77.563 82.055 13.266 1.00 32.71 C ANISOU 1488 CA ILE A 356 3817 3958 4653 -236 -139 1201 C ATOM 1489 C ILE A 356 78.672 81.122 12.783 1.00 33.36 C ANISOU 1489 C ILE A 356 3953 3977 4744 -255 -241 1115 C ATOM 1490 O ILE A 356 78.678 80.713 11.613 1.00 38.51 O ANISOU 1490 O ILE A 356 4601 4582 5449 -290 -324 1073 O ATOM 1491 CB ILE A 356 78.047 83.510 13.398 1.00 33.95 C ANISOU 1491 CB ILE A 356 4016 4169 4715 -176 -64 1124 C ATOM 1492 CG1 ILE A 356 76.858 84.440 13.665 1.00 35.27 C ANISOU 1492 CG1 ILE A 356 4133 4391 4876 -147 31 1204 C ATOM 1493 CG2 ILE A 356 78.745 83.944 12.128 1.00 33.44 C ANISOU 1493 CG2 ILE A 356 3974 4086 4646 -185 -118 1005 C ATOM 1494 CD1 ILE A 356 77.258 85.924 13.836 1.00 43.76 C ANISOU 1494 CD1 ILE A 356 5263 5510 5853 -84 102 1131 C ATOM 1495 N CYS A 357 79.613 80.758 13.667 1.00 32.43 N ANISOU 1495 N CYS A 357 3892 3858 4572 -227 -239 1091 N ATOM 1496 CA CYS A 357 80.693 79.843 13.272 1.00 41.77 C ANISOU 1496 CA CYS A 357 5124 4986 5759 -233 -331 1016 C ATOM 1497 C CYS A 357 80.184 78.478 12.814 1.00 40.33 C ANISOU 1497 C CYS A 357 4925 4727 5670 -288 -426 1069 C ATOM 1498 O CYS A 357 80.823 77.838 11.977 1.00 37.78 O ANISOU 1498 O CYS A 357 4642 4350 5364 -292 -514 997 O ATOM 1499 CB CYS A 357 81.689 79.633 14.414 1.00 47.21 C ANISOU 1499 CB CYS A 357 5868 5689 6380 -194 -313 998 C ATOM 1500 SG CYS A 357 82.509 81.131 15.038 1.00 53.36 S ANISOU 1500 SG CYS A 357 6690 6541 7045 -134 -231 928 S ATOM 1501 N SER A 358 79.059 78.004 13.346 1.00 40.05 N ANISOU 1501 N SER A 358 4838 4684 5695 -327 -413 1198 N ATOM 1502 CA SER A 358 78.574 76.656 13.064 1.00 40.02 C ANISOU 1502 CA SER A 358 4823 4598 5784 -389 -514 1263 C ATOM 1503 C SER A 358 77.713 76.588 11.814 1.00 42.28 C ANISOU 1503 C SER A 358 5068 4844 6151 -443 -582 1275 C ATOM 1504 O SER A 358 77.005 75.599 11.605 1.00 48.55 O ANISOU 1504 O SER A 358 5839 5571 7035 -509 -666 1356 O ATOM 1505 CB SER A 358 77.812 76.117 14.276 1.00 47.27 C ANISOU 1505 CB SER A 358 5699 5527 6734 -413 -474 1411 C ATOM 1506 OG SER A 358 78.666 76.124 15.415 1.00 66.29 O ANISOU 1506 OG SER A 358 8161 7967 9061 -359 -421 1393 O ATOM 1507 N ASP A 359 77.779 77.604 10.969 1.00 45.42 N ANISOU 1507 N ASP A 359 5460 5277 6520 -421 -557 1198 N ATOM 1508 CA ASP A 359 76.965 77.698 9.771 1.00 39.05 C ANISOU 1508 CA ASP A 359 4616 4441 5780 -465 -616 1204 C ATOM 1509 C ASP A 359 77.869 77.689 8.545 1.00 38.99 C ANISOU 1509 C ASP A 359 4680 4393 5742 -440 -688 1064 C ATOM 1510 O ASP A 359 78.994 78.200 8.586 1.00 32.86 O ANISOU 1510 O ASP A 359 3951 3651 4882 -380 -648 966 O ATOM 1511 CB ASP A 359 76.116 78.975 9.806 1.00 35.14 C ANISOU 1511 CB ASP A 359 4048 4026 5277 -454 -515 1248 C ATOM 1512 CG ASP A 359 75.363 79.211 8.524 1.00 37.59 C ANISOU 1512 CG ASP A 359 4322 4314 5646 -492 -573 1243 C ATOM 1513 OD1 ASP A 359 74.268 78.632 8.384 1.00 50.79 O ANISOU 1513 OD1 ASP A 359 5931 5954 7413 -557 -626 1353 O ATOM 1514 OD2 ASP A 359 75.862 79.983 7.665 1.00 38.66 O ANISOU 1514 OD2 ASP A 359 4491 4464 5734 -458 -568 1136 O ATOM 1515 N LYS A 360 77.362 77.102 7.455 1.00 34.80 N ANISOU 1515 N LYS A 360 4155 3789 5277 -485 -798 1063 N ATOM 1516 CA LYS A 360 78.126 77.021 6.212 1.00 40.37 C ANISOU 1516 CA LYS A 360 4935 4452 5950 -453 -871 938 C ATOM 1517 C LYS A 360 78.624 78.387 5.741 1.00 38.96 C ANISOU 1517 C LYS A 360 4754 4353 5698 -399 -786 851 C ATOM 1518 O LYS A 360 79.781 78.529 5.328 1.00 45.51 O ANISOU 1518 O LYS A 360 5641 5190 6459 -342 -786 746 O ATOM 1519 CB LYS A 360 77.273 76.368 5.125 1.00 43.54 C ANISOU 1519 CB LYS A 360 5344 4768 6433 -511 -998 961 C ATOM 1520 CG LYS A 360 78.014 76.168 3.808 1.00 45.44 C ANISOU 1520 CG LYS A 360 5675 4956 6633 -468 -1080 835 C ATOM 1521 CD LYS A 360 77.092 75.832 2.633 1.00 47.07 C ANISOU 1521 CD LYS A 360 5891 5086 6905 -520 -1199 850 C ATOM 1522 CE LYS A 360 77.913 75.105 1.554 1.00 61.57 C ANISOU 1522 CE LYS A 360 7854 6840 8701 -470 -1309 736 C ATOM 1523 NZ LYS A 360 78.313 73.713 1.973 1.00 67.25 N ANISOU 1523 NZ LYS A 360 8648 7466 9438 -473 -1400 745 N ATOM 1524 N TYR A 361 77.767 79.402 5.781 1.00 32.42 N ANISOU 1524 N TYR A 361 3854 3583 4882 -414 -714 900 N ATOM 1525 CA TYR A 361 78.144 80.722 5.295 1.00 37.38 C ANISOU 1525 CA TYR A 361 4481 4276 5444 -369 -642 825 C ATOM 1526 C TYR A 361 78.829 81.546 6.378 1.00 36.41 C ANISOU 1526 C TYR A 361 4360 4229 5245 -323 -530 810 C ATOM 1527 O TYR A 361 79.825 82.224 6.095 1.00 30.36 O ANISOU 1527 O TYR A 361 3631 3496 4410 -279 -500 719 O ATOM 1528 CB TYR A 361 76.906 81.441 4.740 1.00 32.39 C ANISOU 1528 CB TYR A 361 3782 3665 4859 -401 -627 879 C ATOM 1529 CG TYR A 361 76.303 80.637 3.613 1.00 35.53 C ANISOU 1529 CG TYR A 361 4190 3982 5328 -448 -755 886 C ATOM 1530 CD1 TYR A 361 76.971 80.521 2.398 1.00 42.47 C ANISOU 1530 CD1 TYR A 361 5141 4822 6175 -421 -824 778 C ATOM 1531 CD2 TYR A 361 75.111 79.927 3.784 1.00 32.67 C ANISOU 1531 CD2 TYR A 361 3769 3578 5064 -520 -814 1004 C ATOM 1532 CE1 TYR A 361 76.458 79.748 1.365 1.00 42.50 C ANISOU 1532 CE1 TYR A 361 5175 4740 6234 -458 -953 777 C ATOM 1533 CE2 TYR A 361 74.581 79.155 2.749 1.00 34.46 C ANISOU 1533 CE2 TYR A 361 4017 3718 5359 -570 -951 1010 C ATOM 1534 CZ TYR A 361 75.263 79.075 1.543 1.00 42.09 C ANISOU 1534 CZ TYR A 361 5071 4640 6282 -536 -1022 890 C ATOM 1535 OH TYR A 361 74.768 78.325 0.501 1.00 44.04 O ANISOU 1535 OH TYR A 361 5358 4794 6583 -577 -1167 887 O ATOM 1536 N GLY A 362 78.317 81.464 7.615 1.00 33.38 N ANISOU 1536 N GLY A 362 3940 3870 4873 -333 -473 903 N ATOM 1537 CA GLY A 362 78.855 82.250 8.711 1.00 29.67 C ANISOU 1537 CA GLY A 362 3482 3464 4326 -287 -374 895 C ATOM 1538 C GLY A 362 80.278 81.875 9.083 1.00 37.83 C ANISOU 1538 C GLY A 362 4582 4490 5301 -254 -392 819 C ATOM 1539 O GLY A 362 81.043 82.727 9.543 1.00 32.22 O ANISOU 1539 O GLY A 362 3898 3828 4517 -215 -333 770 O ATOM 1540 N SER A 363 80.652 80.605 8.894 1.00 28.02 N ANISOU 1540 N SER A 363 3369 3184 4092 -268 -479 811 N ATOM 1541 CA SER A 363 82.034 80.193 9.113 1.00 33.94 C ANISOU 1541 CA SER A 363 4177 3928 4789 -230 -503 738 C ATOM 1542 C SER A 363 82.997 81.004 8.243 1.00 33.69 C ANISOU 1542 C SER A 363 4168 3929 4703 -191 -494 631 C ATOM 1543 O SER A 363 84.021 81.499 8.726 1.00 35.48 O ANISOU 1543 O SER A 363 4415 4199 4866 -156 -457 586 O ATOM 1544 CB SER A 363 82.170 78.693 8.833 1.00 31.60 C ANISOU 1544 CB SER A 363 3916 3549 4542 -245 -607 744 C ATOM 1545 OG SER A 363 83.528 78.274 8.873 1.00 30.71 O ANISOU 1545 OG SER A 363 3859 3432 4380 -197 -634 669 O ATOM 1546 N TYR A 364 82.683 81.142 6.951 1.00 33.55 N ANISOU 1546 N TYR A 364 4147 3892 4710 -199 -532 596 N ATOM 1547 CA TYR A 364 83.480 81.982 6.054 1.00 25.74 C ANISOU 1547 CA TYR A 364 3170 2939 3670 -164 -516 509 C ATOM 1548 C TYR A 364 83.530 83.432 6.538 1.00 35.04 C ANISOU 1548 C TYR A 364 4324 4188 4800 -157 -423 507 C ATOM 1549 O TYR A 364 84.568 84.096 6.426 1.00 29.35 O ANISOU 1549 O TYR A 364 3619 3508 4024 -129 -399 447 O ATOM 1550 CB TYR A 364 82.898 81.928 4.639 1.00 24.56 C ANISOU 1550 CB TYR A 364 3022 2755 3554 -175 -569 486 C ATOM 1551 CG TYR A 364 83.226 80.685 3.825 1.00 34.23 C ANISOU 1551 CG TYR A 364 4300 3908 4798 -159 -671 449 C ATOM 1552 CD1 TYR A 364 84.521 80.447 3.371 1.00 33.71 C ANISOU 1552 CD1 TYR A 364 4279 3851 4678 -98 -687 371 C ATOM 1553 CD2 TYR A 364 82.231 79.774 3.481 1.00 37.25 C ANISOU 1553 CD2 TYR A 364 4690 4213 5250 -202 -754 495 C ATOM 1554 CE1 TYR A 364 84.828 79.322 2.611 1.00 35.43 C ANISOU 1554 CE1 TYR A 364 4560 4002 4902 -66 -777 334 C ATOM 1555 CE2 TYR A 364 82.521 78.648 2.717 1.00 40.69 C ANISOU 1555 CE2 TYR A 364 5194 4571 5696 -182 -858 456 C ATOM 1556 CZ TYR A 364 83.822 78.425 2.282 1.00 42.26 C ANISOU 1556 CZ TYR A 364 5448 4778 5830 -107 -867 372 C ATOM 1557 OH TYR A 364 84.115 77.306 1.524 1.00 36.50 O ANISOU 1557 OH TYR A 364 4800 3968 5100 -71 -968 330 O ATOM 1558 N VAL A 365 82.412 83.946 7.066 1.00 33.92 N ANISOU 1558 N VAL A 365 4148 4061 4679 -182 -374 576 N ATOM 1559 CA VAL A 365 82.389 85.316 7.573 1.00 32.43 C ANISOU 1559 CA VAL A 365 3953 3929 4439 -166 -289 575 C ATOM 1560 C VAL A 365 83.409 85.491 8.702 1.00 35.66 C ANISOU 1560 C VAL A 365 4398 4365 4786 -141 -261 557 C ATOM 1561 O VAL A 365 84.183 86.457 8.723 1.00 31.55 O ANISOU 1561 O VAL A 365 3898 3880 4210 -124 -233 506 O ATOM 1562 CB VAL A 365 80.963 85.695 8.014 1.00 34.56 C ANISOU 1562 CB VAL A 365 4180 4210 4740 -182 -238 663 C ATOM 1563 CG1 VAL A 365 80.954 87.020 8.751 1.00 28.68 C ANISOU 1563 CG1 VAL A 365 3450 3517 3930 -151 -151 664 C ATOM 1564 CG2 VAL A 365 80.023 85.767 6.795 1.00 33.00 C ANISOU 1564 CG2 VAL A 365 3944 3994 4600 -208 -270 674 C ATOM 1565 N VAL A 366 83.461 84.542 9.636 1.00 29.74 N ANISOU 1565 N VAL A 366 3659 3596 4046 -142 -275 600 N ATOM 1566 CA VAL A 366 84.381 84.698 10.764 1.00 30.60 C ANISOU 1566 CA VAL A 366 3805 3729 4094 -117 -254 587 C ATOM 1567 C VAL A 366 85.832 84.555 10.308 1.00 33.16 C ANISOU 1567 C VAL A 366 4150 4059 4390 -100 -299 508 C ATOM 1568 O VAL A 366 86.716 85.300 10.759 1.00 31.55 O ANISOU 1568 O VAL A 366 3967 3889 4129 -86 -280 474 O ATOM 1569 CB VAL A 366 84.018 83.702 11.879 1.00 33.28 C ANISOU 1569 CB VAL A 366 4149 4045 4449 -120 -256 661 C ATOM 1570 CG1 VAL A 366 85.066 83.718 12.990 1.00 29.04 C ANISOU 1570 CG1 VAL A 366 3659 3527 3848 -92 -250 643 C ATOM 1571 CG2 VAL A 366 82.641 84.044 12.445 1.00 31.56 C ANISOU 1571 CG2 VAL A 366 3902 3841 4247 -126 -192 752 C ATOM 1572 N SER A 367 86.099 83.622 9.394 1.00 26.55 N ANISOU 1572 N SER A 367 3309 3189 3591 -99 -361 482 N ATOM 1573 CA SER A 367 87.447 83.488 8.848 1.00 30.07 C ANISOU 1573 CA SER A 367 3767 3649 4009 -69 -395 414 C ATOM 1574 C SER A 367 87.881 84.736 8.097 1.00 24.91 C ANISOU 1574 C SER A 367 3099 3042 3324 -66 -365 366 C ATOM 1575 O SER A 367 89.045 85.149 8.193 1.00 30.23 O ANISOU 1575 O SER A 367 3774 3754 3959 -50 -364 331 O ATOM 1576 CB SER A 367 87.537 82.266 7.927 1.00 28.14 C ANISOU 1576 CB SER A 367 3533 3355 3803 -54 -465 394 C ATOM 1577 OG SER A 367 87.771 81.120 8.726 1.00 49.79 O ANISOU 1577 OG SER A 367 6299 6063 6557 -46 -502 421 O ATOM 1578 N THR A 368 86.975 85.334 7.319 1.00 26.53 N ANISOU 1578 N THR A 368 3288 3244 3550 -83 -345 369 N ATOM 1579 CA THR A 368 87.337 86.560 6.620 1.00 25.77 C ANISOU 1579 CA THR A 368 3181 3188 3423 -83 -316 329 C ATOM 1580 C THR A 368 87.630 87.671 7.617 1.00 30.92 C ANISOU 1580 C THR A 368 3846 3874 4027 -91 -270 336 C ATOM 1581 O THR A 368 88.601 88.416 7.457 1.00 29.13 O ANISOU 1581 O THR A 368 3620 3682 3766 -90 -267 302 O ATOM 1582 CB THR A 368 86.229 86.974 5.645 1.00 27.23 C ANISOU 1582 CB THR A 368 3348 3359 3638 -98 -306 336 C ATOM 1583 OG1 THR A 368 86.115 85.990 4.610 1.00 26.98 O ANISOU 1583 OG1 THR A 368 3319 3290 3641 -87 -364 318 O ATOM 1584 CG2 THR A 368 86.563 88.337 4.991 1.00 25.35 C ANISOU 1584 CG2 THR A 368 3104 3162 3366 -99 -272 301 C ATOM 1585 N ILE A 369 86.831 87.763 8.680 1.00 29.30 N ANISOU 1585 N ILE A 369 3656 3658 3818 -98 -238 385 N ATOM 1586 CA ILE A 369 87.090 88.757 9.716 1.00 22.13 C ANISOU 1586 CA ILE A 369 2782 2772 2853 -95 -202 389 C ATOM 1587 C ILE A 369 88.476 88.555 10.325 1.00 29.30 C ANISOU 1587 C ILE A 369 3709 3696 3727 -89 -236 364 C ATOM 1588 O ILE A 369 89.239 89.513 10.490 1.00 31.33 O ANISOU 1588 O ILE A 369 3984 3976 3943 -97 -237 338 O ATOM 1589 CB ILE A 369 85.987 88.719 10.786 1.00 25.35 C ANISOU 1589 CB ILE A 369 3208 3169 3255 -87 -158 453 C ATOM 1590 CG1 ILE A 369 84.702 89.328 10.217 1.00 30.13 C ANISOU 1590 CG1 ILE A 369 3789 3773 3885 -90 -116 480 C ATOM 1591 CG2 ILE A 369 86.435 89.469 12.047 1.00 23.60 C ANISOU 1591 CG2 ILE A 369 3046 2961 2962 -70 -135 453 C ATOM 1592 CD1 ILE A 369 83.480 89.113 11.086 1.00 32.18 C ANISOU 1592 CD1 ILE A 369 4044 4030 4154 -76 -67 561 C ATOM 1593 N ILE A 370 88.826 87.305 10.665 1.00 30.93 N ANISOU 1593 N ILE A 370 3912 3886 3952 -77 -272 375 N ATOM 1594 CA ILE A 370 90.107 87.053 11.330 1.00 32.32 C ANISOU 1594 CA ILE A 370 4103 4080 4098 -67 -306 359 C ATOM 1595 C ILE A 370 91.268 87.401 10.406 1.00 32.56 C ANISOU 1595 C ILE A 370 4102 4145 4125 -67 -332 314 C ATOM 1596 O ILE A 370 92.279 87.977 10.832 1.00 23.50 O ANISOU 1596 O ILE A 370 2958 3026 2944 -75 -348 301 O ATOM 1597 CB ILE A 370 90.206 85.590 11.809 1.00 30.17 C ANISOU 1597 CB ILE A 370 3835 3780 3849 -49 -340 383 C ATOM 1598 CG1 ILE A 370 89.224 85.327 12.944 1.00 31.37 C ANISOU 1598 CG1 ILE A 370 4016 3908 3995 -50 -310 442 C ATOM 1599 CG2 ILE A 370 91.645 85.274 12.291 1.00 27.76 C ANISOU 1599 CG2 ILE A 370 3533 3497 3516 -33 -382 363 C ATOM 1600 CD1 ILE A 370 88.802 83.876 13.041 1.00 33.41 C ANISOU 1600 CD1 ILE A 370 4268 4126 4300 -46 -338 480 C ATOM 1601 N GLU A 371 91.151 87.019 9.138 1.00 25.81 N ANISOU 1601 N GLU A 371 3215 3288 3304 -56 -340 294 N ATOM 1602 CA GLU A 371 92.177 87.334 8.164 1.00 35.73 C ANISOU 1602 CA GLU A 371 4437 4585 4555 -45 -352 260 C ATOM 1603 C GLU A 371 92.414 88.838 8.094 1.00 34.63 C ANISOU 1603 C GLU A 371 4293 4476 4388 -78 -328 252 C ATOM 1604 O GLU A 371 93.560 89.297 8.100 1.00 37.05 O ANISOU 1604 O GLU A 371 4577 4823 4677 -85 -345 246 O ATOM 1605 CB GLU A 371 91.765 86.777 6.806 1.00 39.07 C ANISOU 1605 CB GLU A 371 4843 4993 5008 -21 -359 241 C ATOM 1606 CG GLU A 371 92.761 87.021 5.693 1.00 54.88 C ANISOU 1606 CG GLU A 371 6811 7042 7000 5 -362 212 C ATOM 1607 CD GLU A 371 92.481 86.143 4.487 1.00 77.02 C ANISOU 1607 CD GLU A 371 9620 9823 9822 49 -381 189 C ATOM 1608 OE1 GLU A 371 91.471 85.396 4.513 1.00 85.96 O ANISOU 1608 OE1 GLU A 371 10781 10896 10983 45 -401 198 O ATOM 1609 OE2 GLU A 371 93.271 86.193 3.518 1.00 81.89 O ANISOU 1609 OE2 GLU A 371 10214 10479 10423 88 -379 168 O ATOM 1610 N LYS A 372 91.336 89.626 8.043 1.00 33.14 N ANISOU 1610 N LYS A 372 4126 4269 4198 -98 -292 259 N ATOM 1611 CA LYS A 372 91.497 91.076 7.956 1.00 28.45 C ANISOU 1611 CA LYS A 372 3541 3692 3575 -128 -274 251 C ATOM 1612 C LYS A 372 92.076 91.649 9.243 1.00 33.32 C ANISOU 1612 C LYS A 372 4199 4311 4151 -146 -291 260 C ATOM 1613 O LYS A 372 92.773 92.669 9.210 1.00 33.90 O ANISOU 1613 O LYS A 372 4276 4402 4202 -175 -305 252 O ATOM 1614 CB LYS A 372 90.159 91.728 7.630 1.00 29.20 C ANISOU 1614 CB LYS A 372 3654 3764 3675 -134 -232 258 C ATOM 1615 CG LYS A 372 90.143 93.277 7.653 1.00 30.20 C ANISOU 1615 CG LYS A 372 3809 3896 3769 -159 -213 251 C ATOM 1616 CD LYS A 372 91.147 93.849 6.663 1.00 37.31 C ANISOU 1616 CD LYS A 372 4673 4833 4672 -179 -231 231 C ATOM 1617 CE LYS A 372 90.861 93.339 5.249 1.00 37.49 C ANISOU 1617 CE LYS A 372 4650 4866 4728 -159 -221 219 C ATOM 1618 NZ LYS A 372 91.682 94.084 4.247 1.00 47.68 N ANISOU 1618 NZ LYS A 372 5907 6195 6013 -173 -222 209 N ATOM 1619 N LEU A 373 91.819 90.996 10.373 1.00 34.37 N ANISOU 1619 N LEU A 373 4366 4421 4271 -131 -295 280 N ATOM 1620 CA LEU A 373 92.336 91.419 11.665 1.00 32.48 C ANISOU 1620 CA LEU A 373 4180 4177 3984 -140 -318 287 C ATOM 1621 C LEU A 373 93.752 90.933 11.930 1.00 34.57 C ANISOU 1621 C LEU A 373 4417 4469 4250 -145 -374 283 C ATOM 1622 O LEU A 373 94.260 91.114 13.043 1.00 36.74 O ANISOU 1622 O LEU A 373 4736 4737 4486 -152 -407 290 O ATOM 1623 CB LEU A 373 91.407 90.928 12.777 1.00 30.12 C ANISOU 1623 CB LEU A 373 3932 3847 3666 -114 -292 317 C ATOM 1624 CG LEU A 373 90.050 91.619 12.792 1.00 31.84 C ANISOU 1624 CG LEU A 373 4182 4046 3872 -104 -232 333 C ATOM 1625 CD1 LEU A 373 89.256 91.140 14.006 1.00 32.86 C ANISOU 1625 CD1 LEU A 373 4355 4155 3974 -71 -201 376 C ATOM 1626 CD2 LEU A 373 90.266 93.129 12.800 1.00 28.49 C ANISOU 1626 CD2 LEU A 373 3803 3620 3403 -122 -233 310 C ATOM 1627 N THR A 374 94.400 90.309 10.956 1.00 30.94 N ANISOU 1627 N THR A 374 3890 4040 3827 -133 -388 274 N ATOM 1628 CA THR A 374 95.736 89.767 11.144 1.00 31.25 C ANISOU 1628 CA THR A 374 3890 4114 3870 -126 -435 279 C ATOM 1629 C THR A 374 96.753 90.762 10.600 1.00 37.25 C ANISOU 1629 C THR A 374 4606 4918 4629 -161 -456 279 C ATOM 1630 O THR A 374 96.590 91.263 9.481 1.00 35.77 O ANISOU 1630 O THR A 374 4385 4748 4457 -168 -429 270 O ATOM 1631 CB THR A 374 95.880 88.414 10.436 1.00 32.55 C ANISOU 1631 CB THR A 374 4011 4287 4069 -77 -436 275 C ATOM 1632 OG1 THR A 374 94.881 87.503 10.918 1.00 33.29 O ANISOU 1632 OG1 THR A 374 4145 4332 4171 -56 -424 283 O ATOM 1633 CG2 THR A 374 97.246 87.829 10.686 1.00 30.17 C ANISOU 1633 CG2 THR A 374 3670 4026 3769 -57 -480 284 C ATOM 1634 N ALA A 375 97.794 91.044 11.393 1.00 31.37 N ANISOU 1634 N ALA A 375 3859 4191 3867 -187 -509 294 N ATOM 1635 CA ALA A 375 98.922 91.873 10.958 1.00 34.46 C ANISOU 1635 CA ALA A 375 4194 4631 4269 -228 -543 311 C ATOM 1636 C ALA A 375 99.870 91.024 10.113 1.00 33.89 C ANISOU 1636 C ALA A 375 4024 4622 4229 -188 -543 326 C ATOM 1637 O ALA A 375 100.975 90.662 10.524 1.00 34.57 O ANISOU 1637 O ALA A 375 4066 4746 4322 -185 -588 351 O ATOM 1638 CB ALA A 375 99.659 92.476 12.152 1.00 28.61 C ANISOU 1638 CB ALA A 375 3490 3879 3500 -275 -613 327 C ATOM 1639 N ASP A 376 99.416 90.702 8.913 1.00 33.38 N ANISOU 1639 N ASP A 376 3930 4570 4183 -151 -493 311 N ATOM 1640 CA ASP A 376 100.247 90.022 7.940 1.00 32.01 C ANISOU 1640 CA ASP A 376 3674 4458 4029 -98 -482 323 C ATOM 1641 C ASP A 376 100.715 91.034 6.894 1.00 35.54 C ANISOU 1641 C ASP A 376 4060 4957 4486 -126 -463 343 C ATOM 1642 O ASP A 376 100.490 92.246 7.015 1.00 31.36 O ANISOU 1642 O ASP A 376 3553 4411 3951 -193 -469 348 O ATOM 1643 CB ASP A 376 99.489 88.839 7.309 1.00 32.91 C ANISOU 1643 CB ASP A 376 3810 4544 4149 -26 -450 292 C ATOM 1644 CG ASP A 376 98.144 89.243 6.712 1.00 42.41 C ANISOU 1644 CG ASP A 376 5060 5701 5354 -39 -411 265 C ATOM 1645 OD1 ASP A 376 97.999 90.384 6.211 1.00 47.11 O ANISOU 1645 OD1 ASP A 376 5645 6308 5945 -80 -391 268 O ATOM 1646 OD2 ASP A 376 97.221 88.404 6.729 1.00 52.95 O ANISOU 1646 OD2 ASP A 376 6438 6985 6694 -10 -403 246 O ATOM 1647 N SER A 377 101.356 90.529 5.840 1.00 33.49 N ANISOU 1647 N SER A 377 3728 4759 4236 -67 -437 356 N ATOM 1648 CA SER A 377 101.901 91.388 4.798 1.00 40.15 C ANISOU 1648 CA SER A 377 4503 5666 5088 -84 -412 388 C ATOM 1649 C SER A 377 100.830 92.217 4.086 1.00 40.42 C ANISOU 1649 C SER A 377 4582 5662 5115 -112 -374 361 C ATOM 1650 O SER A 377 101.157 93.251 3.494 1.00 40.01 O ANISOU 1650 O SER A 377 4490 5643 5067 -154 -363 391 O ATOM 1651 CB SER A 377 102.689 90.522 3.809 1.00 41.46 C ANISOU 1651 CB SER A 377 4594 5905 5254 10 -380 406 C ATOM 1652 OG SER A 377 101.804 89.920 2.877 1.00 54.34 O ANISOU 1652 OG SER A 377 6272 7505 6870 77 -338 360 O ATOM 1653 N MET A 378 99.562 91.818 4.143 1.00 42.84 N ANISOU 1653 N MET A 378 4966 5899 5413 -93 -357 314 N ATOM 1654 CA MET A 378 98.526 92.627 3.510 1.00 43.03 C ANISOU 1654 CA MET A 378 5028 5888 5431 -119 -325 294 C ATOM 1655 C MET A 378 98.058 93.787 4.383 1.00 42.49 C ANISOU 1655 C MET A 378 5014 5775 5356 -198 -344 295 C ATOM 1656 O MET A 378 97.180 94.547 3.960 1.00 41.98 O ANISOU 1656 O MET A 378 4985 5679 5285 -219 -318 281 O ATOM 1657 CB MET A 378 97.325 91.757 3.119 1.00 44.85 C ANISOU 1657 CB MET A 378 5312 6068 5663 -69 -303 252 C ATOM 1658 CG MET A 378 97.379 91.244 1.676 1.00 55.08 C ANISOU 1658 CG MET A 378 6581 7393 6954 0 -273 240 C ATOM 1659 SD MET A 378 97.962 92.468 0.462 1.00 68.66 S ANISOU 1659 SD MET A 378 8242 9181 8665 -17 -237 269 S ATOM 1660 CE MET A 378 96.575 93.596 0.332 1.00 53.82 C ANISOU 1660 CE MET A 378 6424 7240 6786 -78 -222 249 C ATOM 1661 N ASN A 379 98.618 93.961 5.579 1.00 42.28 N ANISOU 1661 N ASN A 379 5000 5740 5324 -237 -391 312 N ATOM 1662 CA ASN A 379 98.255 95.096 6.419 1.00 35.83 C ANISOU 1662 CA ASN A 379 4251 4875 4489 -302 -417 311 C ATOM 1663 C ASN A 379 99.463 95.965 6.771 1.00 33.26 C ANISOU 1663 C ASN A 379 3891 4578 4168 -369 -474 352 C ATOM 1664 O ASN A 379 99.385 96.765 7.709 1.00 31.18 O ANISOU 1664 O ASN A 379 3697 4268 3883 -420 -519 351 O ATOM 1665 CB ASN A 379 97.546 94.613 7.690 1.00 39.69 C ANISOU 1665 CB ASN A 379 4820 5305 4955 -289 -429 290 C ATOM 1666 CG ASN A 379 96.025 94.468 7.501 1.00 38.94 C ANISOU 1666 CG ASN A 379 4780 5162 4854 -260 -377 261 C ATOM 1667 OD1 ASN A 379 95.410 95.214 6.751 1.00 31.95 O ANISOU 1667 OD1 ASN A 379 3903 4267 3969 -271 -346 254 O ATOM 1668 ND2 ASN A 379 95.422 93.520 8.213 1.00 33.71 N ANISOU 1668 ND2 ASN A 379 4152 4469 4188 -225 -371 254 N ATOM 1669 N VAL A 380 100.574 95.848 6.030 1.00 36.11 N ANISOU 1669 N VAL A 380 4150 5015 4555 -367 -477 393 N ATOM 1670 CA VAL A 380 101.760 96.656 6.341 1.00 35.75 C ANISOU 1670 CA VAL A 380 4056 5003 4525 -439 -539 447 C ATOM 1671 C VAL A 380 101.495 98.144 6.125 1.00 33.11 C ANISOU 1671 C VAL A 380 3761 4632 4186 -516 -555 457 C ATOM 1672 O VAL A 380 102.195 98.992 6.699 1.00 35.60 O ANISOU 1672 O VAL A 380 4081 4936 4508 -595 -628 492 O ATOM 1673 CB VAL A 380 102.996 96.247 5.500 1.00 36.62 C ANISOU 1673 CB VAL A 380 4031 5215 4668 -415 -528 505 C ATOM 1674 CG1 VAL A 380 103.623 94.959 6.022 1.00 36.41 C ANISOU 1674 CG1 VAL A 380 3965 5222 4645 -356 -543 511 C ATOM 1675 CG2 VAL A 380 102.681 96.194 3.996 1.00 36.03 C ANISOU 1675 CG2 VAL A 380 3914 5181 4595 -364 -449 504 C ATOM 1676 N ASP A 381 100.516 98.485 5.286 1.00 29.45 N ANISOU 1676 N ASP A 381 3329 4148 3714 -496 -495 428 N ATOM 1677 CA ASP A 381 100.145 99.877 5.040 1.00 30.57 C ANISOU 1677 CA ASP A 381 3519 4249 3848 -559 -505 432 C ATOM 1678 C ASP A 381 99.334 100.509 6.167 1.00 30.89 C ANISOU 1678 C ASP A 381 3693 4195 3850 -584 -539 394 C ATOM 1679 O ASP A 381 99.049 101.710 6.098 1.00 28.88 O ANISOU 1679 O ASP A 381 3496 3895 3583 -634 -558 395 O ATOM 1680 CB ASP A 381 99.330 99.980 3.752 1.00 34.76 C ANISOU 1680 CB ASP A 381 4040 4788 4377 -519 -428 414 C ATOM 1681 CG ASP A 381 98.057 99.163 3.815 1.00 41.97 C ANISOU 1681 CG ASP A 381 5011 5663 5272 -448 -379 356 C ATOM 1682 OD1 ASP A 381 98.165 97.934 4.035 1.00 43.84 O ANISOU 1682 OD1 ASP A 381 5224 5919 5513 -394 -371 344 O ATOM 1683 OD2 ASP A 381 96.962 99.749 3.658 1.00 40.07 O ANISOU 1683 OD2 ASP A 381 4839 5372 5015 -448 -353 328 O ATOM 1684 N LEU A 382 98.919 99.750 7.177 1.00 30.61 N ANISOU 1684 N LEU A 382 3713 4127 3791 -545 -545 362 N ATOM 1685 CA LEU A 382 98.183 100.364 8.273 1.00 34.48 C ANISOU 1685 CA LEU A 382 4333 4535 4235 -556 -571 331 C ATOM 1686 C LEU A 382 99.093 101.265 9.104 1.00 33.67 C ANISOU 1686 C LEU A 382 4272 4401 4120 -634 -672 356 C ATOM 1687 O LEU A 382 100.285 100.986 9.284 1.00 31.24 O ANISOU 1687 O LEU A 382 3892 4137 3840 -669 -728 395 O ATOM 1688 CB LEU A 382 97.569 99.294 9.174 1.00 35.33 C ANISOU 1688 CB LEU A 382 4484 4622 4318 -493 -550 302 C ATOM 1689 CG LEU A 382 96.399 98.481 8.619 1.00 38.37 C ANISOU 1689 CG LEU A 382 4860 5009 4710 -423 -465 277 C ATOM 1690 CD1 LEU A 382 96.024 97.353 9.600 1.00 33.22 C ANISOU 1690 CD1 LEU A 382 4237 4342 4042 -374 -458 266 C ATOM 1691 CD2 LEU A 382 95.178 99.376 8.309 1.00 30.21 C ANISOU 1691 CD2 LEU A 382 3894 3930 3654 -416 -421 257 C ATOM 1692 N THR A 383 98.518 102.349 9.632 1.00 28.05 N ANISOU 1692 N THR A 383 3683 3610 3364 -658 -700 334 N ATOM 1693 CA THR A 383 99.205 103.110 10.672 1.00 26.92 C ANISOU 1693 CA THR A 383 3619 3414 3194 -721 -809 345 C ATOM 1694 C THR A 383 99.320 102.290 11.963 1.00 28.74 C ANISOU 1694 C THR A 383 3899 3630 3392 -686 -841 328 C ATOM 1695 O THR A 383 98.549 101.353 12.204 1.00 27.45 O ANISOU 1695 O THR A 383 3745 3475 3211 -609 -771 302 O ATOM 1696 CB THR A 383 98.460 104.404 10.988 1.00 35.91 C ANISOU 1696 CB THR A 383 4904 4461 4281 -735 -831 317 C ATOM 1697 OG1 THR A 383 97.156 104.078 11.486 1.00 30.63 O ANISOU 1697 OG1 THR A 383 4324 3756 3559 -646 -758 270 O ATOM 1698 CG2 THR A 383 98.355 105.315 9.746 1.00 32.83 C ANISOU 1698 CG2 THR A 383 4476 4076 3922 -775 -807 336 C ATOM 1699 N SER A 384 100.299 102.658 12.802 1.00 24.59 N ANISOU 1699 N SER A 384 3370 2628 3346 -259 -416 176 N ATOM 1700 CA SER A 384 100.378 102.096 14.148 1.00 32.52 C ANISOU 1700 CA SER A 384 4373 3634 4351 -215 -484 149 C ATOM 1701 C SER A 384 99.055 102.228 14.894 1.00 33.59 C ANISOU 1701 C SER A 384 4561 3812 4391 -188 -528 149 C ATOM 1702 O SER A 384 98.647 101.316 15.612 1.00 36.63 O ANISOU 1702 O SER A 384 4974 4214 4728 -158 -538 141 O ATOM 1703 CB SER A 384 101.490 102.769 14.956 1.00 27.53 C ANISOU 1703 CB SER A 384 3686 2942 3832 -188 -559 129 C ATOM 1704 OG SER A 384 102.732 102.688 14.282 1.00 36.93 O ANISOU 1704 OG SER A 384 4810 4080 5141 -211 -510 140 O ATOM 1705 N ALA A 385 98.372 103.359 14.740 1.00 32.48 N ANISOU 1705 N ALA A 385 4433 3682 4227 -195 -548 162 N ATOM 1706 CA ALA A 385 97.087 103.532 15.406 1.00 32.52 C ANISOU 1706 CA ALA A 385 4484 3718 4155 -166 -574 172 C ATOM 1707 C ALA A 385 96.066 102.533 14.886 1.00 35.80 C ANISOU 1707 C ALA A 385 4926 4170 4507 -186 -523 194 C ATOM 1708 O ALA A 385 95.278 101.977 15.661 1.00 31.23 O ANISOU 1708 O ALA A 385 4374 3606 3888 -151 -528 202 O ATOM 1709 CB ALA A 385 96.584 104.959 15.209 1.00 30.74 C ANISOU 1709 CB ALA A 385 4260 3494 3925 -175 -600 185 C ATOM 1710 N ALA A 386 96.073 102.274 13.576 1.00 36.09 N ANISOU 1710 N ALA A 386 4963 4210 4539 -238 -474 208 N ATOM 1711 CA ALA A 386 95.157 101.264 13.053 1.00 34.65 C ANISOU 1711 CA ALA A 386 4812 4048 4306 -257 -446 227 C ATOM 1712 C ALA A 386 95.577 99.869 13.486 1.00 26.71 C ANISOU 1712 C ALA A 386 3805 3044 3299 -238 -428 213 C ATOM 1713 O ALA A 386 94.719 99.011 13.720 1.00 31.58 O ANISOU 1713 O ALA A 386 4438 3676 3884 -229 -425 227 O ATOM 1714 CB ALA A 386 95.061 101.358 11.532 1.00 29.79 C ANISOU 1714 CB ALA A 386 4225 3422 3671 -308 -412 241 C ATOM 1715 N GLN A 387 96.883 99.632 13.649 1.00 31.53 N ANISOU 1715 N GLN A 387 4390 3634 3957 -230 -418 189 N ATOM 1716 CA GLN A 387 97.325 98.325 14.138 1.00 34.91 C ANISOU 1716 CA GLN A 387 4814 4063 4387 -210 -406 173 C ATOM 1717 C GLN A 387 96.865 98.089 15.576 1.00 25.44 C ANISOU 1717 C GLN A 387 3626 2872 3168 -154 -448 166 C ATOM 1718 O GLN A 387 96.517 96.963 15.947 1.00 30.35 O ANISOU 1718 O GLN A 387 4263 3507 3763 -137 -433 168 O ATOM 1719 CB GLN A 387 98.848 98.193 14.027 1.00 32.17 C ANISOU 1719 CB GLN A 387 4428 3680 4115 -213 -389 153 C ATOM 1720 CG GLN A 387 99.395 98.165 12.597 1.00 35.90 C ANISOU 1720 CG GLN A 387 4903 4133 4606 -256 -316 168 C ATOM 1721 CD GLN A 387 99.280 96.808 11.906 1.00 33.51 C ANISOU 1721 CD GLN A 387 4639 3838 4256 -271 -262 173 C ATOM 1722 OE1 GLN A 387 98.633 95.885 12.409 1.00 35.88 O ANISOU 1722 OE1 GLN A 387 4957 4164 4511 -258 -281 169 O ATOM 1723 NE2 GLN A 387 99.926 96.681 10.744 1.00 30.60 N ANISOU 1723 NE2 GLN A 387 4289 3438 3899 -294 -189 186 N ATOM 1724 N ASN A 388 96.853 99.135 16.399 1.00 35.45 N ANISOU 1724 N ASN A 388 4898 4127 4446 -119 -498 159 N ATOM 1725 CA ASN A 388 96.402 98.966 17.777 1.00 32.95 C ANISOU 1725 CA ASN A 388 4618 3806 4096 -52 -529 155 C ATOM 1726 C ASN A 388 94.917 98.655 17.831 1.00 30.18 C ANISOU 1726 C ASN A 388 4292 3481 3694 -43 -494 194 C ATOM 1727 O ASN A 388 94.488 97.780 18.594 1.00 33.45 O ANISOU 1727 O ASN A 388 4730 3896 4082 0 -476 203 O ATOM 1728 CB ASN A 388 96.708 100.218 18.594 1.00 33.31 C ANISOU 1728 CB ASN A 388 4681 3820 4155 -10 -596 139 C ATOM 1729 CG ASN A 388 98.174 100.373 18.858 1.00 43.25 C ANISOU 1729 CG ASN A 388 5913 5033 5487 -4 -650 102 C ATOM 1730 OD1 ASN A 388 98.869 99.387 19.044 1.00 46.19 O ANISOU 1730 OD1 ASN A 388 6273 5393 5882 2 -647 84 O ATOM 1731 ND2 ASN A 388 98.665 101.614 18.855 1.00 47.66 N ANISOU 1731 ND2 ASN A 388 6454 5560 6095 -6 -705 93 N ATOM 1732 N LEU A 389 94.120 99.370 17.034 1.00 31.96 N ANISOU 1732 N LEU A 389 4508 3719 3915 -81 -484 222 N ATOM 1733 CA LEU A 389 92.698 99.065 16.945 1.00 32.90 C ANISOU 1733 CA LEU A 389 4634 3850 4016 -82 -456 266 C ATOM 1734 C LEU A 389 92.486 97.653 16.418 1.00 38.13 C ANISOU 1734 C LEU A 389 5287 4521 4680 -108 -426 276 C ATOM 1735 O LEU A 389 91.704 96.881 16.984 1.00 37.40 O ANISOU 1735 O LEU A 389 5198 4427 4586 -78 -404 303 O ATOM 1736 CB LEU A 389 91.989 100.092 16.060 1.00 37.42 C ANISOU 1736 CB LEU A 389 5196 4426 4596 -125 -465 291 C ATOM 1737 CG LEU A 389 90.469 99.883 15.940 1.00 40.37 C ANISOU 1737 CG LEU A 389 5564 4797 4979 -128 -449 343 C ATOM 1738 CD1 LEU A 389 89.824 100.017 17.296 1.00 47.08 C ANISOU 1738 CD1 LEU A 389 6431 5635 5824 -52 -427 368 C ATOM 1739 CD2 LEU A 389 89.852 100.856 14.954 1.00 35.78 C ANISOU 1739 CD2 LEU A 389 4974 4212 4408 -178 -470 362 C ATOM 1740 N ARG A 390 93.203 97.287 15.351 1.00 31.08 N ANISOU 1740 N ARG A 390 4386 3630 3792 -160 -421 257 N ATOM 1741 CA ARG A 390 93.127 95.916 14.838 1.00 26.51 C ANISOU 1741 CA ARG A 390 3812 3055 3208 -182 -399 261 C ATOM 1742 C ARG A 390 93.428 94.893 15.928 1.00 34.72 C ANISOU 1742 C ARG A 390 4850 4097 4245 -133 -386 249 C ATOM 1743 O ARG A 390 92.703 93.902 16.084 1.00 29.74 O ANISOU 1743 O ARG A 390 4218 3467 3614 -125 -370 272 O ATOM 1744 CB ARG A 390 94.092 95.739 13.665 1.00 26.68 C ANISOU 1744 CB ARG A 390 3842 3068 3225 -228 -383 239 C ATOM 1745 CG ARG A 390 94.016 94.378 13.004 1.00 28.01 C ANISOU 1745 CG ARG A 390 4032 3233 3377 -250 -365 242 C ATOM 1746 CD ARG A 390 95.333 94.035 12.281 1.00 36.54 C ANISOU 1746 CD ARG A 390 5125 4300 4458 -268 -327 216 C ATOM 1747 NE ARG A 390 96.513 94.268 13.116 1.00 37.22 N ANISOU 1747 NE ARG A 390 5171 4384 4584 -240 -320 188 N ATOM 1748 CZ ARG A 390 96.869 93.502 14.148 1.00 41.10 C ANISOU 1748 CZ ARG A 390 5645 4883 5088 -204 -326 171 C ATOM 1749 NH1 ARG A 390 96.132 92.449 14.492 1.00 29.71 N ANISOU 1749 NH1 ARG A 390 4214 3454 3619 -191 -326 182 N ATOM 1750 NH2 ARG A 390 97.958 93.796 14.845 1.00 38.30 N ANISOU 1750 NH2 ARG A 390 5261 4512 4781 -179 -339 145 N ATOM 1751 N GLU A 391 94.490 95.123 16.704 1.00 30.81 N ANISOU 1751 N GLU A 391 4355 3596 3756 -99 -399 214 N ATOM 1752 CA GLU A 391 94.898 94.136 17.700 1.00 35.42 C ANISOU 1752 CA GLU A 391 4949 4175 4334 -52 -394 197 C ATOM 1753 C GLU A 391 93.841 93.974 18.785 1.00 37.34 C ANISOU 1753 C GLU A 391 5219 4415 4554 10 -380 228 C ATOM 1754 O GLU A 391 93.586 92.859 19.258 1.00 41.12 O ANISOU 1754 O GLU A 391 5705 4894 5025 36 -354 237 O ATOM 1755 CB GLU A 391 96.241 94.542 18.313 1.00 35.12 C ANISOU 1755 CB GLU A 391 4911 4114 4319 -26 -432 154 C ATOM 1756 CG GLU A 391 96.827 93.505 19.251 1.00 44.88 C ANISOU 1756 CG GLU A 391 6163 5339 5552 20 -439 130 C ATOM 1757 CD GLU A 391 97.153 92.200 18.560 1.00 53.92 C ANISOU 1757 CD GLU A 391 7284 6499 6705 -18 -399 126 C ATOM 1758 OE1 GLU A 391 97.476 92.229 17.351 1.00 61.41 O ANISOU 1758 OE1 GLU A 391 8208 7452 7672 -76 -376 128 O ATOM 1759 OE2 GLU A 391 97.094 91.144 19.232 1.00 57.23 O ANISOU 1759 OE2 GLU A 391 7720 6920 7106 15 -389 122 O ATOM 1760 N ARG A 392 93.213 95.077 19.184 1.00 36.32 N ANISOU 1760 N ARG A 392 5106 4276 4417 37 -390 247 N ATOM 1761 CA ARG A 392 92.175 95.023 20.206 1.00 40.35 C ANISOU 1761 CA ARG A 392 5648 4771 4911 104 -357 287 C ATOM 1762 C ARG A 392 90.971 94.212 19.730 1.00 38.57 C ANISOU 1762 C ARG A 392 5388 4550 4716 81 -312 340 C ATOM 1763 O ARG A 392 90.414 93.399 20.482 1.00 34.33 O ANISOU 1763 O ARG A 392 4862 3999 4183 130 -268 370 O ATOM 1764 CB ARG A 392 91.756 96.444 20.587 1.00 38.61 C ANISOU 1764 CB ARG A 392 5454 4536 4679 135 -373 300 C ATOM 1765 CG ARG A 392 90.445 96.500 21.368 1.00 51.90 C ANISOU 1765 CG ARG A 392 7164 6198 6358 198 -316 360 C ATOM 1766 CD ARG A 392 89.738 97.832 21.203 1.00 57.77 C ANISOU 1766 CD ARG A 392 7906 6934 7110 195 -320 388 C ATOM 1767 NE ARG A 392 90.642 98.953 21.433 1.00 69.71 N ANISOU 1767 NE ARG A 392 9454 8441 8590 207 -382 341 N ATOM 1768 CZ ARG A 392 90.325 100.226 21.214 1.00 74.75 C ANISOU 1768 CZ ARG A 392 10093 9077 9231 197 -402 351 C ATOM 1769 NH1 ARG A 392 89.114 100.543 20.761 1.00 69.00 N ANISOU 1769 NH1 ARG A 392 9331 8351 8534 176 -364 405 N ATOM 1770 NH2 ARG A 392 91.223 101.179 21.447 1.00 74.88 N ANISOU 1770 NH2 ARG A 392 10139 9082 9230 209 -467 307 N ATOM 1771 N ALA A 393 90.542 94.429 18.484 1.00 33.95 N ANISOU 1771 N ALA A 393 4765 3975 4160 8 -328 356 N ATOM 1772 CA ALA A 393 89.430 93.639 17.965 1.00 30.55 C ANISOU 1772 CA ALA A 393 4299 3532 3775 -19 -311 405 C ATOM 1773 C ALA A 393 89.825 92.177 17.825 1.00 38.51 C ANISOU 1773 C ALA A 393 5302 4546 4783 -30 -302 390 C ATOM 1774 O ALA A 393 89.031 91.277 18.133 1.00 38.65 O ANISOU 1774 O ALA A 393 5299 4547 4839 -11 -273 431 O ATOM 1775 CB ALA A 393 88.955 94.202 16.632 1.00 25.35 C ANISOU 1775 CB ALA A 393 3621 2870 3140 -91 -351 417 C ATOM 1776 N LEU A 394 91.059 91.921 17.386 1.00 37.98 N ANISOU 1776 N LEU A 394 5249 4499 4684 -58 -321 337 N ATOM 1777 CA LEU A 394 91.545 90.550 17.284 1.00 36.32 C ANISOU 1777 CA LEU A 394 5037 4294 4469 -65 -310 319 C ATOM 1778 C LEU A 394 91.480 89.846 18.638 1.00 34.77 C ANISOU 1778 C LEU A 394 4851 4093 4268 7 -274 327 C ATOM 1779 O LEU A 394 90.967 88.728 18.745 1.00 31.67 O ANISOU 1779 O LEU A 394 4443 3693 3897 13 -251 353 O ATOM 1780 CB LEU A 394 92.976 90.546 16.740 1.00 33.05 C ANISOU 1780 CB LEU A 394 4634 3893 4030 -95 -323 265 C ATOM 1781 CG LEU A 394 93.595 89.161 16.545 1.00 37.61 C ANISOU 1781 CG LEU A 394 5214 4476 4602 -105 -308 245 C ATOM 1782 CD1 LEU A 394 92.766 88.342 15.553 1.00 33.43 C ANISOU 1782 CD1 LEU A 394 4684 3936 4081 -148 -316 273 C ATOM 1783 CD2 LEU A 394 95.032 89.292 16.080 1.00 46.93 C ANISOU 1783 CD2 LEU A 394 6398 5658 5776 -127 -307 200 C ATOM 1784 N GLN A 395 91.985 90.501 19.687 1.00 39.57 N ANISOU 1784 N GLN A 395 5493 4695 4845 66 -273 306 N ATOM 1785 CA GLN A 395 92.011 89.883 21.010 1.00 44.96 C ANISOU 1785 CA GLN A 395 6214 5363 5508 146 -242 309 C ATOM 1786 C GLN A 395 90.602 89.605 21.520 1.00 41.80 C ANISOU 1786 C GLN A 395 5806 4938 5136 189 -182 379 C ATOM 1787 O GLN A 395 90.337 88.535 22.084 1.00 44.94 O ANISOU 1787 O GLN A 395 6208 5325 5542 226 -139 399 O ATOM 1788 CB GLN A 395 92.763 90.773 22.000 1.00 34.57 C ANISOU 1788 CB GLN A 395 4957 4029 4149 207 -271 273 C ATOM 1789 CG GLN A 395 92.809 90.190 23.403 1.00 51.55 C ANISOU 1789 CG GLN A 395 7176 6150 6261 302 -245 273 C ATOM 1790 CD GLN A 395 93.565 88.862 23.449 1.00 65.93 C ANISOU 1790 CD GLN A 395 8989 7981 8081 293 -248 242 C ATOM 1791 OE1 GLN A 395 94.699 88.778 22.983 1.00 69.15 O ANISOU 1791 OE1 GLN A 395 9376 8400 8499 250 -297 192 O ATOM 1792 NE2 GLN A 395 92.937 87.824 24.003 1.00 56.83 N ANISOU 1792 NE2 GLN A 395 7848 6819 6925 335 -189 276 N ATOM 1793 N ARG A 396 89.688 90.556 21.333 1.00 37.56 N ANISOU 1793 N ARG A 396 5256 4389 4626 186 -173 421 N ATOM 1794 CA ARG A 396 88.301 90.334 21.723 1.00 49.07 C ANISOU 1794 CA ARG A 396 6691 5813 6142 223 -109 499 C ATOM 1795 C ARG A 396 87.739 89.104 21.019 1.00 48.34 C ANISOU 1795 C ARG A 396 6534 5715 6120 174 -106 531 C ATOM 1796 O ARG A 396 87.176 88.204 21.655 1.00 46.28 O ANISOU 1796 O ARG A 396 6262 5427 5897 220 -47 575 O ATOM 1797 CB ARG A 396 87.467 91.581 21.411 1.00 57.34 C ANISOU 1797 CB ARG A 396 7720 6846 7222 211 -112 538 C ATOM 1798 CG ARG A 396 85.975 91.441 21.697 1.00 73.95 C ANISOU 1798 CG ARG A 396 9781 8901 9416 243 -43 630 C ATOM 1799 CD ARG A 396 85.615 91.922 23.101 1.00 87.63 C ANISOU 1799 CD ARG A 396 11580 10597 11120 357 43 667 C ATOM 1800 NE ARG A 396 84.973 93.236 23.083 1.00 96.30 N ANISOU 1800 NE ARG A 396 12680 11677 12235 367 51 699 N ATOM 1801 CZ ARG A 396 84.542 93.877 24.166 1.00 93.73 C ANISOU 1801 CZ ARG A 396 12420 11311 11883 465 126 738 C ATOM 1802 NH1 ARG A 396 84.686 93.328 25.368 1.00 92.68 N ANISOU 1802 NH1 ARG A 396 12369 11147 11699 567 200 749 N ATOM 1803 NH2 ARG A 396 83.971 95.069 24.046 1.00 87.67 N ANISOU 1803 NH2 ARG A 396 11649 10529 11134 467 130 767 N ATOM 1804 N LEU A 397 87.928 89.026 19.705 1.00 44.78 N ANISOU 1804 N LEU A 397 6049 5282 5683 86 -170 508 N ATOM 1805 CA LEU A 397 87.413 87.880 18.966 1.00 42.28 C ANISOU 1805 CA LEU A 397 5686 4949 5428 40 -188 534 C ATOM 1806 C LEU A 397 88.124 86.593 19.376 1.00 38.43 C ANISOU 1806 C LEU A 397 5213 4478 4912 59 -169 505 C ATOM 1807 O LEU A 397 87.476 85.554 19.550 1.00 34.16 O ANISOU 1807 O LEU A 397 4639 3911 4431 71 -144 547 O ATOM 1808 CB LEU A 397 87.538 88.128 17.459 1.00 32.60 C ANISOU 1808 CB LEU A 397 4454 3729 4202 -49 -267 510 C ATOM 1809 CG LEU A 397 87.010 87.007 16.563 1.00 34.50 C ANISOU 1809 CG LEU A 397 4668 3941 4500 -98 -312 531 C ATOM 1810 CD1 LEU A 397 85.568 86.646 16.946 1.00 32.77 C ANISOU 1810 CD1 LEU A 397 4383 3665 4404 -75 -292 615 C ATOM 1811 CD2 LEU A 397 87.079 87.418 15.084 1.00 32.84 C ANISOU 1811 CD2 LEU A 397 4483 3721 4272 -172 -392 509 C ATOM 1812 N MET A 398 89.451 86.646 19.561 1.00 36.64 N ANISOU 1812 N MET A 398 5031 4285 4604 64 -181 436 N ATOM 1813 CA MET A 398 90.196 85.440 19.924 1.00 40.06 C ANISOU 1813 CA MET A 398 5478 4732 5011 80 -168 405 C ATOM 1814 C MET A 398 89.784 84.916 21.296 1.00 42.35 C ANISOU 1814 C MET A 398 5785 5000 5307 167 -100 439 C ATOM 1815 O MET A 398 89.779 83.703 21.529 1.00 41.05 O ANISOU 1815 O MET A 398 5610 4832 5157 179 -77 446 O ATOM 1816 CB MET A 398 91.705 85.707 19.893 1.00 35.99 C ANISOU 1816 CB MET A 398 4998 4244 4431 71 -197 331 C ATOM 1817 CG MET A 398 92.294 85.913 18.503 1.00 36.24 C ANISOU 1817 CG MET A 398 5021 4292 4457 -8 -240 300 C ATOM 1818 SD MET A 398 92.120 84.470 17.417 1.00 41.87 S ANISOU 1818 SD MET A 398 5720 5001 5187 -64 -253 306 S ATOM 1819 CE MET A 398 90.699 84.966 16.448 1.00 36.11 C ANISOU 1819 CE MET A 398 4971 4241 4510 -108 -291 361 C ATOM 1820 N THR A 399 89.436 85.811 22.220 1.00 46.42 N ANISOU 1820 N THR A 399 6336 5495 5806 235 -63 461 N ATOM 1821 CA THR A 399 89.038 85.359 23.550 1.00 48.73 C ANISOU 1821 CA THR A 399 6669 5753 6091 332 16 498 C ATOM 1822 C THR A 399 87.783 84.494 23.483 1.00 45.01 C ANISOU 1822 C THR A 399 6133 5249 5721 336 74 579 C ATOM 1823 O THR A 399 87.740 83.400 24.057 1.00 45.49 O ANISOU 1823 O THR A 399 6198 5296 5791 376 122 595 O ATOM 1824 CB THR A 399 88.816 86.558 24.468 1.00 53.50 C ANISOU 1824 CB THR A 399 7342 6331 6656 410 47 513 C ATOM 1825 OG1 THR A 399 90.076 87.175 24.753 1.00 54.57 O ANISOU 1825 OG1 THR A 399 7544 6484 6706 421 -16 436 O ATOM 1826 CG2 THR A 399 88.179 86.104 25.773 1.00 46.00 C ANISOU 1826 CG2 THR A 399 6446 5331 5701 522 150 569 C ATOM 1827 N SER A 400 86.748 84.970 22.782 1.00 37.45 N ANISOU 1827 N SER A 400 5111 4269 4850 295 67 634 N ATOM 1828 CA SER A 400 85.534 84.174 22.624 1.00 40.82 C ANISOU 1828 CA SER A 400 5457 4647 5404 290 105 717 C ATOM 1829 C SER A 400 85.811 82.875 21.881 1.00 42.53 C ANISOU 1829 C SER A 400 5634 4878 5647 229 53 695 C ATOM 1830 O SER A 400 85.283 81.822 22.253 1.00 41.40 O ANISOU 1830 O SER A 400 5454 4701 5574 256 100 743 O ATOM 1831 CB SER A 400 84.444 84.973 21.902 1.00 39.75 C ANISOU 1831 CB SER A 400 5256 4477 5369 248 81 774 C ATOM 1832 OG SER A 400 84.154 86.175 22.584 1.00 50.04 O ANISOU 1832 OG SER A 400 6598 5767 6650 307 134 797 O ATOM 1833 N VAL A 401 86.647 82.921 20.839 1.00 42.71 N ANISOU 1833 N VAL A 401 5670 4944 5615 152 -38 625 N ATOM 1834 CA VAL A 401 86.914 81.716 20.059 1.00 38.30 C ANISOU 1834 CA VAL A 401 5089 4392 5071 96 -89 604 C ATOM 1835 C VAL A 401 87.642 80.683 20.911 1.00 45.11 C ANISOU 1835 C VAL A 401 5982 5274 5884 144 -42 577 C ATOM 1836 O VAL A 401 87.247 79.508 20.961 1.00 42.61 O ANISOU 1836 O VAL A 401 5629 4935 5627 147 -28 607 O ATOM 1837 CB VAL A 401 87.699 82.053 18.776 1.00 43.60 C ANISOU 1837 CB VAL A 401 5788 5095 5682 17 -177 539 C ATOM 1838 CG1 VAL A 401 88.210 80.777 18.107 1.00 38.64 C ANISOU 1838 CG1 VAL A 401 5165 4475 5040 -24 -217 508 C ATOM 1839 CG2 VAL A 401 86.828 82.858 17.806 1.00 41.50 C ANISOU 1839 CG2 VAL A 401 5495 4797 5475 -35 -236 572 C ATOM 1840 N THR A 402 88.699 81.101 21.613 1.00 41.66 N ANISOU 1840 N THR A 402 5612 4872 5346 185 -24 520 N ATOM 1841 CA THR A 402 89.435 80.136 22.425 1.00 51.51 C ANISOU 1841 CA THR A 402 6895 6132 6545 231 9 490 C ATOM 1842 C THR A 402 88.574 79.607 23.580 1.00 51.33 C ANISOU 1842 C THR A 402 6871 6064 6567 317 103 558 C ATOM 1843 O THR A 402 88.731 78.449 23.979 1.00 51.00 O ANISOU 1843 O THR A 402 6829 6020 6529 340 132 559 O ATOM 1844 CB THR A 402 90.764 80.745 22.920 1.00 47.07 C ANISOU 1844 CB THR A 402 6404 5598 5881 256 -13 415 C ATOM 1845 OG1 THR A 402 90.532 81.984 23.597 1.00 52.56 O ANISOU 1845 OG1 THR A 402 7142 6277 6552 309 7 428 O ATOM 1846 CG2 THR A 402 91.671 81.042 21.743 1.00 43.33 C ANISOU 1846 CG2 THR A 402 5920 5159 5383 173 -86 356 C ATOM 1847 N ASN A 403 87.609 80.402 24.065 1.00 43.53 N ANISOU 1847 N ASN A 403 5879 5036 5623 366 160 623 N ATOM 1848 CA ASN A 403 86.702 79.939 25.117 1.00 42.90 C ANISOU 1848 CA ASN A 403 5799 4901 5601 455 272 703 C ATOM 1849 C ASN A 403 85.781 78.814 24.654 1.00 48.36 C ANISOU 1849 C ASN A 403 6389 5556 6428 423 286 770 C ATOM 1850 O ASN A 403 85.361 77.991 25.470 1.00 49.48 O ANISOU 1850 O ASN A 403 6528 5659 6612 489 375 822 O ATOM 1851 CB ASN A 403 85.852 81.100 25.639 1.00 35.90 C ANISOU 1851 CB ASN A 403 4929 3971 4740 514 338 764 C ATOM 1852 CG ASN A 403 86.604 81.965 26.623 1.00 44.21 C ANISOU 1852 CG ASN A 403 6108 5031 5660 593 357 718 C ATOM 1853 OD1 ASN A 403 87.704 81.614 27.050 1.00 55.52 O ANISOU 1853 OD1 ASN A 403 7613 6490 6993 614 325 647 O ATOM 1854 ND2 ASN A 403 86.026 83.108 26.980 1.00 50.01 N ANISOU 1854 ND2 ASN A 403 6872 5734 6396 639 399 757 N ATOM 1855 N ARG A 404 85.424 78.773 23.375 1.00 45.77 N ANISOU 1855 N ARG A 404 5986 5230 6175 327 197 773 N ATOM 1856 CA ARG A 404 84.566 77.724 22.837 1.00 37.68 C ANISOU 1856 CA ARG A 404 4867 4159 5290 289 179 832 C ATOM 1857 C ARG A 404 85.340 76.783 21.922 1.00 39.94 C ANISOU 1857 C ARG A 404 5155 4484 5535 214 82 765 C ATOM 1858 O ARG A 404 84.756 76.119 21.060 1.00 40.69 O ANISOU 1858 O ARG A 404 5186 4544 5731 157 14 794 O ATOM 1859 CB ARG A 404 83.385 78.328 22.075 1.00 53.51 C ANISOU 1859 CB ARG A 404 6790 6108 7433 244 137 899 C ATOM 1860 CG ARG A 404 82.199 78.754 22.928 1.00 70.56 C ANISOU 1860 CG ARG A 404 8903 8195 9713 319 252 1007 C ATOM 1861 CD ARG A 404 81.037 79.181 22.030 1.00 77.12 C ANISOU 1861 CD ARG A 404 9634 8960 10709 260 187 1073 C ATOM 1862 NE ARG A 404 79.890 79.678 22.789 1.00 82.97 N ANISOU 1862 NE ARG A 404 10320 9622 11582 331 305 1183 N ATOM 1863 CZ ARG A 404 78.784 78.978 23.031 1.00 78.81 C ANISOU 1863 CZ ARG A 404 9687 9002 11255 356 363 1292 C ATOM 1864 NH1 ARG A 404 78.669 77.736 22.580 1.00 72.93 N ANISOU 1864 NH1 ARG A 404 8881 8232 10596 314 302 1300 N ATOM 1865 NH2 ARG A 404 77.790 79.522 23.725 1.00 80.99 N ANISOU 1865 NH2 ARG A 404 9918 9202 11653 426 487 1396 N ATOM 1866 N CYS A 405 86.657 76.701 22.111 1.00 45.06 N ANISOU 1866 N CYS A 405 5881 5197 6044 218 71 679 N ATOM 1867 CA CYS A 405 87.516 76.141 21.073 1.00 40.07 C ANISOU 1867 CA CYS A 405 5264 4604 5359 143 -20 609 C ATOM 1868 C CYS A 405 87.198 74.673 20.796 1.00 43.30 C ANISOU 1868 C CYS A 405 5627 4987 5837 123 -38 633 C ATOM 1869 O CYS A 405 87.204 74.237 19.636 1.00 46.09 O ANISOU 1869 O CYS A 405 5969 5333 6208 52 -129 615 O ATOM 1870 CB CYS A 405 88.980 76.326 21.464 1.00 43.51 C ANISOU 1870 CB CYS A 405 5776 5099 5658 160 -15 523 C ATOM 1871 SG CYS A 405 90.111 75.752 20.224 1.00 57.81 S ANISOU 1871 SG CYS A 405 7605 6947 7413 94 -81 452 S ATOM 1872 N GLN A 406 86.900 73.897 21.840 1.00 34.38 N ANISOU 1872 N GLN A 406 4480 3837 4747 189 46 674 N ATOM 1873 CA GLN A 406 86.631 72.480 21.625 1.00 46.96 C ANISOU 1873 CA GLN A 406 6026 5405 6410 172 28 696 C ATOM 1874 C GLN A 406 85.395 72.280 20.755 1.00 43.93 C ANISOU 1874 C GLN A 406 5557 4951 6185 122 -39 766 C ATOM 1875 O GLN A 406 85.394 71.441 19.844 1.00 46.62 O ANISOU 1875 O GLN A 406 5883 5276 6556 64 -131 751 O ATOM 1876 CB GLN A 406 86.465 71.758 22.962 1.00 60.73 C ANISOU 1876 CB GLN A 406 7768 7131 8175 261 143 737 C ATOM 1877 CG GLN A 406 86.744 70.269 22.892 1.00 75.27 C ANISOU 1877 CG GLN A 406 9592 8976 10031 248 129 725 C ATOM 1878 CD GLN A 406 87.980 69.870 23.685 1.00 82.37 C ANISOU 1878 CD GLN A 406 10572 9931 10793 292 170 655 C ATOM 1879 OE1 GLN A 406 88.776 70.724 24.088 1.00 76.56 O ANISOU 1879 OE1 GLN A 406 9909 9233 9947 317 181 602 O ATOM 1880 NE2 GLN A 406 88.152 68.565 23.903 1.00 86.07 N ANISOU 1880 NE2 GLN A 406 11028 10399 11277 301 183 654 N ATOM 1881 N GLU A 407 84.334 73.047 21.008 1.00 36.68 N ANISOU 1881 N GLU A 407 4586 3978 5374 146 -2 842 N ATOM 1882 CA GLU A 407 83.118 72.836 20.232 1.00 47.55 C ANISOU 1882 CA GLU A 407 5869 5269 6928 100 -77 915 C ATOM 1883 C GLU A 407 83.254 73.392 18.819 1.00 48.91 C ANISOU 1883 C GLU A 407 6072 5446 7067 13 -221 867 C ATOM 1884 O GLU A 407 82.648 72.850 17.886 1.00 55.28 O ANISOU 1884 O GLU A 407 6840 6189 7976 -41 -335 890 O ATOM 1885 CB GLU A 407 81.907 73.422 20.958 1.00 50.98 C ANISOU 1885 CB GLU A 407 6227 5632 7511 156 16 1022 C ATOM 1886 CG GLU A 407 81.812 74.923 20.987 1.00 74.38 C ANISOU 1886 CG GLU A 407 9221 8611 10431 163 33 1019 C ATOM 1887 CD GLU A 407 80.371 75.402 20.897 1.00 91.25 C ANISOU 1887 CD GLU A 407 11252 10648 12770 166 42 1127 C ATOM 1888 OE1 GLU A 407 79.894 75.637 19.766 1.00 93.72 O ANISOU 1888 OE1 GLU A 407 11527 10922 13162 90 -90 1131 O ATOM 1889 OE2 GLU A 407 79.710 75.529 21.954 1.00 97.57 O ANISOU 1889 OE2 GLU A 407 12014 11402 13656 248 183 1212 O ATOM 1890 N LEU A 408 84.071 74.435 18.627 1.00 38.97 N ANISOU 1890 N LEU A 408 4890 4251 5664 3 -224 799 N ATOM 1891 CA LEU A 408 84.350 74.896 17.268 1.00 38.58 C ANISOU 1891 CA LEU A 408 4891 4208 5561 -73 -348 748 C ATOM 1892 C LEU A 408 85.210 73.889 16.518 1.00 39.14 C ANISOU 1892 C LEU A 408 5021 4302 5547 -112 -415 683 C ATOM 1893 O LEU A 408 84.971 73.624 15.333 1.00 36.29 O ANISOU 1893 O LEU A 408 4686 3897 5206 -168 -534 674 O ATOM 1894 CB LEU A 408 85.026 76.273 17.295 1.00 35.11 C ANISOU 1894 CB LEU A 408 4513 3827 5002 -70 -321 699 C ATOM 1895 CG LEU A 408 84.180 77.351 17.991 1.00 41.58 C ANISOU 1895 CG LEU A 408 5286 4620 5894 -28 -257 762 C ATOM 1896 CD1 LEU A 408 84.957 78.647 18.269 1.00 37.44 C ANISOU 1896 CD1 LEU A 408 4826 4158 5243 -12 -219 711 C ATOM 1897 CD2 LEU A 408 82.952 77.632 17.174 1.00 50.43 C ANISOU 1897 CD2 LEU A 408 6344 5658 7160 -73 -344 824 C ATOM 1898 N ALA A 409 86.195 73.292 17.202 1.00 36.17 N ANISOU 1898 N ALA A 409 4678 3988 5078 -79 -343 638 N ATOM 1899 CA ALA A 409 87.115 72.377 16.531 1.00 27.74 C ANISOU 1899 CA ALA A 409 3670 2946 3923 -112 -391 575 C ATOM 1900 C ALA A 409 86.413 71.113 16.051 1.00 30.93 C ANISOU 1900 C ALA A 409 4039 3285 4430 -135 -467 611 C ATOM 1901 O ALA A 409 86.831 70.512 15.050 1.00 32.99 O ANISOU 1901 O ALA A 409 4361 3536 4637 -177 -551 570 O ATOM 1902 CB ALA A 409 88.276 72.027 17.467 1.00 30.67 C ANISOU 1902 CB ALA A 409 4072 3389 4193 -68 -300 525 C ATOM 1903 N THR A 410 85.346 70.696 16.732 1.00 30.82 N ANISOU 1903 N THR A 410 3927 3215 4566 -105 -437 692 N ATOM 1904 CA THR A 410 84.654 69.470 16.353 1.00 36.56 C ANISOU 1904 CA THR A 410 4606 3870 5416 -125 -513 733 C ATOM 1905 C THR A 410 83.448 69.700 15.450 1.00 34.75 C ANISOU 1905 C THR A 410 4332 3536 5334 -169 -642 790 C ATOM 1906 O THR A 410 82.764 68.731 15.123 1.00 39.59 O ANISOU 1906 O THR A 410 4896 4070 6076 -186 -724 832 O ATOM 1907 CB THR A 410 84.207 68.692 17.607 1.00 37.88 C ANISOU 1907 CB THR A 410 4685 4021 5685 -65 -405 797 C ATOM 1908 OG1 THR A 410 83.377 69.523 18.432 1.00 40.59 O ANISOU 1908 OG1 THR A 410 4960 4335 6127 -18 -315 871 O ATOM 1909 CG2 THR A 410 85.425 68.230 18.415 1.00 32.88 C ANISOU 1909 CG2 THR A 410 4109 3478 4906 -24 -307 735 C ATOM 1910 N ASN A 411 83.156 70.941 15.060 1.00 39.66 N ANISOU 1910 N ASN A 411 4968 4149 5952 -187 -669 794 N ATOM 1911 CA ASN A 411 81.996 71.234 14.223 1.00 34.58 C ANISOU 1911 CA ASN A 411 4283 3398 5457 -227 -801 847 C ATOM 1912 C ASN A 411 82.392 71.177 12.748 1.00 38.20 C ANISOU 1912 C ASN A 411 4864 3833 5816 -285 -956 782 C ATOM 1913 O ASN A 411 83.518 71.526 12.373 1.00 29.79 O ANISOU 1913 O ASN A 411 3912 2846 4562 -293 -932 702 O ATOM 1914 CB ASN A 411 81.404 72.603 14.578 1.00 30.74 C ANISOU 1914 CB ASN A 411 3751 2906 5025 -213 -749 891 C ATOM 1915 CG ASN A 411 80.289 73.037 13.634 1.00 33.31 C ANISOU 1915 CG ASN A 411 4041 3118 5495 -260 -898 938 C ATOM 1916 OD1 ASN A 411 80.511 73.810 12.686 1.00 33.34 O ANISOU 1916 OD1 ASN A 411 4132 3124 5410 -299 -986 892 O ATOM 1917 ND2 ASN A 411 79.078 72.539 13.885 1.00 35.43 N ANISOU 1917 ND2 ASN A 411 4183 3280 6000 -254 -927 1035 N ATOM 1918 N GLU A 412 81.449 70.709 11.916 1.00 31.36 N ANISOU 1918 N GLU A 412 3979 2848 5087 -322 -1117 821 N ATOM 1919 CA GLU A 412 81.724 70.473 10.500 1.00 30.68 C ANISOU 1919 CA GLU A 412 4031 2714 4910 -366 -1280 765 C ATOM 1920 C GLU A 412 82.104 71.752 9.757 1.00 34.86 C ANISOU 1920 C GLU A 412 4667 3270 5309 -386 -1303 718 C ATOM 1921 O GLU A 412 82.793 71.686 8.731 1.00 35.24 O ANISOU 1921 O GLU A 412 4866 3316 5205 -405 -1372 652 O ATOM 1922 CB GLU A 412 80.500 69.843 9.825 1.00 30.52 C ANISOU 1922 CB GLU A 412 3968 2540 5088 -396 -1469 824 C ATOM 1923 CG GLU A 412 79.249 70.684 9.972 1.00 43.83 C ANISOU 1923 CG GLU A 412 5537 4143 6975 -405 -1508 907 C ATOM 1924 CD GLU A 412 78.050 70.126 9.218 1.00 61.01 C ANISOU 1924 CD GLU A 412 7670 6147 9366 -439 -1721 965 C ATOM 1925 OE1 GLU A 412 78.240 69.402 8.203 1.00 54.25 O ANISOU 1925 OE1 GLU A 412 6934 5228 8449 -464 -1883 920 O ATOM 1926 OE2 GLU A 412 76.914 70.424 9.660 1.00 62.63 O ANISOU 1926 OE2 GLU A 412 7721 6270 9806 -437 -1726 1059 O ATOM 1927 N TYR A 413 81.636 72.915 10.222 1.00 36.04 N ANISOU 1927 N TYR A 413 4745 3432 5516 -378 -1244 755 N ATOM 1928 CA TYR A 413 81.950 74.188 9.577 1.00 33.03 C ANISOU 1928 CA TYR A 413 4452 3074 5022 -396 -1260 715 C ATOM 1929 C TYR A 413 82.923 75.045 10.365 1.00 37.54 C ANISOU 1929 C TYR A 413 5030 3775 5461 -366 -1089 677 C ATOM 1930 O TYR A 413 83.685 75.803 9.762 1.00 34.73 O ANISOU 1930 O TYR A 413 4778 3461 4957 -378 -1083 620 O ATOM 1931 CB TYR A 413 80.673 75.017 9.341 1.00 40.80 C ANISOU 1931 CB TYR A 413 5365 3966 6170 -417 -1349 781 C ATOM 1932 CG TYR A 413 79.641 74.349 8.451 1.00 43.96 C ANISOU 1932 CG TYR A 413 5765 4215 6724 -451 -1554 820 C ATOM 1933 CD1 TYR A 413 79.955 73.988 7.146 1.00 47.74 C ANISOU 1933 CD1 TYR A 413 6407 4636 7094 -479 -1708 763 C ATOM 1934 CD2 TYR A 413 78.365 74.061 8.921 1.00 45.79 C ANISOU 1934 CD2 TYR A 413 5836 4348 7215 -450 -1595 917 C ATOM 1935 CE1 TYR A 413 79.031 73.367 6.331 1.00 49.36 C ANISOU 1935 CE1 TYR A 413 6629 4690 7436 -506 -1918 794 C ATOM 1936 CE2 TYR A 413 77.429 73.431 8.109 1.00 49.50 C ANISOU 1936 CE2 TYR A 413 6297 4664 7846 -483 -1802 954 C ATOM 1937 CZ TYR A 413 77.770 73.090 6.809 1.00 48.69 C ANISOU 1937 CZ TYR A 413 6371 4507 7624 -512 -1974 889 C ATOM 1938 OH TYR A 413 76.855 72.475 5.973 1.00 51.79 O ANISOU 1938 OH TYR A 413 6774 4732 8170 -541 -2205 920 O ATOM 1939 N ALA A 414 82.896 74.979 11.693 1.00 35.30 N ANISOU 1939 N ALA A 414 4640 3542 5228 -323 -953 711 N ATOM 1940 CA ALA A 414 83.732 75.887 12.461 1.00 35.08 C ANISOU 1940 CA ALA A 414 4624 3618 5087 -291 -814 677 C ATOM 1941 C ALA A 414 85.179 75.412 12.555 1.00 38.85 C ANISOU 1941 C ALA A 414 5182 4182 5398 -279 -749 599 C ATOM 1942 O ALA A 414 86.061 76.224 12.863 1.00 34.05 O ANISOU 1942 O ALA A 414 4610 3648 4680 -264 -670 556 O ATOM 1943 CB ALA A 414 83.141 76.078 13.860 1.00 35.45 C ANISOU 1943 CB ALA A 414 4555 3675 5242 -238 -696 743 C ATOM 1944 N ASN A 415 85.441 74.127 12.273 1.00 35.63 N ANISOU 1944 N ASN A 415 4801 3758 4980 -286 -787 583 N ATOM 1945 CA ASN A 415 86.798 73.598 12.394 1.00 39.10 C ANISOU 1945 CA ASN A 415 5305 4271 5278 -274 -720 516 C ATOM 1946 C ASN A 415 87.762 74.352 11.489 1.00 41.33 C ANISOU 1946 C ASN A 415 5702 4584 5417 -296 -726 453 C ATOM 1947 O ASN A 415 88.945 74.485 11.822 1.00 41.49 O ANISOU 1947 O ASN A 415 5752 4676 5337 -279 -639 404 O ATOM 1948 CB ASN A 415 86.829 72.093 12.073 1.00 31.95 C ANISOU 1948 CB ASN A 415 4418 3332 4388 -282 -774 511 C ATOM 1949 CG ASN A 415 86.626 71.801 10.577 1.00 36.67 C ANISOU 1949 CG ASN A 415 5122 3852 4959 -324 -919 494 C ATOM 1950 OD1 ASN A 415 87.575 71.808 9.789 1.00 34.74 O ANISOU 1950 OD1 ASN A 415 4997 3626 4574 -334 -922 436 O ATOM 1951 ND2 ASN A 415 85.386 71.527 10.192 1.00 32.84 N ANISOU 1951 ND2 ASN A 415 4597 3267 4614 -344 -1041 549 N ATOM 1952 N TYR A 416 87.271 74.872 10.355 1.00 31.84 N ANISOU 1952 N TYR A 416 4564 3320 4214 -330 -829 457 N ATOM 1953 CA TYR A 416 88.119 75.687 9.486 1.00 33.32 C ANISOU 1953 CA TYR A 416 4864 3527 4270 -344 -821 406 C ATOM 1954 C TYR A 416 88.624 76.937 10.204 1.00 31.83 C ANISOU 1954 C TYR A 416 4633 3410 4050 -327 -719 395 C ATOM 1955 O TYR A 416 89.719 77.424 9.906 1.00 30.55 O ANISOU 1955 O TYR A 416 4534 3289 3783 -326 -663 349 O ATOM 1956 CB TYR A 416 87.359 76.080 8.214 1.00 33.75 C ANISOU 1956 CB TYR A 416 5001 3490 4333 -377 -956 418 C ATOM 1957 CG TYR A 416 86.991 74.914 7.323 1.00 33.96 C ANISOU 1957 CG TYR A 416 5107 3429 4368 -392 -1080 418 C ATOM 1958 CD1 TYR A 416 87.892 74.411 6.392 1.00 38.26 C ANISOU 1958 CD1 TYR A 416 5802 3961 4773 -390 -1087 368 C ATOM 1959 CD2 TYR A 416 85.735 74.323 7.404 1.00 33.50 C ANISOU 1959 CD2 TYR A 416 4976 3289 4464 -404 -1192 473 C ATOM 1960 CE1 TYR A 416 87.552 73.336 5.568 1.00 37.76 C ANISOU 1960 CE1 TYR A 416 5832 3809 4706 -397 -1211 367 C ATOM 1961 CE2 TYR A 416 85.386 73.248 6.584 1.00 34.73 C ANISOU 1961 CE2 TYR A 416 5209 3353 4635 -417 -1327 472 C ATOM 1962 CZ TYR A 416 86.293 72.767 5.672 1.00 41.53 C ANISOU 1962 CZ TYR A 416 6236 4206 5339 -412 -1340 416 C ATOM 1963 OH TYR A 416 85.948 71.710 4.861 1.00 51.75 O ANISOU 1963 OH TYR A 416 7625 5402 6638 -418 -1481 414 O ATOM 1964 N ILE A 417 87.858 77.453 11.165 1.00 34.50 N ANISOU 1964 N ILE A 417 4866 3757 4484 -309 -691 441 N ATOM 1965 CA ILE A 417 88.289 78.648 11.879 1.00 32.41 C ANISOU 1965 CA ILE A 417 4573 3552 4189 -287 -606 430 C ATOM 1966 C ILE A 417 89.468 78.327 12.787 1.00 31.67 C ANISOU 1966 C ILE A 417 4472 3530 4032 -252 -506 391 C ATOM 1967 O ILE A 417 90.462 79.059 12.811 1.00 27.38 O ANISOU 1967 O ILE A 417 3960 3029 3413 -248 -458 349 O ATOM 1968 CB ILE A 417 87.113 79.260 12.662 1.00 27.75 C ANISOU 1968 CB ILE A 417 3888 2940 3715 -269 -597 494 C ATOM 1969 CG1 ILE A 417 86.007 79.721 11.698 1.00 30.34 C ANISOU 1969 CG1 ILE A 417 4222 3190 4116 -308 -708 531 C ATOM 1970 CG2 ILE A 417 87.583 80.428 13.514 1.00 23.88 C ANISOU 1970 CG2 ILE A 417 3381 2508 3183 -236 -511 481 C ATOM 1971 CD1 ILE A 417 84.693 80.070 12.403 1.00 33.98 C ANISOU 1971 CD1 ILE A 417 4573 3607 4728 -291 -703 610 C ATOM 1972 N ILE A 418 89.385 77.223 13.538 1.00 31.26 N ANISOU 1972 N ILE A 418 4376 3484 4019 -226 -478 404 N ATOM 1973 CA ILE A 418 90.506 76.828 14.395 1.00 29.92 C ANISOU 1973 CA ILE A 418 4205 3372 3791 -192 -397 364 C ATOM 1974 C ILE A 418 91.732 76.489 13.551 1.00 34.80 C ANISOU 1974 C ILE A 418 4899 4006 4316 -216 -397 306 C ATOM 1975 O ILE A 418 92.861 76.886 13.877 1.00 34.95 O ANISOU 1975 O ILE A 418 4931 4066 4281 -202 -341 266 O ATOM 1976 CB ILE A 418 90.089 75.650 15.297 1.00 39.91 C ANISOU 1976 CB ILE A 418 5416 4631 5117 -159 -371 394 C ATOM 1977 CG1 ILE A 418 88.749 75.965 15.978 1.00 38.38 C ANISOU 1977 CG1 ILE A 418 5147 4400 5034 -133 -360 467 C ATOM 1978 CG2 ILE A 418 91.180 75.329 16.338 1.00 30.34 C ANISOU 1978 CG2 ILE A 418 4206 3472 3848 -116 -293 354 C ATOM 1979 CD1 ILE A 418 88.763 77.289 16.767 1.00 30.66 C ANISOU 1979 CD1 ILE A 418 4160 3447 4041 -96 -302 473 C ATOM 1980 N GLN A 419 91.531 75.755 12.452 1.00 28.14 N ANISOU 1980 N GLN A 419 4112 3120 3459 -248 -461 305 N ATOM 1981 CA GLN A 419 92.637 75.476 11.536 1.00 33.18 C ANISOU 1981 CA GLN A 419 4841 3761 4006 -264 -448 259 C ATOM 1982 C GLN A 419 93.309 76.758 11.064 1.00 31.76 C ANISOU 1982 C GLN A 419 4701 3593 3772 -272 -415 236 C ATOM 1983 O GLN A 419 94.539 76.822 10.990 1.00 30.06 O ANISOU 1983 O GLN A 419 4511 3402 3507 -265 -350 201 O ATOM 1984 CB GLN A 419 92.149 74.687 10.327 1.00 26.73 C ANISOU 1984 CB GLN A 419 4106 2878 3173 -290 -535 266 C ATOM 1985 CG GLN A 419 91.769 73.246 10.659 1.00 30.60 C ANISOU 1985 CG GLN A 419 4566 3352 3709 -283 -565 279 C ATOM 1986 CD GLN A 419 91.465 72.465 9.405 1.00 34.91 C ANISOU 1986 CD GLN A 419 5216 3825 4225 -305 -662 277 C ATOM 1987 OE1 GLN A 419 92.372 72.125 8.627 1.00 34.11 O ANISOU 1987 OE1 GLN A 419 5220 3716 4025 -305 -640 241 O ATOM 1988 NE2 GLN A 419 90.180 72.233 9.160 1.00 33.03 N ANISOU 1988 NE2 GLN A 419 4956 3518 4076 -321 -772 320 N ATOM 1989 N HIS A 420 92.516 77.775 10.709 1.00 29.32 N ANISOU 1989 N HIS A 420 4395 3260 3485 -287 -460 261 N ATOM 1990 CA HIS A 420 93.085 79.017 10.192 1.00 32.66 C ANISOU 1990 CA HIS A 420 4859 3690 3862 -296 -432 243 C ATOM 1991 C HIS A 420 93.954 79.695 11.245 1.00 37.58 C ANISOU 1991 C HIS A 420 5417 4371 4492 -270 -354 223 C ATOM 1992 O HIS A 420 95.058 80.165 10.944 1.00 35.23 O ANISOU 1992 O HIS A 420 5147 4083 4157 -270 -302 195 O ATOM 1993 CB HIS A 420 91.969 79.959 9.733 1.00 35.56 C ANISOU 1993 CB HIS A 420 5232 4021 4259 -317 -501 275 C ATOM 1994 CG HIS A 420 92.463 81.273 9.204 1.00 52.05 C ANISOU 1994 CG HIS A 420 7361 6115 6303 -325 -475 260 C ATOM 1995 ND1 HIS A 420 92.524 81.560 7.856 1.00 56.58 N ANISOU 1995 ND1 HIS A 420 8047 6637 6813 -345 -506 254 N ATOM 1996 CD2 HIS A 420 92.939 82.370 9.842 1.00 52.54 C ANISOU 1996 CD2 HIS A 420 7371 6218 6372 -313 -420 252 C ATOM 1997 CE1 HIS A 420 93.009 82.778 7.688 1.00 55.15 C ANISOU 1997 CE1 HIS A 420 7874 6471 6609 -347 -463 245 C ATOM 1998 NE2 HIS A 420 93.270 83.291 8.876 1.00 50.35 N ANISOU 1998 NE2 HIS A 420 7163 5920 6048 -330 -415 243 N ATOM 1999 N ILE A 421 93.479 79.748 12.489 1.00 30.97 N ANISOU 1999 N ILE A 421 4499 3559 3709 -243 -345 241 N ATOM 2000 CA ILE A 421 94.270 80.377 13.541 1.00 34.36 C ANISOU 2000 CA ILE A 421 4886 4028 4140 -211 -291 219 C ATOM 2001 C ILE A 421 95.557 79.598 13.779 1.00 35.13 C ANISOU 2001 C ILE A 421 4990 4145 4215 -199 -246 180 C ATOM 2002 O ILE A 421 96.636 80.184 13.923 1.00 31.43 O ANISOU 2002 O ILE A 421 4516 3686 3740 -192 -212 152 O ATOM 2003 CB ILE A 421 93.449 80.506 14.834 1.00 33.94 C ANISOU 2003 CB ILE A 421 4774 3986 4136 -172 -287 249 C ATOM 2004 CG1 ILE A 421 92.256 81.442 14.606 1.00 32.00 C ANISOU 2004 CG1 ILE A 421 4514 3717 3926 -183 -321 292 C ATOM 2005 CG2 ILE A 421 94.369 80.987 15.960 1.00 27.75 C ANISOU 2005 CG2 ILE A 421 3972 3231 3340 -129 -246 220 C ATOM 2006 CD1 ILE A 421 91.141 81.294 15.595 1.00 27.53 C ANISOU 2006 CD1 ILE A 421 3894 3140 3426 -146 -311 342 C ATOM 2007 N VAL A 422 95.471 78.266 13.765 1.00 35.47 N ANISOU 2007 N VAL A 422 5038 4183 4255 -198 -250 181 N ATOM 2008 CA VAL A 422 96.625 77.428 14.078 1.00 39.52 C ANISOU 2008 CA VAL A 422 5550 4712 4755 -184 -208 147 C ATOM 2009 C VAL A 422 97.649 77.458 12.945 1.00 34.12 C ANISOU 2009 C VAL A 422 4921 4009 4034 -208 -176 124 C ATOM 2010 O VAL A 422 98.855 77.413 13.190 1.00 35.29 O ANISOU 2010 O VAL A 422 5054 4164 4191 -197 -129 97 O ATOM 2011 CB VAL A 422 96.154 75.988 14.403 1.00 37.57 C ANISOU 2011 CB VAL A 422 5292 4464 4517 -174 -221 157 C ATOM 2012 CG1 VAL A 422 97.309 75.005 14.343 1.00 35.28 C ANISOU 2012 CG1 VAL A 422 5018 4182 4205 -171 -184 123 C ATOM 2013 CG2 VAL A 422 95.505 75.945 15.781 1.00 30.02 C ANISOU 2013 CG2 VAL A 422 4280 3524 3602 -132 -216 179 C ATOM 2014 N SER A 423 97.204 77.574 11.705 1.00 31.51 N ANISOU 2014 N SER A 423 4661 3645 3667 -235 -199 138 N ATOM 2015 CA SER A 423 98.121 77.480 10.578 1.00 40.08 C ANISOU 2015 CA SER A 423 5821 4700 4706 -246 -153 124 C ATOM 2016 C SER A 423 98.806 78.795 10.222 1.00 36.12 C ANISOU 2016 C SER A 423 5324 4190 4210 -249 -108 121 C ATOM 2017 O SER A 423 99.649 78.796 9.323 1.00 34.30 O ANISOU 2017 O SER A 423 5154 3927 3951 -251 -47 116 O ATOM 2018 CB SER A 423 97.377 76.979 9.344 1.00 38.45 C ANISOU 2018 CB SER A 423 5720 4445 4444 -264 -202 139 C ATOM 2019 OG SER A 423 96.415 76.027 9.720 1.00 49.50 O ANISOU 2019 OG SER A 423 7097 5844 5865 -266 -269 153 O ATOM 2020 N ASN A 424 98.455 79.904 10.864 1.00 35.80 N ANISOU 2020 N ASN A 424 5226 4170 4205 -247 -130 127 N ATOM 2021 CA ASN A 424 98.916 81.223 10.444 1.00 38.70 C ANISOU 2021 CA ASN A 424 5599 4525 4581 -254 -101 128 C ATOM 2022 C ASN A 424 99.998 81.721 11.392 1.00 38.47 C ANISOU 2022 C ASN A 424 5487 4512 4616 -235 -66 109 C ATOM 2023 O ASN A 424 99.725 81.970 12.571 1.00 33.43 O ANISOU 2023 O ASN A 424 4789 3902 4010 -216 -103 103 O ATOM 2024 CB ASN A 424 97.763 82.224 10.406 1.00 44.05 C ANISOU 2024 CB ASN A 424 6276 5206 5256 -266 -160 149 C ATOM 2025 CG ASN A 424 98.098 83.459 9.573 1.00 53.77 C ANISOU 2025 CG ASN A 424 7543 6412 6475 -279 -133 155 C ATOM 2026 OD1 ASN A 424 99.212 83.990 9.639 1.00 56.53 O ANISOU 2026 OD1 ASN A 424 7864 6756 6857 -271 -73 144 O ATOM 2027 ND2 ASN A 424 97.139 83.907 8.775 1.00 65.90 N ANISOU 2027 ND2 ASN A 424 9140 7924 7974 -298 -179 174 N ATOM 2028 N ASP A 425 101.211 81.908 10.865 1.00 35.26 N ANISOU 2028 N ASP A 425 5086 4076 4235 -235 5 104 N ATOM 2029 CA ASP A 425 102.305 82.360 11.719 1.00 34.50 C ANISOU 2029 CA ASP A 425 4906 3977 4225 -218 22 87 C ATOM 2030 C ASP A 425 102.004 83.715 12.339 1.00 31.53 C ANISOU 2030 C ASP A 425 4486 3612 3882 -214 -26 88 C ATOM 2031 O ASP A 425 102.408 83.980 13.477 1.00 31.08 O ANISOU 2031 O ASP A 425 4367 3561 3880 -192 -62 70 O ATOM 2032 CB ASP A 425 103.609 82.416 10.924 1.00 43.53 C ANISOU 2032 CB ASP A 425 6052 5071 5416 -220 115 94 C ATOM 2033 CG ASP A 425 104.214 81.040 10.685 1.00 43.82 C ANISOU 2033 CG ASP A 425 6111 5094 5445 -213 166 89 C ATOM 2034 OD1 ASP A 425 103.851 80.078 11.403 1.00 42.24 O ANISOU 2034 OD1 ASP A 425 5898 4927 5224 -205 121 72 O ATOM 2035 OD2 ASP A 425 105.061 80.927 9.778 1.00 45.53 O ANISOU 2035 OD2 ASP A 425 6359 5263 5678 -210 260 105 O ATOM 2036 N ASP A 426 101.268 84.575 11.634 1.00 31.29 N ANISOU 2036 N ASP A 426 4496 3579 3815 -232 -35 107 N ATOM 2037 CA ASP A 426 101.027 85.896 12.200 1.00 24.82 C ANISOU 2037 CA ASP A 426 3636 2768 3027 -228 -76 108 C ATOM 2038 C ASP A 426 100.011 85.873 13.336 1.00 33.49 C ANISOU 2038 C ASP A 426 4715 3903 4108 -207 -145 106 C ATOM 2039 O ASP A 426 99.771 86.918 13.948 1.00 34.03 O ANISOU 2039 O ASP A 426 4758 3976 4195 -194 -181 106 O ATOM 2040 CB ASP A 426 100.599 86.870 11.094 1.00 31.56 C ANISOU 2040 CB ASP A 426 4538 3605 3850 -252 -62 130 C ATOM 2041 CG ASP A 426 101.746 87.188 10.121 1.00 38.42 C ANISOU 2041 CG ASP A 426 5422 4426 4751 -259 25 139 C ATOM 2042 OD1 ASP A 426 101.540 87.087 8.897 1.00 41.48 O ANISOU 2042 OD1 ASP A 426 5896 4786 5079 -271 67 157 O ATOM 2043 OD2 ASP A 426 102.863 87.519 10.585 1.00 36.75 O ANISOU 2043 OD2 ASP A 426 5139 4193 4632 -247 50 132 O ATOM 2044 N LEU A 427 99.440 84.704 13.647 1.00 28.13 N ANISOU 2044 N LEU A 427 4049 3242 3398 -199 -157 107 N ATOM 2045 CA LEU A 427 98.572 84.508 14.803 1.00 31.86 C ANISOU 2045 CA LEU A 427 4503 3738 3864 -168 -198 112 C ATOM 2046 C LEU A 427 99.212 83.581 15.840 1.00 35.30 C ANISOU 2046 C LEU A 427 4916 4179 4317 -133 -197 88 C ATOM 2047 O LEU A 427 98.513 82.920 16.614 1.00 33.14 O ANISOU 2047 O LEU A 427 4643 3920 4027 -105 -210 97 O ATOM 2048 CB LEU A 427 97.227 83.955 14.339 1.00 34.66 C ANISOU 2048 CB LEU A 427 4887 4099 4185 -184 -216 143 C ATOM 2049 CG LEU A 427 96.474 84.898 13.390 1.00 34.34 C ANISOU 2049 CG LEU A 427 4874 4045 4129 -215 -235 167 C ATOM 2050 CD1 LEU A 427 95.335 84.168 12.723 1.00 31.73 C ANISOU 2050 CD1 LEU A 427 4576 3700 3782 -237 -268 195 C ATOM 2051 CD2 LEU A 427 95.965 86.143 14.150 1.00 28.07 C ANISOU 2051 CD2 LEU A 427 4050 3260 3356 -195 -259 179 C ATOM 2052 N ALA A 428 100.547 83.561 15.883 1.00 28.42 N ANISOU 2052 N ALA A 428 4021 3288 3489 -131 -181 62 N ATOM 2053 CA ALA A 428 101.280 82.534 16.627 1.00 33.61 C ANISOU 2053 CA ALA A 428 4662 3942 4167 -106 -181 37 C ATOM 2054 C ALA A 428 100.874 82.472 18.098 1.00 35.82 C ANISOU 2054 C ALA A 428 4944 4230 4436 -53 -226 28 C ATOM 2055 O ALA A 428 100.774 81.377 18.667 1.00 34.93 O ANISOU 2055 O ALA A 428 4839 4126 4306 -30 -223 22 O ATOM 2056 CB ALA A 428 102.784 82.771 16.493 1.00 27.98 C ANISOU 2056 CB ALA A 428 3909 3190 3531 -112 -165 16 C ATOM 2057 N VAL A 429 100.622 83.620 18.734 1.00 33.08 N ANISOU 2057 N VAL A 429 4601 3873 4093 -27 -265 29 N ATOM 2058 CA VAL A 429 100.280 83.570 20.155 1.00 39.09 C ANISOU 2058 CA VAL A 429 5392 4629 4832 38 -301 22 C ATOM 2059 C VAL A 429 98.903 82.935 20.346 1.00 34.40 C ANISOU 2059 C VAL A 429 4821 4061 4189 54 -270 58 C ATOM 2060 O VAL A 429 98.649 82.238 21.335 1.00 34.10 O ANISOU 2060 O VAL A 429 4809 4019 4128 105 -267 59 O ATOM 2061 CB VAL A 429 100.370 84.970 20.798 1.00 46.42 C ANISOU 2061 CB VAL A 429 6335 5530 5771 70 -353 14 C ATOM 2062 CG1 VAL A 429 101.684 85.642 20.444 1.00 47.79 C ANISOU 2062 CG1 VAL A 429 6468 5669 6021 46 -385 -13 C ATOM 2063 CG2 VAL A 429 99.192 85.836 20.395 1.00 51.61 C ANISOU 2063 CG2 VAL A 429 7002 6208 6399 58 -337 51 C ATOM 2064 N TYR A 430 98.002 83.138 19.392 1.00 29.48 N ANISOU 2064 N TYR A 430 4189 3455 3557 12 -249 92 N ATOM 2065 CA TYR A 430 96.691 82.512 19.491 1.00 39.05 C ANISOU 2065 CA TYR A 430 5405 4677 4754 22 -226 135 C ATOM 2066 C TYR A 430 96.761 81.036 19.143 1.00 32.10 C ANISOU 2066 C TYR A 430 4518 3806 3874 4 -207 134 C ATOM 2067 O TYR A 430 96.072 80.225 19.762 1.00 33.28 O ANISOU 2067 O TYR A 430 4667 3955 4022 35 -189 157 O ATOM 2068 CB TYR A 430 95.694 83.267 18.611 1.00 36.49 C ANISOU 2068 CB TYR A 430 5074 4354 4438 -16 -230 172 C ATOM 2069 CG TYR A 430 95.593 84.687 19.085 1.00 41.11 C ANISOU 2069 CG TYR A 430 5667 4931 5022 8 -247 173 C ATOM 2070 CD1 TYR A 430 95.044 84.971 20.328 1.00 36.99 C ANISOU 2070 CD1 TYR A 430 5169 4398 4490 77 -239 191 C ATOM 2071 CD2 TYR A 430 96.093 85.740 18.325 1.00 38.70 C ANISOU 2071 CD2 TYR A 430 5356 4624 4723 -29 -266 159 C ATOM 2072 CE1 TYR A 430 94.959 86.277 20.797 1.00 36.18 C ANISOU 2072 CE1 TYR A 430 5086 4282 4378 106 -257 191 C ATOM 2073 CE2 TYR A 430 96.016 87.047 18.778 1.00 40.48 C ANISOU 2073 CE2 TYR A 430 5590 4841 4950 -6 -287 159 C ATOM 2074 CZ TYR A 430 95.436 87.308 20.012 1.00 42.63 C ANISOU 2074 CZ TYR A 430 5889 5103 5207 61 -287 174 C ATOM 2075 OH TYR A 430 95.340 88.595 20.478 1.00 48.49 O ANISOU 2075 OH TYR A 430 6651 5831 5942 89 -311 175 O ATOM 2076 N ARG A 431 97.612 80.672 18.186 1.00 32.43 N ANISOU 2076 N ARG A 431 4555 3850 3918 -42 -203 110 N ATOM 2077 CA ARG A 431 97.933 79.270 17.980 1.00 39.80 C ANISOU 2077 CA ARG A 431 5489 4788 4846 -52 -185 100 C ATOM 2078 C ARG A 431 98.406 78.616 19.275 1.00 39.24 C ANISOU 2078 C ARG A 431 5416 4717 4775 2 -184 78 C ATOM 2079 O ARG A 431 97.929 77.533 19.645 1.00 28.47 O ANISOU 2079 O ARG A 431 4053 3360 3404 19 -169 92 O ATOM 2080 CB ARG A 431 98.993 79.138 16.894 1.00 40.09 C ANISOU 2080 CB ARG A 431 5531 4817 4885 -94 -168 76 C ATOM 2081 CG ARG A 431 99.684 77.794 16.900 1.00 32.54 C ANISOU 2081 CG ARG A 431 4574 3862 3928 -93 -146 56 C ATOM 2082 CD ARG A 431 100.446 77.607 15.609 1.00 40.14 C ANISOU 2082 CD ARG A 431 5558 4808 4886 -133 -111 49 C ATOM 2083 NE ARG A 431 101.611 78.465 15.477 1.00 38.62 N ANISOU 2083 NE ARG A 431 5344 4594 4737 -136 -90 32 N ATOM 2084 CZ ARG A 431 102.038 79.009 14.332 1.00 37.75 C ANISOU 2084 CZ ARG A 431 5255 4459 4629 -164 -51 41 C ATOM 2085 NH1 ARG A 431 101.382 78.839 13.184 1.00 37.02 N ANISOU 2085 NH1 ARG A 431 5226 4360 4481 -189 -39 61 N ATOM 2086 NH2 ARG A 431 103.133 79.745 14.340 1.00 40.08 N ANISOU 2086 NH2 ARG A 431 5514 4727 4989 -162 -27 31 N ATOM 2087 N GLU A 432 99.333 79.267 19.990 1.00 31.29 N ANISOU 2087 N GLU A 432 4411 3696 3782 31 -206 46 N ATOM 2088 CA GLU A 432 99.891 78.641 21.188 1.00 31.93 C ANISOU 2088 CA GLU A 432 4507 3764 3860 85 -220 19 C ATOM 2089 C GLU A 432 98.839 78.514 22.273 1.00 34.91 C ANISOU 2089 C GLU A 432 4921 4140 4205 148 -210 47 C ATOM 2090 O GLU A 432 98.799 77.512 22.999 1.00 34.91 O ANISOU 2090 O GLU A 432 4939 4137 4189 186 -195 45 O ATOM 2091 CB GLU A 432 101.119 79.418 21.693 1.00 33.73 C ANISOU 2091 CB GLU A 432 4735 3959 4124 103 -269 -21 C ATOM 2092 CG GLU A 432 102.259 79.430 20.661 1.00 51.99 C ANISOU 2092 CG GLU A 432 7000 6260 6493 48 -259 -40 C ATOM 2093 CD GLU A 432 103.579 80.028 21.162 1.00 57.25 C ANISOU 2093 CD GLU A 432 7644 6877 7231 63 -312 -75 C ATOM 2094 OE1 GLU A 432 104.489 80.199 20.319 1.00 55.16 O ANISOU 2094 OE1 GLU A 432 7332 6592 7033 22 -291 -79 O ATOM 2095 OE2 GLU A 432 103.713 80.325 22.373 1.00 55.47 O ANISOU 2095 OE2 GLU A 432 7452 6622 7001 120 -376 -96 O ATOM 2096 N CYS A 433 97.953 79.501 22.373 1.00 31.42 N ANISOU 2096 N CYS A 433 4491 3694 3754 162 -207 79 N ATOM 2097 CA CYS A 433 96.924 79.448 23.396 1.00 35.29 C ANISOU 2097 CA CYS A 433 5017 4170 4220 230 -177 116 C ATOM 2098 C CYS A 433 95.878 78.384 23.075 1.00 40.99 C ANISOU 2098 C CYS A 433 5709 4903 4960 217 -128 164 C ATOM 2099 O CYS A 433 95.363 77.721 23.985 1.00 35.85 O ANISOU 2099 O CYS A 433 5082 4238 4302 276 -88 189 O ATOM 2100 CB CYS A 433 96.293 80.831 23.537 1.00 48.31 C ANISOU 2100 CB CYS A 433 6684 5806 5864 249 -182 140 C ATOM 2101 SG CYS A 433 94.793 80.874 24.501 1.00 65.18 S ANISOU 2101 SG CYS A 433 8856 7918 7989 327 -116 208 S ATOM 2102 N ILE A 434 95.565 78.195 21.793 1.00 37.02 N ANISOU 2102 N ILE A 434 5161 4418 4486 143 -134 178 N ATOM 2103 CA ILE A 434 94.669 77.116 21.396 1.00 36.78 C ANISOU 2103 CA ILE A 434 5100 4387 4488 124 -112 220 C ATOM 2104 C ILE A 434 95.291 75.764 21.718 1.00 38.40 C ANISOU 2104 C ILE A 434 5309 4600 4680 135 -101 195 C ATOM 2105 O ILE A 434 94.636 74.866 22.261 1.00 44.20 O ANISOU 2105 O ILE A 434 6035 5324 5434 168 -68 228 O ATOM 2106 CB ILE A 434 94.329 77.237 19.902 1.00 37.86 C ANISOU 2106 CB ILE A 434 5212 4527 4646 46 -144 231 C ATOM 2107 CG1 ILE A 434 93.326 78.371 19.685 1.00 39.04 C ANISOU 2107 CG1 ILE A 434 5350 4661 4824 40 -152 273 C ATOM 2108 CG2 ILE A 434 93.807 75.908 19.364 1.00 33.11 C ANISOU 2108 CG2 ILE A 434 4590 3918 4074 19 -148 254 C ATOM 2109 CD1 ILE A 434 92.762 78.405 18.305 1.00 50.04 C ANISOU 2109 CD1 ILE A 434 6730 6041 6241 -27 -193 292 C ATOM 2110 N ILE A 435 96.565 75.589 21.378 1.00 37.64 N ANISOU 2110 N ILE A 435 5220 4518 4563 109 -124 140 N ATOM 2111 CA ILE A 435 97.204 74.299 21.622 1.00 37.12 C ANISOU 2111 CA ILE A 435 5154 4459 4490 115 -115 115 C ATOM 2112 C ILE A 435 97.217 73.999 23.113 1.00 36.78 C ANISOU 2112 C ILE A 435 5146 4402 4428 197 -96 113 C ATOM 2113 O ILE A 435 96.816 72.916 23.550 1.00 33.32 O ANISOU 2113 O ILE A 435 4706 3962 3993 222 -66 132 O ATOM 2114 CB ILE A 435 98.623 74.280 21.028 1.00 46.14 C ANISOU 2114 CB ILE A 435 6294 5607 5629 78 -135 62 C ATOM 2115 CG1 ILE A 435 98.572 74.339 19.494 1.00 38.42 C ANISOU 2115 CG1 ILE A 435 5307 4636 4656 8 -136 70 C ATOM 2116 CG2 ILE A 435 99.395 73.052 21.517 1.00 43.99 C ANISOU 2116 CG2 ILE A 435 6024 5337 5352 95 -128 32 C ATOM 2117 CD1 ILE A 435 99.931 74.568 18.852 1.00 23.74 C ANISOU 2117 CD1 ILE A 435 3446 2770 2805 -22 -133 31 C ATOM 2118 N GLU A 436 97.625 74.986 23.923 1.00 45.98 N ANISOU 2118 N GLU A 436 6352 5548 5571 244 -116 92 N ATOM 2119 CA GLU A 436 97.823 74.755 25.351 1.00 48.14 C ANISOU 2119 CA GLU A 436 6689 5794 5809 331 -111 80 C ATOM 2120 C GLU A 436 96.503 74.629 26.103 1.00 45.29 C ANISOU 2120 C GLU A 436 6355 5413 5440 396 -46 143 C ATOM 2121 O GLU A 436 96.409 73.843 27.050 1.00 45.41 O ANISOU 2121 O GLU A 436 6414 5408 5431 461 -12 150 O ATOM 2122 CB GLU A 436 98.671 75.877 25.963 1.00 50.90 C ANISOU 2122 CB GLU A 436 7088 6112 6138 366 -170 37 C ATOM 2123 CG GLU A 436 100.137 75.880 25.532 1.00 63.04 C ANISOU 2123 CG GLU A 436 8598 7648 7708 321 -231 -21 C ATOM 2124 CD GLU A 436 100.915 77.084 26.066 1.00 81.53 C ANISOU 2124 CD GLU A 436 10976 9947 10055 351 -305 -57 C ATOM 2125 OE1 GLU A 436 100.812 77.374 27.277 1.00 87.49 O ANISOU 2125 OE1 GLU A 436 11818 10660 10766 434 -332 -64 O ATOM 2126 OE2 GLU A 436 101.627 77.743 25.274 1.00 87.17 O ANISOU 2126 OE2 GLU A 436 11639 10661 10821 295 -337 -76 O ATOM 2127 N LYS A 437 95.475 75.374 25.705 1.00 36.88 N ANISOU 2127 N LYS A 437 5266 4347 4402 383 -21 193 N ATOM 2128 CA LYS A 437 94.262 75.441 26.508 1.00 46.54 C ANISOU 2128 CA LYS A 437 6514 5537 5633 455 52 260 C ATOM 2129 C LYS A 437 93.128 74.603 25.944 1.00 54.33 C ANISOU 2129 C LYS A 437 7424 6523 6695 423 99 326 C ATOM 2130 O LYS A 437 92.146 74.352 26.653 1.00 56.01 O ANISOU 2130 O LYS A 437 7644 6700 6939 487 176 392 O ATOM 2131 CB LYS A 437 93.813 76.907 26.667 1.00 50.24 C ANISOU 2131 CB LYS A 437 7011 5987 6092 479 52 280 C ATOM 2132 CG LYS A 437 94.808 77.746 27.493 1.00 50.58 C ANISOU 2132 CG LYS A 437 7147 6009 6064 533 0 222 C ATOM 2133 CD LYS A 437 94.545 79.251 27.446 1.00 62.59 C ANISOU 2133 CD LYS A 437 8689 7517 7576 540 -20 230 C ATOM 2134 CE LYS A 437 93.469 79.688 28.421 1.00 71.95 C ANISOU 2134 CE LYS A 437 9943 8656 8740 638 59 292 C ATOM 2135 NZ LYS A 437 92.145 79.832 27.752 1.00 77.15 N ANISOU 2135 NZ LYS A 437 10518 9320 9475 602 121 369 N ATOM 2136 N CYS A 438 93.260 74.127 24.714 1.00 45.47 N ANISOU 2136 N CYS A 438 6237 5431 5610 332 55 313 N ATOM 2137 CA CYS A 438 92.181 73.424 24.039 1.00 36.80 C ANISOU 2137 CA CYS A 438 5067 4320 4595 294 69 373 C ATOM 2138 C CYS A 438 92.578 72.013 23.625 1.00 32.83 C ANISOU 2138 C CYS A 438 4540 3833 4100 259 51 353 C ATOM 2139 O CYS A 438 91.870 71.049 23.937 1.00 40.12 O ANISOU 2139 O CYS A 438 5433 4733 5079 282 90 400 O ATOM 2140 CB CYS A 438 91.759 74.284 22.829 1.00 45.06 C ANISOU 2140 CB CYS A 438 6076 5369 5676 221 17 384 C ATOM 2141 SG CYS A 438 90.376 73.757 21.795 1.00 70.66 S ANISOU 2141 SG CYS A 438 9237 8577 9031 161 -13 451 S ATOM 2142 N LEU A 439 93.700 71.853 22.935 1.00 35.75 N ANISOU 2142 N LEU A 439 4923 4237 4425 207 -1 287 N ATOM 2143 CA LEU A 439 94.048 70.545 22.396 1.00 37.72 C ANISOU 2143 CA LEU A 439 5153 4499 4681 169 -19 269 C ATOM 2144 C LEU A 439 94.904 69.712 23.347 1.00 40.57 C ANISOU 2144 C LEU A 439 5546 4870 5000 216 6 232 C ATOM 2145 O LEU A 439 94.778 68.481 23.360 1.00 37.30 O ANISOU 2145 O LEU A 439 5112 4455 4605 214 18 242 O ATOM 2146 CB LEU A 439 94.769 70.705 21.058 1.00 34.09 C ANISOU 2146 CB LEU A 439 4697 4059 4197 92 -75 226 C ATOM 2147 CG LEU A 439 94.193 71.768 20.118 1.00 40.18 C ANISOU 2147 CG LEU A 439 5461 4818 4987 49 -108 247 C ATOM 2148 CD1 LEU A 439 95.057 71.931 18.869 1.00 36.05 C ANISOU 2148 CD1 LEU A 439 4965 4308 4425 -12 -145 203 C ATOM 2149 CD2 LEU A 439 92.748 71.469 19.748 1.00 36.83 C ANISOU 2149 CD2 LEU A 439 4995 4356 4641 35 -124 315 C ATOM 2150 N MET A 440 95.778 70.349 24.125 1.00 36.61 N ANISOU 2150 N MET A 440 5094 4372 4445 258 4 188 N ATOM 2151 CA MET A 440 96.632 69.625 25.058 1.00 37.75 C ANISOU 2151 CA MET A 440 5278 4514 4550 306 11 149 C ATOM 2152 C MET A 440 95.782 68.876 26.077 1.00 30.90 C ANISOU 2152 C MET A 440 4427 3622 3693 379 76 199 C ATOM 2153 O MET A 440 94.810 69.416 26.607 1.00 31.71 O ANISOU 2153 O MET A 440 4542 3695 3812 429 124 254 O ATOM 2154 CB MET A 440 97.569 70.605 25.765 1.00 43.68 C ANISOU 2154 CB MET A 440 6087 5252 5256 345 -23 101 C ATOM 2155 CG MET A 440 98.952 70.075 26.027 1.00 57.81 C ANISOU 2155 CG MET A 440 7896 7043 7027 345 -63 36 C ATOM 2156 SD MET A 440 99.907 69.711 24.531 1.00 61.54 S ANISOU 2156 SD MET A 440 8303 7546 7532 244 -93 0 S ATOM 2157 CE MET A 440 100.626 68.198 25.079 1.00 60.31 C ANISOU 2157 CE MET A 440 8155 7392 7368 264 -89 -31 C ATOM 2158 N ARG A 441 96.156 67.624 26.345 1.00 33.53 N ANISOU 2158 N ARG A 441 4760 3961 4019 388 86 183 N ATOM 2159 CA ARG A 441 95.427 66.675 27.181 1.00 40.75 C ANISOU 2159 CA ARG A 441 5682 4851 4952 450 154 231 C ATOM 2160 C ARG A 441 94.148 66.171 26.513 1.00 39.06 C ANISOU 2160 C ARG A 441 5386 4625 4829 415 182 306 C ATOM 2161 O ARG A 441 93.421 65.376 27.116 1.00 35.54 O ANISOU 2161 O ARG A 441 4927 4151 4426 463 246 359 O ATOM 2162 CB ARG A 441 95.104 67.247 28.573 1.00 45.47 C ANISOU 2162 CB ARG A 441 6365 5405 5508 560 211 255 C ATOM 2163 CG ARG A 441 96.373 67.561 29.387 1.00 53.27 C ANISOU 2163 CG ARG A 441 7448 6383 6409 606 163 180 C ATOM 2164 CD ARG A 441 96.062 68.200 30.729 1.00 53.14 C ANISOU 2164 CD ARG A 441 7547 6310 6333 724 207 200 C ATOM 2165 NE ARG A 441 95.516 69.541 30.548 1.00 67.62 N ANISOU 2165 NE ARG A 441 9385 8133 8174 726 211 227 N ATOM 2166 CZ ARG A 441 96.257 70.627 30.349 1.00 71.75 C ANISOU 2166 CZ ARG A 441 9932 8660 8667 704 131 175 C ATOM 2167 NH1 ARG A 441 97.581 70.529 30.311 1.00 71.27 N ANISOU 2167 NH1 ARG A 441 9888 8609 8582 678 43 98 N ATOM 2168 NH2 ARG A 441 95.676 71.811 30.186 1.00 69.13 N ANISOU 2168 NH2 ARG A 441 9603 8320 8344 706 140 204 N ATOM 2169 N ASN A 442 93.869 66.571 25.270 1.00 32.74 N ANISOU 2169 N ASN A 442 4533 3838 4069 335 131 311 N ATOM 2170 CA ASN A 442 92.712 66.074 24.537 1.00 33.79 C ANISOU 2170 CA ASN A 442 4591 3946 4300 295 127 376 C ATOM 2171 C ASN A 442 93.095 65.476 23.188 1.00 34.00 C ANISOU 2171 C ASN A 442 4594 3994 4332 207 48 342 C ATOM 2172 O ASN A 442 92.210 65.231 22.358 1.00 34.66 O ANISOU 2172 O ASN A 442 4628 4048 4491 163 11 386 O ATOM 2173 CB ASN A 442 91.690 67.193 24.317 1.00 27.76 C ANISOU 2173 CB ASN A 442 3801 3153 3595 294 134 432 C ATOM 2174 CG ASN A 442 91.014 67.636 25.602 1.00 36.87 C ANISOU 2174 CG ASN A 442 4977 4267 4764 390 230 489 C ATOM 2175 OD1 ASN A 442 90.160 66.939 26.131 1.00 46.91 O ANISOU 2175 OD1 ASN A 442 6213 5496 6113 434 298 558 O ATOM 2176 ND2 ASN A 442 91.390 68.819 26.102 1.00 42.20 N ANISOU 2176 ND2 ASN A 442 5716 4949 5369 428 240 464 N ATOM 2177 N LEU A 443 94.384 65.244 22.943 1.00 34.42 N ANISOU 2177 N LEU A 443 4684 4085 4308 183 21 269 N ATOM 2178 CA LEU A 443 94.832 64.895 21.599 1.00 29.27 C ANISOU 2178 CA LEU A 443 4032 3446 3643 108 -41 237 C ATOM 2179 C LEU A 443 94.283 63.548 21.152 1.00 28.93 C ANISOU 2179 C LEU A 443 3957 3383 3650 85 -63 264 C ATOM 2180 O LEU A 443 93.875 63.398 19.998 1.00 30.37 O ANISOU 2180 O LEU A 443 4136 3545 3859 31 -125 276 O ATOM 2181 CB LEU A 443 96.355 64.892 21.543 1.00 25.81 C ANISOU 2181 CB LEU A 443 3634 3042 3131 98 -46 162 C ATOM 2182 CG LEU A 443 97.021 66.245 21.750 1.00 23.91 C ANISOU 2182 CG LEU A 443 3420 2811 2854 107 -46 130 C ATOM 2183 CD1 LEU A 443 98.534 66.082 21.544 1.00 25.39 C ANISOU 2183 CD1 LEU A 443 3628 3016 3003 90 -55 65 C ATOM 2184 CD2 LEU A 443 96.449 67.290 20.769 1.00 26.55 C ANISOU 2184 CD2 LEU A 443 3749 3135 3204 64 -75 152 C ATOM 2185 N LEU A 444 94.274 62.554 22.042 1.00 26.96 N ANISOU 2185 N LEU A 444 3695 3134 3415 128 -21 274 N ATOM 2186 CA LEU A 444 93.759 61.242 21.662 1.00 28.17 C ANISOU 2186 CA LEU A 444 3813 3266 3626 107 -45 302 C ATOM 2187 C LEU A 444 92.272 61.315 21.321 1.00 34.17 C ANISOU 2187 C LEU A 444 4513 3967 4504 96 -71 383 C ATOM 2188 O LEU A 444 91.827 60.775 20.302 1.00 35.19 O ANISOU 2188 O LEU A 444 4627 4064 4680 46 -149 397 O ATOM 2189 CB LEU A 444 94.014 60.241 22.786 1.00 30.41 C ANISOU 2189 CB LEU A 444 4092 3557 3904 163 15 302 C ATOM 2190 CG LEU A 444 93.479 58.829 22.536 1.00 35.40 C ANISOU 2190 CG LEU A 444 4681 4164 4604 148 -5 334 C ATOM 2191 CD1 LEU A 444 94.114 58.260 21.261 1.00 32.90 C ANISOU 2191 CD1 LEU A 444 4394 3862 4246 80 -84 285 C ATOM 2192 CD2 LEU A 444 93.737 57.909 23.754 1.00 28.44 C ANISOU 2192 CD2 LEU A 444 3801 3291 3713 211 67 336 C ATOM 2193 N SER A 445 91.490 61.987 22.169 1.00 29.18 N ANISOU 2193 N SER A 445 3850 3310 3926 147 -10 439 N ATOM 2194 CA SER A 445 90.070 62.185 21.896 1.00 31.61 C ANISOU 2194 CA SER A 445 4087 3552 4370 139 -27 523 C ATOM 2195 C SER A 445 89.840 62.945 20.591 1.00 32.23 C ANISOU 2195 C SER A 445 4175 3616 4455 71 -125 513 C ATOM 2196 O SER A 445 89.058 62.510 19.734 1.00 27.81 O ANISOU 2196 O SER A 445 3579 3001 3987 27 -209 549 O ATOM 2197 CB SER A 445 89.428 62.931 23.061 1.00 39.06 C ANISOU 2197 CB SER A 445 5013 4473 5355 215 76 582 C ATOM 2198 OG SER A 445 88.060 62.629 23.136 1.00 51.14 O ANISOU 2198 OG SER A 445 6455 5928 7050 227 93 681 O ATOM 2199 N LEU A 446 90.491 64.101 20.429 1.00 26.46 N ANISOU 2199 N LEU A 446 3498 2925 3631 63 -123 467 N ATOM 2200 CA LEU A 446 90.207 64.921 19.252 1.00 29.56 C ANISOU 2200 CA LEU A 446 3905 3297 4028 6 -205 463 C ATOM 2201 C LEU A 446 90.721 64.273 17.970 1.00 36.57 C ANISOU 2201 C LEU A 446 4846 4184 4866 -54 -296 417 C ATOM 2202 O LEU A 446 90.165 64.517 16.888 1.00 28.74 O ANISOU 2202 O LEU A 446 3868 3145 3906 -99 -387 431 O ATOM 2203 CB LEU A 446 90.810 66.314 19.414 1.00 27.06 C ANISOU 2203 CB LEU A 446 3632 3022 3629 15 -174 427 C ATOM 2204 CG LEU A 446 90.212 67.195 20.520 1.00 35.26 C ANISOU 2204 CG LEU A 446 4642 4050 4705 75 -97 474 C ATOM 2205 CD1 LEU A 446 91.085 68.445 20.692 1.00 29.13 C ANISOU 2205 CD1 LEU A 446 3921 3318 3828 84 -79 421 C ATOM 2206 CD2 LEU A 446 88.735 67.571 20.245 1.00 30.40 C ANISOU 2206 CD2 LEU A 446 3958 3367 4225 66 -119 559 C ATOM 2207 N SER A 447 91.777 63.456 18.068 1.00 29.90 N ANISOU 2207 N SER A 447 4039 3379 3941 -51 -274 363 N ATOM 2208 CA SER A 447 92.300 62.757 16.900 1.00 32.14 C ANISOU 2208 CA SER A 447 4386 3656 4171 -97 -344 323 C ATOM 2209 C SER A 447 91.299 61.756 16.339 1.00 31.31 C ANISOU 2209 C SER A 447 4254 3481 4160 -119 -432 368 C ATOM 2210 O SER A 447 91.397 61.375 15.168 1.00 33.74 O ANISOU 2210 O SER A 447 4631 3755 4433 -157 -519 347 O ATOM 2211 CB SER A 447 93.603 62.044 17.266 1.00 34.19 C ANISOU 2211 CB SER A 447 4677 3968 4343 -82 -290 265 C ATOM 2212 OG SER A 447 94.659 62.990 17.400 1.00 36.00 O ANISOU 2212 OG SER A 447 4942 4243 4492 -76 -241 217 O ATOM 2213 N GLN A 448 90.342 61.319 17.141 1.00 27.01 N ANISOU 2213 N GLN A 448 3619 2904 3738 -91 -412 432 N ATOM 2214 CA GLN A 448 89.346 60.370 16.678 1.00 39.58 C ANISOU 2214 CA GLN A 448 5169 4418 5451 -111 -502 483 C ATOM 2215 C GLN A 448 88.096 61.055 16.157 1.00 41.46 C ANISOU 2215 C GLN A 448 5365 4576 5813 -134 -583 545 C ATOM 2216 O GLN A 448 87.120 60.370 15.833 1.00 39.03 O ANISOU 2216 O GLN A 448 5004 4183 5643 -149 -671 599 O ATOM 2217 CB GLN A 448 89.005 59.382 17.799 1.00 35.78 C ANISOU 2217 CB GLN A 448 4604 3932 5057 -67 -432 527 C ATOM 2218 CG GLN A 448 90.246 58.692 18.341 1.00 39.80 C ANISOU 2218 CG GLN A 448 5158 4517 5449 -45 -360 464 C ATOM 2219 CD GLN A 448 89.959 57.792 19.529 1.00 36.66 C ANISOU 2219 CD GLN A 448 4691 4117 5123 7 -279 506 C ATOM 2220 OE1 GLN A 448 89.385 56.733 19.370 1.00 41.13 O ANISOU 2220 OE1 GLN A 448 5211 4633 5783 -2 -324 543 O ATOM 2221 NE2 GLN A 448 90.365 58.213 20.719 1.00 34.04 N ANISOU 2221 NE2 GLN A 448 4359 3830 4743 65 -163 500 N ATOM 2222 N GLU A 449 88.122 62.387 16.046 1.00 37.21 N ANISOU 2222 N GLU A 449 4848 4056 5235 -137 -565 537 N ATOM 2223 CA GLU A 449 86.997 63.176 15.556 1.00 40.18 C ANISOU 2223 CA GLU A 449 5187 4359 5722 -159 -639 592 C ATOM 2224 C GLU A 449 87.145 63.471 14.068 1.00 41.41 C ANISOU 2224 C GLU A 449 5448 4479 5809 -211 -771 551 C ATOM 2225 O GLU A 449 88.244 63.753 13.581 1.00 38.93 O ANISOU 2225 O GLU A 449 5238 4220 5335 -221 -753 480 O ATOM 2226 CB GLU A 449 86.896 64.488 16.331 1.00 36.77 C ANISOU 2226 CB GLU A 449 4721 3963 5286 -127 -540 611 C ATOM 2227 CG GLU A 449 86.457 64.299 17.774 1.00 46.33 C ANISOU 2227 CG GLU A 449 5841 5179 6584 -63 -414 670 C ATOM 2228 CD GLU A 449 84.962 64.427 17.942 1.00 59.92 C ANISOU 2228 CD GLU A 449 7452 6804 8511 -55 -430 774 C ATOM 2229 OE1 GLU A 449 84.494 64.391 19.097 1.00 66.87 O ANISOU 2229 OE1 GLU A 449 8262 7673 9472 6 -311 837 O ATOM 2230 OE2 GLU A 449 84.259 64.581 16.921 1.00 66.02 O ANISOU 2230 OE2 GLU A 449 8213 7503 9368 -105 -560 797 O ATOM 2231 N LYS A 450 86.026 63.399 13.345 1.00 44.05 N ANISOU 2231 N LYS A 450 5759 4708 6271 -241 -905 600 N ATOM 2232 CA LYS A 450 86.064 63.635 11.907 1.00 42.65 C ANISOU 2232 CA LYS A 450 5703 4476 6027 -283 -1046 564 C ATOM 2233 C LYS A 450 86.606 65.025 11.594 1.00 38.70 C ANISOU 2233 C LYS A 450 5272 4026 5406 -288 -1003 525 C ATOM 2234 O LYS A 450 87.495 65.186 10.751 1.00 35.83 O ANISOU 2234 O LYS A 450 5042 3684 4888 -301 -1018 462 O ATOM 2235 CB LYS A 450 84.668 63.453 11.311 1.00 45.32 C ANISOU 2235 CB LYS A 450 5994 4678 6548 -310 -1210 630 C ATOM 2236 CG LYS A 450 84.644 63.403 9.784 1.00 46.36 C ANISOU 2236 CG LYS A 450 6277 4727 6612 -346 -1388 593 C ATOM 2237 CD LYS A 450 83.232 63.618 9.258 1.00 57.48 C ANISOU 2237 CD LYS A 450 7633 5995 8211 -372 -1556 659 C ATOM 2238 CE LYS A 450 83.017 62.964 7.899 1.00 63.00 C ANISOU 2238 CE LYS A 450 8474 6576 8888 -398 -1770 634 C ATOM 2239 NZ LYS A 450 83.945 63.468 6.851 1.00 64.14 N ANISOU 2239 NZ LYS A 450 8826 6744 8799 -401 -1789 554 N ATOM 2240 N PHE A 451 86.095 66.043 12.274 1.00 32.12 N ANISOU 2240 N PHE A 451 4353 3208 4643 -275 -940 566 N ATOM 2241 CA PHE A 451 86.514 67.389 11.916 1.00 38.06 C ANISOU 2241 CA PHE A 451 5167 3998 5295 -283 -915 533 C ATOM 2242 C PHE A 451 87.701 67.839 12.749 1.00 34.16 C ANISOU 2242 C PHE A 451 4682 3619 4680 -252 -762 486 C ATOM 2243 O PHE A 451 88.649 68.413 12.202 1.00 35.76 O ANISOU 2243 O PHE A 451 4978 3862 4748 -262 -741 428 O ATOM 2244 CB PHE A 451 85.313 68.346 12.022 1.00 40.95 C ANISOU 2244 CB PHE A 451 5453 4308 5800 -290 -950 599 C ATOM 2245 CG PHE A 451 84.116 67.852 11.243 1.00 43.58 C ANISOU 2245 CG PHE A 451 5765 4511 6284 -321 -1119 650 C ATOM 2246 CD1 PHE A 451 84.147 67.823 9.857 1.00 44.31 C ANISOU 2246 CD1 PHE A 451 5988 4537 6311 -357 -1269 614 C ATOM 2247 CD2 PHE A 451 83.002 67.336 11.895 1.00 40.53 C ANISOU 2247 CD2 PHE A 451 5236 4056 6108 -309 -1129 735 C ATOM 2248 CE1 PHE A 451 83.070 67.327 9.127 1.00 41.79 C ANISOU 2248 CE1 PHE A 451 5662 4082 6134 -384 -1451 656 C ATOM 2249 CE2 PHE A 451 81.925 66.830 11.172 1.00 39.61 C ANISOU 2249 CE2 PHE A 451 5090 3805 6155 -340 -1301 784 C ATOM 2250 CZ PHE A 451 81.964 66.821 9.789 1.00 37.61 C ANISOU 2250 CZ PHE A 451 4972 3484 5833 -379 -1473 742 C ATOM 2251 N ALA A 452 87.726 67.503 14.038 1.00 33.23 N ANISOU 2251 N ALA A 452 4476 3542 4606 -211 -657 509 N ATOM 2252 CA ALA A 452 88.823 67.979 14.871 1.00 34.23 C ANISOU 2252 CA ALA A 452 4617 3762 4626 -178 -533 464 C ATOM 2253 C ALA A 452 90.150 67.303 14.539 1.00 40.90 C ANISOU 2253 C ALA A 452 5542 4654 5343 -184 -515 393 C ATOM 2254 O ALA A 452 91.202 67.897 14.802 1.00 38.48 O ANISOU 2254 O ALA A 452 5270 4409 4943 -172 -445 345 O ATOM 2255 CB ALA A 452 88.485 67.797 16.350 1.00 27.34 C ANISOU 2255 CB ALA A 452 3656 2909 3825 -121 -431 507 C ATOM 2256 N SER A 453 90.137 66.088 13.966 1.00 34.40 N ANISOU 2256 N SER A 453 4749 3798 4525 -201 -577 386 N ATOM 2257 CA SER A 453 91.406 65.467 13.573 1.00 29.52 C ANISOU 2257 CA SER A 453 4212 3217 3786 -205 -552 322 C ATOM 2258 C SER A 453 92.177 66.346 12.595 1.00 31.06 C ANISOU 2258 C SER A 453 4509 3421 3872 -226 -555 278 C ATOM 2259 O SER A 453 93.415 66.344 12.601 1.00 29.42 O ANISOU 2259 O SER A 453 4344 3260 3574 -218 -485 229 O ATOM 2260 CB SER A 453 91.186 64.068 12.964 1.00 33.98 C ANISOU 2260 CB SER A 453 4810 3732 4368 -221 -632 324 C ATOM 2261 OG SER A 453 90.348 64.099 11.818 1.00 32.30 O ANISOU 2261 OG SER A 453 4652 3432 4190 -253 -765 346 O ATOM 2262 N HIS A 454 91.465 67.105 11.753 1.00 28.72 N ANISOU 2262 N HIS A 454 4249 3071 3591 -251 -633 298 N ATOM 2263 CA HIS A 454 92.127 68.082 10.890 1.00 29.58 C ANISOU 2263 CA HIS A 454 4454 3185 3602 -264 -622 263 C ATOM 2264 C HIS A 454 92.808 69.171 11.712 1.00 35.88 C ANISOU 2264 C HIS A 454 5201 4053 4378 -246 -517 247 C ATOM 2265 O HIS A 454 93.889 69.657 11.351 1.00 30.08 O ANISOU 2265 O HIS A 454 4523 3344 3560 -246 -461 208 O ATOM 2266 CB HIS A 454 91.108 68.726 9.951 1.00 38.32 C ANISOU 2266 CB HIS A 454 5604 4215 4739 -290 -733 291 C ATOM 2267 CG HIS A 454 90.466 67.773 8.997 1.00 34.90 C ANISOU 2267 CG HIS A 454 5245 3691 4324 -308 -865 303 C ATOM 2268 ND1 HIS A 454 91.041 67.423 7.795 1.00 34.39 N ANISOU 2268 ND1 HIS A 454 5339 3584 4143 -312 -905 266 N ATOM 2269 CD2 HIS A 454 89.282 67.122 9.053 1.00 33.92 C ANISOU 2269 CD2 HIS A 454 5064 3498 4326 -318 -972 350 C ATOM 2270 CE1 HIS A 454 90.243 66.587 7.157 1.00 34.09 C ANISOU 2270 CE1 HIS A 454 5350 3455 4147 -323 -1044 284 C ATOM 2271 NE2 HIS A 454 89.170 66.386 7.900 1.00 38.95 N ANISOU 2271 NE2 HIS A 454 5827 4052 4919 -330 -1092 335 N ATOM 2272 N VAL A 455 92.169 69.588 12.808 1.00 29.50 N ANISOU 2272 N VAL A 455 4291 3265 3651 -226 -491 282 N ATOM 2273 CA VAL A 455 92.742 70.611 13.677 1.00 32.15 C ANISOU 2273 CA VAL A 455 4590 3659 3969 -201 -407 267 C ATOM 2274 C VAL A 455 93.996 70.083 14.369 1.00 31.89 C ANISOU 2274 C VAL A 455 4553 3677 3885 -176 -330 224 C ATOM 2275 O VAL A 455 94.989 70.808 14.525 1.00 27.97 O ANISOU 2275 O VAL A 455 4070 3214 3343 -169 -280 189 O ATOM 2276 CB VAL A 455 91.668 71.077 14.681 1.00 26.58 C ANISOU 2276 CB VAL A 455 3794 2946 3357 -176 -395 321 C ATOM 2277 CG1 VAL A 455 92.253 71.987 15.726 1.00 28.96 C ANISOU 2277 CG1 VAL A 455 4073 3299 3632 -138 -315 304 C ATOM 2278 CG2 VAL A 455 90.516 71.755 13.928 1.00 28.11 C ANISOU 2278 CG2 VAL A 455 3986 3082 3610 -205 -474 363 C ATOM 2279 N VAL A 456 93.980 68.803 14.768 1.00 26.71 N ANISOU 2279 N VAL A 456 3876 3023 3249 -164 -327 226 N ATOM 2280 CA VAL A 456 95.130 68.227 15.456 1.00 27.39 C ANISOU 2280 CA VAL A 456 3958 3153 3297 -139 -263 186 C ATOM 2281 C VAL A 456 96.341 68.176 14.527 1.00 34.06 C ANISOU 2281 C VAL A 456 4874 4001 4067 -161 -245 140 C ATOM 2282 O VAL A 456 97.466 68.507 14.928 1.00 32.35 O ANISOU 2282 O VAL A 456 4651 3814 3826 -147 -189 105 O ATOM 2283 CB VAL A 456 94.776 66.834 16.001 1.00 29.24 C ANISOU 2283 CB VAL A 456 4158 3383 3569 -123 -265 202 C ATOM 2284 CG1 VAL A 456 96.046 66.131 16.531 1.00 23.31 C ANISOU 2284 CG1 VAL A 456 3414 2670 2772 -103 -211 155 C ATOM 2285 CG2 VAL A 456 93.702 66.955 17.062 1.00 25.65 C ANISOU 2285 CG2 VAL A 456 3631 2919 3196 -88 -250 255 C ATOM 2286 N GLU A 457 96.121 67.780 13.270 1.00 29.33 N ANISOU 2286 N GLU A 457 4348 3361 3437 -190 -294 142 N ATOM 2287 CA GLU A 457 97.177 67.784 12.266 1.00 29.41 C ANISOU 2287 CA GLU A 457 4444 3358 3371 -202 -263 109 C ATOM 2288 C GLU A 457 97.826 69.152 12.140 1.00 34.58 C ANISOU 2288 C GLU A 457 5104 4025 4010 -203 -215 97 C ATOM 2289 O GLU A 457 99.060 69.269 12.187 1.00 33.09 O ANISOU 2289 O GLU A 457 4917 3851 3803 -195 -144 69 O ATOM 2290 CB GLU A 457 96.610 67.356 10.918 1.00 30.96 C ANISOU 2290 CB GLU A 457 4745 3490 3528 -224 -336 121 C ATOM 2291 CG GLU A 457 96.226 65.905 10.839 1.00 32.41 C ANISOU 2291 CG GLU A 457 4942 3650 3721 -224 -387 126 C ATOM 2292 CD GLU A 457 95.845 65.520 9.420 1.00 38.81 C ANISOU 2292 CD GLU A 457 5887 4384 4476 -239 -469 129 C ATOM 2293 OE1 GLU A 457 96.738 65.526 8.552 1.00 44.24 O ANISOU 2293 OE1 GLU A 457 6684 5051 5074 -233 -424 104 O ATOM 2294 OE2 GLU A 457 94.650 65.260 9.165 1.00 40.52 O ANISOU 2294 OE2 GLU A 457 6104 4548 4744 -253 -581 160 O ATOM 2295 N LYS A 458 97.004 70.202 11.963 1.00 33.40 N ANISOU 2295 N LYS A 458 4950 3863 3878 -214 -254 121 N ATOM 2296 CA LYS A 458 97.544 71.558 11.835 1.00 36.65 C ANISOU 2296 CA LYS A 458 5363 4284 4278 -216 -214 111 C ATOM 2297 C LYS A 458 98.359 71.939 13.059 1.00 34.35 C ANISOU 2297 C LYS A 458 4991 4037 4021 -191 -158 91 C ATOM 2298 O LYS A 458 99.408 72.583 12.942 1.00 37.98 O ANISOU 2298 O LYS A 458 5453 4500 4479 -189 -108 71 O ATOM 2299 CB LYS A 458 96.421 72.584 11.632 1.00 29.80 C ANISOU 2299 CB LYS A 458 4491 3399 3433 -229 -271 142 C ATOM 2300 CG LYS A 458 95.597 72.392 10.375 1.00 34.81 C ANISOU 2300 CG LYS A 458 5215 3973 4040 -254 -349 160 C ATOM 2301 CD LYS A 458 96.467 72.240 9.144 1.00 28.95 C ANISOU 2301 CD LYS A 458 4594 3194 3211 -258 -318 138 C ATOM 2302 CE LYS A 458 95.715 72.713 7.902 1.00 38.56 C ANISOU 2302 CE LYS A 458 5920 4345 4387 -275 -394 153 C ATOM 2303 NZ LYS A 458 96.346 72.221 6.646 1.00 53.78 N ANISOU 2303 NZ LYS A 458 8000 6216 6217 -267 -375 138 N ATOM 2304 N ALA A 459 97.875 71.571 14.244 1.00 27.87 N ANISOU 2304 N ALA A 459 4106 3241 3240 -167 -171 100 N ATOM 2305 CA ALA A 459 98.617 71.843 15.467 1.00 31.12 C ANISOU 2305 CA ALA A 459 4465 3683 3676 -134 -135 78 C ATOM 2306 C ALA A 459 100.000 71.202 15.425 1.00 33.49 C ANISOU 2306 C ALA A 459 4770 3986 3968 -131 -92 42 C ATOM 2307 O ALA A 459 101.011 71.851 15.730 1.00 28.64 O ANISOU 2307 O ALA A 459 4134 3372 3376 -122 -65 19 O ATOM 2308 CB ALA A 459 97.827 71.340 16.667 1.00 28.29 C ANISOU 2308 CB ALA A 459 4063 3339 3347 -99 -146 98 C ATOM 2309 N PHE A 460 100.065 69.924 15.042 1.00 24.82 N ANISOU 2309 N PHE A 460 3697 2883 2850 -138 -88 38 N ATOM 2310 CA PHE A 460 101.361 69.261 14.931 1.00 27.22 C ANISOU 2310 CA PHE A 460 4005 3184 3152 -136 -40 8 C ATOM 2311 C PHE A 460 102.232 69.945 13.893 1.00 34.30 C ANISOU 2311 C PHE A 460 4940 4052 4041 -153 8 3 C ATOM 2312 O PHE A 460 103.433 70.130 14.110 1.00 35.80 O ANISOU 2312 O PHE A 460 5099 4234 4271 -145 54 -16 O ATOM 2313 CB PHE A 460 101.189 67.788 14.566 1.00 27.69 C ANISOU 2313 CB PHE A 460 4098 3240 3184 -141 -45 9 C ATOM 2314 CG PHE A 460 101.020 66.879 15.747 1.00 28.47 C ANISOU 2314 CG PHE A 460 4146 3364 3306 -116 -57 3 C ATOM 2315 CD1 PHE A 460 99.768 66.405 16.099 1.00 31.42 C ANISOU 2315 CD1 PHE A 460 4507 3742 3690 -109 -100 32 C ATOM 2316 CD2 PHE A 460 102.118 66.488 16.500 1.00 34.33 C ANISOU 2316 CD2 PHE A 460 4855 4118 4070 -95 -26 -29 C ATOM 2317 CE1 PHE A 460 99.606 65.546 17.197 1.00 44.64 C ANISOU 2317 CE1 PHE A 460 6140 5434 5386 -79 -97 32 C ATOM 2318 CE2 PHE A 460 101.969 65.638 17.594 1.00 37.10 C ANISOU 2318 CE2 PHE A 460 5175 4488 4434 -66 -36 -35 C ATOM 2319 CZ PHE A 460 100.708 65.163 17.943 1.00 41.19 C ANISOU 2319 CZ PHE A 460 5685 5013 4951 -56 -65 -4 C ATOM 2320 N LEU A 461 101.638 70.328 12.757 1.00 27.64 N ANISOU 2320 N LEU A 461 4167 3183 3153 -174 -4 23 N ATOM 2321 CA LEU A 461 102.412 70.862 11.644 1.00 33.02 C ANISOU 2321 CA LEU A 461 4907 3826 3814 -182 57 25 C ATOM 2322 C LEU A 461 103.005 72.228 11.962 1.00 31.18 C ANISOU 2322 C LEU A 461 4620 3593 3634 -180 85 23 C ATOM 2323 O LEU A 461 104.076 72.566 11.454 1.00 35.84 O ANISOU 2323 O LEU A 461 5216 4151 4250 -177 159 23 O ATOM 2324 CB LEU A 461 101.532 70.953 10.392 1.00 44.43 C ANISOU 2324 CB LEU A 461 6460 5234 5188 -198 23 46 C ATOM 2325 CG LEU A 461 101.329 69.628 9.639 1.00 44.39 C ANISOU 2325 CG LEU A 461 6546 5198 5121 -197 8 47 C ATOM 2326 CD1 LEU A 461 100.213 69.708 8.588 1.00 38.98 C ANISOU 2326 CD1 LEU A 461 5970 4467 4375 -210 -70 66 C ATOM 2327 CD2 LEU A 461 102.654 69.179 9.016 1.00 37.99 C ANISOU 2327 CD2 LEU A 461 5789 4357 4290 -182 111 37 C ATOM 2328 N HIS A 462 102.331 73.024 12.785 1.00 31.76 N ANISOU 2328 N HIS A 462 4641 3694 3733 -177 31 26 N ATOM 2329 CA HIS A 462 102.707 74.411 12.987 1.00 29.97 C ANISOU 2329 CA HIS A 462 4377 3462 3549 -175 40 27 C ATOM 2330 C HIS A 462 103.098 74.750 14.418 1.00 34.74 C ANISOU 2330 C HIS A 462 4898 4085 4215 -151 13 7 C ATOM 2331 O HIS A 462 103.405 75.919 14.690 1.00 36.75 O ANISOU 2331 O HIS A 462 5121 4331 4511 -147 5 5 O ATOM 2332 CB HIS A 462 101.553 75.325 12.551 1.00 34.32 C ANISOU 2332 CB HIS A 462 4960 4014 4066 -190 -3 50 C ATOM 2333 CG HIS A 462 101.257 75.256 11.087 1.00 38.36 C ANISOU 2333 CG HIS A 462 5572 4489 4516 -210 11 66 C ATOM 2334 ND1 HIS A 462 101.977 75.968 10.151 1.00 37.83 N ANISOU 2334 ND1 HIS A 462 5549 4384 4441 -214 75 73 N ATOM 2335 CD2 HIS A 462 100.324 74.557 10.395 1.00 37.01 C ANISOU 2335 CD2 HIS A 462 5475 4301 4287 -221 -35 79 C ATOM 2336 CE1 HIS A 462 101.496 75.716 8.945 1.00 38.12 C ANISOU 2336 CE1 HIS A 462 5699 4383 4402 -222 71 87 C ATOM 2337 NE2 HIS A 462 100.492 74.865 9.066 1.00 38.25 N ANISOU 2337 NE2 HIS A 462 5735 4409 4388 -228 -6 89 N ATOM 2338 N ALA A 463 103.049 73.788 15.342 1.00 32.93 N ANISOU 2338 N ALA A 463 4645 3877 3989 -130 -9 -8 N ATOM 2339 CA ALA A 463 103.372 74.068 16.737 1.00 32.83 C ANISOU 2339 CA ALA A 463 4582 3872 4020 -96 -45 -28 C ATOM 2340 C ALA A 463 104.819 74.529 16.857 1.00 33.97 C ANISOU 2340 C ALA A 463 4684 3979 4243 -93 -29 -49 C ATOM 2341 O ALA A 463 105.696 74.012 16.150 1.00 32.06 O ANISOU 2341 O ALA A 463 4438 3713 4029 -108 27 -50 O ATOM 2342 CB ALA A 463 103.164 72.823 17.605 1.00 30.05 C ANISOU 2342 CB ALA A 463 4227 3539 3653 -70 -61 -39 C ATOM 2343 N PRO A 464 105.113 75.496 17.727 1.00 29.37 N ANISOU 2343 N PRO A 464 4069 3381 3708 -70 -76 -62 N ATOM 2344 CA PRO A 464 106.514 75.786 18.047 1.00 36.45 C ANISOU 2344 CA PRO A 464 4913 4230 4708 -63 -84 -83 C ATOM 2345 C PRO A 464 107.100 74.595 18.785 1.00 31.05 C ANISOU 2345 C PRO A 464 4214 3540 4045 -42 -99 -108 C ATOM 2346 O PRO A 464 106.374 73.818 19.405 1.00 33.48 O ANISOU 2346 O PRO A 464 4553 3881 4285 -20 -120 -114 O ATOM 2347 CB PRO A 464 106.434 77.034 18.941 1.00 36.24 C ANISOU 2347 CB PRO A 464 4874 4186 4710 -36 -159 -93 C ATOM 2348 CG PRO A 464 105.078 76.919 19.616 1.00 30.88 C ANISOU 2348 CG PRO A 464 4246 3551 3935 -9 -190 -87 C ATOM 2349 CD PRO A 464 104.173 76.247 18.582 1.00 28.42 C ANISOU 2349 CD PRO A 464 3964 3279 3556 -42 -132 -58 C ATOM 2350 N LEU A 465 108.430 74.460 18.723 1.00 35.51 N ANISOU 2350 N LEU A 465 4726 4054 4714 -46 -86 -119 N ATOM 2351 CA LEU A 465 109.065 73.182 19.062 1.00 41.62 C ANISOU 2351 CA LEU A 465 5485 4819 5511 -38 -79 -138 C ATOM 2352 C LEU A 465 108.785 72.738 20.501 1.00 43.02 C ANISOU 2352 C LEU A 465 5684 5006 5656 7 -164 -169 C ATOM 2353 O LEU A 465 108.625 71.536 20.762 1.00 40.03 O ANISOU 2353 O LEU A 465 5323 4652 5233 16 -153 -179 O ATOM 2354 CB LEU A 465 110.570 73.251 18.797 1.00 46.33 C ANISOU 2354 CB LEU A 465 6008 5344 6253 -48 -53 -138 C ATOM 2355 CG LEU A 465 110.897 73.350 17.297 1.00 54.14 C ANISOU 2355 CG LEU A 465 6994 6317 7261 -82 68 -100 C ATOM 2356 CD1 LEU A 465 112.330 72.951 17.001 1.00 61.20 C ANISOU 2356 CD1 LEU A 465 7818 7140 8297 -86 126 -90 C ATOM 2357 CD2 LEU A 465 109.936 72.532 16.432 1.00 45.46 C ANISOU 2357 CD2 LEU A 465 5976 5273 6022 -96 130 -85 C ATOM 2358 N GLU A 466 108.704 73.677 21.449 1.00 39.48 N ANISOU 2358 N GLU A 466 5245 4534 5223 41 -248 -185 N ATOM 2359 CA GLU A 466 108.455 73.266 22.831 1.00 38.15 C ANISOU 2359 CA GLU A 466 5123 4362 5011 97 -323 -213 C ATOM 2360 C GLU A 466 107.062 72.665 22.994 1.00 42.13 C ANISOU 2360 C GLU A 466 5687 4930 5390 113 -288 -194 C ATOM 2361 O GLU A 466 106.895 71.651 23.687 1.00 40.12 O ANISOU 2361 O GLU A 466 5463 4686 5096 144 -294 -206 O ATOM 2362 CB GLU A 466 108.648 74.441 23.784 1.00 43.55 C ANISOU 2362 CB GLU A 466 5828 4993 5726 139 -424 -232 C ATOM 2363 CG GLU A 466 110.112 74.798 24.031 1.00 55.87 C ANISOU 2363 CG GLU A 466 7328 6467 7434 137 -497 -257 C ATOM 2364 CD GLU A 466 110.961 73.593 24.413 1.00 71.25 C ANISOU 2364 CD GLU A 466 9254 8385 9432 145 -514 -281 C ATOM 2365 OE1 GLU A 466 112.084 73.463 23.877 1.00 77.96 O ANISOU 2365 OE1 GLU A 466 10019 9187 10415 112 -498 -278 O ATOM 2366 OE2 GLU A 466 110.512 72.779 25.252 1.00 73.17 O ANISOU 2366 OE2 GLU A 466 9564 8649 9588 187 -537 -300 O ATOM 2367 N LEU A 467 106.048 73.268 22.369 1.00 37.75 N ANISOU 2367 N LEU A 467 5147 4412 4785 94 -251 -162 N ATOM 2368 CA LEU A 467 104.716 72.670 22.424 1.00 37.58 C ANISOU 2368 CA LEU A 467 5164 4438 4676 104 -217 -135 C ATOM 2369 C LEU A 467 104.669 71.380 21.618 1.00 34.00 C ANISOU 2369 C LEU A 467 4697 4013 4208 68 -162 -126 C ATOM 2370 O LEU A 467 104.029 70.408 22.030 1.00 37.09 O ANISOU 2370 O LEU A 467 5110 4427 4557 88 -150 -117 O ATOM 2371 CB LEU A 467 103.661 73.647 21.911 1.00 35.99 C ANISOU 2371 CB LEU A 467 4974 4257 4443 89 -202 -100 C ATOM 2372 CG LEU A 467 103.397 74.862 22.784 1.00 45.37 C ANISOU 2372 CG LEU A 467 6191 5422 5624 134 -251 -102 C ATOM 2373 CD1 LEU A 467 102.199 75.678 22.252 1.00 34.91 C ANISOU 2373 CD1 LEU A 467 4874 4122 4267 118 -227 -62 C ATOM 2374 CD2 LEU A 467 103.171 74.389 24.209 1.00 45.80 C ANISOU 2374 CD2 LEU A 467 6301 5461 5639 208 -279 -114 C ATOM 2375 N LEU A 468 105.339 71.353 20.467 1.00 34.73 N ANISOU 2375 N LEU A 468 4762 4098 4337 20 -123 -124 N ATOM 2376 CA LEU A 468 105.377 70.132 19.669 1.00 33.01 C ANISOU 2376 CA LEU A 468 4548 3897 4097 -8 -72 -117 C ATOM 2377 C LEU A 468 105.938 68.972 20.477 1.00 36.15 C ANISOU 2377 C LEU A 468 4937 4292 4507 17 -84 -143 C ATOM 2378 O LEU A 468 105.406 67.851 20.414 1.00 35.02 O ANISOU 2378 O LEU A 468 4812 4175 4319 16 -66 -135 O ATOM 2379 CB LEU A 468 106.191 70.354 18.391 1.00 33.43 C ANISOU 2379 CB LEU A 468 4589 3926 4188 -49 -17 -110 C ATOM 2380 CG LEU A 468 106.494 69.094 17.575 1.00 36.27 C ANISOU 2380 CG LEU A 468 4967 4287 4527 -69 39 -107 C ATOM 2381 CD1 LEU A 468 105.199 68.505 16.979 1.00 31.35 C ANISOU 2381 CD1 LEU A 468 4399 3696 3817 -83 39 -83 C ATOM 2382 CD2 LEU A 468 107.524 69.374 16.506 1.00 37.57 C ANISOU 2382 CD2 LEU A 468 5124 4409 4741 -92 110 -97 C ATOM 2383 N ALA A 469 106.988 69.233 21.276 1.00 33.84 N ANISOU 2383 N ALA A 469 4618 3960 4280 41 -126 -174 N ATOM 2384 CA ALA A 469 107.544 68.195 22.142 1.00 36.62 C ANISOU 2384 CA ALA A 469 4968 4301 4645 70 -151 -203 C ATOM 2385 C ALA A 469 106.502 67.712 23.140 1.00 36.70 C ANISOU 2385 C ALA A 469 5028 4338 4577 117 -172 -199 C ATOM 2386 O ALA A 469 106.393 66.508 23.405 1.00 31.43 O ANISOU 2386 O ALA A 469 4371 3688 3884 127 -157 -204 O ATOM 2387 CB ALA A 469 108.798 68.708 22.876 1.00 21.74 C ANISOU 2387 CB ALA A 469 3052 2352 2857 91 -217 -236 C ATOM 2388 N GLU A 470 105.712 68.636 23.691 1.00 30.40 N ANISOU 2388 N GLU A 470 4265 3540 3746 149 -198 -186 N ATOM 2389 CA GLU A 470 104.672 68.238 24.637 1.00 32.88 C ANISOU 2389 CA GLU A 470 4629 3868 3993 203 -196 -171 C ATOM 2390 C GLU A 470 103.572 67.433 23.945 1.00 33.70 C ANISOU 2390 C GLU A 470 4725 4017 4063 176 -137 -130 C ATOM 2391 O GLU A 470 103.037 66.481 24.525 1.00 38.72 O ANISOU 2391 O GLU A 470 5379 4663 4670 207 -119 -118 O ATOM 2392 CB GLU A 470 104.081 69.469 25.321 1.00 33.94 C ANISOU 2392 CB GLU A 470 4808 3985 4104 248 -225 -159 C ATOM 2393 CG GLU A 470 104.942 70.100 26.402 1.00 49.37 C ANISOU 2393 CG GLU A 470 6803 5880 6075 301 -306 -200 C ATOM 2394 CD GLU A 470 104.332 71.406 26.928 1.00 60.46 C ANISOU 2394 CD GLU A 470 8259 7263 7449 344 -332 -187 C ATOM 2395 OE1 GLU A 470 105.053 72.421 27.021 1.00 61.08 O ANISOU 2395 OE1 GLU A 470 8335 7301 7571 344 -398 -211 O ATOM 2396 OE2 GLU A 470 103.119 71.422 27.230 1.00 65.12 O ANISOU 2396 OE2 GLU A 470 8889 7873 7981 378 -284 -147 O ATOM 2397 N MET A 471 103.214 67.805 22.711 1.00 25.39 N ANISOU 2397 N MET A 471 3649 2982 3017 120 -113 -106 N ATOM 2398 CA MET A 471 102.192 67.063 21.975 1.00 30.28 C ANISOU 2398 CA MET A 471 4265 3627 3614 92 -82 -69 C ATOM 2399 C MET A 471 102.676 65.658 21.625 1.00 32.66 C ANISOU 2399 C MET A 471 4557 3937 3914 72 -65 -83 C ATOM 2400 O MET A 471 101.946 64.679 21.807 1.00 29.76 O ANISOU 2400 O MET A 471 4193 3583 3533 82 -54 -63 O ATOM 2401 CB MET A 471 101.807 67.821 20.709 1.00 30.69 C ANISOU 2401 CB MET A 471 4313 3681 3667 41 -77 -47 C ATOM 2402 CG MET A 471 101.220 69.205 20.973 1.00 34.42 C ANISOU 2402 CG MET A 471 4791 4147 4141 56 -93 -29 C ATOM 2403 SD MET A 471 100.870 70.054 19.418 1.00 36.68 S ANISOU 2403 SD MET A 471 5081 4431 4426 -5 -90 -7 S ATOM 2404 CE MET A 471 99.719 68.908 18.669 1.00 36.20 C ANISOU 2404 CE MET A 471 5031 4375 4350 -31 -92 30 C ATOM 2405 N MET A 472 103.902 65.546 21.101 1.00 32.28 N ANISOU 2405 N MET A 472 4496 3878 3890 46 -57 -114 N ATOM 2406 CA MET A 472 104.498 64.236 20.848 1.00 36.61 C ANISOU 2406 CA MET A 472 5040 4431 4440 33 -36 -131 C ATOM 2407 C MET A 472 104.514 63.381 22.114 1.00 36.42 C ANISOU 2407 C MET A 472 5018 4411 4409 80 -52 -146 C ATOM 2408 O MET A 472 104.107 62.214 22.094 1.00 29.81 O ANISOU 2408 O MET A 472 4184 3591 3552 80 -38 -137 O ATOM 2409 CB MET A 472 105.914 64.406 20.302 1.00 31.51 C ANISOU 2409 CB MET A 472 4372 3758 3843 10 -16 -156 C ATOM 2410 CG MET A 472 105.955 64.988 18.914 1.00 34.27 C ANISOU 2410 CG MET A 472 4736 4097 4189 -32 22 -136 C ATOM 2411 SD MET A 472 105.553 63.751 17.685 1.00 38.55 S ANISOU 2411 SD MET A 472 5326 4647 4674 -62 59 -119 S ATOM 2412 CE MET A 472 106.005 64.555 16.144 1.00 38.98 C ANISOU 2412 CE MET A 472 5421 4666 4724 -93 114 -102 C ATOM 2413 N ASP A 473 104.961 63.956 23.234 1.00 36.41 N ANISOU 2413 N ASP A 473 5024 4387 4423 125 -87 -169 N ATOM 2414 CA ASP A 473 105.028 63.192 24.477 1.00 40.35 C ANISOU 2414 CA ASP A 473 5547 4878 4905 180 -105 -186 C ATOM 2415 C ASP A 473 103.646 62.810 24.985 1.00 36.12 C ANISOU 2415 C ASP A 473 5038 4361 4326 216 -79 -146 C ATOM 2416 O ASP A 473 103.500 61.795 25.672 1.00 28.06 O ANISOU 2416 O ASP A 473 4032 3341 3287 251 -67 -146 O ATOM 2417 CB ASP A 473 105.775 63.982 25.552 1.00 48.23 C ANISOU 2417 CB ASP A 473 6571 5831 5922 229 -165 -221 C ATOM 2418 CG ASP A 473 106.125 63.125 26.756 1.00 61.16 C ANISOU 2418 CG ASP A 473 8249 7448 7542 286 -193 -248 C ATOM 2419 OD1 ASP A 473 105.615 63.402 27.864 1.00 63.76 O ANISOU 2419 OD1 ASP A 473 8646 7756 7826 356 -211 -245 O ATOM 2420 OD2 ASP A 473 106.891 62.153 26.585 1.00 65.53 O ANISOU 2420 OD2 ASP A 473 8774 8002 8123 266 -191 -272 O ATOM 2421 N GLU A 474 102.624 63.605 24.675 1.00 32.19 N ANISOU 2421 N GLU A 474 4541 3869 3821 211 -66 -106 N ATOM 2422 CA GLU A 474 101.281 63.213 25.077 1.00 34.13 C ANISOU 2422 CA GLU A 474 4795 4120 4053 243 -32 -55 C ATOM 2423 C GLU A 474 100.827 61.968 24.314 1.00 32.36 C ANISOU 2423 C GLU A 474 4538 3916 3843 203 -12 -33 C ATOM 2424 O GLU A 474 100.188 61.082 24.889 1.00 31.07 O ANISOU 2424 O GLU A 474 4374 3750 3683 236 14 -6 O ATOM 2425 CB GLU A 474 100.303 64.368 24.873 1.00 31.95 C ANISOU 2425 CB GLU A 474 4519 3838 3783 244 -25 -14 C ATOM 2426 CG GLU A 474 98.847 63.898 24.916 1.00 32.75 C ANISOU 2426 CG GLU A 474 4601 3936 3907 258 15 53 C ATOM 2427 CD GLU A 474 97.862 64.998 25.116 1.00 30.47 C ANISOU 2427 CD GLU A 474 4317 3629 3631 282 31 98 C ATOM 2428 OE1 GLU A 474 98.301 66.127 25.432 1.00 31.62 O ANISOU 2428 OE1 GLU A 474 4495 3767 3752 301 12 75 O ATOM 2429 OE2 GLU A 474 96.639 64.728 24.956 1.00 30.81 O ANISOU 2429 OE2 GLU A 474 4326 3659 3720 282 60 161 O ATOM 2430 N ILE A 475 101.174 61.872 23.028 1.00 30.01 N ANISOU 2430 N ILE A 475 4220 3629 3552 136 -24 -43 N ATOM 2431 CA ILE A 475 100.831 60.691 22.237 1.00 30.33 C ANISOU 2431 CA ILE A 475 4248 3679 3599 100 -21 -28 C ATOM 2432 C ILE A 475 101.699 59.499 22.641 1.00 36.76 C ANISOU 2432 C ILE A 475 5063 4501 4404 111 -13 -63 C ATOM 2433 O ILE A 475 101.205 58.378 22.816 1.00 33.75 O ANISOU 2433 O ILE A 475 4673 4124 4027 120 -4 -45 O ATOM 2434 CB ILE A 475 100.966 61.001 20.732 1.00 35.49 C ANISOU 2434 CB ILE A 475 4911 4329 4246 38 -36 -28 C ATOM 2435 CG1 ILE A 475 100.008 62.130 20.307 1.00 31.60 C ANISOU 2435 CG1 ILE A 475 4418 3825 3765 26 -53 8 C ATOM 2436 CG2 ILE A 475 100.693 59.752 19.905 1.00 36.75 C ANISOU 2436 CG2 ILE A 475 5079 4486 4400 7 -47 -18 C ATOM 2437 CD1 ILE A 475 98.566 61.768 20.539 1.00 34.07 C ANISOU 2437 CD1 ILE A 475 4708 4124 4113 39 -62 64 C ATOM 2438 N PHE A 476 103.003 59.712 22.792 1.00 32.93 N ANISOU 2438 N PHE A 476 4582 4013 3917 111 -18 -110 N ATOM 2439 CA PHE A 476 103.874 58.593 23.111 1.00 31.69 C ANISOU 2439 CA PHE A 476 4422 3858 3760 118 -13 -144 C ATOM 2440 C PHE A 476 103.698 58.107 24.542 1.00 31.97 C ANISOU 2440 C PHE A 476 4473 3889 3785 182 -15 -148 C ATOM 2441 O PHE A 476 103.970 56.935 24.816 1.00 36.57 O ANISOU 2441 O PHE A 476 5054 4479 4363 190 -7 -161 O ATOM 2442 CB PHE A 476 105.335 58.974 22.859 1.00 24.53 C ANISOU 2442 CB PHE A 476 3504 2934 2881 100 -19 -187 C ATOM 2443 CG PHE A 476 105.665 59.145 21.401 1.00 33.04 C ANISOU 2443 CG PHE A 476 4579 4009 3965 44 7 -181 C ATOM 2444 CD1 PHE A 476 105.398 58.125 20.494 1.00 30.46 C ANISOU 2444 CD1 PHE A 476 4269 3692 3612 15 27 -168 C ATOM 2445 CD2 PHE A 476 106.217 60.331 20.931 1.00 34.96 C ANISOU 2445 CD2 PHE A 476 4815 4232 4237 28 11 -185 C ATOM 2446 CE1 PHE A 476 105.682 58.273 19.147 1.00 27.19 C ANISOU 2446 CE1 PHE A 476 3881 3264 3187 -23 55 -161 C ATOM 2447 CE2 PHE A 476 106.502 60.495 19.580 1.00 36.39 C ANISOU 2447 CE2 PHE A 476 5010 4402 4415 -13 49 -174 C ATOM 2448 CZ PHE A 476 106.239 59.461 18.686 1.00 30.36 C ANISOU 2448 CZ PHE A 476 4280 3644 3612 -35 73 -162 C ATOM 2449 N ASP A 477 103.245 58.959 25.458 1.00 27.44 N ANISOU 2449 N ASP A 477 3927 3299 3201 233 -20 -136 N ATOM 2450 CA ASP A 477 103.319 58.579 26.866 1.00 34.96 C ANISOU 2450 CA ASP A 477 4922 4231 4130 307 -21 -147 C ATOM 2451 C ASP A 477 102.358 59.356 27.763 1.00 37.20 C ANISOU 2451 C ASP A 477 5251 4492 4390 374 -2 -111 C ATOM 2452 O ASP A 477 102.594 59.481 28.967 1.00 41.11 O ANISOU 2452 O ASP A 477 5813 4954 4851 448 -12 -128 O ATOM 2453 CB ASP A 477 104.761 58.756 27.360 1.00 40.74 C ANISOU 2453 CB ASP A 477 5672 4937 4870 320 -73 -209 C ATOM 2454 CG ASP A 477 105.024 58.044 28.686 1.00 51.25 C ANISOU 2454 CG ASP A 477 7060 6242 6172 392 -86 -231 C ATOM 2455 OD1 ASP A 477 105.759 58.605 29.527 1.00 54.79 O ANISOU 2455 OD1 ASP A 477 7558 6645 6615 436 -144 -269 O ATOM 2456 OD2 ASP A 477 104.487 56.936 28.892 1.00 53.57 O ANISOU 2456 OD2 ASP A 477 7354 6553 6448 407 -46 -210 O ATOM 2457 N GLY A 478 101.266 59.875 27.206 1.00 35.13 N ANISOU 2457 N GLY A 478 4963 4239 4145 355 26 -59 N ATOM 2458 CA GLY A 478 100.337 60.631 28.028 1.00 27.85 C ANISOU 2458 CA GLY A 478 4082 3291 3210 421 58 -17 C ATOM 2459 C GLY A 478 99.138 59.837 28.523 1.00 33.96 C ANISOU 2459 C GLY A 478 4850 4052 4001 465 127 48 C ATOM 2460 O GLY A 478 98.418 60.305 29.402 1.00 39.99 O ANISOU 2460 O GLY A 478 5660 4781 4752 539 175 88 O ATOM 2461 N TYR A 479 98.894 58.640 27.989 1.00 29.19 N ANISOU 2461 N TYR A 479 4193 3466 3431 427 138 64 N ATOM 2462 CA TYR A 479 97.662 57.928 28.299 1.00 26.01 C ANISOU 2462 CA TYR A 479 3763 3043 3077 459 202 137 C ATOM 2463 C TYR A 479 97.945 56.566 28.904 1.00 28.77 C ANISOU 2463 C TYR A 479 4124 3392 3416 491 226 128 C ATOM 2464 O TYR A 479 98.896 55.878 28.517 1.00 34.59 O ANISOU 2464 O TYR A 479 4853 4157 4133 449 183 73 O ATOM 2465 CB TYR A 479 96.778 57.784 27.050 1.00 24.78 C ANISOU 2465 CB TYR A 479 3524 2892 2998 385 184 183 C ATOM 2466 CG TYR A 479 96.327 59.134 26.506 1.00 31.27 C ANISOU 2466 CG TYR A 479 4337 3708 3836 361 165 202 C ATOM 2467 CD1 TYR A 479 95.152 59.734 26.954 1.00 30.21 C ANISOU 2467 CD1 TYR A 479 4190 3536 3750 405 217 274 C ATOM 2468 CD2 TYR A 479 97.091 59.814 25.559 1.00 27.03 C ANISOU 2468 CD2 TYR A 479 3805 3198 3268 297 105 151 C ATOM 2469 CE1 TYR A 479 94.737 60.969 26.456 1.00 24.21 C ANISOU 2469 CE1 TYR A 479 3422 2771 3007 382 198 290 C ATOM 2470 CE2 TYR A 479 96.679 61.037 25.052 1.00 23.05 C ANISOU 2470 CE2 TYR A 479 3293 2687 2776 275 88 168 C ATOM 2471 CZ TYR A 479 95.512 61.615 25.507 1.00 24.61 C ANISOU 2471 CZ TYR A 479 3479 2853 3019 315 129 235 C ATOM 2472 OH TYR A 479 95.122 62.848 24.994 1.00 27.76 O ANISOU 2472 OH TYR A 479 3871 3247 3431 291 109 249 O ATOM 2473 N ILE A 480 97.099 56.190 29.849 1.00 32.74 N ANISOU 2473 N ILE A 480 4645 3858 3938 568 305 186 N ATOM 2474 CA ILE A 480 97.148 54.863 30.473 1.00 28.14 C ANISOU 2474 CA ILE A 480 4071 3267 3355 606 343 193 C ATOM 2475 C ILE A 480 96.769 53.811 29.435 1.00 33.38 C ANISOU 2475 C ILE A 480 4638 3952 4095 529 320 215 C ATOM 2476 O ILE A 480 95.708 53.935 28.798 1.00 35.25 O ANISOU 2476 O ILE A 480 4805 4170 4419 498 326 279 O ATOM 2477 CB ILE A 480 96.201 54.825 31.677 1.00 35.88 C ANISOU 2477 CB ILE A 480 5096 4190 4346 715 452 266 C ATOM 2478 CG1 ILE A 480 96.607 55.904 32.687 1.00 43.12 C ANISOU 2478 CG1 ILE A 480 6137 5076 5171 799 464 240 C ATOM 2479 CG2 ILE A 480 96.163 53.441 32.317 1.00 29.86 C ANISOU 2479 CG2 ILE A 480 4341 3413 3590 759 504 282 C ATOM 2480 CD1 ILE A 480 95.430 56.586 33.377 1.00 46.83 C ANISOU 2480 CD1 ILE A 480 6642 5488 5664 885 569 326 C ATOM 2481 N PRO A 481 97.604 52.795 29.194 1.00 31.45 N ANISOU 2481 N PRO A 481 4388 3737 3825 496 282 164 N ATOM 2482 CA PRO A 481 97.223 51.731 28.254 1.00 31.93 C ANISOU 2482 CA PRO A 481 4373 3808 3952 431 255 185 C ATOM 2483 C PRO A 481 95.950 51.019 28.692 1.00 41.22 C ANISOU 2483 C PRO A 481 5499 4940 5221 472 321 274 C ATOM 2484 O PRO A 481 95.605 50.985 29.877 1.00 37.82 O ANISOU 2484 O PRO A 481 5106 4477 4786 561 406 310 O ATOM 2485 CB PRO A 481 98.427 50.780 28.288 1.00 36.00 C ANISOU 2485 CB PRO A 481 4912 4356 4410 415 225 114 C ATOM 2486 CG PRO A 481 99.574 51.653 28.723 1.00 35.68 C ANISOU 2486 CG PRO A 481 4939 4327 4290 434 201 46 C ATOM 2487 CD PRO A 481 98.965 52.599 29.721 1.00 30.87 C ANISOU 2487 CD PRO A 481 4379 3681 3669 513 252 83 C ATOM 2488 N HIS A 482 95.258 50.435 27.716 1.00 38.86 N ANISOU 2488 N HIS A 482 5122 4631 5013 411 279 312 N ATOM 2489 CA HIS A 482 94.012 49.737 28.004 1.00 42.35 C ANISOU 2489 CA HIS A 482 5493 5018 5579 441 330 405 C ATOM 2490 C HIS A 482 94.272 48.580 28.961 1.00 37.28 C ANISOU 2490 C HIS A 482 4870 4373 4922 498 392 406 C ATOM 2491 O HIS A 482 95.182 47.773 28.717 1.00 33.53 O ANISOU 2491 O HIS A 482 4414 3939 4387 466 346 342 O ATOM 2492 CB HIS A 482 93.367 49.208 26.728 1.00 52.69 C ANISOU 2492 CB HIS A 482 6723 6306 6991 360 241 435 C ATOM 2493 CG HIS A 482 91.975 48.699 26.933 1.00 73.12 C ANISOU 2493 CG HIS A 482 9218 8820 9746 384 279 542 C ATOM 2494 ND1 HIS A 482 91.702 47.390 27.274 1.00 76.94 N ANISOU 2494 ND1 HIS A 482 9657 9278 10297 403 304 577 N ATOM 2495 CD2 HIS A 482 90.777 49.327 26.856 1.00 75.38 C ANISOU 2495 CD2 HIS A 482 9438 9042 10159 394 298 629 C ATOM 2496 CE1 HIS A 482 90.395 47.232 27.388 1.00 80.29 C ANISOU 2496 CE1 HIS A 482 9989 9624 10896 423 337 682 C ATOM 2497 NE2 HIS A 482 89.811 48.393 27.142 1.00 79.90 N ANISOU 2497 NE2 HIS A 482 9923 9547 10888 418 335 717 N ATOM 2498 N PRO A 483 93.501 48.458 30.045 1.00 38.59 N ANISOU 2498 N PRO A 483 5035 4488 5141 587 504 481 N ATOM 2499 CA PRO A 483 93.826 47.455 31.079 1.00 41.69 C ANISOU 2499 CA PRO A 483 5469 4875 5497 656 574 478 C ATOM 2500 C PRO A 483 93.737 46.021 30.598 1.00 48.81 C ANISOU 2500 C PRO A 483 6298 5779 6467 610 537 486 C ATOM 2501 O PRO A 483 94.449 45.158 31.125 1.00 50.41 O ANISOU 2501 O PRO A 483 6544 6004 6604 635 551 444 O ATOM 2502 CB PRO A 483 92.791 47.736 32.185 1.00 35.49 C ANISOU 2502 CB PRO A 483 4695 4015 4774 763 716 577 C ATOM 2503 CG PRO A 483 91.705 48.534 31.524 1.00 38.75 C ANISOU 2503 CG PRO A 483 5022 4390 5310 731 710 650 C ATOM 2504 CD PRO A 483 92.382 49.333 30.436 1.00 34.87 C ANISOU 2504 CD PRO A 483 4540 3957 4751 638 582 569 C ATOM 2505 N ASP A 484 92.889 45.735 29.611 1.00 42.46 N ANISOU 2505 N ASP A 484 5391 4947 5794 546 480 537 N ATOM 2506 CA ASP A 484 92.646 44.357 29.200 1.00 49.87 C ANISOU 2506 CA ASP A 484 6260 5872 6816 511 440 557 C ATOM 2507 C ASP A 484 93.635 43.862 28.146 1.00 55.23 C ANISOU 2507 C ASP A 484 6960 6610 7413 424 317 465 C ATOM 2508 O ASP A 484 94.014 42.687 28.162 1.00 65.47 O ANISOU 2508 O ASP A 484 8252 7922 8703 415 301 442 O ATOM 2509 CB ASP A 484 91.208 44.228 28.695 1.00 59.07 C ANISOU 2509 CB ASP A 484 7305 6956 8181 490 425 664 C ATOM 2510 CG ASP A 484 90.191 44.720 29.721 1.00 75.25 C ANISOU 2510 CG ASP A 484 9325 8935 10330 582 568 769 C ATOM 2511 OD1 ASP A 484 90.370 44.408 30.925 1.00 75.29 O ANISOU 2511 OD1 ASP A 484 9385 8934 10289 672 692 783 O ATOM 2512 OD2 ASP A 484 89.228 45.422 29.333 1.00 79.09 O ANISOU 2512 OD2 ASP A 484 9744 9367 10939 568 560 838 O ATOM 2513 N THR A 485 94.081 44.735 27.241 1.00 41.38 N ANISOU 2513 N THR A 485 5238 4887 5598 365 239 413 N ATOM 2514 CA THR A 485 94.921 44.332 26.126 1.00 37.82 C ANISOU 2514 CA THR A 485 4814 4476 5079 288 135 338 C ATOM 2515 C THR A 485 96.296 44.970 26.127 1.00 39.60 C ANISOU 2515 C THR A 485 5124 4765 5158 280 131 245 C ATOM 2516 O THR A 485 97.175 44.487 25.404 1.00 37.54 O ANISOU 2516 O THR A 485 4892 4536 4834 232 76 183 O ATOM 2517 CB THR A 485 94.240 44.689 24.796 1.00 42.56 C ANISOU 2517 CB THR A 485 5381 5041 5747 220 33 363 C ATOM 2518 OG1 THR A 485 94.230 46.121 24.650 1.00 39.59 O ANISOU 2518 OG1 THR A 485 5033 4673 5337 217 38 356 O ATOM 2519 CG2 THR A 485 92.797 44.158 24.774 1.00 41.33 C ANISOU 2519 CG2 THR A 485 5128 4804 5773 226 20 464 C ATOM 2520 N GLY A 486 96.498 46.052 26.881 1.00 38.18 N ANISOU 2520 N GLY A 486 4983 4593 4931 326 187 237 N ATOM 2521 CA GLY A 486 97.736 46.797 26.840 1.00 34.82 C ANISOU 2521 CA GLY A 486 4625 4212 4395 316 170 157 C ATOM 2522 C GLY A 486 97.902 47.715 25.646 1.00 37.99 C ANISOU 2522 C GLY A 486 5033 4623 4780 251 106 135 C ATOM 2523 O GLY A 486 98.986 48.283 25.478 1.00 39.92 O ANISOU 2523 O GLY A 486 5322 4898 4949 236 92 71 O ATOM 2524 N LYS A 487 96.876 47.869 24.807 1.00 36.72 N ANISOU 2524 N LYS A 487 4829 4428 4694 214 65 187 N ATOM 2525 CA LYS A 487 96.940 48.841 23.719 1.00 38.71 C ANISOU 2525 CA LYS A 487 5101 4681 4926 162 8 171 C ATOM 2526 C LYS A 487 97.164 50.244 24.265 1.00 37.19 C ANISOU 2526 C LYS A 487 4935 4501 4696 192 47 160 C ATOM 2527 O LYS A 487 96.504 50.664 25.223 1.00 39.62 O ANISOU 2527 O LYS A 487 5228 4788 5039 249 106 206 O ATOM 2528 CB LYS A 487 95.649 48.809 22.901 1.00 33.97 C ANISOU 2528 CB LYS A 487 4453 4026 4428 129 -52 237 C ATOM 2529 CG LYS A 487 95.614 47.715 21.864 1.00 46.66 C ANISOU 2529 CG LYS A 487 6065 5614 6050 79 -136 228 C ATOM 2530 CD LYS A 487 94.189 47.314 21.544 1.00 53.10 C ANISOU 2530 CD LYS A 487 6812 6356 7008 68 -193 308 C ATOM 2531 CE LYS A 487 93.611 48.178 20.460 1.00 54.84 C ANISOU 2531 CE LYS A 487 7047 6534 7255 25 -278 325 C ATOM 2532 NZ LYS A 487 92.950 47.334 19.429 1.00 51.56 N ANISOU 2532 NZ LYS A 487 6628 6051 6912 -16 -402 349 N ATOM 2533 N ASP A 488 98.088 50.976 23.655 1.00 28.12 N ANISOU 2533 N ASP A 488 3828 3378 3477 158 21 105 N ATOM 2534 CA ASP A 488 98.320 52.359 24.048 1.00 33.27 C ANISOU 2534 CA ASP A 488 4505 4037 4100 180 43 93 C ATOM 2535 C ASP A 488 97.727 53.309 22.998 1.00 31.21 C ANISOU 2535 C ASP A 488 4238 3758 3861 135 0 116 C ATOM 2536 O ASP A 488 97.099 52.883 22.024 1.00 32.06 O ANISOU 2536 O ASP A 488 4331 3843 4009 92 -52 142 O ATOM 2537 CB ASP A 488 99.816 52.595 24.304 1.00 33.90 C ANISOU 2537 CB ASP A 488 4627 4147 4106 184 47 18 C ATOM 2538 CG ASP A 488 100.698 52.294 23.098 1.00 38.21 C ANISOU 2538 CG ASP A 488 5189 4708 4622 122 12 -25 C ATOM 2539 OD1 ASP A 488 100.222 52.338 21.941 1.00 36.93 O ANISOU 2539 OD1 ASP A 488 5029 4531 4470 76 -24 -6 O ATOM 2540 OD2 ASP A 488 101.900 52.010 23.321 1.00 40.68 O ANISOU 2540 OD2 ASP A 488 5519 5036 4903 125 21 -77 O ATOM 2541 N ALA A 489 97.917 54.614 23.218 1.00 32.36 N ANISOU 2541 N ALA A 489 4403 3910 3982 148 14 106 N ATOM 2542 CA ALA A 489 97.312 55.620 22.344 1.00 35.78 C ANISOU 2542 CA ALA A 489 4833 4327 4437 112 -21 131 C ATOM 2543 C ALA A 489 97.776 55.461 20.897 1.00 39.80 C ANISOU 2543 C ALA A 489 5373 4836 4914 47 -78 100 C ATOM 2544 O ALA A 489 96.979 55.588 19.956 1.00 37.80 O ANISOU 2544 O ALA A 489 5119 4550 4692 12 -131 132 O ATOM 2545 CB ALA A 489 97.637 57.024 22.856 1.00 37.50 C ANISOU 2545 CB ALA A 489 5072 4554 4623 138 3 115 C ATOM 2546 N LEU A 490 99.057 55.164 20.702 1.00 37.59 N ANISOU 2546 N LEU A 490 5127 4582 4573 36 -66 42 N ATOM 2547 CA LEU A 490 99.574 54.944 19.358 1.00 40.31 C ANISOU 2547 CA LEU A 490 5519 4919 4879 -13 -98 17 C ATOM 2548 C LEU A 490 98.879 53.766 18.680 1.00 40.88 C ANISOU 2548 C LEU A 490 5599 4962 4972 -35 -149 42 C ATOM 2549 O LEU A 490 98.496 53.859 17.506 1.00 38.74 O ANISOU 2549 O LEU A 490 5373 4656 4690 -69 -205 52 O ATOM 2550 CB LEU A 490 101.083 54.730 19.430 1.00 40.44 C ANISOU 2550 CB LEU A 490 5557 4959 4849 -12 -58 -39 C ATOM 2551 CG LEU A 490 101.972 55.000 18.226 1.00 35.48 C ANISOU 2551 CG LEU A 490 4984 4320 4177 -46 -50 -67 C ATOM 2552 CD1 LEU A 490 101.763 56.406 17.664 1.00 30.24 C ANISOU 2552 CD1 LEU A 490 4339 3643 3509 -60 -56 -56 C ATOM 2553 CD2 LEU A 490 103.414 54.787 18.693 1.00 30.43 C ANISOU 2553 CD2 LEU A 490 4333 3696 3531 -33 -1 -112 C ATOM 2554 N ASP A 491 98.699 52.652 19.406 1.00 31.36 N ANISOU 2554 N ASP A 491 4356 3763 3797 -12 -138 51 N ATOM 2555 CA ASP A 491 97.954 51.519 18.857 1.00 36.98 C ANISOU 2555 CA ASP A 491 5065 4439 4547 -31 -197 80 C ATOM 2556 C ASP A 491 96.562 51.954 18.393 1.00 39.53 C ANISOU 2556 C ASP A 491 5364 4709 4948 -46 -263 140 C ATOM 2557 O ASP A 491 96.144 51.636 17.278 1.00 47.12 O ANISOU 2557 O ASP A 491 6367 5622 5914 -80 -347 148 O ATOM 2558 CB ASP A 491 97.833 50.394 19.892 1.00 35.71 C ANISOU 2558 CB ASP A 491 4853 4291 4426 3 -166 92 C ATOM 2559 CG ASP A 491 99.160 49.687 20.186 1.00 45.95 C ANISOU 2559 CG ASP A 491 6175 5627 5655 11 -125 33 C ATOM 2560 OD1 ASP A 491 99.911 49.356 19.235 1.00 45.50 O ANISOU 2560 OD1 ASP A 491 6175 5571 5542 -20 -143 -3 O ATOM 2561 OD2 ASP A 491 99.444 49.457 21.391 1.00 43.69 O ANISOU 2561 OD2 ASP A 491 5860 5367 5375 53 -72 26 O ATOM 2562 N ILE A 492 95.825 52.671 19.250 1.00 33.30 N ANISOU 2562 N ILE A 492 4513 3916 4223 -17 -228 183 N ATOM 2563 CA ILE A 492 94.490 53.149 18.890 1.00 35.66 C ANISOU 2563 CA ILE A 492 4774 4157 4618 -29 -284 246 C ATOM 2564 C ILE A 492 94.549 53.968 17.605 1.00 31.55 C ANISOU 2564 C ILE A 492 4322 3614 4050 -72 -353 228 C ATOM 2565 O ILE A 492 93.861 53.669 16.625 1.00 36.14 O ANISOU 2565 O ILE A 492 4927 4135 4671 -104 -453 250 O ATOM 2566 CB ILE A 492 93.877 53.976 20.038 1.00 32.65 C ANISOU 2566 CB ILE A 492 4330 3778 4297 17 -211 292 C ATOM 2567 CG1 ILE A 492 93.680 53.138 21.309 1.00 34.17 C ANISOU 2567 CG1 ILE A 492 4470 3975 4537 72 -136 322 C ATOM 2568 CG2 ILE A 492 92.550 54.606 19.605 1.00 28.76 C ANISOU 2568 CG2 ILE A 492 3793 3221 3913 2 -264 360 C ATOM 2569 CD1 ILE A 492 92.664 52.043 21.198 1.00 40.52 C ANISOU 2569 CD1 ILE A 492 5209 4720 5466 67 -175 384 C ATOM 2570 N MET A 493 95.409 54.988 17.583 1.00 28.34 N ANISOU 2570 N MET A 493 3957 3250 3561 -71 -305 186 N ATOM 2571 CA MET A 493 95.357 55.990 16.519 1.00 32.04 C ANISOU 2571 CA MET A 493 4484 3696 3994 -103 -351 178 C ATOM 2572 C MET A 493 95.816 55.440 15.174 1.00 32.45 C ANISOU 2572 C MET A 493 4638 3719 3974 -135 -411 146 C ATOM 2573 O MET A 493 95.244 55.793 14.137 1.00 35.80 O ANISOU 2573 O MET A 493 5119 4087 4397 -160 -493 160 O ATOM 2574 CB MET A 493 96.204 57.199 16.901 1.00 30.74 C ANISOU 2574 CB MET A 493 4330 3579 3770 -90 -278 145 C ATOM 2575 CG MET A 493 95.597 58.021 18.015 1.00 34.63 C ANISOU 2575 CG MET A 493 4754 4083 4320 -56 -235 181 C ATOM 2576 SD MET A 493 96.817 59.136 18.741 1.00 39.24 S ANISOU 2576 SD MET A 493 5353 4722 4835 -30 -158 131 S ATOM 2577 CE MET A 493 97.040 60.329 17.425 1.00 29.13 C ANISOU 2577 CE MET A 493 4131 3427 3511 -73 -192 116 C ATOM 2578 N MET A 494 96.858 54.598 15.163 1.00 31.08 N ANISOU 2578 N MET A 494 4500 3573 3735 -130 -371 103 N ATOM 2579 CA MET A 494 97.392 54.095 13.898 1.00 30.87 C ANISOU 2579 CA MET A 494 4588 3513 3626 -149 -408 74 C ATOM 2580 C MET A 494 96.348 53.344 13.084 1.00 32.14 C ANISOU 2580 C MET A 494 4791 3598 3824 -167 -534 104 C ATOM 2581 O MET A 494 96.456 53.274 11.857 1.00 35.76 O ANISOU 2581 O MET A 494 5373 4003 4213 -179 -593 89 O ATOM 2582 CB MET A 494 98.572 53.166 14.157 1.00 35.01 C ANISOU 2582 CB MET A 494 5128 4077 4098 -137 -341 33 C ATOM 2583 CG MET A 494 99.832 53.848 14.561 1.00 39.21 C ANISOU 2583 CG MET A 494 5652 4659 4589 -125 -238 -4 C ATOM 2584 SD MET A 494 101.133 52.618 14.628 1.00 42.48 S ANISOU 2584 SD MET A 494 6089 5095 4956 -115 -178 -46 S ATOM 2585 CE MET A 494 100.471 51.455 15.848 1.00 39.59 C ANISOU 2585 CE MET A 494 5628 4752 4660 -98 -202 -29 C ATOM 2586 N PHE A 495 95.355 52.747 13.741 1.00 26.80 N ANISOU 2586 N PHE A 495 4021 2903 3260 -163 -578 148 N ATOM 2587 CA PHE A 495 94.334 51.986 13.046 1.00 34.86 C ANISOU 2587 CA PHE A 495 5063 3836 4346 -180 -714 181 C ATOM 2588 C PHE A 495 92.987 52.678 13.048 1.00 34.23 C ANISOU 2588 C PHE A 495 4918 3699 4391 -191 -790 241 C ATOM 2589 O PHE A 495 92.013 52.097 12.563 1.00 31.86 O ANISOU 2589 O PHE A 495 4613 3311 4182 -206 -918 278 O ATOM 2590 CB PHE A 495 94.202 50.588 13.664 1.00 31.39 C ANISOU 2590 CB PHE A 495 4560 3399 3966 -169 -717 193 C ATOM 2591 CG PHE A 495 95.444 49.765 13.531 1.00 32.61 C ANISOU 2591 CG PHE A 495 4785 3597 4008 -161 -662 137 C ATOM 2592 CD1 PHE A 495 95.728 49.102 12.341 1.00 31.35 C ANISOU 2592 CD1 PHE A 495 4758 3384 3768 -172 -737 111 C ATOM 2593 CD2 PHE A 495 96.338 49.673 14.577 1.00 31.24 C ANISOU 2593 CD2 PHE A 495 4555 3507 3809 -139 -537 112 C ATOM 2594 CE1 PHE A 495 96.875 48.350 12.208 1.00 38.84 C ANISOU 2594 CE1 PHE A 495 5770 4367 4619 -161 -674 65 C ATOM 2595 CE2 PHE A 495 97.494 48.915 14.448 1.00 46.21 C ANISOU 2595 CE2 PHE A 495 6506 5435 5616 -133 -487 63 C ATOM 2596 CZ PHE A 495 97.764 48.262 13.264 1.00 43.57 C ANISOU 2596 CZ PHE A 495 6293 5053 5209 -144 -548 42 C ATOM 2597 N HIS A 496 92.900 53.892 13.574 1.00 29.74 N ANISOU 2597 N HIS A 496 4297 3166 3836 -184 -723 254 N ATOM 2598 CA HIS A 496 91.609 54.560 13.678 1.00 33.82 C ANISOU 2598 CA HIS A 496 4739 3627 4485 -191 -780 317 C ATOM 2599 C HIS A 496 91.297 55.305 12.379 1.00 28.37 C ANISOU 2599 C HIS A 496 4150 2871 3757 -220 -889 310 C ATOM 2600 O HIS A 496 92.196 55.828 11.709 1.00 30.76 O ANISOU 2600 O HIS A 496 4566 3201 3921 -224 -861 259 O ATOM 2601 CB HIS A 496 91.595 55.514 14.880 1.00 25.80 C ANISOU 2601 CB HIS A 496 3630 2674 3501 -162 -658 337 C ATOM 2602 CG HIS A 496 90.253 56.108 15.158 1.00 34.24 C ANISOU 2602 CG HIS A 496 4605 3684 4721 -161 -691 412 C ATOM 2603 ND1 HIS A 496 89.818 57.273 14.556 1.00 29.95 N ANISOU 2603 ND1 HIS A 496 4087 3110 4183 -181 -739 423 N ATOM 2604 CD2 HIS A 496 89.236 55.684 15.947 1.00 27.00 C ANISOU 2604 CD2 HIS A 496 3569 2726 3966 -140 -679 486 C ATOM 2605 CE1 HIS A 496 88.592 57.542 14.970 1.00 33.09 C ANISOU 2605 CE1 HIS A 496 4380 3451 4743 -174 -759 500 C ATOM 2606 NE2 HIS A 496 88.218 56.598 15.817 1.00 30.94 N ANISOU 2606 NE2 HIS A 496 4017 3169 4572 -148 -717 542 N ATOM 2607 N GLN A 497 90.003 55.363 12.035 1.00 33.82 N ANISOU 2607 N GLN A 497 4800 3467 4583 -237 -1012 367 N ATOM 2608 CA GLN A 497 89.608 55.909 10.733 1.00 37.88 C ANISOU 2608 CA GLN A 497 5426 3898 5068 -263 -1147 361 C ATOM 2609 C GLN A 497 90.071 57.347 10.550 1.00 33.81 C ANISOU 2609 C GLN A 497 4957 3430 4458 -264 -1078 336 C ATOM 2610 O GLN A 497 90.386 57.755 9.428 1.00 35.02 O ANISOU 2610 O GLN A 497 5255 3548 4504 -275 -1135 302 O ATOM 2611 CB GLN A 497 88.092 55.820 10.540 1.00 37.81 C ANISOU 2611 CB GLN A 497 5341 3773 5253 -282 -1295 433 C ATOM 2612 CG GLN A 497 87.259 56.375 11.679 1.00 42.18 C ANISOU 2612 CG GLN A 497 5715 4339 5972 -269 -1220 504 C ATOM 2613 CD GLN A 497 85.762 56.308 11.375 1.00 56.79 C ANISOU 2613 CD GLN A 497 7485 6055 8039 -289 -1372 583 C ATOM 2614 OE1 GLN A 497 85.361 56.018 10.247 1.00 52.48 O ANISOU 2614 OE1 GLN A 497 7029 5405 7506 -316 -1552 577 O ATOM 2615 NE2 GLN A 497 84.935 56.577 12.381 1.00 62.32 N ANISOU 2615 NE2 GLN A 497 8019 6746 8913 -272 -1301 660 N ATOM 2616 N PHE A 498 90.151 58.121 11.630 1.00 28.53 N ANISOU 2616 N PHE A 498 4180 2836 3823 -248 -953 352 N ATOM 2617 CA PHE A 498 90.663 59.483 11.555 1.00 26.34 C ANISOU 2617 CA PHE A 498 3939 2609 3461 -247 -883 327 C ATOM 2618 C PHE A 498 92.013 59.658 12.217 1.00 33.14 C ANISOU 2618 C PHE A 498 4805 3574 4212 -224 -733 277 C ATOM 2619 O PHE A 498 92.829 60.444 11.729 1.00 32.79 O ANISOU 2619 O PHE A 498 4840 3558 4062 -228 -691 237 O ATOM 2620 CB PHE A 498 89.648 60.457 12.178 1.00 30.51 C ANISOU 2620 CB PHE A 498 4354 3124 4115 -245 -875 385 C ATOM 2621 CG PHE A 498 88.251 60.303 11.608 1.00 36.53 C ANISOU 2621 CG PHE A 498 5086 3770 5024 -268 -1027 445 C ATOM 2622 CD1 PHE A 498 88.042 60.350 10.227 1.00 44.02 C ANISOU 2622 CD1 PHE A 498 6161 4634 5929 -296 -1174 427 C ATOM 2623 CD2 PHE A 498 87.168 60.044 12.433 1.00 31.89 C ANISOU 2623 CD2 PHE A 498 4351 3143 4624 -257 -1027 521 C ATOM 2624 CE1 PHE A 498 86.756 60.179 9.673 1.00 37.63 C ANISOU 2624 CE1 PHE A 498 5328 3700 5270 -319 -1342 480 C ATOM 2625 CE2 PHE A 498 85.889 59.872 11.896 1.00 34.60 C ANISOU 2625 CE2 PHE A 498 4652 3363 5132 -280 -1177 582 C ATOM 2626 CZ PHE A 498 85.686 59.954 10.511 1.00 28.87 C ANISOU 2626 CZ PHE A 498 4050 2552 4369 -314 -1345 559 C ATOM 2627 N GLY A 499 92.278 58.936 13.305 1.00 34.04 N ANISOU 2627 N GLY A 499 4838 3738 4358 -200 -656 280 N ATOM 2628 CA GLY A 499 93.538 59.106 14.001 1.00 29.46 C ANISOU 2628 CA GLY A 499 4258 3244 3691 -177 -532 233 C ATOM 2629 C GLY A 499 94.747 58.727 13.174 1.00 31.91 C ANISOU 2629 C GLY A 499 4680 3568 3876 -186 -516 175 C ATOM 2630 O GLY A 499 95.847 59.219 13.445 1.00 31.07 O ANISOU 2630 O GLY A 499 4586 3516 3703 -175 -426 137 O ATOM 2631 N ASN A 500 94.568 57.848 12.176 1.00 28.10 N ANISOU 2631 N ASN A 500 4281 3026 3370 -202 -603 171 N ATOM 2632 CA ASN A 500 95.698 57.382 11.382 1.00 24.73 C ANISOU 2632 CA ASN A 500 3972 2601 2823 -201 -574 122 C ATOM 2633 C ASN A 500 96.346 58.532 10.630 1.00 27.98 C ANISOU 2633 C ASN A 500 4471 3012 3148 -204 -533 99 C ATOM 2634 O ASN A 500 97.563 58.520 10.405 1.00 27.43 O ANISOU 2634 O ASN A 500 4455 2969 2999 -193 -444 63 O ATOM 2635 CB ASN A 500 95.253 56.278 10.403 1.00 31.69 C ANISOU 2635 CB ASN A 500 4950 3403 3689 -210 -690 125 C ATOM 2636 CG ASN A 500 94.546 56.834 9.162 1.00 31.56 C ANISOU 2636 CG ASN A 500 5045 3296 3648 -225 -808 138 C ATOM 2637 OD1 ASN A 500 95.189 57.232 8.188 1.00 37.36 O ANISOU 2637 OD1 ASN A 500 5921 4007 4268 -220 -790 110 O ATOM 2638 ND2 ASN A 500 93.225 56.859 9.199 1.00 29.58 N ANISOU 2638 ND2 ASN A 500 4737 2986 3515 -241 -926 184 N ATOM 2639 N TYR A 501 95.547 59.531 10.235 1.00 30.76 N ANISOU 2639 N TYR A 501 4833 3329 3526 -217 -591 124 N ATOM 2640 CA TYR A 501 96.110 60.704 9.574 1.00 33.80 C ANISOU 2640 CA TYR A 501 5294 3713 3836 -219 -546 106 C ATOM 2641 C TYR A 501 96.983 61.514 10.526 1.00 32.85 C ANISOU 2641 C TYR A 501 5085 3673 3722 -207 -422 90 C ATOM 2642 O TYR A 501 97.948 62.146 10.087 1.00 34.30 O ANISOU 2642 O TYR A 501 5324 3865 3842 -202 -348 67 O ATOM 2643 CB TYR A 501 94.993 61.576 8.992 1.00 28.62 C ANISOU 2643 CB TYR A 501 4662 2998 3213 -237 -647 137 C ATOM 2644 CG TYR A 501 94.236 60.898 7.881 1.00 29.34 C ANISOU 2644 CG TYR A 501 4870 2988 3290 -246 -790 148 C ATOM 2645 CD1 TYR A 501 94.756 60.848 6.579 1.00 30.98 C ANISOU 2645 CD1 TYR A 501 5265 3136 3370 -236 -808 122 C ATOM 2646 CD2 TYR A 501 93.014 60.279 8.127 1.00 34.80 C ANISOU 2646 CD2 TYR A 501 5493 3630 4099 -259 -910 187 C ATOM 2647 CE1 TYR A 501 94.059 60.208 5.549 1.00 33.90 C ANISOU 2647 CE1 TYR A 501 5767 3397 3716 -238 -959 128 C ATOM 2648 CE2 TYR A 501 92.308 59.632 7.098 1.00 37.44 C ANISOU 2648 CE2 TYR A 501 5936 3854 4433 -268 -1069 196 C ATOM 2649 CZ TYR A 501 92.840 59.601 5.820 1.00 37.69 C ANISOU 2649 CZ TYR A 501 6170 3828 4323 -256 -1099 162 C ATOM 2650 OH TYR A 501 92.150 58.971 4.811 1.00 46.39 O ANISOU 2650 OH TYR A 501 7402 4809 5415 -257 -1271 167 O ATOM 2651 N VAL A 502 96.691 61.478 11.830 1.00 27.81 N ANISOU 2651 N VAL A 502 4318 3084 3164 -197 -398 104 N ATOM 2652 CA VAL A 502 97.506 62.231 12.780 1.00 29.71 C ANISOU 2652 CA VAL A 502 4491 3389 3411 -180 -301 86 C ATOM 2653 C VAL A 502 98.880 61.577 12.944 1.00 28.19 C ANISOU 2653 C VAL A 502 4311 3225 3174 -167 -223 46 C ATOM 2654 O VAL A 502 99.917 62.245 12.866 1.00 32.16 O ANISOU 2654 O VAL A 502 4825 3744 3652 -163 -154 22 O ATOM 2655 CB VAL A 502 96.762 62.376 14.120 1.00 35.70 C ANISOU 2655 CB VAL A 502 5135 4176 4253 -161 -298 114 C ATOM 2656 CG1 VAL A 502 97.629 63.116 15.144 1.00 30.80 C ANISOU 2656 CG1 VAL A 502 4466 3609 3630 -136 -217 90 C ATOM 2657 CG2 VAL A 502 95.443 63.091 13.904 1.00 33.24 C ANISOU 2657 CG2 VAL A 502 4803 3827 4000 -173 -365 160 C ATOM 2658 N VAL A 503 98.909 60.259 13.156 1.00 32.25 N ANISOU 2658 N VAL A 503 4819 3741 3692 -162 -235 41 N ATOM 2659 CA VAL A 503 100.186 59.550 13.214 1.00 30.19 C ANISOU 2659 CA VAL A 503 4576 3500 3396 -151 -165 5 C ATOM 2660 C VAL A 503 100.980 59.783 11.941 1.00 34.34 C ANISOU 2660 C VAL A 503 5212 3988 3848 -157 -128 -10 C ATOM 2661 O VAL A 503 102.200 60.014 11.981 1.00 33.97 O ANISOU 2661 O VAL A 503 5162 3954 3792 -148 -40 -32 O ATOM 2662 CB VAL A 503 99.957 58.047 13.448 1.00 33.18 C ANISOU 2662 CB VAL A 503 4946 3877 3783 -146 -195 5 C ATOM 2663 CG1 VAL A 503 101.325 57.317 13.644 1.00 27.62 C ANISOU 2663 CG1 VAL A 503 4247 3197 3051 -134 -118 -32 C ATOM 2664 CG2 VAL A 503 98.984 57.819 14.602 1.00 34.82 C ANISOU 2664 CG2 VAL A 503 5055 4106 4070 -134 -227 34 C ATOM 2665 N AGLN A 504 100.304 59.703 10.788 0.60 29.02 N ANISOU 2665 N AGLN A 504 4643 3256 3126 -168 -193 5 N ATOM 2666 N BGLN A 504 100.327 59.716 10.775 0.40 30.49 N ANISOU 2666 N BGLN A 504 4831 3442 3312 -168 -192 5 N ATOM 2667 CA AGLN A 504 100.933 59.951 9.496 0.60 36.41 C ANISOU 2667 CA AGLN A 504 5716 4141 3977 -163 -155 -3 C ATOM 2668 CA BGLN A 504 101.061 59.938 9.533 0.40 36.12 C ANISOU 2668 CA BGLN A 504 5676 4108 3941 -162 -144 -5 C ATOM 2669 C AGLN A 504 101.591 61.325 9.476 0.60 34.06 C ANISOU 2669 C AGLN A 504 5399 3857 3687 -161 -75 -4 C ATOM 2670 C BGLN A 504 101.635 61.347 9.489 0.40 34.22 C ANISOU 2670 C BGLN A 504 5417 3878 3707 -161 -71 -5 C ATOM 2671 O AGLN A 504 102.744 61.482 9.054 0.60 33.91 O ANISOU 2671 O AGLN A 504 5420 3824 3641 -147 26 -15 O ATOM 2672 O BGLN A 504 102.772 61.553 9.046 0.40 33.49 O ANISOU 2672 O BGLN A 504 5366 3771 3588 -147 29 -14 O ATOM 2673 CB AGLN A 504 99.875 59.827 8.390 0.60 41.17 C ANISOU 2673 CB AGLN A 504 6441 4669 4532 -171 -268 15 C ATOM 2674 CB BGLN A 504 100.169 59.691 8.318 0.40 41.12 C ANISOU 2674 CB BGLN A 504 6448 4663 4512 -166 -244 10 C ATOM 2675 CG AGLN A 504 100.291 58.970 7.199 0.60 47.31 C ANISOU 2675 CG AGLN A 504 7389 5379 5209 -152 -267 5 C ATOM 2676 CG BGLN A 504 100.890 59.900 6.982 0.40 44.80 C ANISOU 2676 CG BGLN A 504 7084 5065 4872 -146 -187 3 C ATOM 2677 CD AGLN A 504 99.203 58.025 6.668 0.60 49.25 C ANISOU 2677 CD AGLN A 504 7712 5559 5440 -158 -417 15 C ATOM 2678 CD BGLN A 504 101.779 58.721 6.603 0.40 46.95 C ANISOU 2678 CD BGLN A 504 7435 5317 5086 -122 -125 -13 C ATOM 2679 OE1AGLN A 504 99.532 57.021 6.054 0.60 49.88 O ANISOU 2679 OE1AGLN A 504 7904 5597 5453 -139 -425 3 O ATOM 2680 OE1BGLN A 504 101.399 57.570 6.778 0.40 44.99 O ANISOU 2680 OE1BGLN A 504 7187 5065 4842 -124 -192 -18 O ATOM 2681 NE2AGLN A 504 97.923 58.353 6.876 0.60 24.72 N ANISOU 2681 NE2AGLN A 504 4550 2436 2407 -180 -538 40 N ATOM 2682 NE2BGLN A 504 102.964 59.012 6.082 0.40 46.22 N ANISOU 2682 NE2BGLN A 504 7407 5206 4949 -97 8 -17 N ATOM 2683 N CYS A 505 100.867 62.328 9.961 1.00 33.12 N ANISOU 2683 N CYS A 505 5211 3759 3615 -173 -116 10 N ATOM 2684 CA CYS A 505 101.394 63.676 10.077 1.00 33.95 C ANISOU 2684 CA CYS A 505 5283 3878 3738 -173 -55 9 C ATOM 2685 C CYS A 505 102.628 63.710 10.985 1.00 31.76 C ANISOU 2685 C CYS A 505 4913 3642 3511 -160 34 -12 C ATOM 2686 O CYS A 505 103.665 64.279 10.625 1.00 32.84 O ANISOU 2686 O CYS A 505 5063 3762 3652 -153 118 -17 O ATOM 2687 CB CYS A 505 100.274 64.580 10.598 1.00 34.65 C ANISOU 2687 CB CYS A 505 5307 3984 3873 -186 -125 30 C ATOM 2688 SG CYS A 505 100.774 66.247 10.865 1.00 47.34 S ANISOU 2688 SG CYS A 505 6867 5612 5509 -185 -69 29 S ATOM 2689 N MET A 506 102.544 63.061 12.153 1.00 29.86 N ANISOU 2689 N MET A 506 4583 3445 3318 -153 14 -22 N ATOM 2690 CA MET A 506 103.696 62.944 13.042 1.00 32.80 C ANISOU 2690 CA MET A 506 4879 3845 3741 -139 75 -46 C ATOM 2691 C MET A 506 104.892 62.327 12.323 1.00 36.33 C ANISOU 2691 C MET A 506 5374 4260 4169 -133 156 -57 C ATOM 2692 O MET A 506 106.027 62.796 12.471 1.00 34.98 O ANISOU 2692 O MET A 506 5163 4079 4049 -126 226 -66 O ATOM 2693 CB MET A 506 103.336 62.100 14.276 1.00 32.85 C ANISOU 2693 CB MET A 506 4814 3890 3779 -126 37 -55 C ATOM 2694 CG MET A 506 102.248 62.693 15.203 1.00 27.97 C ANISOU 2694 CG MET A 506 4140 3297 3192 -117 -17 -37 C ATOM 2695 SD MET A 506 101.626 61.460 16.408 1.00 35.19 S ANISOU 2695 SD MET A 506 5000 4238 4131 -93 -47 -33 S ATOM 2696 CE MET A 506 103.117 61.045 17.302 1.00 32.48 C ANISOU 2696 CE MET A 506 4619 3913 3810 -70 3 -76 C ATOM 2697 N LEU A 507 104.658 61.270 11.539 1.00 32.00 N ANISOU 2697 N LEU A 507 4914 3687 3557 -133 147 -54 N ATOM 2698 CA LEU A 507 105.762 60.635 10.830 1.00 32.67 C ANISOU 2698 CA LEU A 507 5059 3735 3618 -120 236 -60 C ATOM 2699 C LEU A 507 106.335 61.568 9.768 1.00 37.58 C ANISOU 2699 C LEU A 507 5756 4304 4218 -112 317 -42 C ATOM 2700 O LEU A 507 107.563 61.672 9.613 1.00 38.06 O ANISOU 2700 O LEU A 507 5800 4339 4322 -98 424 -39 O ATOM 2701 CB LEU A 507 105.294 59.308 10.210 1.00 33.65 C ANISOU 2701 CB LEU A 507 5280 3837 3668 -116 198 -60 C ATOM 2702 CG LEU A 507 106.379 58.517 9.468 1.00 37.63 C ANISOU 2702 CG LEU A 507 5863 4299 4136 -95 295 -63 C ATOM 2703 CD1 LEU A 507 107.472 58.142 10.446 1.00 40.68 C ANISOU 2703 CD1 LEU A 507 6130 4717 4609 -91 357 -81 C ATOM 2704 CD2 LEU A 507 105.821 57.258 8.785 1.00 34.52 C ANISOU 2704 CD2 LEU A 507 5586 3874 3655 -88 240 -64 C ATOM 2705 N THR A 508 105.462 62.280 9.048 1.00 32.93 N ANISOU 2705 N THR A 508 5246 3693 3575 -120 270 -26 N ATOM 2706 CA THR A 508 105.938 63.193 8.012 1.00 37.43 C ANISOU 2706 CA THR A 508 5900 4207 4114 -107 350 -6 C ATOM 2707 C THR A 508 106.818 64.293 8.600 1.00 38.93 C ANISOU 2707 C THR A 508 5975 4412 4407 -109 420 -3 C ATOM 2708 O THR A 508 107.874 64.618 8.044 1.00 34.67 O ANISOU 2708 O THR A 508 5456 3824 3894 -91 538 13 O ATOM 2709 CB THR A 508 104.752 63.800 7.272 1.00 39.83 C ANISOU 2709 CB THR A 508 6301 4485 4347 -116 266 7 C ATOM 2710 OG1 THR A 508 103.943 62.744 6.744 1.00 40.46 O ANISOU 2710 OG1 THR A 508 6487 4538 4350 -114 180 5 O ATOM 2711 CG2 THR A 508 105.219 64.749 6.136 1.00 32.58 C ANISOU 2711 CG2 THR A 508 5493 3503 3384 -97 353 29 C ATOM 2712 N ILE A 509 106.390 64.882 9.720 1.00 31.02 N ANISOU 2712 N ILE A 509 4854 3464 3469 -126 350 -15 N ATOM 2713 CA ILE A 509 107.179 65.923 10.373 1.00 34.20 C ANISOU 2713 CA ILE A 509 5148 3874 3974 -127 389 -16 C ATOM 2714 C ILE A 509 108.580 65.410 10.687 1.00 42.90 C ANISOU 2714 C ILE A 509 6186 4954 5159 -113 474 -22 C ATOM 2715 O ILE A 509 109.586 66.066 10.386 1.00 37.90 O ANISOU 2715 O ILE A 509 5524 4276 4601 -105 562 -5 O ATOM 2716 CB ILE A 509 106.464 66.402 11.645 1.00 32.34 C ANISOU 2716 CB ILE A 509 4814 3695 3777 -137 291 -31 C ATOM 2717 CG1 ILE A 509 105.207 67.192 11.282 1.00 39.89 C ANISOU 2717 CG1 ILE A 509 5816 4659 4681 -150 226 -16 C ATOM 2718 CG2 ILE A 509 107.380 67.250 12.473 1.00 34.97 C ANISOU 2718 CG2 ILE A 509 5041 4027 4219 -131 311 -40 C ATOM 2719 CD1 ILE A 509 104.344 67.528 12.495 1.00 38.28 C ANISOU 2719 CD1 ILE A 509 5533 4505 4508 -152 140 -22 C ATOM 2720 N CYS A 510 108.665 64.219 11.290 1.00 37.61 N ANISOU 2720 N CYS A 510 5488 4310 4490 -110 448 -43 N ATOM 2721 CA CYS A 510 109.964 63.682 11.692 1.00 36.80 C ANISOU 2721 CA CYS A 510 5317 4187 4480 -99 513 -51 C ATOM 2722 C CYS A 510 110.853 63.393 10.493 1.00 40.30 C ANISOU 2722 C CYS A 510 5834 4560 4917 -82 647 -23 C ATOM 2723 O CYS A 510 112.054 63.678 10.529 1.00 45.94 O ANISOU 2723 O CYS A 510 6480 5228 5746 -72 734 -8 O ATOM 2724 CB CYS A 510 109.770 62.426 12.527 1.00 40.65 C ANISOU 2724 CB CYS A 510 5774 4717 4955 -98 456 -79 C ATOM 2725 SG CYS A 510 109.160 62.861 14.143 1.00 43.49 S ANISOU 2725 SG CYS A 510 6034 5135 5356 -100 337 -105 S ATOM 2726 N CYS A 511 110.284 62.829 9.423 1.00 36.28 N ANISOU 2726 N CYS A 511 5470 4033 4282 -73 665 -11 N ATOM 2727 CA CYS A 511 111.061 62.564 8.216 1.00 43.19 C ANISOU 2727 CA CYS A 511 6451 4831 5130 -43 803 20 C ATOM 2728 C CYS A 511 111.488 63.851 7.526 1.00 45.85 C ANISOU 2728 C CYS A 511 6806 5112 5502 -31 894 56 C ATOM 2729 O CYS A 511 112.598 63.928 6.999 1.00 47.85 O ANISOU 2729 O CYS A 511 7063 5296 5822 -5 1038 89 O ATOM 2730 CB CYS A 511 110.271 61.676 7.251 1.00 48.08 C ANISOU 2730 CB CYS A 511 7247 5432 5590 -29 778 21 C ATOM 2731 SG CYS A 511 109.835 60.049 7.927 1.00 56.94 S ANISOU 2731 SG CYS A 511 8352 6606 6675 -39 685 -14 S ATOM 2732 N ASP A 512 110.624 64.870 7.505 1.00 46.12 N ANISOU 2732 N ASP A 512 6851 5170 5502 -48 820 54 N ATOM 2733 CA ASP A 512 111.040 66.158 6.954 1.00 45.80 C ANISOU 2733 CA ASP A 512 6813 5080 5508 -39 901 87 C ATOM 2734 C ASP A 512 112.199 66.756 7.745 1.00 51.28 C ANISOU 2734 C ASP A 512 7335 5760 6389 -44 952 96 C ATOM 2735 O ASP A 512 113.078 67.407 7.167 1.00 50.58 O ANISOU 2735 O ASP A 512 7238 5599 6379 -25 1078 137 O ATOM 2736 CB ASP A 512 109.863 67.135 6.923 1.00 47.32 C ANISOU 2736 CB ASP A 512 7034 5307 5639 -61 797 80 C ATOM 2737 CG ASP A 512 108.797 66.747 5.909 1.00 57.97 C ANISOU 2737 CG ASP A 512 8565 6638 6822 -52 749 82 C ATOM 2738 OD1 ASP A 512 109.046 65.837 5.085 1.00 65.72 O ANISOU 2738 OD1 ASP A 512 9676 7570 7725 -23 811 91 O ATOM 2739 OD2 ASP A 512 107.711 67.367 5.930 1.00 65.10 O ANISOU 2739 OD2 ASP A 512 9487 7568 7678 -73 644 74 O ATOM 2740 N ALA A 513 112.232 66.531 9.059 1.00 47.35 N ANISOU 2740 N ALA A 513 6705 5318 5969 -66 853 61 N ATOM 2741 CA ALA A 513 113.292 67.103 9.879 1.00 50.93 C ANISOU 2741 CA ALA A 513 7001 5745 6605 -70 867 63 C ATOM 2742 C ALA A 513 114.633 66.436 9.597 1.00 52.64 C ANISOU 2742 C ALA A 513 7180 5890 6930 -48 996 90 C ATOM 2743 O ALA A 513 115.639 67.115 9.361 1.00 49.01 O ANISOU 2743 O ALA A 513 6652 5356 6615 -38 1093 129 O ATOM 2744 CB ALA A 513 112.928 66.987 11.358 1.00 47.86 C ANISOU 2744 CB ALA A 513 6512 5423 6251 -88 718 16 C ATOM 2745 N VAL A 514 114.673 65.105 9.612 1.00 51.10 N ANISOU 2745 N VAL A 514 7025 5710 6679 -41 1004 75 N ATOM 2746 CA VAL A 514 115.956 64.438 9.427 1.00 60.19 C ANISOU 2746 CA VAL A 514 8132 6792 7944 -20 1126 101 C ATOM 2747 C VAL A 514 116.463 64.617 8.000 1.00 60.09 C ANISOU 2747 C VAL A 514 8226 6691 7913 17 1311 162 C ATOM 2748 O VAL A 514 117.675 64.581 7.755 1.00 65.12 O ANISOU 2748 O VAL A 514 8801 7243 8697 39 1447 206 O ATOM 2749 CB VAL A 514 115.851 62.949 9.814 1.00 63.34 C ANISOU 2749 CB VAL A 514 8552 7232 8283 -20 1086 69 C ATOM 2750 CG1 VAL A 514 115.378 62.806 11.264 1.00 58.80 C ANISOU 2750 CG1 VAL A 514 7878 6734 7728 -47 917 14 C ATOM 2751 CG2 VAL A 514 114.926 62.217 8.863 1.00 59.74 C ANISOU 2751 CG2 VAL A 514 8278 6796 7624 -7 1098 67 C ATOM 2752 N SER A 515 115.566 64.832 7.042 1.00 51.92 N ANISOU 2752 N SER A 515 7358 5663 6708 29 1323 170 N ATOM 2753 CA SER A 515 115.950 64.951 5.644 1.00 62.99 C ANISOU 2753 CA SER A 515 8903 6973 8057 76 1498 226 C ATOM 2754 C SER A 515 116.167 66.399 5.215 1.00 68.35 C ANISOU 2754 C SER A 515 9562 7602 8807 83 1566 267 C ATOM 2755 O SER A 515 116.191 66.683 4.011 1.00 66.58 O ANISOU 2755 O SER A 515 9489 7309 8501 124 1694 311 O ATOM 2756 CB SER A 515 114.898 64.287 4.753 1.00 73.11 C ANISOU 2756 CB SER A 515 10404 8269 9104 94 1466 212 C ATOM 2757 OG SER A 515 113.687 65.022 4.766 1.00 79.06 O ANISOU 2757 OG SER A 515 11204 9077 9760 68 1334 187 O ATOM 2758 N GLY A 516 116.311 67.317 6.170 1.00 66.92 N ANISOU 2758 N GLY A 516 9209 7449 8768 47 1481 254 N ATOM 2759 CA GLY A 516 116.623 68.698 5.879 1.00 53.09 C ANISOU 2759 CA GLY A 516 7412 5646 7112 50 1540 293 C ATOM 2760 C GLY A 516 115.491 69.533 5.327 1.00 56.38 C ANISOU 2760 C GLY A 516 7948 6096 7376 44 1484 285 C ATOM 2761 O GLY A 516 115.685 70.736 5.131 1.00 65.66 O ANISOU 2761 O GLY A 516 9084 7237 8628 44 1523 315 O ATOM 2762 N ARG A 517 114.315 68.956 5.067 1.00 55.36 N ANISOU 2762 N ARG A 517 7961 6027 7047 39 1389 248 N ATOM 2763 CA ARG A 517 113.207 69.750 4.541 1.00 63.35 C ANISOU 2763 CA ARG A 517 9083 7060 7925 31 1323 242 C ATOM 2764 C ARG A 517 112.461 70.536 5.616 1.00 67.03 C ANISOU 2764 C ARG A 517 9428 7611 8428 -17 1154 202 C ATOM 2765 O ARG A 517 111.524 71.269 5.279 1.00 67.24 O ANISOU 2765 O ARG A 517 9526 7659 8364 -27 1090 197 O ATOM 2766 CB ARG A 517 112.217 68.859 3.787 1.00 73.10 C ANISOU 2766 CB ARG A 517 10520 8306 8949 46 1274 224 C ATOM 2767 CG ARG A 517 112.851 68.005 2.707 1.00 86.38 C ANISOU 2767 CG ARG A 517 12358 9900 10563 103 1431 259 C ATOM 2768 CD ARG A 517 112.167 66.656 2.608 1.00 93.27 C ANISOU 2768 CD ARG A 517 13344 10802 11294 105 1343 223 C ATOM 2769 NE ARG A 517 111.321 66.546 1.425 1.00102.74 N ANISOU 2769 NE ARG A 517 14785 11954 12299 137 1321 227 N ATOM 2770 CZ ARG A 517 110.453 65.560 1.220 1.00106.00 C ANISOU 2770 CZ ARG A 517 15318 12383 12576 136 1205 195 C ATOM 2771 NH1 ARG A 517 110.313 64.602 2.129 1.00106.03 N ANISOU 2771 NH1 ARG A 517 15217 12455 12616 105 1115 160 N ATOM 2772 NH2 ARG A 517 109.723 65.532 0.111 1.00103.07 N ANISOU 2772 NH2 ARG A 517 15176 11950 12037 168 1171 200 N ATOM 2773 N ARG A 518 112.843 70.403 6.888 1.00 61.81 N ANISOU 2773 N ARG A 518 8600 6993 7894 -41 1079 175 N ATOM 2774 CA ARG A 518 112.236 71.155 7.976 1.00 51.99 C ANISOU 2774 CA ARG A 518 7251 5817 6687 -75 931 140 C ATOM 2775 C ARG A 518 113.326 71.681 8.898 1.00 52.11 C ANISOU 2775 C ARG A 518 7089 5803 6906 -81 931 143 C ATOM 2776 O ARG A 518 114.280 70.967 9.216 1.00 61.94 O ANISOU 2776 O ARG A 518 8265 7014 8254 -72 977 147 O ATOM 2777 CB ARG A 518 111.238 70.295 8.776 1.00 48.53 C ANISOU 2777 CB ARG A 518 6819 5464 6156 -93 789 92 C ATOM 2778 CG ARG A 518 110.696 70.977 10.031 1.00 47.89 C ANISOU 2778 CG ARG A 518 6634 5444 6118 -116 652 60 C ATOM 2779 CD ARG A 518 109.812 70.048 10.853 1.00 49.48 C ANISOU 2779 CD ARG A 518 6839 5717 6247 -124 540 23 C ATOM 2780 NE ARG A 518 108.410 70.181 10.476 1.00 51.91 N ANISOU 2780 NE ARG A 518 7236 6062 6428 -135 472 22 N ATOM 2781 CZ ARG A 518 107.488 70.806 11.210 1.00 51.47 C ANISOU 2781 CZ ARG A 518 7144 6053 6361 -146 372 9 C ATOM 2782 NH1 ARG A 518 107.815 71.367 12.384 1.00 39.82 N ANISOU 2782 NH1 ARG A 518 5562 4594 4975 -143 324 -8 N ATOM 2783 NH2 ARG A 518 106.237 70.879 10.759 1.00 37.79 N ANISOU 2783 NH2 ARG A 518 5487 4339 4530 -157 316 16 N ATOM 2784 N GLN A 519 113.177 72.941 9.308 1.00 54.95 N ANISOU 2784 N GLN A 519 7382 6169 7329 -95 872 142 N ATOM 2785 CA GLN A 519 114.063 73.563 10.284 1.00 60.80 C ANISOU 2785 CA GLN A 519 7961 6878 8263 -101 829 139 C ATOM 2786 C GLN A 519 113.981 72.839 11.623 1.00 64.86 C ANISOU 2786 C GLN A 519 8408 7442 8795 -109 698 87 C ATOM 2787 O GLN A 519 112.896 72.702 12.201 1.00 67.93 O ANISOU 2787 O GLN A 519 8835 7908 9065 -117 587 50 O ATOM 2788 CB GLN A 519 113.684 75.036 10.467 1.00 65.27 C ANISOU 2788 CB GLN A 519 8493 7450 8857 -114 768 141 C ATOM 2789 CG GLN A 519 114.496 76.026 9.648 1.00 79.36 C ANISOU 2789 CG GLN A 519 10247 9146 10761 -104 892 198 C ATOM 2790 CD GLN A 519 115.916 76.200 10.171 1.00 89.41 C ANISOU 2790 CD GLN A 519 11361 10331 12280 -98 919 219 C ATOM 2791 OE1 GLN A 519 116.210 75.873 11.323 1.00 90.49 O ANISOU 2791 OE1 GLN A 519 11406 10477 12497 -106 803 182 O ATOM 2792 NE2 GLN A 519 116.804 76.718 9.322 1.00 87.13 N ANISOU 2792 NE2 GLN A 519 11042 9945 12118 -82 1070 284 N ATOM 2793 N THR A 520 115.129 72.385 12.125 1.00 56.63 N ANISOU 2793 N THR A 520 7264 6346 7908 -102 714 89 N ATOM 2794 CA THR A 520 115.191 71.828 13.468 1.00 55.03 C ANISOU 2794 CA THR A 520 6996 6173 7740 -103 583 41 C ATOM 2795 C THR A 520 115.661 72.832 14.507 1.00 61.84 C ANISOU 2795 C THR A 520 7748 6997 8751 -104 469 25 C ATOM 2796 O THR A 520 115.412 72.623 15.701 1.00 62.31 O ANISOU 2796 O THR A 520 7789 7088 8798 -98 334 -21 O ATOM 2797 CB THR A 520 116.117 70.612 13.507 1.00 53.45 C ANISOU 2797 CB THR A 520 6760 5935 7615 -94 642 44 C ATOM 2798 OG1 THR A 520 117.439 71.004 13.123 1.00 59.21 O ANISOU 2798 OG1 THR A 520 7393 6556 8549 -88 740 91 O ATOM 2799 CG2 THR A 520 115.613 69.536 12.570 1.00 52.52 C ANISOU 2799 CG2 THR A 520 6766 5853 7338 -89 735 53 C ATOM 2800 N LYS A 521 116.346 73.896 14.085 1.00 65.03 N ANISOU 2800 N LYS A 521 8086 7326 9297 -106 520 64 N ATOM 2801 CA LYS A 521 116.722 74.978 14.984 1.00 66.90 C ANISOU 2801 CA LYS A 521 8228 7518 9674 -107 399 51 C ATOM 2802 C LYS A 521 115.524 75.893 15.197 1.00 61.67 C ANISOU 2802 C LYS A 521 7632 6926 8875 -111 317 30 C ATOM 2803 O LYS A 521 114.823 76.240 14.244 1.00 70.21 O ANISOU 2803 O LYS A 521 8791 8044 9842 -120 396 53 O ATOM 2804 CB LYS A 521 117.904 75.777 14.418 1.00 73.34 C ANISOU 2804 CB LYS A 521 8937 8217 10713 -108 487 108 C ATOM 2805 CG LYS A 521 118.941 74.962 13.642 1.00 79.35 C ANISOU 2805 CG LYS A 521 9658 8903 11587 -100 650 158 C ATOM 2806 CD LYS A 521 119.508 75.725 12.434 1.00 85.94 C ANISOU 2806 CD LYS A 521 10471 9656 12527 -94 824 235 C ATOM 2807 CE LYS A 521 120.787 76.495 12.782 1.00 90.74 C ANISOU 2807 CE LYS A 521 10904 10132 13442 -93 809 274 C ATOM 2808 NZ LYS A 521 121.585 76.892 11.572 1.00 92.41 N ANISOU 2808 NZ LYS A 521 11079 10240 13794 -78 1023 364 N ATOM 2809 N GLU A 522 115.279 76.273 16.448 1.00 58.59 N ANISOU 2809 N GLU A 522 7221 6548 8492 -101 157 -14 N ATOM 2810 CA GLU A 522 114.242 77.247 16.793 1.00 66.39 C ANISOU 2810 CA GLU A 522 8261 7588 9376 -99 75 -32 C ATOM 2811 C GLU A 522 114.910 78.264 17.705 1.00 80.67 C ANISOU 2811 C GLU A 522 9988 9321 11342 -87 -50 -45 C ATOM 2812 O GLU A 522 114.970 78.060 18.922 1.00 67.75 O ANISOU 2812 O GLU A 522 8353 7674 9715 -62 -185 -89 O ATOM 2813 CB GLU A 522 113.023 76.601 17.457 1.00 59.80 C ANISOU 2813 CB GLU A 522 7519 6848 8355 -86 7 -70 C ATOM 2814 CG GLU A 522 111.852 77.565 17.627 1.00 63.33 C ANISOU 2814 CG GLU A 522 8024 7348 8691 -83 -47 -76 C ATOM 2815 CD GLU A 522 110.600 76.917 18.214 1.00 65.23 C ANISOU 2815 CD GLU A 522 8348 7671 8765 -67 -92 -100 C ATOM 2816 OE1 GLU A 522 109.726 76.507 17.417 1.00 59.65 O ANISOU 2816 OE1 GLU A 522 7702 7020 7943 -84 -25 -82 O ATOM 2817 OE2 GLU A 522 110.478 76.843 19.465 1.00 62.64 O ANISOU 2817 OE2 GLU A 522 8031 7342 8427 -33 -195 -133 O ATOM 2818 N GLY A 523 115.410 79.344 17.103 1.00108.20 N ANISOU 2818 N GLY A 523 13415 12747 14951 -100 -8 -7 N ATOM 2819 CA GLY A 523 116.148 80.364 17.819 1.00117.27 C ANISOU 2819 CA GLY A 523 14475 13805 16278 -91 -125 -13 C ATOM 2820 C GLY A 523 117.638 80.132 17.904 1.00122.79 C ANISOU 2820 C GLY A 523 15045 14381 17227 -92 -123 9 C ATOM 2821 O GLY A 523 118.279 80.660 18.819 1.00130.72 O ANISOU 2821 O GLY A 523 15982 15300 18385 -79 -271 -10 O ATOM 2822 N GLY A 524 118.214 79.366 16.975 1.00113.16 N ANISOU 2822 N GLY A 524 13793 13139 16062 -103 38 52 N ATOM 2823 CA GLY A 524 119.602 78.965 17.060 1.00106.02 C ANISOU 2823 CA GLY A 524 12763 12118 15402 -102 55 78 C ATOM 2824 C GLY A 524 119.848 77.723 17.888 1.00 98.97 C ANISOU 2824 C GLY A 524 11876 11231 14496 -90 -21 35 C ATOM 2825 O GLY A 524 120.949 77.157 17.822 1.00 96.66 O ANISOU 2825 O GLY A 524 11486 10849 14391 -91 18 61 O ATOM 2826 N TYR A 525 118.859 77.283 18.663 1.00 95.30 N ANISOU 2826 N TYR A 525 11521 10864 13827 -76 -122 -25 N ATOM 2827 CA TYR A 525 118.946 76.055 19.443 1.00 85.01 C ANISOU 2827 CA TYR A 525 10242 9578 12479 -61 -186 -67 C ATOM 2828 C TYR A 525 118.415 74.891 18.618 1.00 71.18 C ANISOU 2828 C TYR A 525 8564 7917 10565 -71 -33 -55 C ATOM 2829 O TYR A 525 117.302 74.958 18.089 1.00 63.25 O ANISOU 2829 O TYR A 525 7658 7009 9367 -77 25 -54 O ATOM 2830 CB TYR A 525 118.154 76.198 20.741 1.00 80.12 C ANISOU 2830 CB TYR A 525 9711 9004 11726 -31 -364 -132 C ATOM 2831 CG TYR A 525 118.622 77.356 21.584 1.00 86.23 C ANISOU 2831 CG TYR A 525 10440 9683 12640 -14 -532 -149 C ATOM 2832 CD1 TYR A 525 119.622 77.184 22.535 1.00 93.99 C ANISOU 2832 CD1 TYR A 525 11363 10553 13797 6 -681 -175 C ATOM 2833 CD2 TYR A 525 118.081 78.627 21.420 1.00 86.84 C ANISOU 2833 CD2 TYR A 525 10539 9774 12683 -16 -552 -139 C ATOM 2834 CE1 TYR A 525 120.064 78.239 23.310 1.00 99.66 C ANISOU 2834 CE1 TYR A 525 12050 11168 14648 25 -856 -193 C ATOM 2835 CE2 TYR A 525 118.520 79.687 22.184 1.00 92.57 C ANISOU 2835 CE2 TYR A 525 11230 10406 13538 3 -715 -155 C ATOM 2836 CZ TYR A 525 119.509 79.489 23.134 1.00 98.39 C ANISOU 2836 CZ TYR A 525 11914 11025 14445 24 -872 -183 C ATOM 2837 OH TYR A 525 119.952 80.539 23.909 1.00 97.23 O ANISOU 2837 OH TYR A 525 11744 10769 14430 46 -1055 -201 O ATOM 2838 N ASP A 526 119.208 73.826 18.514 1.00 68.97 N ANISOU 2838 N ASP A 526 8237 7599 10370 -72 21 -46 N ATOM 2839 CA ASP A 526 118.889 72.707 17.636 1.00 65.05 C ANISOU 2839 CA ASP A 526 7805 7166 9745 -79 172 -29 C ATOM 2840 C ASP A 526 118.116 71.634 18.400 1.00 61.05 C ANISOU 2840 C ASP A 526 7384 6748 9063 -67 96 -84 C ATOM 2841 O ASP A 526 118.600 71.104 19.410 1.00 62.03 O ANISOU 2841 O ASP A 526 7475 6840 9255 -53 -12 -120 O ATOM 2842 CB ASP A 526 120.158 72.117 17.026 1.00 67.15 C ANISOU 2842 CB ASP A 526 7978 7339 10197 -83 295 18 C ATOM 2843 CG ASP A 526 119.896 71.438 15.703 1.00 67.39 C ANISOU 2843 CG ASP A 526 8086 7410 10109 -86 492 58 C ATOM 2844 OD1 ASP A 526 120.833 71.324 14.880 1.00 68.98 O ANISOU 2844 OD1 ASP A 526 8231 7527 10453 -82 641 117 O ATOM 2845 OD2 ASP A 526 118.739 71.032 15.482 1.00 64.05 O ANISOU 2845 OD2 ASP A 526 7788 7094 9456 -87 497 34 O ATOM 2846 N HIS A 527 116.917 71.316 17.910 1.00 45.90 N ANISOU 2846 N HIS A 527 5576 4933 6929 -72 149 -88 N ATOM 2847 CA HIS A 527 116.092 70.251 18.462 1.00 39.69 C ANISOU 2847 CA HIS A 527 4869 4231 5979 -61 104 -127 C ATOM 2848 C HIS A 527 116.178 68.970 17.641 1.00 38.01 C ANISOU 2848 C HIS A 527 4690 4042 5708 -70 226 -110 C ATOM 2849 O HIS A 527 115.361 68.063 17.844 1.00 41.51 O ANISOU 2849 O HIS A 527 5207 4561 6005 -65 210 -134 O ATOM 2850 CB HIS A 527 114.633 70.709 18.557 1.00 42.64 C ANISOU 2850 CB HIS A 527 5337 4693 6170 -58 65 -140 C ATOM 2851 CG HIS A 527 114.423 71.866 19.479 1.00 58.42 C ANISOU 2851 CG HIS A 527 7326 6675 8198 -41 -60 -161 C ATOM 2852 ND1 HIS A 527 114.905 73.130 19.209 1.00 56.11 N ANISOU 2852 ND1 HIS A 527 6976 6322 8020 -49 -66 -139 N ATOM 2853 CD2 HIS A 527 113.770 71.956 20.662 1.00 60.06 C ANISOU 2853 CD2 HIS A 527 7582 6911 8328 -10 -180 -199 C ATOM 2854 CE1 HIS A 527 114.568 73.944 20.191 1.00 55.92 C ANISOU 2854 CE1 HIS A 527 6968 6292 7987 -26 -194 -167 C ATOM 2855 NE2 HIS A 527 113.878 73.258 21.084 1.00 57.38 N ANISOU 2855 NE2 HIS A 527 7223 6528 8052 1 -261 -203 N ATOM 2856 N ALA A 528 117.152 68.878 16.727 1.00 32.97 N ANISOU 2856 N ALA A 528 4002 3335 5189 -78 352 -66 N ATOM 2857 CA ALA A 528 117.310 67.691 15.888 1.00 36.65 C ANISOU 2857 CA ALA A 528 4513 3812 5601 -78 478 -46 C ATOM 2858 C ALA A 528 117.293 66.405 16.704 1.00 39.05 C ANISOU 2858 C ALA A 528 4822 4150 5863 -71 413 -88 C ATOM 2859 O ALA A 528 116.697 65.410 16.285 1.00 39.51 O ANISOU 2859 O ALA A 528 4964 4267 5780 -71 460 -93 O ATOM 2860 CB ALA A 528 118.614 67.784 15.089 1.00 30.07 C ANISOU 2860 CB ALA A 528 3604 2872 4948 -76 617 9 C ATOM 2861 N ILE A 529 117.953 66.403 17.868 1.00 43.28 N ANISOU 2861 N ILE A 529 5276 4643 6525 -62 298 -119 N ATOM 2862 CA ILE A 529 118.003 65.201 18.701 1.00 39.22 C ANISOU 2862 CA ILE A 529 4769 4153 5977 -51 233 -159 C ATOM 2863 C ILE A 529 116.592 64.739 19.066 1.00 42.03 C ANISOU 2863 C ILE A 529 5234 4619 6118 -43 182 -191 C ATOM 2864 O ILE A 529 116.312 63.535 19.131 1.00 41.42 O ANISOU 2864 O ILE A 529 5198 4587 5955 -40 198 -206 O ATOM 2865 CB ILE A 529 118.868 65.452 19.953 1.00 42.18 C ANISOU 2865 CB ILE A 529 5058 4451 6516 -36 92 -190 C ATOM 2866 CG1 ILE A 529 119.045 64.160 20.745 1.00 48.24 C ANISOU 2866 CG1 ILE A 529 5835 5233 7260 -22 35 -229 C ATOM 2867 CG2 ILE A 529 118.290 66.594 20.841 1.00 42.22 C ANISOU 2867 CG2 ILE A 529 5087 4464 6492 -20 -49 -219 C ATOM 2868 CD1 ILE A 529 120.384 64.047 21.445 1.00 52.45 C ANISOU 2868 CD1 ILE A 529 6263 5655 8013 -15 -44 -240 C ATOM 2869 N SER A 530 115.675 65.692 19.261 1.00 39.36 N ANISOU 2869 N SER A 530 4938 4319 5700 -40 128 -196 N ATOM 2870 CA SER A 530 114.320 65.372 19.697 1.00 41.42 C ANISOU 2870 CA SER A 530 5285 4667 5785 -29 78 -217 C ATOM 2871 C SER A 530 113.521 64.733 18.569 1.00 37.61 C ANISOU 2871 C SER A 530 4875 4242 5172 -47 176 -192 C ATOM 2872 O SER A 530 112.811 63.741 18.782 1.00 38.76 O ANISOU 2872 O SER A 530 5070 4442 5214 -42 164 -205 O ATOM 2873 CB SER A 530 113.634 66.652 20.173 1.00 39.67 C ANISOU 2873 CB SER A 530 5082 4457 5535 -18 2 -222 C ATOM 2874 OG SER A 530 114.171 67.087 21.411 1.00 40.00 O ANISOU 2874 OG SER A 530 5089 4447 5661 11 -118 -254 O ATOM 2875 N PHE A 531 113.621 65.310 17.367 1.00 40.59 N ANISOU 2875 N PHE A 531 5266 4599 5558 -66 268 -155 N ATOM 2876 CA PHE A 531 113.037 64.716 16.171 1.00 38.57 C ANISOU 2876 CA PHE A 531 5097 4373 5187 -78 357 -130 C ATOM 2877 C PHE A 531 113.559 63.307 15.936 1.00 44.96 C ANISOU 2877 C PHE A 531 5916 5175 5993 -75 413 -134 C ATOM 2878 O PHE A 531 112.794 62.409 15.560 1.00 36.75 O ANISOU 2878 O PHE A 531 4953 4180 4831 -77 421 -136 O ATOM 2879 CB PHE A 531 113.346 65.585 14.953 1.00 35.78 C ANISOU 2879 CB PHE A 531 4762 3972 4860 -87 457 -89 C ATOM 2880 CG PHE A 531 112.539 66.840 14.886 1.00 34.24 C ANISOU 2880 CG PHE A 531 4587 3798 4624 -94 413 -82 C ATOM 2881 CD1 PHE A 531 111.208 66.798 14.492 1.00 26.06 C ANISOU 2881 CD1 PHE A 531 3641 2817 3442 -101 387 -80 C ATOM 2882 CD2 PHE A 531 113.109 68.065 15.209 1.00 34.84 C ANISOU 2882 CD2 PHE A 531 4588 3829 4818 -93 392 -76 C ATOM 2883 CE1 PHE A 531 110.457 67.968 14.410 1.00 32.04 C ANISOU 2883 CE1 PHE A 531 4415 3590 4169 -108 349 -71 C ATOM 2884 CE2 PHE A 531 112.368 69.246 15.136 1.00 32.23 C ANISOU 2884 CE2 PHE A 531 4278 3518 4449 -100 354 -69 C ATOM 2885 CZ PHE A 531 111.036 69.198 14.733 1.00 28.75 C ANISOU 2885 CZ PHE A 531 3929 3137 3857 -107 337 -67 C ATOM 2886 N GLN A 532 114.865 63.101 16.126 1.00 40.47 N ANISOU 2886 N GLN A 532 5268 4544 5567 -70 449 -131 N ATOM 2887 CA GLN A 532 115.414 61.763 15.966 1.00 40.20 C ANISOU 2887 CA GLN A 532 5237 4499 5537 -65 502 -134 C ATOM 2888 C GLN A 532 114.794 60.810 16.976 1.00 38.09 C ANISOU 2888 C GLN A 532 4983 4295 5192 -59 404 -176 C ATOM 2889 O GLN A 532 114.463 59.667 16.639 1.00 32.84 O ANISOU 2889 O GLN A 532 4375 3662 4439 -59 434 -179 O ATOM 2890 CB GLN A 532 116.941 61.791 16.093 1.00 44.28 C ANISOU 2890 CB GLN A 532 5648 4927 6250 -61 550 -120 C ATOM 2891 CG GLN A 532 117.641 62.506 14.917 1.00 66.38 C ANISOU 2891 CG GLN A 532 8436 7649 9134 -60 690 -63 C ATOM 2892 CD GLN A 532 119.120 62.844 15.177 1.00 83.29 C ANISOU 2892 CD GLN A 532 10442 9686 11519 -57 722 -39 C ATOM 2893 OE1 GLN A 532 119.463 63.981 15.513 1.00 87.19 O ANISOU 2893 OE1 GLN A 532 10859 10133 12136 -61 676 -31 O ATOM 2894 NE2 GLN A 532 119.996 61.858 14.999 1.00 85.46 N ANISOU 2894 NE2 GLN A 532 10684 9915 11873 -49 800 -25 N ATOM 2895 N ASP A 533 114.602 61.276 18.211 1.00 30.32 N ANISOU 2895 N ASP A 533 3959 3323 4236 -48 289 -207 N ATOM 2896 CA ASP A 533 113.950 60.456 19.229 1.00 36.52 C ANISOU 2896 CA ASP A 533 4769 4162 4944 -31 205 -242 C ATOM 2897 C ASP A 533 112.558 60.026 18.770 1.00 36.41 C ANISOU 2897 C ASP A 533 4841 4218 4774 -37 215 -231 C ATOM 2898 O ASP A 533 112.223 58.837 18.813 1.00 33.73 O ANISOU 2898 O ASP A 533 4533 3912 4371 -35 219 -239 O ATOM 2899 CB ASP A 533 113.886 61.238 20.552 1.00 39.08 C ANISOU 2899 CB ASP A 533 5066 4475 5307 -7 87 -270 C ATOM 2900 CG ASP A 533 113.236 60.448 21.698 1.00 44.83 C ANISOU 2900 CG ASP A 533 5832 5246 5955 23 11 -302 C ATOM 2901 OD1 ASP A 533 112.325 60.992 22.359 1.00 55.22 O ANISOU 2901 OD1 ASP A 533 7188 6589 7204 46 -46 -307 O ATOM 2902 OD2 ASP A 533 113.641 59.303 21.959 1.00 54.44 O ANISOU 2902 OD2 ASP A 533 7042 6464 7179 28 16 -318 O ATOM 2903 N TRP A 534 111.739 60.985 18.301 1.00 34.60 N ANISOU 2903 N TRP A 534 4647 4005 4493 -46 214 -211 N ATOM 2904 CA TRP A 534 110.369 60.664 17.895 1.00 31.32 C ANISOU 2904 CA TRP A 534 4304 3642 3953 -52 204 -197 C ATOM 2905 C TRP A 534 110.361 59.737 16.696 1.00 32.08 C ANISOU 2905 C TRP A 534 4461 3734 3992 -67 275 -180 C ATOM 2906 O TRP A 534 109.546 58.810 16.623 1.00 32.28 O ANISOU 2906 O TRP A 534 4532 3793 3940 -68 252 -180 O ATOM 2907 CB TRP A 534 109.579 61.934 17.579 1.00 29.59 C ANISOU 2907 CB TRP A 534 4108 3431 3706 -59 187 -177 C ATOM 2908 CG TRP A 534 109.569 62.894 18.720 1.00 34.05 C ANISOU 2908 CG TRP A 534 4628 3993 4317 -39 118 -193 C ATOM 2909 CD1 TRP A 534 109.536 62.587 20.053 1.00 30.48 C ANISOU 2909 CD1 TRP A 534 4158 3551 3874 -7 51 -219 C ATOM 2910 CD2 TRP A 534 109.626 64.319 18.636 1.00 34.36 C ANISOU 2910 CD2 TRP A 534 4650 4011 4395 -42 105 -183 C ATOM 2911 NE1 TRP A 534 109.570 63.735 20.803 1.00 32.42 N ANISOU 2911 NE1 TRP A 534 4386 3777 4155 13 -5 -228 N ATOM 2912 CE2 TRP A 534 109.616 64.814 19.957 1.00 33.51 C ANISOU 2912 CE2 TRP A 534 4518 3899 4316 -11 24 -207 C ATOM 2913 CE3 TRP A 534 109.679 65.226 17.571 1.00 34.91 C ANISOU 2913 CE3 TRP A 534 4733 4060 4473 -64 155 -157 C ATOM 2914 CZ2 TRP A 534 109.657 66.174 20.241 1.00 31.86 C ANISOU 2914 CZ2 TRP A 534 4292 3666 4146 -3 -15 -206 C ATOM 2915 CZ3 TRP A 534 109.731 66.578 17.854 1.00 34.44 C ANISOU 2915 CZ3 TRP A 534 4645 3982 4460 -61 122 -155 C ATOM 2916 CH2 TRP A 534 109.716 67.041 19.180 1.00 32.35 C ANISOU 2916 CH2 TRP A 534 4351 3714 4225 -32 35 -179 C ATOM 2917 N LEU A 535 111.282 59.958 15.757 1.00 29.73 N ANISOU 2917 N LEU A 535 4170 3386 3738 -74 363 -163 N ATOM 2918 CA LEU A 535 111.369 59.087 14.592 1.00 31.95 C ANISOU 2918 CA LEU A 535 4533 3649 3956 -77 439 -145 C ATOM 2919 C LEU A 535 111.703 57.648 14.995 1.00 32.24 C ANISOU 2919 C LEU A 535 4560 3700 3990 -70 438 -165 C ATOM 2920 O LEU A 535 111.147 56.696 14.436 1.00 34.68 O ANISOU 2920 O LEU A 535 4946 4022 4207 -71 440 -162 O ATOM 2921 CB LEU A 535 112.405 59.638 13.618 1.00 32.95 C ANISOU 2921 CB LEU A 535 4669 3707 4142 -73 555 -116 C ATOM 2922 CG LEU A 535 112.475 58.864 12.297 1.00 42.81 C ANISOU 2922 CG LEU A 535 6037 4923 5306 -63 647 -93 C ATOM 2923 CD1 LEU A 535 111.099 58.854 11.605 1.00 32.57 C ANISOU 2923 CD1 LEU A 535 4860 3650 3865 -69 592 -87 C ATOM 2924 CD2 LEU A 535 113.557 59.434 11.406 1.00 37.28 C ANISOU 2924 CD2 LEU A 535 5347 4144 4676 -48 785 -55 C ATOM 2925 N LYS A 536 112.589 57.471 15.980 1.00 32.59 N ANISOU 2925 N LYS A 536 4512 3735 4135 -62 422 -187 N ATOM 2926 CA LYS A 536 112.951 56.121 16.413 1.00 37.93 C ANISOU 2926 CA LYS A 536 5175 4423 4814 -56 419 -208 C ATOM 2927 C LYS A 536 111.772 55.415 17.063 1.00 33.87 C ANISOU 2927 C LYS A 536 4688 3972 4210 -52 335 -225 C ATOM 2928 O LYS A 536 111.559 54.218 16.835 1.00 30.74 O ANISOU 2928 O LYS A 536 4330 3592 3759 -53 343 -229 O ATOM 2929 CB LYS A 536 114.139 56.159 17.378 1.00 35.37 C ANISOU 2929 CB LYS A 536 4748 4063 4627 -47 402 -229 C ATOM 2930 CG LYS A 536 115.461 56.535 16.721 1.00 54.73 C ANISOU 2930 CG LYS A 536 7154 6437 7203 -49 501 -204 C ATOM 2931 CD LYS A 536 116.623 55.802 17.384 1.00 67.46 C ANISOU 2931 CD LYS A 536 8684 8010 8937 -42 499 -221 C ATOM 2932 CE LYS A 536 116.573 55.931 18.905 1.00 75.09 C ANISOU 2932 CE LYS A 536 9594 8991 9945 -31 363 -264 C ATOM 2933 NZ LYS A 536 116.820 54.618 19.585 1.00 75.26 N ANISOU 2933 NZ LYS A 536 9606 9028 9961 -22 330 -294 N ATOM 2934 N LYS A 537 110.981 56.155 17.820 1.00 32.57 N ANISOU 2934 N LYS A 537 4505 3836 4036 -46 260 -231 N ATOM 2935 CA LYS A 537 109.776 55.589 18.455 1.00 26.00 C ANISOU 2935 CA LYS A 537 3693 3053 3133 -37 198 -234 C ATOM 2936 C LYS A 537 108.801 55.138 17.370 1.00 29.07 C ANISOU 2936 C LYS A 537 4158 3453 3436 -54 204 -208 C ATOM 2937 O LYS A 537 108.316 54.061 17.474 1.00 32.72 O ANISOU 2937 O LYS A 537 4640 3935 3856 -52 181 -208 O ATOM 2938 CB LYS A 537 109.148 56.604 19.407 1.00 29.44 C ANISOU 2938 CB LYS A 537 4105 3504 3577 -19 136 -235 C ATOM 2939 CG LYS A 537 109.977 56.949 20.626 1.00 29.84 C ANISOU 2939 CG LYS A 537 4101 3531 3705 5 102 -265 C ATOM 2940 CD LYS A 537 109.456 58.118 21.354 1.00 37.80 C ANISOU 2940 CD LYS A 537 5108 4541 4715 27 49 -264 C ATOM 2941 CE LYS A 537 108.993 57.785 22.744 1.00 47.78 C ANISOU 2941 CE LYS A 537 6386 5823 5944 70 -2 -277 C ATOM 2942 NZ LYS A 537 110.106 57.833 23.708 1.00 58.91 N ANISOU 2942 NZ LYS A 537 7778 7194 7412 104 -56 -313 N ATOM 2943 N LEU A 538 108.570 55.964 16.363 1.00 29.84 N ANISOU 2943 N LEU A 538 4302 3529 3509 -68 227 -186 N ATOM 2944 CA LEU A 538 107.634 55.619 15.272 1.00 32.80 C ANISOU 2944 CA LEU A 538 4766 3896 3802 -81 215 -163 C ATOM 2945 C LEU A 538 108.190 54.441 14.473 1.00 36.25 C ANISOU 2945 C LEU A 538 5266 4309 4200 -81 261 -166 C ATOM 2946 O LEU A 538 107.438 53.552 14.186 1.00 36.77 O ANISOU 2946 O LEU A 538 5386 4377 4208 -84 219 -161 O ATOM 2947 CB LEU A 538 107.372 56.836 14.382 1.00 29.23 C ANISOU 2947 CB LEU A 538 4364 3415 3327 -91 231 -141 C ATOM 2948 CG LEU A 538 106.607 57.993 15.017 1.00 37.28 C ANISOU 2948 CG LEU A 538 5339 4455 4370 -94 180 -133 C ATOM 2949 CD1 LEU A 538 106.581 59.193 14.107 1.00 40.92 C ANISOU 2949 CD1 LEU A 538 5847 4884 4818 -104 211 -114 C ATOM 2950 CD2 LEU A 538 105.211 57.601 15.412 1.00 28.24 C ANISOU 2950 CD2 LEU A 538 4195 3336 3199 -95 100 -118 C ATOM 2951 N HIS A 539 109.485 54.439 14.208 1.00 31.19 N ANISOU 2951 N HIS A 539 4616 3634 3599 -74 349 -171 N ATOM 2952 CA HIS A 539 110.088 53.355 13.445 1.00 31.74 C ANISOU 2952 CA HIS A 539 4751 3673 3634 -66 412 -170 C ATOM 2953 C HIS A 539 110.027 52.044 14.214 1.00 36.27 C ANISOU 2953 C HIS A 539 5289 4283 4210 -64 372 -192 C ATOM 2954 O HIS A 539 109.731 50.991 13.642 1.00 32.94 O ANISOU 2954 O HIS A 539 4941 3852 3720 -62 365 -191 O ATOM 2955 CB HIS A 539 111.537 53.696 13.101 1.00 36.75 C ANISOU 2955 CB HIS A 539 5362 4258 4342 -56 527 -162 C ATOM 2956 CG HIS A 539 112.247 52.608 12.366 1.00 44.00 C ANISOU 2956 CG HIS A 539 6346 5138 5232 -40 611 -156 C ATOM 2957 ND1 HIS A 539 112.141 52.438 11.003 1.00 50.99 N ANISOU 2957 ND1 HIS A 539 7377 5972 6024 -24 672 -131 N ATOM 2958 CD2 HIS A 539 113.048 51.609 12.808 1.00 55.23 C ANISOU 2958 CD2 HIS A 539 7721 6561 6703 -34 642 -171 C ATOM 2959 CE1 HIS A 539 112.858 51.391 10.633 1.00 54.65 C ANISOU 2959 CE1 HIS A 539 7882 6406 6477 -6 744 -129 C ATOM 2960 NE2 HIS A 539 113.421 50.870 11.710 1.00 53.70 N ANISOU 2960 NE2 HIS A 539 7639 6319 6447 -15 729 -153 N ATOM 2961 N SER A 540 110.302 52.085 15.512 1.00 38.57 N ANISOU 2961 N SER A 540 5475 4606 4573 -60 340 -214 N ATOM 2962 CA SER A 540 110.276 50.845 16.267 1.00 38.35 C ANISOU 2962 CA SER A 540 5418 4608 4545 -54 308 -235 C ATOM 2963 C SER A 540 108.857 50.295 16.347 1.00 33.19 C ANISOU 2963 C SER A 540 4797 3985 3827 -57 230 -225 C ATOM 2964 O SER A 540 108.654 49.084 16.220 1.00 40.54 O ANISOU 2964 O SER A 540 5757 4923 4725 -57 216 -228 O ATOM 2965 CB SER A 540 110.872 51.064 17.657 1.00 38.02 C ANISOU 2965 CB SER A 540 5277 4581 4587 -41 283 -261 C ATOM 2966 OG SER A 540 110.430 50.067 18.559 1.00 45.68 O ANISOU 2966 OG SER A 540 6228 5587 5541 -29 233 -277 O ATOM 2967 N ARG A 541 107.855 51.167 16.528 1.00 35.01 N ANISOU 2967 N ARG A 541 5023 4229 4052 -61 179 -208 N ATOM 2968 CA ARG A 541 106.469 50.699 16.569 1.00 31.97 C ANISOU 2968 CA ARG A 541 4655 3857 3635 -64 107 -187 C ATOM 2969 C ARG A 541 106.053 50.098 15.233 1.00 37.94 C ANISOU 2969 C ARG A 541 5512 4577 4325 -78 90 -172 C ATOM 2970 O ARG A 541 105.446 49.023 15.188 1.00 31.93 O ANISOU 2970 O ARG A 541 4769 3815 3547 -79 41 -167 O ATOM 2971 CB ARG A 541 105.514 51.836 16.941 1.00 25.48 C ANISOU 2971 CB ARG A 541 3806 3044 2832 -64 66 -165 C ATOM 2972 CG ARG A 541 104.020 51.429 16.836 1.00 24.98 C ANISOU 2972 CG ARG A 541 3753 2976 2761 -69 -6 -132 C ATOM 2973 CD ARG A 541 103.672 50.386 17.939 1.00 32.39 C ANISOU 2973 CD ARG A 541 4634 3942 3732 -49 -22 -131 C ATOM 2974 NE ARG A 541 104.123 50.854 19.255 1.00 35.68 N ANISOU 2974 NE ARG A 541 4991 4386 4182 -19 7 -148 N ATOM 2975 CZ ARG A 541 103.311 51.213 20.246 1.00 36.24 C ANISOU 2975 CZ ARG A 541 5021 4466 4283 8 -6 -125 C ATOM 2976 NH1 ARG A 541 101.993 51.142 20.087 1.00 30.66 N ANISOU 2976 NH1 ARG A 541 4305 3744 3598 5 -42 -79 N ATOM 2977 NH2 ARG A 541 103.813 51.654 21.396 1.00 33.57 N ANISOU 2977 NH2 ARG A 541 4657 4141 3958 44 15 -145 N ATOM 2978 N VAL A 542 106.358 50.799 14.134 1.00 40.54 N ANISOU 2978 N VAL A 542 5919 4868 4618 -83 125 -164 N ATOM 2979 CA VAL A 542 105.940 50.369 12.805 1.00 33.45 C ANISOU 2979 CA VAL A 542 5150 3919 3641 -87 100 -151 C ATOM 2980 C VAL A 542 106.637 49.072 12.419 1.00 34.03 C ANISOU 2980 C VAL A 542 5279 3976 3677 -76 137 -165 C ATOM 2981 O VAL A 542 106.046 48.198 11.775 1.00 34.91 O ANISOU 2981 O VAL A 542 5476 4055 3733 -75 77 -159 O ATOM 2982 CB VAL A 542 106.227 51.487 11.787 1.00 33.95 C ANISOU 2982 CB VAL A 542 5294 3939 3667 -85 146 -138 C ATOM 2983 CG1 VAL A 542 106.085 50.956 10.377 1.00 33.65 C ANISOU 2983 CG1 VAL A 542 5421 3833 3530 -74 137 -129 C ATOM 2984 CG2 VAL A 542 105.285 52.656 12.009 1.00 27.58 C ANISOU 2984 CG2 VAL A 542 4451 3143 2885 -98 87 -121 C ATOM 2985 N THR A 543 107.905 48.928 12.804 1.00 27.95 N ANISOU 2985 N THR A 543 4459 3217 2943 -66 229 -183 N ATOM 2986 CA THR A 543 108.624 47.688 12.548 1.00 32.77 C ANISOU 2986 CA THR A 543 5109 3814 3530 -54 274 -196 C ATOM 2987 C THR A 543 107.984 46.510 13.284 1.00 35.97 C ANISOU 2987 C THR A 543 5470 4256 3943 -59 195 -206 C ATOM 2988 O THR A 543 107.831 45.420 12.713 1.00 33.91 O ANISOU 2988 O THR A 543 5287 3971 3628 -54 172 -207 O ATOM 2989 CB THR A 543 110.095 47.856 12.946 1.00 38.00 C ANISOU 2989 CB THR A 543 5701 4476 4263 -45 383 -208 C ATOM 2990 OG1 THR A 543 110.725 48.773 12.040 1.00 42.82 O ANISOU 2990 OG1 THR A 543 6368 5034 4868 -35 473 -188 O ATOM 2991 CG2 THR A 543 110.839 46.517 12.891 1.00 40.23 C ANISOU 2991 CG2 THR A 543 5999 4749 4537 -34 428 -221 C ATOM 2992 N LYS A 544 107.582 46.710 14.546 1.00 33.60 N ANISOU 2992 N LYS A 544 5053 4006 3708 -64 154 -212 N ATOM 2993 CA LYS A 544 106.997 45.601 15.302 1.00 32.75 C ANISOU 2993 CA LYS A 544 4900 3928 3616 -63 95 -216 C ATOM 2994 C LYS A 544 105.594 45.263 14.821 1.00 33.87 C ANISOU 2994 C LYS A 544 5088 4048 3734 -73 -3 -188 C ATOM 2995 O LYS A 544 105.202 44.093 14.845 1.00 38.55 O ANISOU 2995 O LYS A 544 5690 4636 4320 -72 -50 -186 O ATOM 2996 CB LYS A 544 106.981 45.914 16.801 1.00 24.71 C ANISOU 2996 CB LYS A 544 3765 2957 2666 -53 92 -225 C ATOM 2997 CG LYS A 544 108.384 45.909 17.411 1.00 34.17 C ANISOU 2997 CG LYS A 544 4913 4165 3904 -42 159 -257 C ATOM 2998 CD LYS A 544 108.369 46.081 18.922 1.00 37.67 C ANISOU 2998 CD LYS A 544 5269 4642 4400 -23 138 -271 C ATOM 2999 CE LYS A 544 108.062 47.519 19.336 1.00 35.14 C ANISOU 2999 CE LYS A 544 4922 4323 4105 -16 126 -261 C ATOM 3000 NZ LYS A 544 108.114 47.691 20.827 1.00 37.04 N ANISOU 3000 NZ LYS A 544 5106 4583 4384 15 105 -277 N ATOM 3001 N GLU A 545 104.833 46.253 14.360 1.00 33.45 N ANISOU 3001 N GLU A 545 5061 3972 3676 -82 -43 -165 N ATOM 3002 CA GLU A 545 103.460 46.034 13.932 1.00 32.88 C ANISOU 3002 CA GLU A 545 5021 3865 3608 -92 -152 -134 C ATOM 3003 C GLU A 545 103.319 45.961 12.411 1.00 38.02 C ANISOU 3003 C GLU A 545 5825 4444 4177 -96 -194 -130 C ATOM 3004 O GLU A 545 102.207 46.114 11.888 1.00 35.16 O ANISOU 3004 O GLU A 545 5503 4035 3822 -106 -297 -104 O ATOM 3005 CB GLU A 545 102.559 47.123 14.517 1.00 35.19 C ANISOU 3005 CB GLU A 545 5238 4170 3962 -97 -182 -107 C ATOM 3006 CG GLU A 545 101.984 46.770 15.899 1.00 42.04 C ANISOU 3006 CG GLU A 545 5986 5077 4911 -85 -191 -91 C ATOM 3007 CD GLU A 545 101.056 45.534 15.880 1.00 48.19 C ANISOU 3007 CD GLU A 545 6754 5829 5729 -88 -270 -66 C ATOM 3008 OE1 GLU A 545 99.826 45.691 16.063 1.00 47.87 O ANISOU 3008 OE1 GLU A 545 6666 5762 5762 -91 -333 -21 O ATOM 3009 OE2 GLU A 545 101.552 44.401 15.698 1.00 48.36 O ANISOU 3009 OE2 GLU A 545 6806 5850 5719 -87 -268 -86 O ATOM 3010 N ARG A 546 104.412 45.676 11.696 1.00 32.57 N ANISOU 3010 N ARG A 546 5228 3734 3415 -82 -118 -151 N ATOM 3011 CA ARG A 546 104.396 45.814 10.243 1.00 35.85 C ANISOU 3011 CA ARG A 546 5816 4071 3734 -71 -135 -146 C ATOM 3012 C ARG A 546 103.350 44.912 9.590 1.00 36.27 C ANISOU 3012 C ARG A 546 5961 4063 3758 -73 -276 -135 C ATOM 3013 O ARG A 546 102.698 45.319 8.617 1.00 29.58 O ANISOU 3013 O ARG A 546 5232 3143 2862 -71 -357 -121 O ATOM 3014 CB ARG A 546 105.787 45.541 9.671 1.00 41.06 C ANISOU 3014 CB ARG A 546 6559 4713 4329 -46 -7 -163 C ATOM 3015 CG ARG A 546 106.349 44.146 9.916 1.00 51.07 C ANISOU 3015 CG ARG A 546 7822 5993 5590 -36 17 -181 C ATOM 3016 CD ARG A 546 107.692 44.007 9.201 1.00 61.07 C ANISOU 3016 CD ARG A 546 9183 7224 6798 -6 156 -188 C ATOM 3017 NE ARG A 546 108.396 42.763 9.497 1.00 60.46 N ANISOU 3017 NE ARG A 546 9088 7161 6723 4 200 -205 N ATOM 3018 CZ ARG A 546 109.069 42.528 10.618 1.00 63.87 C ANISOU 3018 CZ ARG A 546 9371 7657 7242 -7 252 -221 C ATOM 3019 NH1 ARG A 546 109.128 43.446 11.571 1.00 60.05 N ANISOU 3019 NH1 ARG A 546 8749 7223 6845 -24 264 -223 N ATOM 3020 NH2 ARG A 546 109.686 41.367 10.786 1.00 71.59 N ANISOU 3020 NH2 ARG A 546 10346 8641 8216 3 287 -236 N ATOM 3021 N HIS A 547 103.147 43.697 10.120 1.00 30.94 N ANISOU 3021 N HIS A 547 5234 3405 3118 -76 -319 -139 N ATOM 3022 CA HIS A 547 102.211 42.779 9.469 1.00 35.99 C ANISOU 3022 CA HIS A 547 5960 3973 3742 -78 -464 -127 C ATOM 3023 C HIS A 547 100.777 43.300 9.547 1.00 36.76 C ANISOU 3023 C HIS A 547 6007 4037 3922 -99 -598 -92 C ATOM 3024 O HIS A 547 100.085 43.385 8.526 1.00 38.61 O ANISOU 3024 O HIS A 547 6367 4181 4121 -98 -716 -81 O ATOM 3025 CB HIS A 547 102.326 41.380 10.076 1.00 42.34 C ANISOU 3025 CB HIS A 547 6705 4803 4578 -77 -477 -137 C ATOM 3026 CG HIS A 547 103.500 40.603 9.562 1.00 48.97 C ANISOU 3026 CG HIS A 547 7650 5634 5322 -52 -392 -166 C ATOM 3027 ND1 HIS A 547 104.622 40.354 10.324 1.00 52.72 N ANISOU 3027 ND1 HIS A 547 8040 6180 5813 -47 -260 -188 N ATOM 3028 CD2 HIS A 547 103.735 40.038 8.355 1.00 53.46 C ANISOU 3028 CD2 HIS A 547 8411 6122 5778 -27 -418 -175 C ATOM 3029 CE1 HIS A 547 105.493 39.660 9.612 1.00 51.75 C ANISOU 3029 CE1 HIS A 547 8036 6023 5603 -22 -201 -205 C ATOM 3030 NE2 HIS A 547 104.978 39.453 8.414 1.00 53.81 N ANISOU 3030 NE2 HIS A 547 8474 6194 5778 -6 -289 -197 N ATOM 3031 N ARG A 548 100.318 43.677 10.747 1.00 31.64 N ANISOU 3031 N ARG A 548 5183 3452 3388 -115 -581 -73 N ATOM 3032 CA ARG A 548 98.988 44.265 10.862 1.00 32.69 C ANISOU 3032 CA ARG A 548 5254 3549 3616 -132 -686 -31 C ATOM 3033 C ARG A 548 98.896 45.570 10.075 1.00 36.68 C ANISOU 3033 C ARG A 548 5844 4021 4072 -135 -692 -29 C ATOM 3034 O ARG A 548 97.856 45.865 9.474 1.00 31.22 O ANISOU 3034 O ARG A 548 5194 3254 3414 -146 -820 -2 O ATOM 3035 CB ARG A 548 98.637 44.484 12.341 1.00 35.52 C ANISOU 3035 CB ARG A 548 5423 3978 4093 -135 -632 -8 C ATOM 3036 CG ARG A 548 97.596 43.470 12.908 1.00 34.82 C ANISOU 3036 CG ARG A 548 5240 3865 4127 -139 -718 31 C ATOM 3037 CD ARG A 548 97.324 43.671 14.408 1.00 28.14 C ANISOU 3037 CD ARG A 548 4228 3082 3383 -127 -638 58 C ATOM 3038 NE ARG A 548 98.499 43.341 15.203 1.00 26.08 N ANISOU 3038 NE ARG A 548 3939 2902 3067 -109 -516 18 N ATOM 3039 CZ ARG A 548 98.746 42.124 15.684 1.00 32.05 C ANISOU 3039 CZ ARG A 548 4665 3676 3837 -99 -504 10 C ATOM 3040 NH1 ARG A 548 97.885 41.132 15.465 1.00 34.85 N ANISOU 3040 NH1 ARG A 548 5006 3976 4262 -107 -602 41 N ATOM 3041 NH2 ARG A 548 99.860 41.886 16.363 1.00 29.01 N ANISOU 3041 NH2 ARG A 548 4263 3358 3403 -83 -401 -30 N ATOM 3042 N LEU A 549 99.981 46.349 10.039 1.00 31.74 N ANISOU 3042 N LEU A 549 5244 3441 3375 -125 -561 -55 N ATOM 3043 CA LEU A 549 99.925 47.649 9.389 1.00 37.53 C ANISOU 3043 CA LEU A 549 6044 4149 4069 -126 -554 -50 C ATOM 3044 C LEU A 549 99.915 47.523 7.871 1.00 42.56 C ANISOU 3044 C LEU A 549 6893 4686 4591 -111 -619 -57 C ATOM 3045 O LEU A 549 99.337 48.382 7.186 1.00 31.50 O ANISOU 3045 O LEU A 549 5566 3231 3173 -115 -684 -43 O ATOM 3046 CB LEU A 549 101.094 48.522 9.858 1.00 37.67 C ANISOU 3046 CB LEU A 549 6012 4236 4065 -118 -395 -70 C ATOM 3047 CG LEU A 549 100.918 49.188 11.236 1.00 31.01 C ANISOU 3047 CG LEU A 549 4991 3469 3322 -127 -352 -59 C ATOM 3048 CD1 LEU A 549 102.241 49.745 11.711 1.00 27.03 C ANISOU 3048 CD1 LEU A 549 4447 3021 2803 -117 -214 -86 C ATOM 3049 CD2 LEU A 549 99.889 50.291 11.144 1.00 28.01 C ANISOU 3049 CD2 LEU A 549 4588 3067 2986 -141 -417 -29 C ATOM 3050 N SER A 550 100.520 46.454 7.334 1.00 28.98 N ANISOU 3050 N SER A 550 5286 2936 2791 -89 -607 -78 N ATOM 3051 CA SER A 550 100.565 46.275 5.885 1.00 34.91 C ANISOU 3051 CA SER A 550 6270 3579 3413 -61 -663 -85 C ATOM 3052 C SER A 550 99.185 46.041 5.280 1.00 37.09 C ANISOU 3052 C SER A 550 6619 3756 3717 -71 -876 -65 C ATOM 3053 O SER A 550 99.031 46.195 4.063 1.00 39.72 O ANISOU 3053 O SER A 550 7159 3986 3946 -46 -949 -70 O ATOM 3054 CB SER A 550 101.510 45.122 5.526 1.00 29.12 C ANISOU 3054 CB SER A 550 5641 2833 2591 -29 -597 -109 C ATOM 3055 OG SER A 550 101.224 43.956 6.283 1.00 40.22 O ANISOU 3055 OG SER A 550 6939 4272 4071 -45 -652 -111 O ATOM 3056 N ARG A 551 98.183 45.694 6.104 1.00 36.79 N ANISOU 3056 N ARG A 551 6418 3735 3824 -103 -977 -40 N ATOM 3057 CA ARG A 551 96.813 45.483 5.636 1.00 35.41 C ANISOU 3057 CA ARG A 551 6276 3456 3722 -118 -1190 -13 C ATOM 3058 C ARG A 551 96.093 46.785 5.288 1.00 34.80 C ANISOU 3058 C ARG A 551 6207 3339 3675 -131 -1250 9 C ATOM 3059 O ARG A 551 95.046 46.740 4.635 1.00 37.62 O ANISOU 3059 O ARG A 551 6633 3586 4074 -139 -1437 29 O ATOM 3060 CB ARG A 551 95.989 44.736 6.704 1.00 40.08 C ANISOU 3060 CB ARG A 551 6666 4073 4488 -144 -1254 19 C ATOM 3061 CG ARG A 551 96.500 43.353 7.105 1.00 48.99 C ANISOU 3061 CG ARG A 551 7772 5233 5609 -135 -1222 3 C ATOM 3062 CD ARG A 551 95.807 42.809 8.385 1.00 44.51 C ANISOU 3062 CD ARG A 551 6981 4712 5220 -156 -1234 39 C ATOM 3063 NE ARG A 551 94.431 43.280 8.457 1.00 37.94 N ANISOU 3063 NE ARG A 551 6063 3814 4539 -179 -1365 92 N ATOM 3064 CZ ARG A 551 93.693 43.361 9.563 1.00 38.36 C ANISOU 3064 CZ ARG A 551 5914 3899 4761 -192 -1347 140 C ATOM 3065 NH1 ARG A 551 94.167 42.979 10.748 1.00 27.69 N ANISOU 3065 NH1 ARG A 551 4431 2647 3441 -184 -1210 139 N ATOM 3066 NH2 ARG A 551 92.458 43.841 9.475 1.00 36.93 N ANISOU 3066 NH2 ARG A 551 5669 3641 4722 -210 -1465 193 N ATOM 3067 N PHE A 552 96.607 47.939 5.726 1.00 41.22 N ANISOU 3067 N PHE A 552 6948 4235 4478 -135 -1106 7 N ATOM 3068 CA PHE A 552 95.934 49.224 5.554 1.00 38.02 C ANISOU 3068 CA PHE A 552 6525 3807 4112 -151 -1149 29 C ATOM 3069 C PHE A 552 96.787 50.147 4.694 1.00 35.91 C ANISOU 3069 C PHE A 552 6416 3530 3696 -126 -1053 4 C ATOM 3070 O PHE A 552 98.022 50.112 4.764 1.00 40.06 O ANISOU 3070 O PHE A 552 6970 4113 4138 -105 -891 -21 O ATOM 3071 CB PHE A 552 95.657 49.922 6.906 1.00 35.55 C ANISOU 3071 CB PHE A 552 5978 3594 3935 -176 -1068 55 C ATOM 3072 CG PHE A 552 94.855 49.088 7.891 1.00 40.01 C ANISOU 3072 CG PHE A 552 6374 4173 4657 -191 -1124 88 C ATOM 3073 CD1 PHE A 552 95.454 48.052 8.605 1.00 30.26 C ANISOU 3073 CD1 PHE A 552 5074 2999 3425 -182 -1048 74 C ATOM 3074 CD2 PHE A 552 93.509 49.359 8.117 1.00 37.48 C ANISOU 3074 CD2 PHE A 552 5954 3799 4489 -213 -1243 139 C ATOM 3075 CE1 PHE A 552 94.717 47.289 9.513 1.00 31.59 C ANISOU 3075 CE1 PHE A 552 5091 3173 3737 -191 -1088 109 C ATOM 3076 CE2 PHE A 552 92.768 48.615 9.029 1.00 35.45 C ANISOU 3076 CE2 PHE A 552 5535 3543 4390 -221 -1275 181 C ATOM 3077 CZ PHE A 552 93.374 47.575 9.732 1.00 35.33 C ANISOU 3077 CZ PHE A 552 5466 3591 4369 -209 -1195 166 C ATOM 3078 N SER A 553 96.121 50.996 3.896 1.00 36.29 N ANISOU 3078 N SER A 553 6563 3499 3725 -128 -1152 16 N ATOM 3079 CA SER A 553 96.848 51.962 3.072 1.00 36.89 C ANISOU 3079 CA SER A 553 6791 3559 3667 -101 -1058 0 C ATOM 3080 C SER A 553 97.720 52.872 3.929 1.00 36.31 C ANISOU 3080 C SER A 553 6572 3607 3617 -109 -861 -3 C ATOM 3081 O SER A 553 98.907 53.065 3.638 1.00 40.52 O ANISOU 3081 O SER A 553 7178 4163 4054 -81 -708 -22 O ATOM 3082 CB SER A 553 95.881 52.797 2.222 1.00 40.83 C ANISOU 3082 CB SER A 553 7397 3958 4159 -106 -1205 16 C ATOM 3083 OG SER A 553 94.868 51.996 1.631 1.00 60.36 O ANISOU 3083 OG SER A 553 9963 6310 6659 -107 -1426 24 O ATOM 3084 N SER A 554 97.148 53.447 4.991 1.00 35.84 N ANISOU 3084 N SER A 554 6309 3618 3692 -143 -863 18 N ATOM 3085 CA SER A 554 97.943 54.302 5.873 1.00 32.06 C ANISOU 3085 CA SER A 554 5696 3245 3240 -148 -698 13 C ATOM 3086 C SER A 554 99.144 53.549 6.432 1.00 35.00 C ANISOU 3086 C SER A 554 6024 3684 3589 -133 -563 -12 C ATOM 3087 O SER A 554 100.234 54.119 6.570 1.00 36.15 O ANISOU 3087 O SER A 554 6157 3876 3703 -121 -417 -26 O ATOM 3088 CB SER A 554 97.085 54.835 7.019 1.00 37.87 C ANISOU 3088 CB SER A 554 6232 4036 4120 -177 -728 41 C ATOM 3089 OG SER A 554 96.634 53.774 7.843 1.00 36.67 O ANISOU 3089 OG SER A 554 5969 3904 4060 -185 -773 53 O ATOM 3090 N GLY A 555 98.960 52.268 6.768 1.00 35.06 N ANISOU 3090 N GLY A 555 6002 3693 3627 -134 -613 -15 N ATOM 3091 CA GLY A 555 100.074 51.480 7.268 1.00 30.89 C ANISOU 3091 CA GLY A 555 5437 3221 3078 -119 -495 -38 C ATOM 3092 C GLY A 555 101.148 51.260 6.218 1.00 34.37 C ANISOU 3092 C GLY A 555 6055 3616 3388 -85 -408 -58 C ATOM 3093 O GLY A 555 102.339 51.463 6.479 1.00 40.50 O ANISOU 3093 O GLY A 555 6799 4437 4151 -72 -257 -71 O ATOM 3094 N LYS A 556 100.738 50.844 5.015 1.00 36.77 N ANISOU 3094 N LYS A 556 6553 3817 3599 -65 -505 -58 N ATOM 3095 CA LYS A 556 101.686 50.698 3.914 1.00 41.64 C ANISOU 3095 CA LYS A 556 7373 4371 4077 -19 -414 -69 C ATOM 3096 C LYS A 556 102.428 52.003 3.649 1.00 40.06 C ANISOU 3096 C LYS A 556 7190 4182 3848 -6 -273 -63 C ATOM 3097 O LYS A 556 103.643 51.997 3.419 1.00 46.79 O ANISOU 3097 O LYS A 556 8086 5036 4655 25 -111 -67 O ATOM 3098 CB LYS A 556 100.963 50.230 2.652 1.00 51.60 C ANISOU 3098 CB LYS A 556 8866 5505 5236 7 -564 -69 C ATOM 3099 CG LYS A 556 101.908 49.931 1.492 1.00 66.67 C ANISOU 3099 CG LYS A 556 11015 7333 6983 69 -465 -77 C ATOM 3100 CD LYS A 556 101.187 49.570 0.182 1.00 78.03 C ANISOU 3100 CD LYS A 556 12723 8626 8299 106 -626 -79 C ATOM 3101 CE LYS A 556 99.901 48.758 0.370 1.00 87.27 C ANISOU 3101 CE LYS A 556 13857 9758 9544 74 -863 -80 C ATOM 3102 NZ LYS A 556 100.008 47.635 1.356 1.00 91.20 N ANISOU 3102 NZ LYS A 556 14187 10331 10134 48 -860 -86 N ATOM 3103 N LYS A 557 101.720 53.134 3.703 1.00 38.41 N ANISOU 3103 N LYS A 557 6937 3977 3679 -29 -329 -49 N ATOM 3104 CA LYS A 557 102.369 54.425 3.494 1.00 43.33 C ANISOU 3104 CA LYS A 557 7564 4611 4287 -19 -203 -41 C ATOM 3105 C LYS A 557 103.453 54.670 4.538 1.00 47.49 C ANISOU 3105 C LYS A 557 7911 5233 4899 -29 -48 -47 C ATOM 3106 O LYS A 557 104.563 55.112 4.208 1.00 42.16 O ANISOU 3106 O LYS A 557 7272 4547 4200 -3 105 -42 O ATOM 3107 CB LYS A 557 101.326 55.538 3.527 1.00 49.67 C ANISOU 3107 CB LYS A 557 8327 5411 5134 -48 -304 -27 C ATOM 3108 CG LYS A 557 101.906 56.927 3.438 1.00 61.72 C ANISOU 3108 CG LYS A 557 9834 6956 6661 -44 -186 -18 C ATOM 3109 CD LYS A 557 100.822 57.942 3.118 1.00 70.58 C ANISOU 3109 CD LYS A 557 10979 8047 7793 -63 -300 -4 C ATOM 3110 CE LYS A 557 100.790 58.261 1.641 1.00 76.70 C ANISOU 3110 CE LYS A 557 12003 8708 8431 -24 -315 1 C ATOM 3111 NZ LYS A 557 101.858 59.222 1.263 1.00 82.72 N ANISOU 3111 NZ LYS A 557 12807 9470 9152 4 -136 10 N ATOM 3112 N MET A 558 103.155 54.381 5.808 1.00 41.01 N ANISOU 3112 N MET A 558 6900 4495 4186 -62 -86 -54 N ATOM 3113 CA MET A 558 104.163 54.578 6.847 1.00 42.96 C ANISOU 3113 CA MET A 558 6988 4821 4515 -67 36 -63 C ATOM 3114 C MET A 558 105.357 53.666 6.621 1.00 39.92 C ANISOU 3114 C MET A 558 6650 4422 4097 -39 149 -74 C ATOM 3115 O MET A 558 106.510 54.106 6.713 1.00 41.12 O ANISOU 3115 O MET A 558 6763 4581 4279 -26 287 -72 O ATOM 3116 CB MET A 558 103.571 54.341 8.239 1.00 40.78 C ANISOU 3116 CB MET A 558 6530 4622 4343 -96 -31 -68 C ATOM 3117 CG MET A 558 102.415 55.257 8.581 1.00 36.40 C ANISOU 3117 CG MET A 558 5912 4081 3838 -120 -123 -50 C ATOM 3118 SD MET A 558 102.264 55.530 10.354 1.00 41.63 S ANISOU 3118 SD MET A 558 6359 4836 4621 -134 -115 -52 S ATOM 3119 CE MET A 558 101.680 53.944 10.931 1.00 31.32 C ANISOU 3119 CE MET A 558 5011 3542 3347 -135 -187 -51 C ATOM 3120 N ILE A 559 105.100 52.386 6.330 1.00 39.90 N ANISOU 3120 N ILE A 559 6725 4392 4044 -30 89 -82 N ATOM 3121 CA ILE A 559 106.194 51.442 6.116 1.00 41.88 C ANISOU 3121 CA ILE A 559 7024 4627 4261 -1 196 -91 C ATOM 3122 C ILE A 559 107.081 51.911 4.970 1.00 38.21 C ANISOU 3122 C ILE A 559 6715 4086 3718 43 331 -74 C ATOM 3123 O ILE A 559 108.313 51.886 5.068 1.00 43.56 O ANISOU 3123 O ILE A 559 7356 4765 4432 62 483 -68 O ATOM 3124 CB ILE A 559 105.645 50.023 5.871 1.00 49.22 C ANISOU 3124 CB ILE A 559 8035 5529 5138 5 93 -102 C ATOM 3125 CG1 ILE A 559 105.040 49.458 7.157 1.00 42.80 C ANISOU 3125 CG1 ILE A 559 7044 4795 4425 -32 5 -112 C ATOM 3126 CG2 ILE A 559 106.750 49.082 5.329 1.00 43.68 C ANISOU 3126 CG2 ILE A 559 7438 4789 4371 45 208 -107 C ATOM 3127 CD1 ILE A 559 104.126 48.267 6.924 1.00 39.02 C ANISOU 3127 CD1 ILE A 559 6627 4280 3918 -35 -135 -114 C ATOM 3128 N GLU A 560 106.470 52.404 3.893 1.00 50.34 N ANISOU 3128 N GLU A 560 8423 5547 5157 62 281 -61 N ATOM 3129 CA GLU A 560 107.233 52.802 2.717 1.00 55.84 C ANISOU 3129 CA GLU A 560 9300 6156 5761 116 415 -40 C ATOM 3130 C GLU A 560 107.956 54.124 2.934 1.00 58.42 C ANISOU 3130 C GLU A 560 9527 6503 6165 112 547 -20 C ATOM 3131 O GLU A 560 109.081 54.304 2.452 1.00 64.27 O ANISOU 3131 O GLU A 560 10318 7197 6903 152 722 3 O ATOM 3132 CB GLU A 560 106.316 52.877 1.499 1.00 58.08 C ANISOU 3132 CB GLU A 560 9821 6341 5907 144 304 -35 C ATOM 3133 CG GLU A 560 106.389 51.625 0.640 1.00 74.99 C ANISOU 3133 CG GLU A 560 12174 8398 7921 193 283 -41 C ATOM 3134 CD GLU A 560 105.091 51.313 -0.083 1.00 85.06 C ANISOU 3134 CD GLU A 560 13621 9595 9103 197 71 -51 C ATOM 3135 OE1 GLU A 560 104.238 52.220 -0.206 1.00 89.89 O ANISOU 3135 OE1 GLU A 560 14230 10196 9728 174 -31 -46 O ATOM 3136 OE2 GLU A 560 104.929 50.157 -0.533 1.00 84.07 O ANISOU 3136 OE2 GLU A 560 13633 9411 8898 225 0 -63 O ATOM 3137 N THR A 561 107.334 55.060 3.652 1.00 55.20 N ANISOU 3137 N THR A 561 8979 6159 5838 67 470 -25 N ATOM 3138 CA THR A 561 108.043 56.284 4.008 1.00 49.92 C ANISOU 3138 CA THR A 561 8194 5514 5261 60 581 -9 C ATOM 3139 C THR A 561 109.296 55.972 4.811 1.00 46.20 C ANISOU 3139 C THR A 561 7570 5080 4903 59 703 -11 C ATOM 3140 O THR A 561 110.358 56.560 4.579 1.00 55.55 O ANISOU 3140 O THR A 561 8735 6229 6141 81 854 14 O ATOM 3141 CB THR A 561 107.137 57.215 4.804 1.00 49.98 C ANISOU 3141 CB THR A 561 8067 5588 5337 12 467 -18 C ATOM 3142 OG1 THR A 561 105.922 57.440 4.085 1.00 49.66 O ANISOU 3142 OG1 THR A 561 8155 5505 5208 10 338 -15 O ATOM 3143 CG2 THR A 561 107.841 58.543 5.059 1.00 45.17 C ANISOU 3143 CG2 THR A 561 7359 4991 4813 8 569 -2 C ATOM 3144 N LEU A 562 109.198 55.035 5.750 1.00 38.64 N ANISOU 3144 N LEU A 562 6505 4185 3994 35 638 -37 N ATOM 3145 CA LEU A 562 110.350 54.725 6.587 1.00 47.28 C ANISOU 3145 CA LEU A 562 7451 5310 5203 32 731 -42 C ATOM 3146 C LEU A 562 111.474 54.091 5.775 1.00 53.04 C ANISOU 3146 C LEU A 562 8281 5966 5907 78 887 -20 C ATOM 3147 O LEU A 562 112.637 54.481 5.918 1.00 54.15 O ANISOU 3147 O LEU A 562 8339 6083 6152 90 1022 1 O ATOM 3148 CB LEU A 562 109.930 53.823 7.753 1.00 41.92 C ANISOU 3148 CB LEU A 562 6653 4708 4567 2 624 -75 C ATOM 3149 CG LEU A 562 109.215 54.594 8.873 1.00 41.58 C ANISOU 3149 CG LEU A 562 6465 4736 4596 -34 521 -88 C ATOM 3150 CD1 LEU A 562 108.451 53.672 9.793 1.00 29.23 C ANISOU 3150 CD1 LEU A 562 4834 3231 3041 -53 408 -111 C ATOM 3151 CD2 LEU A 562 110.205 55.455 9.671 1.00 32.12 C ANISOU 3151 CD2 LEU A 562 5121 3556 3528 -40 593 -88 C ATOM 3152 N ALA A 563 111.149 53.122 4.910 1.00 52.71 N ANISOU 3152 N ALA A 563 8418 5876 5734 108 871 -21 N ATOM 3153 CA ALA A 563 112.194 52.436 4.148 1.00 52.11 C ANISOU 3153 CA ALA A 563 8452 5724 5624 161 1028 3 C ATOM 3154 C ALA A 563 112.908 53.395 3.202 1.00 58.54 C ANISOU 3154 C ALA A 563 9359 6452 6432 206 1195 50 C ATOM 3155 O ALA A 563 114.139 53.361 3.094 1.00 61.80 O ANISOU 3155 O ALA A 563 9735 6820 6928 235 1369 82 O ATOM 3156 CB ALA A 563 111.611 51.252 3.373 1.00 38.15 C ANISOU 3156 CB ALA A 563 6883 3912 3700 190 961 -9 C ATOM 3157 N ASN A 564 112.153 54.265 2.520 1.00 56.81 N ANISOU 3157 N ASN A 564 9256 6201 6127 213 1147 58 N ATOM 3158 CA ASN A 564 112.757 55.282 1.665 1.00 65.21 C ANISOU 3158 CA ASN A 564 10405 7185 7188 256 1304 105 C ATOM 3159 C ASN A 564 113.763 56.126 2.430 1.00 74.86 C ANISOU 3159 C ASN A 564 11404 8432 8607 234 1414 126 C ATOM 3160 O ASN A 564 114.827 56.472 1.903 1.00 79.41 O ANISOU 3160 O ASN A 564 12000 8929 9242 278 1606 176 O ATOM 3161 CB ASN A 564 111.678 56.198 1.081 1.00 68.53 C ANISOU 3161 CB ASN A 564 10942 7589 7510 252 1201 103 C ATOM 3162 CG ASN A 564 110.804 55.502 0.060 1.00 74.06 C ANISOU 3162 CG ASN A 564 11902 8221 8014 289 1104 91 C ATOM 3163 OD1 ASN A 564 111.098 54.384 -0.374 1.00 71.01 O ANISOU 3163 OD1 ASN A 564 11641 7789 7550 329 1140 91 O ATOM 3164 ND2 ASN A 564 109.713 56.164 -0.328 1.00 72.54 N ANISOU 3164 ND2 ASN A 564 11797 8017 7746 277 970 82 N ATOM 3165 N LEU A 565 113.441 56.467 3.677 1.00 75.00 N ANISOU 3165 N LEU A 565 11213 8547 8735 171 1292 93 N ATOM 3166 CA LEU A 565 114.180 57.507 4.380 1.00 71.27 C ANISOU 3166 CA LEU A 565 10548 8090 8440 149 1351 109 C ATOM 3167 C LEU A 565 115.601 57.063 4.706 1.00 79.83 C ANISOU 3167 C LEU A 565 11519 9138 9674 165 1494 133 C ATOM 3168 O LEU A 565 116.568 57.754 4.363 1.00 74.45 O ANISOU 3168 O LEU A 565 10800 8385 9102 190 1649 182 O ATOM 3169 CB LEU A 565 113.435 57.903 5.650 1.00 66.18 C ANISOU 3169 CB LEU A 565 9738 7550 7857 88 1176 65 C ATOM 3170 CG LEU A 565 114.137 58.976 6.473 1.00 69.81 C ANISOU 3170 CG LEU A 565 10006 8022 8496 65 1204 74 C ATOM 3171 CD1 LEU A 565 114.017 60.328 5.783 1.00 74.28 C ANISOU 3171 CD1 LEU A 565 10622 8546 9055 75 1255 107 C ATOM 3172 CD2 LEU A 565 113.545 59.020 7.860 1.00 66.96 C ANISOU 3172 CD2 LEU A 565 9497 7757 8187 18 1041 28 C ATOM 3173 N ARG A 566 115.753 55.918 5.372 1.00 86.86 N ANISOU 3173 N ARG A 566 12347 10071 10585 150 1445 103 N ATOM 3174 CA ARG A 566 117.071 55.501 5.832 1.00 96.01 C ANISOU 3174 CA ARG A 566 13373 11198 11907 158 1556 121 C ATOM 3175 C ARG A 566 117.854 54.727 4.780 1.00 94.08 C ANISOU 3175 C ARG A 566 13268 10857 11620 220 1739 166 C ATOM 3176 O ARG A 566 119.010 54.371 5.030 1.00 92.61 O ANISOU 3176 O ARG A 566 12978 10627 11581 232 1854 192 O ATOM 3177 CB ARG A 566 116.961 54.682 7.124 1.00103.18 C ANISOU 3177 CB ARG A 566 14141 12191 12870 116 1423 69 C ATOM 3178 CG ARG A 566 116.683 55.539 8.369 1.00107.70 C ANISOU 3178 CG ARG A 566 14538 12832 13550 68 1290 37 C ATOM 3179 CD ARG A 566 117.843 56.498 8.691 1.00107.89 C ANISOU 3179 CD ARG A 566 14412 12800 13783 68 1376 70 C ATOM 3180 NE ARG A 566 117.418 57.618 9.536 1.00105.52 N ANISOU 3180 NE ARG A 566 14003 12545 13543 34 1256 47 N ATOM 3181 CZ ARG A 566 118.242 58.404 10.228 1.00101.88 C ANISOU 3181 CZ ARG A 566 13383 12053 13273 22 1256 56 C ATOM 3182 NH1 ARG A 566 119.552 58.211 10.182 1.00105.27 N ANISOU 3182 NH1 ARG A 566 13726 12400 13872 38 1371 91 N ATOM 3183 NH2 ARG A 566 117.754 59.391 10.967 1.00 95.86 N ANISOU 3183 NH2 ARG A 566 12549 11331 12541 -3 1138 33 N ATOM 3184 N SER A 567 117.260 54.464 3.614 1.00 92.17 N ANISOU 3184 N SER A 567 13265 10572 11184 264 1766 177 N ATOM 3185 CA SER A 567 118.044 54.065 2.453 1.00 96.69 C ANISOU 3185 CA SER A 567 14002 11027 11709 340 1974 233 C ATOM 3186 C SER A 567 118.676 55.261 1.754 1.00100.48 C ANISOU 3186 C SER A 567 14504 11415 12260 379 2148 300 C ATOM 3187 O SER A 567 119.512 55.071 0.864 1.00104.89 O ANISOU 3187 O SER A 567 15173 11862 12819 450 2359 361 O ATOM 3188 CB SER A 567 117.179 53.277 1.462 1.00 92.56 C ANISOU 3188 CB SER A 567 13755 10476 10939 382 1925 218 C ATOM 3189 OG SER A 567 116.523 54.139 0.547 1.00 89.45 O ANISOU 3189 OG SER A 567 13533 10034 10418 410 1921 234 O ATOM 3190 N THR A 568 118.286 56.482 2.130 1.00 96.72 N ANISOU 3190 N THR A 568 13928 10978 11843 339 2072 292 N ATOM 3191 CA THR A 568 118.965 57.701 1.711 1.00 98.71 C ANISOU 3191 CA THR A 568 14142 11153 12211 364 2225 354 C ATOM 3192 C THR A 568 119.736 58.364 2.845 1.00 95.39 C ANISOU 3192 C THR A 568 13434 10757 12054 315 2212 359 C ATOM 3193 O THR A 568 120.571 59.236 2.578 1.00 95.03 O ANISOU 3193 O THR A 568 13317 10629 12159 337 2360 420 O ATOM 3194 CB THR A 568 117.956 58.703 1.126 1.00 98.39 C ANISOU 3194 CB THR A 568 14231 11119 12034 365 2154 348 C ATOM 3195 OG1 THR A 568 116.939 57.989 0.415 1.00 99.12 O ANISOU 3195 OG1 THR A 568 14564 11215 11884 388 2064 317 O ATOM 3196 CG2 THR A 568 118.647 59.666 0.160 1.00 98.62 C ANISOU 3196 CG2 THR A 568 14335 11030 12107 425 2369 426 C ATOM 3197 N HIS A 569 119.482 57.974 4.093 1.00 93.80 N ANISOU 3197 N HIS A 569 13071 10655 11913 253 2038 298 N ATOM 3198 CA HIS A 569 120.248 58.442 5.245 1.00 93.58 C ANISOU 3198 CA HIS A 569 12786 10639 12129 211 2001 295 C ATOM 3199 C HIS A 569 120.582 57.273 6.172 1.00 88.05 C ANISOU 3199 C HIS A 569 11982 9984 11490 187 1929 256 C ATOM 3200 O HIS A 569 121.223 56.303 5.762 1.00 84.06 O ANISOU 3200 O HIS A 569 11525 9426 10988 222 2047 281 O ATOM 3201 CB HIS A 569 119.479 59.521 6.016 1.00 94.91 C ANISOU 3201 CB HIS A 569 12861 10886 12313 159 1829 255 C ATOM 3202 CG HIS A 569 118.823 60.540 5.137 1.00 97.03 C ANISOU 3202 CG HIS A 569 13258 11137 12472 175 1856 277 C ATOM 3203 ND1 HIS A 569 117.659 60.287 4.443 1.00 97.71 N ANISOU 3203 ND1 HIS A 569 13546 11255 12324 185 1793 254 N ATOM 3204 CD2 HIS A 569 119.165 61.817 4.843 1.00 98.57 C ANISOU 3204 CD2 HIS A 569 13409 11277 12765 182 1931 320 C ATOM 3205 CE1 HIS A 569 117.315 61.361 3.756 1.00 97.64 C ANISOU 3205 CE1 HIS A 569 13617 11215 12267 199 1828 280 C ATOM 3206 NE2 HIS A 569 118.212 62.304 3.982 1.00 98.96 N ANISOU 3206 NE2 HIS A 569 13638 11332 12629 198 1918 321 N TER 3207 HIS A 569 ATOM 3208 O5' U B 1 91.307 55.665 0.317 1.00 53.96 O ANISOU 3208 O5' U B 1 9738 4342 6422 1302 -3667 -638 O ATOM 3209 C5' U B 1 90.143 54.968 0.736 1.00 50.54 C ANISOU 3209 C5' U B 1 9363 3799 6041 1180 -3786 -662 C ATOM 3210 C4' U B 1 89.795 55.259 2.174 1.00 51.91 C ANISOU 3210 C4' U B 1 9464 3968 6292 1022 -3769 -584 C ATOM 3211 O4' U B 1 90.773 54.653 3.058 1.00 51.22 O ANISOU 3211 O4' U B 1 9365 3885 6209 1048 -3772 -547 O ATOM 3212 C3' U B 1 89.780 56.722 2.586 1.00 52.82 C ANISOU 3212 C3' U B 1 9455 4180 6435 953 -3631 -508 C ATOM 3213 O3' U B 1 88.575 57.361 2.227 1.00 58.09 O ANISOU 3213 O3' U B 1 10112 4831 7127 863 -3632 -520 O ATOM 3214 C2' U B 1 89.980 56.641 4.094 1.00 52.33 C ANISOU 3214 C2' U B 1 9333 4118 6432 843 -3622 -434 C ATOM 3215 O2' U B 1 88.754 56.342 4.741 1.00 51.06 O ANISOU 3215 O2' U B 1 9192 3875 6335 683 -3710 -438 O ATOM 3216 C1' U B 1 90.922 55.433 4.219 1.00 44.16 C ANISOU 3216 C1' U B 1 8363 3049 5366 945 -3686 -457 C ATOM 3217 N1 U B 1 92.334 55.861 4.311 1.00 46.76 N ANISOU 3217 N1 U B 1 8626 3483 5656 1055 -3578 -411 N ATOM 3218 C2 U B 1 92.822 56.203 5.552 1.00 43.45 C ANISOU 3218 C2 U B 1 8120 3114 5276 987 -3516 -327 C ATOM 3219 O2 U B 1 92.157 56.148 6.563 1.00 51.03 O ANISOU 3219 O2 U B 1 9057 4032 6300 843 -3548 -291 O ATOM 3220 N3 U B 1 94.127 56.610 5.573 1.00 43.41 N ANISOU 3220 N3 U B 1 8052 3214 5227 1092 -3418 -286 N ATOM 3221 C4 U B 1 94.982 56.722 4.498 1.00 51.83 C ANISOU 3221 C4 U B 1 9133 4341 6219 1253 -3375 -323 C ATOM 3222 O4 U B 1 96.135 57.115 4.682 1.00 53.23 O ANISOU 3222 O4 U B 1 9242 4618 6363 1328 -3288 -279 O ATOM 3223 C5 U B 1 94.405 56.349 3.242 1.00 50.59 C ANISOU 3223 C5 U B 1 9070 4125 6027 1314 -3443 -412 C ATOM 3224 C6 U B 1 93.129 55.946 3.191 1.00 48.97 C ANISOU 3224 C6 U B 1 8928 3817 5861 1216 -3538 -451 C ATOM 3225 P G B 2 88.578 58.860 1.649 1.00 57.34 P ANISOU 3225 P G B 2 9930 4842 7015 883 -3492 -485 P ATOM 3226 OP1 G B 2 87.397 58.951 0.752 1.00 61.57 O ANISOU 3226 OP1 G B 2 10517 5329 7549 857 -3544 -541 O ATOM 3227 OP2 G B 2 89.912 59.158 1.076 1.00 52.95 O ANISOU 3227 OP2 G B 2 9348 4380 6391 1043 -3403 -480 O ATOM 3228 O5' G B 2 88.324 59.769 2.941 1.00 55.24 O ANISOU 3228 O5' G B 2 9549 4620 6818 729 -3415 -392 O ATOM 3229 C5' G B 2 87.407 59.355 3.948 1.00 48.14 C ANISOU 3229 C5' G B 2 8657 3644 5990 565 -3497 -380 C ATOM 3230 C4' G B 2 87.375 60.314 5.115 1.00 46.71 C ANISOU 3230 C4' G B 2 8358 3525 5864 437 -3405 -290 C ATOM 3231 O4' G B 2 88.640 60.295 5.820 1.00 51.94 O ANISOU 3231 O4' G B 2 8970 4249 6516 489 -3342 -236 O ATOM 3232 C3' G B 2 87.163 61.778 4.764 1.00 44.50 C ANISOU 3232 C3' G B 2 7989 3338 5582 419 -3278 -249 C ATOM 3233 O3' G B 2 85.799 62.075 4.543 1.00 55.24 O ANISOU 3233 O3' G B 2 9321 4692 6975 324 -3273 -239 O ATOM 3234 C2' G B 2 87.777 62.515 5.954 1.00 46.95 C ANISOU 3234 C2' G B 2 8185 3730 5925 351 -3176 -156 C ATOM 3235 O2' G B 2 86.869 62.618 7.045 1.00 45.06 O ANISOU 3235 O2' G B 2 7903 3458 5759 166 -3205 -121 O ATOM 3236 C1' G B 2 88.923 61.576 6.349 1.00 44.13 C ANISOU 3236 C1' G B 2 7859 3365 5543 440 -3206 -156 C ATOM 3237 N9 G B 2 90.214 62.038 5.809 1.00 43.98 N ANISOU 3237 N9 G B 2 7800 3452 5458 595 -3103 -136 N ATOM 3238 C8 G B 2 90.717 61.843 4.540 1.00 41.07 C ANISOU 3238 C8 G B 2 7486 3101 5018 756 -3102 -192 C ATOM 3239 N7 G B 2 91.888 62.391 4.382 1.00 46.26 N ANISOU 3239 N7 G B 2 8081 3869 5628 860 -2999 -157 N ATOM 3240 C5 G B 2 92.167 62.997 5.615 1.00 43.75 C ANISOU 3240 C5 G B 2 7661 3611 5350 764 -2926 -70 C ATOM 3241 C6 G B 2 93.288 63.751 6.058 1.00 51.24 C ANISOU 3241 C6 G B 2 8507 4687 6274 806 -2806 1 C ATOM 3242 O6 G B 2 94.308 64.059 5.428 1.00 47.19 O ANISOU 3242 O6 G B 2 7968 4264 5697 940 -2737 1 O ATOM 3243 N1 G B 2 93.149 64.165 7.387 1.00 48.47 N ANISOU 3243 N1 G B 2 8076 4359 5982 669 -2769 75 N ATOM 3244 C2 G B 2 92.061 63.894 8.185 1.00 42.16 C ANISOU 3244 C2 G B 2 7294 3470 5257 508 -2839 79 C ATOM 3245 N2 G B 2 92.089 64.375 9.434 1.00 36.14 N ANISOU 3245 N2 G B 2 6445 2746 4542 388 -2790 151 N ATOM 3246 N3 G B 2 91.013 63.193 7.786 1.00 40.18 N ANISOU 3246 N3 G B 2 7135 3100 5029 465 -2953 13 N ATOM 3247 C4 G B 2 91.136 62.787 6.501 1.00 43.39 C ANISOU 3247 C4 G B 2 7621 3485 5379 600 -2988 -57 C ATOM 3248 P U B 3 85.382 63.146 3.421 1.00 57.69 P ANISOU 3248 P U B 3 9622 5044 7256 364 -3212 -260 P ATOM 3249 OP1 U B 3 83.895 63.167 3.358 1.00 52.05 O ANISOU 3249 OP1 U B 3 8848 4346 6581 270 -3185 -219 O ATOM 3250 OP2 U B 3 86.223 63.000 2.212 1.00 50.03 O ANISOU 3250 OP2 U B 3 8717 4086 6207 545 -3211 -320 O ATOM 3251 O5' U B 3 85.891 64.520 4.019 1.00 47.33 O ANISOU 3251 O5' U B 3 8196 3830 5957 320 -3080 -184 O ATOM 3252 C5' U B 3 85.839 65.691 3.233 1.00 42.78 C ANISOU 3252 C5' U B 3 7565 3339 5351 367 -2970 -164 C ATOM 3253 C4' U B 3 84.856 66.663 3.813 1.00 48.34 C ANISOU 3253 C4' U B 3 8190 4065 6113 207 -2925 -115 C ATOM 3254 O4' U B 3 85.217 66.947 5.188 1.00 47.50 O ANISOU 3254 O4' U B 3 8002 3995 6053 102 -2882 -46 O ATOM 3255 C3' U B 3 84.811 68.020 3.134 1.00 55.94 C ANISOU 3255 C3' U B 3 9080 5127 7049 245 -2796 -79 C ATOM 3256 O3' U B 3 83.946 67.985 2.008 1.00 49.74 O ANISOU 3256 O3' U B 3 8355 4301 6244 278 -2840 -136 O ATOM 3257 C2' U B 3 84.349 68.946 4.257 1.00 50.28 C ANISOU 3257 C2' U B 3 8256 4454 6394 79 -2731 -6 C ATOM 3258 O2' U B 3 82.945 68.839 4.431 1.00 60.78 O ANISOU 3258 O2' U B 3 9554 5770 7768 -33 -2746 9 O ATOM 3259 C1' U B 3 85.009 68.307 5.478 1.00 44.02 C ANISOU 3259 C1' U B 3 7451 3644 5631 30 -2762 20 C ATOM 3260 N1 U B 3 86.318 68.904 5.853 1.00 39.77 N ANISOU 3260 N1 U B 3 6833 3214 5064 100 -2640 84 N ATOM 3261 C2 U B 3 86.348 69.797 6.921 1.00 45.67 C ANISOU 3261 C2 U B 3 7471 4029 5853 -19 -2555 159 C ATOM 3262 O2 U B 3 85.356 70.144 7.542 1.00 45.43 O ANISOU 3262 O2 U B 3 7403 3978 5880 -178 -2575 174 O ATOM 3263 N3 U B 3 87.588 70.308 7.235 1.00 45.59 N ANISOU 3263 N3 U B 3 7389 4122 5809 53 -2447 216 N ATOM 3264 C4 U B 3 88.789 70.010 6.623 1.00 45.21 C ANISOU 3264 C4 U B 3 7364 4123 5693 226 -2419 206 C ATOM 3265 O4 U B 3 89.817 70.538 7.045 1.00 40.41 O ANISOU 3265 O4 U B 3 6678 3616 5060 267 -2323 263 O ATOM 3266 C5 U B 3 88.690 69.069 5.541 1.00 44.07 C ANISOU 3266 C5 U B 3 7332 3903 5510 338 -2514 124 C ATOM 3267 C6 U B 3 87.490 68.563 5.213 1.00 41.22 C ANISOU 3267 C6 U B 3 7046 3436 5180 273 -2617 68 C ATOM 3268 P A B 4 84.005 69.108 0.871 1.00 49.87 P ANISOU 3268 P A B 4 8329 4409 6209 375 -2727 -122 P ATOM 3269 OP1 A B 4 83.165 68.647 -0.258 1.00 51.35 O ANISOU 3269 OP1 A B 4 8608 4527 6374 419 -2810 -198 O ATOM 3270 OP2 A B 4 85.405 69.516 0.611 1.00 59.65 O ANISOU 3270 OP2 A B 4 9522 5752 7389 511 -2623 -93 O ATOM 3271 O5' A B 4 83.265 70.320 1.570 1.00 55.03 O ANISOU 3271 O5' A B 4 8877 5115 6916 225 -2644 -51 O ATOM 3272 C5' A B 4 83.145 71.572 0.934 1.00 44.65 C ANISOU 3272 C5' A B 4 7494 3892 5577 258 -2526 -13 C ATOM 3273 C4' A B 4 82.526 72.554 1.881 1.00 45.42 C ANISOU 3273 C4' A B 4 7491 4032 5734 97 -2461 56 C ATOM 3274 O4' A B 4 83.386 72.763 3.027 1.00 48.80 O ANISOU 3274 O4' A B 4 7847 4512 6182 54 -2402 115 O ATOM 3275 C3' A B 4 82.297 73.943 1.339 1.00 45.94 C ANISOU 3275 C3' A B 4 7477 4195 5781 113 -2332 104 C ATOM 3276 O3' A B 4 81.130 73.975 0.557 1.00 54.30 O ANISOU 3276 O3' A B 4 8580 5208 6845 92 -2382 65 O ATOM 3277 C2' A B 4 82.189 74.773 2.607 1.00 50.53 C ANISOU 3277 C2' A B 4 7949 4832 6417 -36 -2260 178 C ATOM 3278 O2' A B 4 80.895 74.633 3.172 1.00 49.97 O ANISOU 3278 O2' A B 4 7877 4702 6409 -205 -2345 164 O ATOM 3279 C1' A B 4 83.196 74.067 3.525 1.00 48.43 C ANISOU 3279 C1' A B 4 7686 4555 6159 -33 -2285 187 C ATOM 3280 N9 A B 4 84.499 74.745 3.555 1.00 45.65 N ANISOU 3280 N9 A B 4 7265 4316 5763 67 -2156 242 N ATOM 3281 C8 A B 4 85.617 74.431 2.820 1.00 45.97 C ANISOU 3281 C8 A B 4 7339 4394 5735 241 -2134 224 C ATOM 3282 N7 A B 4 86.627 75.232 3.061 1.00 50.56 N ANISOU 3282 N7 A B 4 7834 5090 6288 290 -2011 286 N ATOM 3283 C5 A B 4 86.141 76.117 4.015 1.00 45.61 C ANISOU 3283 C5 A B 4 7117 4498 5715 142 -1946 348 C ATOM 3284 C6 A B 4 86.730 77.195 4.694 1.00 47.93 C ANISOU 3284 C6 A B 4 7299 4903 6010 108 -1814 426 C ATOM 3285 N6 A B 4 87.991 77.579 4.491 1.00 40.56 N ANISOU 3285 N6 A B 4 6320 4072 5018 230 -1721 460 N ATOM 3286 N1 A B 4 85.975 77.868 5.594 1.00 43.43 N ANISOU 3286 N1 A B 4 6660 4340 5502 -59 -1784 464 N ATOM 3287 C2 A B 4 84.714 77.470 5.788 1.00 38.67 C ANISOU 3287 C2 A B 4 6094 3646 4954 -184 -1885 427 C ATOM 3288 N3 A B 4 84.046 76.475 5.216 1.00 39.54 N ANISOU 3288 N3 A B 4 6306 3651 5068 -168 -2014 357 N ATOM 3289 C4 A B 4 84.828 75.830 4.331 1.00 43.72 C ANISOU 3289 C4 A B 4 6908 4168 5536 1 -2035 320 C ATOM 3290 P A B 5 81.134 74.615 -0.905 1.00 51.56 P ANISOU 3290 P A B 5 8240 4916 6433 232 -2313 55 P ATOM 3291 OP1 A B 5 80.318 73.701 -1.747 1.00 61.40 O ANISOU 3291 OP1 A B 5 9598 6062 7671 260 -2440 -28 O ATOM 3292 OP2 A B 5 82.509 74.986 -1.308 1.00 57.41 O ANISOU 3292 OP2 A B 5 8947 5754 7111 380 -2212 80 O ATOM 3293 O5' A B 5 80.282 75.935 -0.696 1.00 58.50 O ANISOU 3293 O5' A B 5 9023 5857 7346 126 -2220 118 O ATOM 3294 C5' A B 5 80.886 77.214 -0.592 1.00 52.50 C ANISOU 3294 C5' A B 5 8157 5221 6569 151 -2062 195 C ATOM 3295 C4' A B 5 79.819 78.282 -0.545 1.00 46.73 C ANISOU 3295 C4' A B 5 7359 4525 5872 48 -2003 237 C ATOM 3296 O4' A B 5 80.215 79.307 0.402 1.00 46.12 O ANISOU 3296 O4' A B 5 7166 4538 5819 -27 -1883 317 O ATOM 3297 C3' A B 5 79.520 79.003 -1.863 1.00 43.63 C ANISOU 3297 C3' A B 5 6965 4181 5431 153 -1935 240 C ATOM 3298 O3' A B 5 78.135 79.343 -1.914 1.00 51.11 O ANISOU 3298 O3' A B 5 7904 5098 6417 44 -1964 239 O ATOM 3299 C2' A B 5 80.314 80.293 -1.718 1.00 42.43 C ANISOU 3299 C2' A B 5 6704 4158 5258 191 -1765 323 C ATOM 3300 O2' A B 5 79.850 81.373 -2.506 1.00 44.33 O ANISOU 3300 O2' A B 5 6900 4464 5479 226 -1668 359 O ATOM 3301 C1' A B 5 80.165 80.569 -0.223 1.00 40.54 C ANISOU 3301 C1' A B 5 6393 3923 5085 23 -1749 367 C ATOM 3302 N9 A B 5 81.219 81.415 0.339 1.00 40.28 N ANISOU 3302 N9 A B 5 6268 3994 5042 42 -1613 438 N ATOM 3303 C8 A B 5 81.037 82.508 1.148 1.00 37.03 C ANISOU 3303 C8 A B 5 5753 3649 4667 -67 -1510 503 C ATOM 3304 N7 A B 5 82.147 83.106 1.486 1.00 33.78 N ANISOU 3304 N7 A B 5 5278 3324 4233 -17 -1395 556 N ATOM 3305 C5 A B 5 83.122 82.356 0.860 1.00 38.99 C ANISOU 3305 C5 A B 5 5998 3980 4836 134 -1429 525 C ATOM 3306 C6 A B 5 84.514 82.498 0.845 1.00 39.43 C ANISOU 3306 C6 A B 5 6023 4116 4844 245 -1355 555 C ATOM 3307 N6 A B 5 85.134 83.475 1.519 1.00 32.64 N ANISOU 3307 N6 A B 5 5068 3347 3986 217 -1228 626 N ATOM 3308 N1 A B 5 85.220 81.588 0.126 1.00 44.59 N ANISOU 3308 N1 A B 5 6746 4748 5446 378 -1423 503 N ATOM 3309 C2 A B 5 84.561 80.618 -0.538 1.00 39.41 C ANISOU 3309 C2 A B 5 6194 3994 4788 402 -1551 426 C ATOM 3310 N3 A B 5 83.253 80.381 -0.585 1.00 32.89 N ANISOU 3310 N3 A B 5 5409 3085 4004 308 -1630 394 N ATOM 3311 C4 A B 5 82.578 81.302 0.143 1.00 36.95 C ANISOU 3311 C4 A B 5 5844 3626 4568 173 -1563 449 C ATOM 3312 P A B 6 77.075 78.407 -2.681 1.00 47.90 P ANISOU 3312 P A B 6 7606 4584 6011 46 -2108 158 P ATOM 3313 OP1 A B 6 76.350 77.667 -1.619 1.00 52.29 O ANISOU 3313 OP1 A B 6 8179 5056 6632 -119 -2229 133 O ATOM 3314 OP2 A B 6 77.723 77.722 -3.827 1.00 52.36 O ANISOU 3314 OP2 A B 6 8257 5128 6508 222 -2142 101 O ATOM 3315 O5' A B 6 76.059 79.421 -3.350 1.00 48.94 O ANISOU 3315 O5' A B 6 7695 4757 6142 28 -2046 187 O ATOM 3316 C5' A B 6 76.476 80.279 -4.396 1.00 49.43 C ANISOU 3316 C5' A B 6 7728 4906 6146 165 -1929 218 C ATOM 3317 C4' A B 6 75.591 81.488 -4.435 1.00 52.04 C ANISOU 3317 C4' A B 6 7979 5294 6499 95 -1840 276 C ATOM 3318 O4' A B 6 76.015 82.432 -3.419 1.00 47.08 O ANISOU 3318 O4' A B 6 7243 4745 5902 16 -1725 352 O ATOM 3319 C3' A B 6 75.600 82.301 -5.715 1.00 51.72 C ANISOU 3319 C3' A B 6 7924 5326 6403 226 -1746 299 C ATOM 3320 O3' A B 6 74.829 81.713 -6.752 1.00 53.88 O ANISOU 3320 O3' A B 6 8281 5537 6652 277 -1839 236 O ATOM 3321 C2' A B 6 75.090 83.648 -5.231 1.00 52.84 C ANISOU 3321 C2' A B 6 7955 5541 6580 132 -1623 380 C ATOM 3322 O2' A B 6 73.687 83.616 -5.015 1.00 55.85 O ANISOU 3322 O2' A B 6 8341 5870 7010 3 -1693 366 O ATOM 3323 C1' A B 6 75.789 83.746 -3.871 1.00 53.40 C ANISOU 3323 C1' A B 6 7966 5634 6689 42 -1588 415 C ATOM 3324 N9 A B 6 77.095 84.418 -4.007 1.00 49.23 N ANISOU 3324 N9 A B 6 7385 5203 6119 153 -1453 467 N ATOM 3325 C8 A B 6 78.332 83.890 -4.310 1.00 42.27 C ANISOU 3325 C8 A B 6 6536 4337 5188 279 -1457 447 C ATOM 3326 N7 A B 6 79.274 84.798 -4.387 1.00 41.48 N ANISOU 3326 N7 A B 6 6361 4340 5058 351 -1317 509 N ATOM 3327 C5 A B 6 78.603 85.990 -4.122 1.00 43.21 C ANISOU 3327 C5 A B 6 6499 4607 5311 271 -1210 574 C ATOM 3328 C6 A B 6 79.015 87.323 -4.029 1.00 36.89 C ANISOU 3328 C6 A B 6 5600 3909 4506 287 -1040 656 C ATOM 3329 N6 A B 6 80.264 87.740 -4.231 1.00 30.82 N ANISOU 3329 N6 A B 6 4788 3225 3699 391 -944 696 N ATOM 3330 N1 A B 6 78.073 88.250 -3.747 1.00 45.07 N ANISOU 3330 N1 A B 6 6581 4960 5583 190 -970 695 N ATOM 3331 C2 A B 6 76.806 87.867 -3.552 1.00 43.80 C ANISOU 3331 C2 A B 6 6452 4726 5465 77 -1072 656 C ATOM 3332 N3 A B 6 76.301 86.642 -3.597 1.00 46.63 N ANISOU 3332 N3 A B 6 6896 4990 5833 45 -1238 583 N ATOM 3333 C4 A B 6 77.262 85.760 -3.900 1.00 43.52 C ANISOU 3333 C4 A B 6 6563 4576 5398 151 -1294 546 C ATOM 3334 P U B 7 75.243 81.953 -8.284 1.00 50.18 P ANISOU 3334 P U B 7 7839 5125 6103 463 -1792 220 P ATOM 3335 OP1 U B 7 74.361 81.162 -9.164 1.00 56.82 O ANISOU 3335 OP1 U B 7 8777 5884 6929 492 -1913 145 O ATOM 3336 OP2 U B 7 76.716 81.840 -8.426 1.00 55.68 O ANISOU 3336 OP2 U B 7 8531 5876 6750 582 -1744 218 O ATOM 3337 O5' U B 7 74.892 83.488 -8.489 1.00 48.55 O ANISOU 3337 O5' U B 7 7528 5022 5898 453 -1640 309 O ATOM 3338 C5' U B 7 75.330 84.187 -9.632 1.00 46.38 C ANISOU 3338 C5' U B 7 7228 4833 5560 593 -1547 330 C ATOM 3339 C4' U B 7 74.208 85.006 -10.189 1.00 50.78 C ANISOU 3339 C4' U B 7 7753 5416 6125 569 -1502 366 C ATOM 3340 O4' U B 7 74.085 86.251 -9.468 1.00 44.93 O ANISOU 3340 O4' U B 7 6901 4745 5424 487 -1367 461 O ATOM 3341 C3' U B 7 74.353 85.433 -11.631 1.00 58.64 C ANISOU 3341 C3' U B 7 8754 6473 7052 716 -1453 362 C ATOM 3342 O3' U B 7 74.009 84.387 -12.512 1.00 67.82 O ANISOU 3342 O3' U B 7 10025 7566 8178 784 -1583 269 O ATOM 3343 C2' U B 7 73.413 86.627 -11.724 1.00 56.39 C ANISOU 3343 C2' U B 7 8391 6240 6793 661 -1357 438 C ATOM 3344 O2' U B 7 72.076 86.196 -11.927 1.00 64.79 O ANISOU 3344 O2' U B 7 9506 7230 7880 598 -1456 401 O ATOM 3345 C1' U B 7 73.524 87.227 -10.318 1.00 49.00 C ANISOU 3345 C1' U B 7 7373 5323 5922 532 -1280 507 C ATOM 3346 N1 U B 7 74.349 88.450 -10.287 1.00 43.82 N ANISOU 3346 N1 U B 7 6615 4777 5256 576 -1111 593 N ATOM 3347 C2 U B 7 73.634 89.615 -10.438 1.00 45.23 C ANISOU 3347 C2 U B 7 6720 5009 5456 544 -1004 665 C ATOM 3348 O2 U B 7 72.421 89.608 -10.591 1.00 48.68 O ANISOU 3348 O2 U B 7 7176 5407 5913 487 -1049 655 O ATOM 3349 N3 U B 7 74.378 90.767 -10.401 1.00 41.76 N ANISOU 3349 N3 U B 7 6184 4666 5019 576 -847 748 N ATOM 3350 C4 U B 7 75.748 90.851 -10.240 1.00 39.53 C ANISOU 3350 C4 U B 7 5872 4430 4718 630 -797 762 C ATOM 3351 O4 U B 7 76.276 91.971 -10.234 1.00 42.25 O ANISOU 3351 O4 U B 7 6124 4852 5077 633 -668 836 O ATOM 3352 C5 U B 7 76.416 89.586 -10.092 1.00 43.45 C ANISOU 3352 C5 U B 7 6452 4871 5186 667 -915 681 C ATOM 3353 C6 U B 7 75.716 88.444 -10.120 1.00 45.97 C ANISOU 3353 C6 U B 7 6867 5095 5505 641 -1064 602 C ATOM 3354 P A B 8 74.793 84.212 -13.897 1.00 72.03 P ANISOU 3354 P A B 8 10604 8142 8623 966 -1577 216 P ATOM 3355 OP1 A B 8 73.789 83.624 -14.808 1.00 81.10 O ANISOU 3355 OP1 A B 8 11832 9230 9751 995 -1679 152 O ATOM 3356 OP2 A B 8 76.076 83.530 -13.626 1.00 66.94 O ANISOU 3356 OP2 A B 8 9991 7490 7952 1024 -1601 175 O ATOM 3357 O5' A B 8 75.091 85.716 -14.375 1.00 74.36 O ANISOU 3357 O5' A B 8 10796 8562 8896 1016 -1409 301 O TER 3358 A B 8 HETATM 3359 C1 EDO A 601 102.104 95.046 12.997 1.00 34.80 C HETATM 3360 O1 EDO A 601 102.688 96.267 13.451 1.00 41.73 O HETATM 3361 C2 EDO A 601 102.566 93.918 13.909 1.00 40.02 C HETATM 3362 O2 EDO A 601 102.192 94.217 15.261 1.00 37.54 O HETATM 3363 C1 EDO A 602 99.191 96.435 18.076 1.00 49.82 C HETATM 3364 O1 EDO A 602 100.058 97.516 18.416 1.00 50.64 O HETATM 3365 C2 EDO A 602 99.986 95.287 17.462 1.00 56.59 C HETATM 3366 O2 EDO A 602 100.417 95.643 16.144 1.00 62.36 O HETATM 3367 C1 EDO A 603 87.435 108.003 -2.330 1.00 49.94 C HETATM 3368 O1 EDO A 603 86.914 107.687 -1.035 1.00 46.31 O HETATM 3369 C2 EDO A 603 86.854 109.344 -2.733 1.00 55.19 C HETATM 3370 O2 EDO A 603 86.770 110.144 -1.549 1.00 57.80 O HETATM 3371 C1 EDO A 604 101.389 55.924 30.368 1.00 38.79 C HETATM 3372 O1 EDO A 604 102.774 55.963 30.701 1.00 41.36 O HETATM 3373 C2 EDO A 604 100.647 56.827 31.344 1.00 43.59 C HETATM 3374 O2 EDO A 604 101.303 58.099 31.347 1.00 52.63 O HETATM 3375 C1 EDO A 605 86.558 110.521 -10.829 1.00 57.82 C HETATM 3376 O1 EDO A 605 86.392 111.560 -11.795 1.00 59.79 O HETATM 3377 C2 EDO A 605 85.267 110.343 -10.045 1.00 54.30 C HETATM 3378 O2 EDO A 605 85.084 111.446 -9.146 1.00 58.56 O HETATM 3379 C1 EDO A 606 69.204 111.212 -8.844 1.00 62.49 C HETATM 3380 O1 EDO A 606 69.628 111.340 -7.482 1.00 62.19 O HETATM 3381 C2 EDO A 606 68.520 112.504 -9.280 1.00 63.17 C HETATM 3382 O2 EDO A 606 67.362 112.753 -8.471 1.00 62.16 O HETATM 3383 C1 EDO A 607 82.963 112.159 -17.199 1.00 59.14 C HETATM 3384 O1 EDO A 607 82.028 113.222 -17.426 1.00 58.60 O HETATM 3385 C2 EDO A 607 82.239 110.816 -17.127 1.00 53.26 C HETATM 3386 O2 EDO A 607 81.322 110.683 -18.224 1.00 48.53 O HETATM 3387 C1 EDO A 608 110.305 65.547 24.111 1.00 67.43 C HETATM 3388 O1 EDO A 608 109.051 64.859 23.922 1.00 68.66 O HETATM 3389 C2 EDO A 608 111.460 64.561 24.270 1.00 64.17 C HETATM 3390 O2 EDO A 608 112.149 64.375 23.024 1.00 63.94 O HETATM 3391 C1 EDO A 609 80.296 100.942 -9.934 1.00 64.64 C HETATM 3392 O1 EDO A 609 79.066 100.683 -9.235 1.00 53.99 O HETATM 3393 C2 EDO A 609 80.203 100.422 -11.368 1.00 70.19 C HETATM 3394 O2 EDO A 609 81.286 100.954 -12.144 1.00 65.99 O HETATM 3395 C1 EDO A 610 95.756 68.851 7.252 1.00 72.68 C HETATM 3396 O1 EDO A 610 97.035 68.955 6.603 1.00 70.18 O HETATM 3397 C2 EDO A 610 94.819 68.009 6.388 1.00 68.76 C HETATM 3398 O2 EDO A 610 93.559 67.845 7.051 1.00 65.88 O HETATM 3399 C1 EDO A 611 91.714 72.181 5.100 1.00 67.15 C HETATM 3400 O1 EDO A 611 92.258 71.028 5.766 1.00 66.05 O HETATM 3401 C2 EDO A 611 92.656 73.353 5.337 1.00 63.18 C HETATM 3402 O2 EDO A 611 93.972 72.935 4.946 1.00 56.93 O HETATM 3403 C1 EDO A 612 93.160 53.673 8.514 1.00 43.71 C HETATM 3404 O1 EDO A 612 94.565 53.396 8.500 1.00 37.42 O HETATM 3405 C2 EDO A 612 92.420 52.575 9.256 1.00 47.97 C HETATM 3406 O2 EDO A 612 91.082 53.045 9.454 1.00 61.77 O HETATM 3407 C1 EDO B 101 89.388 81.060 2.204 1.00 73.59 C HETATM 3408 O1 EDO B 101 89.203 82.169 3.094 1.00 72.32 O HETATM 3409 C2 EDO B 101 88.325 81.085 1.108 1.00 73.94 C HETATM 3410 O2 EDO B 101 88.351 79.844 0.388 1.00 79.37 O HETATM 3411 O HOH A 701 65.165 107.656 2.663 1.00 49.01 O HETATM 3412 O HOH A 702 96.611 64.432 6.479 1.00 54.15 O HETATM 3413 O HOH A 703 70.659 109.460 -6.385 1.00 39.11 O HETATM 3414 O HOH A 704 61.965 106.838 -19.493 1.00 42.86 O HETATM 3415 O HOH A 705 86.164 79.403 8.020 1.00 33.44 O HETATM 3416 O HOH A 706 59.980 103.951 -16.805 1.00 47.88 O HETATM 3417 O HOH A 707 105.674 82.702 8.123 1.00 55.79 O HETATM 3418 O HOH A 708 78.784 106.141 -20.246 1.00 41.74 O HETATM 3419 O HOH A 709 67.242 112.624 -23.854 1.00 59.62 O HETATM 3420 O HOH A 710 64.412 89.930 -5.947 1.00 43.46 O HETATM 3421 O HOH A 711 92.154 45.563 17.765 1.00 38.76 O HETATM 3422 O HOH A 712 92.008 47.356 24.205 1.00 45.08 O HETATM 3423 O HOH A 713 101.582 98.832 9.902 1.00 38.41 O HETATM 3424 O HOH A 714 99.025 55.107 26.040 1.00 46.07 O HETATM 3425 O HOH A 715 106.997 69.643 8.363 1.00 54.64 O HETATM 3426 O HOH A 716 81.233 76.372 5.194 1.00 34.05 O HETATM 3427 O HOH A 717 95.104 85.456 9.268 1.00 32.83 O HETATM 3428 O HOH A 718 88.247 53.744 13.103 1.00 44.30 O HETATM 3429 O HOH A 719 86.436 77.257 0.306 1.00 53.47 O HETATM 3430 O HOH A 720 79.183 113.473 -23.609 1.00 40.46 O HETATM 3431 O HOH A 721 98.628 47.628 17.406 1.00 42.40 O HETATM 3432 O HOH A 722 71.526 118.434 -17.657 1.00 51.84 O HETATM 3433 O HOH A 723 82.502 97.169 -8.636 1.00 44.25 O HETATM 3434 O HOH A 724 106.617 79.979 21.958 1.00 54.93 O HETATM 3435 O HOH A 725 77.596 110.520 -7.223 1.00 45.66 O HETATM 3436 O HOH A 726 98.348 53.508 9.927 1.00 32.73 O HETATM 3437 O HOH A 727 82.680 105.189 -12.045 1.00 32.80 O HETATM 3438 O HOH A 728 82.400 71.073 6.113 1.00 48.73 O HETATM 3439 O HOH A 729 92.408 62.881 24.793 1.00 37.16 O HETATM 3440 O HOH A 730 100.643 93.983 9.115 1.00 31.31 O HETATM 3441 O HOH A 731 84.575 66.257 14.787 1.00 41.58 O HETATM 3442 O HOH A 732 118.460 79.781 26.073 1.00 59.81 O HETATM 3443 O HOH A 733 77.259 82.099 -0.777 1.00 34.42 O HETATM 3444 O HOH A 734 73.846 87.119 -5.604 1.00 49.55 O HETATM 3445 O HOH A 735 101.319 48.586 26.878 1.00 48.50 O HETATM 3446 O HOH A 736 104.071 55.096 22.780 1.00 36.70 O HETATM 3447 O HOH A 737 69.965 108.644 -27.647 1.00 46.38 O HETATM 3448 O HOH A 738 94.245 93.255 4.826 1.00 44.97 O HETATM 3449 O HOH A 739 102.794 51.125 25.773 1.00 37.78 O HETATM 3450 O HOH A 740 76.816 99.386 -18.768 1.00 48.97 O HETATM 3451 O HOH A 741 110.970 48.952 9.292 1.00 64.86 O HETATM 3452 O HOH A 742 82.806 82.275 23.404 1.00 50.89 O HETATM 3453 O HOH A 743 67.443 97.164 7.839 1.00 51.77 O HETATM 3454 O HOH A 744 86.376 89.947 1.837 1.00 43.34 O HETATM 3455 O HOH A 745 102.782 66.098 27.267 1.00 46.04 O HETATM 3456 O HOH A 746 99.685 66.264 27.840 1.00 44.09 O HETATM 3457 O HOH A 747 99.193 74.296 6.674 1.00 40.09 O HETATM 3458 O HOH A 748 77.472 95.185 18.187 1.00 53.14 O HETATM 3459 O HOH A 749 105.829 71.823 14.294 1.00 36.32 O HETATM 3460 O HOH A 750 101.473 42.787 13.415 1.00 35.50 O HETATM 3461 O HOH A 751 101.428 47.025 19.534 1.00 47.58 O HETATM 3462 O HOH A 752 71.359 106.566 -28.230 1.00 48.72 O HETATM 3463 O HOH A 753 82.763 87.009 -0.954 1.00 32.25 O HETATM 3464 O HOH A 754 101.037 55.576 22.857 1.00 29.72 O HETATM 3465 O HOH A 755 104.332 77.358 10.897 1.00 41.05 O HETATM 3466 O HOH A 756 62.437 90.514 -15.040 1.00 48.81 O HETATM 3467 O HOH A 757 64.835 90.314 0.412 1.00 45.94 O HETATM 3468 O HOH A 758 113.056 69.607 22.169 1.00 46.65 O HETATM 3469 O HOH A 759 98.301 62.777 7.316 1.00 43.73 O HETATM 3470 O HOH A 760 85.543 88.720 23.951 1.00 55.00 O HETATM 3471 O HOH A 761 76.676 72.678 12.327 1.00 49.69 O HETATM 3472 O HOH A 762 79.263 69.139 12.909 1.00 46.59 O HETATM 3473 O HOH A 763 91.732 51.724 16.635 1.00 47.04 O HETATM 3474 O HOH A 764 89.983 101.728 11.221 1.00 35.22 O HETATM 3475 O HOH A 765 66.470 86.850 -3.208 1.00 54.09 O HETATM 3476 O HOH A 766 98.245 89.392 13.835 1.00 36.75 O HETATM 3477 O HOH A 767 93.754 49.511 17.641 1.00 49.21 O HETATM 3478 O HOH A 768 103.931 42.532 12.692 1.00 33.39 O HETATM 3479 O HOH A 769 88.123 71.350 2.926 1.00 65.42 O HETATM 3480 O HOH A 770 85.390 111.120 -14.525 1.00 47.83 O HETATM 3481 O HOH A 771 92.900 59.531 2.022 1.00 37.35 O HETATM 3482 O HOH A 772 104.784 86.713 8.501 1.00 45.68 O HETATM 3483 O HOH A 773 83.631 62.312 14.689 1.00 41.51 O HETATM 3484 O HOH A 774 94.262 52.978 5.435 1.00 46.80 O HETATM 3485 O HOH A 775 59.771 98.848 -4.940 1.00 51.51 O HETATM 3486 O HOH A 776 75.997 85.407 24.691 1.00 54.72 O HETATM 3487 O HOH A 777 89.287 107.449 0.743 1.00 41.20 O HETATM 3488 O HOH A 778 74.189 115.695 -15.084 1.00 50.68 O HETATM 3489 O HOH A 779 99.355 56.135 10.366 1.00 39.33 O HETATM 3490 O HOH A 780 81.820 100.044 14.808 1.00 50.58 O HETATM 3491 O HOH A 781 53.931 94.355 -32.627 1.00 61.49 O HETATM 3492 O HOH A 782 63.694 89.567 -10.545 1.00 42.76 O HETATM 3493 O HOH A 783 68.947 96.980 15.032 1.00 51.08 O HETATM 3494 O HOH A 784 100.109 57.346 25.552 1.00 37.70 O HETATM 3495 O HOH A 785 95.804 54.271 25.802 1.00 47.73 O HETATM 3496 O HOH A 786 79.837 110.474 -21.069 1.00 46.21 O HETATM 3497 O HOH A 787 108.296 61.683 23.924 1.00 48.42 O HETATM 3498 O HOH A 788 95.104 58.384 30.638 1.00 45.09 O HETATM 3499 O HOH A 789 67.147 111.081 0.870 1.00 55.61 O HETATM 3500 O HOH A 790 74.706 75.476 7.596 1.00 45.82 O HETATM 3501 O HOH A 791 61.327 105.953 -15.582 1.00 44.59 O HETATM 3502 O HOH A 792 79.149 84.896 -7.985 1.00 54.38 O HETATM 3503 O HOH A 793 71.566 81.039 -5.883 1.00 57.83 O HETATM 3504 O HOH A 794 102.923 63.145 29.567 1.00 55.29 O HETATM 3505 O HOH A 795 113.901 52.247 15.892 1.00 53.77 O HETATM 3506 O HOH A 796 91.106 97.825 8.945 1.00 52.87 O HETATM 3507 O HOH A 797 76.923 96.470 -14.605 1.00 46.54 O HETATM 3508 O HOH A 798 71.727 115.238 -10.751 1.00 46.20 O HETATM 3509 O HOH A 799 61.834 108.662 -2.977 1.00 39.76 O HETATM 3510 O HOH A 800 102.113 81.124 7.798 1.00 58.09 O HETATM 3511 O HOH A 801 61.942 93.028 -8.890 1.00 51.30 O HETATM 3512 O HOH A 802 68.305 99.154 -30.788 1.00 71.21 O HETATM 3513 O HOH A 803 111.071 61.799 3.871 1.00 53.43 O HETATM 3514 O HOH A 804 94.496 40.418 30.674 1.00 57.87 O HETATM 3515 O HOH A 805 70.177 81.103 3.586 1.00 55.43 O HETATM 3516 O HOH A 806 106.021 79.512 16.226 1.00 55.22 O HETATM 3517 O HOH A 807 83.000 103.394 -10.357 1.00 39.15 O HETATM 3518 O HOH A 808 96.097 60.096 32.039 1.00 58.02 O HETATM 3519 O HOH A 809 120.621 71.277 22.291 1.00 50.61 O HETATM 3520 O HOH A 810 73.994 106.185 -26.747 1.00 58.08 O HETATM 3521 O HOH A 811 88.543 86.278 2.009 1.00 57.34 O HETATM 3522 O HOH A 812 103.494 58.672 34.232 1.00 51.26 O HETATM 3523 O HOH A 813 84.217 112.147 0.287 1.00 48.51 O HETATM 3524 O HOH A 814 96.366 63.447 29.135 1.00 49.03 O HETATM 3525 O HOH A 815 81.276 121.716 -10.340 1.00 56.26 O HETATM 3526 O HOH A 816 66.513 84.471 5.478 1.00 64.56 O HETATM 3527 O HOH A 817 87.739 115.040 -10.238 1.00 57.04 O HETATM 3528 O HOH A 818 86.962 90.052 26.009 1.00 51.85 O HETATM 3529 O HOH A 819 101.463 66.169 6.173 1.00 53.87 O HETATM 3530 O HOH A 820 105.494 43.219 6.026 1.00 66.78 O HETATM 3531 O HOH A 821 69.925 79.461 8.713 1.00 57.15 O HETATM 3532 O HOH B 201 90.960 57.659 -0.937 1.00 35.75 O HETATM 3533 O HOH B 202 87.241 83.176 4.501 1.00 51.88 O HETATM 3534 O HOH B 203 88.531 63.550 8.887 1.00 40.76 O HETATM 3535 O HOH B 204 79.704 78.478 -5.436 1.00 55.99 O HETATM 3536 O HOH B 205 88.797 57.807 7.051 1.00 41.62 O HETATM 3537 O HOH B 206 70.837 87.975 -13.709 1.00 43.65 O HETATM 3538 O HOH B 207 89.560 74.592 2.404 1.00 51.13 O HETATM 3539 O HOH B 208 94.153 61.728 1.979 1.00 52.92 O CONECT 1871 2141 CONECT 2141 1871 CONECT 3359 3360 3361 CONECT 3360 3359 CONECT 3361 3359 3362 CONECT 3362 3361 CONECT 3363 3364 3365 CONECT 3364 3363 CONECT 3365 3363 3366 CONECT 3366 3365 CONECT 3367 3368 3369 CONECT 3368 3367 CONECT 3369 3367 3370 CONECT 3370 3369 CONECT 3371 3372 3373 CONECT 3372 3371 CONECT 3373 3371 3374 CONECT 3374 3373 CONECT 3375 3376 3377 CONECT 3376 3375 CONECT 3377 3375 3378 CONECT 3378 3377 CONECT 3379 3380 3381 CONECT 3380 3379 CONECT 3381 3379 3382 CONECT 3382 3381 CONECT 3383 3384 3385 CONECT 3384 3383 CONECT 3385 3383 3386 CONECT 3386 3385 CONECT 3387 3388 3389 CONECT 3388 3387 CONECT 3389 3387 3390 CONECT 3390 3389 CONECT 3391 3392 3393 CONECT 3392 3391 CONECT 3393 3391 3394 CONECT 3394 3393 CONECT 3395 3396 3397 CONECT 3396 3395 CONECT 3397 3395 3398 CONECT 3398 3397 CONECT 3399 3400 3401 CONECT 3400 3399 CONECT 3401 3399 3402 CONECT 3402 3401 CONECT 3403 3404 3405 CONECT 3404 3403 CONECT 3405 3403 3406 CONECT 3406 3405 CONECT 3407 3408 3409 CONECT 3408 3407 CONECT 3409 3407 3410 CONECT 3410 3409 MASTER 365 0 13 29 0 0 18 6 3528 2 54 33 END
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Related entries of code: 6noh
Entries with 90% protein sequence similarity cutoff in PDBbind
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Protein Sequence Similarity
3k5q
RCSB PDB
PDBbind
412aa, >3K5Q_1|Chain... at 100%
3k5y
RCSB PDB
PDBbind
412aa, >3K5Y_1|Chain... at 100%
3k5z
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PDBbind
412aa, >3K5Z_1|Chain... at 100%
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RCSB PDB
PDBbind
412aa, >3K61_1|Chain... at 100%
3k62
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PDBbind
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3k64
RCSB PDB
PDBbind
412aa, >3K64_1|Chain... at 100%
3qg9
RCSB PDB
PDBbind
413aa, >3QG9_1|Chain... *
3qgb
RCSB PDB
PDBbind
413aa, >3QGB_1|Chain... at 99%
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RCSB PDB
PDBbind
413aa, >3QGC_1|Chain... at 99%
6nof
RCSB PDB
PDBbind
413aa, >6NOF_1|Chain... at 99%
6noc
RCSB PDB
PDBbind
413aa, >6NOC_1|Chain... at 99%
Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
2w42
RCSB PDB
PDBbind
8-mer
3eqt
RCSB PDB
PDBbind
8-mer
3igm
RCSB PDB
PDBbind
8-mer
3l25
RCSB PDB
PDBbind
8-mer
5en1
RCSB PDB
PDBbind
8-mer
6nof
RCSB PDB
PDBbind
8-mer
6nod
RCSB PDB
PDBbind
8-mer
6noc
RCSB PDB
PDBbind
8-mer
Entry Information
PDB ID
6noh
Complex Type
Protein-Nucleic Acid
PDBbind Subset
general set
Protein Name
FBF-2 repeat 5 SS/Y mutant (C363S, R364Y, Q367S)
Ligand Name
8-mer
EC.Number
E.C.-.-.-.-
Resolution
2.25(Å)
Affinity (Kd/Ki/IC50)
Kd=22.7nM
Release Year
2019
Protein/NA Sequence
Check fasta file
Primary Reference
(2019) Elife Vol. 8: pp. e43788
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UniProt accession number (AC):
Q09312
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