Browse entries in the PDBbind-CN Database
HEADER RNA BINDING PROTEIN/RNA 20-NOV-17 5YTT TITLE CRYSTAL STRUCTURE OF YB1 COLD-SHOCK DOMAIN IN COMPLEX WITH UCAUGU COMPND MOL_ID: 1; COMPND 2 MOLECULE: NUCLEASE-SENSITIVE ELEMENT-BINDING PROTEIN 1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: CCAAT-BINDING TRANSCRIPTION FACTOR I SUBUNIT A,CBF-A,DNA- COMPND 5 BINDING PROTEIN B,DBPB,ENHANCER FACTOR I SUBUNIT A,EFI-A,Y-BOX COMPND 6 TRANSCRIPTION FACTOR,Y-BOX-BINDING PROTEIN 1,YB-1; COMPND 7 ENGINEERED: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: RNA (5'-R(P*UP*CP*AP*UP*GP*U)-3'); COMPND 10 CHAIN: B; COMPND 11 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: YBX1, NSEP1, YB1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 SYNTHETIC: YES; SOURCE 10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 11 ORGANISM_TAXID: 32630 KEYWDS YB1, COLD-SHOCK DOMAIN, CAUG, RNA BINDING PROTEIN, RNA BINDING KEYWDS 2 PROTEIN-RNA COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR X.YANG,Y.HUANG REVDAT 3 24-JUL-19 5YTT 1 JRNL REVDAT 2 19-JUN-19 5YTT 1 JRNL REVDAT 1 05-DEC-18 5YTT 0 JRNL AUTH X.J.YANG,H.ZHU,S.R.MU,W.J.WEI,X.YUAN,M.WANG,Y.LIU,J.HUI, JRNL AUTH 2 Y.HUANG JRNL TITL CRYSTAL STRUCTURE OF A Y-BOX BINDING PROTEIN 1 (YB-1)-RNA JRNL TITL 2 COMPLEX REVEALS KEY FEATURES AND RESIDUES INTERACTING WITH JRNL TITL 3 RNA. JRNL REF J.BIOL.CHEM. V. 294 10998 2019 JRNL REFN ESSN 1083-351X JRNL PMID 31160337 JRNL DOI 10.1074/JBC.RA119.007545 REMARK 2 REMARK 2 RESOLUTION. 1.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.9_1692 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 : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 46.6 REMARK 3 NUMBER OF REFLECTIONS : 10965 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.186 REMARK 3 R VALUE (WORKING SET) : 0.182 REMARK 3 FREE R VALUE : 0.218 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.040 REMARK 3 FREE R VALUE TEST SET COUNT : 1101 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 30.5441 - 3.1930 0.61 1616 182 0.1782 0.2371 REMARK 3 2 3.1930 - 2.5347 0.56 1497 162 0.1980 0.2260 REMARK 3 3 2.5347 - 2.2144 0.52 1360 154 0.1744 0.1919 REMARK 3 4 2.2144 - 2.0120 0.51 1356 152 0.1712 0.1782 REMARK 3 5 2.0120 - 1.8678 0.48 1290 140 0.1730 0.2126 REMARK 3 6 1.8678 - 1.7577 0.41 1073 124 0.1835 0.1993 REMARK 3 7 1.7577 - 1.6697 0.35 913 103 0.1960 0.2881 REMARK 3 8 1.6697 - 1.5970 0.28 759 84 0.2267 0.2031 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL 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) : 0.170 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.640 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 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 : 0.007 776 REMARK 3 ANGLE : 1.072 1082 REMARK 3 CHIRALITY : 0.045 131 REMARK 3 PLANARITY : 0.005 117 REMARK 3 DIHEDRAL : 14.940 304 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ALL REMARK 3 ORIGIN FOR THE GROUP (A): -6.2485 23.1717 36.1764 REMARK 3 T TENSOR REMARK 3 T11: 0.0461 T22: 0.0806 REMARK 3 T33: 0.0923 T12: -0.0187 REMARK 3 T13: 0.0274 T23: -0.0269 REMARK 3 L TENSOR REMARK 3 L11: 3.1957 L22: 2.3306 REMARK 3 L33: 1.6701 L12: 0.3045 REMARK 3 L13: -0.4893 L23: -0.3600 REMARK 3 S TENSOR REMARK 3 S11: -0.0790 S12: 0.0819 S13: -0.3140 REMARK 3 S21: -0.0379 S22: -0.0020 S23: -0.0518 REMARK 3 S31: 0.2126 S32: -0.0960 S33: 0.0147 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 5YTT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-NOV-17. REMARK 100 THE DEPOSITION ID IS D_1300005400. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 12-DEC-14 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 4.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRF REMARK 200 BEAMLINE : BL17U1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97852 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11696 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600 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 (%) : 96.4 REMARK 200 DATA REDUNDANCY : 9.200 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <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: PHENIX REMARK 200 STARTING MODEL: 3PF5 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 41.56 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 30 % (V/V) 2-METHYL-2,4-PENTANEDIOL, REMARK 280 0.1 M SODIUM ACETATE, PH 4.5, 25 % (W/V) PEG 1500, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 290K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 -X,-Y,Z REMARK 290 5555 Y,-X+Y,Z+2/3 REMARK 290 6555 X-Y,X,Z+1/3 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 24.05333 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 12.02667 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 0.00000 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 24.05333 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 12.02667 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A 48 REMARK 465 SER A 49 REMARK 465 GLY A 50 REMARK 465 ASP A 51 REMARK 465 ASN A 95 REMARK 465 PRO A 96 REMARK 465 ARG A 97 REMARK 465 GLY A 130 REMARK 465 U B 6 REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 353 DISTANCE = 6.63 ANGSTROMS REMARK 525 HOH A 354 DISTANCE = 6.66 ANGSTROMS REMARK 525 HOH A 355 DISTANCE = 7.28 ANGSTROMS REMARK 525 HOH A 356 DISTANCE = 9.99 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 202 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5YTS RELATED DB: PDB REMARK 900 RELATED ID: 5YTV RELATED DB: PDB REMARK 900 RELATED ID: 5YTX RELATED DB: PDB DBREF 5YTT A 50 130 UNP P67809 YBOX1_HUMAN 50 130 DBREF 5YTT B 1 7 PDB 5YTT 5YTT 1 7 SEQADV 5YTT GLY A 48 UNP P67809 EXPRESSION TAG SEQADV 5YTT SER A 49 UNP P67809 EXPRESSION TAG SEQRES 1 A 83 GLY SER GLY ASP LYS LYS VAL ILE ALA THR LYS VAL LEU SEQRES 2 A 83 GLY THR VAL LYS TRP PHE ASN VAL ARG ASN GLY TYR GLY SEQRES 3 A 83 PHE ILE ASN ARG ASN ASP THR LYS GLU ASP VAL PHE VAL SEQRES 4 A 83 HIS GLN THR ALA ILE LYS LYS ASN ASN PRO ARG LYS TYR SEQRES 5 A 83 LEU ARG SER VAL GLY ASP GLY GLU THR VAL GLU PHE ASP SEQRES 6 A 83 VAL VAL GLU GLY GLU LYS GLY ALA GLU ALA ALA ASN VAL SEQRES 7 A 83 THR GLY PRO GLY GLY SEQRES 1 B 7 U C A U G U U HET SO4 A 201 5 HET SO4 A 202 5 HETNAM SO4 SULFATE ION FORMUL 3 SO4 2(O4 S 2-) FORMUL 5 HOH *62(H2 O) HELIX 1 AA1 THR A 89 ILE A 91 5 3 SHEET 1 AA1 6 LYS A 53 ASN A 67 0 SHEET 2 AA1 6 TYR A 72 ARG A 77 -1 O ASN A 76 N THR A 62 SHEET 3 AA1 6 ASP A 83 HIS A 87 -1 O VAL A 84 N ILE A 75 SHEET 4 AA1 6 GLY A 119 THR A 126 1 O ALA A 122 N PHE A 85 SHEET 5 AA1 6 THR A 108 GLY A 116 -1 N ASP A 112 O ALA A 123 SHEET 6 AA1 6 LYS A 53 ASN A 67 -1 N ILE A 55 O VAL A 113 SITE 1 AC1 5 LYS A 52 LYS A 53 VAL A 54 ARG A 101 SITE 2 AC1 5 SO4 A 202 SITE 1 AC2 4 LYS A 92 LYS A 93 ARG A 101 SO4 A 201 CRYST1 66.218 66.218 36.080 90.00 90.00 120.00 P 62 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 0.015102 0.008719 0.000000 0.00000 SCALE2 0.000000 0.017438 0.000000 0.00000 SCALE3 0.000000 0.000000 0.027716 0.00000 ATOM 1 N LYS A 52 5.169 10.639 36.954 1.00 73.70 N ANISOU 1 N LYS A 52 8756 8029 11217 506 827 199 N ATOM 2 CA LYS A 52 5.047 12.028 36.528 1.00 72.67 C ANISOU 2 CA LYS A 52 8643 8057 10911 463 781 126 C ATOM 3 C LYS A 52 6.197 12.874 37.062 1.00 64.57 C ANISOU 3 C LYS A 52 7529 7140 9866 518 696 242 C ATOM 4 O LYS A 52 6.708 12.631 38.158 1.00 74.34 O ANISOU 4 O LYS A 52 8704 8372 11169 571 622 412 O ATOM 5 CB LYS A 52 3.707 12.615 36.984 1.00 76.31 C ANISOU 5 CB LYS A 52 9169 8580 11246 389 721 123 C ATOM 6 CG LYS A 52 3.508 12.627 38.490 1.00 82.94 C ANISOU 6 CG LYS A 52 9986 9434 12093 413 622 321 C ATOM 7 CD LYS A 52 2.160 13.224 38.848 1.00 86.14 C ANISOU 7 CD LYS A 52 10459 9894 12377 340 583 307 C ATOM 8 CE LYS A 52 1.018 12.338 38.374 1.00 90.28 C ANISOU 8 CE LYS A 52 11055 10311 12938 269 662 203 C ATOM 9 NZ LYS A 52 -0.310 12.924 38.710 1.00 88.70 N ANISOU 9 NZ LYS A 52 10913 10165 12623 188 627 191 N ATOM 10 N LYS A 53 6.587 13.882 36.289 1.00 41.87 N ANISOU 10 N LYS A 53 4648 4371 6889 499 700 154 N ATOM 11 CA LYS A 53 7.713 14.733 36.650 1.00 22.04 C ANISOU 11 CA LYS A 53 2049 1963 4362 536 626 239 C ATOM 12 C LYS A 53 7.293 16.201 36.709 1.00 22.94 C ANISOU 12 C LYS A 53 2186 2226 4303 477 546 213 C ATOM 13 O LYS A 53 6.467 16.639 35.914 1.00 22.07 O ANISOU 13 O LYS A 53 2151 2148 4087 418 586 92 O ATOM 14 CB LYS A 53 8.852 14.568 35.644 1.00 25.32 C ANISOU 14 CB LYS A 53 2414 2357 4848 577 718 174 C ATOM 15 CG LYS A 53 9.408 13.151 35.514 1.00 34.64 C ANISOU 15 CG LYS A 53 3559 3384 6220 647 810 190 C ATOM 16 CD LYS A 53 10.622 13.146 34.605 1.00 39.38 C ANISOU 16 CD LYS A 53 4093 3983 6885 696 898 135 C ATOM 17 CE LYS A 53 11.305 11.794 34.579 1.00 45.43 C ANISOU 17 CE LYS A 53 4804 4593 7864 780 987 165 C ATOM 18 NZ LYS A 53 10.435 10.749 33.967 1.00 54.15 N ANISOU 18 NZ LYS A 53 6003 5563 9008 755 1095 39 N ATOM 19 N VAL A 54 7.879 16.956 37.631 1.00 20.26 N ANISOU 19 N VAL A 54 1782 1981 3936 489 431 324 N ATOM 20 CA VAL A 54 7.659 18.400 37.693 1.00 19.16 C ANISOU 20 CA VAL A 54 1651 1976 3651 433 358 296 C ATOM 21 C VAL A 54 8.484 19.090 36.611 1.00 16.49 C ANISOU 21 C VAL A 54 1287 1689 3291 424 411 217 C ATOM 22 O VAL A 54 9.706 18.917 36.560 1.00 18.45 O ANISOU 22 O VAL A 54 1448 1928 3632 469 420 262 O ATOM 23 CB VAL A 54 8.038 18.969 39.076 1.00 18.04 C ANISOU 23 CB VAL A 54 1451 1925 3478 435 209 425 C ATOM 24 CG1 VAL A 54 7.884 20.492 39.094 1.00 18.89 C ANISOU 24 CG1 VAL A 54 1568 2160 3451 370 142 374 C ATOM 25 CG2 VAL A 54 7.182 18.322 40.162 1.00 22.31 C ANISOU 25 CG2 VAL A 54 2026 2436 4013 444 155 523 C ATOM 26 N AILE A 55 7.812 19.842 35.745 0.41 13.82 N ANISOU 26 N AILE A 55 1016 1403 2833 368 447 113 N ATOM 27 N CILE A 55 7.838 19.872 35.746 0.59 13.82 N ANISOU 27 N CILE A 55 1014 1405 2832 368 445 114 N ATOM 28 CA AILE A 55 8.499 20.557 34.680 0.41 18.25 C ANISOU 28 CA AILE A 55 1558 2020 3354 355 500 57 C ATOM 29 CA CILE A 55 8.581 20.559 34.686 0.59 16.91 C ANISOU 29 CA CILE A 55 1383 1852 3190 357 500 61 C ATOM 30 C AILE A 55 8.793 21.987 35.102 0.41 16.57 C ANISOU 30 C AILE A 55 1312 1915 3071 313 408 96 C ATOM 31 C CILE A 55 8.641 22.073 34.879 0.59 16.86 C ANISOU 31 C CILE A 55 1365 1957 3086 304 422 77 C ATOM 32 O AILE A 55 9.866 22.517 34.813 0.41 17.17 O ANISOU 32 O AILE A 55 1318 2028 3180 317 416 115 O ATOM 33 O CILE A 55 9.403 22.754 34.199 0.59 16.54 O ANISOU 33 O CILE A 55 1286 1963 3036 294 453 65 O ATOM 34 CB AILE A 55 7.682 20.579 33.378 0.41 21.30 C ANISOU 34 CB AILE A 55 2036 2418 3640 317 589 -65 C ATOM 35 CB CILE A 55 7.997 20.270 33.288 0.59 14.04 C ANISOU 35 CB CILE A 55 1100 1474 2761 336 613 -63 C ATOM 36 CG1AILE A 55 7.323 19.160 32.946 0.41 21.30 C ANISOU 36 CG1AILE A 55 2078 2306 3709 341 679 -130 C ATOM 37 CG1CILE A 55 6.542 20.723 33.205 0.59 20.84 C ANISOU 37 CG1CILE A 55 2052 2375 3489 274 582 -116 C ATOM 38 CG2AILE A 55 8.468 21.275 32.283 0.41 18.81 C ANISOU 38 CG2AILE A 55 1695 2171 3283 312 649 -97 C ATOM 39 CG2CILE A 55 8.132 18.795 32.941 0.59 18.04 C ANISOU 39 CG2CILE A 55 1615 1860 3381 382 707 -105 C ATOM 40 CD1AILE A 55 8.528 18.283 32.739 0.41 25.46 C ANISOU 40 CD1AILE A 55 2535 2755 4382 411 752 -113 C ATOM 41 CD1CILE A 55 5.937 20.537 31.829 0.59 27.47 C ANISOU 41 CD1CILE A 55 2968 3232 4239 242 668 -233 C ATOM 42 N ALA A 56 7.834 22.601 35.793 1.00 14.24 N ANISOU 42 N ALA A 56 1062 1662 2688 269 329 102 N ATOM 43 CA ALA A 56 7.932 24.006 36.165 1.00 12.52 C ANISOU 43 CA ALA A 56 829 1531 2398 217 250 114 C ATOM 44 C ALA A 56 7.228 24.260 37.492 1.00 11.89 C ANISOU 44 C ALA A 56 763 1481 2275 195 142 152 C ATOM 45 O ALA A 56 6.282 23.553 37.833 1.00 13.02 O ANISOU 45 O ALA A 56 951 1590 2408 207 147 155 O ATOM 46 CB ALA A 56 7.329 24.898 35.077 1.00 16.18 C ANISOU 46 CB ALA A 56 1355 2036 2757 170 300 46 C ATOM 47 N THR A 57 7.697 25.250 38.252 1.00 13.54 N ANISOU 47 N THR A 57 930 1755 2462 159 48 177 N ATOM 48 CA ATHR A 57 7.018 25.606 39.492 0.14 14.06 C ANISOU 48 CA ATHR A 57 1013 1869 2461 129 -56 196 C ATOM 49 CA BTHR A 57 7.055 25.617 39.513 0.86 14.44 C ANISOU 49 CA BTHR A 57 1059 1919 2510 129 -58 198 C ATOM 50 C THR A 57 6.734 27.102 39.555 1.00 12.72 C ANISOU 50 C THR A 57 866 1752 2213 58 -92 138 C ATOM 51 O THR A 57 7.358 27.895 38.853 1.00 12.14 O ANISOU 51 O THR A 57 773 1680 2159 33 -59 115 O ATOM 52 CB ATHR A 57 7.828 25.187 40.741 0.14 16.73 C ANISOU 52 CB ATHR A 57 1281 2240 2835 151 -166 287 C ATOM 53 CB BTHR A 57 7.944 25.265 40.732 0.86 18.70 C ANISOU 53 CB BTHR A 57 1523 2493 3087 149 -170 286 C ATOM 54 OG1ATHR A 57 7.034 25.402 41.915 0.14 15.44 O ANISOU 54 OG1ATHR A 57 1153 2138 2574 120 -264 306 O ATOM 55 OG1BTHR A 57 9.172 26.005 40.667 0.86 19.84 O ANISOU 55 OG1BTHR A 57 1592 2673 3272 126 -202 282 O ATOM 56 CG2ATHR A 57 9.112 25.992 40.856 0.14 19.28 C ANISOU 56 CG2ATHR A 57 1523 2610 3192 124 -219 287 C ATOM 57 CG2BTHR A 57 8.249 23.776 40.758 0.86 18.98 C ANISOU 57 CG2BTHR A 57 1532 2459 3220 227 -134 367 C ATOM 58 N LYS A 58 5.757 27.464 40.382 1.00 12.28 N ANISOU 58 N LYS A 58 853 1732 2079 25 -151 119 N ATOM 59 CA LYS A 58 5.366 28.852 40.591 1.00 12.76 C ANISOU 59 CA LYS A 58 943 1826 2080 -42 -183 56 C ATOM 60 C LYS A 58 5.032 29.544 39.272 1.00 11.61 C ANISOU 60 C LYS A 58 838 1641 1934 -54 -87 19 C ATOM 61 O LYS A 58 5.399 30.707 39.033 1.00 14.92 O ANISOU 61 O LYS A 58 1249 2054 2367 -96 -90 1 O ATOM 62 CB LYS A 58 6.462 29.629 41.344 1.00 19.99 C ANISOU 62 CB LYS A 58 1799 2787 3010 -85 -275 53 C ATOM 63 CG LYS A 58 6.923 29.016 42.690 1.00 27.67 C ANISOU 63 CG LYS A 58 2734 3825 3956 -75 -396 101 C ATOM 64 CD LYS A 58 5.883 28.080 43.317 1.00 53.30 C ANISOU 64 CD LYS A 58 6034 7085 7132 -46 -417 147 C ATOM 65 CE LYS A 58 5.547 28.393 44.772 1.00 61.80 C ANISOU 65 CE LYS A 58 7154 8257 8071 -92 -539 138 C ATOM 66 NZ LYS A 58 4.926 27.203 45.432 1.00 61.09 N ANISOU 66 NZ LYS A 58 7101 8201 7909 -54 -557 247 N ATOM 67 N VAL A 59 4.318 28.819 38.421 1.00 8.21 N ANISOU 67 N VAL A 59 452 1181 1486 -20 -7 14 N ATOM 68 CA VAL A 59 3.788 29.359 37.168 1.00 7.86 C ANISOU 68 CA VAL A 59 456 1123 1407 -29 66 -9 C ATOM 69 C VAL A 59 2.481 30.106 37.421 1.00 8.54 C ANISOU 69 C VAL A 59 597 1214 1435 -56 52 -40 C ATOM 70 O VAL A 59 1.637 29.608 38.146 1.00 10.30 O ANISOU 70 O VAL A 59 840 1446 1627 -53 32 -57 O ATOM 71 CB VAL A 59 3.528 28.224 36.140 1.00 8.18 C ANISOU 71 CB VAL A 59 524 1146 1437 8 144 -18 C ATOM 72 CG1 VAL A 59 3.011 28.794 34.820 1.00 10.53 C ANISOU 72 CG1 VAL A 59 862 1461 1677 -5 199 -33 C ATOM 73 CG2 VAL A 59 4.800 27.409 35.914 1.00 11.47 C ANISOU 73 CG2 VAL A 59 884 1541 1935 45 173 6 C ATOM 74 N LEU A 60 2.331 31.291 36.831 1.00 8.98 N ANISOU 74 N LEU A 60 665 1258 1491 -78 68 -43 N ATOM 75 CA LEU A 60 1.063 32.029 36.889 1.00 8.64 C ANISOU 75 CA LEU A 60 663 1204 1415 -89 69 -70 C ATOM 76 C LEU A 60 0.256 31.795 35.635 1.00 7.50 C ANISOU 76 C LEU A 60 550 1078 1221 -69 123 -52 C ATOM 77 O LEU A 60 0.808 31.684 34.527 1.00 7.49 O ANISOU 77 O LEU A 60 536 1094 1215 -64 165 -25 O ATOM 78 CB LEU A 60 1.321 33.528 37.054 1.00 8.97 C ANISOU 78 CB LEU A 60 685 1204 1518 -123 52 -81 C ATOM 79 CG LEU A 60 1.962 33.928 38.380 1.00 12.55 C ANISOU 79 CG LEU A 60 1114 1649 2007 -161 -21 -125 C ATOM 80 CD1 LEU A 60 2.528 35.331 38.275 1.00 21.62 C ANISOU 80 CD1 LEU A 60 2239 2736 3241 -205 -27 -135 C ATOM 81 CD2 LEU A 60 0.924 33.861 39.505 1.00 14.55 C ANISOU 81 CD2 LEU A 60 1401 1921 2207 -167 -55 -199 C ATOM 82 N GLY A 61 -1.056 31.740 35.800 1.00 5.66 N ANISOU 82 N GLY A 61 350 853 946 -63 121 -74 N ATOM 83 CA GLY A 61 -1.922 31.501 34.670 1.00 5.20 C ANISOU 83 CA GLY A 61 311 827 839 -53 153 -58 C ATOM 84 C GLY A 61 -3.306 32.012 34.956 1.00 7.02 C ANISOU 84 C GLY A 61 550 1064 1053 -49 140 -70 C ATOM 85 O GLY A 61 -3.654 32.364 36.093 1.00 8.36 O ANISOU 85 O GLY A 61 723 1213 1240 -50 121 -105 O ATOM 86 N THR A 62 -4.111 32.030 33.908 1.00 6.48 N ANISOU 86 N THR A 62 475 1037 951 -46 156 -48 N ATOM 87 CA ATHR A 62 -5.490 32.470 33.996 0.65 6.14 C ANISOU 87 CA ATHR A 62 417 1015 902 -35 142 -45 C ATOM 88 CA BTHR A 62 -5.499 32.451 34.039 0.35 6.59 C ANISOU 88 CA BTHR A 62 474 1070 958 -35 141 -47 C ATOM 89 C THR A 62 -6.420 31.301 33.690 1.00 7.28 C ANISOU 89 C THR A 62 580 1206 980 -51 130 -76 C ATOM 90 O THR A 62 -6.245 30.634 32.670 1.00 8.50 O ANISOU 90 O THR A 62 738 1414 1079 -72 140 -88 O ATOM 91 CB ATHR A 62 -5.783 33.602 33.013 0.65 10.25 C ANISOU 91 CB ATHR A 62 883 1572 1440 -21 151 26 C ATOM 92 CB BTHR A 62 -5.849 33.641 33.140 0.35 10.08 C ANISOU 92 CB BTHR A 62 861 1545 1425 -19 149 22 C ATOM 93 OG1ATHR A 62 -4.784 34.626 33.139 0.65 15.98 O ANISOU 93 OG1ATHR A 62 1600 2224 2248 -19 168 61 O ATOM 94 OG1BTHR A 62 -5.635 33.284 31.770 0.35 10.83 O ANISOU 94 OG1BTHR A 62 956 1721 1439 -34 159 65 O ATOM 95 CG2ATHR A 62 -7.159 34.185 33.275 0.65 12.67 C ANISOU 95 CG2ATHR A 62 1158 1882 1774 13 130 45 C ATOM 96 CG2BTHR A 62 -5.004 34.852 33.497 0.35 12.40 C ANISOU 96 CG2BTHR A 62 1146 1749 1817 -11 162 51 C ATOM 97 N VAL A 63 -7.399 31.064 34.557 1.00 5.29 N ANISOU 97 N VAL A 63 333 944 733 -48 118 -97 N ATOM 98 CA VAL A 63 -8.351 29.986 34.331 1.00 4.89 C ANISOU 98 CA VAL A 63 282 932 642 -76 109 -126 C ATOM 99 C VAL A 63 -9.213 30.282 33.121 1.00 6.55 C ANISOU 99 C VAL A 63 440 1232 815 -86 84 -104 C ATOM 100 O VAL A 63 -9.923 31.288 33.096 1.00 9.02 O ANISOU 100 O VAL A 63 707 1557 1162 -54 69 -54 O ATOM 101 CB VAL A 63 -9.264 29.774 35.557 1.00 5.53 C ANISOU 101 CB VAL A 63 365 991 744 -73 115 -136 C ATOM 102 CG1 VAL A 63 -10.272 28.656 35.294 1.00 8.13 C ANISOU 102 CG1 VAL A 63 678 1355 1056 -113 111 -160 C ATOM 103 CG2 VAL A 63 -8.433 29.452 36.786 1.00 5.76 C ANISOU 103 CG2 VAL A 63 432 977 779 -72 131 -153 C ATOM 104 N LYS A 64 -9.161 29.407 32.118 1.00 8.24 N ANISOU 104 N LYS A 64 651 1522 960 -132 79 -142 N ATOM 105 CA LYS A 64 -9.994 29.567 30.938 1.00 8.84 C ANISOU 105 CA LYS A 64 667 1729 963 -160 34 -121 C ATOM 106 C LYS A 64 -11.428 29.187 31.252 1.00 12.99 C ANISOU 106 C LYS A 64 1163 2262 1512 -176 -2 -131 C ATOM 107 O LYS A 64 -12.366 29.962 31.050 1.00 12.11 O ANISOU 107 O LYS A 64 995 2188 1419 -148 -43 -64 O ATOM 108 CB LYS A 64 -9.481 28.695 29.791 1.00 11.09 C ANISOU 108 CB LYS A 64 982 2087 1143 -217 42 -186 C ATOM 109 CG LYS A 64 -8.438 29.356 28.914 1.00 27.43 C ANISOU 109 CG LYS A 64 3083 4187 3152 -193 70 -133 C ATOM 110 CD LYS A 64 -8.031 28.430 27.764 1.00 38.71 C ANISOU 110 CD LYS A 64 4562 5690 4458 -247 95 -219 C ATOM 111 CE LYS A 64 -9.206 27.837 26.969 1.00 45.00 C ANISOU 111 CE LYS A 64 5344 6608 5147 -317 22 -276 C ATOM 112 NZ LYS A 64 -10.448 28.669 26.899 1.00 58.15 N ANISOU 112 NZ LYS A 64 6930 8357 6808 -304 -77 -173 N ATOM 113 N TRP A 65 -11.579 27.963 31.728 1.00 8.29 N ANISOU 113 N TRP A 65 598 1622 931 -220 20 -206 N ATOM 114 CA TRP A 65 -12.866 27.457 32.178 1.00 9.50 C ANISOU 114 CA TRP A 65 720 1765 1126 -244 6 -211 C ATOM 115 C TRP A 65 -12.643 26.308 33.145 1.00 7.98 C ANISOU 115 C TRP A 65 569 1483 978 -270 56 -259 C ATOM 116 O TRP A 65 -11.604 25.638 33.099 1.00 7.87 O ANISOU 116 O TRP A 65 602 1430 957 -287 89 -307 O ATOM 117 CB TRP A 65 -13.741 27.013 30.995 1.00 13.37 C ANISOU 117 CB TRP A 65 1166 2357 1557 -305 -55 -237 C ATOM 118 CG TRP A 65 -13.176 25.930 30.112 1.00 15.70 C ANISOU 118 CG TRP A 65 1506 2681 1779 -378 -48 -337 C ATOM 119 CD1 TRP A 65 -12.394 26.096 29.000 1.00 21.56 C ANISOU 119 CD1 TRP A 65 2274 3504 2415 -394 -56 -363 C ATOM 120 CD2 TRP A 65 -13.375 24.520 30.253 1.00 13.08 C ANISOU 120 CD2 TRP A 65 1200 2287 1482 -445 -21 -428 C ATOM 121 NE1 TRP A 65 -12.084 24.872 28.450 1.00 22.72 N ANISOU 121 NE1 TRP A 65 2472 3630 2532 -459 -27 -478 N ATOM 122 CE2 TRP A 65 -12.684 23.887 29.197 1.00 22.21 C ANISOU 122 CE2 TRP A 65 2405 3472 2563 -492 -8 -519 C ATOM 123 CE3 TRP A 65 -14.066 23.726 31.177 1.00 10.77 C ANISOU 123 CE3 TRP A 65 896 1912 1285 -470 0 -434 C ATOM 124 CZ2 TRP A 65 -12.667 22.498 29.034 1.00 19.39 C ANISOU 124 CZ2 TRP A 65 2085 3041 2240 -555 27 -624 C ATOM 125 CZ3 TRP A 65 -14.059 22.354 31.008 1.00 14.74 C ANISOU 125 CZ3 TRP A 65 1429 2354 1819 -541 27 -523 C ATOM 126 CH2 TRP A 65 -13.357 21.749 29.952 1.00 18.18 C ANISOU 126 CH2 TRP A 65 1916 2798 2195 -580 40 -622 C ATOM 127 N PHE A 66 -13.603 26.124 34.046 1.00 7.41 N ANISOU 127 N PHE A 66 470 1381 963 -271 67 -233 N ATOM 128 CA PHE A 66 -13.567 25.002 34.967 1.00 7.81 C ANISOU 128 CA PHE A 66 547 1364 1057 -303 113 -252 C ATOM 129 C PHE A 66 -14.962 24.496 35.189 1.00 8.59 C ANISOU 129 C PHE A 66 585 1476 1204 -347 109 -240 C ATOM 130 O PHE A 66 -15.828 25.241 35.619 1.00 9.00 O ANISOU 130 O PHE A 66 582 1553 1284 -314 109 -189 O ATOM 131 CB PHE A 66 -12.927 25.394 36.309 1.00 6.64 C ANISOU 131 CB PHE A 66 436 1163 922 -251 154 -209 C ATOM 132 CG PHE A 66 -12.731 24.213 37.210 1.00 6.83 C ANISOU 132 CG PHE A 66 484 1132 981 -286 200 -206 C ATOM 133 CD1 PHE A 66 -11.624 23.382 37.031 1.00 7.90 C ANISOU 133 CD1 PHE A 66 660 1212 1131 -304 219 -235 C ATOM 134 CD2 PHE A 66 -13.647 23.915 38.194 1.00 8.22 C ANISOU 134 CD2 PHE A 66 631 1307 1186 -301 236 -164 C ATOM 135 CE1 PHE A 66 -11.441 22.275 37.839 1.00 9.34 C ANISOU 135 CE1 PHE A 66 856 1327 1367 -336 267 -210 C ATOM 136 CE2 PHE A 66 -13.486 22.798 39.004 1.00 10.46 C ANISOU 136 CE2 PHE A 66 931 1540 1503 -340 285 -137 C ATOM 137 CZ PHE A 66 -12.373 21.980 38.827 1.00 9.72 C ANISOU 137 CZ PHE A 66 881 1379 1433 -358 297 -154 C ATOM 138 N ASN A 67 -15.181 23.219 34.885 1.00 8.97 N ANISOU 138 N ASN A 67 634 1497 1278 -424 113 -291 N ATOM 139 CA ASN A 67 -16.517 22.647 34.970 1.00 10.10 C ANISOU 139 CA ASN A 67 708 1650 1479 -482 103 -281 C ATOM 140 C ASN A 67 -16.661 21.820 36.235 1.00 10.31 C ANISOU 140 C ASN A 67 742 1603 1572 -505 172 -242 C ATOM 141 O ASN A 67 -15.957 20.831 36.407 1.00 10.37 O ANISOU 141 O ASN A 67 804 1532 1605 -538 206 -268 O ATOM 142 CB ASN A 67 -16.795 21.803 33.732 1.00 11.18 C ANISOU 142 CB ASN A 67 837 1805 1605 -566 54 -366 C ATOM 143 CG ASN A 67 -18.212 21.302 33.695 1.00 13.36 C ANISOU 143 CG ASN A 67 1027 2100 1950 -635 23 -356 C ATOM 144 OD1 ASN A 67 -18.607 20.510 34.540 1.00 13.91 O ANISOU 144 OD1 ASN A 67 1082 2104 2100 -674 71 -331 O ATOM 145 ND2 ASN A 67 -18.989 21.754 32.714 1.00 19.44 N ANISOU 145 ND2 ASN A 67 1732 2964 2692 -654 -61 -365 N ATOM 146 N VAL A 68 -17.570 22.219 37.124 1.00 10.62 N ANISOU 146 N VAL A 68 723 1668 1646 -485 201 -171 N ATOM 147 CA VAL A 68 -17.693 21.573 38.425 1.00 10.97 C ANISOU 147 CA VAL A 68 773 1668 1726 -501 278 -112 C ATOM 148 C VAL A 68 -18.475 20.267 38.341 1.00 12.34 C ANISOU 148 C VAL A 68 906 1802 1982 -602 287 -112 C ATOM 149 O VAL A 68 -18.463 19.459 39.280 1.00 13.15 O ANISOU 149 O VAL A 68 1023 1854 2119 -635 351 -56 O ATOM 150 CB VAL A 68 -18.366 22.504 39.469 1.00 11.54 C ANISOU 150 CB VAL A 68 801 1794 1791 -440 328 -43 C ATOM 151 CG1 VAL A 68 -17.523 23.774 39.656 1.00 13.14 C ANISOU 151 CG1 VAL A 68 1057 2012 1924 -348 323 -53 C ATOM 152 CG2 VAL A 68 -19.802 22.849 39.070 1.00 14.73 C ANISOU 152 CG2 VAL A 68 1089 2252 2256 -454 308 -24 C ATOM 153 N ARG A 69 -19.166 20.054 37.228 1.00 13.14 N ANISOU 153 N ARG A 69 954 1927 2111 -658 221 -167 N ATOM 154 CA ARG A 69 -19.906 18.813 37.047 1.00 14.68 C ANISOU 154 CA ARG A 69 1110 2076 2393 -768 218 -183 C ATOM 155 C ARG A 69 -18.927 17.691 36.720 1.00 15.42 C ANISOU 155 C ARG A 69 1297 2056 2504 -812 234 -254 C ATOM 156 O ARG A 69 -18.980 16.628 37.329 1.00 16.45 O ANISOU 156 O ARG A 69 1443 2094 2712 -867 287 -223 O ATOM 157 CB ARG A 69 -20.975 18.974 35.960 1.00 15.79 C ANISOU 157 CB ARG A 69 1157 2287 2555 -819 129 -225 C ATOM 158 CG ARG A 69 -21.666 17.706 35.588 1.00 17.58 C ANISOU 158 CG ARG A 69 1348 2464 2868 -946 108 -267 C ATOM 159 CD ARG A 69 -22.884 17.984 34.727 1.00 21.04 C ANISOU 159 CD ARG A 69 1666 2992 3336 -996 12 -282 C ATOM 160 NE ARG A 69 -23.630 16.751 34.504 1.00 37.73 N ANISOU 160 NE ARG A 69 3736 5055 5546 -1132 -9 -317 N ATOM 161 CZ ARG A 69 -24.799 16.680 33.877 1.00 48.74 C ANISOU 161 CZ ARG A 69 5010 6511 6998 -1209 -96 -327 C ATOM 162 NH1 ARG A 69 -25.374 17.778 33.403 1.00 56.15 N ANISOU 162 NH1 ARG A 69 5856 7563 7916 -1152 -168 -297 N ATOM 163 NH2 ARG A 69 -25.397 15.506 33.730 1.00 48.29 N ANISOU 163 NH2 ARG A 69 4920 6394 7032 -1343 -113 -364 N ATOM 164 N ASN A 70 -18.004 17.958 35.797 1.00 14.05 N ANISOU 164 N ASN A 70 1186 1887 2265 -780 198 -339 N ATOM 165 CA ASN A 70 -17.047 16.949 35.349 1.00 18.86 C ANISOU 165 CA ASN A 70 1878 2386 2901 -808 224 -421 C ATOM 166 C ASN A 70 -15.732 16.998 36.115 1.00 15.97 C ANISOU 166 C ASN A 70 1584 1951 2532 -735 286 -376 C ATOM 167 O ASN A 70 -14.930 16.072 36.041 1.00 14.88 O ANISOU 167 O ASN A 70 1504 1693 2455 -744 329 -412 O ATOM 168 CB ASN A 70 -16.777 17.107 33.853 1.00 23.68 C ANISOU 168 CB ASN A 70 2509 3050 3437 -823 163 -545 C ATOM 169 CG ASN A 70 -18.013 16.872 33.016 1.00 33.80 C ANISOU 169 CG ASN A 70 3723 4396 4725 -910 87 -595 C ATOM 170 OD1 ASN A 70 -18.735 15.893 33.214 1.00 43.54 O ANISOU 170 OD1 ASN A 70 4926 5561 6055 -996 94 -604 O ATOM 171 ND2 ASN A 70 -18.274 17.775 32.084 1.00 36.81 N ANISOU 171 ND2 ASN A 70 4074 4908 5006 -893 9 -618 N ATOM 172 N GLY A 71 -15.506 18.092 36.830 1.00 12.00 N ANISOU 172 N GLY A 71 1074 1520 1967 -659 291 -299 N ATOM 173 CA GLY A 71 -14.362 18.198 37.728 1.00 11.17 C ANISOU 173 CA GLY A 71 1023 1366 1855 -598 339 -237 C ATOM 174 C GLY A 71 -13.025 18.508 37.086 1.00 12.66 C ANISOU 174 C GLY A 71 1263 1537 2010 -548 331 -296 C ATOM 175 O GLY A 71 -11.993 18.175 37.654 1.00 11.20 O ANISOU 175 O GLY A 71 1117 1274 1863 -516 373 -255 O ATOM 176 N TYR A 72 -13.032 19.163 35.927 1.00 10.00 N ANISOU 176 N TYR A 72 917 1278 1603 -542 281 -377 N ATOM 177 CA TYR A 72 -11.785 19.606 35.324 1.00 9.28 C ANISOU 177 CA TYR A 72 863 1192 1470 -496 283 -423 C ATOM 178 C TYR A 72 -11.970 20.851 34.469 1.00 9.29 C ANISOU 178 C TYR A 72 841 1323 1364 -469 224 -443 C ATOM 179 O TYR A 72 -13.089 21.287 34.213 1.00 9.20 O ANISOU 179 O TYR A 72 785 1389 1323 -485 177 -428 O ATOM 180 CB TYR A 72 -11.168 18.466 34.502 1.00 10.84 C ANISOU 180 CB TYR A 72 1102 1293 1725 -531 321 -523 C ATOM 181 CG TYR A 72 -11.825 18.210 33.160 1.00 11.26 C ANISOU 181 CG TYR A 72 1148 1405 1724 -591 284 -632 C ATOM 182 CD1 TYR A 72 -11.388 18.872 32.015 1.00 17.36 C ANISOU 182 CD1 TYR A 72 1930 2275 2389 -578 259 -694 C ATOM 183 CD2 TYR A 72 -12.863 17.299 33.034 1.00 20.36 C ANISOU 183 CD2 TYR A 72 2284 2523 2930 -667 272 -664 C ATOM 184 CE1 TYR A 72 -11.972 18.649 30.790 1.00 21.57 C ANISOU 184 CE1 TYR A 72 2461 2882 2853 -636 219 -779 C ATOM 185 CE2 TYR A 72 -13.451 17.063 31.804 1.00 23.84 C ANISOU 185 CE2 TYR A 72 2716 3026 3315 -730 226 -764 C ATOM 186 CZ TYR A 72 -13.005 17.744 30.688 1.00 28.37 C ANISOU 186 CZ TYR A 72 3305 3708 3765 -712 197 -819 C ATOM 187 OH TYR A 72 -13.585 17.513 29.460 1.00 36.77 O ANISOU 187 OH TYR A 72 4367 4851 4754 -778 144 -909 O ATOM 188 N GLY A 73 -10.853 21.421 34.038 1.00 8.10 N ANISOU 188 N GLY A 73 714 1190 1172 -427 229 -462 N ATOM 189 CA GLY A 73 -10.873 22.589 33.185 1.00 7.76 C ANISOU 189 CA GLY A 73 653 1262 1035 -403 182 -462 C ATOM 190 C GLY A 73 -9.490 22.813 32.652 1.00 7.90 C ANISOU 190 C GLY A 73 694 1277 1031 -381 212 -498 C ATOM 191 O GLY A 73 -8.663 21.890 32.660 1.00 7.90 O ANISOU 191 O GLY A 73 728 1182 1091 -388 268 -549 O ATOM 192 N PHE A 74 -9.240 24.035 32.195 1.00 7.01 N ANISOU 192 N PHE A 74 563 1252 849 -343 181 -458 N ATOM 193 CA PHE A 74 -7.930 24.394 31.653 1.00 9.20 C ANISOU 193 CA PHE A 74 870 1527 1097 -298 215 -457 C ATOM 194 C PHE A 74 -7.523 25.758 32.142 1.00 9.00 C ANISOU 194 C PHE A 74 837 1510 1074 -228 188 -353 C ATOM 195 O PHE A 74 -8.375 26.648 32.311 1.00 6.56 O ANISOU 195 O PHE A 74 501 1243 748 -214 142 -298 O ATOM 196 CB PHE A 74 -7.940 24.378 30.131 1.00 8.74 C ANISOU 196 CB PHE A 74 830 1564 926 -335 209 -521 C ATOM 197 CG PHE A 74 -7.989 22.991 29.556 1.00 10.56 C ANISOU 197 CG PHE A 74 1098 1749 1166 -394 244 -641 C ATOM 198 CD1 PHE A 74 -6.824 22.308 29.259 1.00 13.67 C ANISOU 198 CD1 PHE A 74 1535 2055 1605 -365 316 -677 C ATOM 199 CD2 PHE A 74 -9.206 22.365 29.376 1.00 15.29 C ANISOU 199 CD2 PHE A 74 1680 2365 1764 -460 203 -679 C ATOM 200 CE1 PHE A 74 -6.885 21.007 28.753 1.00 15.13 C ANISOU 200 CE1 PHE A 74 1751 2174 1824 -408 355 -774 C ATOM 201 CE2 PHE A 74 -9.277 21.076 28.877 1.00 17.39 C ANISOU 201 CE2 PHE A 74 1982 2567 2061 -506 237 -773 C ATOM 202 CZ PHE A 74 -8.106 20.405 28.562 1.00 16.65 C ANISOU 202 CZ PHE A 74 1936 2386 2006 -481 316 -827 C ATOM 203 N ILE A 75 -6.213 25.906 32.352 1.00 7.51 N ANISOU 203 N ILE A 75 676 1258 921 -181 213 -322 N ATOM 204 CA ILE A 75 -5.582 27.153 32.763 1.00 5.40 C ANISOU 204 CA ILE A 75 408 974 671 -130 191 -239 C ATOM 205 C ILE A 75 -4.647 27.553 31.643 1.00 8.34 C ANISOU 205 C ILE A 75 780 1377 1013 -120 222 -228 C ATOM 206 O ILE A 75 -3.882 26.719 31.145 1.00 11.08 O ANISOU 206 O ILE A 75 1143 1702 1364 -122 269 -271 O ATOM 207 CB ILE A 75 -4.792 26.985 34.075 1.00 6.64 C ANISOU 207 CB ILE A 75 574 1053 896 -100 190 -210 C ATOM 208 CG1 ILE A 75 -5.712 26.583 35.232 1.00 7.22 C ANISOU 208 CG1 ILE A 75 649 1113 981 -112 175 -209 C ATOM 209 CG2 ILE A 75 -4.035 28.270 34.397 1.00 10.23 C ANISOU 209 CG2 ILE A 75 1017 1498 1371 -70 171 -155 C ATOM 210 CD1 ILE A 75 -4.944 26.024 36.425 1.00 8.38 C ANISOU 210 CD1 ILE A 75 791 1218 1176 -98 186 -189 C ATOM 211 N ASN A 76 -4.689 28.811 31.223 1.00 6.16 N ANISOU 211 N ASN A 76 483 1144 713 -107 211 -166 N ATOM 212 CA ASN A 76 -3.719 29.271 30.238 1.00 7.27 C ANISOU 212 CA ASN A 76 621 1312 829 -99 255 -132 C ATOM 213 C ASN A 76 -2.498 29.873 30.927 1.00 6.78 C ANISOU 213 C ASN A 76 542 1168 865 -69 269 -81 C ATOM 214 O ASN A 76 -2.618 30.842 31.681 1.00 7.41 O ANISOU 214 O ASN A 76 601 1214 1001 -60 238 -41 O ATOM 215 CB ASN A 76 -4.386 30.282 29.292 1.00 8.99 C ANISOU 215 CB ASN A 76 812 1640 963 -110 243 -66 C ATOM 216 CG ASN A 76 -3.513 30.636 28.112 1.00 11.07 C ANISOU 216 CG ASN A 76 1088 1952 1168 -111 298 -20 C ATOM 217 OD1 ASN A 76 -2.849 31.670 28.110 1.00 13.76 O ANISOU 217 OD1 ASN A 76 1404 2260 1564 -95 321 67 O ATOM 218 ND2 ASN A 76 -3.489 29.759 27.114 1.00 13.75 N ANISOU 218 ND2 ASN A 76 1466 2356 1402 -136 325 -85 N ATOM 219 N ARG A 77 -1.314 29.301 30.671 1.00 6.24 N ANISOU 219 N ARG A 77 472 1075 823 -54 315 -89 N ATOM 220 CA ARG A 77 -0.078 29.776 31.293 1.00 6.21 C ANISOU 220 CA ARG A 77 428 1032 900 -36 310 -40 C ATOM 221 C ARG A 77 0.234 31.185 30.829 1.00 10.66 C ANISOU 221 C ARG A 77 955 1626 1470 -49 319 30 C ATOM 222 O ARG A 77 0.234 31.446 29.642 1.00 8.85 O ANISOU 222 O ARG A 77 741 1400 1220 -62 393 41 O ATOM 223 CB ARG A 77 1.108 28.870 30.932 1.00 7.84 C ANISOU 223 CB ARG A 77 619 1233 1126 -16 359 -63 C ATOM 224 CG ARG A 77 1.050 27.524 31.616 1.00 10.42 C ANISOU 224 CG ARG A 77 962 1507 1488 -4 351 -120 C ATOM 225 CD ARG A 77 2.198 26.652 31.139 1.00 9.70 C ANISOU 225 CD ARG A 77 849 1395 1442 25 415 -143 C ATOM 226 NE ARG A 77 3.478 27.256 31.464 1.00 9.81 N ANISOU 226 NE ARG A 77 799 1408 1521 36 407 -91 N ATOM 227 CZ ARG A 77 4.612 26.570 31.530 1.00 14.54 C ANISOU 227 CZ ARG A 77 1353 1972 2201 68 441 -94 C ATOM 228 NH1 ARG A 77 4.592 25.259 31.304 1.00 17.27 N ANISOU 228 NH1 ARG A 77 1717 2269 2576 96 493 -145 N ATOM 229 NH2 ARG A 77 5.746 27.182 31.837 1.00 15.55 N ANISOU 229 NH2 ARG A 77 1413 2100 2393 68 426 -48 N ATOM 230 N ASN A 78 0.535 32.090 31.746 1.00 6.97 N ANISOU 230 N ASN A 78 464 1120 1063 -71 273 27 N ATOM 231 CA ASN A 78 0.826 33.449 31.290 1.00 10.21 C ANISOU 231 CA ASN A 78 855 1503 1523 -93 295 82 C ATOM 232 C ASN A 78 2.203 33.563 30.603 1.00 13.66 C ANISOU 232 C ASN A 78 1260 1944 1987 -105 347 113 C ATOM 233 O ASN A 78 2.418 34.476 29.799 1.00 15.81 O ANISOU 233 O ASN A 78 1521 2212 2273 -121 389 186 O ATOM 234 CB ASN A 78 0.728 34.432 32.457 1.00 11.06 C ANISOU 234 CB ASN A 78 952 1530 1720 -100 241 86 C ATOM 235 CG ASN A 78 -0.692 34.562 33.012 1.00 12.93 C ANISOU 235 CG ASN A 78 1209 1762 1940 -84 209 63 C ATOM 236 OD1 ASN A 78 -1.686 34.124 32.403 1.00 13.61 O ANISOU 236 OD1 ASN A 78 1308 1908 1957 -70 221 68 O ATOM 237 ND2 ASN A 78 -0.798 35.200 34.173 1.00 16.04 N ANISOU 237 ND2 ASN A 78 1599 2089 2405 -92 172 28 N ATOM 238 N ASP A 79 3.120 32.633 30.892 1.00 7.82 N ANISOU 238 N ASP A 79 502 1210 1261 -91 349 76 N ATOM 239 CA ASP A 79 4.473 32.698 30.347 1.00 10.33 C ANISOU 239 CA ASP A 79 772 1531 1622 -97 401 101 C ATOM 240 C ASP A 79 4.635 32.096 28.947 1.00 11.56 C ANISOU 240 C ASP A 79 933 1766 1692 -91 493 94 C ATOM 241 O ASP A 79 5.514 32.506 28.193 1.00 17.76 O ANISOU 241 O ASP A 79 1685 2569 2493 -107 558 132 O ATOM 242 CB ASP A 79 5.475 32.045 31.326 1.00 11.28 C ANISOU 242 CB ASP A 79 851 1615 1818 -78 365 78 C ATOM 243 CG ASP A 79 5.162 30.565 31.644 1.00 13.55 C ANISOU 243 CG ASP A 79 1163 1910 2076 -36 359 31 C ATOM 244 OD1 ASP A 79 4.076 30.064 31.313 1.00 10.87 O ANISOU 244 OD1 ASP A 79 877 1595 1660 -25 367 5 O ATOM 245 OD2 ASP A 79 6.027 29.899 32.262 1.00 19.90 O ANISOU 245 OD2 ASP A 79 1926 2686 2950 -13 346 27 O ATOM 246 N THR A 80 3.805 31.120 28.597 1.00 9.26 N ANISOU 246 N THR A 80 682 1529 1308 -70 502 48 N ATOM 247 CA THR A 80 3.944 30.487 27.294 1.00 10.25 C ANISOU 247 CA THR A 80 822 1739 1335 -55 586 35 C ATOM 248 C THR A 80 2.674 30.560 26.456 1.00 10.35 C ANISOU 248 C THR A 80 935 1715 1283 -24 631 86 C ATOM 249 O THR A 80 2.693 30.232 25.273 1.00 11.87 O ANISOU 249 O THR A 80 1174 1958 1379 -32 722 58 O ATOM 250 CB THR A 80 4.335 29.016 27.446 1.00 10.45 C ANISOU 250 CB THR A 80 854 1726 1390 5 617 -22 C ATOM 251 OG1 THR A 80 3.296 28.334 28.155 1.00 9.56 O ANISOU 251 OG1 THR A 80 796 1554 1283 15 563 -66 O ATOM 252 CG2 THR A 80 5.664 28.891 28.212 1.00 10.69 C ANISOU 252 CG2 THR A 80 818 1690 1553 14 608 -23 C ATOM 253 N LYS A 81 1.585 30.972 27.100 1.00 9.40 N ANISOU 253 N LYS A 81 836 1561 1174 -67 573 54 N ATOM 254 CA LYS A 81 0.261 31.082 26.497 1.00 14.14 C ANISOU 254 CA LYS A 81 1477 2262 1631 -86 532 57 C ATOM 255 C LYS A 81 -0.308 29.722 26.082 1.00 15.00 C ANISOU 255 C LYS A 81 1637 2420 1641 -86 526 -47 C ATOM 256 O LYS A 81 -1.223 29.667 25.264 1.00 13.70 O ANISOU 256 O LYS A 81 1507 2361 1338 -117 497 -63 O ATOM 257 CB LYS A 81 0.295 32.036 25.299 1.00 13.51 C ANISOU 257 CB LYS A 81 1408 2271 1455 -109 565 152 C ATOM 258 CG LYS A 81 0.827 33.428 25.623 1.00 15.09 C ANISOU 258 CG LYS A 81 1557 2418 1759 -119 558 261 C ATOM 259 CD LYS A 81 0.224 34.013 26.899 1.00 23.24 C ANISOU 259 CD LYS A 81 2556 3377 2899 -107 472 277 C ATOM 260 CE LYS A 81 0.766 35.420 27.176 1.00 28.44 C ANISOU 260 CE LYS A 81 3173 3956 3678 -114 467 380 C ATOM 261 NZ LYS A 81 0.396 35.973 28.529 1.00 18.56 N ANISOU 261 NZ LYS A 81 1897 2602 2551 -106 399 362 N ATOM 262 N GLU A 82 0.217 28.632 26.649 1.00 9.64 N ANISOU 262 N GLU A 82 955 1672 1036 -59 540 -118 N ATOM 263 CA GLU A 82 -0.344 27.290 26.387 1.00 9.83 C ANISOU 263 CA GLU A 82 1025 1704 1006 -77 536 -239 C ATOM 264 C GLU A 82 -1.310 26.870 27.472 1.00 10.09 C ANISOU 264 C GLU A 82 1056 1692 1087 -97 458 -278 C ATOM 265 O GLU A 82 -1.101 27.172 28.634 1.00 9.04 O ANISOU 265 O GLU A 82 891 1492 1053 -74 423 -232 O ATOM 266 CB GLU A 82 0.758 26.227 26.291 1.00 12.41 C ANISOU 266 CB GLU A 82 1349 1973 1396 -41 609 -297 C ATOM 267 CG GLU A 82 1.615 26.321 25.058 1.00 15.41 C ANISOU 267 CG GLU A 82 1735 2413 1707 -22 706 -290 C ATOM 268 CD GLU A 82 0.886 25.905 23.799 1.00 29.74 C ANISOU 268 CD GLU A 82 3625 4316 3358 -65 727 -374 C ATOM 269 OE1 GLU A 82 0.013 25.020 23.881 1.00 26.56 O ANISOU 269 OE1 GLU A 82 3258 3899 2935 -105 684 -478 O ATOM 270 OE2 GLU A 82 1.187 26.462 22.722 1.00 40.44 O ANISOU 270 OE2 GLU A 82 5002 5760 4604 -65 785 -333 O ATOM 271 N ASP A 83 -2.345 26.129 27.092 1.00 9.29 N ANISOU 271 N ASP A 83 986 1630 912 -144 433 -366 N ATOM 272 CA ASP A 83 -3.309 25.628 28.071 1.00 9.88 C ANISOU 272 CA ASP A 83 1051 1665 1037 -170 378 -404 C ATOM 273 C ASP A 83 -2.716 24.434 28.805 1.00 11.48 C ANISOU 273 C ASP A 83 1259 1744 1358 -151 416 -453 C ATOM 274 O ASP A 83 -1.997 23.616 28.215 1.00 11.29 O ANISOU 274 O ASP A 83 1256 1684 1351 -140 481 -510 O ATOM 275 CB ASP A 83 -4.608 25.180 27.401 1.00 13.00 C ANISOU 275 CB ASP A 83 1460 2148 1330 -240 339 -481 C ATOM 276 CG ASP A 83 -5.454 26.327 26.897 1.00 23.35 C ANISOU 276 CG ASP A 83 2745 3597 2529 -257 276 -410 C ATOM 277 OD1 ASP A 83 -5.163 27.499 27.222 1.00 17.78 O ANISOU 277 OD1 ASP A 83 2011 2899 1845 -214 269 -301 O ATOM 278 OD2 ASP A 83 -6.428 26.032 26.171 1.00 23.31 O ANISOU 278 OD2 ASP A 83 2744 3689 2426 -313 228 -456 O ATOM 279 N VAL A 84 -3.015 24.358 30.091 1.00 7.73 N ANISOU 279 N VAL A 84 763 1209 964 -142 380 -422 N ATOM 280 CA AVAL A 84 -2.662 23.247 30.951 0.48 11.11 C ANISOU 280 CA AVAL A 84 1189 1527 1506 -126 409 -446 C ATOM 281 CA BVAL A 84 -2.686 23.176 30.871 0.52 7.71 C ANISOU 281 CA BVAL A 84 760 1096 1073 -129 413 -454 C ATOM 282 C VAL A 84 -3.946 22.640 31.544 1.00 8.07 C ANISOU 282 C VAL A 84 806 1123 1135 -178 391 -492 C ATOM 283 O VAL A 84 -4.791 23.376 32.071 1.00 8.58 O ANISOU 283 O VAL A 84 852 1244 1165 -192 337 -449 O ATOM 284 CB AVAL A 84 -1.732 23.718 32.086 0.48 10.71 C ANISOU 284 CB AVAL A 84 1102 1432 1535 -69 387 -348 C ATOM 285 CB BVAL A 84 -1.594 23.434 31.942 0.52 12.24 C ANISOU 285 CB BVAL A 84 1299 1612 1741 -67 404 -364 C ATOM 286 CG1AVAL A 84 -1.281 22.558 32.916 0.48 13.49 C ANISOU 286 CG1AVAL A 84 1439 1679 2008 -42 420 -350 C ATOM 287 CG1BVAL A 84 -0.249 23.737 31.282 0.52 12.35 C ANISOU 287 CG1BVAL A 84 1294 1634 1765 -26 443 -337 C ATOM 288 CG2AVAL A 84 -0.530 24.451 31.515 0.48 10.61 C ANISOU 288 CG2AVAL A 84 1068 1448 1514 -32 405 -301 C ATOM 289 CG2BVAL A 84 -2.007 24.533 32.903 0.52 9.24 C ANISOU 289 CG2BVAL A 84 901 1269 1341 -64 331 -288 C ATOM 290 N PHE A 85 -4.098 21.329 31.464 1.00 8.34 N ANISOU 290 N PHE A 85 860 1074 1236 -205 442 -573 N ATOM 291 CA PHE A 85 -5.227 20.639 32.083 1.00 8.46 C ANISOU 291 CA PHE A 85 877 1045 1294 -260 440 -615 C ATOM 292 C PHE A 85 -5.190 20.810 33.584 1.00 9.11 C ANISOU 292 C PHE A 85 935 1083 1443 -222 406 -487 C ATOM 293 O PHE A 85 -4.117 20.773 34.169 1.00 12.02 O ANISOU 293 O PHE A 85 1290 1398 1879 -155 422 -421 O ATOM 294 CB PHE A 85 -5.149 19.164 31.714 1.00 9.78 C ANISOU 294 CB PHE A 85 1075 1093 1550 -288 497 -694 C ATOM 295 CG PHE A 85 -6.170 18.290 32.380 1.00 10.21 C ANISOU 295 CG PHE A 85 1132 1065 1684 -347 492 -702 C ATOM 296 CD1 PHE A 85 -7.431 18.141 31.838 1.00 14.00 C ANISOU 296 CD1 PHE A 85 1608 1617 2094 -429 448 -754 C ATOM 297 CD2 PHE A 85 -5.834 17.553 33.504 1.00 11.25 C ANISOU 297 CD2 PHE A 85 1264 1048 1963 -315 527 -628 C ATOM 298 CE1 PHE A 85 -8.350 17.281 32.413 1.00 13.79 C ANISOU 298 CE1 PHE A 85 1577 1518 2145 -478 444 -741 C ATOM 299 CE2 PHE A 85 -6.761 16.696 34.094 1.00 13.81 C ANISOU 299 CE2 PHE A 85 1589 1303 2356 -368 524 -597 C ATOM 300 CZ PHE A 85 -8.015 16.573 33.558 1.00 13.60 C ANISOU 300 CZ PHE A 85 1557 1349 2260 -449 487 -659 C ATOM 301 N VAL A 86 -6.343 21.033 34.216 1.00 7.83 N ANISOU 301 N VAL A 86 761 959 1256 -264 360 -449 N ATOM 302 CA VAL A 86 -6.391 21.035 35.672 1.00 7.05 C ANISOU 302 CA VAL A 86 653 828 1199 -238 344 -340 C ATOM 303 C VAL A 86 -7.573 20.197 36.154 1.00 11.08 C ANISOU 303 C VAL A 86 1162 1295 1752 -306 357 -337 C ATOM 304 O VAL A 86 -8.716 20.398 35.722 1.00 10.47 O ANISOU 304 O VAL A 86 1063 1284 1633 -368 336 -384 O ATOM 305 CB VAL A 86 -6.485 22.467 36.263 1.00 7.50 C ANISOU 305 CB VAL A 86 689 986 1176 -207 292 -277 C ATOM 306 CG1 VAL A 86 -7.636 23.265 35.634 1.00 8.01 C ANISOU 306 CG1 VAL A 86 739 1142 1161 -237 254 -309 C ATOM 307 CG2 VAL A 86 -6.623 22.406 37.777 1.00 11.85 C ANISOU 307 CG2 VAL A 86 1243 1524 1735 -193 282 -187 C ATOM 308 N HIS A 87 -7.277 19.230 37.013 1.00 8.45 N ANISOU 308 N HIS A 87 844 851 1513 -295 391 -268 N ATOM 309 CA HIS A 87 -8.303 18.405 37.629 1.00 9.00 C ANISOU 309 CA HIS A 87 911 866 1642 -362 418 -233 C ATOM 310 C HIS A 87 -8.611 18.945 39.019 1.00 8.65 C ANISOU 310 C HIS A 87 859 891 1539 -340 403 -106 C ATOM 311 O HIS A 87 -7.746 19.533 39.645 1.00 10.67 O ANISOU 311 O HIS A 87 1125 1185 1744 -271 373 -40 O ATOM 312 CB HIS A 87 -7.841 16.956 37.721 1.00 12.85 C ANISOU 312 CB HIS A 87 1426 1175 2283 -365 478 -217 C ATOM 313 CG HIS A 87 -8.920 16.033 38.159 1.00 15.94 C ANISOU 313 CG HIS A 87 1819 1513 2725 -426 497 -184 C ATOM 314 ND1 HIS A 87 -9.022 15.543 39.448 1.00 22.35 N ANISOU 314 ND1 HIS A 87 2637 2277 3580 -418 519 -29 N ATOM 315 CD2 HIS A 87 -9.988 15.541 37.487 1.00 15.82 C ANISOU 315 CD2 HIS A 87 1797 1503 2712 -498 489 -274 C ATOM 316 CE1 HIS A 87 -10.087 14.774 39.540 1.00 24.62 C ANISOU 316 CE1 HIS A 87 2920 2531 3906 -484 534 -30 C ATOM 317 NE2 HIS A 87 -10.690 14.755 38.361 1.00 18.02 N ANISOU 317 NE2 HIS A 87 2071 1721 3054 -536 513 -180 N ATOM 318 N GLN A 88 -9.830 18.725 39.515 1.00 9.11 N ANISOU 318 N GLN A 88 898 971 1593 -399 421 -77 N ATOM 319 CA GLN A 88 -10.219 19.248 40.826 1.00 9.45 C ANISOU 319 CA GLN A 88 934 1092 1563 -388 433 27 C ATOM 320 C GLN A 88 -9.282 18.817 41.969 1.00 12.87 C ANISOU 320 C GLN A 88 1410 1487 1995 -336 438 162 C ATOM 321 O GLN A 88 -9.046 19.599 42.896 1.00 12.99 O ANISOU 321 O GLN A 88 1440 1601 1896 -296 414 218 O ATOM 322 CB GLN A 88 -11.677 18.845 41.145 1.00 10.37 C ANISOU 322 CB GLN A 88 1024 1232 1683 -444 450 47 C ATOM 323 CG GLN A 88 -11.939 17.364 41.088 1.00 16.33 C ANISOU 323 CG GLN A 88 1791 1857 2556 -500 484 72 C ATOM 324 CD GLN A 88 -13.420 17.060 41.005 1.00 17.18 C ANISOU 324 CD GLN A 88 1851 1996 2680 -569 487 57 C ATOM 325 OE1 GLN A 88 -14.268 17.955 41.196 1.00 17.45 O ANISOU 325 OE1 GLN A 88 1838 2150 2641 -562 472 56 O ATOM 326 NE2 GLN A 88 -13.747 15.803 40.700 1.00 19.32 N ANISOU 326 NE2 GLN A 88 2127 2152 3062 -630 507 44 N ATOM 327 N THR A 89 -8.740 17.599 41.909 1.00 12.53 N ANISOU 327 N THR A 89 1385 1299 2075 -333 464 213 N ATOM 328 CA THR A 89 -7.885 17.109 42.994 1.00 14.59 C ANISOU 328 CA THR A 89 1674 1526 2344 -277 455 374 C ATOM 329 C THR A 89 -6.539 17.841 43.087 1.00 15.31 C ANISOU 329 C THR A 89 1766 1676 2375 -189 379 384 C ATOM 330 O THR A 89 -5.844 17.736 44.101 1.00 18.06 O ANISOU 330 O THR A 89 2126 2053 2684 -143 340 519 O ATOM 331 CB THR A 89 -7.613 15.595 42.863 1.00 12.68 C ANISOU 331 CB THR A 89 1442 1086 2291 -283 508 441 C ATOM 332 OG1 THR A 89 -6.975 15.303 41.614 1.00 17.12 O ANISOU 332 OG1 THR A 89 1997 1547 2962 -261 514 311 O ATOM 333 CG2 THR A 89 -8.903 14.813 42.945 1.00 19.01 C ANISOU 333 CG2 THR A 89 2245 1846 3132 -367 555 431 C ATOM 334 N ALA A 90 -6.183 18.582 42.046 1.00 11.08 N ANISOU 334 N ALA A 90 1212 1168 1829 -173 353 251 N ATOM 335 CA ALA A 90 -4.912 19.316 42.010 1.00 10.69 C ANISOU 335 CA ALA A 90 1147 1168 1747 -104 289 251 C ATOM 336 C ALA A 90 -5.009 20.692 42.656 1.00 14.39 C ANISOU 336 C ALA A 90 1620 1786 2060 -103 233 239 C ATOM 337 O ALA A 90 -4.005 21.396 42.822 1.00 14.36 O ANISOU 337 O ALA A 90 1600 1832 2024 -64 171 242 O ATOM 338 CB ALA A 90 -4.439 19.460 40.557 1.00 15.21 C ANISOU 338 CB ALA A 90 1700 1698 2383 -91 306 123 C ATOM 339 N ILE A 91 -6.228 21.092 42.979 1.00 9.74 N ANISOU 339 N ILE A 91 1046 1262 1395 -151 263 212 N ATOM 340 CA ILE A 91 -6.488 22.403 43.558 1.00 10.01 C ANISOU 340 CA ILE A 91 1087 1418 1298 -151 235 174 C ATOM 341 C ILE A 91 -6.425 22.380 45.082 1.00 15.96 C ANISOU 341 C ILE A 91 1877 2249 1937 -149 220 272 C ATOM 342 O ILE A 91 -7.060 21.534 45.733 1.00 16.80 O ANISOU 342 O ILE A 91 2002 2348 2035 -176 271 363 O ATOM 343 CB ILE A 91 -7.864 22.912 43.086 1.00 10.16 C ANISOU 343 CB ILE A 91 1087 1470 1303 -190 285 92 C ATOM 344 CG1 ILE A 91 -7.907 22.909 41.550 1.00 7.84 C ANISOU 344 CG1 ILE A 91 761 1126 1091 -198 283 5 C ATOM 345 CG2 ILE A 91 -8.159 24.272 43.644 1.00 10.26 C ANISOU 345 CG2 ILE A 91 1105 1579 1214 -177 276 42 C ATOM 346 CD1 ILE A 91 -9.326 23.101 40.997 1.00 11.97 C ANISOU 346 CD1 ILE A 91 1246 1681 1622 -243 317 -51 C ATOM 347 N LYS A 92 -5.662 23.299 45.670 1.00 13.98 N ANISOU 347 N LYS A 92 1638 2080 1592 -127 150 255 N ATOM 348 CA LYS A 92 -5.534 23.288 47.124 1.00 16.29 C ANISOU 348 CA LYS A 92 1975 2475 1741 -133 122 338 C ATOM 349 C LYS A 92 -6.805 23.824 47.783 1.00 21.66 C ANISOU 349 C LYS A 92 2687 3240 2302 -168 201 290 C ATOM 350 O LYS A 92 -7.459 24.703 47.235 1.00 26.04 O ANISOU 350 O LYS A 92 3224 3794 2875 -172 239 168 O ATOM 351 CB LYS A 92 -4.300 24.077 47.563 1.00 24.61 C ANISOU 351 CB LYS A 92 3026 3599 2727 -115 10 318 C ATOM 352 CG LYS A 92 -3.005 23.331 47.264 1.00 36.38 C ANISOU 352 CG LYS A 92 4468 5027 4327 -74 -64 415 C ATOM 353 CD LYS A 92 -1.797 23.955 47.947 1.00 49.61 C ANISOU 353 CD LYS A 92 6124 6796 5928 -68 -191 427 C ATOM 354 CE LYS A 92 -2.024 24.151 49.436 1.00 54.67 C ANISOU 354 CE LYS A 92 6829 7589 6355 -100 -234 472 C ATOM 355 NZ LYS A 92 -0.892 24.890 50.064 1.00 56.52 N ANISOU 355 NZ LYS A 92 7042 7930 6502 -116 -376 449 N ATOM 356 N LYS A 93 -7.153 23.287 48.954 1.00 37.91 N ANISOU 356 N LYS A 93 4788 5373 4243 -187 233 396 N ATOM 357 CA LYS A 93 -8.447 23.581 49.579 1.00 49.90 C ANISOU 357 CA LYS A 93 6329 6969 5663 -219 342 365 C ATOM 358 C LYS A 93 -8.690 25.084 49.769 1.00 57.83 C ANISOU 358 C LYS A 93 7346 8049 6576 -213 352 198 C ATOM 359 O LYS A 93 -7.809 25.829 50.212 1.00 54.97 O ANISOU 359 O LYS A 93 7019 7746 6122 -205 268 141 O ATOM 360 CB LYS A 93 -8.580 22.851 50.923 1.00 55.09 C ANISOU 360 CB LYS A 93 7042 7701 6188 -235 367 508 C ATOM 361 CG LYS A 93 -7.731 23.402 52.057 1.00 62.39 C ANISOU 361 CG LYS A 93 8030 8744 6931 -223 274 502 C ATOM 362 CD LYS A 93 -8.108 22.757 53.387 1.00 66.23 C ANISOU 362 CD LYS A 93 8579 9285 7298 -233 313 613 C ATOM 363 CE LYS A 93 -8.318 23.805 54.475 1.00 66.44 C ANISOU 363 CE LYS A 93 8676 9426 7143 -236 323 492 C ATOM 364 NZ LYS A 93 -7.033 24.326 55.020 1.00 66.64 N ANISOU 364 NZ LYS A 93 8731 9537 7054 -232 175 467 N ATOM 365 N ASN A 94 -9.897 25.516 49.408 1.00 66.38 N ANISOU 365 N ASN A 94 8398 9087 7735 -206 439 114 N ATOM 366 CA ASN A 94 -10.268 26.927 49.417 1.00 74.06 C ANISOU 366 CA ASN A 94 9374 10058 8709 -175 452 -35 C ATOM 367 C ASN A 94 -10.514 27.395 50.844 1.00 75.24 C ANISOU 367 C ASN A 94 9595 10283 8709 -170 487 -65 C ATOM 368 O ASN A 94 -10.739 26.582 51.740 1.00 76.62 O ANISOU 368 O ASN A 94 9810 10511 8793 -187 524 33 O ATOM 369 CB ASN A 94 -11.506 27.148 48.527 1.00 81.60 C ANISOU 369 CB ASN A 94 10257 10935 9812 -154 515 -71 C ATOM 370 CG ASN A 94 -12.065 28.571 48.599 1.00 91.02 C ANISOU 370 CG ASN A 94 11445 12113 11027 -110 542 -184 C ATOM 371 OD1 ASN A 94 -12.398 29.085 49.669 1.00 96.66 O ANISOU 371 OD1 ASN A 94 12206 12873 11650 -96 594 -225 O ATOM 372 ND2 ASN A 94 -12.167 29.213 47.440 1.00 92.59 N ANISOU 372 ND2 ASN A 94 11588 12243 11348 -85 510 -228 N ATOM 373 N LYS A 98 -20.433 22.980 48.972 1.00 56.30 N ANISOU 373 N LYS A 98 6534 7791 7068 -296 975 350 N ATOM 374 CA LYS A 98 -19.155 23.654 49.160 1.00 52.74 C ANISOU 374 CA LYS A 98 6212 7279 6550 -235 969 290 C ATOM 375 C LYS A 98 -18.171 22.931 48.240 1.00 41.87 C ANISOU 375 C LYS A 98 4859 5826 5224 -280 872 297 C ATOM 376 O LYS A 98 -17.718 21.830 48.546 1.00 23.58 O ANISOU 376 O LYS A 98 2581 3472 2907 -327 878 379 O ATOM 377 CB LYS A 98 -18.724 23.599 50.639 1.00 54.68 C ANISOU 377 CB LYS A 98 6582 7539 6655 -226 1072 315 C ATOM 378 CG LYS A 98 -17.237 23.850 50.994 1.00 51.60 C ANISOU 378 CG LYS A 98 6323 7152 6129 -227 1026 277 C ATOM 379 CD LYS A 98 -16.597 24.895 50.077 1.00 54.37 C ANISOU 379 CD LYS A 98 6658 7497 6501 -183 922 174 C ATOM 380 CE LYS A 98 -15.116 25.059 50.282 1.00 57.92 C ANISOU 380 CE LYS A 98 7204 7963 6841 -190 834 147 C ATOM 381 NZ LYS A 98 -14.607 26.220 49.489 1.00 55.62 N ANISOU 381 NZ LYS A 98 6897 7652 6583 -151 750 33 N ATOM 382 N TYR A 99 -17.876 23.548 47.098 1.00 38.86 N ANISOU 382 N TYR A 99 4453 5419 4894 -263 789 218 N ATOM 383 CA TYR A 99 -16.938 22.986 46.130 1.00 27.04 C ANISOU 383 CA TYR A 99 2976 3858 3440 -298 702 206 C ATOM 384 C TYR A 99 -15.530 23.224 46.632 1.00 38.95 C ANISOU 384 C TYR A 99 4589 5359 4850 -274 688 193 C ATOM 385 O TYR A 99 -14.849 24.138 46.177 1.00 35.06 O ANISOU 385 O TYR A 99 4122 4868 4331 -238 625 113 O ATOM 386 CB TYR A 99 -17.164 23.593 44.736 1.00 24.92 C ANISOU 386 CB TYR A 99 2659 3566 3244 -286 616 124 C ATOM 387 CG TYR A 99 -18.573 23.392 44.195 1.00 33.59 C ANISOU 387 CG TYR A 99 3650 4684 4431 -318 618 138 C ATOM 388 CD1 TYR A 99 -19.524 24.409 44.266 1.00 35.40 C ANISOU 388 CD1 TYR A 99 3814 4963 4675 -266 645 124 C ATOM 389 CD2 TYR A 99 -18.951 22.181 43.620 1.00 31.03 C ANISOU 389 CD2 TYR A 99 3283 4327 4179 -406 591 162 C ATOM 390 CE1 TYR A 99 -20.821 24.215 43.779 1.00 35.05 C ANISOU 390 CE1 TYR A 99 3655 4950 4713 -298 641 149 C ATOM 391 CE2 TYR A 99 -20.244 21.979 43.128 1.00 23.38 C ANISOU 391 CE2 TYR A 99 2208 3385 3290 -450 583 171 C ATOM 392 CZ TYR A 99 -21.168 22.999 43.211 1.00 34.99 C ANISOU 392 CZ TYR A 99 3604 4920 4771 -395 606 172 C ATOM 393 OH TYR A 99 -22.436 22.781 42.722 1.00 32.36 O ANISOU 393 OH TYR A 99 3156 4622 4517 -440 589 190 O ATOM 394 N LEU A 100 -15.106 22.380 47.570 1.00 53.27 N ANISOU 394 N LEU A 100 6466 7164 6610 -304 742 279 N ATOM 395 CA LEU A 100 -13.859 22.589 48.303 1.00 59.08 C ANISOU 395 CA LEU A 100 7302 7939 7207 -297 713 287 C ATOM 396 C LEU A 100 -12.642 22.699 47.388 1.00 59.42 C ANISOU 396 C LEU A 100 7347 7954 7275 -291 612 256 C ATOM 397 O LEU A 100 -11.627 23.321 47.744 1.00 65.06 O ANISOU 397 O LEU A 100 8108 8729 7884 -264 555 238 O ATOM 398 CB LEU A 100 -13.687 21.474 49.357 1.00 57.56 C ANISOU 398 CB LEU A 100 7175 7748 6947 -348 758 416 C ATOM 399 CG LEU A 100 -12.443 21.537 50.225 1.00 59.05 C ANISOU 399 CG LEU A 100 7444 8011 6981 -322 690 487 C ATOM 400 CD1 LEU A 100 -12.362 22.902 50.887 1.00 58.90 C ANISOU 400 CD1 LEU A 100 7464 8099 6817 -275 681 383 C ATOM 401 CD2 LEU A 100 -12.473 20.442 51.288 1.00 68.76 C ANISOU 401 CD2 LEU A 100 8728 9246 8154 -355 726 645 C ATOM 402 N ARG A 101 -12.727 22.095 46.211 1.00 29.67 N ANISOU 402 N ARG A 101 3524 4102 3646 -317 589 246 N ATOM 403 CA ARG A 101 -11.658 22.261 45.243 1.00 31.53 C ANISOU 403 CA ARG A 101 3760 4306 3914 -311 514 196 C ATOM 404 C ARG A 101 -12.267 22.695 43.913 1.00 24.91 C ANISOU 404 C ARG A 101 2866 3435 3165 -299 471 96 C ATOM 405 O ARG A 101 -12.872 21.911 43.184 1.00 22.23 O ANISOU 405 O ARG A 101 2490 3042 2915 -340 465 92 O ATOM 406 CB ARG A 101 -10.839 20.972 45.132 1.00 20.23 C ANISOU 406 CB ARG A 101 2358 2770 2561 -325 494 286 C ATOM 407 CG ARG A 101 -10.182 20.606 46.448 1.00 22.43 C ANISOU 407 CG ARG A 101 2695 3084 2744 -303 488 421 C ATOM 408 CD ARG A 101 -9.388 19.314 46.359 1.00 19.37 C ANISOU 408 CD ARG A 101 2323 2569 2466 -295 468 534 C ATOM 409 NE ARG A 101 -9.051 18.782 47.683 1.00 18.89 N ANISOU 409 NE ARG A 101 2307 2549 2320 -284 471 710 N ATOM 410 CZ ARG A 101 -7.852 18.914 48.234 1.00 36.37 C ANISOU 410 CZ ARG A 101 4550 4806 4463 -227 382 782 C ATOM 411 NH1 ARG A 101 -6.909 19.575 47.579 1.00 29.30 N ANISOU 411 NH1 ARG A 101 3635 3907 3589 -182 299 684 N ATOM 412 NH2 ARG A 101 -7.594 18.406 49.433 1.00 33.94 N ANISOU 412 NH2 ARG A 101 4281 4556 4060 -220 373 961 N ATOM 413 N SER A 102 -12.124 23.981 43.629 1.00 17.15 N ANISOU 413 N SER A 102 1883 2488 2144 -247 430 23 N ATOM 414 CA SER A 102 -12.558 24.531 42.364 1.00 9.20 C ANISOU 414 CA SER A 102 840 1463 1194 -229 377 -39 C ATOM 415 C SER A 102 -11.831 25.834 42.159 1.00 9.68 C ANISOU 415 C SER A 102 922 1539 1219 -178 335 -88 C ATOM 416 O SER A 102 -11.274 26.386 43.106 1.00 11.30 O ANISOU 416 O SER A 102 1160 1778 1356 -160 350 -95 O ATOM 417 CB SER A 102 -14.075 24.760 42.332 1.00 13.60 C ANISOU 417 CB SER A 102 1341 2044 1784 -230 401 -35 C ATOM 418 OG SER A 102 -14.455 25.749 43.278 1.00 18.35 O ANISOU 418 OG SER A 102 1947 2688 2337 -185 445 -41 O ATOM 419 N VAL A 103 -11.790 26.274 40.910 1.00 9.43 N ANISOU 419 N VAL A 103 873 1486 1222 -164 282 -119 N ATOM 420 CA VAL A 103 -11.314 27.607 40.564 1.00 7.72 C ANISOU 420 CA VAL A 103 665 1270 997 -119 249 -148 C ATOM 421 C VAL A 103 -12.396 28.248 39.716 1.00 9.28 C ANISOU 421 C VAL A 103 816 1478 1233 -103 235 -144 C ATOM 422 O VAL A 103 -13.274 27.546 39.198 1.00 10.41 O ANISOU 422 O VAL A 103 921 1634 1401 -133 232 -133 O ATOM 423 CB VAL A 103 -9.964 27.571 39.804 1.00 7.69 C ANISOU 423 CB VAL A 103 684 1241 996 -117 208 -158 C ATOM 424 CG1 VAL A 103 -8.823 27.166 40.747 1.00 7.42 C ANISOU 424 CG1 VAL A 103 670 1215 935 -125 221 -153 C ATOM 425 CG2 VAL A 103 -10.039 26.628 38.615 1.00 9.58 C ANISOU 425 CG2 VAL A 103 916 1465 1260 -147 192 -163 C ATOM 426 N GLY A 104 -12.338 29.569 39.559 1.00 7.55 N ANISOU 426 N GLY A 104 587 1254 1028 -59 229 -151 N ATOM 427 CA GLY A 104 -13.371 30.273 38.812 1.00 7.31 C ANISOU 427 CA GLY A 104 491 1238 1046 -33 222 -126 C ATOM 428 C GLY A 104 -12.844 30.754 37.481 1.00 6.17 C ANISOU 428 C GLY A 104 337 1094 912 -25 173 -108 C ATOM 429 O GLY A 104 -11.664 31.107 37.368 1.00 7.40 O ANISOU 429 O GLY A 104 534 1226 1053 -18 162 -118 O ATOM 430 N ASP A 105 -13.705 30.784 36.469 1.00 7.65 N ANISOU 430 N ASP A 105 460 1319 1126 -30 141 -78 N ATOM 431 CA ASP A 105 -13.301 31.240 35.140 1.00 8.88 C ANISOU 431 CA ASP A 105 598 1506 1272 -25 93 -56 C ATOM 432 C ASP A 105 -12.766 32.674 35.235 1.00 7.71 C ANISOU 432 C ASP A 105 438 1314 1179 33 110 -28 C ATOM 433 O ASP A 105 -13.427 33.535 35.819 1.00 8.66 O ANISOU 433 O ASP A 105 512 1399 1378 81 145 -14 O ATOM 434 CB ASP A 105 -14.470 31.223 34.155 1.00 8.67 C ANISOU 434 CB ASP A 105 488 1553 1253 -35 41 -25 C ATOM 435 CG ASP A 105 -15.067 29.836 33.919 1.00 12.42 C ANISOU 435 CG ASP A 105 958 2074 1689 -106 20 -62 C ATOM 436 OD1 ASP A 105 -14.735 28.859 34.615 1.00 12.23 O ANISOU 436 OD1 ASP A 105 986 2010 1650 -141 55 -105 O ATOM 437 OD2 ASP A 105 -15.923 29.756 33.024 1.00 15.40 O ANISOU 437 OD2 ASP A 105 1270 2525 2056 -128 -38 -44 O ATOM 438 N GLY A 106 -11.592 32.921 34.667 1.00 7.96 N ANISOU 438 N GLY A 106 500 1341 1182 29 97 -21 N ATOM 439 CA GLY A 106 -11.020 34.265 34.619 1.00 10.23 C ANISOU 439 CA GLY A 106 765 1588 1534 76 112 3 C ATOM 440 C GLY A 106 -10.087 34.573 35.779 1.00 11.68 C ANISOU 440 C GLY A 106 1002 1713 1722 82 150 -40 C ATOM 441 O GLY A 106 -9.394 35.589 35.767 1.00 10.62 O ANISOU 441 O GLY A 106 867 1508 1658 101 161 -37 O ATOM 442 N GLU A 107 -10.083 33.708 36.790 1.00 7.84 N ANISOU 442 N GLU A 107 569 1218 1190 52 162 -97 N ATOM 443 CA GLU A 107 -9.230 33.874 37.979 1.00 8.03 C ANISOU 443 CA GLU A 107 640 1199 1213 40 180 -169 C ATOM 444 C GLU A 107 -7.743 33.688 37.654 1.00 8.56 C ANISOU 444 C GLU A 107 728 1251 1273 11 156 -170 C ATOM 445 O GLU A 107 -7.416 32.845 36.826 1.00 9.27 O ANISOU 445 O GLU A 107 829 1369 1323 -8 137 -132 O ATOM 446 CB GLU A 107 -9.671 32.860 39.044 1.00 15.70 C ANISOU 446 CB GLU A 107 1643 2201 2122 16 196 -203 C ATOM 447 CG GLU A 107 -8.914 32.884 40.326 1.00 24.98 C ANISOU 447 CG GLU A 107 2853 3375 3265 -1 212 -275 C ATOM 448 CD GLU A 107 -9.485 31.948 41.391 1.00 21.29 C ANISOU 448 CD GLU A 107 2408 2954 2726 -20 240 -283 C ATOM 449 OE1 GLU A 107 -10.325 31.048 41.095 1.00 18.93 O ANISOU 449 OE1 GLU A 107 2098 2672 2423 -30 244 -234 O ATOM 450 OE2 GLU A 107 -9.085 32.127 42.555 1.00 26.63 O ANISOU 450 OE2 GLU A 107 3118 3655 3347 -31 260 -341 O ATOM 451 N THR A 108 -6.853 34.466 38.281 1.00 5.78 N ANISOU 451 N THR A 108 372 850 973 5 164 -222 N ATOM 452 CA THR A 108 -5.413 34.227 38.180 1.00 5.28 C ANISOU 452 CA THR A 108 320 776 911 -29 133 -216 C ATOM 453 C THR A 108 -4.984 33.271 39.294 1.00 7.57 C ANISOU 453 C THR A 108 641 1102 1133 -54 111 -256 C ATOM 454 O THR A 108 -5.320 33.478 40.463 1.00 8.67 O ANISOU 454 O THR A 108 810 1250 1235 -58 114 -313 O ATOM 455 CB THR A 108 -4.602 35.544 38.286 1.00 12.51 C ANISOU 455 CB THR A 108 1230 1606 1916 -41 126 -231 C ATOM 456 OG1 THR A 108 -4.869 36.350 37.133 1.00 12.02 O ANISOU 456 OG1 THR A 108 1138 1505 1924 -16 148 -155 O ATOM 457 CG2 THR A 108 -3.100 35.260 38.382 1.00 13.28 C ANISOU 457 CG2 THR A 108 1319 1704 2025 -83 89 -229 C ATOM 458 N VAL A 109 -4.253 32.226 38.923 1.00 7.40 N ANISOU 458 N VAL A 109 613 1105 1094 -66 96 -220 N ATOM 459 CA VAL A 109 -3.772 31.240 39.886 1.00 7.49 C ANISOU 459 CA VAL A 109 643 1144 1059 -79 69 -221 C ATOM 460 C VAL A 109 -2.281 30.954 39.702 1.00 8.69 C ANISOU 460 C VAL A 109 763 1284 1255 -87 34 -190 C ATOM 461 O VAL A 109 -1.690 31.281 38.665 1.00 8.41 O ANISOU 461 O VAL A 109 702 1221 1273 -83 49 -164 O ATOM 462 CB VAL A 109 -4.544 29.913 39.752 1.00 7.85 C ANISOU 462 CB VAL A 109 700 1216 1068 -76 99 -195 C ATOM 463 CG1 VAL A 109 -6.004 30.085 40.206 1.00 8.97 C ANISOU 463 CG1 VAL A 109 853 1383 1171 -74 134 -219 C ATOM 464 CG2 VAL A 109 -4.487 29.429 38.306 1.00 7.25 C ANISOU 464 CG2 VAL A 109 626 1113 1016 -67 114 -164 C ATOM 465 N GLU A 110 -1.688 30.352 40.725 1.00 7.88 N ANISOU 465 N GLU A 110 664 1207 1122 -94 -13 -176 N ATOM 466 CA GLU A 110 -0.284 29.970 40.686 1.00 7.38 C ANISOU 466 CA GLU A 110 547 1140 1116 -91 -55 -133 C ATOM 467 C GLU A 110 -0.248 28.463 40.849 1.00 9.65 C ANISOU 467 C GLU A 110 837 1429 1400 -62 -46 -73 C ATOM 468 O GLU A 110 -1.026 27.915 41.611 1.00 8.56 O ANISOU 468 O GLU A 110 746 1314 1192 -64 -44 -59 O ATOM 469 CB GLU A 110 0.514 30.672 41.786 1.00 12.08 C ANISOU 469 CB GLU A 110 1127 1766 1697 -127 -143 -156 C ATOM 470 CG GLU A 110 2.021 30.427 41.694 1.00 13.50 C ANISOU 470 CG GLU A 110 1219 1949 1962 -128 -198 -105 C ATOM 471 CD GLU A 110 2.811 31.293 42.659 1.00 30.82 C ANISOU 471 CD GLU A 110 3383 4180 4146 -184 -302 -144 C ATOM 472 OE1 GLU A 110 2.252 32.292 43.154 1.00 30.52 O ANISOU 472 OE1 GLU A 110 3400 4139 4055 -224 -310 -234 O ATOM 473 OE2 GLU A 110 3.994 30.985 42.915 1.00 30.86 O ANISOU 473 OE2 GLU A 110 3323 4215 4187 -186 -361 -86 O ATOM 474 N PHE A 111 0.633 27.787 40.128 1.00 8.35 N ANISOU 474 N PHE A 111 620 1231 1321 -34 -24 -35 N ATOM 475 CA PHE A 111 0.639 26.322 40.139 1.00 7.67 C ANISOU 475 CA PHE A 111 536 1110 1268 1 5 16 C ATOM 476 C PHE A 111 1.981 25.778 39.642 1.00 8.08 C ANISOU 476 C PHE A 111 508 1124 1440 44 17 58 C ATOM 477 O PHE A 111 2.802 26.510 39.063 1.00 8.47 O ANISOU 477 O PHE A 111 522 1181 1516 38 20 40 O ATOM 478 CB PHE A 111 -0.503 25.787 39.260 1.00 7.33 C ANISOU 478 CB PHE A 111 542 1034 1209 -5 86 -28 C ATOM 479 CG PHE A 111 -0.520 26.393 37.880 1.00 7.43 C ANISOU 479 CG PHE A 111 543 1048 1232 -13 137 -83 C ATOM 480 CD1 PHE A 111 0.068 25.742 36.819 1.00 11.33 C ANISOU 480 CD1 PHE A 111 1040 1505 1760 9 190 -91 C ATOM 481 CD2 PHE A 111 -1.088 27.635 37.661 1.00 6.12 C ANISOU 481 CD2 PHE A 111 409 914 1004 -36 120 -104 C ATOM 482 CE1 PHE A 111 0.065 26.316 35.544 1.00 13.12 C ANISOU 482 CE1 PHE A 111 1295 1752 1939 0 217 -115 C ATOM 483 CE2 PHE A 111 -1.080 28.214 36.393 1.00 9.86 C ANISOU 483 CE2 PHE A 111 904 1387 1455 -36 145 -105 C ATOM 484 CZ PHE A 111 -0.506 27.545 35.342 1.00 10.36 C ANISOU 484 CZ PHE A 111 964 1439 1531 -22 191 -109 C ATOM 485 N ASP A 112 2.209 24.497 39.906 1.00 8.89 N ANISOU 485 N ASP A 112 599 1177 1602 87 30 120 N ATOM 486 CA ASP A 112 3.314 23.777 39.295 1.00 8.57 C ANISOU 486 CA ASP A 112 490 1075 1691 143 75 147 C ATOM 487 C ASP A 112 2.780 23.077 38.064 1.00 11.55 C ANISOU 487 C ASP A 112 921 1382 2085 148 192 70 C ATOM 488 O ASP A 112 1.590 22.783 37.978 1.00 11.14 O ANISOU 488 O ASP A 112 927 1317 1990 120 223 29 O ATOM 489 CB ASP A 112 3.917 22.772 40.276 1.00 11.81 C ANISOU 489 CB ASP A 112 851 1455 2182 199 22 269 C ATOM 490 CG ASP A 112 4.351 23.422 41.577 1.00 21.34 C ANISOU 490 CG ASP A 112 2023 2764 3322 178 -120 343 C ATOM 491 OD1 ASP A 112 4.786 24.597 41.551 1.00 20.97 O ANISOU 491 OD1 ASP A 112 1964 2780 3224 131 -164 285 O ATOM 492 OD2 ASP A 112 4.236 22.767 42.630 1.00 23.66 O ANISOU 492 OD2 ASP A 112 2333 3073 3584 195 -182 446 O ATOM 493 N VAL A 113 3.646 22.819 37.099 1.00 10.18 N ANISOU 493 N VAL A 113 739 1175 1953 170 249 41 N ATOM 494 CA VAL A 113 3.238 22.038 35.948 1.00 8.93 C ANISOU 494 CA VAL A 113 633 958 1801 168 350 -42 C ATOM 495 C VAL A 113 3.970 20.711 35.999 1.00 10.26 C ANISOU 495 C VAL A 113 771 1020 2107 226 400 -12 C ATOM 496 O VAL A 113 5.186 20.684 36.197 1.00 11.08 O ANISOU 496 O VAL A 113 808 1121 2280 267 383 48 O ATOM 497 CB VAL A 113 3.545 22.741 34.619 1.00 11.77 C ANISOU 497 CB VAL A 113 1014 1373 2085 145 392 -104 C ATOM 498 CG1 VAL A 113 3.061 21.878 33.452 1.00 16.08 C ANISOU 498 CG1 VAL A 113 1616 1878 2615 133 483 -200 C ATOM 499 CG2 VAL A 113 2.880 24.116 34.581 1.00 14.47 C ANISOU 499 CG2 VAL A 113 1383 1804 2310 96 339 -107 C ATOM 500 N VAL A 114 3.214 19.620 35.869 1.00 10.67 N ANISOU 500 N VAL A 114 868 979 2209 224 459 -52 N ATOM 501 CA VAL A 114 3.781 18.284 35.884 1.00 13.34 C ANISOU 501 CA VAL A 114 1186 1191 2690 273 516 -27 C ATOM 502 C VAL A 114 3.352 17.534 34.633 1.00 14.55 C ANISOU 502 C VAL A 114 1403 1284 2842 241 621 -167 C ATOM 503 O VAL A 114 2.315 17.805 34.056 1.00 15.56 O ANISOU 503 O VAL A 114 1593 1452 2866 175 632 -262 O ATOM 504 CB VAL A 114 3.387 17.489 37.157 1.00 20.14 C ANISOU 504 CB VAL A 114 2037 1972 3642 302 479 90 C ATOM 505 CG1 VAL A 114 3.638 18.319 38.406 1.00 21.07 C ANISOU 505 CG1 VAL A 114 2102 2187 3715 320 355 222 C ATOM 506 CG2 VAL A 114 1.944 17.081 37.101 1.00 25.83 C ANISOU 506 CG2 VAL A 114 2832 2639 4342 249 516 27 C ATOM 507 N GLU A 115 4.188 16.624 34.162 1.00 20.43 N ANISOU 507 N GLU A 115 2126 1945 3693 283 694 -185 N ATOM 508 CA GLU A 115 3.889 15.996 32.888 1.00 32.07 C ANISOU 508 CA GLU A 115 3658 3382 5146 248 791 -334 C ATOM 509 C GLU A 115 3.885 14.492 33.015 1.00 47.04 C ANISOU 509 C GLU A 115 5558 5117 7197 271 859 -347 C ATOM 510 O GLU A 115 4.931 13.856 32.930 1.00 46.95 O ANISOU 510 O GLU A 115 5496 5032 7309 337 913 -320 O ATOM 511 CB GLU A 115 4.891 16.429 31.805 1.00 40.29 C ANISOU 511 CB GLU A 115 4679 4487 6141 271 844 -386 C ATOM 512 CG GLU A 115 4.596 15.872 30.404 1.00 51.49 C ANISOU 512 CG GLU A 115 6164 5898 7504 234 941 -546 C ATOM 513 CD GLU A 115 4.757 16.910 29.299 1.00 52.25 C ANISOU 513 CD GLU A 115 6280 6139 7433 210 953 -599 C ATOM 514 OE1 GLU A 115 5.562 17.847 29.471 1.00 49.00 O ANISOU 514 OE1 GLU A 115 5811 5802 7005 243 923 -513 O ATOM 515 OE2 GLU A 115 4.079 16.784 28.256 1.00 59.66 O ANISOU 515 OE2 GLU A 115 7288 7122 8257 156 988 -719 O ATOM 516 N GLY A 116 2.702 13.937 33.258 1.00 54.92 N ANISOU 516 N GLY A 116 6609 6058 8201 215 857 -381 N ATOM 517 CA GLY A 116 2.431 12.560 32.893 1.00 67.97 C ANISOU 517 CA GLY A 116 8292 7570 9964 202 939 -458 C ATOM 518 C GLY A 116 2.202 12.612 31.392 1.00 74.67 C ANISOU 518 C GLY A 116 9198 8474 10699 144 999 -645 C ATOM 519 O GLY A 116 2.124 13.701 30.827 1.00 72.95 O ANISOU 519 O GLY A 116 8995 8401 10321 116 964 -680 O ATOM 520 N GLU A 117 2.081 11.461 30.740 1.00 83.63 N ANISOU 520 N GLU A 117 10367 9501 11910 126 1084 -760 N ATOM 521 CA GLU A 117 1.991 11.434 29.283 1.00 86.28 C ANISOU 521 CA GLU A 117 10757 9894 12130 78 1142 -939 C ATOM 522 C GLU A 117 0.555 11.357 28.756 1.00 73.16 C ANISOU 522 C GLU A 117 9165 8283 10348 -39 1108 -1061 C ATOM 523 O GLU A 117 0.319 10.890 27.643 1.00 77.77 O ANISOU 523 O GLU A 117 9802 8875 10873 -88 1159 -1221 O ATOM 524 CB GLU A 117 2.848 10.289 28.722 1.00 97.17 C ANISOU 524 CB GLU A 117 12131 11138 13651 132 1264 -1018 C ATOM 525 CG GLU A 117 4.355 10.530 28.874 1.00100.89 C ANISOU 525 CG GLU A 117 12525 11604 14206 244 1304 -924 C ATOM 526 CD GLU A 117 4.835 10.570 30.316 1.00103.50 C ANISOU 526 CD GLU A 117 12772 11879 14674 315 1241 -718 C ATOM 527 OE1 GLU A 117 4.255 9.854 31.159 1.00103.15 O ANISOU 527 OE1 GLU A 117 12730 11727 14737 306 1218 -655 O ATOM 528 OE2 GLU A 117 5.723 11.405 30.609 1.00101.98 O ANISOU 528 OE2 GLU A 117 12516 11770 14464 370 1203 -615 O ATOM 529 N LYS A 118 -0.397 11.840 29.554 1.00 58.01 N ANISOU 529 N LYS A 118 7244 6409 8389 -84 1019 -986 N ATOM 530 CA LYS A 118 -1.659 12.334 29.010 1.00 36.51 C ANISOU 530 CA LYS A 118 4563 3809 5500 -188 956 -1070 C ATOM 531 C LYS A 118 -1.471 13.795 28.619 1.00 34.60 C ANISOU 531 C LYS A 118 4315 3749 5082 -182 901 -1037 C ATOM 532 O LYS A 118 -2.318 14.390 27.961 1.00 42.82 O ANISOU 532 O LYS A 118 5383 4922 5964 -254 847 -1095 O ATOM 533 CB LYS A 118 -2.813 12.189 30.001 1.00 42.54 C ANISOU 533 CB LYS A 118 5321 4538 6305 -240 895 -1009 C ATOM 534 CG LYS A 118 -3.992 11.392 29.458 1.00 49.21 C ANISOU 534 CG LYS A 118 6205 5357 7135 -344 890 -1135 C ATOM 535 CD LYS A 118 -4.924 10.898 30.548 1.00 54.77 C ANISOU 535 CD LYS A 118 6896 5974 7941 -380 858 -1057 C ATOM 536 CE LYS A 118 -4.200 10.056 31.578 1.00 62.97 C ANISOU 536 CE LYS A 118 7911 6831 9184 -299 913 -936 C ATOM 537 NZ LYS A 118 -5.134 9.558 32.628 1.00 63.97 N ANISOU 537 NZ LYS A 118 8032 6877 9397 -338 884 -842 N ATOM 538 N GLY A 119 -0.344 14.365 29.031 1.00 31.57 N ANISOU 538 N GLY A 119 3887 3371 4735 -94 909 -933 N ATOM 539 CA GLY A 119 -0.016 15.738 28.690 1.00 31.27 C ANISOU 539 CA GLY A 119 3839 3487 4555 -80 865 -887 C ATOM 540 C GLY A 119 0.380 16.547 29.908 1.00 23.31 C ANISOU 540 C GLY A 119 2776 2489 3594 -25 805 -733 C ATOM 541 O GLY A 119 0.595 15.993 30.989 1.00 25.49 O ANISOU 541 O GLY A 119 3019 2655 4013 15 805 -653 O ATOM 542 N ALA A 120 0.486 17.860 29.734 1.00 21.60 N ANISOU 542 N ALA A 120 2548 2404 3255 -22 753 -685 N ATOM 543 CA ALA A 120 0.916 18.723 30.829 1.00 18.21 C ANISOU 543 CA ALA A 120 2066 1995 2857 24 692 -552 C ATOM 544 C ALA A 120 -0.260 19.104 31.691 1.00 21.82 C ANISOU 544 C ALA A 120 2532 2476 3284 -18 622 -522 C ATOM 545 O ALA A 120 -1.312 19.532 31.187 1.00 20.71 O ANISOU 545 O ALA A 120 2424 2418 3027 -84 591 -578 O ATOM 546 CB ALA A 120 1.610 19.958 30.296 1.00 20.30 C ANISOU 546 CB ALA A 120 2310 2377 3027 45 674 -509 C ATOM 547 N GLU A 121 -0.092 18.970 33.002 1.00 15.44 N ANISOU 547 N GLU A 121 1686 1604 2577 22 595 -427 N ATOM 548 CA AGLU A 121 -1.181 19.234 33.930 0.30 13.74 C ANISOU 548 CA AGLU A 121 1474 1402 2346 -8 550 -397 C ATOM 549 CA BGLU A 121 -1.184 19.303 33.894 0.70 13.78 C ANISOU 549 CA BGLU A 121 1479 1415 2343 -10 547 -398 C ATOM 550 C GLU A 121 -0.731 20.105 35.102 1.00 15.45 C ANISOU 550 C GLU A 121 1634 1669 2566 38 483 -271 C ATOM 551 O GLU A 121 0.428 20.086 35.493 1.00 12.51 O ANISOU 551 O GLU A 121 1216 1273 2263 99 469 -193 O ATOM 552 CB AGLU A 121 -1.779 17.922 34.441 0.30 14.34 C ANISOU 552 CB AGLU A 121 1571 1334 2544 -23 591 -409 C ATOM 553 CB BGLU A 121 -1.906 18.045 34.351 0.70 15.71 C ANISOU 553 CB BGLU A 121 1748 1525 2695 -33 587 -421 C ATOM 554 CG AGLU A 121 -0.770 16.914 34.947 0.30 17.72 C ANISOU 554 CG AGLU A 121 1970 1629 3133 49 624 -326 C ATOM 555 CG BGLU A 121 -1.172 17.203 35.352 0.70 13.75 C ANISOU 555 CG BGLU A 121 1470 1145 2611 40 600 -303 C ATOM 556 CD AGLU A 121 -1.419 15.634 35.440 0.30 26.46 C ANISOU 556 CD AGLU A 121 3105 2594 4355 24 655 -306 C ATOM 557 CD BGLU A 121 -2.033 16.040 35.827 0.70 23.79 C ANISOU 557 CD BGLU A 121 2779 2284 3975 -4 624 -289 C ATOM 558 OE1AGLU A 121 -1.052 15.164 36.538 0.30 30.22 O ANISOU 558 OE1AGLU A 121 3555 2990 4937 79 637 -158 O ATOM 559 OE1BGLU A 121 -3.190 16.287 36.230 0.70 28.87 O ANISOU 559 OE1BGLU A 121 3447 2986 4536 -81 578 -275 O ATOM 560 OE2AGLU A 121 -2.292 15.097 34.728 0.30 26.47 O ANISOU 560 OE2AGLU A 121 3149 2579 4329 -56 685 -423 O ATOM 561 OE2BGLU A 121 -1.563 14.883 35.774 0.70 31.60 O ANISOU 561 OE2BGLU A 121 3762 3161 5083 23 672 -272 O ATOM 562 N ALA A 122 -1.662 20.859 35.650 1.00 13.30 N ANISOU 562 N ALA A 122 1382 1480 2191 -8 411 -240 N ATOM 563 CA ALA A 122 -1.393 21.700 36.795 1.00 7.64 C ANISOU 563 CA ALA A 122 639 824 1439 11 330 -138 C ATOM 564 C ALA A 122 -1.363 20.879 38.081 1.00 13.71 C ANISOU 564 C ALA A 122 1410 1533 2265 32 303 -33 C ATOM 565 O ALA A 122 -2.078 19.875 38.223 1.00 16.42 O ANISOU 565 O ALA A 122 1787 1801 2653 7 339 -31 O ATOM 566 CB ALA A 122 -2.464 22.794 36.893 1.00 10.88 C ANISOU 566 CB ALA A 122 1073 1334 1728 -39 285 -158 C ATOM 567 N ALA A 123 -0.555 21.331 39.030 1.00 9.72 N ANISOU 567 N ALA A 123 867 1070 1755 68 233 61 N ATOM 568 CA ALA A 123 -0.512 20.721 40.341 1.00 8.98 C ANISOU 568 CA ALA A 123 778 961 1673 85 188 186 C ATOM 569 C ALA A 123 -0.387 21.820 41.375 1.00 9.01 C ANISOU 569 C ALA A 123 779 1091 1555 70 92 228 C ATOM 570 O ALA A 123 0.158 22.894 41.081 1.00 10.36 O ANISOU 570 O ALA A 123 918 1321 1698 66 57 178 O ATOM 571 CB ALA A 123 0.663 19.738 40.453 1.00 15.48 C ANISOU 571 CB ALA A 123 1544 1688 2650 163 197 274 C ATOM 572 N ASN A 124 -0.891 21.552 42.578 1.00 9.30 N ANISOU 572 N ASN A 124 852 1165 1517 55 57 313 N ATOM 573 CA ASN A 124 -0.738 22.486 43.694 1.00 8.85 C ANISOU 573 CA ASN A 124 805 1235 1325 36 -32 340 C ATOM 574 C ASN A 124 -1.260 23.863 43.321 1.00 13.09 C ANISOU 574 C ASN A 124 1360 1833 1782 -6 -28 212 C ATOM 575 O ASN A 124 -0.572 24.867 43.473 1.00 10.84 O ANISOU 575 O ASN A 124 1048 1602 1468 -12 -91 176 O ATOM 576 CB ASN A 124 0.726 22.572 44.124 1.00 14.73 C ANISOU 576 CB ASN A 124 1478 2011 2110 78 -128 416 C ATOM 577 CG ASN A 124 1.274 21.234 44.579 1.00 25.12 C ANISOU 577 CG ASN A 124 2763 3262 3521 136 -141 573 C ATOM 578 OD1 ASN A 124 0.591 20.473 45.262 1.00 25.57 O ANISOU 578 OD1 ASN A 124 2871 3305 3541 130 -120 664 O ATOM 579 ND2 ASN A 124 2.513 20.937 44.198 1.00 28.79 N ANISOU 579 ND2 ASN A 124 3134 3679 4126 198 -165 618 N ATOM 580 N VAL A 125 -2.483 23.897 42.800 1.00 7.58 N ANISOU 580 N VAL A 125 697 1117 1066 -35 44 147 N ATOM 581 CA VAL A 125 -3.057 25.160 42.323 1.00 8.49 C ANISOU 581 CA VAL A 125 820 1274 1134 -60 55 43 C ATOM 582 C VAL A 125 -3.559 26.012 43.488 1.00 8.61 C ANISOU 582 C VAL A 125 870 1373 1027 -82 30 24 C ATOM 583 O VAL A 125 -4.410 25.567 44.271 1.00 10.47 O ANISOU 583 O VAL A 125 1142 1641 1194 -98 62 58 O ATOM 584 CB VAL A 125 -4.221 24.918 41.335 1.00 6.39 C ANISOU 584 CB VAL A 125 560 974 893 -81 127 -11 C ATOM 585 CG1 VAL A 125 -4.730 26.260 40.804 1.00 8.29 C ANISOU 585 CG1 VAL A 125 793 1254 1103 -89 128 -86 C ATOM 586 CG2 VAL A 125 -3.790 24.015 40.187 1.00 7.57 C ANISOU 586 CG2 VAL A 125 690 1046 1141 -69 162 -22 C ATOM 587 N THR A 126 -3.036 27.236 43.583 1.00 9.32 N ANISOU 587 N THR A 126 951 1494 1095 -88 -16 -38 N ATOM 588 CA ATHR A 126 -3.331 28.185 44.666 0.77 9.35 C ANISOU 588 CA ATHR A 126 994 1568 989 -112 -38 -94 C ATOM 589 CA BTHR A 126 -3.441 28.159 44.641 0.06 10.72 C ANISOU 589 CA BTHR A 126 1170 1741 1162 -112 -31 -94 C ATOM 590 CA CTHR A 126 -3.447 28.158 44.640 0.17 10.56 C ANISOU 590 CA CTHR A 126 1150 1721 1142 -112 -31 -94 C ATOM 591 C THR A 126 -3.597 29.580 44.106 1.00 9.84 C ANISOU 591 C THR A 126 1048 1602 1088 -118 -19 -197 C ATOM 592 O THR A 126 -3.470 29.819 42.904 1.00 10.33 O ANISOU 592 O THR A 126 1073 1606 1245 -105 0 -202 O ATOM 593 CB ATHR A 126 -2.165 28.317 45.664 0.77 13.41 C ANISOU 593 CB ATHR A 126 1506 2146 1442 -127 -142 -69 C ATOM 594 CB BTHR A 126 -2.427 28.167 45.801 0.06 12.67 C ANISOU 594 CB BTHR A 126 1426 2061 1329 -127 -127 -61 C ATOM 595 CB CTHR A 126 -2.444 28.160 45.807 0.17 12.84 C ANISOU 595 CB CTHR A 126 1447 2082 1348 -127 -126 -61 C ATOM 596 OG1ATHR A 126 -1.026 28.874 44.991 0.77 13.63 O ANISOU 596 OG1ATHR A 126 1472 2135 1571 -128 -195 -90 O ATOM 597 OG1BTHR A 126 -1.513 27.072 45.650 0.06 14.25 O ANISOU 597 OG1BTHR A 126 1583 2239 1595 -100 -171 53 O ATOM 598 OG1CTHR A 126 -2.884 29.074 46.818 0.17 11.31 O ANISOU 598 OG1CTHR A 126 1308 1963 1027 -159 -131 -148 O ATOM 599 CG2ATHR A 126 -1.787 26.973 46.264 0.77 16.80 C ANISOU 599 CG2ATHR A 126 1934 2602 1846 -109 -175 68 C ATOM 600 CG2BTHR A 126 -3.143 28.053 47.141 0.06 12.83 C ANISOU 600 CG2BTHR A 126 1513 2177 1184 -148 -114 -55 C ATOM 601 CG2CTHR A 126 -1.070 28.580 45.325 0.17 14.25 C ANISOU 601 CG2CTHR A 126 1561 2235 1618 -127 -203 -65 C ATOM 602 N GLY A 127 -3.903 30.522 44.996 1.00 14.58 N ANISOU 602 N GLY A 127 1687 2241 1612 -137 -20 -278 N ATOM 603 CA GLY A 127 -3.940 31.915 44.581 1.00 13.71 C ANISOU 603 CA GLY A 127 1568 2076 1566 -141 -9 -372 C ATOM 604 C GLY A 127 -2.498 32.368 44.369 1.00 15.36 C ANISOU 604 C GLY A 127 1739 2259 1839 -167 -92 -375 C ATOM 605 O GLY A 127 -1.561 31.709 44.838 1.00 16.88 O ANISOU 605 O GLY A 127 1915 2500 1999 -182 -167 -322 O ATOM 606 N PRO A 128 -2.295 33.482 43.647 1.00 12.90 N ANISOU 606 N PRO A 128 1401 1868 1632 -173 -80 -421 N ATOM 607 CA PRO A 128 -0.935 34.001 43.471 1.00 17.09 C ANISOU 607 CA PRO A 128 1883 2370 2241 -213 -149 -426 C ATOM 608 C PRO A 128 -0.318 34.368 44.818 1.00 23.43 C ANISOU 608 C PRO A 128 2708 3231 2962 -271 -238 -504 C ATOM 609 O PRO A 128 -0.990 34.957 45.659 1.00 28.10 O ANISOU 609 O PRO A 128 3367 3836 3475 -285 -216 -604 O ATOM 610 CB PRO A 128 -1.136 35.235 42.577 1.00 21.44 C ANISOU 610 CB PRO A 128 2416 2815 2915 -212 -98 -456 C ATOM 611 CG PRO A 128 -2.569 35.577 42.695 1.00 25.68 C ANISOU 611 CG PRO A 128 3000 3335 3424 -173 -23 -499 C ATOM 612 CD PRO A 128 -3.290 34.280 42.914 1.00 15.72 C ANISOU 612 CD PRO A 128 1758 2156 2058 -143 -2 -448 C ATOM 613 N GLY A 129 0.944 33.998 45.018 1.00 34.30 N ANISOU 613 N GLY A 129 4032 4645 4355 -297 -330 -450 N ATOM 614 CA GLY A 129 1.564 34.107 46.325 1.00 45.84 C ANISOU 614 CA GLY A 129 5525 6178 5716 -342 -428 -476 C ATOM 615 C GLY A 129 0.982 33.111 47.316 1.00 47.45 C ANISOU 615 C GLY A 129 5783 6501 5744 -323 -444 -444 C ATOM 616 O GLY A 129 0.496 32.038 46.937 1.00 36.75 O ANISOU 616 O GLY A 129 4416 5172 4375 -277 -401 -356 O TER 617 GLY A 129 ATOM 618 P U B 1 -20.001 11.295 32.803 1.00112.11 P ANISOU 618 P U B 1 13638 13829 15130 -1357 152 -810 P ATOM 619 OP1 U B 1 -19.728 12.673 32.317 1.00106.83 O ANISOU 619 OP1 U B 1 12959 13328 14303 -1269 95 -807 O ATOM 620 OP2 U B 1 -20.139 10.186 31.823 1.00110.97 O ANISOU 620 OP2 U B 1 13528 13598 15040 -1463 130 -971 O ATOM 621 O5' U B 1 -18.861 10.898 33.846 1.00 78.39 O ANISOU 621 O5' U B 1 9447 9414 10924 -1273 269 -729 O ATOM 622 C5' U B 1 -18.835 11.459 35.156 1.00 66.38 C ANISOU 622 C5' U B 1 7901 7919 9400 -1207 315 -560 C ATOM 623 C4' U B 1 -17.601 12.300 35.376 1.00 57.00 C ANISOU 623 C4' U B 1 6772 6764 8121 -1078 340 -531 C ATOM 624 O4' U B 1 -17.860 13.281 36.418 1.00 46.08 O ANISOU 624 O4' U B 1 5345 5481 6682 -1020 349 -391 O ATOM 625 C3' U B 1 -16.351 11.536 35.812 1.00 61.42 C ANISOU 625 C3' U B 1 7418 7161 8758 -1023 423 -512 C ATOM 626 O3' U B 1 -15.205 12.187 35.270 1.00 60.00 O ANISOU 626 O3' U B 1 7287 7018 8493 -934 420 -570 O ATOM 627 C2' U B 1 -16.358 11.727 37.325 1.00 56.49 C ANISOU 627 C2' U B 1 6781 6531 8150 -983 473 -328 C ATOM 628 O2' U B 1 -15.097 11.582 37.948 1.00 54.85 O ANISOU 628 O2' U B 1 6638 6237 7966 -894 527 -258 O ATOM 629 C1' U B 1 -16.891 13.152 37.441 1.00 43.10 C ANISOU 629 C1' U B 1 5026 5026 6323 -950 421 -294 C ATOM 630 N1 U B 1 -17.535 13.446 38.725 1.00 35.97 N ANISOU 630 N1 U B 1 4077 4179 5410 -949 457 -146 N ATOM 631 C2 U B 1 -17.056 14.527 39.450 1.00 31.50 C ANISOU 631 C2 U B 1 3520 3706 4743 -858 468 -71 C ATOM 632 O2 U B 1 -16.141 15.235 39.073 1.00 29.90 O ANISOU 632 O2 U B 1 3356 3532 4473 -785 443 -115 O ATOM 633 N3 U B 1 -17.700 14.745 40.638 1.00 28.10 N ANISOU 633 N3 U B 1 3051 3338 4287 -862 514 53 N ATOM 634 C4 U B 1 -18.757 14.001 41.142 1.00 18.24 C ANISOU 634 C4 U B 1 1753 2072 3107 -949 553 115 C ATOM 635 O4 U B 1 -19.224 14.326 42.221 1.00 24.65 O ANISOU 635 O4 U B 1 2536 2962 3866 -941 606 219 O ATOM 636 C5 U B 1 -19.197 12.896 40.340 1.00 30.68 C ANISOU 636 C5 U B 1 3315 3539 4802 -1045 535 42 C ATOM 637 C6 U B 1 -18.578 12.667 39.177 1.00 37.22 C ANISOU 637 C6 U B 1 4186 4303 5653 -1041 486 -90 C ATOM 638 P C B 2 -13.966 11.335 34.710 1.00 63.89 P ANISOU 638 P C B 2 7854 7365 9054 -896 478 -661 P ATOM 639 OP1 C B 2 -14.143 11.211 33.241 1.00 64.06 O ANISOU 639 OP1 C B 2 7887 7437 9016 -949 440 -839 O ATOM 640 OP2 C B 2 -13.792 10.112 35.539 1.00 61.43 O ANISOU 640 OP2 C B 2 7565 6866 8908 -903 551 -580 O ATOM 641 O5' C B 2 -12.720 12.293 34.974 1.00 41.56 O ANISOU 641 O5' C B 2 5052 4586 6152 -778 493 -610 O ATOM 642 C5' C B 2 -12.628 13.559 34.327 1.00 30.63 C ANISOU 642 C5' C B 2 3653 3367 4617 -750 437 -656 C ATOM 643 C4' C B 2 -11.267 13.771 33.708 1.00 21.27 C ANISOU 643 C4' C B 2 2512 2169 3403 -678 470 -718 C ATOM 644 O4' C B 2 -10.292 13.992 34.757 1.00 27.29 O ANISOU 644 O4' C B 2 3283 2868 4216 -592 509 -597 O ATOM 645 C3' C B 2 -10.739 12.609 32.876 1.00 30.14 C ANISOU 645 C3' C B 2 3676 3171 4604 -692 527 -838 C ATOM 646 O3' C B 2 -9.923 13.135 31.835 1.00 28.87 O ANISOU 646 O3' C B 2 3537 3088 4344 -655 532 -928 O ATOM 647 C2' C B 2 -9.866 11.848 33.872 1.00 33.25 C ANISOU 647 C2' C B 2 4088 3392 5154 -623 601 -735 C ATOM 648 O2' C B 2 -8.843 11.074 33.279 1.00 33.08 O ANISOU 648 O2' C B 2 4097 3259 5212 -579 670 -810 O ATOM 649 C1' C B 2 -9.291 12.984 34.717 1.00 25.45 C ANISOU 649 C1' C B 2 3084 2477 4108 -547 580 -609 C ATOM 650 N1 C B 2 -9.019 12.615 36.114 1.00 28.14 N ANISOU 650 N1 C B 2 3421 2719 4550 -503 606 -439 N ATOM 651 C2 C B 2 -7.796 12.943 36.705 1.00 30.34 C ANISOU 651 C2 C B 2 3702 2967 4858 -404 622 -340 C ATOM 652 O2 C B 2 -6.938 13.515 36.024 1.00 29.00 O ANISOU 652 O2 C B 2 3533 2839 4646 -356 625 -408 O ATOM 653 N3 C B 2 -7.581 12.626 38.006 1.00 33.96 N ANISOU 653 N3 C B 2 4158 3363 5384 -365 630 -160 N ATOM 654 C4 C B 2 -8.538 12.007 38.704 1.00 42.67 C ANISOU 654 C4 C B 2 5261 4433 6520 -423 636 -83 C ATOM 655 N4 C B 2 -8.285 11.702 39.975 1.00 49.87 N ANISOU 655 N4 C B 2 6174 5303 7470 -383 644 107 N ATOM 656 C5 C B 2 -9.797 11.663 38.131 1.00 40.35 C ANISOU 656 C5 C B 2 4960 4157 6216 -527 629 -187 C ATOM 657 C6 C B 2 -9.989 11.989 36.847 1.00 37.52 C ANISOU 657 C6 C B 2 4599 3862 5793 -562 607 -361 C ATOM 658 P A B 3 -10.079 12.603 30.331 1.00 35.31 P ANISOU 658 P A B 3 4382 3934 5100 -718 533 -1103 P ATOM 659 OP1 A B 3 -11.473 12.140 30.107 1.00 40.48 O ANISOU 659 OP1 A B 3 5018 4607 5755 -827 474 -1152 O ATOM 660 OP2 A B 3 -8.945 11.671 30.102 1.00 37.04 O ANISOU 660 OP2 A B 3 4640 4005 5427 -668 630 -1156 O ATOM 661 O5' A B 3 -9.810 13.893 29.436 1.00 35.46 O ANISOU 661 O5' A B 3 4398 4146 4927 -696 485 -1128 O ATOM 662 C5' A B 3 -10.741 14.970 29.349 1.00 32.18 C ANISOU 662 C5' A B 3 3941 3897 4388 -725 390 -1082 C ATOM 663 C4' A B 3 -10.215 16.072 28.456 1.00 31.80 C ANISOU 663 C4' A B 3 3899 4001 4181 -691 364 -1090 C ATOM 664 O4' A B 3 -9.031 16.649 29.070 1.00 29.57 O ANISOU 664 O4' A B 3 3621 3685 3930 -599 413 -1013 O ATOM 665 C3' A B 3 -9.779 15.623 27.062 1.00 33.86 C ANISOU 665 C3' A B 3 4210 4292 4362 -717 389 -1221 C ATOM 666 O3' A B 3 -9.905 16.713 26.149 1.00 33.69 O ANISOU 666 O3' A B 3 4183 4455 4163 -719 326 -1208 O ATOM 667 C2' A B 3 -8.299 15.335 27.264 1.00 32.56 C ANISOU 667 C2' A B 3 4077 4017 4279 -635 492 -1216 C ATOM 668 O2' A B 3 -7.531 15.357 26.081 1.00 43.14 O ANISOU 668 O2' A B 3 5459 5408 5524 -622 530 -1297 O ATOM 669 C1' A B 3 -7.907 16.454 28.223 1.00 27.57 C ANISOU 669 C1' A B 3 3408 3418 3651 -564 474 -1076 C ATOM 670 N9 A B 3 -6.769 16.126 29.075 1.00 20.61 N ANISOU 670 N9 A B 3 2528 2397 2905 -484 549 -1019 N ATOM 671 C8 A B 3 -6.760 15.236 30.120 1.00 18.79 C ANISOU 671 C8 A B 3 2292 2008 2839 -470 588 -978 C ATOM 672 N7 A B 3 -5.601 15.149 30.724 1.00 22.10 N ANISOU 672 N7 A B 3 2704 2334 3357 -384 641 -910 N ATOM 673 C5 A B 3 -4.799 16.040 30.017 1.00 16.97 C ANISOU 673 C5 A B 3 2056 1788 2604 -344 640 -915 C ATOM 674 C6 A B 3 -3.461 16.415 30.172 1.00 24.04 C ANISOU 674 C6 A B 3 2935 2663 3535 -254 675 -851 C ATOM 675 N6 A B 3 -2.665 15.903 31.113 1.00 31.51 N ANISOU 675 N6 A B 3 3857 3481 4636 -182 713 -769 N ATOM 676 N1 A B 3 -2.965 17.327 29.307 1.00 41.95 N ANISOU 676 N1 A B 3 5209 5053 5677 -238 665 -859 N ATOM 677 C2 A B 3 -3.778 17.830 28.367 1.00 41.32 C ANISOU 677 C2 A B 3 5151 5108 5443 -303 619 -918 C ATOM 678 N3 A B 3 -5.058 17.563 28.130 1.00 32.54 N ANISOU 678 N3 A B 3 4047 4037 4279 -387 573 -978 N ATOM 679 C4 A B 3 -5.506 16.652 29.004 1.00 25.70 C ANISOU 679 C4 A B 3 3173 3045 3545 -405 587 -977 C ATOM 680 P U B 4 -10.847 16.598 24.856 1.00 80.45 P ANISOU 680 P U B 4 10114 10509 9945 -809 246 -1301 P ATOM 681 OP1 U B 4 -11.857 15.535 25.096 1.00 77.98 O ANISOU 681 OP1 U B 4 9789 10113 9726 -892 221 -1370 O ATOM 682 OP2 U B 4 -9.963 16.542 23.665 1.00 84.39 O ANISOU 682 OP2 U B 4 10676 11057 10333 -797 293 -1386 O ATOM 683 O5' U B 4 -11.600 17.998 24.823 1.00 51.69 O ANISOU 683 O5' U B 4 6411 7039 6189 -799 140 -1181 O ATOM 684 C5' U B 4 -12.412 18.408 25.913 1.00 40.97 C ANISOU 684 C5' U B 4 4986 5669 4910 -790 95 -1078 C ATOM 685 C4' U B 4 -12.656 19.894 25.889 1.00 33.65 C ANISOU 685 C4' U B 4 4010 4883 3891 -742 28 -953 C ATOM 686 O4' U B 4 -11.467 20.582 26.367 1.00 30.55 O ANISOU 686 O4' U B 4 3636 4462 3511 -659 91 -891 O ATOM 687 C3' U B 4 -12.977 20.486 24.512 1.00 27.38 C ANISOU 687 C3' U B 4 3216 4262 2924 -768 -49 -958 C ATOM 688 O3' U B 4 -14.007 21.469 24.644 1.00 45.61 O ANISOU 688 O3' U B 4 5445 6677 5207 -757 -148 -842 O ATOM 689 C2' U B 4 -11.658 21.156 24.109 1.00 36.41 C ANISOU 689 C2' U B 4 4406 5436 3994 -703 11 -927 C ATOM 690 O2' U B 4 -11.787 22.240 23.214 1.00 41.14 O ANISOU 690 O2' U B 4 4991 6197 4443 -688 -53 -848 O ATOM 691 C1' U B 4 -11.117 21.608 25.460 1.00 26.49 C ANISOU 691 C1' U B 4 3125 4081 2857 -633 61 -844 C ATOM 692 N1 U B 4 -9.657 21.823 25.497 1.00 27.16 N ANISOU 692 N1 U B 4 3254 4115 2950 -571 146 -837 N ATOM 693 C2 U B 4 -9.165 23.074 25.853 1.00 23.87 C ANISOU 693 C2 U B 4 2813 3741 2515 -506 140 -724 C ATOM 694 O2 U B 4 -9.885 24.004 26.160 1.00 23.50 O ANISOU 694 O2 U B 4 2712 3770 2448 -494 72 -633 O ATOM 695 N3 U B 4 -7.790 23.220 25.855 1.00 20.22 N ANISOU 695 N3 U B 4 2388 3221 2073 -450 218 -714 N ATOM 696 C4 U B 4 -6.880 22.235 25.530 1.00 25.03 C ANISOU 696 C4 U B 4 3050 3737 2724 -443 302 -800 C ATOM 697 O4 U B 4 -5.679 22.480 25.568 1.00 29.83 O ANISOU 697 O4 U B 4 3674 4298 3361 -381 366 -766 O ATOM 698 C5 U B 4 -7.457 20.975 25.171 1.00 28.28 C ANISOU 698 C5 U B 4 3485 4108 3151 -509 308 -920 C ATOM 699 C6 U B 4 -8.786 20.815 25.160 1.00 25.77 C ANISOU 699 C6 U B 4 3137 3844 2810 -574 231 -937 C ATOM 700 P G B 5 -15.468 21.207 24.014 1.00 57.33 P ANISOU 700 P G B 5 6875 8254 6655 -837 -266 -864 P ATOM 701 OP1 G B 5 -15.413 19.941 23.242 1.00 57.02 O ANISOU 701 OP1 G B 5 6896 8184 6584 -924 -253 -1028 O ATOM 702 OP2 G B 5 -15.915 22.457 23.351 1.00 61.52 O ANISOU 702 OP2 G B 5 7355 8948 7073 -804 -359 -747 O ATOM 703 O5' G B 5 -16.403 20.970 25.282 1.00 45.69 O ANISOU 703 O5' G B 5 5327 6687 5348 -841 -276 -818 O ATOM 704 C5' G B 5 -16.293 19.775 26.039 1.00 49.39 C ANISOU 704 C5' G B 5 5822 6997 5945 -879 -204 -894 C ATOM 705 C4' G B 5 -17.046 19.840 27.346 1.00 56.11 C ANISOU 705 C4' G B 5 6604 7777 6939 -863 -199 -806 C ATOM 706 O4' G B 5 -16.444 20.788 28.259 1.00 60.57 O ANISOU 706 O4' G B 5 7168 8321 7526 -763 -149 -701 O ATOM 707 C3' G B 5 -18.497 20.279 27.289 1.00 61.09 C ANISOU 707 C3' G B 5 7124 8494 7592 -890 -303 -739 C ATOM 708 O3' G B 5 -19.363 19.267 26.806 1.00 66.86 O ANISOU 708 O3' G B 5 7827 9220 8357 -1000 -359 -828 O ATOM 709 C2' G B 5 -18.781 20.676 28.737 1.00 59.79 C ANISOU 709 C2' G B 5 6908 8256 7553 -830 -252 -630 C ATOM 710 O2' G B 5 -19.110 19.539 29.521 1.00 59.20 O ANISOU 710 O2' G B 5 6829 8059 7603 -890 -203 -660 O ATOM 711 C1' G B 5 -17.417 21.207 29.196 1.00 59.58 C ANISOU 711 C1' G B 5 6959 8187 7492 -742 -170 -604 C ATOM 712 N9 G B 5 -17.410 22.672 29.370 1.00 55.90 N ANISOU 712 N9 G B 5 6454 7793 6992 -650 -192 -492 N ATOM 713 C8 G B 5 -18.146 23.290 30.348 1.00 50.60 C ANISOU 713 C8 G B 5 5711 7102 6411 -602 -185 -397 C ATOM 714 N7 G B 5 -18.036 24.581 30.368 1.00 49.95 N ANISOU 714 N7 G B 5 5605 7067 6306 -519 -199 -314 N ATOM 715 C5 G B 5 -17.167 24.842 29.322 1.00 42.67 C ANISOU 715 C5 G B 5 4738 6211 5262 -517 -222 -342 C ATOM 716 C6 G B 5 -16.693 26.096 28.878 1.00 41.17 C ANISOU 716 C6 G B 5 4547 6088 5009 -447 -243 -265 C ATOM 717 O6 G B 5 -16.961 27.219 29.346 1.00 30.13 O ANISOU 717 O6 G B 5 3101 4684 3665 -369 -246 -168 O ATOM 718 N1 G B 5 -15.830 25.933 27.797 1.00 48.78 N ANISOU 718 N1 G B 5 5572 7118 5844 -477 -251 -313 N ATOM 719 C2 G B 5 -15.478 24.728 27.225 1.00 42.98 C ANISOU 719 C2 G B 5 4897 6375 5060 -555 -233 -436 C ATOM 720 N2 G B 5 -14.632 24.796 26.181 1.00 35.14 N ANISOU 720 N2 G B 5 3960 5450 3942 -566 -227 -470 N ATOM 721 N3 G B 5 -15.922 23.545 27.635 1.00 32.20 N ANISOU 721 N3 G B 5 3536 4928 3769 -617 -213 -517 N ATOM 722 C4 G B 5 -16.766 23.679 28.682 1.00 47.34 C ANISOU 722 C4 G B 5 5390 6793 5804 -597 -213 -456 C ATOM 723 P U B 7 -20.443 21.287 24.636 1.00 88.70 P ANISOU 723 P U B 7 10483 12355 10864 -972 -603 -718 P ATOM 724 OP1 U B 7 -20.003 19.950 24.162 1.00 92.73 O ANISOU 724 OP1 U B 7 11083 12801 11348 -1066 -569 -885 O ATOM 725 OP2 U B 7 -20.597 22.395 23.659 1.00 91.24 O ANISOU 725 OP2 U B 7 10775 12844 11048 -931 -696 -634 O ATOM 726 O5' U B 7 -21.828 21.110 25.404 1.00 86.74 O ANISOU 726 O5' U B 7 10102 12072 10784 -1003 -650 -667 O ATOM 727 C5' U B 7 -21.907 21.239 26.817 1.00 82.51 C ANISOU 727 C5' U B 7 9530 11420 10398 -950 -562 -592 C ATOM 728 C4' U B 7 -22.379 22.613 27.222 1.00 79.21 C ANISOU 728 C4' U B 7 9021 11058 10019 -845 -582 -448 C ATOM 729 O4' U B 7 -21.278 23.363 27.798 1.00 73.36 O ANISOU 729 O4' U B 7 8355 10270 9248 -743 -490 -395 O ATOM 730 C3' U B 7 -22.885 23.504 26.097 1.00 80.06 C ANISOU 730 C3' U B 7 9066 11323 10029 -823 -706 -393 C ATOM 731 O3' U B 7 -24.223 23.217 25.725 1.00 84.42 O ANISOU 731 O3' U B 7 9492 11940 10644 -889 -816 -397 O ATOM 732 C2' U B 7 -22.698 24.903 26.668 1.00 75.57 C ANISOU 732 C2' U B 7 8466 10752 9495 -689 -666 -258 C ATOM 733 O2' U B 7 -23.755 25.219 27.562 1.00 74.06 O ANISOU 733 O2' U B 7 8146 10518 9474 -653 -654 -194 O ATOM 734 C1' U B 7 -21.412 24.734 27.481 1.00 71.86 C ANISOU 734 C1' U B 7 8116 10166 9021 -654 -536 -288 C ATOM 735 N1 U B 7 -20.201 25.179 26.748 1.00 66.71 N ANISOU 735 N1 U B 7 7565 9563 8219 -623 -524 -291 N ATOM 736 C2 U B 7 -19.897 26.528 26.753 1.00 58.15 C ANISOU 736 C2 U B 7 6466 8511 7117 -522 -523 -175 C ATOM 737 O2 U B 7 -20.584 27.360 27.318 1.00 58.57 O ANISOU 737 O2 U B 7 6432 8547 7275 -452 -529 -83 O ATOM 738 N3 U B 7 -18.759 26.876 26.065 1.00 55.39 N ANISOU 738 N3 U B 7 6202 8208 6636 -505 -506 -171 N ATOM 739 C4 U B 7 -17.902 26.034 25.385 1.00 56.70 C ANISOU 739 C4 U B 7 6464 8390 6688 -570 -480 -281 C ATOM 740 O4 U B 7 -16.911 26.499 24.810 1.00 51.39 O ANISOU 740 O4 U B 7 5851 7763 5910 -544 -456 -260 O ATOM 741 C5 U B 7 -18.281 24.653 25.431 1.00 63.79 C ANISOU 741 C5 U B 7 7378 9240 7619 -665 -477 -411 C ATOM 742 C6 U B 7 -19.384 24.283 26.095 1.00 67.65 C ANISOU 742 C6 U B 7 7786 9684 8235 -690 -502 -406 C TER 743 U B 7 HETATM 744 S SO4 A 201 -8.100 16.119 51.807 1.00 93.64 S ANISOU 744 S SO4 A 201 11931 12082 11566 -239 430 1315 S HETATM 745 O1 SO4 A 201 -6.745 16.454 51.375 1.00 98.07 O ANISOU 745 O1 SO4 A 201 12463 12642 12158 -171 316 1319 O HETATM 746 O2 SO4 A 201 -9.055 16.561 50.796 1.00 91.16 O ANISOU 746 O2 SO4 A 201 11579 11726 11331 -289 506 1150 O HETATM 747 O3 SO4 A 201 -8.208 14.673 51.982 1.00 98.67 O ANISOU 747 O3 SO4 A 201 12569 12574 12349 -244 467 1456 O HETATM 748 O4 SO4 A 201 -8.391 16.786 53.072 1.00 92.50 O ANISOU 748 O4 SO4 A 201 11846 12124 11176 -252 432 1321 O HETATM 749 S SO4 A 202 -4.803 20.395 50.343 1.00 74.66 S ANISOU 749 S SO4 A 202 9452 9972 8945 -119 67 899 S HETATM 750 O1 SO4 A 202 -5.410 21.671 49.978 1.00 65.03 O ANISOU 750 O1 SO4 A 202 8239 8807 7663 -147 100 693 O HETATM 751 O2 SO4 A 202 -4.318 19.705 49.149 1.00 71.00 O ANISOU 751 O2 SO4 A 202 8929 9328 8720 -81 72 895 O HETATM 752 O3 SO4 A 202 -5.799 19.563 51.015 1.00 76.15 O ANISOU 752 O3 SO4 A 202 9677 10164 9091 -155 168 1029 O HETATM 753 O4 SO4 A 202 -3.682 20.640 51.244 1.00 78.99 O ANISOU 753 O4 SO4 A 202 10005 10643 9363 -95 -68 982 O HETATM 754 O HOH A 301 -2.874 15.122 25.936 1.00 54.31 O ANISOU 754 O HOH A 301 6900 6606 7128 -336 816 -1240 O HETATM 755 O HOH A 302 -2.272 20.259 29.277 1.00 38.50 O ANISOU 755 O HOH A 302 4728 4853 5046 -171 568 -684 O HETATM 756 O HOH A 303 -16.260 18.891 31.141 1.00 49.50 O ANISOU 756 O HOH A 303 5793 6581 6433 -777 26 -669 O HETATM 757 O HOH A 304 -14.901 21.143 44.459 1.00 85.01 O ANISOU 757 O HOH A 304 10378 11043 10879 -396 567 203 O HETATM 758 O HOH A 305 -6.869 33.359 42.755 1.00 15.71 O ANISOU 758 O HOH A 305 1766 2216 1986 -54 179 -418 O HETATM 759 O HOH A 306 -14.655 20.389 41.851 1.00 19.95 O ANISOU 759 O HOH A 306 2116 2676 2787 -452 452 60 O HETATM 760 O HOH A 307 -16.704 27.300 37.042 1.00 10.19 O ANISOU 760 O HOH A 307 672 1708 1493 -192 165 -96 O HETATM 761 O HOH A 308 -15.830 27.010 39.699 1.00 17.81 O ANISOU 761 O HOH A 308 1740 2617 2411 -164 290 -89 O HETATM 762 O HOH A 309 -7.364 37.229 36.287 1.00 10.95 O ANISOU 762 O HOH A 309 947 1368 1846 86 187 -69 O HETATM 763 O HOH A 310 -2.799 33.610 29.962 1.00 23.00 O ANISOU 763 O HOH A 310 2508 3269 2961 -65 270 154 O HETATM 764 O HOH A 311 -3.073 36.739 35.133 1.00 30.27 O ANISOU 764 O HOH A 311 3401 3802 4297 -51 163 -5 O HETATM 765 O HOH A 312 0.737 38.535 27.677 1.00 25.90 O ANISOU 765 O HOH A 312 2787 3426 3626 -115 439 616 O HETATM 766 O HOH A 313 5.557 32.735 44.319 1.00 40.04 O ANISOU 766 O HOH A 313 4450 5444 5320 -323 -517 -158 O HETATM 767 O HOH A 314 4.050 25.721 27.773 1.00 14.77 O ANISOU 767 O HOH A 314 1485 2128 1998 68 667 -223 O HETATM 768 O HOH A 315 -17.008 17.767 41.012 1.00 20.93 O ANISOU 768 O HOH A 315 2136 2680 3135 -666 470 56 O HETATM 769 O HOH A 316 -13.260 14.029 37.665 1.00 24.95 O ANISOU 769 O HOH A 316 2884 2648 3948 -707 477 -277 O HETATM 770 O HOH A 317 3.472 32.187 33.983 1.00 25.44 O ANISOU 770 O HOH A 317 2718 3351 3597 -82 196 20 O HETATM 771 O HOH A 318 -4.358 18.582 37.276 1.00 11.53 O ANISOU 771 O HOH A 318 1237 1093 2053 -131 426 -179 O HETATM 772 O HOH A 319 -2.979 30.971 23.504 1.00 42.36 O ANISOU 772 O HOH A 319 5152 6254 4688 -166 397 80 O HETATM 773 O HOH A 320 -21.506 20.728 31.990 1.00 29.06 O ANISOU 773 O HOH A 320 2760 4242 4038 -817 -177 -384 O HETATM 774 O HOH A 321 -1.572 23.057 25.484 1.00 26.96 O ANISOU 774 O HOH A 321 3317 3790 3136 -173 587 -641 O HETATM 775 O HOH A 322 -3.350 33.087 25.691 1.00 39.84 O ANISOU 775 O HOH A 322 4710 5779 4649 -109 329 278 O HETATM 776 O HOH A 323 -2.859 25.793 24.282 1.00 24.99 O ANISOU 776 O HOH A 323 3056 3829 2608 -216 470 -460 O HETATM 777 O HOH A 324 3.243 26.704 42.769 1.00 37.85 O ANISOU 777 O HOH A 324 4225 5058 5097 -1 -262 160 O HETATM 778 O HOH A 325 -11.251 28.356 53.989 1.00 52.47 O ANISOU 778 O HOH A 325 6884 7577 5474 -159 603 -150 O HETATM 779 O HOH A 326 -4.523 15.746 38.767 1.00 49.41 O ANISOU 779 O HOH A 326 6061 5565 7147 -130 516 5 O HETATM 780 O HOH A 327 1.307 27.043 43.968 1.00 28.49 O ANISOU 780 O HOH A 327 3197 3940 3686 -52 -254 103 O HETATM 781 O HOH A 328 -1.566 18.777 43.227 1.00 17.68 O ANISOU 781 O HOH A 328 1953 2018 2748 77 152 509 O HETATM 782 O HOH A 329 6.907 31.439 34.658 1.00 42.68 O ANISOU 782 O HOH A 329 4735 5524 5959 -73 181 57 O HETATM 783 O HOH A 330 1.764 36.491 34.992 1.00 27.61 O ANISOU 783 O HOH A 330 3001 3442 4047 -164 142 24 O HETATM 784 O HOH A 331 4.796 32.600 35.734 1.00 28.48 O ANISOU 784 O HOH A 331 3033 3703 4084 -114 102 12 O HETATM 785 O HOH A 332 -10.489 25.590 45.897 1.00 39.33 O ANISOU 785 O HOH A 332 4805 5451 4686 -196 421 5 O HETATM 786 O HOH A 333 -11.719 29.895 43.521 1.00 34.66 O ANISOU 786 O HOH A 333 4120 4744 4305 -55 356 -229 O HETATM 787 O HOH A 334 -1.548 17.022 39.169 1.00 28.25 O ANISOU 787 O HOH A 334 3285 2996 4453 75 421 135 O HETATM 788 O HOH A 335 3.432 23.871 45.360 1.00 47.41 O ANISOU 788 O HOH A 335 5453 6332 6229 88 -397 497 O HETATM 789 O HOH A 336 -18.588 26.545 46.981 1.00 50.04 O ANISOU 789 O HOH A 336 5835 6890 6289 -114 802 56 O HETATM 790 O HOH A 337 -8.918 36.968 33.014 1.00 39.82 O ANISOU 790 O HOH A 337 4498 5220 5410 136 123 211 O HETATM 791 O HOH A 338 -14.082 28.826 42.863 1.00 30.51 O ANISOU 791 O HOH A 338 3495 4226 3869 -68 401 -145 O HETATM 792 O HOH A 339 -17.190 27.044 41.769 1.00 40.46 O ANISOU 792 O HOH A 339 4564 5523 5284 -144 427 -43 O HETATM 793 O HOH A 340 -28.815 18.558 33.628 1.00 45.83 O ANISOU 793 O HOH A 340 4093 6411 6909 -1208 -259 -106 O HETATM 794 O HOH A 341 -0.382 37.945 36.444 1.00 40.90 O ANISOU 794 O HOH A 341 4707 5003 5831 -164 119 -86 O HETATM 795 O HOH A 342 1.588 25.347 46.911 1.00 60.05 O ANISOU 795 O HOH A 342 7240 8110 7466 -36 -419 356 O HETATM 796 O HOH A 343 -9.137 29.836 53.141 1.00 56.78 O ANISOU 796 O HOH A 343 7427 8080 6068 -174 384 -319 O HETATM 797 O HOH A 344 -8.606 30.136 49.585 1.00 40.86 O ANISOU 797 O HOH A 344 5223 5846 4456 -147 315 -342 O HETATM 798 O HOH A 345 -4.395 34.143 47.552 1.00 56.02 O ANISOU 798 O HOH A 345 7071 7518 6695 -209 1 -666 O HETATM 799 O HOH A 346 -6.747 34.036 45.178 1.00 24.93 O ANISOU 799 O HOH A 346 3033 3449 2991 -91 190 -575 O HETATM 800 O HOH A 347 4.112 34.913 34.152 1.00 33.33 O ANISOU 800 O HOH A 347 3669 4259 4737 -157 177 64 O HETATM 801 O HOH A 348 -2.583 16.610 41.836 1.00 44.30 O ANISOU 801 O HOH A 348 5359 5084 6389 41 339 432 O HETATM 802 O HOH A 349 -6.492 31.820 47.962 1.00 37.62 O ANISOU 802 O HOH A 349 4759 5321 4215 -158 152 -490 O HETATM 803 O HOH A 350 -17.624 18.873 43.604 1.00 24.84 O ANISOU 803 O HOH A 350 2608 3351 3482 -597 590 235 O HETATM 804 O HOH A 351 0.137 40.395 29.581 1.00 33.72 O ANISOU 804 O HOH A 351 3737 4144 4932 -112 375 611 O HETATM 805 O HOH A 352 -10.055 30.619 55.017 1.00 44.21 O ANISOU 805 O HOH A 352 5945 6578 4273 -161 501 -422 O HETATM 806 O HOH A 353 0.946 42.240 30.628 1.00 53.09 O ANISOU 806 O HOH A 353 6157 6345 7670 -154 369 587 O HETATM 807 O HOH A 354 -5.721 40.985 31.378 1.00 55.72 O ANISOU 807 O HOH A 354 6520 6870 7781 128 225 546 O HETATM 808 O HOH A 355 2.485 30.106 53.858 1.00 59.77 O ANISOU 808 O HOH A 355 7541 8674 6495 -351 -860 -123 O HETATM 809 O HOH A 356 6.205 12.961 48.937 1.00 54.51 O ANISOU 809 O HOH A 356 6172 6575 7964 586 -309 1784 O HETATM 810 O HOH B 101 -6.065 13.013 33.988 1.00 39.18 O ANISOU 810 O HOH B 101 4845 4114 5926 -345 688 -640 O HETATM 811 O HOH B 102 -14.392 27.631 26.721 1.00 36.32 O ANISOU 811 O HOH B 102 4027 5659 4113 -396 -257 -195 O HETATM 812 O HOH B 103 -20.707 24.647 30.543 1.00 31.71 O ANISOU 812 O HOH B 103 3080 4813 4156 -557 -291 -242 O HETATM 813 O HOH B 104 -4.787 24.254 23.686 1.00 35.04 O ANISOU 813 O HOH B 104 4364 5168 3782 -338 382 -648 O HETATM 814 O HOH B 105 -3.912 13.922 32.630 1.00 55.62 O ANISOU 814 O HOH B 105 6918 6287 7930 -229 735 -717 O HETATM 815 O HOH B 106 -23.071 23.286 31.099 1.00 46.71 O ANISOU 815 O HOH B 106 4784 6689 6274 -690 -325 -246 O CONECT 744 745 746 747 748 CONECT 745 744 CONECT 746 744 CONECT 747 744 CONECT 748 744 CONECT 749 750 751 752 753 CONECT 750 749 CONECT 751 749 CONECT 752 749 CONECT 753 749 MASTER 264 0 2 1 6 0 3 6 779 2 10 8 END
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Related entries of code: 5ytt
Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code
Check Database
Protein Sequence Similarity
6a6j
RCSB PDB
PDBbind
93aa, >6A6J_1|Chains... *
5ytx
RCSB PDB
PDBbind
83aa, >5YTX_1|Chain... at 97%
5ytv
RCSB PDB
PDBbind
83aa, >5YTV_1|Chain... at 97%
5yts
RCSB PDB
PDBbind
83aa, >5YTS_1|Chain... at 97%
Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
No complexes with the same small molecule ligand are found!
Entry Information
PDB ID
5ytt
Complex Type
Protein-Nucleic Acid
PDBbind Subset
general set
Protein Name
Nuclease-sensitive element-binding protein 1, YB1 cold-shock domain
Ligand Name
RNA C4G (UCAUGU)
EC.Number
E.C.-.-.-.-
Resolution
1.6(Å)
Affinity (Kd/Ki/IC50)
Kd=3.77uM
Release Year
2018
Protein/NA Sequence
Check fasta file
Primary Reference
(2019) J.Biol.Chem. Vol. 294: pp. 10998-11010
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
P67809
Entrez Gene ID
NCBI Entrez Gene ID:
4904
ASD
Information of known allosteric effects of PDB entries
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