Browse entries in the PDBbind-CN Database
HEADER RNA BINDING PROTEIN/RNA 20-NOV-17 5YTX TITLE CRYSTAL STRUCTURE OF YB1 COLD-SHOCK DOMAIN IN COMPLEX WITH UCAACU 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*AP*CP*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, CAAC, RNA BINDING PROTEIN, RNA BINDING KEYWDS 2 PROTEIN-RNA COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR X.YANG,Y.HUANG REVDAT 3 24-JUL-19 5YTX 1 JRNL REVDAT 2 19-JUN-19 5YTX 1 JRNL REVDAT 1 05-DEC-18 5YTX 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. 1.55 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) : 1.55 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.80 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.400 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0 REMARK 3 NUMBER OF REFLECTIONS : 12345 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.204 REMARK 3 R VALUE (WORKING SET) : 0.200 REMARK 3 FREE R VALUE : 0.240 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.830 REMARK 3 FREE R VALUE TEST SET COUNT : 1213 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 28.8055 - 3.2244 0.97 1256 138 0.1830 0.2156 REMARK 3 2 3.2244 - 2.5598 0.99 1237 129 0.2044 0.2538 REMARK 3 3 2.5598 - 2.2363 0.99 1253 136 0.1862 0.2198 REMARK 3 4 2.2363 - 2.0319 0.99 1247 131 0.1745 0.2289 REMARK 3 5 2.0319 - 1.8863 0.99 1238 132 0.1912 0.2343 REMARK 3 6 1.8863 - 1.7751 0.99 1207 137 0.2044 0.2510 REMARK 3 7 1.7751 - 1.6862 1.00 1243 135 0.2605 0.2980 REMARK 3 8 1.6862 - 1.6128 1.00 1238 142 0.3002 0.3416 REMARK 3 9 1.6128 - 1.5508 0.99 1213 133 0.3269 0.3657 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) : 0.220 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.310 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 : 0.006 698 REMARK 3 ANGLE : 0.919 962 REMARK 3 CHIRALITY : 0.037 114 REMARK 3 PLANARITY : 0.004 109 REMARK 3 DIHEDRAL : 11.942 271 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): -23.0586 -6.8096 -35.2714 REMARK 3 T TENSOR REMARK 3 T11: 0.1936 T22: 0.1589 REMARK 3 T33: 0.1954 T12: -0.0083 REMARK 3 T13: -0.0194 T23: -0.0045 REMARK 3 L TENSOR REMARK 3 L11: 4.5388 L22: 5.0538 REMARK 3 L33: 2.6391 L12: -1.5298 REMARK 3 L13: 0.0896 L23: -1.1461 REMARK 3 S TENSOR REMARK 3 S11: -0.0437 S12: -0.1801 S13: 0.2135 REMARK 3 S21: 0.1607 S22: -0.0346 S23: -0.4653 REMARK 3 S31: -0.1685 S32: 0.2495 S33: 0.0337 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 5YTX 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_1300005910. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 21-DEC-14 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRF REMARK 200 BEAMLINE : BL19U1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97915 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-3000 REMARK 200 DATA SCALING SOFTWARE : HKL-3000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12349 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9 REMARK 200 DATA REDUNDANCY : 6.000 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 35.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.61 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 (%): 37.95 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98 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 22.42200 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 11.21100 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 22.42200 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 11.21100 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 94 REMARK 465 ASN A 95 REMARK 465 PRO A 96 REMARK 465 ARG A 97 REMARK 465 GLY A 130 REMARK 465 U B 1 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 249 DISTANCE = 7.60 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5YTS RELATED DB: PDB REMARK 900 RELATED ID: 5YTT RELATED DB: PDB REMARK 900 RELATED ID: 5YTV RELATED DB: PDB DBREF 5YTX A 50 130 UNP P67809 YBOX1_HUMAN 50 130 DBREF 5YTX B 1 6 PDB 5YTX 5YTX 1 6 SEQADV 5YTX GLY A 48 UNP P67809 EXPRESSION TAG SEQADV 5YTX 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 6 U C A A C U FORMUL 3 HOH *50(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 CRYST1 66.512 66.512 33.633 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 0.015035 0.008680 0.000000 0.00000 SCALE2 0.000000 0.017361 0.000000 0.00000 SCALE3 0.000000 0.000000 0.029733 0.00000 ATOM 1 N LYS A 52 -9.183 -9.720 -37.541 1.00 73.42 N ANISOU 1 N LYS A 52 6857 9318 11722 92 256 1121 N ATOM 2 CA LYS A 52 -9.455 -10.446 -38.778 1.00 67.95 C ANISOU 2 CA LYS A 52 6312 8640 10865 295 631 1146 C ATOM 3 C LYS A 52 -9.541 -11.952 -38.544 1.00 55.73 C ANISOU 3 C LYS A 52 4855 7112 9207 506 640 1097 C ATOM 4 O LYS A 52 -10.046 -12.681 -39.396 1.00 55.02 O ANISOU 4 O LYS A 52 4983 7005 8917 671 872 1035 O ATOM 5 CB LYS A 52 -8.385 -10.144 -39.832 1.00 73.84 C ANISOU 5 CB LYS A 52 6886 9390 11780 338 924 1316 C ATOM 6 CG LYS A 52 -7.641 -8.837 -39.616 1.00 76.17 C ANISOU 6 CG LYS A 52 6977 9628 12335 118 804 1412 C ATOM 7 CD LYS A 52 -6.605 -8.596 -40.705 1.00 78.01 C ANISOU 7 CD LYS A 52 7075 9857 12709 183 1111 1602 C ATOM 8 CE LYS A 52 -5.284 -9.276 -40.378 1.00 85.13 C ANISOU 8 CE LYS A 52 7714 10787 13844 259 1083 1700 C ATOM 9 NZ LYS A 52 -4.601 -8.631 -39.219 1.00 77.80 N ANISOU 9 NZ LYS A 52 6549 9814 13197 53 717 1704 N ATOM 10 N LYS A 53 -9.060 -12.412 -37.389 1.00 46.17 N ANISOU 10 N LYS A 53 3489 5927 8128 504 371 1122 N ATOM 11 CA LYS A 53 -9.114 -13.835 -37.044 1.00 37.23 C ANISOU 11 CA LYS A 53 2428 4785 6931 702 360 1111 C ATOM 12 C LYS A 53 -10.554 -14.334 -36.911 1.00 33.12 C ANISOU 12 C LYS A 53 2311 4208 6065 718 320 944 C ATOM 13 O LYS A 53 -11.311 -13.874 -36.048 1.00 32.41 O ANISOU 13 O LYS A 53 2368 4129 5819 581 81 863 O ATOM 14 CB LYS A 53 -8.353 -14.098 -35.746 1.00 40.56 C ANISOU 14 CB LYS A 53 2681 5253 7475 668 38 1172 C ATOM 15 CG LYS A 53 -8.104 -15.559 -35.466 1.00 44.82 C ANISOU 15 CG LYS A 53 3260 5769 7999 874 60 1212 C ATOM 16 CD LYS A 53 -6.956 -15.751 -34.476 1.00 56.33 C ANISOU 16 CD LYS A 53 4494 7292 9616 862 -183 1312 C ATOM 17 CE LYS A 53 -5.679 -15.092 -34.980 1.00 60.61 C ANISOU 17 CE LYS A 53 4751 7860 10419 792 -94 1403 C ATOM 18 NZ LYS A 53 -4.529 -15.226 -34.033 1.00 62.67 N ANISOU 18 NZ LYS A 53 4770 8183 10857 777 -351 1495 N ATOM 19 N VAL A 54 -10.926 -15.282 -37.761 1.00 34.36 N ANISOU 19 N VAL A 54 2641 4298 6117 892 554 888 N ATOM 20 CA VAL A 54 -12.284 -15.811 -37.744 1.00 34.11 C ANISOU 20 CA VAL A 54 2952 4189 5821 896 519 737 C ATOM 21 C VAL A 54 -12.465 -16.834 -36.620 1.00 29.43 C ANISOU 21 C VAL A 54 2389 3551 5243 956 332 771 C ATOM 22 O VAL A 54 -11.754 -17.844 -36.552 1.00 31.54 O ANISOU 22 O VAL A 54 2538 3771 5676 1128 387 856 O ATOM 23 CB VAL A 54 -12.656 -16.450 -39.095 1.00 34.25 C ANISOU 23 CB VAL A 54 3163 4128 5721 1048 795 631 C ATOM 24 CG1 VAL A 54 -14.099 -16.897 -39.083 1.00 33.84 C ANISOU 24 CG1 VAL A 54 3428 3984 5447 1011 713 473 C ATOM 25 CG2 VAL A 54 -12.422 -15.460 -40.227 1.00 38.24 C ANISOU 25 CG2 VAL A 54 3649 4703 6177 1023 1007 644 C ATOM 26 N ILE A 55 -13.432 -16.560 -35.748 1.00 28.35 N ANISOU 26 N ILE A 55 2413 3426 4935 831 133 724 N ATOM 27 CA AILE A 55 -13.717 -17.415 -34.602 0.47 31.81 C ANISOU 27 CA AILE A 55 2901 3840 5347 880 -32 794 C ATOM 28 CA BILE A 55 -13.705 -17.419 -34.605 0.53 31.82 C ANISOU 28 CA BILE A 55 2900 3841 5350 881 -32 795 C ATOM 29 C ILE A 55 -14.850 -18.384 -34.911 1.00 33.71 C ANISOU 29 C ILE A 55 3387 3931 5491 933 62 720 C ATOM 30 O ILE A 55 -14.814 -19.557 -34.520 1.00 35.93 O ANISOU 30 O ILE A 55 3681 4110 5861 1054 57 802 O ATOM 31 CB AILE A 55 -14.078 -16.573 -33.366 0.47 34.69 C ANISOU 31 CB AILE A 55 3298 4318 5565 738 -289 803 C ATOM 32 CB BILE A 55 -14.035 -16.575 -33.363 0.53 34.88 C ANISOU 32 CB BILE A 55 3313 4343 5595 740 -291 806 C ATOM 33 CG1AILE A 55 -12.844 -15.821 -32.873 0.47 38.09 C ANISOU 33 CG1AILE A 55 3463 4867 6145 688 -460 874 C ATOM 34 CG1BILE A 55 -12.850 -15.667 -33.020 0.53 38.41 C ANISOU 34 CG1BILE A 55 3501 4905 6188 671 -441 858 C ATOM 35 CG2AILE A 55 -14.633 -17.445 -32.257 0.47 37.15 C ANISOU 35 CG2AILE A 55 3726 4616 5772 802 -408 891 C ATOM 36 CG2BILE A 55 -14.390 -17.459 -32.186 0.53 37.35 C ANISOU 36 CG2BILE A 55 3708 4656 5829 815 -428 912 C ATOM 37 CD1AILE A 55 -11.674 -16.719 -32.624 0.47 40.84 C ANISOU 37 CD1AILE A 55 3570 5225 6721 845 -492 1036 C ATOM 38 CD1BILE A 55 -13.178 -14.586 -32.009 0.53 35.77 C ANISOU 38 CD1BILE A 55 3229 4664 5697 518 -697 793 C ATOM 39 N ALA A 56 -15.851 -17.891 -35.628 1.00 27.09 N ANISOU 39 N ALA A 56 2728 3063 4500 840 135 575 N ATOM 40 CA ALA A 56 -16.991 -18.711 -35.998 1.00 24.92 C ANISOU 40 CA ALA A 56 2663 2639 4166 857 189 485 C ATOM 41 C ALA A 56 -17.594 -18.244 -37.320 1.00 26.34 C ANISOU 41 C ALA A 56 2982 2796 4229 818 308 314 C ATOM 42 O ALA A 56 -17.480 -17.072 -37.687 1.00 27.46 O ANISOU 42 O ALA A 56 3095 3051 4286 737 327 290 O ATOM 43 CB ALA A 56 -18.037 -18.693 -34.888 1.00 29.80 C ANISOU 43 CB ALA A 56 3376 3266 4680 760 49 539 C ATOM 44 N THR A 57 -18.209 -19.159 -38.063 1.00 24.77 N ANISOU 44 N THR A 57 2939 2440 4033 882 375 195 N ATOM 45 CA THR A 57 -18.932 -18.732 -39.267 1.00 23.22 C ANISOU 45 CA THR A 57 2906 2239 3679 849 434 24 C ATOM 46 C THR A 57 -20.376 -19.217 -39.280 1.00 24.59 C ANISOU 46 C THR A 57 3240 2283 3821 766 329 -75 C ATOM 47 O THR A 57 -20.721 -20.200 -38.612 1.00 26.95 O ANISOU 47 O THR A 57 3540 2439 4261 769 269 -26 O ATOM 48 CB THR A 57 -18.261 -19.228 -40.570 1.00 29.56 C ANISOU 48 CB THR A 57 3770 2991 4469 1025 617 -90 C ATOM 49 OG1 THR A 57 -18.260 -20.661 -40.607 1.00 32.74 O ANISOU 49 OG1 THR A 57 4241 3187 5012 1147 629 -157 O ATOM 50 CG2 THR A 57 -16.856 -18.680 -40.714 1.00 33.69 C ANISOU 50 CG2 THR A 57 4096 3649 5055 1109 764 31 C ATOM 51 N LYS A 58 -21.196 -18.515 -40.057 1.00 23.23 N ANISOU 51 N LYS A 58 3182 2158 3487 693 307 -189 N ATOM 52 CA LYS A 58 -22.594 -18.874 -40.280 1.00 26.30 C ANISOU 52 CA LYS A 58 3694 2435 3864 608 191 -296 C ATOM 53 C LYS A 58 -23.351 -18.944 -38.967 1.00 24.16 C ANISOU 53 C LYS A 58 3343 2142 3694 492 95 -156 C ATOM 54 O LYS A 58 -24.154 -19.851 -38.733 1.00 28.62 O ANISOU 54 O LYS A 58 3934 2542 4400 452 31 -162 O ATOM 55 CB LYS A 58 -22.694 -20.202 -41.038 1.00 37.29 C ANISOU 55 CB LYS A 58 5210 3613 5344 703 190 -461 C ATOM 56 CG LYS A 58 -22.004 -20.171 -42.394 1.00 47.03 C ANISOU 56 CG LYS A 58 6567 4884 6420 859 312 -620 C ATOM 57 CD LYS A 58 -22.033 -21.532 -43.073 1.00 56.04 C ANISOU 57 CD LYS A 58 7860 5789 7642 980 306 -823 C ATOM 58 CE LYS A 58 -21.134 -21.556 -44.307 1.00 65.07 C ANISOU 58 CE LYS A 58 9131 6991 8601 1194 486 -963 C ATOM 59 NZ LYS A 58 -19.698 -21.327 -43.966 1.00 69.42 N ANISOU 59 NZ LYS A 58 9502 7656 9220 1318 702 -782 N ATOM 60 N VAL A 59 -23.066 -17.974 -38.108 1.00 20.23 N ANISOU 60 N VAL A 59 2751 1806 3129 444 92 -27 N ATOM 61 CA VAL A 59 -23.724 -17.831 -36.821 1.00 20.77 C ANISOU 61 CA VAL A 59 2769 1906 3215 367 31 108 C ATOM 62 C VAL A 59 -25.031 -17.076 -37.028 1.00 17.85 C ANISOU 62 C VAL A 59 2446 1571 2766 264 -14 57 C ATOM 63 O VAL A 59 -25.064 -16.103 -37.779 1.00 20.07 O ANISOU 63 O VAL A 59 2763 1934 2926 245 -11 -26 O ATOM 64 CB VAL A 59 -22.827 -17.059 -35.809 1.00 22.29 C ANISOU 64 CB VAL A 59 2870 2260 3338 378 17 225 C ATOM 65 CG1 VAL A 59 -23.513 -16.935 -34.466 1.00 23.51 C ANISOU 65 CG1 VAL A 59 3019 2468 3446 338 -31 350 C ATOM 66 CG2 VAL A 59 -21.448 -17.740 -35.660 1.00 25.35 C ANISOU 66 CG2 VAL A 59 3167 2632 3832 491 44 293 C ATOM 67 N LEU A 60 -26.098 -17.531 -36.383 1.00 18.92 N ANISOU 67 N LEU A 60 2561 1637 2989 207 -43 134 N ATOM 68 CA LEU A 60 -27.379 -16.825 -36.459 1.00 19.62 C ANISOU 68 CA LEU A 60 2649 1763 3042 122 -76 117 C ATOM 69 C LEU A 60 -27.589 -16.018 -35.192 1.00 16.98 C ANISOU 69 C LEU A 60 2276 1566 2610 117 -37 247 C ATOM 70 O LEU A 60 -27.211 -16.449 -34.107 1.00 19.54 O ANISOU 70 O LEU A 60 2575 1913 2936 159 -5 381 O ATOM 71 CB LEU A 60 -28.536 -17.820 -36.651 1.00 21.24 C ANISOU 71 CB LEU A 60 2826 1794 3449 57 -124 120 C ATOM 72 CG LEU A 60 -28.567 -18.503 -38.012 1.00 25.19 C ANISOU 72 CG LEU A 60 3404 2148 4017 57 -212 -74 C ATOM 73 CD1 LEU A 60 -29.493 -19.709 -37.977 1.00 32.51 C ANISOU 73 CD1 LEU A 60 4283 2847 5223 -21 -285 -62 C ATOM 74 CD2 LEU A 60 -29.032 -17.509 -39.076 1.00 24.82 C ANISOU 74 CD2 LEU A 60 3418 2202 3812 38 -283 -212 C ATOM 75 N GLY A 61 -28.203 -14.842 -35.320 1.00 18.57 N ANISOU 75 N GLY A 61 2488 1857 2710 85 -42 205 N ATOM 76 CA GLY A 61 -28.436 -14.050 -34.136 1.00 15.98 C ANISOU 76 CA GLY A 61 2156 1644 2272 104 1 287 C ATOM 77 C GLY A 61 -29.553 -13.065 -34.367 1.00 18.63 C ANISOU 77 C GLY A 61 2485 2013 2581 78 12 253 C ATOM 78 O GLY A 61 -30.026 -12.916 -35.486 1.00 18.80 O ANISOU 78 O GLY A 61 2501 1986 2654 41 -39 173 O ATOM 79 N THR A 62 -29.967 -12.402 -33.303 1.00 17.81 N ANISOU 79 N THR A 62 2390 1995 2381 119 76 314 N ATOM 80 CA ATHR A 62 -31.038 -11.419 -33.381 0.54 17.33 C ANISOU 80 CA ATHR A 62 2314 1962 2310 127 113 295 C ATOM 81 CA BTHR A 62 -31.025 -11.409 -33.434 0.46 16.98 C ANISOU 81 CA BTHR A 62 2270 1915 2267 125 109 290 C ATOM 82 C THR A 62 -30.472 -10.044 -33.097 1.00 18.07 C ANISOU 82 C THR A 62 2499 2120 2247 163 101 200 C ATOM 83 O THR A 62 -29.771 -9.875 -32.107 1.00 19.44 O ANISOU 83 O THR A 62 2737 2358 2293 206 101 197 O ATOM 84 CB ATHR A 62 -32.150 -11.714 -32.372 0.54 22.31 C ANISOU 84 CB ATHR A 62 2878 2620 2977 172 240 442 C ATOM 85 CB BTHR A 62 -32.234 -11.710 -32.532 0.46 21.89 C ANISOU 85 CB BTHR A 62 2816 2556 2945 162 231 435 C ATOM 86 OG1ATHR A 62 -32.534 -13.095 -32.467 0.54 26.18 O ANISOU 86 OG1ATHR A 62 3269 3016 3661 120 251 558 O ATOM 87 OG1BTHR A 62 -31.816 -11.796 -31.162 0.46 20.58 O ANISOU 87 OG1BTHR A 62 2717 2482 2619 246 315 516 O ATOM 88 CG2ATHR A 62 -33.350 -10.810 -32.621 0.54 18.83 C ANISOU 88 CG2ATHR A 62 2379 2190 2587 192 286 433 C ATOM 89 CG2BTHR A 62 -32.899 -13.023 -32.952 0.46 25.45 C ANISOU 89 CG2BTHR A 62 3141 2892 3635 90 221 530 C ATOM 90 N VAL A 63 -30.789 -9.068 -33.939 1.00 14.93 N ANISOU 90 N VAL A 63 2109 1695 1868 148 73 127 N ATOM 91 CA VAL A 63 -30.302 -7.716 -33.681 1.00 13.84 C ANISOU 91 CA VAL A 63 2053 1568 1637 171 60 40 C ATOM 92 C VAL A 63 -30.958 -7.141 -32.437 1.00 17.38 C ANISOU 92 C VAL A 63 2551 2062 1991 263 145 40 C ATOM 93 O VAL A 63 -32.188 -7.062 -32.354 1.00 20.78 O ANISOU 93 O VAL A 63 2926 2495 2473 315 236 100 O ATOM 94 CB VAL A 63 -30.579 -6.774 -34.868 1.00 15.86 C ANISOU 94 CB VAL A 63 2310 1765 1951 151 31 1 C ATOM 95 CG1 VAL A 63 -30.108 -5.344 -34.520 1.00 13.62 C ANISOU 95 CG1 VAL A 63 2106 1441 1625 166 24 -78 C ATOM 96 CG2 VAL A 63 -29.898 -7.286 -36.116 1.00 17.94 C ANISOU 96 CG2 VAL A 63 2561 2008 2246 95 -25 -2 C ATOM 97 N LYS A 64 -30.149 -6.757 -31.453 1.00 15.36 N ANISOU 97 N LYS A 64 2395 1848 1593 295 111 -30 N ATOM 98 CA LYS A 64 -30.704 -6.209 -30.233 1.00 16.77 C ANISOU 98 CA LYS A 64 2669 2082 1619 414 194 -62 C ATOM 99 C LYS A 64 -31.043 -4.743 -30.480 1.00 18.83 C ANISOU 99 C LYS A 64 2993 2256 1908 445 196 -187 C ATOM 100 O LYS A 64 -32.167 -4.304 -30.262 1.00 20.77 O ANISOU 100 O LYS A 64 3236 2497 2160 547 323 -168 O ATOM 101 CB LYS A 64 -29.729 -6.363 -29.056 1.00 29.26 C ANISOU 101 CB LYS A 64 4364 3751 3002 453 115 -113 C ATOM 102 CG LYS A 64 -30.046 -5.451 -27.877 1.00 41.08 C ANISOU 102 CG LYS A 64 6030 5295 4282 589 154 -232 C ATOM 103 CD LYS A 64 -29.045 -5.584 -26.730 1.00 53.83 C ANISOU 103 CD LYS A 64 7779 7014 5661 634 18 -304 C ATOM 104 CE LYS A 64 -29.543 -4.838 -25.481 1.00 66.64 C ANISOU 104 CE LYS A 64 9613 8708 7000 814 82 -428 C ATOM 105 NZ LYS A 64 -30.835 -5.364 -24.939 1.00 72.67 N ANISOU 105 NZ LYS A 64 10374 9576 7663 972 361 -253 N ATOM 106 N TRP A 65 -30.054 -3.996 -30.939 1.00 18.64 N ANISOU 106 N TRP A 65 3005 2145 1930 362 67 -295 N ATOM 107 CA TRP A 65 -30.322 -2.658 -31.451 1.00 17.45 C ANISOU 107 CA TRP A 65 2892 1862 1877 368 65 -376 C ATOM 108 C TRP A 65 -29.225 -2.263 -32.407 1.00 17.61 C ANISOU 108 C TRP A 65 2874 1788 2028 234 -47 -389 C ATOM 109 O TRP A 65 -28.123 -2.808 -32.365 1.00 18.79 O ANISOU 109 O TRP A 65 2990 1978 2173 153 -134 -388 O ATOM 110 CB TRP A 65 -30.463 -1.631 -30.326 1.00 20.70 C ANISOU 110 CB TRP A 65 3465 2230 2171 474 73 -541 C ATOM 111 CG TRP A 65 -29.314 -1.520 -29.377 1.00 27.84 C ANISOU 111 CG TRP A 65 4482 3157 2940 445 -79 -686 C ATOM 112 CD1 TRP A 65 -29.159 -2.186 -28.195 1.00 35.56 C ANISOU 112 CD1 TRP A 65 5544 4286 3682 526 -91 -704 C ATOM 113 CD2 TRP A 65 -28.163 -0.680 -29.518 1.00 25.90 C ANISOU 113 CD2 TRP A 65 4265 2777 2799 327 -262 -821 C ATOM 114 NE1 TRP A 65 -27.981 -1.818 -27.597 1.00 38.26 N ANISOU 114 NE1 TRP A 65 5973 4611 3954 471 -303 -861 N ATOM 115 CE2 TRP A 65 -27.350 -0.893 -28.388 1.00 34.91 C ANISOU 115 CE2 TRP A 65 5499 4002 3763 336 -414 -941 C ATOM 116 CE3 TRP A 65 -27.740 0.234 -30.490 1.00 25.52 C ANISOU 116 CE3 TRP A 65 4161 2544 2992 214 -311 -831 C ATOM 117 CZ2 TRP A 65 -26.140 -0.219 -28.197 1.00 39.34 C ANISOU 117 CZ2 TRP A 65 6077 4458 4414 217 -645 -1092 C ATOM 118 CZ3 TRP A 65 -26.538 0.904 -30.298 1.00 30.38 C ANISOU 118 CZ3 TRP A 65 4787 3039 3715 93 -499 -957 C ATOM 119 CH2 TRP A 65 -25.752 0.671 -29.163 1.00 33.95 C ANISOU 119 CH2 TRP A 65 5310 3571 4020 86 -678 -1097 C ATOM 120 N PHE A 66 -29.545 -1.354 -33.314 1.00 17.01 N ANISOU 120 N PHE A 66 2787 1593 2084 223 -26 -369 N ATOM 121 CA PHE A 66 -28.542 -0.825 -34.222 1.00 16.57 C ANISOU 121 CA PHE A 66 2695 1438 2162 110 -88 -345 C ATOM 122 C PHE A 66 -28.827 0.641 -34.425 1.00 20.04 C ANISOU 122 C PHE A 66 3196 1693 2725 131 -79 -385 C ATOM 123 O PHE A 66 -29.930 1.020 -34.838 1.00 18.46 O ANISOU 123 O PHE A 66 2999 1461 2554 224 -2 -326 O ATOM 124 CB PHE A 66 -28.529 -1.574 -35.563 1.00 16.76 C ANISOU 124 CB PHE A 66 2627 1524 2217 74 -53 -197 C ATOM 125 CG PHE A 66 -27.451 -1.085 -36.493 1.00 18.13 C ANISOU 125 CG PHE A 66 2762 1623 2504 -17 -64 -134 C ATOM 126 CD1 PHE A 66 -26.143 -1.530 -36.347 1.00 22.75 C ANISOU 126 CD1 PHE A 66 3283 2239 3121 -101 -108 -140 C ATOM 127 CD2 PHE A 66 -27.732 -0.142 -37.475 1.00 18.31 C ANISOU 127 CD2 PHE A 66 2798 1545 2616 -6 -19 -42 C ATOM 128 CE1 PHE A 66 -25.132 -1.057 -37.179 1.00 21.72 C ANISOU 128 CE1 PHE A 66 3082 2041 3128 -179 -80 -51 C ATOM 129 CE2 PHE A 66 -26.724 0.337 -38.311 1.00 21.62 C ANISOU 129 CE2 PHE A 66 3173 1895 3147 -82 11 59 C ATOM 130 CZ PHE A 66 -25.427 -0.134 -38.163 1.00 21.45 C ANISOU 130 CZ PHE A 66 3068 1908 3172 -172 -7 56 C ATOM 131 N ASN A 67 -27.846 1.477 -34.105 1.00 19.23 N ANISOU 131 N ASN A 67 3129 1452 2727 46 -170 -482 N ATOM 132 CA ASN A 67 -28.091 2.906 -34.145 1.00 20.98 C ANISOU 132 CA ASN A 67 3425 1446 3100 65 -170 -542 C ATOM 133 C ASN A 67 -27.407 3.506 -35.365 1.00 23.31 C ANISOU 133 C ASN A 67 3637 1608 3612 -45 -158 -387 C ATOM 134 O ASN A 67 -26.196 3.447 -35.485 1.00 22.66 O ANISOU 134 O ASN A 67 3476 1500 3633 -182 -223 -369 O ATOM 135 CB ASN A 67 -27.606 3.576 -32.854 1.00 23.09 C ANISOU 135 CB ASN A 67 3815 1598 3359 54 -296 -788 C ATOM 136 CG ASN A 67 -27.969 5.040 -32.798 1.00 29.90 C ANISOU 136 CG ASN A 67 4782 2185 4393 96 -294 -887 C ATOM 137 OD1 ASN A 67 -27.505 5.824 -33.617 1.00 29.91 O ANISOU 137 OD1 ASN A 67 4727 1991 4645 -4 -304 -793 O ATOM 138 ND2 ASN A 67 -28.801 5.422 -31.830 1.00 32.18 N ANISOU 138 ND2 ASN A 67 5227 2445 4554 259 -260 -1065 N ATOM 139 N VAL A 68 -28.176 4.117 -36.261 1.00 22.21 N ANISOU 139 N VAL A 68 3504 1384 3552 24 -67 -251 N ATOM 140 CA VAL A 68 -27.599 4.592 -37.514 1.00 26.27 C ANISOU 140 CA VAL A 68 3949 1807 4223 -52 -19 -46 C ATOM 141 C VAL A 68 -26.863 5.915 -37.358 1.00 24.59 C ANISOU 141 C VAL A 68 3750 1299 4295 -154 -62 -75 C ATOM 142 O VAL A 68 -26.098 6.314 -38.240 1.00 30.33 O ANISOU 142 O VAL A 68 4394 1934 5195 -250 -12 111 O ATOM 143 CB VAL A 68 -28.675 4.732 -38.610 1.00 25.10 C ANISOU 143 CB VAL A 68 3808 1695 4032 71 70 143 C ATOM 144 CG1 VAL A 68 -29.300 3.370 -38.901 1.00 28.17 C ANISOU 144 CG1 VAL A 68 4161 2352 4191 135 76 171 C ATOM 145 CG2 VAL A 68 -29.725 5.775 -38.210 1.00 25.87 C ANISOU 145 CG2 VAL A 68 3985 1616 4227 197 84 89 C ATOM 146 N ARG A 69 -27.091 6.616 -36.248 1.00 26.05 N ANISOU 146 N ARG A 69 4043 1319 4538 -128 -147 -306 N ATOM 147 CA ARG A 69 -26.382 7.854 -35.983 1.00 28.95 C ANISOU 147 CA ARG A 69 4432 1386 5183 -240 -225 -382 C ATOM 148 C ARG A 69 -24.962 7.516 -35.540 1.00 30.07 C ANISOU 148 C ARG A 69 4467 1572 5386 -428 -358 -456 C ATOM 149 O ARG A 69 -23.996 8.132 -35.988 1.00 36.44 O ANISOU 149 O ARG A 69 5160 2273 6413 -572 -364 -343 O ATOM 150 CB ARG A 69 -27.112 8.677 -34.921 1.00 33.31 C ANISOU 150 CB ARG A 69 5155 1819 5680 -126 -257 -625 C ATOM 151 CG ARG A 69 -26.353 9.884 -34.433 1.00 51.92 C ANISOU 151 CG ARG A 69 7551 3961 8216 -244 -349 -747 C ATOM 152 CD ARG A 69 -27.125 10.614 -33.356 1.00 70.39 C ANISOU 152 CD ARG A 69 10085 6194 10466 -107 -353 -1002 C ATOM 153 NE ARG A 69 -26.532 10.410 -32.039 1.00 81.24 N ANISOU 153 NE ARG A 69 11523 7641 11703 -158 -510 -1286 N ATOM 154 CZ ARG A 69 -26.850 11.117 -30.959 1.00 94.60 C ANISOU 154 CZ ARG A 69 13384 9241 13318 -77 -542 -1544 C ATOM 155 NH1 ARG A 69 -27.757 12.083 -31.039 1.00 98.69 N ANISOU 155 NH1 ARG A 69 14019 9566 13914 57 -410 -1560 N ATOM 156 NH2 ARG A 69 -26.257 10.862 -29.801 1.00 98.90 N ANISOU 156 NH2 ARG A 69 13988 9890 13699 -117 -708 -1779 N ATOM 157 N ASN A 70 -24.853 6.524 -34.663 1.00 28.14 N ANISOU 157 N ASN A 70 4246 1503 4941 -410 -463 -625 N ATOM 158 CA ASN A 70 -23.559 6.123 -34.119 1.00 30.69 C ANISOU 158 CA ASN A 70 4460 1893 5308 -561 -622 -702 C ATOM 159 C ASN A 70 -22.835 5.126 -35.018 1.00 28.65 C ANISOU 159 C ASN A 70 4008 1815 5064 -629 -538 -467 C ATOM 160 O ASN A 70 -21.615 4.998 -34.950 1.00 32.39 O ANISOU 160 O ASN A 70 4321 2277 5711 -776 -634 -443 O ATOM 161 CB ASN A 70 -23.736 5.546 -32.715 1.00 38.90 C ANISOU 161 CB ASN A 70 5628 3082 6070 -482 -767 -963 C ATOM 162 CG ASN A 70 -23.751 6.623 -31.651 1.00 55.88 C ANISOU 162 CG ASN A 70 7915 5114 8203 -468 -871 -1199 C ATOM 163 OD1 ASN A 70 -24.744 6.811 -30.953 1.00 61.92 O ANISOU 163 OD1 ASN A 70 8862 5898 8766 -303 -822 -1347 O ATOM 164 ND2 ASN A 70 -22.641 7.340 -31.524 1.00 68.16 N ANISOU 164 ND2 ASN A 70 9373 6541 9982 -634 -1006 -1230 N ATOM 165 N GLY A 71 -23.600 4.442 -35.858 1.00 24.89 N ANISOU 165 N GLY A 71 3542 1512 4403 -510 -358 -299 N ATOM 166 CA GLY A 71 -23.076 3.487 -36.822 1.00 23.53 C ANISOU 166 CA GLY A 71 3232 1524 4183 -525 -241 -91 C ATOM 167 C GLY A 71 -22.646 2.145 -36.257 1.00 26.73 C ANISOU 167 C GLY A 71 3584 2158 4413 -513 -303 -156 C ATOM 168 O GLY A 71 -21.795 1.479 -36.844 1.00 25.24 O ANISOU 168 O GLY A 71 3254 2068 4269 -553 -242 -25 O ATOM 169 N TYR A 72 -23.232 1.730 -35.139 1.00 21.53 N ANISOU 169 N TYR A 72 3040 1583 3558 -437 -401 -338 N ATOM 170 CA TYR A 72 -22.956 0.399 -34.592 1.00 20.37 C ANISOU 170 CA TYR A 72 2857 1648 3234 -401 -446 -363 C ATOM 171 C TYR A 72 -24.139 -0.093 -33.782 1.00 22.55 C ANISOU 171 C TYR A 72 3282 2031 3254 -264 -436 -462 C ATOM 172 O TYR A 72 -25.082 0.651 -33.523 1.00 21.25 O ANISOU 172 O TYR A 72 3239 1781 3054 -194 -407 -539 O ATOM 173 CB TYR A 72 -21.687 0.411 -33.724 1.00 22.09 C ANISOU 173 CB TYR A 72 2981 1853 3557 -508 -645 -458 C ATOM 174 CG TYR A 72 -21.835 1.109 -32.383 1.00 23.90 C ANISOU 174 CG TYR A 72 3356 2003 3723 -504 -843 -703 C ATOM 175 CD1 TYR A 72 -22.241 0.405 -31.258 1.00 33.31 C ANISOU 175 CD1 TYR A 72 4672 3357 4627 -391 -916 -817 C ATOM 176 CD2 TYR A 72 -21.563 2.468 -32.241 1.00 33.38 C ANISOU 176 CD2 TYR A 72 4583 2955 5145 -603 -952 -819 C ATOM 177 CE1 TYR A 72 -22.377 1.022 -30.034 1.00 35.79 C ANISOU 177 CE1 TYR A 72 5156 3623 4818 -352 -1086 -1054 C ATOM 178 CE2 TYR A 72 -21.696 3.095 -31.015 1.00 37.46 C ANISOU 178 CE2 TYR A 72 5270 3389 5575 -580 -1148 -1088 C ATOM 179 CZ TYR A 72 -22.115 2.366 -29.918 1.00 36.51 C ANISOU 179 CZ TYR A 72 5296 3468 5109 -442 -1210 -1212 C ATOM 180 OH TYR A 72 -22.250 2.961 -28.682 1.00 44.90 O ANISOU 180 OH TYR A 72 6534 4522 6002 -376 -1338 -1441 O ATOM 181 N GLY A 73 -24.078 -1.352 -33.375 1.00 18.37 N ANISOU 181 N GLY A 73 2730 1679 2571 -217 -443 -440 N ATOM 182 CA GLY A 73 -25.090 -1.913 -32.500 1.00 17.91 C ANISOU 182 CA GLY A 73 2785 1729 2292 -93 -415 -492 C ATOM 183 C GLY A 73 -24.596 -3.236 -31.958 1.00 18.09 C ANISOU 183 C GLY A 73 2759 1910 2205 -72 -457 -445 C ATOM 184 O GLY A 73 -23.394 -3.493 -31.947 1.00 18.75 O ANISOU 184 O GLY A 73 2739 2009 2376 -145 -558 -427 O ATOM 185 N PHE A 74 -25.536 -4.060 -31.502 1.00 16.88 N ANISOU 185 N PHE A 74 2661 1862 1892 33 -372 -401 N ATOM 186 CA PHE A 74 -25.206 -5.371 -30.956 1.00 16.75 C ANISOU 186 CA PHE A 74 2609 1973 1783 70 -391 -321 C ATOM 187 C PHE A 74 -26.185 -6.400 -31.442 1.00 21.28 C ANISOU 187 C PHE A 74 3149 2582 2354 118 -244 -195 C ATOM 188 O PHE A 74 -27.384 -6.135 -31.549 1.00 16.23 O ANISOU 188 O PHE A 74 2546 1925 1697 166 -143 -186 O ATOM 189 CB PHE A 74 -25.202 -5.350 -29.433 1.00 18.48 C ANISOU 189 CB PHE A 74 2951 2285 1786 156 -476 -395 C ATOM 190 CG PHE A 74 -24.068 -4.557 -28.854 1.00 20.56 C ANISOU 190 CG PHE A 74 3237 2519 2056 95 -696 -542 C ATOM 191 CD1 PHE A 74 -22.845 -5.166 -28.593 1.00 27.17 C ANISOU 191 CD1 PHE A 74 3970 3422 2931 53 -852 -500 C ATOM 192 CD2 PHE A 74 -24.220 -3.208 -28.583 1.00 26.03 C ANISOU 192 CD2 PHE A 74 4041 3099 2752 81 -763 -724 C ATOM 193 CE1 PHE A 74 -21.793 -4.434 -28.069 1.00 27.70 C ANISOU 193 CE1 PHE A 74 4022 3457 3046 -22 -1097 -636 C ATOM 194 CE2 PHE A 74 -23.173 -2.480 -28.063 1.00 29.88 C ANISOU 194 CE2 PHE A 74 4539 3527 3289 1 -1004 -880 C ATOM 195 CZ PHE A 74 -21.964 -3.098 -27.806 1.00 30.35 C ANISOU 195 CZ PHE A 74 4473 3667 3393 -59 -1183 -835 C ATOM 196 N ILE A 75 -25.640 -7.580 -31.729 1.00 16.89 N ANISOU 196 N ILE A 75 2509 2060 1848 106 -246 -100 N ATOM 197 CA ILE A 75 -26.414 -8.731 -32.137 1.00 14.47 C ANISOU 197 CA ILE A 75 2165 1754 1578 133 -147 5 C ATOM 198 C ILE A 75 -26.294 -9.775 -31.050 1.00 19.77 C ANISOU 198 C ILE A 75 2844 2499 2168 198 -150 103 C ATOM 199 O ILE A 75 -25.198 -10.050 -30.563 1.00 19.35 O ANISOU 199 O ILE A 75 2771 2491 2088 207 -248 115 O ATOM 200 CB ILE A 75 -25.906 -9.310 -33.470 1.00 16.63 C ANISOU 200 CB ILE A 75 2362 1971 1987 87 -134 26 C ATOM 201 CG1 ILE A 75 -26.025 -8.282 -34.586 1.00 19.34 C ANISOU 201 CG1 ILE A 75 2713 2260 2376 43 -115 -28 C ATOM 202 CG2 ILE A 75 -26.688 -10.575 -33.831 1.00 19.35 C ANISOU 202 CG2 ILE A 75 2682 2280 2389 107 -75 97 C ATOM 203 CD1 ILE A 75 -25.216 -8.640 -35.821 1.00 21.32 C ANISOU 203 CD1 ILE A 75 2915 2487 2701 25 -87 -12 C ATOM 204 N ASN A 76 -27.412 -10.360 -30.655 1.00 17.11 N ANISOU 204 N ASN A 76 2518 2175 1810 248 -43 199 N ATOM 205 CA ASN A 76 -27.345 -11.460 -29.707 1.00 17.64 C ANISOU 205 CA ASN A 76 2586 2296 1820 315 -14 347 C ATOM 206 C ASN A 76 -27.251 -12.789 -30.440 1.00 18.00 C ANISOU 206 C ASN A 76 2537 2240 2063 278 8 442 C ATOM 207 O ASN A 76 -28.148 -13.145 -31.194 1.00 17.29 O ANISOU 207 O ASN A 76 2396 2058 2116 233 69 455 O ATOM 208 CB ASN A 76 -28.566 -11.427 -28.794 1.00 20.12 C ANISOU 208 CB ASN A 76 2947 2671 2025 398 127 442 C ATOM 209 CG ASN A 76 -28.439 -12.366 -27.649 1.00 24.80 C ANISOU 209 CG ASN A 76 3571 3346 2504 491 172 625 C ATOM 210 OD1 ASN A 76 -29.000 -13.457 -27.675 1.00 25.29 O ANISOU 210 OD1 ASN A 76 3554 3348 2708 488 278 806 O ATOM 211 ND2 ASN A 76 -27.695 -11.959 -26.625 1.00 25.19 N ANISOU 211 ND2 ASN A 76 3740 3526 2306 576 78 587 N ATOM 212 N ARG A 77 -26.158 -13.518 -30.217 1.00 16.85 N ANISOU 212 N ARG A 77 2366 2099 1938 306 -60 497 N ATOM 213 CA ARG A 77 -25.959 -14.818 -30.859 1.00 17.25 C ANISOU 213 CA ARG A 77 2347 2024 2185 297 -37 569 C ATOM 214 C ARG A 77 -26.978 -15.815 -30.373 1.00 17.76 C ANISOU 214 C ARG A 77 2394 2022 2333 315 66 740 C ATOM 215 O ARG A 77 -27.184 -15.962 -29.172 1.00 21.10 O ANISOU 215 O ARG A 77 2852 2535 2631 389 114 892 O ATOM 216 CB ARG A 77 -24.565 -15.384 -30.568 1.00 17.55 C ANISOU 216 CB ARG A 77 2345 2082 2242 355 -119 621 C ATOM 217 CG ARG A 77 -23.448 -14.612 -31.211 1.00 17.88 C ANISOU 217 CG ARG A 77 2342 2156 2297 324 -202 488 C ATOM 218 CD ARG A 77 -22.109 -15.130 -30.718 1.00 18.29 C ANISOU 218 CD ARG A 77 2313 2250 2386 393 -294 570 C ATOM 219 NE ARG A 77 -21.870 -16.498 -31.146 1.00 19.74 N ANISOU 219 NE ARG A 77 2446 2307 2748 454 -231 660 N ATOM 220 CZ ARG A 77 -20.683 -17.096 -31.106 1.00 25.55 C ANISOU 220 CZ ARG A 77 3080 3035 3593 533 -276 729 C ATOM 221 NH1 ARG A 77 -19.615 -16.439 -30.665 1.00 28.08 N ANISOU 221 NH1 ARG A 77 3314 3482 3875 540 -406 725 N ATOM 222 NH2 ARG A 77 -20.565 -18.351 -31.512 1.00 30.03 N ANISOU 222 NH2 ARG A 77 3622 3452 4337 605 -201 796 N ATOM 223 N ASN A 78 -27.586 -16.544 -31.299 1.00 18.40 N ANISOU 223 N ASN A 78 2422 1939 2631 252 95 725 N ATOM 224 CA ASN A 78 -28.580 -17.524 -30.892 1.00 22.92 C ANISOU 224 CA ASN A 78 2939 2405 3364 238 187 903 C ATOM 225 C ASN A 78 -27.946 -18.773 -30.281 1.00 26.10 C ANISOU 225 C ASN A 78 3329 2727 3860 305 203 1087 C ATOM 226 O ASN A 78 -28.608 -19.493 -29.527 1.00 28.20 O ANISOU 226 O ASN A 78 3558 2942 4215 321 306 1312 O ATOM 227 CB ASN A 78 -29.468 -17.903 -32.078 1.00 25.81 C ANISOU 227 CB ASN A 78 3244 2597 3966 131 161 806 C ATOM 228 CG ASN A 78 -30.363 -16.762 -32.528 1.00 25.04 C ANISOU 228 CG ASN A 78 3134 2578 3802 83 155 698 C ATOM 229 OD1 ASN A 78 -30.513 -15.749 -31.829 1.00 23.48 O ANISOU 229 OD1 ASN A 78 2970 2538 3415 132 210 718 O ATOM 230 ND2 ASN A 78 -30.988 -16.930 -33.693 1.00 25.99 N ANISOU 230 ND2 ASN A 78 3215 2581 4080 -1 75 578 N ATOM 231 N ASP A 79 -26.665 -19.020 -30.580 1.00 20.36 N ANISOU 231 N ASP A 79 2618 1988 3130 354 119 1021 N ATOM 232 CA ASP A 79 -26.004 -20.248 -30.141 1.00 24.47 C ANISOU 232 CA ASP A 79 3115 2403 3779 435 125 1193 C ATOM 233 C ASP A 79 -25.385 -20.116 -28.747 1.00 23.25 C ANISOU 233 C ASP A 79 2992 2437 3405 554 107 1382 C ATOM 234 O ASP A 79 -25.202 -21.118 -28.040 1.00 26.97 O ANISOU 234 O ASP A 79 3451 2848 3949 638 142 1620 O ATOM 235 CB ASP A 79 -24.947 -20.680 -31.172 1.00 25.51 C ANISOU 235 CB ASP A 79 3230 2420 4044 462 62 1042 C ATOM 236 CG ASP A 79 -23.837 -19.642 -31.371 1.00 26.09 C ANISOU 236 CG ASP A 79 3299 2674 3941 492 -15 908 C ATOM 237 OD1 ASP A 79 -24.046 -18.454 -31.048 1.00 23.28 O ANISOU 237 OD1 ASP A 79 2972 2488 3386 452 -45 850 O ATOM 238 OD2 ASP A 79 -22.752 -20.013 -31.878 1.00 27.76 O ANISOU 238 OD2 ASP A 79 3465 2838 4243 559 -38 863 O ATOM 239 N THR A 80 -25.051 -18.888 -28.349 1.00 22.67 N ANISOU 239 N THR A 80 2970 2583 3062 568 35 1278 N ATOM 240 CA THR A 80 -24.419 -18.677 -27.050 1.00 24.06 C ANISOU 240 CA THR A 80 3201 2954 2986 684 -39 1406 C ATOM 241 C THR A 80 -25.155 -17.668 -26.186 1.00 24.26 C ANISOU 241 C THR A 80 3337 3165 2714 707 0 1390 C ATOM 242 O THR A 80 -24.890 -17.575 -24.991 1.00 26.25 O ANISOU 242 O THR A 80 3680 3589 2706 826 -43 1509 O ATOM 243 CB THR A 80 -22.968 -18.185 -27.209 1.00 24.30 C ANISOU 243 CB THR A 80 3189 3072 2971 706 -224 1278 C ATOM 244 OG1 THR A 80 -22.996 -16.894 -27.828 1.00 21.97 O ANISOU 244 OG1 THR A 80 2907 2829 2613 607 -268 1031 O ATOM 245 CG2 THR A 80 -22.139 -19.164 -28.075 1.00 23.84 C ANISOU 245 CG2 THR A 80 3016 2841 3200 725 -231 1291 C ATOM 246 N LYS A 81 -26.057 -16.907 -26.813 1.00 22.69 N ANISOU 246 N LYS A 81 3141 2935 2545 614 73 1236 N ATOM 247 CA LYS A 81 -26.865 -15.874 -26.149 1.00 25.05 C ANISOU 247 CA LYS A 81 3539 3378 2601 647 142 1190 C ATOM 248 C LYS A 81 -25.997 -14.721 -25.625 1.00 28.23 C ANISOU 248 C LYS A 81 4047 3944 2735 688 -33 1010 C ATOM 249 O LYS A 81 -26.407 -13.967 -24.735 1.00 26.60 O ANISOU 249 O LYS A 81 3974 3879 2255 771 -6 974 O ATOM 250 CB LYS A 81 -27.706 -16.468 -25.017 1.00 31.50 C ANISOU 250 CB LYS A 81 4402 4264 3302 759 322 1463 C ATOM 251 CG LYS A 81 -28.568 -17.668 -25.424 1.00 36.45 C ANISOU 251 CG LYS A 81 4896 4696 4258 699 485 1674 C ATOM 252 CD LYS A 81 -29.457 -17.390 -26.635 1.00 36.37 C ANISOU 252 CD LYS A 81 4778 4536 4506 551 519 1521 C ATOM 253 CE LYS A 81 -30.315 -18.620 -26.977 1.00 45.39 C ANISOU 253 CE LYS A 81 5778 5461 6008 473 633 1716 C ATOM 254 NZ LYS A 81 -30.916 -18.595 -28.353 1.00 33.57 N ANISOU 254 NZ LYS A 81 4174 3787 4793 318 571 1534 N ATOM 255 N GLU A 82 -24.804 -14.594 -26.201 1.00 25.04 N ANISOU 255 N GLU A 82 3576 3507 2431 632 -207 891 N ATOM 256 CA GLU A 82 -23.910 -13.467 -25.918 1.00 26.80 C ANISOU 256 CA GLU A 82 3846 3832 2505 620 -407 701 C ATOM 257 C GLU A 82 -24.076 -12.385 -26.959 1.00 26.20 C ANISOU 257 C GLU A 82 3740 3668 2548 496 -404 485 C ATOM 258 O GLU A 82 -24.256 -12.682 -28.142 1.00 19.66 O ANISOU 258 O GLU A 82 2815 2710 1944 418 -322 475 O ATOM 259 CB GLU A 82 -22.446 -13.919 -25.896 1.00 23.62 C ANISOU 259 CB GLU A 82 3338 3448 2188 630 -597 736 C ATOM 260 CG GLU A 82 -22.073 -14.768 -24.710 1.00 36.08 C ANISOU 260 CG GLU A 82 4962 5146 3601 775 -668 945 C ATOM 261 CD GLU A 82 -22.212 -14.042 -23.389 1.00 46.09 C ANISOU 261 CD GLU A 82 6421 6612 4480 874 -776 898 C ATOM 262 OE1 GLU A 82 -21.740 -12.891 -23.295 1.00 53.61 O ANISOU 262 OE1 GLU A 82 7413 7612 5345 820 -960 663 O ATOM 263 OE2 GLU A 82 -22.776 -14.629 -22.441 1.00 48.86 O ANISOU 263 OE2 GLU A 82 6889 7063 4611 1014 -674 1098 O ATOM 264 N ASP A 83 -23.980 -11.126 -26.531 1.00 24.46 N ANISOU 264 N ASP A 83 3616 3507 2171 488 -505 310 N ATOM 265 CA ASP A 83 -23.999 -10.013 -27.475 1.00 23.61 C ANISOU 265 CA ASP A 83 3478 3299 2196 374 -516 130 C ATOM 266 C ASP A 83 -22.667 -9.893 -28.190 1.00 23.49 C ANISOU 266 C ASP A 83 3316 3230 2379 279 -654 84 C ATOM 267 O ASP A 83 -21.597 -10.050 -27.583 1.00 24.10 O ANISOU 267 O ASP A 83 3346 3378 2433 295 -833 97 O ATOM 268 CB ASP A 83 -24.309 -8.694 -26.766 1.00 25.81 C ANISOU 268 CB ASP A 83 3911 3612 2285 400 -580 -51 C ATOM 269 CG ASP A 83 -25.753 -8.583 -26.340 1.00 37.89 C ANISOU 269 CG ASP A 83 5557 5172 3666 501 -379 -18 C ATOM 270 OD1 ASP A 83 -26.591 -9.358 -26.851 1.00 30.33 O ANISOU 270 OD1 ASP A 83 4521 4177 2825 501 -200 132 O ATOM 271 OD2 ASP A 83 -26.050 -7.712 -25.493 1.00 40.68 O ANISOU 271 OD2 ASP A 83 6074 5579 3801 583 -403 -150 O ATOM 272 N VAL A 84 -22.740 -9.641 -29.489 1.00 19.09 N ANISOU 272 N VAL A 84 2676 2560 2016 192 -563 52 N ATOM 273 CA AVAL A 84 -21.572 -9.337 -30.296 0.48 24.34 C ANISOU 273 CA AVAL A 84 3195 3172 2879 108 -630 24 C ATOM 274 CA BVAL A 84 -21.542 -9.305 -30.245 0.52 18.22 C ANISOU 274 CA BVAL A 84 2422 2401 2101 107 -639 20 C ATOM 275 C VAL A 84 -21.718 -7.932 -30.869 1.00 17.82 C ANISOU 275 C VAL A 84 2391 2262 2119 14 -628 -101 C ATOM 276 O VAL A 84 -22.792 -7.582 -31.370 1.00 18.42 O ANISOU 276 O VAL A 84 2547 2288 2166 17 -503 -124 O ATOM 277 CB AVAL A 84 -21.411 -10.342 -31.443 0.48 19.98 C ANISOU 277 CB AVAL A 84 2542 2562 2486 118 -493 121 C ATOM 278 CB BVAL A 84 -21.204 -10.330 -31.357 0.52 21.35 C ANISOU 278 CB BVAL A 84 2699 2744 2668 117 -517 123 C ATOM 279 CG1AVAL A 84 -20.141 -10.071 -32.216 0.48 20.29 C ANISOU 279 CG1AVAL A 84 2419 2573 2719 64 -515 124 C ATOM 280 CG1BVAL A 84 -20.645 -11.625 -30.762 0.52 22.04 C ANISOU 280 CG1BVAL A 84 2729 2881 2765 207 -557 252 C ATOM 281 CG2AVAL A 84 -21.394 -11.753 -30.901 0.48 21.09 C ANISOU 281 CG2AVAL A 84 2674 2736 2604 214 -479 252 C ATOM 282 CG2BVAL A 84 -22.403 -10.595 -32.256 0.52 16.51 C ANISOU 282 CG2BVAL A 84 2155 2061 2057 120 -349 124 C ATOM 283 N PHE A 85 -20.652 -7.148 -30.784 1.00 19.14 N ANISOU 283 N PHE A 85 2468 2400 2403 -70 -775 -164 N ATOM 284 CA PHE A 85 -20.592 -5.835 -31.398 1.00 19.56 C ANISOU 284 CA PHE A 85 2509 2333 2591 -174 -772 -247 C ATOM 285 C PHE A 85 -20.697 -5.920 -32.914 1.00 18.98 C ANISOU 285 C PHE A 85 2362 2197 2655 -197 -573 -150 C ATOM 286 O PHE A 85 -20.094 -6.790 -33.531 1.00 21.00 O ANISOU 286 O PHE A 85 2500 2486 2992 -173 -499 -46 O ATOM 287 CB PHE A 85 -19.282 -5.165 -30.992 1.00 21.52 C ANISOU 287 CB PHE A 85 2625 2547 3005 -278 -986 -303 C ATOM 288 CG PHE A 85 -19.044 -3.825 -31.639 1.00 22.86 C ANISOU 288 CG PHE A 85 2744 2550 3391 -408 -984 -354 C ATOM 289 CD1 PHE A 85 -19.603 -2.674 -31.112 1.00 24.13 C ANISOU 289 CD1 PHE A 85 3061 2604 3502 -438 -1073 -522 C ATOM 290 CD2 PHE A 85 -18.231 -3.722 -32.758 1.00 26.42 C ANISOU 290 CD2 PHE A 85 2993 2942 4104 -486 -877 -219 C ATOM 291 CE1 PHE A 85 -19.355 -1.435 -31.700 1.00 24.17 C ANISOU 291 CE1 PHE A 85 3015 2416 3752 -562 -1073 -548 C ATOM 292 CE2 PHE A 85 -17.985 -2.498 -33.350 1.00 29.31 C ANISOU 292 CE2 PHE A 85 3300 3143 4695 -607 -854 -217 C ATOM 293 CZ PHE A 85 -18.551 -1.353 -32.822 1.00 27.38 C ANISOU 293 CZ PHE A 85 3207 2764 4434 -654 -962 -378 C ATOM 294 N VAL A 86 -21.466 -5.021 -33.530 1.00 17.49 N ANISOU 294 N VAL A 86 2253 1918 2476 -223 -486 -181 N ATOM 295 CA VAL A 86 -21.473 -4.952 -34.983 1.00 18.70 C ANISOU 295 CA VAL A 86 2354 2027 2724 -235 -322 -83 C ATOM 296 C VAL A 86 -21.311 -3.509 -35.445 1.00 22.45 C ANISOU 296 C VAL A 86 2815 2367 3347 -324 -315 -87 C ATOM 297 O VAL A 86 -22.080 -2.627 -35.053 1.00 21.00 O ANISOU 297 O VAL A 86 2749 2103 3126 -327 -355 -175 O ATOM 298 CB VAL A 86 -22.751 -5.564 -35.602 1.00 17.93 C ANISOU 298 CB VAL A 86 2365 1961 2487 -149 -200 -60 C ATOM 299 CG1 VAL A 86 -24.043 -4.996 -34.985 1.00 18.44 C ANISOU 299 CG1 VAL A 86 2560 2001 2444 -117 -221 -136 C ATOM 300 CG2 VAL A 86 -22.733 -5.409 -37.119 1.00 18.82 C ANISOU 300 CG2 VAL A 86 2462 2048 2642 -143 -64 25 C ATOM 301 N HIS A 87 -20.275 -3.265 -36.245 1.00 19.09 N ANISOU 301 N HIS A 87 2237 1904 3111 -387 -248 24 N ATOM 302 CA HIS A 87 -20.087 -1.936 -36.813 1.00 21.59 C ANISOU 302 CA HIS A 87 2523 2070 3611 -476 -207 77 C ATOM 303 C HIS A 87 -20.750 -1.912 -38.175 1.00 20.63 C ANISOU 303 C HIS A 87 2475 1962 3404 -401 -4 204 C ATOM 304 O HIS A 87 -20.890 -2.931 -38.810 1.00 21.64 O ANISOU 304 O HIS A 87 2621 2208 3392 -307 99 252 O ATOM 305 CB HIS A 87 -18.606 -1.562 -36.924 1.00 26.75 C ANISOU 305 CB HIS A 87 2942 2662 4559 -597 -232 169 C ATOM 306 CG HIS A 87 -18.393 -0.146 -37.358 1.00 35.00 C ANISOU 306 CG HIS A 87 3941 3508 5850 -713 -203 237 C ATOM 307 ND1 HIS A 87 -17.925 0.189 -38.611 1.00 35.32 N ANISOU 307 ND1 HIS A 87 3871 3511 6036 -727 19 465 N ATOM 308 CD2 HIS A 87 -18.632 1.020 -36.719 1.00 35.89 C ANISOU 308 CD2 HIS A 87 4118 3431 6086 -806 -353 114 C ATOM 309 CE1 HIS A 87 -17.873 1.504 -38.720 1.00 32.47 C ANISOU 309 CE1 HIS A 87 3492 2937 5910 -839 3 509 C ATOM 310 NE2 HIS A 87 -18.293 2.032 -37.583 1.00 39.40 N ANISOU 310 NE2 HIS A 87 4476 3704 6792 -893 -232 281 N ATOM 311 N GLN A 88 -21.142 -0.726 -38.633 1.00 24.13 N ANISOU 311 N GLN A 88 2968 2269 3931 -434 40 255 N ATOM 312 CA AGLN A 88 -21.865 -0.626 -39.895 0.56 19.52 C ANISOU 312 CA AGLN A 88 2477 1713 3228 -343 199 384 C ATOM 313 CA BGLN A 88 -21.832 -0.569 -39.902 0.44 24.94 C ANISOU 313 CA BGLN A 88 3158 2391 3926 -348 200 388 C ATOM 314 C GLN A 88 -21.087 -1.182 -41.095 1.00 21.13 C ANISOU 314 C GLN A 88 2603 2016 3410 -295 386 557 C ATOM 315 O GLN A 88 -21.693 -1.747 -42.007 1.00 25.72 O ANISOU 315 O GLN A 88 3295 2705 3774 -176 476 596 O ATOM 316 CB AGLN A 88 -22.263 0.826 -40.164 0.56 20.79 C ANISOU 316 CB AGLN A 88 2687 1689 3525 -380 216 451 C ATOM 317 CB BGLN A 88 -22.070 0.917 -40.144 0.44 31.45 C ANISOU 317 CB BGLN A 88 4013 3021 4915 -400 216 461 C ATOM 318 CG AGLN A 88 -21.089 1.793 -40.174 0.56 23.20 C ANISOU 318 CG AGLN A 88 2837 1822 4156 -525 232 552 C ATOM 319 CG BGLN A 88 -23.267 1.209 -40.978 0.44 20.64 C ANISOU 319 CG BGLN A 88 2786 1663 3392 -286 288 538 C ATOM 320 CD AGLN A 88 -21.529 3.241 -40.170 0.56 25.49 C ANISOU 320 CD AGLN A 88 3189 1869 4627 -572 211 579 C ATOM 321 CD BGLN A 88 -23.945 2.502 -40.593 0.44 30.98 C ANISOU 321 CD BGLN A 88 4168 2769 4834 -302 228 506 C ATOM 322 OE1AGLN A 88 -22.716 3.547 -40.291 0.56 25.70 O ANISOU 322 OE1AGLN A 88 3370 1874 4519 -471 211 551 O ATOM 323 OE1BGLN A 88 -23.297 3.450 -40.144 0.44 28.33 O ANISOU 323 OE1BGLN A 88 3772 2234 4757 -418 185 494 O ATOM 324 NE2AGLN A 88 -20.573 4.141 -40.011 0.56 27.15 N ANISOU 324 NE2AGLN A 88 3261 1875 5181 -728 184 637 N ATOM 325 NE2BGLN A 88 -25.262 2.541 -40.747 0.44 20.71 N ANISOU 325 NE2BGLN A 88 2986 1500 3385 -185 215 484 N ATOM 326 N THR A 89 -19.763 -1.045 -41.093 1.00 22.87 N ANISOU 326 N THR A 89 2632 2206 3852 -377 440 652 N ATOM 327 CA THR A 89 -18.953 -1.507 -42.218 1.00 27.00 C ANISOU 327 CA THR A 89 3067 2826 4365 -306 669 835 C ATOM 328 C THR A 89 -18.935 -3.036 -42.312 1.00 26.00 C ANISOU 328 C THR A 89 2979 2868 4033 -180 694 746 C ATOM 329 O THR A 89 -18.542 -3.587 -43.335 1.00 28.22 O ANISOU 329 O THR A 89 3264 3247 4209 -63 894 847 O ATOM 330 CB THR A 89 -17.499 -0.995 -42.133 1.00 28.55 C ANISOU 330 CB THR A 89 2991 2942 4915 -429 735 983 C ATOM 331 OG1 THR A 89 -16.913 -1.410 -40.896 1.00 34.01 O ANISOU 331 OG1 THR A 89 3545 3629 5747 -515 525 837 O ATOM 332 CG2 THR A 89 -17.444 0.531 -42.224 1.00 38.53 C ANISOU 332 CG2 THR A 89 4208 3994 6438 -562 737 1102 C ATOM 333 N ALA A 90 -19.372 -3.709 -41.252 1.00 22.34 N ANISOU 333 N ALA A 90 2556 2425 3507 -189 506 562 N ATOM 334 CA ALA A 90 -19.401 -5.189 -41.234 1.00 22.48 C ANISOU 334 CA ALA A 90 2609 2555 3378 -79 513 481 C ATOM 335 C ALA A 90 -20.656 -5.793 -41.881 1.00 25.24 C ANISOU 335 C ALA A 90 3174 2957 3461 29 521 404 C ATOM 336 O ALA A 90 -20.774 -7.014 -42.032 1.00 24.81 O ANISOU 336 O ALA A 90 3170 2957 3298 119 528 329 O ATOM 337 CB ALA A 90 -19.275 -5.684 -39.806 1.00 24.46 C ANISOU 337 CB ALA A 90 2799 2803 3691 -130 317 364 C ATOM 338 N ILE A 91 -21.605 -4.941 -42.239 1.00 20.77 N ANISOU 338 N ILE A 91 2721 2353 2817 18 498 419 N ATOM 339 CA ILE A 91 -22.880 -5.371 -42.800 1.00 20.43 C ANISOU 339 CA ILE A 91 2849 2354 2560 101 452 350 C ATOM 340 C ILE A 91 -22.788 -5.371 -44.317 1.00 30.39 C ANISOU 340 C ILE A 91 4209 3688 3649 215 599 443 C ATOM 341 O ILE A 91 -22.345 -4.387 -44.908 1.00 31.05 O ANISOU 341 O ILE A 91 4269 3755 3773 212 724 609 O ATOM 342 CB ILE A 91 -24.012 -4.434 -42.348 1.00 22.20 C ANISOU 342 CB ILE A 91 3128 2509 2798 54 338 328 C ATOM 343 CG1 ILE A 91 -24.074 -4.391 -40.822 1.00 20.33 C ANISOU 343 CG1 ILE A 91 2829 2218 2678 -27 217 228 C ATOM 344 CG2 ILE A 91 -25.338 -4.858 -42.952 1.00 22.16 C ANISOU 344 CG2 ILE A 91 3251 2553 2617 132 267 277 C ATOM 345 CD1 ILE A 91 -25.013 -3.289 -40.274 1.00 21.38 C ANISOU 345 CD1 ILE A 91 3011 2263 2852 -54 145 201 C ATOM 346 N LYS A 92 -23.192 -6.464 -44.957 1.00 22.85 N ANISOU 346 N LYS A 92 3375 2806 2501 323 585 342 N ATOM 347 CA LYS A 92 -23.124 -6.521 -46.410 1.00 28.91 C ANISOU 347 CA LYS A 92 4284 3666 3034 464 710 400 C ATOM 348 C LYS A 92 -24.242 -5.656 -46.992 1.00 34.88 C ANISOU 348 C LYS A 92 5159 4435 3657 482 621 459 C ATOM 349 O LYS A 92 -25.315 -5.537 -46.398 1.00 36.49 O ANISOU 349 O LYS A 92 5363 4589 3913 419 435 381 O ATOM 350 CB LYS A 92 -23.211 -7.969 -46.911 1.00 34.24 C ANISOU 350 CB LYS A 92 5080 4391 3538 581 689 227 C ATOM 351 CG LYS A 92 -21.948 -8.790 -46.651 1.00 44.33 C ANISOU 351 CG LYS A 92 6251 5666 4928 624 837 214 C ATOM 352 CD LYS A 92 -21.938 -10.090 -47.451 1.00 55.95 C ANISOU 352 CD LYS A 92 7886 7168 6203 787 868 48 C ATOM 353 CE LYS A 92 -20.826 -11.028 -46.992 1.00 62.48 C ANISOU 353 CE LYS A 92 8590 7957 7194 837 986 21 C ATOM 354 NZ LYS A 92 -20.874 -12.344 -47.695 1.00 65.87 N ANISOU 354 NZ LYS A 92 9197 8367 7462 1004 1003 -176 N ATOM 355 N LYS A 93 -23.985 -5.027 -48.136 1.00 43.70 N ANISOU 355 N LYS A 93 6367 5623 4613 583 767 624 N ATOM 356 CA LYS A 93 -24.961 -4.099 -48.708 1.00 48.31 C ANISOU 356 CA LYS A 93 7053 6218 5084 617 685 728 C ATOM 357 C LYS A 93 -26.203 -4.820 -49.235 1.00 51.76 C ANISOU 357 C LYS A 93 7651 6731 5283 699 460 563 C ATOM 358 O LYS A 93 -26.170 -6.017 -49.513 1.00 56.89 O ANISOU 358 O LYS A 93 8386 7435 5796 759 412 382 O ATOM 359 CB LYS A 93 -24.325 -3.270 -49.825 1.00 53.67 C ANISOU 359 CB LYS A 93 7796 6962 5635 722 917 991 C ATOM 360 CG LYS A 93 -23.298 -2.250 -49.339 1.00 55.81 C ANISOU 360 CG LYS A 93 7871 7109 6224 605 1103 1202 C ATOM 361 CD LYS A 93 -22.213 -1.961 -50.374 1.00 60.50 C ANISOU 361 CD LYS A 93 8469 7786 6733 712 1423 1457 C ATOM 362 CE LYS A 93 -22.563 -2.504 -51.750 1.00 61.31 C ANISOU 362 CE LYS A 93 8790 8076 6430 917 1426 1405 C ATOM 363 NZ LYS A 93 -21.351 -2.652 -52.601 1.00 68.24 N ANISOU 363 NZ LYS A 93 9618 9036 7274 1017 1688 1511 N ATOM 364 N LYS A 98 -29.187 6.847 -48.245 1.00 79.37 N ANISOU 364 N LYS A 98 10861 8932 10364 565 532 1943 N ATOM 365 CA LYS A 98 -29.907 5.721 -47.661 1.00 70.03 C ANISOU 365 CA LYS A 98 9696 7862 9050 611 404 1758 C ATOM 366 C LYS A 98 -28.925 4.710 -47.074 1.00 53.82 C ANISOU 366 C LYS A 98 7594 5882 6975 483 451 1576 C ATOM 367 O LYS A 98 -27.775 4.624 -47.515 1.00 37.82 O ANISOU 367 O LYS A 98 5553 3879 4937 431 605 1688 O ATOM 368 CB LYS A 98 -30.810 5.061 -48.706 1.00 71.41 C ANISOU 368 CB LYS A 98 9956 8290 8887 767 276 1808 C ATOM 369 CG LYS A 98 -31.804 6.028 -49.336 1.00 77.79 C ANISOU 369 CG LYS A 98 10777 9067 9713 877 184 1952 C ATOM 370 CD LYS A 98 -32.676 6.704 -48.287 1.00 79.03 C ANISOU 370 CD LYS A 98 10851 9019 10158 888 116 1869 C ATOM 371 CE LYS A 98 -33.724 5.753 -47.725 1.00 75.95 C ANISOU 371 CE LYS A 98 10408 8737 9712 953 -43 1711 C ATOM 372 NZ LYS A 98 -34.672 6.440 -46.803 1.00 69.39 N ANISOU 372 NZ LYS A 98 9483 7735 9148 1002 -77 1642 N ATOM 373 N TYR A 99 -29.395 3.939 -46.097 1.00 43.59 N ANISOU 373 N TYR A 99 6252 4633 5678 441 327 1306 N ATOM 374 CA TYR A 99 -28.506 3.176 -45.228 1.00 32.95 C ANISOU 374 CA TYR A 99 4834 3305 4378 310 346 1115 C ATOM 375 C TYR A 99 -28.133 1.808 -45.796 1.00 42.18 C ANISOU 375 C TYR A 99 6028 4702 5295 331 353 1059 C ATOM 376 O TYR A 99 -28.513 0.764 -45.241 1.00 35.74 O ANISOU 376 O TYR A 99 5194 3979 4406 317 251 864 O ATOM 377 CB TYR A 99 -29.151 3.021 -43.849 1.00 27.88 C ANISOU 377 CB TYR A 99 4149 2603 3843 273 236 881 C ATOM 378 CG TYR A 99 -29.618 4.347 -43.277 1.00 35.76 C ANISOU 378 CG TYR A 99 5153 3365 5069 291 232 893 C ATOM 379 CD1 TYR A 99 -30.974 4.642 -43.155 1.00 41.62 C ANISOU 379 CD1 TYR A 99 5907 4093 5815 415 165 884 C ATOM 380 CD2 TYR A 99 -28.698 5.325 -42.902 1.00 39.47 C ANISOU 380 CD2 TYR A 99 5607 3608 5782 188 294 918 C ATOM 381 CE1 TYR A 99 -31.400 5.865 -42.645 1.00 46.70 C ANISOU 381 CE1 TYR A 99 6567 4500 6675 462 183 886 C ATOM 382 CE2 TYR A 99 -29.116 6.548 -42.394 1.00 43.36 C ANISOU 382 CE2 TYR A 99 6130 3844 6501 212 283 901 C ATOM 383 CZ TYR A 99 -30.465 6.812 -42.268 1.00 49.29 C ANISOU 383 CZ TYR A 99 6915 4585 7227 363 240 881 C ATOM 384 OH TYR A 99 -30.869 8.030 -41.766 1.00 53.16 O ANISOU 384 OH TYR A 99 7446 4802 7950 415 250 854 O ATOM 385 N LEU A 100 -27.362 1.825 -46.884 1.00 48.77 N ANISOU 385 N LEU A 100 6909 5612 6010 375 493 1239 N ATOM 386 CA LEU A 100 -26.902 0.603 -47.556 1.00 48.23 C ANISOU 386 CA LEU A 100 6894 5744 5687 431 536 1186 C ATOM 387 C LEU A 100 -26.344 -0.435 -46.592 1.00 48.36 C ANISOU 387 C LEU A 100 6820 5779 5777 334 508 968 C ATOM 388 O LEU A 100 -26.470 -1.637 -46.820 1.00 52.03 O ANISOU 388 O LEU A 100 7334 6373 6061 383 456 833 O ATOM 389 CB LEU A 100 -25.834 0.921 -48.609 1.00 49.40 C ANISOU 389 CB LEU A 100 7072 5942 5756 485 772 1428 C ATOM 390 CG LEU A 100 -26.173 1.494 -49.988 1.00 53.75 C ANISOU 390 CG LEU A 100 7774 6581 6069 648 847 1683 C ATOM 391 CD1 LEU A 100 -27.315 2.500 -49.969 1.00 57.32 C ANISOU 391 CD1 LEU A 100 8249 6928 6602 676 703 1763 C ATOM 392 CD2 LEU A 100 -24.934 2.119 -50.566 1.00 63.50 C ANISOU 392 CD2 LEU A 100 8918 7793 7415 617 1090 1878 C ATOM 393 N ARG A 101 -25.720 0.024 -45.514 1.00 38.85 N ANISOU 393 N ARG A 101 5490 4431 4841 202 524 929 N ATOM 394 CA ARG A 101 -25.253 -0.896 -44.495 1.00 34.06 C ANISOU 394 CA ARG A 101 4799 3845 4298 125 469 742 C ATOM 395 C ARG A 101 -25.949 -0.577 -43.180 1.00 34.14 C ANISOU 395 C ARG A 101 4781 3752 4439 61 327 596 C ATOM 396 O ARG A 101 -25.571 0.332 -42.458 1.00 34.71 O ANISOU 396 O ARG A 101 4799 3674 4713 -24 318 591 O ATOM 397 CB ARG A 101 -23.729 -0.839 -44.373 1.00 32.64 C ANISOU 397 CB ARG A 101 4488 3634 4282 44 601 816 C ATOM 398 CG ARG A 101 -23.014 -1.162 -45.685 1.00 31.27 C ANISOU 398 CG ARG A 101 4338 3577 3965 142 802 981 C ATOM 399 CD ARG A 101 -21.503 -1.226 -45.515 1.00 36.25 C ANISOU 399 CD ARG A 101 4784 4188 4800 71 949 1067 C ATOM 400 NE ARG A 101 -20.795 -1.342 -46.791 1.00 34.37 N ANISOU 400 NE ARG A 101 4560 4058 4442 187 1205 1270 N ATOM 401 CZ ARG A 101 -20.327 -2.485 -47.282 1.00 41.81 C ANISOU 401 CZ ARG A 101 5530 5150 5209 307 1314 1220 C ATOM 402 NH1 ARG A 101 -20.511 -3.617 -46.615 1.00 34.55 N ANISOU 402 NH1 ARG A 101 4619 4267 4244 310 1170 987 N ATOM 403 NH2 ARG A 101 -19.688 -2.503 -48.445 1.00 45.09 N ANISOU 403 NH2 ARG A 101 5974 5670 5489 441 1582 1412 N ATOM 404 N SER A 102 -27.008 -1.324 -42.901 1.00 23.46 N ANISOU 404 N SER A 102 3470 2474 2970 111 218 475 N ATOM 405 CA SER A 102 -27.710 -1.237 -41.630 1.00 19.52 C ANISOU 405 CA SER A 102 2948 1917 2551 85 126 345 C ATOM 406 C SER A 102 -28.502 -2.528 -41.447 1.00 21.26 C ANISOU 406 C SER A 102 3168 2251 2658 121 51 249 C ATOM 407 O SER A 102 -28.775 -3.240 -42.409 1.00 24.68 O ANISOU 407 O SER A 102 3640 2773 2966 170 29 266 O ATOM 408 CB SER A 102 -28.642 -0.027 -41.568 1.00 26.42 C ANISOU 408 CB SER A 102 3854 2678 3507 131 107 391 C ATOM 409 OG SER A 102 -29.722 -0.170 -42.467 1.00 30.25 O ANISOU 409 OG SER A 102 4375 3238 3882 229 63 463 O ATOM 410 N VAL A 103 -28.838 -2.823 -40.201 1.00 21.57 N ANISOU 410 N VAL A 103 3172 2278 2745 99 13 148 N ATOM 411 CA VAL A 103 -29.755 -3.907 -39.872 1.00 17.73 C ANISOU 411 CA VAL A 103 2657 1862 2217 124 -41 95 C ATOM 412 C VAL A 103 -30.838 -3.314 -38.967 1.00 21.45 C ANISOU 412 C VAL A 103 3106 2293 2752 166 -41 78 C ATOM 413 O VAL A 103 -30.663 -2.221 -38.415 1.00 21.77 O ANISOU 413 O VAL A 103 3179 2247 2847 175 -8 58 O ATOM 414 CB VAL A 103 -29.039 -5.086 -39.177 1.00 19.86 C ANISOU 414 CB VAL A 103 2896 2175 2473 82 -39 34 C ATOM 415 CG1 VAL A 103 -28.123 -5.802 -40.166 1.00 19.37 C ANISOU 415 CG1 VAL A 103 2851 2153 2356 79 -17 46 C ATOM 416 CG2 VAL A 103 -28.250 -4.607 -37.960 1.00 21.08 C ANISOU 416 CG2 VAL A 103 3043 2297 2670 45 -25 -9 C ATOM 417 N GLY A 104 -31.955 -4.018 -38.828 1.00 19.55 N ANISOU 417 N GLY A 104 2802 2099 2526 197 -71 83 N ATOM 418 CA GLY A 104 -33.066 -3.503 -38.041 1.00 18.40 C ANISOU 418 CA GLY A 104 2609 1932 2452 265 -30 95 C ATOM 419 C GLY A 104 -33.203 -4.194 -36.704 1.00 16.75 C ANISOU 419 C GLY A 104 2369 1763 2232 270 36 62 C ATOM 420 O GLY A 104 -32.920 -5.385 -36.599 1.00 17.36 O ANISOU 420 O GLY A 104 2416 1887 2294 218 16 66 O ATOM 421 N ASP A 105 -33.632 -3.458 -35.682 1.00 15.39 N ANISOU 421 N ASP A 105 2220 1568 2060 352 125 36 N ATOM 422 CA ASP A 105 -33.841 -4.050 -34.368 1.00 17.33 C ANISOU 422 CA ASP A 105 2460 1878 2246 393 217 30 C ATOM 423 C ASP A 105 -34.806 -5.233 -34.480 1.00 19.26 C ANISOU 423 C ASP A 105 2550 2178 2589 380 239 147 C ATOM 424 O ASP A 105 -35.861 -5.097 -35.089 1.00 19.24 O ANISOU 424 O ASP A 105 2430 2162 2719 404 224 214 O ATOM 425 CB ASP A 105 -34.423 -3.051 -33.380 1.00 19.44 C ANISOU 425 CB ASP A 105 2785 2122 2478 528 334 -17 C ATOM 426 CG ASP A 105 -33.518 -1.865 -33.122 1.00 22.17 C ANISOU 426 CG ASP A 105 3290 2370 2765 531 290 -162 C ATOM 427 OD1 ASP A 105 -32.473 -1.720 -33.803 1.00 21.66 O ANISOU 427 OD1 ASP A 105 3253 2254 2723 420 181 -188 O ATOM 428 OD2 ASP A 105 -33.909 -1.064 -32.249 1.00 23.94 O ANISOU 428 OD2 ASP A 105 3602 2556 2939 654 375 -246 O ATOM 429 N GLY A 106 -34.436 -6.364 -33.889 1.00 17.38 N ANISOU 429 N GLY A 106 2301 1988 2314 339 261 180 N ATOM 430 CA GLY A 106 -35.296 -7.543 -33.902 1.00 19.29 C ANISOU 430 CA GLY A 106 2387 2241 2700 306 285 303 C ATOM 431 C GLY A 106 -35.134 -8.454 -35.103 1.00 20.40 C ANISOU 431 C GLY A 106 2476 2329 2945 192 129 290 C ATOM 432 O GLY A 106 -35.715 -9.546 -35.133 1.00 23.02 O ANISOU 432 O GLY A 106 2685 2630 3432 136 114 368 O ATOM 433 N GLU A 107 -34.339 -8.031 -36.079 1.00 18.20 N ANISOU 433 N GLU A 107 2296 2032 2588 161 21 193 N ATOM 434 CA GLU A 107 -34.079 -8.822 -37.282 1.00 18.77 C ANISOU 434 CA GLU A 107 2373 2068 2692 90 -117 146 C ATOM 435 C GLU A 107 -33.205 -10.049 -36.978 1.00 17.30 C ANISOU 435 C GLU A 107 2217 1857 2501 44 -112 131 C ATOM 436 O GLU A 107 -32.280 -9.960 -36.158 1.00 18.40 O ANISOU 436 O GLU A 107 2419 2028 2546 66 -39 133 O ATOM 437 CB GLU A 107 -33.395 -7.936 -38.322 1.00 22.27 C ANISOU 437 CB GLU A 107 2928 2520 3014 106 -175 82 C ATOM 438 CG GLU A 107 -33.185 -8.549 -39.676 1.00 29.10 C ANISOU 438 CG GLU A 107 3839 3375 3841 79 -300 23 C ATOM 439 CD GLU A 107 -32.577 -7.592 -40.680 1.00 34.19 C ANISOU 439 CD GLU A 107 4595 4049 4347 120 -309 13 C ATOM 440 OE1 GLU A 107 -32.248 -6.431 -40.318 1.00 30.69 O ANISOU 440 OE1 GLU A 107 4178 3601 3883 147 -227 54 O ATOM 441 OE2 GLU A 107 -32.425 -8.004 -41.851 1.00 37.75 O ANISOU 441 OE2 GLU A 107 5117 4519 4707 133 -396 -34 O ATOM 442 N THR A 108 -33.491 -11.183 -37.622 1.00 15.31 N ANISOU 442 N THR A 108 1920 1534 2362 -13 -207 110 N ATOM 443 CA THR A 108 -32.592 -12.334 -37.560 1.00 17.74 C ANISOU 443 CA THR A 108 2273 1783 2683 -37 -210 81 C ATOM 444 C THR A 108 -31.561 -12.182 -38.671 1.00 18.84 C ANISOU 444 C THR A 108 2540 1934 2684 -14 -262 -40 C ATOM 445 O THR A 108 -31.910 -11.936 -39.826 1.00 22.15 O ANISOU 445 O THR A 108 3003 2357 3058 -9 -362 -114 O ATOM 446 CB THR A 108 -33.342 -13.683 -37.694 1.00 20.81 C ANISOU 446 CB THR A 108 2567 2044 3296 -108 -283 100 C ATOM 447 OG1 THR A 108 -34.061 -13.953 -36.483 1.00 21.81 O ANISOU 447 OG1 THR A 108 2564 2164 3559 -119 -169 270 O ATOM 448 CG2 THR A 108 -32.331 -14.807 -37.921 1.00 22.16 C ANISOU 448 CG2 THR A 108 2818 2121 3482 -110 -302 35 C ATOM 449 N VAL A 109 -30.281 -12.281 -38.308 1.00 18.04 N ANISOU 449 N VAL A 109 2492 1854 2508 16 -189 -42 N ATOM 450 CA VAL A 109 -29.194 -12.147 -39.261 1.00 15.23 C ANISOU 450 CA VAL A 109 2226 1519 2044 55 -182 -118 C ATOM 451 C VAL A 109 -28.189 -13.303 -39.150 1.00 17.78 C ANISOU 451 C VAL A 109 2559 1784 2412 84 -148 -138 C ATOM 452 O VAL A 109 -28.150 -14.015 -38.140 1.00 20.03 O ANISOU 452 O VAL A 109 2787 2027 2796 74 -128 -66 O ATOM 453 CB VAL A 109 -28.431 -10.817 -39.062 1.00 16.77 C ANISOU 453 CB VAL A 109 2436 1795 2142 71 -114 -82 C ATOM 454 CG1 VAL A 109 -29.313 -9.625 -39.470 1.00 19.59 C ANISOU 454 CG1 VAL A 109 2807 2179 2459 69 -140 -68 C ATOM 455 CG2 VAL A 109 -27.984 -10.685 -37.628 1.00 21.29 C ANISOU 455 CG2 VAL A 109 2960 2392 2739 61 -74 -23 C ATOM 456 N GLU A 110 -27.401 -13.481 -40.207 1.00 20.98 N ANISOU 456 N GLU A 110 3042 2191 2740 142 -126 -219 N ATOM 457 CA GLU A 110 -26.358 -14.506 -40.249 1.00 20.11 C ANISOU 457 CA GLU A 110 2940 2021 2679 206 -69 -244 C ATOM 458 C GLU A 110 -25.033 -13.782 -40.399 1.00 19.94 C ANISOU 458 C GLU A 110 2894 2095 2585 257 43 -198 C ATOM 459 O GLU A 110 -24.926 -12.833 -41.165 1.00 20.65 O ANISOU 459 O GLU A 110 3025 2258 2562 268 81 -200 O ATOM 460 CB GLU A 110 -26.583 -15.481 -41.402 1.00 22.14 C ANISOU 460 CB GLU A 110 3309 2178 2924 257 -120 -398 C ATOM 461 CG GLU A 110 -25.662 -16.703 -41.365 1.00 24.49 C ANISOU 461 CG GLU A 110 3619 2367 3319 342 -57 -435 C ATOM 462 CD GLU A 110 -26.061 -17.745 -42.394 1.00 40.79 C ANISOU 462 CD GLU A 110 5822 4285 5393 389 -138 -632 C ATOM 463 OE1 GLU A 110 -27.250 -17.770 -42.781 1.00 44.88 O ANISOU 463 OE1 GLU A 110 6379 4757 5917 312 -294 -715 O ATOM 464 OE2 GLU A 110 -25.202 -18.558 -42.795 1.00 40.94 O ANISOU 464 OE2 GLU A 110 5904 4224 5428 509 -58 -712 O ATOM 465 N PHE A 111 -24.017 -14.219 -39.669 1.00 18.76 N ANISOU 465 N PHE A 111 2660 1942 2525 288 91 -133 N ATOM 466 CA PHE A 111 -22.769 -13.484 -39.672 1.00 16.15 C ANISOU 466 CA PHE A 111 2247 1696 2192 311 175 -66 C ATOM 467 C PHE A 111 -21.618 -14.379 -39.252 1.00 19.67 C ANISOU 467 C PHE A 111 2596 2117 2760 388 221 -16 C ATOM 468 O PHE A 111 -21.819 -15.491 -38.741 1.00 21.13 O ANISOU 468 O PHE A 111 2786 2214 3027 419 181 -13 O ATOM 469 CB PHE A 111 -22.860 -12.266 -38.731 1.00 18.33 C ANISOU 469 CB PHE A 111 2460 2039 2465 215 116 1 C ATOM 470 CG PHE A 111 -23.316 -12.613 -37.336 1.00 22.46 C ANISOU 470 CG PHE A 111 2958 2556 3020 183 26 41 C ATOM 471 CD1 PHE A 111 -22.405 -12.758 -36.306 1.00 23.09 C ANISOU 471 CD1 PHE A 111 2947 2675 3152 196 -16 111 C ATOM 472 CD2 PHE A 111 -24.658 -12.806 -37.057 1.00 18.11 C ANISOU 472 CD2 PHE A 111 2466 1971 2443 153 -13 28 C ATOM 473 CE1 PHE A 111 -22.830 -13.093 -35.022 1.00 22.65 C ANISOU 473 CE1 PHE A 111 2900 2639 3069 196 -86 168 C ATOM 474 CE2 PHE A 111 -25.085 -13.145 -35.778 1.00 19.87 C ANISOU 474 CE2 PHE A 111 2670 2204 2677 147 -47 101 C ATOM 475 CZ PHE A 111 -24.168 -13.293 -34.764 1.00 21.07 C ANISOU 475 CZ PHE A 111 2771 2407 2827 177 -78 172 C ATOM 476 N ASP A 112 -20.413 -13.884 -39.494 1.00 18.76 N ANISOU 476 N ASP A 112 2373 2068 2687 421 310 45 N ATOM 477 CA ASP A 112 -19.216 -14.500 -38.945 1.00 20.06 C ANISOU 477 CA ASP A 112 2386 2234 3003 491 333 128 C ATOM 478 C ASP A 112 -18.851 -13.738 -37.679 1.00 23.10 C ANISOU 478 C ASP A 112 2643 2691 3444 393 198 215 C ATOM 479 O ASP A 112 -19.209 -12.571 -37.521 1.00 22.27 O ANISOU 479 O ASP A 112 2556 2627 3280 287 145 202 O ATOM 480 CB ASP A 112 -18.064 -14.480 -39.955 1.00 27.32 C ANISOU 480 CB ASP A 112 3222 3186 3973 598 520 158 C ATOM 481 CG ASP A 112 -18.411 -15.179 -41.261 1.00 31.84 C ANISOU 481 CG ASP A 112 3973 3703 4424 726 652 34 C ATOM 482 OD1 ASP A 112 -19.207 -16.140 -41.238 1.00 29.18 O ANISOU 482 OD1 ASP A 112 3770 3255 4063 751 577 -75 O ATOM 483 OD2 ASP A 112 -17.869 -14.772 -42.315 1.00 32.15 O ANISOU 483 OD2 ASP A 112 4020 3804 4393 806 830 47 O ATOM 484 N VAL A 113 -18.170 -14.409 -36.762 1.00 23.74 N ANISOU 484 N VAL A 113 2612 2778 3631 439 125 296 N ATOM 485 CA VAL A 113 -17.646 -13.754 -35.577 1.00 23.94 C ANISOU 485 CA VAL A 113 2520 2885 3689 369 -39 361 C ATOM 486 C VAL A 113 -16.134 -13.727 -35.708 1.00 24.18 C ANISOU 486 C VAL A 113 2314 2956 3917 411 -19 451 C ATOM 487 O VAL A 113 -15.525 -14.761 -35.916 1.00 23.84 O ANISOU 487 O VAL A 113 2193 2880 3985 543 59 511 O ATOM 488 CB VAL A 113 -18.051 -14.481 -34.280 1.00 25.76 C ANISOU 488 CB VAL A 113 2800 3125 3862 399 -174 417 C ATOM 489 CG1 VAL A 113 -17.461 -13.778 -33.073 1.00 33.12 C ANISOU 489 CG1 VAL A 113 3645 4165 4772 348 -376 455 C ATOM 490 CG2 VAL A 113 -19.577 -14.564 -34.158 1.00 24.89 C ANISOU 490 CG2 VAL A 113 2881 2972 3605 361 -158 362 C ATOM 491 N VAL A 114 -15.538 -12.535 -35.641 1.00 25.70 N ANISOU 491 N VAL A 114 2377 3197 4189 302 -79 466 N ATOM 492 CA VAL A 114 -14.098 -12.393 -35.788 1.00 29.76 C ANISOU 492 CA VAL A 114 2610 3746 4951 316 -60 574 C ATOM 493 C VAL A 114 -13.499 -11.643 -34.605 1.00 28.36 C ANISOU 493 C VAL A 114 2283 3623 4868 198 -341 591 C ATOM 494 O VAL A 114 -14.224 -11.036 -33.809 1.00 27.62 O ANISOU 494 O VAL A 114 2342 3540 4614 107 -515 495 O ATOM 495 CB VAL A 114 -13.724 -11.654 -37.089 1.00 31.84 C ANISOU 495 CB VAL A 114 2800 3994 5304 291 167 608 C ATOM 496 CG1 VAL A 114 -14.355 -12.348 -38.293 1.00 29.74 C ANISOU 496 CG1 VAL A 114 2728 3691 4880 424 412 555 C ATOM 497 CG2 VAL A 114 -14.176 -10.192 -37.017 1.00 27.63 C ANISOU 497 CG2 VAL A 114 2320 3439 4739 112 84 559 C ATOM 498 N GLU A 115 -12.178 -11.710 -34.486 1.00 33.03 N ANISOU 498 N GLU A 115 2576 4251 5723 212 -393 706 N ATOM 499 CA GLU A 115 -11.461 -11.003 -33.430 1.00 40.82 C ANISOU 499 CA GLU A 115 3385 5285 6839 92 -707 710 C ATOM 500 C GLU A 115 -11.080 -9.596 -33.863 1.00 41.99 C ANISOU 500 C GLU A 115 3399 5375 7180 -94 -712 693 C ATOM 501 O GLU A 115 -10.145 -9.403 -34.643 1.00 45.98 O ANISOU 501 O GLU A 115 3634 5862 7973 -107 -554 825 O ATOM 502 CB GLU A 115 -10.203 -11.770 -33.013 1.00 42.00 C ANISOU 502 CB GLU A 115 3233 5498 7226 191 -811 859 C ATOM 503 CG GLU A 115 -9.608 -11.333 -31.671 1.00 51.47 C ANISOU 503 CG GLU A 115 4301 6774 8482 100 -1230 842 C ATOM 504 CD GLU A 115 -10.526 -11.556 -30.465 1.00 64.97 C ANISOU 504 CD GLU A 115 6317 8545 9824 132 -1454 739 C ATOM 505 OE1 GLU A 115 -11.684 -11.999 -30.631 1.00 65.38 O ANISOU 505 OE1 GLU A 115 6657 8568 9616 200 -1281 692 O ATOM 506 OE2 GLU A 115 -10.071 -11.286 -29.332 1.00 76.56 O ANISOU 506 OE2 GLU A 115 7745 10096 11247 94 -1793 703 O ATOM 507 N GLY A 116 -11.820 -8.615 -33.360 1.00 51.19 N ANISOU 507 N GLY A 116 4750 6498 8200 -228 -871 545 N ATOM 508 CA GLY A 116 -11.523 -7.225 -33.641 1.00 55.71 C ANISOU 508 CA GLY A 116 5217 6970 8980 -416 -911 519 C ATOM 509 C GLY A 116 -10.570 -6.640 -32.619 1.00 63.86 C ANISOU 509 C GLY A 116 6027 7998 10238 -553 -1283 481 C ATOM 510 O GLY A 116 -10.065 -7.353 -31.751 1.00 58.16 O ANISOU 510 O GLY A 116 5234 7382 9483 -478 -1492 494 O ATOM 511 N GLU A 117 -10.340 -5.334 -32.720 1.00 73.49 N ANISOU 511 N GLU A 117 7202 9084 11637 -736 -1348 424 N ATOM 512 CA GLU A 117 -9.385 -4.633 -31.866 1.00 77.32 C ANISOU 512 CA GLU A 117 7590 9529 12258 -849 -1630 348 C ATOM 513 C GLU A 117 -9.794 -4.662 -30.396 1.00 69.64 C ANISOU 513 C GLU A 117 6842 8631 10986 -829 -1985 133 C ATOM 514 O GLU A 117 -8.946 -4.627 -29.504 1.00 73.44 O ANISOU 514 O GLU A 117 7237 9164 11501 -850 -2243 89 O ATOM 515 CB GLU A 117 -9.232 -3.184 -32.336 1.00 87.10 C ANISOU 515 CB GLU A 117 8804 10571 13716 -1025 -1584 323 C ATOM 516 CG GLU A 117 -9.276 -3.024 -33.852 1.00 92.22 C ANISOU 516 CG GLU A 117 9356 11153 14530 -1018 -1181 528 C ATOM 517 CD GLU A 117 -8.182 -2.117 -34.379 1.00101.75 C ANISOU 517 CD GLU A 117 10329 12232 16098 -1133 -1105 665 C ATOM 518 OE1 GLU A 117 -7.042 -2.194 -33.871 1.00106.34 O ANISOU 518 OE1 GLU A 117 10691 12835 16880 -1170 -1275 698 O ATOM 519 OE2 GLU A 117 -8.466 -1.326 -35.303 1.00102.77 O ANISOU 519 OE2 GLU A 117 10491 12241 16315 -1182 -878 754 O ATOM 520 N LYS A 118 -11.099 -4.726 -30.154 1.00 58.44 N ANISOU 520 N LYS A 118 5720 7228 9257 -773 -1985 8 N ATOM 521 CA LYS A 118 -11.636 -4.670 -28.798 1.00 55.07 C ANISOU 521 CA LYS A 118 5568 6880 8477 -720 -2254 -193 C ATOM 522 C LYS A 118 -12.397 -5.941 -28.433 1.00 55.66 C ANISOU 522 C LYS A 118 5798 7118 8233 -528 -2227 -139 C ATOM 523 O LYS A 118 -13.300 -5.922 -27.592 1.00 51.68 O ANISOU 523 O LYS A 118 5594 6673 7370 -450 -2319 -275 O ATOM 524 CB LYS A 118 -12.540 -3.445 -28.646 1.00 51.24 C ANISOU 524 CB LYS A 118 5344 6250 7876 -802 -2273 -406 C ATOM 525 CG LYS A 118 -11.818 -2.140 -28.935 1.00 55.59 C ANISOU 525 CG LYS A 118 5760 6608 8751 -983 -2310 -447 C ATOM 526 CD LYS A 118 -12.778 -1.032 -29.329 1.00 62.89 C ANISOU 526 CD LYS A 118 6888 7347 9660 -1045 -2195 -566 C ATOM 527 CE LYS A 118 -12.027 0.264 -29.590 1.00 70.75 C ANISOU 527 CE LYS A 118 7747 8134 10999 -1214 -2235 -579 C ATOM 528 NZ LYS A 118 -10.926 0.081 -30.578 1.00 71.96 N ANISOU 528 NZ LYS A 118 7544 8265 11534 -1287 -2083 -319 N ATOM 529 N GLY A 119 -12.018 -7.048 -29.066 1.00 55.40 N ANISOU 529 N GLY A 119 5586 7149 8315 -426 -2041 74 N ATOM 530 CA GLY A 119 -12.656 -8.326 -28.810 1.00 52.43 C ANISOU 530 CA GLY A 119 5378 6888 7657 -229 -1913 162 C ATOM 531 C GLY A 119 -13.452 -8.835 -29.998 1.00 49.37 C ANISOU 531 C GLY A 119 5080 6437 7240 -163 -1512 239 C ATOM 532 O GLY A 119 -13.259 -8.391 -31.131 1.00 47.59 O ANISOU 532 O GLY A 119 4740 6117 7223 -235 -1312 276 O ATOM 533 N ALA A 120 -14.353 -9.773 -29.733 1.00 44.13 N ANISOU 533 N ALA A 120 4623 5826 6318 -24 -1403 273 N ATOM 534 CA ALA A 120 -15.178 -10.364 -30.778 1.00 36.66 C ANISOU 534 CA ALA A 120 3778 4816 5337 38 -1080 319 C ATOM 535 C ALA A 120 -16.079 -9.319 -31.420 1.00 37.47 C ANISOU 535 C ALA A 120 4024 4830 5383 -59 -958 201 C ATOM 536 O ALA A 120 -16.570 -8.411 -30.752 1.00 40.51 O ANISOU 536 O ALA A 120 4543 5207 5639 -123 -1091 72 O ATOM 537 CB ALA A 120 -16.010 -11.505 -30.217 1.00 42.97 C ANISOU 537 CB ALA A 120 4753 5659 5915 176 -1030 379 C ATOM 538 N GLU A 121 -16.277 -9.449 -32.724 1.00 27.20 N ANISOU 538 N GLU A 121 2704 3462 4168 -51 -709 244 N ATOM 539 CA GLU A 121 -17.204 -8.590 -33.444 1.00 25.35 C ANISOU 539 CA GLU A 121 2611 3153 3870 -114 -583 170 C ATOM 540 C GLU A 121 -17.788 -9.335 -34.622 1.00 24.24 C ANISOU 540 C GLU A 121 2539 2986 3683 -30 -341 214 C ATOM 541 O GLU A 121 -17.218 -10.317 -35.096 1.00 26.79 O ANISOU 541 O GLU A 121 2773 3322 4084 59 -242 291 O ATOM 542 CB GLU A 121 -16.510 -7.314 -33.916 1.00 24.74 C ANISOU 542 CB GLU A 121 2397 2999 4002 -247 -599 166 C ATOM 543 CG GLU A 121 -15.378 -7.545 -34.900 1.00 29.08 C ANISOU 543 CG GLU A 121 2706 3544 4798 -240 -447 310 C ATOM 544 CD GLU A 121 -14.634 -6.262 -35.244 1.00 44.50 C ANISOU 544 CD GLU A 121 4485 5408 7016 -392 -464 350 C ATOM 545 OE1 GLU A 121 -14.494 -5.958 -36.446 1.00 53.52 O ANISOU 545 OE1 GLU A 121 5574 6510 8250 -391 -223 459 O ATOM 546 OE2 GLU A 121 -14.181 -5.565 -34.313 1.00 38.49 O ANISOU 546 OE2 GLU A 121 3643 4609 6371 -511 -723 277 O ATOM 547 N ALA A 122 -18.932 -8.874 -35.096 1.00 20.05 N ANISOU 547 N ALA A 122 2174 2415 3030 -48 -261 153 N ATOM 548 CA ALA A 122 -19.575 -9.503 -36.237 1.00 20.61 C ANISOU 548 CA ALA A 122 2332 2463 3037 23 -85 163 C ATOM 549 C ALA A 122 -18.865 -9.085 -37.517 1.00 19.85 C ANISOU 549 C ALA A 122 2152 2351 3040 24 72 224 C ATOM 550 O ALA A 122 -18.281 -7.993 -37.589 1.00 25.24 O ANISOU 550 O ALA A 122 2735 3010 3846 -66 63 264 O ATOM 551 CB ALA A 122 -21.050 -9.125 -36.290 1.00 21.55 C ANISOU 551 CB ALA A 122 2625 2555 3008 7 -83 95 C ATOM 552 N ALA A 123 -18.910 -9.965 -38.515 1.00 22.43 N ANISOU 552 N ALA A 123 2524 2681 3316 131 223 234 N ATOM 553 CA ALA A 123 -18.402 -9.675 -39.855 1.00 18.89 C ANISOU 553 CA ALA A 123 2052 2244 2881 181 421 297 C ATOM 554 C ALA A 123 -19.330 -10.313 -40.874 1.00 21.02 C ANISOU 554 C ALA A 123 2525 2510 2951 281 504 218 C ATOM 555 O ALA A 123 -20.011 -11.295 -40.556 1.00 21.54 O ANISOU 555 O ALA A 123 2684 2543 2959 317 425 129 O ATOM 556 CB ALA A 123 -16.965 -10.198 -40.035 1.00 23.66 C ANISOU 556 CB ALA A 123 2452 2878 3658 255 535 395 C ATOM 557 N ASN A 124 -19.358 -9.757 -42.087 1.00 21.28 N ANISOU 557 N ASN A 124 2627 2571 2887 323 649 259 N ATOM 558 CA ASN A 124 -20.134 -10.339 -43.183 1.00 21.20 C ANISOU 558 CA ASN A 124 2824 2575 2655 435 700 167 C ATOM 559 C ASN A 124 -21.584 -10.572 -42.806 1.00 22.65 C ANISOU 559 C ASN A 124 3139 2714 2752 381 511 49 C ATOM 560 O ASN A 124 -22.110 -11.672 -42.996 1.00 22.26 O ANISOU 560 O ASN A 124 3189 2624 2645 440 458 -69 O ATOM 561 CB ASN A 124 -19.516 -11.670 -43.634 1.00 25.43 C ANISOU 561 CB ASN A 124 3380 3105 3176 590 810 104 C ATOM 562 CG ASN A 124 -18.097 -11.508 -44.115 1.00 37.12 C ANISOU 562 CG ASN A 124 4709 4643 4751 678 1042 239 C ATOM 563 OD1 ASN A 124 -17.783 -10.556 -44.830 1.00 41.15 O ANISOU 563 OD1 ASN A 124 5200 5214 5221 681 1189 364 O ATOM 564 ND2 ASN A 124 -17.222 -12.424 -43.713 1.00 43.45 N ANISOU 564 ND2 ASN A 124 5382 5421 5707 757 1091 245 N ATOM 565 N VAL A 125 -22.220 -9.535 -42.268 1.00 19.47 N ANISOU 565 N VAL A 125 2722 2301 2373 272 416 83 N ATOM 566 CA VAL A 125 -23.565 -9.660 -41.727 1.00 16.29 C ANISOU 566 CA VAL A 125 2390 1864 1937 222 262 6 C ATOM 567 C VAL A 125 -24.595 -9.607 -42.851 1.00 23.50 C ANISOU 567 C VAL A 125 3449 2793 2688 270 229 -43 C ATOM 568 O VAL A 125 -24.659 -8.640 -43.603 1.00 20.29 O ANISOU 568 O VAL A 125 3088 2425 2196 288 279 28 O ATOM 569 CB VAL A 125 -23.882 -8.554 -40.693 1.00 15.73 C ANISOU 569 CB VAL A 125 2259 1773 1943 121 188 46 C ATOM 570 CG1 VAL A 125 -25.278 -8.762 -40.085 1.00 20.48 C ANISOU 570 CG1 VAL A 125 2908 2352 2522 98 76 -10 C ATOM 571 CG2 VAL A 125 -22.829 -8.506 -39.602 1.00 18.75 C ANISOU 571 CG2 VAL A 125 2513 2154 2459 73 169 77 C ATOM 572 N THR A 126 -25.396 -10.661 -42.957 1.00 22.97 N ANISOU 572 N THR A 126 3447 2687 2594 290 128 -155 N ATOM 573 CA THR A 126 -26.407 -10.787 -44.007 1.00 20.99 C ANISOU 573 CA THR A 126 3327 2449 2200 331 31 -235 C ATOM 574 C THR A 126 -27.718 -11.271 -43.413 1.00 22.76 C ANISOU 574 C THR A 126 3513 2605 2531 255 -138 -291 C ATOM 575 O THR A 126 -27.804 -11.552 -42.232 1.00 20.61 O ANISOU 575 O THR A 126 3137 2285 2411 191 -141 -256 O ATOM 576 CB THR A 126 -26.001 -11.801 -45.081 1.00 28.88 C ANISOU 576 CB THR A 126 4462 3447 3065 448 61 -358 C ATOM 577 OG1 THR A 126 -25.969 -13.109 -44.492 1.00 30.85 O ANISOU 577 OG1 THR A 126 4679 3583 3460 433 12 -455 O ATOM 578 CG2 THR A 126 -24.635 -11.475 -45.653 1.00 37.01 C ANISOU 578 CG2 THR A 126 5501 4551 4008 549 284 -278 C ATOM 579 N GLY A 127 -28.734 -11.404 -44.252 1.00 25.56 N ANISOU 579 N GLY A 127 3945 2961 2805 269 -281 -367 N ATOM 580 CA GLY A 127 -29.921 -12.122 -43.837 1.00 28.72 C ANISOU 580 CA GLY A 127 4278 3275 3360 193 -445 -423 C ATOM 581 C GLY A 127 -29.611 -13.602 -43.707 1.00 29.92 C ANISOU 581 C GLY A 127 4447 3305 3615 189 -466 -535 C ATOM 582 O GLY A 127 -28.573 -14.077 -44.175 1.00 33.63 O ANISOU 582 O GLY A 127 5012 3770 3995 275 -373 -600 O ATOM 583 N PRO A 128 -30.518 -14.348 -43.072 1.00 28.94 N ANISOU 583 N PRO A 128 4220 3068 3709 97 -572 -539 N ATOM 584 CA PRO A 128 -30.360 -15.794 -42.895 1.00 29.53 C ANISOU 584 CA PRO A 128 4300 2974 3945 79 -606 -625 C ATOM 585 C PRO A 128 -30.388 -16.524 -44.242 1.00 38.93 C ANISOU 585 C PRO A 128 5665 4093 5033 138 -745 -854 C ATOM 586 O PRO A 128 -31.213 -16.207 -45.094 1.00 43.80 O ANISOU 586 O PRO A 128 6336 4751 5553 130 -922 -941 O ATOM 587 CB PRO A 128 -31.558 -16.171 -42.019 1.00 36.42 C ANISOU 587 CB PRO A 128 4999 3750 5088 -46 -687 -534 C ATOM 588 CG PRO A 128 -32.568 -15.110 -42.285 1.00 36.99 C ANISOU 588 CG PRO A 128 5012 3931 5112 -75 -773 -489 C ATOM 589 CD PRO A 128 -31.787 -13.847 -42.516 1.00 28.48 C ANISOU 589 CD PRO A 128 4019 3019 3784 13 -650 -443 C ATOM 590 N GLY A 129 -29.484 -17.479 -44.428 1.00 47.51 N ANISOU 590 N GLY A 129 6846 5077 6128 217 -674 -958 N ATOM 591 CA GLY A 129 -29.328 -18.137 -45.714 1.00 58.71 C ANISOU 591 CA GLY A 129 8480 6435 7393 319 -771 -1208 C ATOM 592 C GLY A 129 -28.590 -17.259 -46.711 1.00 62.43 C ANISOU 592 C GLY A 129 9109 7111 7499 474 -650 -1225 C ATOM 593 O GLY A 129 -28.126 -16.165 -46.369 1.00 57.98 O ANISOU 593 O GLY A 129 8465 6707 6859 481 -490 -1033 O TER 594 GLY A 129 ATOM 595 P C B 2 -17.386 5.980 -35.574 1.00122.74 P ANISOU 595 P C B 2 15050 13579 18005 -1247 -764 -119 P ATOM 596 OP1 C B 2 -16.131 6.772 -35.659 1.00124.34 O ANISOU 596 OP1 C B 2 15035 13660 18550 -1395 -823 -37 O ATOM 597 OP2 C B 2 -18.644 6.644 -35.146 1.00121.06 O ANISOU 597 OP2 C B 2 15115 13251 17632 -1156 -790 -297 O ATOM 598 O5' C B 2 -17.119 4.744 -34.604 1.00 54.31 O ANISOU 598 O5' C B 2 6367 5122 9146 -1219 -951 -277 O ATOM 599 C5' C B 2 -18.159 4.201 -33.796 1.00 52.38 C ANISOU 599 C5' C B 2 6360 4969 8574 -1097 -1039 -486 C ATOM 600 C4' C B 2 -17.711 2.952 -33.074 1.00 51.53 C ANISOU 600 C4' C B 2 6192 5079 8310 -1070 -1190 -553 C ATOM 601 O4' C B 2 -17.416 1.909 -34.046 1.00 46.85 O ANISOU 601 O4' C B 2 5434 4639 7728 -1036 -986 -309 O ATOM 602 C3' C B 2 -16.454 3.103 -32.219 1.00 54.79 C ANISOU 602 C3' C B 2 6456 5517 8846 -1164 -1436 -636 C ATOM 603 O3' C B 2 -16.572 2.269 -31.069 1.00 54.91 O ANISOU 603 O3' C B 2 6580 5716 8565 -1072 -1630 -801 O ATOM 604 C2' C B 2 -15.356 2.556 -33.131 1.00 56.90 C ANISOU 604 C2' C B 2 6402 5844 9375 -1236 -1315 -368 C ATOM 605 O2' C B 2 -14.215 2.076 -32.455 1.00 60.24 O ANISOU 605 O2' C B 2 6640 6376 9874 -1276 -1516 -385 O ATOM 606 C1' C B 2 -16.093 1.437 -33.857 1.00 50.95 C ANISOU 606 C1' C B 2 5685 5223 8449 -1128 -1105 -242 C ATOM 607 N1 C B 2 -15.535 1.099 -35.177 1.00 50.89 N ANISOU 607 N1 C B 2 5467 5259 8609 -1129 -820 51 N ATOM 608 C2 C B 2 -15.185 -0.231 -35.463 1.00 55.16 C ANISOU 608 C2 C B 2 5913 6024 9020 -1013 -703 165 C ATOM 609 O2 C B 2 -15.342 -1.107 -34.595 1.00 53.33 O ANISOU 609 O2 C B 2 5759 5940 8563 -926 -847 44 O ATOM 610 N3 C B 2 -14.686 -0.536 -36.687 1.00 56.19 N ANISOU 610 N3 C B 2 5883 6200 9267 -979 -418 412 N ATOM 611 C4 C B 2 -14.531 0.424 -37.601 1.00 55.95 C ANISOU 611 C4 C B 2 5780 6020 9460 -1058 -243 578 C ATOM 612 N4 C B 2 -14.033 0.081 -38.791 1.00 57.95 N ANISOU 612 N4 C B 2 5897 6348 9774 -992 64 832 N ATOM 613 C5 C B 2 -14.873 1.781 -37.335 1.00 59.00 C ANISOU 613 C5 C B 2 6267 6188 9961 -1164 -355 490 C ATOM 614 C6 C B 2 -15.370 2.071 -36.126 1.00 55.94 C ANISOU 614 C6 C B 2 6042 5741 9471 -1194 -640 215 C ATOM 615 P A B 3 -16.067 2.790 -29.637 1.00 66.86 P ANISOU 615 P A B 3 8180 7235 9990 -1088 -1934 -1040 P ATOM 616 OP1 A B 3 -16.297 4.254 -29.553 1.00 66.56 O ANISOU 616 OP1 A B 3 8250 6958 10080 -1151 -1950 -1168 O ATOM 617 OP2 A B 3 -14.710 2.232 -29.421 1.00 69.75 O ANISOU 617 OP2 A B 3 8281 7704 10516 -1162 -2093 -950 O ATOM 618 O5' A B 3 -17.028 2.062 -28.599 1.00 62.12 O ANISOU 618 O5' A B 3 7858 6824 8923 -901 -1992 -1202 O ATOM 619 C5' A B 3 -18.445 2.128 -28.720 1.00 55.30 C ANISOU 619 C5' A B 3 7236 5943 7832 -771 -1813 -1257 C ATOM 620 C4' A B 3 -19.113 1.084 -27.860 1.00 46.77 C ANISOU 620 C4' A B 3 6336 5097 6336 -588 -1829 -1312 C ATOM 621 O4' A B 3 -18.978 -0.217 -28.493 1.00 45.20 O ANISOU 621 O4' A B 3 5993 5045 6137 -566 -1739 -1106 O ATOM 622 C3' A B 3 -18.524 0.934 -26.460 1.00 47.12 C ANISOU 622 C3' A B 3 6449 5286 6170 -542 -2070 -1444 C ATOM 623 O3' A B 3 -19.555 0.528 -25.564 1.00 53.38 O ANISOU 623 O3' A B 3 7506 6234 6541 -339 -2001 -1524 O ATOM 624 C2' A B 3 -17.541 -0.218 -26.635 1.00 44.64 C ANISOU 624 C2' A B 3 5899 5125 5938 -579 -2163 -1268 C ATOM 625 O2' A B 3 -17.241 -0.910 -25.441 1.00 50.49 O ANISOU 625 O2' A B 3 6713 6077 6393 -472 -2331 -1302 O ATOM 626 C1' A B 3 -18.291 -1.101 -27.625 1.00 41.77 C ANISOU 626 C1' A B 3 5514 4804 5554 -521 -1937 -1102 C ATOM 627 N9 A B 3 -17.443 -1.963 -28.447 1.00 36.74 N ANISOU 627 N9 A B 3 4588 4232 5139 -575 -1854 -860 N ATOM 628 C8 A B 3 -16.647 -1.609 -29.504 1.00 40.22 C ANISOU 628 C8 A B 3 4770 4547 5967 -723 -1786 -732 C ATOM 629 N7 A B 3 -16.031 -2.627 -30.061 1.00 39.59 N ANISOU 629 N7 A B 3 4482 4579 5981 -695 -1676 -524 N ATOM 630 C5 A B 3 -16.470 -3.722 -29.331 1.00 37.23 C ANISOU 630 C5 A B 3 4315 4469 5361 -533 -1688 -513 C ATOM 631 C6 A B 3 -16.187 -5.096 -29.420 1.00 36.90 C ANISOU 631 C6 A B 3 4176 4577 5266 -423 -1606 -340 C ATOM 632 N6 A B 3 -15.365 -5.632 -30.324 1.00 40.73 N ANISOU 632 N6 A B 3 4410 5062 6005 -443 -1482 -164 N ATOM 633 N1 A B 3 -16.792 -5.916 -28.534 1.00 45.86 N ANISOU 633 N1 A B 3 5489 5854 6081 -275 -1634 -342 N ATOM 634 C2 A B 3 -17.622 -5.384 -27.625 1.00 39.70 C ANISOU 634 C2 A B 3 4967 5093 5025 -225 -1716 -507 C ATOM 635 N3 A B 3 -17.962 -4.111 -27.438 1.00 40.76 N ANISOU 635 N3 A B 3 5228 5104 5155 -296 -1794 -706 N ATOM 636 C4 A B 3 -17.346 -3.326 -28.338 1.00 34.90 C ANISOU 636 C4 A B 3 4303 4195 4764 -459 -1786 -700 C ATOM 637 P A B 4 -19.956 1.455 -24.319 1.00 69.81 P ANISOU 637 P A B 4 9842 8295 8388 -248 -2076 -1769 P ATOM 638 OP1 A B 4 -19.555 2.848 -24.638 1.00 69.90 O ANISOU 638 OP1 A B 4 9806 8039 8712 -401 -2152 -1895 O ATOM 639 OP2 A B 4 -19.452 0.805 -23.082 1.00 74.22 O ANISOU 639 OP2 A B 4 10466 9076 8660 -165 -2260 -1802 O ATOM 640 O5' A B 4 -21.547 1.389 -24.298 1.00 49.02 O ANISOU 640 O5' A B 4 7426 5698 5503 -56 -1791 -1771 O ATOM 641 C5' A B 4 -22.323 2.091 -25.268 1.00 44.04 C ANISOU 641 C5' A B 4 6798 4871 5066 -76 -1596 -1759 C ATOM 642 C4' A B 4 -23.769 1.658 -25.246 1.00 49.01 C ANISOU 642 C4' A B 4 7573 5596 5454 124 -1327 -1701 C ATOM 643 O4' A B 4 -23.845 0.263 -25.638 1.00 50.56 O ANISOU 643 O4' A B 4 7687 5965 5559 160 -1257 -1502 O ATOM 644 C3' A B 4 -24.454 1.754 -23.887 1.00 60.41 C ANISOU 644 C3' A B 4 9243 7175 6536 321 -1273 -1819 C ATOM 645 O3' A B 4 -25.845 2.016 -24.074 1.00 60.22 O ANISOU 645 O3' A B 4 9314 7119 6448 473 -995 -1798 O ATOM 646 C2' A B 4 -24.264 0.352 -23.319 1.00 59.63 C ANISOU 646 C2' A B 4 9137 7347 6174 404 -1288 -1673 C ATOM 647 O2' A B 4 -25.213 -0.018 -22.343 1.00 64.80 O ANISOU 647 O2' A B 4 9964 8175 6484 621 -1113 -1647 O ATOM 648 C1' A B 4 -24.368 -0.514 -24.575 1.00 58.87 C ANISOU 648 C1' A B 4 8875 7248 6245 344 -1183 -1466 C ATOM 649 N9 A B 4 -23.564 -1.734 -24.500 1.00 62.56 N ANISOU 649 N9 A B 4 9231 7881 6659 314 -1302 -1319 N ATOM 650 C8 A B 4 -22.262 -1.827 -24.079 1.00 70.06 C ANISOU 650 C8 A B 4 10083 8869 7668 213 -1570 -1349 C ATOM 651 N7 A B 4 -21.779 -3.044 -24.119 1.00 72.19 N ANISOU 651 N7 A B 4 10244 9289 7895 228 -1617 -1171 N ATOM 652 C5 A B 4 -22.837 -3.801 -24.601 1.00 63.84 C ANISOU 652 C5 A B 4 9193 8284 6778 322 -1321 -988 C ATOM 653 C6 A B 4 -22.965 -5.174 -24.875 1.00 60.97 C ANISOU 653 C6 A B 4 8710 8035 6420 363 -1171 -722 C ATOM 654 N6 A B 4 -21.986 -6.066 -24.694 1.00 63.95 N ANISOU 654 N6 A B 4 8965 8508 6826 347 -1313 -599 N ATOM 655 N1 A B 4 -24.154 -5.601 -25.346 1.00 55.79 N ANISOU 655 N1 A B 4 8054 7374 5771 423 -879 -586 N ATOM 656 C2 A B 4 -25.138 -4.711 -25.530 1.00 58.62 C ANISOU 656 C2 A B 4 8508 7642 6123 456 -741 -690 C ATOM 657 N3 A B 4 -25.142 -3.399 -25.311 1.00 60.40 N ANISOU 657 N3 A B 4 8857 7756 6336 447 -834 -925 N ATOM 658 C4 A B 4 -23.945 -3.006 -24.841 1.00 61.94 C ANISOU 658 C4 A B 4 9068 7938 6529 371 -1132 -1075 C ATOM 659 P C B 5 -26.521 3.316 -23.413 1.00 91.99 P ANISOU 659 P C B 5 13515 11015 10421 578 -927 -2007 P ATOM 660 OP1 C B 5 -25.512 4.002 -22.565 1.00 91.18 O ANISOU 660 OP1 C B 5 13490 10858 10296 495 -1199 -2223 O ATOM 661 OP2 C B 5 -27.819 2.895 -22.826 1.00 94.52 O ANISOU 661 OP2 C B 5 13949 11499 10468 818 -658 -1938 O ATOM 662 O5' C B 5 -26.840 4.260 -24.655 1.00 87.58 O ANISOU 662 O5' C B 5 12868 10178 10231 488 -843 -1995 O ATOM 663 C5' C B 5 -25.808 4.970 -25.325 1.00 83.48 C ANISOU 663 C5' C B 5 12232 9442 10043 267 -1025 -2032 C ATOM 664 C4' C B 5 -26.203 5.282 -26.747 1.00 78.81 C ANISOU 664 C4' C B 5 11517 8670 9756 205 -885 -1879 C ATOM 665 O4' C B 5 -26.308 4.045 -27.502 1.00 67.86 O ANISOU 665 O4' C B 5 10013 7428 8342 202 -811 -1668 O ATOM 666 C3' C B 5 -27.564 5.943 -26.921 1.00 78.65 C ANISOU 666 C3' C B 5 11587 8550 9747 373 -651 -1885 C ATOM 667 O3' C B 5 -27.534 7.347 -26.718 1.00 83.32 O ANISOU 667 O3' C B 5 12260 8896 10502 350 -682 -2049 O ATOM 668 C2' C B 5 -27.955 5.537 -28.334 1.00 70.66 C ANISOU 668 C2' C B 5 10430 7493 8923 345 -526 -1648 C ATOM 669 O2' C B 5 -27.278 6.335 -29.293 1.00 72.93 O ANISOU 669 O2' C B 5 10612 7542 9555 168 -594 -1585 O ATOM 670 C1' C B 5 -27.391 4.117 -28.404 1.00 61.72 C ANISOU 670 C1' C B 5 9218 6580 7654 290 -597 -1540 C ATOM 671 N1 C B 5 -28.392 3.100 -28.006 1.00 50.84 N ANISOU 671 N1 C B 5 7896 5426 5994 480 -426 -1463 N ATOM 672 C2 C B 5 -29.472 2.816 -28.852 1.00 51.97 C ANISOU 672 C2 C B 5 7922 5606 6218 545 -204 -1249 C ATOM 673 O2 C B 5 -29.582 3.420 -29.930 1.00 53.61 O ANISOU 673 O2 C B 5 8040 5653 6678 478 -176 -1157 O ATOM 674 N3 C B 5 -30.379 1.885 -28.474 1.00 50.72 N ANISOU 674 N3 C B 5 7742 5658 5872 681 -33 -1132 N ATOM 675 C4 C B 5 -30.241 1.246 -27.311 1.00 52.40 C ANISOU 675 C4 C B 5 8061 6047 5800 768 -44 -1193 C ATOM 676 N4 C B 5 -31.162 0.338 -26.986 1.00 52.63 N ANISOU 676 N4 C B 5 8045 6261 5691 893 154 -1031 N ATOM 677 C5 C B 5 -29.154 1.513 -26.432 1.00 55.10 C ANISOU 677 C5 C B 5 8547 6383 6003 725 -272 -1402 C ATOM 678 C6 C B 5 -28.264 2.436 -26.817 1.00 51.78 C ANISOU 678 C6 C B 5 8100 5763 5813 560 -460 -1519 C TER 679 C B 5 HETATM 680 O HOH A 201 -18.425 -8.267 -29.237 1.00 35.97 O ANISOU 680 O HOH A 201 4383 4712 4573 -22 -1149 -69 O HETATM 681 O HOH A 202 -31.168 -6.364 -43.104 1.00 56.08 O ANISOU 681 O HOH A 202 7604 6892 6811 216 -289 53 O HETATM 682 O HOH A 203 -12.661 -13.166 -28.744 1.00 45.84 O ANISOU 682 O HOH A 203 4517 6225 6674 380 -1512 733 O HETATM 683 O HOH A 204 -18.253 -5.715 -44.477 1.00 41.80 O ANISOU 683 O HOH A 204 5097 5180 5607 218 1105 785 O HETATM 684 O HOH A 205 -32.246 -12.273 -28.769 1.00 37.70 O ANISOU 684 O HOH A 205 4947 4818 4559 428 554 781 O HETATM 685 O HOH A 206 -13.713 -4.339 -32.182 1.00 63.44 O ANISOU 685 O HOH A 206 6799 7711 9596 -700 -1322 17 O HETATM 686 O HOH A 207 -15.583 -9.467 -44.154 1.00 56.25 O ANISOU 686 O HOH A 207 6601 7143 7627 565 1354 689 O HETATM 687 O HOH A 208 -32.659 -10.538 -42.039 1.00 29.79 O ANISOU 687 O HOH A 208 4083 3420 3815 57 -542 -185 O HETATM 688 O HOH A 209 -30.690 -14.535 -29.554 1.00 31.70 O ANISOU 688 O HOH A 209 4120 3872 4053 306 376 867 O HETATM 689 O HOH A 210 -33.474 -15.943 -34.940 1.00 40.83 O ANISOU 689 O HOH A 210 4926 4437 6150 -131 -22 487 O HETATM 690 O HOH A 211 -34.471 -5.479 -29.956 1.00 43.12 O ANISOU 690 O HOH A 211 5838 5428 5116 671 620 125 O HETATM 691 O HOH A 212 -15.584 -3.634 -40.365 1.00 61.57 O ANISOU 691 O HOH A 212 6810 7354 9231 -390 518 794 O HETATM 692 O HOH A 213 -15.720 -7.106 -38.502 1.00 29.98 O ANISOU 692 O HOH A 213 2884 3595 4913 -142 237 514 O HETATM 693 O HOH A 214 -31.229 0.357 -38.905 1.00 25.52 O ANISOU 693 O HOH A 214 3722 2486 3487 261 33 142 O HETATM 694 O HOH A 215 -32.148 0.783 -36.337 1.00 18.51 O ANISOU 694 O HOH A 215 2883 1542 2606 376 100 -87 O HETATM 695 O HOH A 216 -18.419 -5.471 -36.643 1.00 23.46 O ANISOU 695 O HOH A 216 2506 2648 3759 -299 -157 187 O HETATM 696 O HOH A 217 -19.594 -12.449 -24.888 1.00 49.39 O ANISOU 696 O HOH A 217 6500 6919 5346 595 -1235 492 O HETATM 697 O HOH A 218 -36.035 -12.254 -35.381 1.00 23.40 O ANISOU 697 O HOH A 218 2563 2517 3813 -37 16 466 O HETATM 698 O HOH A 219 -20.352 -16.197 -27.371 1.00 29.84 O ANISOU 698 O HOH A 219 3758 4012 3568 659 -630 953 O HETATM 699 O HOH A 220 -33.804 -16.904 -45.903 1.00 40.65 O ANISOU 699 O HOH A 220 5829 4189 5429 -59 -1480 -1127 O HETATM 700 O HOH A 221 -17.509 -7.754 -42.932 1.00 29.57 O ANISOU 700 O HOH A 221 3388 3649 4199 249 932 583 O HETATM 701 O HOH A 222 -19.018 -14.184 -29.005 1.00 31.72 O ANISOU 701 O HOH A 222 3805 4228 4019 451 -744 602 O HETATM 702 O HOH A 223 -25.872 -20.949 -44.221 1.00 48.72 O ANISOU 702 O HOH A 223 7174 4788 6549 601 -258 -1151 O HETATM 703 O HOH A 224 -15.926 -20.566 -32.075 1.00 65.24 O ANISOU 703 O HOH A 224 7540 7812 9436 1056 -216 1061 O HETATM 704 O HOH A 225 -21.865 -16.223 -42.372 1.00 37.70 O ANISOU 704 O HOH A 225 5218 4239 4867 654 384 -344 O HETATM 705 O HOH A 226 -23.346 -14.232 -43.582 1.00 36.30 O ANISOU 705 O HOH A 226 5199 4225 4366 549 300 -371 O HETATM 706 O HOH A 227 -23.627 -10.421 -23.720 1.00 51.69 O ANISOU 706 O HOH A 227 7402 7279 4960 726 -754 235 O HETATM 707 O HOH A 228 -26.211 -20.286 -35.344 1.00 36.88 O ANISOU 707 O HOH A 228 4779 3563 5670 254 -19 350 O HETATM 708 O HOH A 229 -8.893 -16.568 -39.541 1.00 40.19 O ANISOU 708 O HOH A 229 3136 5021 7114 1268 1103 1024 O HETATM 709 O HOH A 230 -29.161 8.208 -30.765 1.00 47.47 O ANISOU 709 O HOH A 230 7404 3914 6719 347 -264 -1414 O HETATM 710 O HOH A 231 -16.186 -4.087 -38.078 1.00 39.46 O ANISOU 710 O HOH A 231 4112 4557 6323 -456 49 475 O HETATM 711 O HOH A 232 -29.290 -10.990 -47.191 1.00 53.27 O ANISOU 711 O HOH A 232 7796 6633 5812 470 -433 -485 O HETATM 712 O HOH A 233 -29.916 13.153 -32.923 1.00 48.36 O ANISOU 712 O HOH A 233 7671 2947 7756 371 -59 -1126 O HETATM 713 O HOH A 234 -24.340 -21.271 -34.309 1.00 50.75 O ANISOU 713 O HOH A 234 6478 5305 7498 442 34 557 O HETATM 714 O HOH A 235 -21.441 -14.278 -45.207 1.00 62.94 O ANISOU 714 O HOH A 235 8635 7710 7569 813 655 -354 O HETATM 715 O HOH A 236 -33.603 -16.361 -31.203 1.00 61.77 O ANISOU 715 O HOH A 236 7531 7285 8653 56 440 1048 O HETATM 716 O HOH A 237 -18.761 -14.152 -23.371 1.00 64.01 O ANISOU 716 O HOH A 237 8347 8963 7013 840 -1409 852 O HETATM 717 O HOH A 238 -32.289 1.537 -41.163 1.00 48.65 O ANISOU 717 O HOH A 238 6665 5368 6451 394 8 433 O HETATM 718 O HOH A 239 -25.257 5.894 -42.228 1.00 39.47 O ANISOU 718 O HOH A 239 5395 3337 6266 -210 392 931 O HETATM 719 O HOH A 240 -32.970 -19.173 -31.502 1.00 47.16 O ANISOU 719 O HOH A 240 5614 5042 7263 -48 364 1202 O HETATM 720 O HOH A 241 -16.815 -15.007 -28.559 1.00 39.58 O ANISOU 720 O HOH A 241 4506 5295 5236 561 -968 773 O HETATM 721 O HOH A 242 -29.557 -12.906 -22.919 1.00 57.22 O ANISOU 721 O HOH A 242 8085 7986 5671 1045 553 1131 O HETATM 722 O HOH A 243 -27.393 -8.979 -47.025 1.00 63.89 O ANISOU 722 O HOH A 243 9073 8088 7112 518 -9 -146 O HETATM 723 O HOH A 244 -31.286 -8.698 -45.624 1.00 56.82 O ANISOU 723 O HOH A 244 7930 7073 6585 307 -540 -189 O HETATM 724 O HOH A 245 -25.697 -23.098 -42.137 1.00 63.06 O ANISOU 724 O HOH A 245 8770 6164 9026 535 -238 -924 O HETATM 725 O HOH A 246 -33.604 -19.407 -47.433 1.00 66.25 O ANISOU 725 O HOH A 246 9306 7175 8689 -18 -1666 -1528 O HETATM 726 O HOH A 247 -8.567 3.343 -34.411 1.00 79.26 O ANISOU 726 O HOH A 247 7704 8553 13859 -1686 -1355 417 O HETATM 727 O HOH A 248 -17.173 -14.201 -25.359 1.00 50.19 O ANISOU 727 O HOH A 248 6164 6997 5909 665 -1426 784 O HETATM 728 O HOH A 249 -36.112 -12.472 -24.931 1.00 83.81 O ANISOU 728 O HOH A 249 10669 11016 10159 923 1537 1544 O HETATM 729 O HOH B 101 -32.291 1.574 -29.649 1.00 48.22 O ANISOU 729 O HOH B 101 7214 5378 5731 796 261 -834 O MASTER 255 0 0 1 6 0 0 6 708 2 0 8 END
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Related entries of code: 5ytx
Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code
Check Database
Protein Sequence Similarity
6a6j
RCSB PDB
PDBbind
93aa, >6A6J_1|Chains... *
5ytv
RCSB PDB
PDBbind
83aa, >5YTV_1|Chain... at 97%
5ytt
RCSB PDB
PDBbind
83aa, >5YTT_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
5ytx
Complex Type
Protein-Nucleic Acid
PDBbind Subset
general set
Protein Name
Nuclease-sensitive element-binding protein 1, YB1 cold-shock domain
Ligand Name
RNA U3A (UCAACU)
EC.Number
E.C.-.-.-.-
Resolution
1.55(Å)
Affinity (Kd/Ki/IC50)
Kd=1.34uM
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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times since Nov 2007.
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