HEADER PROTEIN TRANSPORT 21-FEB-17 5UWI

TITLE CRYSTAL STRUCTURE OF HDAC5 NES PEPTIDE IN COMPLEX WITH CRM1-RAN-RANBP1

COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GTP-BINDING NUCLEAR PROTEIN RAN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ANDROGEN RECEPTOR-ASSOCIATED PROTEIN 24, GTPASE RAN, RAS-
COMPND 5 LIKE PROTEIN TC4, RAS-RELATED NUCLEAR PROTEIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: RAN-SPECIFIC GTPASE-ACTIVATING PROTEIN 1;
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: CHROMOSOME STABILITY PROTEIN 20, PERINUCLEAR ARRAY-LOCALIZED
COMPND 11 PROTEIN, RAN-BINDING PROTEIN 1, RANBP1;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: EXPORTIN-1;
COMPND 15 CHAIN: C;
COMPND 16 SYNONYM: CHROMOSOME REGION MAINTENANCE PROTEIN 1, KARYOPHERIN-124;
COMPND 17 ENGINEERED: YES;
COMPND 18 MOL_ID: 4;
COMPND 19 MOLECULE: HISTONE DEACETYLASE 5;
COMPND 20 CHAIN: D;
COMPND 21 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: RAN, ARA24, OK/SW-CL.81;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 12 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 13 ORGANISM_TAXID: 4932;
SOURCE 14 GENE: YRB1, CST20, HTN1, SFO1, YDR002W, YD8119.08;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PGEX-4T3-TEV;
SOURCE 19 MOL_ID: 3;
SOURCE 20 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 21 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 22 ORGANISM_TAXID: 4932;
SOURCE 23 GENE: CRM1, KAP124, XPO1, YGR218W, G8514;
SOURCE 24 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 25 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 26 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 27 EXPRESSION_SYSTEM_PLASMID: PGEX-4T3-TEV;
SOURCE 28 MOL_ID: 4;
SOURCE 29 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 30 ORGANISM_COMMON: HUMAN;
SOURCE 31 ORGANISM_TAXID: 9606;
SOURCE 32 GENE: HDAC5;
SOURCE 33 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 34 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 35 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 36 EXPRESSION_SYSTEM_PLASMID: PMAL-TEV
KEYWDS HEAT REPEAT, NES, NUCLEAR EXPORT, KARYOPHERIN, PROTEIN TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR H.Y.J.FUNG,Y.M.CHOOK
REVDAT 6 04-OCT-23 5UWI 1 LINK
REVDAT 5 20-NOV-19 5UWI 1 REMARK
REVDAT 4 24-APR-19 5UWI 1 REMARK
REVDAT 3 27-SEP-17 5UWI 1 REMARK
REVDAT 2 13-SEP-17 5UWI 1 REMARK
REVDAT 1 22-MAR-17 5UWI 0
JRNL AUTH H.Y.FUNG,S.C.FU,Y.M.CHOOK
JRNL TITL NUCLEAR EXPORT RECEPTOR CRM1 RECOGNIZES DIVERSE
JRNL TITL 2 CONFORMATIONS IN NUCLEAR EXPORT SIGNALS.
JRNL REF ELIFE V. 6 2017
JRNL REFN ESSN 2050-084X
JRNL PMID 28282025
JRNL DOI 10.7554/ELIFE.23961
REMARK 2
REMARK 2 RESOLUTION. 2.14 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
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) : 2.14
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.29
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 94939
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.110
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
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 40.2968 - 5.1627 0.96 6945 149 0.1790 0.1991
REMARK 3 2 5.1627 - 4.0991 0.98 6761 146 0.1443 0.1592
REMARK 3 3 4.0991 - 3.5813 0.98 6731 145 0.1612 0.2002
REMARK 3 4 3.5813 - 3.2540 0.99 6716 145 0.1805 0.2421
REMARK 3 5 3.2540 - 3.0209 0.99 6675 143 0.1899 0.2237
REMARK 3 6 3.0209 - 2.8428 0.99 6694 144 0.1894 0.2638
REMARK 3 7 2.8428 - 2.7005 0.99 6670 144 0.1865 0.1946
REMARK 3 8 2.7005 - 2.5829 0.99 6657 143 0.1845 0.2232
REMARK 3 9 2.5829 - 2.4835 0.99 6667 144 0.1920 0.2116
REMARK 3 10 2.4835 - 2.3978 1.00 6657 143 0.1943 0.2633
REMARK 3 11 2.3978 - 2.3229 1.00 6635 142 0.2070 0.2581
REMARK 3 12 2.3229 - 2.2565 0.99 6629 143 0.2180 0.2350
REMARK 3 13 2.2565 - 2.1971 0.97 6488 140 0.2380 0.2602
REMARK 3 14 2.1971 - 2.1435 0.91 6014 129 0.2538 0.3262
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) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.110
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.31
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 : 0.002 11340
REMARK 3 ANGLE : 0.536 15368
REMARK 3 CHIRALITY : 0.038 1752
REMARK 3 PLANARITY : 0.003 1956
REMARK 3 DIHEDRAL : 15.222 6893
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 19
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 9 THROUGH 66 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.1477 48.6272 32.9569
REMARK 3 T TENSOR
REMARK 3 T11: 0.1451 T22: 0.2540
REMARK 3 T33: 0.3094 T12: -0.1128
REMARK 3 T13: 0.0838 T23: -0.1386
REMARK 3 L TENSOR
REMARK 3 L11: 0.0395 L22: 0.0473
REMARK 3 L33: 0.0141 L12: 0.0447
REMARK 3 L13: -0.0262 L23: -0.0272
REMARK 3 S TENSOR
REMARK 3 S11: 0.0512 S12: 0.0354 S13: 0.0229
REMARK 3 S21: -0.0113 S22: 0.0425 S23: -0.1313
REMARK 3 S31: -0.1214 S32: 0.1126 S33: 0.1235
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 67 THROUGH 91 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.1032 37.1923 37.1475
REMARK 3 T TENSOR
REMARK 3 T11: 0.0357 T22: 0.2263
REMARK 3 T33: 0.3491 T12: 0.0111
REMARK 3 T13: -0.0376 T23: -0.1052
REMARK 3 L TENSOR
REMARK 3 L11: 0.0070 L22: 0.0285
REMARK 3 L33: 0.0044 L12: -0.0123
REMARK 3 L13: 0.0026 L23: -0.0105
REMARK 3 S TENSOR
REMARK 3 S11: 0.0101 S12: -0.0197 S13: -0.0170
REMARK 3 S21: 0.0309 S22: -0.0012 S23: -0.1311
REMARK 3 S31: 0.0091 S32: 0.0659 S33: -0.0275
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 92 THROUGH 111 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.5689 34.0686 38.6985
REMARK 3 T TENSOR
REMARK 3 T11: 0.0589 T22: 0.1388
REMARK 3 T33: 0.2242 T12: 0.0087
REMARK 3 T13: -0.0351 T23: -0.0720
REMARK 3 L TENSOR
REMARK 3 L11: 0.0342 L22: 0.0194
REMARK 3 L33: 0.0100 L12: 0.0240
REMARK 3 L13: -0.0193 L23: -0.0135
REMARK 3 S TENSOR
REMARK 3 S11: -0.0239 S12: 0.0285 S13: -0.0969
REMARK 3 S21: -0.0123 S22: -0.0003 S23: -0.0509
REMARK 3 S31: 0.0293 S32: 0.0055 S33: -0.0732
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 112 THROUGH 132 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.2971 43.0950 34.3638
REMARK 3 T TENSOR
REMARK 3 T11: 0.0886 T22: 0.1695
REMARK 3 T33: 0.1758 T12: 0.0115
REMARK 3 T13: -0.0428 T23: -0.0530
REMARK 3 L TENSOR
REMARK 3 L11: 0.0114 L22: 0.0239
REMARK 3 L33: 0.0087 L12: 0.0059
REMARK 3 L13: -0.0106 L23: -0.0013
REMARK 3 S TENSOR
REMARK 3 S11: 0.0315 S12: 0.0303 S13: 0.0155
REMARK 3 S21: -0.0443 S22: -0.0110 S23: 0.0145
REMARK 3 S31: 0.0121 S32: -0.0651 S33: 0.0204
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 133 THROUGH 148 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.1076 42.7087 42.5137
REMARK 3 T TENSOR
REMARK 3 T11: 0.0791 T22: 0.1966
REMARK 3 T33: 0.1633 T12: 0.0083
REMARK 3 T13: -0.0341 T23: -0.0647
REMARK 3 L TENSOR
REMARK 3 L11: 0.0019 L22: 0.0063
REMARK 3 L33: 0.0221 L12: 0.0005
REMARK 3 L13: -0.0069 L23: 0.0010
REMARK 3 S TENSOR
REMARK 3 S11: 0.0370 S12: 0.0097 S13: 0.0060
REMARK 3 S21: -0.0079 S22: 0.0079 S23: 0.0114
REMARK 3 S31: 0.0295 S32: -0.0409 S33: 0.0040
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 149 THROUGH 179 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.5980 56.5677 38.9199
REMARK 3 T TENSOR
REMARK 3 T11: 0.2280 T22: 0.1786
REMARK 3 T33: 0.2414 T12: -0.0361
REMARK 3 T13: 0.0387 T23: -0.0589
REMARK 3 L TENSOR
REMARK 3 L11: 0.0101 L22: 0.0126
REMARK 3 L33: 0.0029 L12: -0.0043
REMARK 3 L13: 0.0016 L23: -0.0064
REMARK 3 S TENSOR
REMARK 3 S11: 0.1223 S12: 0.0226 S13: 0.1274
REMARK 3 S21: -0.0709 S22: -0.0011 S23: -0.0084
REMARK 3 S31: -0.1105 S32: -0.0080 S33: 0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 180 THROUGH 190 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.6676 73.7658 20.2550
REMARK 3 T TENSOR
REMARK 3 T11: 0.6177 T22: 0.7933
REMARK 3 T33: 0.6284 T12: -0.2783
REMARK 3 T13: 0.1324 T23: -0.1138
REMARK 3 L TENSOR
REMARK 3 L11: 0.0054 L22: 0.0036
REMARK 3 L33: 0.0036 L12: 0.0047
REMARK 3 L13: 0.0024 L23: 0.0027
REMARK 3 S TENSOR
REMARK 3 S11: 0.0218 S12: 0.0069 S13: 0.0053
REMARK 3 S21: 0.0078 S22: -0.0122 S23: -0.0107
REMARK 3 S31: 0.0100 S32: 0.0049 S33: 0.0000
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 191 THROUGH 206 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.5354 62.7018 4.4811
REMARK 3 T TENSOR
REMARK 3 T11: 0.5209 T22: 0.6246
REMARK 3 T33: 0.5015 T12: -0.1686
REMARK 3 T13: 0.1280 T23: -0.1199
REMARK 3 L TENSOR
REMARK 3 L11: 0.0012 L22: 0.0006
REMARK 3 L33: 0.0035 L12: 0.0005
REMARK 3 L13: -0.0015 L23: -0.0002
REMARK 3 S TENSOR
REMARK 3 S11: 0.0135 S12: 0.0016 S13: 0.0042
REMARK 3 S21: -0.0134 S22: 0.0126 S23: -0.0109
REMARK 3 S31: 0.0110 S32: -0.0102 S33: 0.0000
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 207 THROUGH 216 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.6438 56.3627 12.1647
REMARK 3 T TENSOR
REMARK 3 T11: 0.3396 T22: 0.3600
REMARK 3 T33: 0.4840 T12: -0.0941
REMARK 3 T13: 0.1262 T23: -0.1126
REMARK 3 L TENSOR
REMARK 3 L11: 0.0024 L22: 0.0024
REMARK 3 L33: 0.0013 L12: 0.0006
REMARK 3 L13: 0.0003 L23: 0.0006
REMARK 3 S TENSOR
REMARK 3 S11: -0.0021 S12: 0.0043 S13: -0.0032
REMARK 3 S21: 0.0010 S22: 0.0185 S23: -0.0001
REMARK 3 S31: -0.0009 S32: 0.0029 S33: -0.0000
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 64 THROUGH 82 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.6115 81.6931 49.5681
REMARK 3 T TENSOR
REMARK 3 T11: 0.7974 T22: 0.7595
REMARK 3 T33: 0.6902 T12: -0.1503
REMARK 3 T13: 0.0458 T23: -0.0204
REMARK 3 L TENSOR
REMARK 3 L11: 0.0084 L22: 0.0099
REMARK 3 L33: 0.0026 L12: 0.0107
REMARK 3 L13: -0.0014 L23: -0.0005
REMARK 3 S TENSOR
REMARK 3 S11: 0.0070 S12: -0.0003 S13: 0.0115
REMARK 3 S21: -0.0082 S22: 0.0044 S23: 0.0201
REMARK 3 S31: -0.0028 S32: 0.0092 S33: 0.0000
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 83 THROUGH 106 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.8231 63.1823 17.3802
REMARK 3 T TENSOR
REMARK 3 T11: 0.4453 T22: 0.3174
REMARK 3 T33: 0.4653 T12: -0.1325
REMARK 3 T13: 0.1872 T23: -0.0360
REMARK 3 L TENSOR
REMARK 3 L11: 0.0163 L22: 0.0071
REMARK 3 L33: 0.0126 L12: 0.0077
REMARK 3 L13: 0.0046 L23: -0.0046
REMARK 3 S TENSOR
REMARK 3 S11: -0.0226 S12: 0.0267 S13: 0.0099
REMARK 3 S21: 0.0549 S22: 0.0018 S23: -0.0064
REMARK 3 S31: -0.0880 S32: 0.0674 S33: 0.0000
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 107 THROUGH 133 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.5291 73.1873 25.0504
REMARK 3 T TENSOR
REMARK 3 T11: 0.5616 T22: 0.2616
REMARK 3 T33: 0.4627 T12: -0.2394
REMARK 3 T13: 0.2243 T23: -0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 0.0123 L22: 0.0158
REMARK 3 L33: 0.0019 L12: 0.0037
REMARK 3 L13: -0.0021 L23: -0.0032
REMARK 3 S TENSOR
REMARK 3 S11: -0.0343 S12: -0.0071 S13: -0.0165
REMARK 3 S21: -0.0121 S22: -0.0038 S23: 0.0153
REMARK 3 S31: -0.0639 S32: 0.0383 S33: -0.0508
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 134 THROUGH 200 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.9444 70.5532 13.1966
REMARK 3 T TENSOR
REMARK 3 T11: 0.4993 T22: 0.3392
REMARK 3 T33: 0.4595 T12: -0.2644
REMARK 3 T13: 0.1416 T23: -0.0148
REMARK 3 L TENSOR
REMARK 3 L11: 0.0052 L22: 0.0550
REMARK 3 L33: 0.0287 L12: 0.0147
REMARK 3 L13: 0.0118 L23: 0.0406
REMARK 3 S TENSOR
REMARK 3 S11: -0.0109 S12: 0.0092 S13: -0.0173
REMARK 3 S21: -0.0714 S22: -0.0009 S23: 0.0057
REMARK 3 S31: -0.2399 S32: 0.1973 S33: -0.0041
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'C' AND (RESID -1 THROUGH 245 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.1332 24.7364 52.8357
REMARK 3 T TENSOR
REMARK 3 T11: -0.1125 T22: 0.2851
REMARK 3 T33: 0.4596 T12: 0.2245
REMARK 3 T13: -0.2764 T23: -0.0464
REMARK 3 L TENSOR
REMARK 3 L11: 0.0594 L22: 0.4074
REMARK 3 L33: 0.2061 L12: 0.0094
REMARK 3 L13: 0.0271 L23: 0.2046
REMARK 3 S TENSOR
REMARK 3 S11: -0.0120 S12: -0.2363 S13: -0.1113
REMARK 3 S21: 0.4757 S22: 0.2640 S23: -0.7387
REMARK 3 S31: 0.1852 S32: 0.5787 S33: 0.6914
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 246 THROUGH 569 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.2553 52.4807 49.3027
REMARK 3 T TENSOR
REMARK 3 T11: 0.1261 T22: 0.2259
REMARK 3 T33: 0.0973 T12: 0.0212
REMARK 3 T13: 0.0157 T23: -0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 0.3096 L22: 0.3939
REMARK 3 L33: 0.6139 L12: -0.0447
REMARK 3 L13: -0.1032 L23: 0.1874
REMARK 3 S TENSOR
REMARK 3 S11: 0.0500 S12: 0.0267 S13: 0.0031
REMARK 3 S21: 0.0272 S22: 0.0224 S23: -0.0209
REMARK 3 S31: -0.1519 S32: -0.2249 S33: 0.4621
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 570 THROUGH 692 )
REMARK 3 ORIGIN FOR THE GROUP (A): -33.4897 62.7561 9.9087
REMARK 3 T TENSOR
REMARK 3 T11: 0.5091 T22: 0.4917
REMARK 3 T33: 0.1660 T12: 0.3075
REMARK 3 T13: 0.1195 T23: 0.1265
REMARK 3 L TENSOR
REMARK 3 L11: 0.1519 L22: 0.2912
REMARK 3 L33: 0.4445 L12: -0.0280
REMARK 3 L13: -0.2421 L23: 0.1247
REMARK 3 S TENSOR
REMARK 3 S11: 0.0568 S12: -0.0960 S13: 0.1764
REMARK 3 S21: -0.1048 S22: 0.1831 S23: 0.0523
REMARK 3 S31: -0.4120 S32: -0.3331 S33: 0.6405
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 693 THROUGH 897 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.7445 39.5749 0.7744
REMARK 3 T TENSOR
REMARK 3 T11: 0.1554 T22: 0.2444
REMARK 3 T33: 0.1170 T12: 0.0248
REMARK 3 T13: 0.0573 T23: -0.0197
REMARK 3 L TENSOR
REMARK 3 L11: 0.1983 L22: 0.2625
REMARK 3 L33: 0.1438 L12: -0.0613
REMARK 3 L13: 0.0905 L23: -0.0744
REMARK 3 S TENSOR
REMARK 3 S11: 0.0307 S12: 0.1552 S13: -0.0098
REMARK 3 S21: -0.0950 S22: 0.0842 S23: -0.0098
REMARK 3 S31: -0.1087 S32: -0.0315 S33: 0.4201
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 898 THROUGH 1053 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.9252 10.4271 20.5824
REMARK 3 T TENSOR
REMARK 3 T11: 0.1267 T22: 0.1648
REMARK 3 T33: 0.2842 T12: 0.0215
REMARK 3 T13: -0.0124 T23: -0.0501
REMARK 3 L TENSOR
REMARK 3 L11: 0.1743 L22: 0.3801
REMARK 3 L33: 0.1776 L12: -0.0065
REMARK 3 L13: 0.1242 L23: -0.1574
REMARK 3 S TENSOR
REMARK 3 S11: 0.0747 S12: -0.0154 S13: -0.2748
REMARK 3 S21: -0.1460 S22: 0.0634 S23: 0.1516
REMARK 3 S31: 0.1033 S32: 0.0216 S33: 0.0634
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'D' AND (RESID -1 THROUGH 1095 )
REMARK 3 ORIGIN FOR THE GROUP (A): -40.4757 74.5065 28.4898
REMARK 3 T TENSOR
REMARK 3 T11: 0.7676 T22: 0.6453
REMARK 3 T33: 0.6630 T12: 0.3073
REMARK 3 T13: 0.1438 T23: 0.0374
REMARK 3 L TENSOR
REMARK 3 L11: 0.0011 L22: 0.0016
REMARK 3 L33: 0.0001 L12: -0.0007
REMARK 3 L13: 0.0002 L23: -0.0002
REMARK 3 S TENSOR
REMARK 3 S11: -0.0030 S12: -0.0109 S13: -0.0011
REMARK 3 S21: -0.0058 S22: 0.0136 S23: 0.0022
REMARK 3 S31: -0.0086 S32: -0.0125 S33: -0.0000
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 5UWI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1000226206.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JUL-15
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 6.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 95683
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.140
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.14
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : 0.95600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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: PDB ENTRY 4HB2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 17% PEG3350, 100 MM BIS-TRIS, PH 6.4,
REMARK 280 200 MM AMMONIUM NITRATE, 10 MM SPERMINE-HCL, 16 MM HCL, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 152.36150
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 53.19550
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 53.19550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 228.54225
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 53.19550
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 53.19550
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 76.18075
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 53.19550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 53.19550
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 228.54225
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 53.19550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 53.19550
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 76.18075
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 152.36150
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 57960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH C1645 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -20
REMARK 465 GLU A -19
REMARK 465 THR A -18
REMARK 465 GLY A -17
REMARK 465 SER A -16
REMARK 465 SER A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 SER A -8
REMARK 465 SER A -7
REMARK 465 GLY A -6
REMARK 465 LEU A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 ALA A 3
REMARK 465 GLN A 4
REMARK 465 GLY A 5
REMARK 465 GLU A 6
REMARK 465 PRO A 7
REMARK 465 GLN A 8
REMARK 465 GLY B 59
REMARK 465 GLY B 60
REMARK 465 SER B 61
REMARK 465 ASP B 62
REMARK 465 ILE B 63
REMARK 465 HIS B 70
REMARK 465 LEU B 71
REMARK 465 GLU B 72
REMARK 465 LYS B 73
REMARK 465 VAL B 74
REMARK 465 ASP B 75
REMARK 465 VAL B 76
REMARK 465 LYS B 77
REMARK 465 ALA B 201
REMARK 465 GLY C -2
REMARK 465 GLU C 440
REMARK 465 ASP C 441
REMARK 465 LEU C 442
REMARK 465 VAL C 443
REMARK 465 VAL C 444
REMARK 465 GLU C 445
REMARK 465 ASN C 446
REMARK 465 ASP C 447
REMARK 465 GLU C 448
REMARK 465 GLY C 449
REMARK 465 GLU C 450
REMARK 465 ILE C 451
REMARK 465 VAL C 452
REMARK 465 ARG C 453
REMARK 465 GLU C 454
REMARK 465 PHE C 455
REMARK 465 VAL C 456
REMARK 465 ASP C 1054
REMARK 465 LYS C 1055
REMARK 465 GLU C 1056
REMARK 465 ASN C 1057
REMARK 465 ALA C 1058
REMARK 465 GLY D -3
REMARK 465 GLY D -2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD2 ASP A 107 HO1 GOL A 303 1.49
REMARK 500 O LYS C 127 HZ1 LYS C 178 1.52
REMARK 500 HH TYR C 557 O HOH C 1216 1.58
REMARK 500 OD1 ASP C 593 HE21 GLN C 640 1.59
REMARK 500 OD2 ASP A 77 O HOH A 401 2.02
REMARK 500 O HOH A 493 O HOH A 523 2.04
REMARK 500 O HOH C 1366 O HOH C 1711 2.06
REMARK 500 NE2 HIS C 585 O HOH C 1201 2.11
REMARK 500 OE1 GLU C 484 O HOH C 1202 2.13
REMARK 500 O HOH B 327 O HOH B 328 2.14
REMARK 500 O HOH C 1667 O HOH C 1678 2.15
REMARK 500 O HOH C 1251 O HOH C 1296 2.15
REMARK 500 O HOH C 1588 O HOH C 1598 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ARG A 76 -120.12 55.90
REMARK 500 ASN A 114 75.36 -151.66
REMARK 500 LYS A 123 31.25 74.97
REMARK 500 LYS B 130 -67.42 71.90
REMARK 500 ALA B 169 97.57 -59.10
REMARK 500 GLU C 2 5.17 -69.90
REMARK 500 TRP C 134 50.58 -165.38
REMARK 500 SER C 148 133.41 -171.38
REMARK 500 TRP C 223 -18.53 -142.36
REMARK 500 THR C 240 -80.54 -127.03
REMARK 500 GLU C 355 105.80 -161.98
REMARK 500 ASN C 479 88.85 -155.38
REMARK 500 ASN C 686 85.63 -151.44
REMARK 500 SER C 870 55.53 -147.65
REMARK 500 SER C 870 53.14 -146.46
REMARK 500 ASN C 969 56.43 38.96
REMARK 500 GLU D1082 74.65 49.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH C1754 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH C1755 DISTANCE = 7.04 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 24 OG1
REMARK 620 2 THR A 42 OG1 82.7
REMARK 620 3 GNP A 301 O3G 171.6 88.9
REMARK 620 4 GNP A 301 O1B 90.8 173.2 97.7
REMARK 620 5 HOH A 418 O 88.6 85.3 90.8 92.7
REMARK 620 6 HOH A 445 O 86.8 95.1 94.0 86.4 175.2
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GNP A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 1102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 1103
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5UWH RELATED DB: PDB
REMARK 900 RELATED ID: 5UWJ RELATED DB: PDB
REMARK 900 RELATED ID: 5UWU RELATED DB: PDB
REMARK 900 RELATED ID: 5UWO RELATED DB: PDB
REMARK 900 RELATED ID: 5UWP RELATED DB: PDB
REMARK 900 RELATED ID: 5UWQ RELATED DB: PDB
REMARK 900 RELATED ID: 5UWR RELATED DB: PDB
REMARK 900 RELATED ID: 5UWS RELATED DB: PDB
REMARK 900 RELATED ID: 5UWT RELATED DB: PDB
REMARK 900 RELATED ID: 5UWW RELATED DB: PDB
DBREF 5UWI A 1 216 UNP P62826 RAN_HUMAN 1 216
DBREF 5UWI B 62 201 UNP P41920 YRB1_YEAST 62 201
DBREF 5UWI C 1 376 UNP P30822 XPO1_YEAST 1 376
DBREF 5UWI C 414 1058 UNP P30822 XPO1_YEAST 414 1058
DBREF 5UWI D -3 1095 PDB 5UWI 5UWI -3 1095
SEQADV 5UWI MET A -20 UNP P62826 EXPRESSION TAG
SEQADV 5UWI GLU A -19 UNP P62826 EXPRESSION TAG
SEQADV 5UWI THR A -18 UNP P62826 EXPRESSION TAG
SEQADV 5UWI GLY A -17 UNP P62826 EXPRESSION TAG
SEQADV 5UWI SER A -16 UNP P62826 EXPRESSION TAG
SEQADV 5UWI SER A -15 UNP P62826 EXPRESSION TAG
SEQADV 5UWI HIS A -14 UNP P62826 EXPRESSION TAG
SEQADV 5UWI HIS A -13 UNP P62826 EXPRESSION TAG
SEQADV 5UWI HIS A -12 UNP P62826 EXPRESSION TAG
SEQADV 5UWI HIS A -11 UNP P62826 EXPRESSION TAG
SEQADV 5UWI HIS A -10 UNP P62826 EXPRESSION TAG
SEQADV 5UWI HIS A -9 UNP P62826 EXPRESSION TAG
SEQADV 5UWI SER A -8 UNP P62826 EXPRESSION TAG
SEQADV 5UWI SER A -7 UNP P62826 EXPRESSION TAG
SEQADV 5UWI GLY A -6 UNP P62826 EXPRESSION TAG
SEQADV 5UWI LEU A -5 UNP P62826 EXPRESSION TAG
SEQADV 5UWI PRO A -4 UNP P62826 EXPRESSION TAG
SEQADV 5UWI ARG A -3 UNP P62826 EXPRESSION TAG
SEQADV 5UWI GLY A -2 UNP P62826 EXPRESSION TAG
SEQADV 5UWI SER A -1 UNP P62826 EXPRESSION TAG
SEQADV 5UWI HIS A 0 UNP P62826 EXPRESSION TAG
SEQADV 5UWI GLY B 59 UNP P41920 EXPRESSION TAG
SEQADV 5UWI GLY B 60 UNP P41920 EXPRESSION TAG
SEQADV 5UWI SER B 61 UNP P41920 EXPRESSION TAG
SEQADV 5UWI GLY C -2 UNP P30822 EXPRESSION TAG
SEQADV 5UWI GLY C -1 UNP P30822 EXPRESSION TAG
SEQADV 5UWI SER C 0 UNP P30822 EXPRESSION TAG
SEQADV 5UWI ASP C 441 UNP P30822 VAL 441 CONFLICT
SEQADV 5UWI GLY C 537 UNP P30822 ASP 537 CONFLICT
SEQADV 5UWI CYS C 539 UNP P30822 THR 539 CONFLICT
SEQADV 5UWI GLU C 540 UNP P30822 VAL 540 CONFLICT
SEQADV 5UWI GLN C 541 UNP P30822 LYS 541 CONFLICT
SEQADV 5UWI CYS C 1022 UNP P30822 TYR 1022 CONFLICT
SEQRES 1 A 237 MET GLU THR GLY SER SER HIS HIS HIS HIS HIS HIS SER
SEQRES 2 A 237 SER GLY LEU PRO ARG GLY SER HIS MET ALA ALA GLN GLY
SEQRES 3 A 237 GLU PRO GLN VAL GLN PHE LYS LEU VAL LEU VAL GLY ASP
SEQRES 4 A 237 GLY GLY THR GLY LYS THR THR PHE VAL LYS ARG HIS LEU
SEQRES 5 A 237 THR GLY GLU PHE GLU LYS LYS TYR VAL ALA THR LEU GLY
SEQRES 6 A 237 VAL GLU VAL HIS PRO LEU VAL PHE HIS THR ASN ARG GLY
SEQRES 7 A 237 PRO ILE LYS PHE ASN VAL TRP ASP THR ALA GLY GLN GLU
SEQRES 8 A 237 LYS PHE GLY GLY LEU ARG ASP GLY TYR TYR ILE GLN ALA
SEQRES 9 A 237 GLN CYS ALA ILE ILE MET PHE ASP VAL THR SER ARG VAL
SEQRES 10 A 237 THR TYR LYS ASN VAL PRO ASN TRP HIS ARG ASP LEU VAL
SEQRES 11 A 237 ARG VAL CYS GLU ASN ILE PRO ILE VAL LEU CYS GLY ASN
SEQRES 12 A 237 LYS VAL ASP ILE LYS ASP ARG LYS VAL LYS ALA LYS SER
SEQRES 13 A 237 ILE VAL PHE HIS ARG LYS LYS ASN LEU GLN TYR TYR ASP
SEQRES 14 A 237 ILE SER ALA LYS SER ASN TYR ASN PHE GLU LYS PRO PHE
SEQRES 15 A 237 LEU TRP LEU ALA ARG LYS LEU ILE GLY ASP PRO ASN LEU
SEQRES 16 A 237 GLU PHE VAL ALA MET PRO ALA LEU ALA PRO PRO GLU VAL
SEQRES 17 A 237 VAL MET ASP PRO ALA LEU ALA ALA GLN TYR GLU HIS ASP
SEQRES 18 A 237 LEU GLU VAL ALA GLN THR THR ALA LEU PRO ASP GLU ASP
SEQRES 19 A 237 ASP ASP LEU
SEQRES 1 B 143 GLY GLY SER ASP ILE HIS PHE GLU PRO VAL VAL HIS LEU
SEQRES 2 B 143 GLU LYS VAL ASP VAL LYS THR MET GLU GLU ASP GLU GLU
SEQRES 3 B 143 VAL LEU TYR LYS VAL ARG ALA LYS LEU PHE ARG PHE ASP
SEQRES 4 B 143 ALA ASP ALA LYS GLU TRP LYS GLU ARG GLY THR GLY ASP
SEQRES 5 B 143 CYS LYS PHE LEU LYS ASN LYS LYS THR ASN LYS VAL ARG
SEQRES 6 B 143 ILE LEU MET ARG ARG ASP LYS THR LEU LYS ILE CYS ALA
SEQRES 7 B 143 ASN HIS ILE ILE ALA PRO GLU TYR THR LEU LYS PRO ASN
SEQRES 8 B 143 VAL GLY SER ASP ARG SER TRP VAL TYR ALA CYS THR ALA
SEQRES 9 B 143 ASP ILE ALA GLU GLY GLU ALA GLU ALA PHE THR PHE ALA
SEQRES 10 B 143 ILE ARG PHE GLY SER LYS GLU ASN ALA ASP LYS PHE LYS
SEQRES 11 B 143 GLU GLU PHE GLU LYS ALA GLN GLU ILE ASN LYS LYS ALA
SEQRES 1 C 1024 GLY GLY SER MET GLU GLY ILE LEU ASP PHE SER ASN ASP
SEQRES 2 C 1024 LEU ASP ILE ALA LEU LEU ASP GLN VAL VAL SER THR PHE
SEQRES 3 C 1024 TYR GLN GLY SER GLY VAL GLN GLN LYS GLN ALA GLN GLU
SEQRES 4 C 1024 ILE LEU THR LYS PHE GLN ASP ASN PRO ASP ALA TRP GLN
SEQRES 5 C 1024 LYS ALA ASP GLN ILE LEU GLN PHE SER THR ASN PRO GLN
SEQRES 6 C 1024 SER LYS PHE ILE ALA LEU SER ILE LEU ASP LYS LEU ILE
SEQRES 7 C 1024 THR ARG LYS TRP LYS LEU LEU PRO ASN ASP HIS ARG ILE
SEQRES 8 C 1024 GLY ILE ARG ASN PHE VAL VAL GLY MET ILE ILE SER MET
SEQRES 9 C 1024 CYS GLN ASP ASP GLU VAL PHE LYS THR GLN LYS ASN LEU
SEQRES 10 C 1024 ILE ASN LYS SER ASP LEU THR LEU VAL GLN ILE LEU LYS
SEQRES 11 C 1024 GLN GLU TRP PRO GLN ASN TRP PRO GLU PHE ILE PRO GLU
SEQRES 12 C 1024 LEU ILE GLY SER SER SER SER SER VAL ASN VAL CYS GLU
SEQRES 13 C 1024 ASN ASN MET ILE VAL LEU LYS LEU LEU SER GLU GLU VAL
SEQRES 14 C 1024 PHE ASP PHE SER ALA GLU GLN MET THR GLN ALA LYS ALA
SEQRES 15 C 1024 LEU HIS LEU LYS ASN SER MET SER LYS GLU PHE GLU GLN
SEQRES 16 C 1024 ILE PHE LYS LEU CYS PHE GLN VAL LEU GLU GLN GLY SER
SEQRES 17 C 1024 SER SER SER LEU ILE VAL ALA THR LEU GLU SER LEU LEU
SEQRES 18 C 1024 ARG TYR LEU HIS TRP ILE PRO TYR ARG TYR ILE TYR GLU
SEQRES 19 C 1024 THR ASN ILE LEU GLU LEU LEU SER THR LYS PHE MET THR
SEQRES 20 C 1024 SER PRO ASP THR ARG ALA ILE THR LEU LYS CYS LEU THR
SEQRES 21 C 1024 GLU VAL SER ASN LEU LYS ILE PRO GLN ASP ASN ASP LEU
SEQRES 22 C 1024 ILE LYS ARG GLN THR VAL LEU PHE PHE GLN ASN THR LEU
SEQRES 23 C 1024 GLN GLN ILE ALA THR SER VAL MET PRO VAL THR ALA ASP
SEQRES 24 C 1024 LEU LYS ALA THR TYR ALA ASN ALA ASN GLY ASN ASP GLN
SEQRES 25 C 1024 SER PHE LEU GLN ASP LEU ALA MET PHE LEU THR THR TYR
SEQRES 26 C 1024 LEU ALA ARG ASN ARG ALA LEU LEU GLU SER ASP GLU SER
SEQRES 27 C 1024 LEU ARG GLU LEU LEU LEU ASN ALA HIS GLN TYR LEU ILE
SEQRES 28 C 1024 GLN LEU SER LYS ILE GLU GLU ARG GLU LEU PHE LYS THR
SEQRES 29 C 1024 THR LEU ASP TYR TRP HIS ASN LEU VAL ALA ASP LEU PHE
SEQRES 30 C 1024 TYR GLU PRO LEU LYS LYS HIS ILE TYR GLU GLU ILE CYS
SEQRES 31 C 1024 SER GLN LEU ARG LEU VAL ILE ILE GLU ASN MET VAL ARG
SEQRES 32 C 1024 PRO GLU GLU ASP LEU VAL VAL GLU ASN ASP GLU GLY GLU
SEQRES 33 C 1024 ILE VAL ARG GLU PHE VAL LYS GLU SER ASP THR ILE GLN
SEQRES 34 C 1024 LEU TYR LYS SER GLU ARG GLU VAL LEU VAL TYR LEU THR
SEQRES 35 C 1024 HIS LEU ASN VAL ILE ASP THR GLU GLU ILE MET ILE SER
SEQRES 36 C 1024 LYS LEU ALA ARG GLN ILE ASP GLY SER GLU TRP SER TRP
SEQRES 37 C 1024 HIS ASN ILE ASN THR LEU SER TRP ALA ILE GLY SER ILE
SEQRES 38 C 1024 SER GLY THR MET SER GLU ASP THR GLU LYS ARG PHE VAL
SEQRES 39 C 1024 VAL THR VAL ILE LYS ASP LEU LEU GLY LEU CYS GLU GLN
SEQRES 40 C 1024 LYS ARG GLY LYS ASP ASN LYS ALA VAL VAL ALA SER ASP
SEQRES 41 C 1024 ILE MET TYR VAL VAL GLY GLN TYR PRO ARG PHE LEU LYS
SEQRES 42 C 1024 ALA HIS TRP ASN PHE LEU ARG THR VAL ILE LEU LYS LEU
SEQRES 43 C 1024 PHE GLU PHE MET HIS GLU THR HIS GLU GLY VAL GLN ASP
SEQRES 44 C 1024 MET ALA CYS ASP THR PHE ILE LYS ILE VAL GLN LYS CYS
SEQRES 45 C 1024 LYS TYR HIS PHE VAL ILE GLN GLN PRO ARG GLU SER GLU
SEQRES 46 C 1024 PRO PHE ILE GLN THR ILE ILE ARG ASP ILE GLN LYS THR
SEQRES 47 C 1024 THR ALA ASP LEU GLN PRO GLN GLN VAL HIS THR PHE TYR
SEQRES 48 C 1024 LYS ALA CYS GLY ILE ILE ILE SER GLU GLU ARG SER VAL
SEQRES 49 C 1024 ALA GLU ARG ASN ARG LEU LEU SER ASP LEU MET GLN LEU
SEQRES 50 C 1024 PRO ASN MET ALA TRP ASP THR ILE VAL GLU GLN SER THR
SEQRES 51 C 1024 ALA ASN PRO THR LEU LEU LEU ASP SER GLU THR VAL LYS
SEQRES 52 C 1024 ILE ILE ALA ASN ILE ILE LYS THR ASN VAL ALA VAL CYS
SEQRES 53 C 1024 THR SER MET GLY ALA ASP PHE TYR PRO GLN LEU GLY HIS
SEQRES 54 C 1024 ILE TYR TYR ASN MET LEU GLN LEU TYR ARG ALA VAL SER
SEQRES 55 C 1024 SER MET ILE SER ALA GLN VAL ALA ALA GLU GLY LEU ILE
SEQRES 56 C 1024 ALA THR LYS THR PRO LYS VAL ARG GLY LEU ARG THR ILE
SEQRES 57 C 1024 LYS LYS GLU ILE LEU LYS LEU VAL GLU THR TYR ILE SER
SEQRES 58 C 1024 LYS ALA ARG ASN LEU ASP ASP VAL VAL LYS VAL LEU VAL
SEQRES 59 C 1024 GLU PRO LEU LEU ASN ALA VAL LEU GLU ASP TYR MET ASN
SEQRES 60 C 1024 ASN VAL PRO ASP ALA ARG ASP ALA GLU VAL LEU ASN CYS
SEQRES 61 C 1024 MET THR THR VAL VAL GLU LYS VAL GLY HIS MET ILE PRO
SEQRES 62 C 1024 GLN GLY VAL ILE LEU ILE LEU GLN SER VAL PHE GLU CYS
SEQRES 63 C 1024 THR LEU ASP MET ILE ASN LYS ASP PHE THR GLU TYR PRO
SEQRES 64 C 1024 GLU HIS ARG VAL GLU PHE TYR LYS LEU LEU LYS VAL ILE
SEQRES 65 C 1024 ASN GLU LYS SER PHE ALA ALA PHE LEU GLU LEU PRO PRO
SEQRES 66 C 1024 ALA ALA PHE LYS LEU PHE VAL ASP ALA ILE CYS TRP ALA
SEQRES 67 C 1024 PHE LYS HIS ASN ASN ARG ASP VAL GLU VAL ASN GLY LEU
SEQRES 68 C 1024 GLN ILE ALA LEU ASP LEU VAL LYS ASN ILE GLU ARG MET
SEQRES 69 C 1024 GLY ASN VAL PRO PHE ALA ASN GLU PHE HIS LYS ASN TYR
SEQRES 70 C 1024 PHE PHE ILE PHE VAL SER GLU THR PHE PHE VAL LEU THR
SEQRES 71 C 1024 ASP SER ASP HIS LYS SER GLY PHE SER LYS GLN ALA LEU
SEQRES 72 C 1024 LEU LEU MET LYS LEU ILE SER LEU VAL TYR ASP ASN LYS
SEQRES 73 C 1024 ILE SER VAL PRO LEU TYR GLN GLU ALA GLU VAL PRO GLN
SEQRES 74 C 1024 GLY THR SER ASN GLN VAL TYR LEU SER GLN TYR LEU ALA
SEQRES 75 C 1024 ASN MET LEU SER ASN ALA PHE PRO HIS LEU THR SER GLU
SEQRES 76 C 1024 GLN ILE ALA SER PHE LEU SER ALA LEU THR LYS GLN CYS
SEQRES 77 C 1024 LYS ASP LEU VAL VAL PHE LYS GLY THR LEU ARG ASP PHE
SEQRES 78 C 1024 LEU VAL GLN ILE LYS GLU VAL GLY GLY ASP PRO THR ASP
SEQRES 79 C 1024 TYR LEU PHE ALA GLU ASP LYS GLU ASN ALA
SEQRES 1 D 18 GLY GLY SER TYR GLU ALA GLU THR VAL SER ALA MET ALA
SEQRES 2 D 18 LEU LEU SER VAL GLY
HET GNP A 301 44
HET MG A 302 1
HET GOL A 303 14
HET GOL C1101 14
HET GOL C1102 14
HET GOL C1103 14
HETNAM GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER
HETNAM MG MAGNESIUM ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 GNP C10 H17 N6 O13 P3
FORMUL 6 MG MG 2+
FORMUL 7 GOL 4(C3 H8 O3)
FORMUL 11 HOH *735(H2 O)
HELIX 1 AA1 GLY A 22 GLY A 33 1 12
HELIX 2 AA2 GLN A 69 GLY A 73 5 5
HELIX 3 AA3 LEU A 75 ILE A 81 5 7
HELIX 4 AA4 SER A 94 ASN A 100 1 7
HELIX 5 AA5 ASN A 100 CYS A 112 1 13
HELIX 6 AA6 LYS A 132 ILE A 136 5 5
HELIX 7 AA7 PHE A 138 ASN A 143 1 6
HELIX 8 AA8 GLU A 158 GLY A 170 1 13
HELIX 9 AA9 ASP A 190 ALA A 192 5 3
HELIX 10 AB1 LEU A 193 THR A 206 1 14
HELIX 11 AB2 SER B 180 LYS B 199 1 20
HELIX 12 AB3 SER C 0 ASP C 6 5 7
HELIX 13 AB4 ASP C 12 GLY C 26 1 15
HELIX 14 AB5 SER C 27 ASN C 44 1 18
HELIX 15 AB6 ASP C 46 GLN C 49 5 4
HELIX 16 AB7 LYS C 50 SER C 58 1 9
HELIX 17 AB8 ASN C 60 TRP C 79 1 20
HELIX 18 AB9 LYS C 80 LEU C 82 5 3
HELIX 19 AC1 PRO C 83 ASP C 104 1 22
HELIX 20 AC2 ASP C 104 GLN C 111 1 8
HELIX 21 AC3 GLN C 111 TRP C 130 1 20
HELIX 22 AC4 GLU C 136 SER C 146 1 11
HELIX 23 AC5 SER C 148 ASP C 168 1 21
HELIX 24 AC6 PHE C 169 MET C 174 1 6
HELIX 25 AC7 THR C 175 GLU C 189 1 15
HELIX 26 AC8 GLU C 189 GLY C 204 1 16
HELIX 27 AC9 SER C 206 LEU C 221 1 16
HELIX 28 AD1 TYR C 226 GLU C 231 1 6
HELIX 29 AD2 ASN C 233 THR C 240 1 8
HELIX 30 AD3 THR C 240 SER C 245 1 6
HELIX 31 AD4 SER C 245 SER C 260 1 16
HELIX 32 AD5 ASN C 268 VAL C 290 1 23
HELIX 33 AD6 ASP C 296 ALA C 304 1 9
HELIX 34 AD7 ASN C 307 ARG C 327 1 21
HELIX 35 AD8 ARG C 327 SER C 332 1 6
HELIX 36 AD9 ASP C 333 SER C 335 5 3
HELIX 37 AE1 LEU C 336 SER C 351 1 16
HELIX 38 AE2 GLU C 355 GLU C 376 1 22
HELIX 39 AE3 LYS C 416 ILE C 419 5 4
HELIX 40 AE4 TYR C 420 ASN C 434 1 15
HELIX 41 AE5 GLU C 458 ASN C 479 1 22
HELIX 42 AE6 ASN C 479 ASP C 496 1 18
HELIX 43 AE7 SER C 501 ILE C 515 1 15
HELIX 44 AE8 SER C 520 LYS C 542 1 23
HELIX 45 AE9 ARG C 543 TYR C 562 1 20
HELIX 46 AF1 TYR C 562 HIS C 569 1 8
HELIX 47 AF2 HIS C 569 MET C 584 1 16
HELIX 48 AF3 GLY C 590 LYS C 607 1 18
HELIX 49 AF4 LYS C 607 ILE C 612 1 6
HELIX 50 AF5 PRO C 620 ASP C 628 1 9
HELIX 51 AF6 ASP C 628 ALA C 634 1 7
HELIX 52 AF7 GLN C 637 GLU C 654 1 18
HELIX 53 AF8 SER C 657 MET C 669 1 13
HELIX 54 AF9 MET C 669 ASN C 686 1 18
HELIX 55 AG1 PRO C 687 LEU C 691 5 5
HELIX 56 AG2 ASP C 692 GLY C 714 1 23
HELIX 57 AG3 PHE C 717 GLY C 747 1 31
HELIX 58 AG4 LEU C 748 LYS C 752 5 5
HELIX 59 AG5 THR C 753 ALA C 777 1 25
HELIX 60 AG6 ASN C 779 LEU C 787 1 9
HELIX 61 AG7 LEU C 787 ASN C 802 1 16
HELIX 62 AG8 VAL C 803 ARG C 807 5 5
HELIX 63 AG9 ASP C 808 GLY C 823 1 16
HELIX 64 AH1 ILE C 826 ASN C 846 1 21
HELIX 65 AH2 TYR C 852 SER C 870 1 19
HELIX 66 AH3 PHE C 871 GLU C 876 1 6
HELIX 67 AH4 PRO C 878 LYS C 894 1 17
HELIX 68 AH5 ASN C 897 MET C 918 1 22
HELIX 69 AH6 VAL C 921 ASP C 945 1 25
HELIX 70 AH7 HIS C 948 SER C 950 5 3
HELIX 71 AH8 GLY C 951 ASP C 968 1 18
HELIX 72 AH9 SER C 986 PHE C 1003 1 18
HELIX 73 AI1 THR C 1007 GLN C 1021 1 15
HELIX 74 AI2 ASP C 1024 ILE C 1039 1 16
HELIX 75 AI3 ASP C 1045 PHE C 1051 5 7
HELIX 76 AI4 GLU D 1082 LEU D 1091 1 10
SHEET 1 AA1 6 VAL A 45 THR A 54 0
SHEET 2 AA1 6 GLY A 57 THR A 66 -1 O PHE A 61 N LEU A 50
SHEET 3 AA1 6 GLN A 10 GLY A 17 1 N LEU A 13 O TRP A 64
SHEET 4 AA1 6 CYS A 85 ASP A 91 1 O MET A 89 N VAL A 16
SHEET 5 AA1 6 ILE A 117 ASN A 122 1 O CYS A 120 N ILE A 88
SHEET 6 AA1 6 GLN A 145 ASP A 148 1 O GLN A 145 N LEU A 119
SHEET 1 AA2 6 ILE B 134 ILE B 139 0
SHEET 2 AA2 6 VAL B 122 ARG B 127 -1 N ILE B 124 O HIS B 138
SHEET 3 AA2 6 GLU B 102 ASN B 116 -1 N LYS B 112 O LEU B 125
SHEET 4 AA2 6 GLU B 83 ASP B 97 -1 N VAL B 89 O CYS B 111
SHEET 5 AA2 6 GLU B 170 ARG B 177 -1 O ALA B 175 N PHE B 94
SHEET 6 AA2 6 SER B 155 ASP B 163 -1 N CYS B 160 O PHE B 172
LINK OG1 THR A 24 MG MG A 302 1555 1555 2.04
LINK OG1 THR A 42 MG MG A 302 1555 1555 2.13
LINK O3G GNP A 301 MG MG A 302 1555 1555 1.97
LINK O1B GNP A 301 MG MG A 302 1555 1555 2.08
LINK MG MG A 302 O HOH A 418 1555 1555 2.08
LINK MG MG A 302 O HOH A 445 1555 1555 2.06
CISPEP 1 TRP C 130 PRO C 131 0 -2.82
SITE 1 AC1 26 GLY A 19 GLY A 20 THR A 21 GLY A 22
SITE 2 AC1 26 LYS A 23 THR A 24 THR A 25 PHE A 35
SITE 3 AC1 26 GLU A 36 LYS A 37 TYR A 39 THR A 42
SITE 4 AC1 26 GLY A 68 ASN A 122 LYS A 123 ASP A 125
SITE 5 AC1 26 ILE A 126 SER A 150 ALA A 151 LYS A 152
SITE 6 AC1 26 MG A 302 HOH A 402 HOH A 418 HOH A 435
SITE 7 AC1 26 HOH A 442 HOH A 445
SITE 1 AC2 5 THR A 24 THR A 42 GNP A 301 HOH A 418
SITE 2 AC2 5 HOH A 445
SITE 1 AC3 4 ASN A 103 TRP A 104 ASP A 107 HOH A 466
SITE 1 AC4 5 ARG C 77 HIS C1005 ILE C1039 LYS C1040
SITE 2 AC4 5 GLU C1041
SITE 1 AC5 3 GLU C 191 ARG C 227 GLU C 231
SITE 1 AC6 3 ASN C 846 ASP C 887 TRP C 891
CRYST1 106.391 106.391 304.723 90.00 90.00 90.00 P 43 21 2 8
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 0.009399 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009399 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003282 0.00000
ATOM 21983 N SER D -1 -52.530 65.099 30.881 1.00102.32 N
ANISOU21983 N SER D -1 13667 12540 12669 3077 1414 444 N
ATOM 21984 CA SER D -1 -52.404 66.556 31.172 1.00102.84 C
ANISOU21984 CA SER D -1 13737 12606 12733 3081 1416 440 C
ATOM 21985 C SER D -1 -51.375 67.192 30.238 1.00103.55 C
ANISOU21985 C SER D -1 13832 12689 12824 3078 1418 434 C
ATOM 21986 O SER D -1 -50.865 66.531 29.333 1.00103.42 O
ANISOU21986 O SER D -1 13818 12670 12809 3073 1417 433 O
ATOM 21987 CB SER D -1 -52.025 66.776 32.639 1.00102.67 C
ANISOU21987 CB SER D -1 13712 12588 12711 3085 1417 439 C
ATOM 21988 OG SER D -1 -53.143 66.555 33.482 1.00102.48 O
ANISOU21988 OG SER D -1 13683 12569 12685 3089 1416 444 O
ATOM 21989 H SER D -1 -53.181 64.970 30.287 1.00122.80 H
ATOM 21990 HA SER D -1 -53.259 66.986 31.014 1.00123.44 H
ATOM 21991 HB2 SER D -1 -51.320 66.156 32.880 1.00123.23 H
ATOM 21992 HB3 SER D -1 -51.719 67.689 32.753 1.00123.23 H
ATOM 21993 HG SER D -1 -52.927 66.677 34.284 1.00123.00 H
ATOM 21994 N TYR D 0 -51.071 68.471 30.457 1.00104.15 N
ANISOU21994 N TYR D 0 13911 12764 12898 3081 1420 431 N
ATOM 21995 CA TYR D 0 -50.272 69.242 29.511 1.00104.44 C
ANISOU21995 CA TYR D 0 13953 12796 12935 3079 1421 426 C
ATOM 21996 C TYR D 0 -48.999 69.810 30.118 1.00 97.48 C
ANISOU21996 C TYR D 0 13074 11912 12054 3080 1423 419 C
ATOM 21997 O TYR D 0 -47.929 69.693 29.508 1.00 99.40 O
ANISOU21997 O TYR D 0 13320 12150 12298 3076 1424 415 O
ATOM 21998 CB TYR D 0 -51.131 70.380 28.920 1.00110.96 C
ANISOU21998 CB TYR D 0 14781 13620 13759 3081 1421 427 C
ATOM 21999 CG TYR D 0 -52.099 69.944 27.830 1.00117.50 C
ANISOU21999 CG TYR D 0 15610 14448 14588 3078 1419 432 C
ATOM 22000 CD1 TYR D 0 -51.804 68.874 26.992 1.00120.77 C
ANISOU22000 CD1 TYR D 0 16025 14860 15004 3073 1418 432 C
ATOM 22001 CD2 TYR D 0 -53.305 70.608 27.638 1.00120.64 C
ANISOU22001 CD2 TYR D 0 16008 14848 14984 3081 1419 436 C
ATOM 22002 CE1 TYR D 0 -52.679 68.477 26.001 1.00123.93 C
ANISOU22002 CE1 TYR D 0 16424 15258 15404 3070 1416 437 C
ATOM 22003 CE2 TYR D 0 -54.188 70.216 26.646 1.00123.82 C
ANISOU22003 CE2 TYR D 0 16410 15249 15386 3078 1417 440 C
ATOM 22004 CZ TYR D 0 -53.868 69.150 25.831 1.00126.24 C
ANISOU22004 CZ TYR D 0 16716 15553 15694 3073 1416 440 C
ATOM 22005 OH TYR D 0 -54.737 68.751 24.841 1.00129.09 O
ANISOU22005 OH TYR D 0 17078 15913 16056 3071 1414 444 O
ATOM 22006 H TYR D 0 -51.318 68.916 31.151 1.00125.01 H
ATOM 22007 HA TYR D 0 -50.013 68.660 28.780 1.00125.36 H
ATOM 22008 HB2 TYR D 0 -51.653 70.777 29.634 1.00133.18 H
ATOM 22009 HB3 TYR D 0 -50.540 71.047 28.538 1.00133.18 H
ATOM 22010 HD1 TYR D 0 -51.003 68.416 27.102 1.00144.95 H
ATOM 22011 HD2 TYR D 0 -53.524 71.327 28.186 1.00144.80 H
ATOM 22012 HE1 TYR D 0 -52.465 67.759 25.450 1.00148.74 H
ATOM 22013 HE2 TYR D 0 -54.992 70.668 26.529 1.00148.61 H
ATOM 22014 HH TYR D 0 -55.420 69.240 24.844 1.00154.93 H
ATOM 22015 N GLU D1082 -49.071 70.421 31.298 1.00 88.16 N
ANISOU22015 N GLU D1082 11891 10735 10872 3085 1425 419 N
ATOM 22016 CA GLU D1082 -47.917 71.086 31.902 1.00 79.64 C
ANISOU22016 CA GLU D1082 10813 9654 9792 3086 1427 413 C
ATOM 22017 C GLU D1082 -47.242 72.014 30.886 1.00 73.35 C
ANISOU22017 C GLU D1082 10022 8851 8995 3084 1428 408 C
ATOM 22018 O GLU D1082 -46.173 71.734 30.341 1.00 72.08 O
ANISOU22018 O GLU D1082 9865 8686 8836 3080 1429 404 O
ATOM 22019 CB GLU D1082 -46.922 70.059 32.455 1.00 78.30 C
ANISOU22019 CB GLU D1082 10641 9484 9624 3084 1427 411 C
ATOM 22020 CG GLU D1082 -47.212 69.604 33.883 1.00 78.42 C
ANISOU22020 CG GLU D1082 10652 9505 9639 3088 1427 413 C
ATOM 22021 CD GLU D1082 -47.826 68.218 33.955 1.00 79.83 C
ANISOU22021 CD GLU D1082 10826 9687 9819 3086 1424 418 C
ATOM 22022 OE1 GLU D1082 -48.400 67.759 32.944 1.00 80.34 O
ANISOU22022 OE1 GLU D1082 10892 9750 9884 3083 1423 421 O
ATOM 22023 OE2 GLU D1082 -47.730 67.583 35.027 1.00 80.44 O
ANISOU22023 OE2 GLU D1082 10899 9767 9896 3087 1424 419 O
ATOM 22024 H GLU D1082 -49.786 70.466 31.775 1.00105.82 H
ATOM 22025 HA GLU D1082 -48.223 71.631 32.644 1.00 95.59 H
ATOM 22026 HB2 GLU D1082 -46.940 69.273 31.887 1.00 93.98 H
ATOM 22027 HB3 GLU D1082 -46.035 70.449 32.445 1.00 93.98 H
ATOM 22028 HG2 GLU D1082 -46.381 69.589 34.383 1.00 94.13 H
ATOM 22029 HG3 GLU D1082 -47.833 70.227 34.292 1.00 94.13 H
ATOM 22030 N ALA D1083 -47.912 73.144 30.651 1.00 69.22 N
ANISOU22030 N ALA D1083 9501 8328 8470 3087 1429 409 N
ATOM 22031 CA ALA D1083 -47.492 74.072 29.609 1.00 65.83 C
ANISOU22031 CA ALA D1083 9078 7894 8041 3085 1430 405 C
ATOM 22032 C ALA D1083 -46.351 74.983 30.040 1.00 63.47 C
ANISOU22032 C ALA D1083 8782 7593 7742 3087 1433 398 C
ATOM 22033 O ALA D1083 -45.663 75.537 29.175 1.00 61.80 O
ANISOU22033 O ALA D1083 8575 7376 7531 3085 1434 394 O
ATOM 22034 CB ALA D1083 -48.682 74.922 29.158 1.00 65.65 C
ANISOU22034 CB ALA D1083 9056 7872 8016 3088 1430 408 C
ATOM 22035 H ALA D1083 -48.613 73.393 31.083 1.00 83.09 H
ATOM 22036 HA ALA D1083 -47.187 73.561 28.843 1.00 79.02 H
ATOM 22037 HB1 ALA D1083 -48.388 75.534 28.466 1.00 78.80 H
ATOM 22038 HB2 ALA D1083 -49.374 74.337 28.811 1.00 78.80 H
ATOM 22039 HB3 ALA D1083 -49.020 75.420 29.919 1.00 78.80 H
ATOM 22040 N GLU D1084 -46.133 75.164 31.345 1.00 63.41 N
ANISOU22040 N GLU D1084 8771 7588 7733 3091 1434 397 N
ATOM 22041 CA GLU D1084 -45.017 75.993 31.788 1.00 65.38 C
ANISOU22041 CA GLU D1084 9023 7835 7982 3092 1436 391 C
ATOM 22042 C GLU D1084 -43.691 75.255 31.675 1.00 62.02 C
ANISOU22042 C GLU D1084 8599 7407 7559 3088 1437 387 C
ATOM 22043 O GLU D1084 -42.665 75.878 31.376 1.00 60.10 O
ANISOU22043 O GLU D1084 8360 7160 7316 3087 1438 381 O
ATOM 22044 CB GLU D1084 -45.232 76.463 33.227 1.00 71.51 C
ANISOU22044 CB GLU D1084 9797 8617 8757 3098 1437 391 C
ATOM 22045 CG GLU D1084 -44.239 77.533 33.664 1.00 77.61 C
ANISOU22045 CG GLU D1084 10572 9388 9529 3100 1440 385 C
ATOM 22046 CD GLU D1084 -44.389 77.918 35.123 1.00 83.60 C
ANISOU22046 CD GLU D1084 11328 10151 10287 3105 1441 385 C
ATOM 22047 OE1 GLU D1084 -45.531 77.904 35.630 1.00 85.56 O
ANISOU22047 OE1 GLU D1084 11572 10403 10533 3108 1440 390 O
ATOM 22048 OE2 GLU D1084 -43.360 78.230 35.762 1.00 85.38 O
ANISOU22048 OE2 GLU D1084 11554 10375 10512 3106 1442 381 O
ATOM 22049 H GLU D1084 -46.606 74.824 31.979 1.00 76.11 H
ATOM 22050 HA GLU D1084 -44.969 76.779 31.222 1.00 78.48 H
ATOM 22051 HB2 GLU D1084 -46.125 76.834 33.306 1.00 85.84 H
ATOM 22052 HB3 GLU D1084 -45.135 75.705 33.823 1.00 85.84 H
ATOM 22053 HG2 GLU D1084 -43.337 77.199 33.534 1.00 93.16 H
ATOM 22054 HG3 GLU D1084 -44.377 78.330 33.129 1.00 93.16 H
ATOM 22055 N THR D1085 -43.684 73.943 31.918 1.00 62.52 N
ANISOU22055 N THR D1085 8658 7472 7624 3086 1435 389 N
ATOM 22056 CA THR D1085 -42.496 73.147 31.629 1.00 61.92 C
ANISOU22056 CA THR D1085 8583 7392 7550 3082 1435 386 C
ATOM 22057 C THR D1085 -42.101 73.296 30.167 1.00 59.84 C
ANISOU22057 C THR D1085 8325 7123 7288 3077 1435 384 C
ATOM 22058 O THR D1085 -40.944 73.595 29.847 1.00 57.96 O
ANISOU22058 O THR D1085 8090 6881 7051 3075 1436 378 O
ATOM 22059 CB THR D1085 -42.753 71.677 31.966 1.00 63.39 C
ANISOU22059 CB THR D1085 8766 7582 7738 3080 1433 390 C
ATOM 22060 OG1 THR D1085 -43.213 71.563 33.318 1.00 65.19 O
ANISOU22060 OG1 THR D1085 8988 7815 7964 3084 1433 392 O
ATOM 22061 CG2 THR D1085 -41.481 70.852 31.797 1.00 62.41 C
ANISOU22061 CG2 THR D1085 8642 7454 7616 3076 1433 386 C
ATOM 22062 H THR D1085 -44.344 73.498 32.244 1.00 75.05 H
ATOM 22063 HA THR D1085 -41.760 73.461 32.177 1.00 74.32 H
ATOM 22064 HB THR D1085 -43.428 71.323 31.367 1.00 76.10 H
ATOM 22065 HG1 THR D1085 -43.355 70.757 33.507 1.00 78.25 H
ATOM 22066 HG21 THR D1085 -41.657 69.923 32.014 1.00 74.91 H
ATOM 22067 HG22 THR D1085 -41.169 70.908 30.880 1.00 74.91 H
ATOM 22068 HG23 THR D1085 -40.788 71.187 32.387 1.00 74.91 H
ATOM 22069 N VAL D1086 -43.062 73.096 29.262 1.00 59.76 N
ANISOU22069 N VAL D1086 8316 7113 7278 3076 1433 388 N
ATOM 22070 CA VAL D1086 -42.802 73.244 27.832 1.00 59.20 C
ANISOU22070 CA VAL D1086 8249 7037 7208 3071 1433 386 C
ATOM 22071 C VAL D1086 -42.231 74.625 27.539 1.00 57.51 C
ANISOU22071 C VAL D1086 8040 6820 6993 3073 1436 381 C
ATOM 22072 O VAL D1086 -41.195 74.763 26.877 1.00 57.20 O
ANISOU22072 O VAL D1086 8005 6775 6955 3069 1437 376 O
ATOM 22073 CB VAL D1086 -44.090 72.986 27.030 1.00 60.05 C
ANISOU22073 CB VAL D1086 8356 7145 7315 3070 1431 392 C
ATOM 22074 CG1 VAL D1086 -43.874 73.269 25.547 1.00 60.59 C
ANISOU22074 CG1 VAL D1086 8429 7208 7384 3066 1431 390 C
ATOM 22075 CG2 VAL D1086 -44.561 71.552 27.240 1.00 58.92 C
ANISOU22075 CG2 VAL D1086 8208 7005 7173 3069 1429 397 C
ATOM 22076 H VAL D1086 -43.871 72.874 29.452 1.00 71.74 H
ATOM 22077 HA VAL D1086 -42.144 72.585 27.561 1.00 71.07 H
ATOM 22078 HB VAL D1086 -44.787 73.580 27.350 1.00 72.08 H
ATOM 22079 HG11 VAL D1086 -44.701 73.098 25.069 1.00 72.73 H
ATOM 22080 HG12 VAL D1086 -43.615 74.197 25.437 1.00 72.73 H
ATOM 22081 HG13 VAL D1086 -43.173 72.687 25.213 1.00 72.73 H
ATOM 22082 HG21 VAL D1086 -45.372 71.408 26.728 1.00 70.73 H
ATOM 22083 HG22 VAL D1086 -43.867 70.945 26.939 1.00 70.73 H
ATOM 22084 HG23 VAL D1086 -44.736 71.413 28.184 1.00 70.73 H
ATOM 22085 N SER D1087 -42.908 75.671 28.020 1.00 55.35 N
ANISOU22085 N SER D1087 7765 6548 6716 3077 1436 382 N
ATOM 22086 CA SER D1087 -42.454 77.032 27.759 1.00 54.68 C
ANISOU22086 CA SER D1087 7685 6459 6630 3079 1439 378 C
ATOM 22087 C SER D1087 -41.002 77.214 28.179 1.00 54.66 C
ANISOU22087 C SER D1087 7684 6454 6629 3078 1440 371 C
ATOM 22088 O SER D1087 -40.158 77.626 27.376 1.00 54.65 O
ANISOU22088 O SER D1087 7687 6448 6628 3076 1442 367 O
ATOM 22089 CB SER D1087 -43.356 78.035 28.482 1.00 54.79 C
ANISOU22089 CB SER D1087 7698 6478 6643 3085 1439 380 C
ATOM 22090 OG SER D1087 -44.678 77.989 27.974 1.00 54.73 O
ANISOU22090 OG SER D1087 7690 6472 6634 3085 1438 385 O
ATOM 22091 H SER D1087 -43.623 75.617 28.495 1.00 66.44 H
ATOM 22092 HA SER D1087 -42.515 77.208 26.807 1.00 65.49 H
ATOM 22093 HB2 SER D1087 -43.374 77.817 29.427 1.00 65.78 H
ATOM 22094 HB3 SER D1087 -43.000 78.928 28.355 1.00 65.78 H
ATOM 22095 HG SER D1087 -45.000 77.220 28.077 1.00 65.70 H
ATOM 22096 N ALA D1088 -40.687 76.895 29.437 1.00 54.66 N
ANISOU22096 N ALA D1088 7681 6458 6629 3081 1441 371 N
ATOM 22097 CA ALA D1088 -39.314 77.030 29.912 1.00 54.64 C
ANISOU22097 CA ALA D1088 7680 6454 6628 3080 1443 365 C
ATOM 22098 C ALA D1088 -38.357 76.143 29.125 1.00 54.62 C
ANISOU22098 C ALA D1088 7679 6447 6627 3075 1442 362 C
ATOM 22099 O ALA D1088 -37.192 76.509 28.929 1.00 54.61 O
ANISOU22099 O ALA D1088 7681 6441 6626 3073 1444 357 O
ATOM 22100 CB ALA D1088 -39.242 76.700 31.403 1.00 54.65 C
ANISOU22100 CB ALA D1088 7676 6459 6628 3084 1443 365 C
ATOM 22101 H ALA D1088 -41.243 76.603 30.024 1.00 65.53 H
ATOM 22102 HA ALA D1088 -39.031 77.950 29.796 1.00 65.45 H
ATOM 22103 HB1 ALA D1088 -38.325 76.794 31.703 1.00 65.45 H
ATOM 22104 HB2 ALA D1088 -39.814 77.314 31.890 1.00 65.45 H
ATOM 22105 HB3 ALA D1088 -39.543 75.788 31.540 1.00 65.45 H
ATOM 22106 N MET D1089 -38.822 74.977 28.669 1.00 54.62 N
ANISOU22106 N MET D1089 7677 6447 6628 3072 1440 366 N
ATOM 22107 CA MET D1089 -37.977 74.110 27.851 1.00 54.65 C
ANISOU22107 CA MET D1089 7682 6447 6634 3066 1439 364 C
ATOM 22108 C MET D1089 -37.655 74.767 26.515 1.00 54.76 C
ANISOU22108 C MET D1089 7702 6455 6649 3063 1440 361 C
ATOM 22109 O MET D1089 -36.512 74.709 26.047 1.00 54.57 O
ANISOU22109 O MET D1089 7681 6427 6627 3060 1441 357 O
ATOM 22110 CB MET D1089 -38.669 72.763 27.637 1.00 54.59 C
ANISOU22110 CB MET D1089 7672 6442 6629 3064 1437 370 C
ATOM 22111 CG MET D1089 -37.905 71.757 26.773 1.00 54.79 C
ANISOU22111 CG MET D1089 7698 6463 6656 3058 1436 368 C
ATOM 22112 SD MET D1089 -36.493 70.998 27.602 1.00 54.55 S
ANISOU22112 SD MET D1089 7667 6433 6628 3056 1437 364 S
ATOM 22113 CE MET D1089 -35.158 72.039 27.027 1.00 54.54 C
ANISOU22113 CE MET D1089 7671 6425 6627 3055 1439 356 C
ATOM 22114 H MET D1089 -39.612 74.671 28.817 1.00 65.42 H
ATOM 22115 HA MET D1089 -37.147 73.945 28.326 1.00 65.60 H
ATOM 22116 HB2 MET D1089 -38.814 72.351 28.503 1.00 65.39 H
ATOM 22117 HB3 MET D1089 -39.525 72.922 27.208 1.00 65.39 H
ATOM 22118 HG2 MET D1089 -38.512 71.046 26.513 1.00 65.77 H
ATOM 22119 HG3 MET D1089 -37.575 72.212 25.983 1.00 65.77 H
ATOM 22120 HE1 MET D1089 -34.325 71.725 27.413 1.00 65.38 H
ATOM 22121 HE2 MET D1089 -35.115 71.990 26.059 1.00 65.38 H
ATOM 22122 HE3 MET D1089 -35.329 72.953 27.305 1.00 65.38 H
ATOM 22123 N ALA D1090 -38.651 75.400 25.890 1.00 54.71 N
ANISOU22123 N ALA D1090 7697 6449 6641 3064 1440 364 N
ATOM 22124 CA ALA D1090 -38.437 76.057 24.606 1.00 55.45 C
ANISOU22124 CA ALA D1090 7796 6538 6736 3062 1440 362 C
ATOM 22125 C ALA D1090 -37.407 77.174 24.689 1.00 58.11 C
ANISOU22125 C ALA D1090 8136 6870 7071 3063 1443 355 C
ATOM 22126 O ALA D1090 -36.839 77.554 23.658 1.00 56.83 O
ANISOU22126 O ALA D1090 7980 6704 6911 3060 1444 352 O
ATOM 22127 CB ALA D1090 -39.759 76.616 24.081 1.00 54.68 C
ANISOU22127 CB ALA D1090 7699 6442 6636 3063 1439 366 C
ATOM 22128 H ALA D1090 -39.455 75.463 26.190 1.00 65.67 H
ATOM 22129 HA ALA D1090 -38.116 75.401 23.968 1.00 66.57 H
ATOM 22130 HB1 ALA D1090 -39.601 77.049 23.227 1.00 65.64 H
ATOM 22131 HB2 ALA D1090 -40.389 75.887 23.970 1.00 65.64 H
ATOM 22132 HB3 ALA D1090 -40.106 77.259 24.719 1.00 65.64 H
ATOM 22133 N LEU D1091 -37.150 77.706 25.882 1.00 62.30 N
ANISOU22133 N LEU D1091 8666 7405 7602 3067 1444 354 N
ATOM 22134 CA LEU D1091 -36.232 78.824 26.055 1.00 66.89 C
ANISOU22134 CA LEU D1091 9251 7983 8182 3068 1447 348 C
ATOM 22135 C LEU D1091 -34.844 78.394 26.507 1.00 68.75 C
ANISOU22135 C LEU D1091 9486 8216 8419 3067 1448 343 C
ATOM 22136 O LEU D1091 -33.975 79.253 26.680 1.00 71.13 O
ANISOU22136 O LEU D1091 9790 8515 8720 3068 1450 337 O
ATOM 22137 CB LEU D1091 -36.807 79.824 27.063 1.00 68.40 C
ANISOU22137 CB LEU D1091 9441 8178 8371 3074 1448 348 C
ATOM 22138 CG LEU D1091 -38.276 80.202 26.861 1.00 68.83 C
ANISOU22138 CG LEU D1091 9494 8235 8424 3077 1447 354 C
ATOM 22139 CD1 LEU D1091 -38.726 81.194 27.923 1.00 68.78 C
ANISOU22139 CD1 LEU D1091 9486 8233 8415 3083 1448 354 C
ATOM 22140 CD2 LEU D1091 -38.523 80.752 25.463 1.00 68.43 C
ANISOU22140 CD2 LEU D1091 9447 8180 8372 3074 1447 354 C
ATOM 22141 H LEU D1091 -37.501 77.431 26.617 1.00 74.79 H
ATOM 22142 HA LEU D1091 -36.137 79.282 25.205 1.00 80.30 H
ATOM 22143 HB2 LEU D1091 -36.725 79.444 27.952 1.00 82.11 H
ATOM 22144 HB3 LEU D1091 -36.288 80.642 27.013 1.00 82.11 H
ATOM 22145 HG LEU D1091 -38.817 79.402 26.960 1.00 82.62 H
ATOM 22146 HD11 LEU D1091 -39.658 81.416 27.773 1.00 82.56 H
ATOM 22147 HD12 LEU D1091 -38.619 80.789 28.798 1.00 82.56 H
ATOM 22148 HD13 LEU D1091 -38.180 81.994 27.859 1.00 82.56 H
ATOM 22149 HD21 LEU D1091 -39.462 80.979 25.375 1.00 82.14 H
ATOM 22150 HD22 LEU D1091 -37.978 81.544 25.335 1.00 82.14 H
ATOM 22151 HD23 LEU D1091 -38.283 80.076 24.811 1.00 82.14 H
ATOM 22152 N LEU D1092 -34.614 77.097 26.711 1.00 67.13 N
ANISOU22152 N LEU D1092 9279 8013 8216 3064 1446 344 N
ATOM 22153 CA LEU D1092 -33.288 76.632 27.095 1.00 64.19 C
ANISOU22153 CA LEU D1092 8907 7639 7845 3062 1447 340 C
ATOM 22154 C LEU D1092 -32.249 77.153 26.113 1.00 62.18 C
ANISOU22154 C LEU D1092 8657 7377 7591 3059 1449 334 C
ATOM 22155 O LEU D1092 -32.428 77.068 24.895 1.00 61.08 O
ANISOU22155 O LEU D1092 8521 7235 7453 3056 1448 335 O
ATOM 22156 CB LEU D1092 -33.250 75.102 27.144 1.00 63.59 C
ANISOU22156 CB LEU D1092 8827 7564 7771 3059 1445 342 C
ATOM 22157 CG LEU D1092 -31.878 74.501 27.471 1.00 63.34 C
ANISOU22157 CG LEU D1092 8796 7530 7741 3057 1446 338 C
ATOM 22158 CD1 LEU D1092 -31.382 74.979 28.823 1.00 62.99 C
ANISOU22158 CD1 LEU D1092 8750 7488 7696 3061 1448 335 C
ATOM 22159 CD2 LEU D1092 -31.913 72.983 27.443 1.00 63.66 C
ANISOU22159 CD2 LEU D1092 8833 7571 7783 3053 1444 341 C
ATOM 22160 H LEU D1092 -35.203 76.475 26.634 1.00 80.58 H
ATOM 22161 HA LEU D1092 -33.072 76.971 27.978 1.00 77.06 H
ATOM 22162 HB2 LEU D1092 -33.872 74.798 27.823 1.00 76.33 H
ATOM 22163 HB3 LEU D1092 -33.521 74.758 26.278 1.00 76.33 H
ATOM 22164 HG LEU D1092 -31.240 74.795 26.802 1.00 76.04 H
ATOM 22165 HD11 LEU D1092 -30.515 74.582 29.000 1.00 75.62 H
ATOM 22166 HD12 LEU D1092 -31.307 75.946 28.808 1.00 75.62 H
ATOM 22167 HD13 LEU D1092 -32.016 74.707 29.506 1.00 75.62 H
ATOM 22168 HD21 LEU D1092 -31.029 72.643 27.654 1.00 76.42 H
ATOM 22169 HD22 LEU D1092 -32.554 72.670 28.100 1.00 76.42 H
ATOM 22170 HD23 LEU D1092 -32.177 72.690 26.556 1.00 76.42 H
ATOM 22171 N SER D1093 -31.161 77.696 26.651 1.00 63.15 N
ANISOU22171 N SER D1093 8782 7498 7714 3060 1451 329 N
ATOM 22172 CA SER D1093 -30.127 78.310 25.835 1.00 66.14 C
ANISOU22172 CA SER D1093 9165 7871 8094 3058 1452 323 C
ATOM 22173 C SER D1093 -28.757 77.889 26.341 1.00 69.78 C
ANISOU22173 C SER D1093 9626 8330 8556 3056 1453 318 C
ATOM 22174 O SER D1093 -28.527 77.808 27.551 1.00 68.54 O
ANISOU22174 O SER D1093 9466 8176 8399 3059 1454 317 O
ATOM 22175 CB SER D1093 -30.239 79.839 25.852 1.00 67.31 C
ANISOU22175 CB SER D1093 9317 8019 8241 3061 1454 321 C
ATOM 22176 OG SER D1093 -29.231 80.432 25.052 1.00 68.43 O
ANISOU22176 OG SER D1093 9464 8155 8383 3059 1456 315 O
ATOM 22177 H SER D1093 -31.000 77.721 27.495 1.00 75.80 H
ATOM 22178 HA SER D1093 -30.220 78.007 24.918 1.00 79.39 H
ATOM 22179 HB2 SER D1093 -31.108 80.096 25.505 1.00 80.80 H
ATOM 22180 HB3 SER D1093 -30.141 80.152 26.765 1.00 80.80 H
ATOM 22181 HG SER D1093 -29.304 81.268 25.070 1.00 82.14 H
ATOM 22182 N VAL D1094 -27.852 77.618 25.397 1.00 75.60 N
ANISOU22182 N VAL D1094 10367 9062 9295 3051 1454 315 N
ATOM 22183 CA VAL D1094 -26.455 77.349 25.724 1.00 81.94 C
ANISOU22183 CA VAL D1094 11171 9863 10100 3050 1455 309 C
ATOM 22184 C VAL D1094 -25.640 78.631 25.805 1.00 87.80 C
ANISOU22184 C VAL D1094 11916 10601 10841 3051 1457 304 C
ATOM 22185 O VAL D1094 -24.492 78.598 26.273 1.00 87.26 O
ANISOU22185 O VAL D1094 11850 10532 10774 3051 1459 299 O
ATOM 22186 CB VAL D1094 -25.879 76.360 24.687 1.00 82.63 C
ANISOU22186 CB VAL D1094 11260 9946 10190 3044 1454 309 C
ATOM 22187 CG1 VAL D1094 -24.366 76.201 24.823 1.00 83.22 C
ANISOU22187 CG1 VAL D1094 11336 10017 10266 3041 1455 303 C
ATOM 22188 CG2 VAL D1094 -26.563 75.006 24.835 1.00 82.31 C
ANISOU22188 CG2 VAL D1094 11215 9909 10150 3042 1451 314 C
ATOM 22189 H VAL D1094 -28.026 77.584 24.555 1.00 90.74 H
ATOM 22190 HA VAL D1094 -26.417 76.920 26.594 1.00 98.35 H
ATOM 22191 HB VAL D1094 -26.066 76.694 23.796 1.00 99.18 H
ATOM 22192 HG11 VAL D1094 -24.053 75.573 24.153 1.00 99.88 H
ATOM 22193 HG12 VAL D1094 -23.945 77.065 24.689 1.00 99.88 H
ATOM 22194 HG13 VAL D1094 -24.162 75.867 25.710 1.00 99.88 H
ATOM 22195 HG21 VAL D1094 -26.194 74.394 24.179 1.00 98.80 H
ATOM 22196 HG22 VAL D1094 -26.403 74.668 25.730 1.00 98.80 H
ATOM 22197 HG23 VAL D1094 -27.515 75.116 24.686 1.00 98.80 H
ATOM 22198 N GLY D1095 -26.205 79.763 25.395 1.00 93.35 N
ANISOU22198 N GLY D1095 12622 11304 11542 3054 1458 304 N
ATOM 22199 CA GLY D1095 -25.501 81.031 25.409 1.00 97.91 C
ANISOU22199 CA GLY D1095 13204 11879 12120 3055 1460 298 C
ATOM 22200 C GLY D1095 -25.759 81.829 24.146 1.00101.08 C
ANISOU22200 C GLY D1095 13609 12276 12520 3054 1461 298 C
ATOM 22201 O GLY D1095 -26.618 82.711 24.118 1.00102.05 O
ANISOU22201 O GLY D1095 13733 12400 12641 3057 1461 300 O
ATOM 22202 OXT GLY D1095 -25.123 81.603 23.115 1.00102.06 O
ANISOU22202 OXT GLY D1095 13737 12395 12646 3049 1461 295 O
ATOM 22203 H GLY D1095 -27.011 79.819 25.100 1.00112.04 H
ATOM 22204 HA2 GLY D1095 -25.791 81.557 26.171 1.00117.52 H
ATOM 22205 HA3 GLY D1095 -24.547 80.873 25.486 1.00117.52 H
TER 22206 GLY D1095
CONECT 22622251
CONECT 53322251
CONECT2220722208222092221022211
CONECT2220822207
CONECT2220922207
CONECT222102220722251
CONECT22211222072221222239
CONECT2221222211222132221422215
CONECT222132221222251
CONECT2221422212
CONECT222152221222216
CONECT2221622215222172221822219
CONECT2221722216
CONECT2221822216
CONECT222192221622220
CONECT2222022219222212224022241
CONECT2222122220222222222322242
CONECT222222222122227
CONECT2222322221222242222522243
CONECT2222422223
CONECT2222522223222262222722244
CONECT222262222522245
CONECT2222722222222252222822246
CONECT22228222272222922238
CONECT22229222282223022247
CONECT222302222922231
CONECT22231222302223222238
CONECT22232222312223322234
CONECT2223322232
CONECT22234222322223522248
CONECT22235222342223622237
CONECT22236222352224922250
CONECT222372223522238
CONECT22238222282223122237
CONECT2223922211
CONECT2224022220
CONECT2224122220
CONECT2224222221
CONECT2224322223
CONECT2224422225
CONECT2224522226
CONECT2224622227
CONECT2224722229
CONECT2224822234
CONECT2224922236
CONECT2225022236
CONECT22251 226 5332221022213
CONECT222512232522352
CONECT2225222253222542225822259
CONECT222532225222260
CONECT2225422252222552225622261
CONECT222552225422262
CONECT2225622254222572226322264
CONECT222572225622265
CONECT2225822252
CONECT2225922252
CONECT2226022253
CONECT2226122254
CONECT2226222255
CONECT2226322256
CONECT2226422256
CONECT2226522257
CONECT2226622267222682227222273
CONECT222672226622274
CONECT2226822266222692227022275
CONECT222692226822276
CONECT2227022268222712227722278
CONECT222712227022279
CONECT2227222266
CONECT2227322266
CONECT2227422267
CONECT2227522268
CONECT2227622269
CONECT2227722270
CONECT2227822270
CONECT2227922271
CONECT2228022281222822228622287
CONECT222812228022288
CONECT2228222280222832228422289
CONECT222832228222290
CONECT2228422282222852229122292
CONECT222852228422293
CONECT2228622280
CONECT2228722280
CONECT2228822281
CONECT2228922282
CONECT2229022283
CONECT2229122284
CONECT2229222284
CONECT2229322285
CONECT2229422295222962230022301
CONECT222952229422302
CONECT2229622294222972229822303
CONECT222972229622304
CONECT2229822296222992230522306
CONECT222992229822307
CONECT2230022294
CONECT2230122294
CONECT2230222295
CONECT2230322296
CONECT2230422297
CONECT2230522298
CONECT2230622298
CONECT2230722299
CONECT2232522251
CONECT2235222251
MASTER 712 0 6 76 12 0 14 611703 4 106 111
END