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HEADER HYDROLASE 27-JUL-15 5CW2
TITLE CRYSTAL STRUCTURE OF EPOXIDE HYDROLASE A FROM MYCOBACTERIUM
TITLE 2 THERMORESISTIBILE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE EPOXIDE HYDROLASE EPHA;
COMPND 3 CHAIN: C, A, B, D;
COMPND 4 EC: 3.3.2.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM THERMORESISTIBILE ATCC 19527;
SOURCE 3 ORGANISM_TAXID: 1078020;
SOURCE 4 GENE: KEK_07967;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: ROSETTA II
KEYWDS EPOXIDE HYDROLASE, 1, 3-DIPHENYLUREA MYCOBACTERIUM ALPHA/BETA,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.C.SCHULZ,M.WILMANNS
REVDAT 1 17-AUG-16 5CW2 0
JRNL AUTH E.C.SCHULZ,M.WILMANNS,S.HENDERSON,S.SOUTHALL
JRNL TITL THE CRYSTAL STRUCTURE OF MYCOBACTERIAL EPOXIDE HYDROLASE A
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 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 : TWIN_LSQ_F
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.82
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 93380
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 4703
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 47.3122 - 5.4266 0.94 4531 239 0.2090 0.2300
REMARK 3 2 5.4266 - 4.3082 0.94 4466 235 0.1619 0.2097
REMARK 3 3 4.3082 - 3.7638 0.94 4422 233 0.1622 0.2111
REMARK 3 4 3.7638 - 3.4198 0.95 4428 233 0.1951 0.2309
REMARK 3 5 3.4198 - 3.1748 0.95 4482 236 0.2041 0.2636
REMARK 3 6 3.1748 - 2.9876 0.94 4404 231 0.2107 0.2537
REMARK 3 7 2.9876 - 2.8380 0.94 4403 232 0.2154 0.2694
REMARK 3 8 2.8380 - 2.7145 0.95 4447 234 0.2250 0.2631
REMARK 3 9 2.7145 - 2.6100 0.95 4433 234 0.2309 0.2686
REMARK 3 10 2.6100 - 2.5199 0.95 4443 233 0.2305 0.2616
REMARK 3 11 2.5199 - 2.4411 0.95 4415 233 0.2345 0.2731
REMARK 3 12 2.4411 - 2.3714 0.94 4421 232 0.2352 0.2691
REMARK 3 13 2.3714 - 2.3089 0.94 4439 234 0.2328 0.2485
REMARK 3 14 2.3089 - 2.2526 0.95 4433 233 0.2356 0.2834
REMARK 3 15 2.2526 - 2.2014 0.95 4397 232 0.2441 0.2891
REMARK 3 16 2.2014 - 2.1546 0.95 4441 234 0.2440 0.2750
REMARK 3 17 2.1546 - 2.1115 0.95 4430 233 0.2487 0.2855
REMARK 3 18 2.1115 - 2.0716 0.95 4404 232 0.2532 0.2804
REMARK 3 19 2.0716 - 2.0346 0.95 4456 234 0.2562 0.2934
REMARK 3 20 2.0346 - 2.0001 0.95 4397 232 0.2634 0.2962
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 38.230
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 : 0.014 10239
REMARK 3 ANGLE : 1.500 13983
REMARK 3 CHIRALITY : 0.058 1489
REMARK 3 PLANARITY : 0.008 1882
REMARK 3 DIHEDRAL : 16.339 3677
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 37
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 3 THROUGH 77 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.5509 -14.7581 -9.1714
REMARK 3 T TENSOR
REMARK 3 T11: 0.0622 T22: 0.0464
REMARK 3 T33: 0.0703 T12: -0.0054
REMARK 3 T13: 0.0016 T23: 0.0135
REMARK 3 L TENSOR
REMARK 3 L11: 0.0030 L22: -0.0014
REMARK 3 L33: 0.0003 L12: 0.0005
REMARK 3 L13: -0.0009 L23: 0.0029
REMARK 3 S TENSOR
REMARK 3 S11: -0.0170 S12: 0.0013 S13: 0.0047
REMARK 3 S21: 0.0187 S22: -0.0055 S23: 0.0237
REMARK 3 S31: -0.0096 S32: -0.0021 S33: -0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 78 THROUGH 96 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.8926 -9.0736 -18.7311
REMARK 3 T TENSOR
REMARK 3 T11: 0.0081 T22: 0.0280
REMARK 3 T33: 0.0312 T12: -0.0024
REMARK 3 T13: -0.0348 T23: 0.0161
REMARK 3 L TENSOR
REMARK 3 L11: 0.0006 L22: 0.0003
REMARK 3 L33: 0.0001 L12: -0.0003
REMARK 3 L13: -0.0000 L23: -0.0003
REMARK 3 S TENSOR
REMARK 3 S11: -0.0049 S12: 0.0112 S13: -0.0022
REMARK 3 S21: -0.0009 S22: -0.0003 S23: 0.0024
REMARK 3 S31: 0.0002 S32: -0.0000 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 97 THROUGH 126 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.5233 -10.3558 -19.0904
REMARK 3 T TENSOR
REMARK 3 T11: -0.0135 T22: 0.0046
REMARK 3 T33: -0.0374 T12: -0.0551
REMARK 3 T13: -0.0627 T23: 0.1183
REMARK 3 L TENSOR
REMARK 3 L11: 0.0001 L22: -0.0005
REMARK 3 L33: -0.0005 L12: 0.0008
REMARK 3 L13: -0.0008 L23: -0.0008
REMARK 3 S TENSOR
REMARK 3 S11: -0.0034 S12: -0.0025 S13: 0.0029
REMARK 3 S21: 0.0024 S22: -0.0096 S23: 0.0013
REMARK 3 S31: -0.0039 S32: -0.0032 S33: 0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 127 THROUGH 203 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.3326 -33.0415 -18.7784
REMARK 3 T TENSOR
REMARK 3 T11: 0.0314 T22: 0.0360
REMARK 3 T33: 0.0392 T12: 0.0153
REMARK 3 T13: -0.0151 T23: 0.0325
REMARK 3 L TENSOR
REMARK 3 L11: 0.0001 L22: 0.0009
REMARK 3 L33: 0.0009 L12: -0.0026
REMARK 3 L13: -0.0008 L23: 0.0019
REMARK 3 S TENSOR
REMARK 3 S11: 0.0027 S12: 0.0202 S13: -0.0234
REMARK 3 S21: 0.0149 S22: -0.0055 S23: 0.0089
REMARK 3 S31: 0.0025 S32: 0.0004 S33: 0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 204 THROUGH 231 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.5635 -29.8393 -1.3937
REMARK 3 T TENSOR
REMARK 3 T11: 0.0530 T22: 0.0459
REMARK 3 T33: 0.0530 T12: -0.0093
REMARK 3 T13: 0.0029 T23: 0.0146
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0003
REMARK 3 L33: 0.0003 L12: 0.0000
REMARK 3 L13: 0.0004 L23: -0.0008
REMARK 3 S TENSOR
REMARK 3 S11: -0.0051 S12: 0.0033 S13: -0.0064
REMARK 3 S21: 0.0191 S22: -0.0027 S23: 0.0087
REMARK 3 S31: 0.0007 S32: -0.0044 S33: -0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 232 THROUGH 251 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.5100 -22.9480 -27.4052
REMARK 3 T TENSOR
REMARK 3 T11: 0.0103 T22: 0.0624
REMARK 3 T33: 0.0601 T12: 0.0140
REMARK 3 T13: 0.0146 T23: 0.0327
REMARK 3 L TENSOR
REMARK 3 L11: 0.0010 L22: 0.0001
REMARK 3 L33: -0.0006 L12: -0.0022
REMARK 3 L13: -0.0018 L23: -0.0012
REMARK 3 S TENSOR
REMARK 3 S11: -0.0085 S12: 0.0053 S13: -0.0018
REMARK 3 S21: 0.0018 S22: -0.0139 S23: 0.0106
REMARK 3 S31: 0.0002 S32: -0.0052 S33: -0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 252 THROUGH 278 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.2272 -14.2808 -20.0437
REMARK 3 T TENSOR
REMARK 3 T11: 0.0368 T22: 0.0461
REMARK 3 T33: 0.0543 T12: -0.0376
REMARK 3 T13: -0.0109 T23: 0.0646
REMARK 3 L TENSOR
REMARK 3 L11: 0.0016 L22: -0.0002
REMARK 3 L33: -0.0003 L12: 0.0005
REMARK 3 L13: -0.0016 L23: -0.0011
REMARK 3 S TENSOR
REMARK 3 S11: 0.0082 S12: -0.0028 S13: -0.0010
REMARK 3 S21: 0.0011 S22: 0.0020 S23: -0.0052
REMARK 3 S31: 0.0002 S32: 0.0052 S33: -0.0000
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 279 THROUGH 303 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.6981 -13.1469 -12.7645
REMARK 3 T TENSOR
REMARK 3 T11: 0.0562 T22: 0.0598
REMARK 3 T33: 0.0475 T12: -0.0448
REMARK 3 T13: -0.0436 T23: 0.0972
REMARK 3 L TENSOR
REMARK 3 L11: 0.0018 L22: -0.0000
REMARK 3 L33: -0.0002 L12: 0.0009
REMARK 3 L13: 0.0007 L23: -0.0005
REMARK 3 S TENSOR
REMARK 3 S11: 0.0094 S12: -0.0045 S13: 0.0198
REMARK 3 S21: 0.0039 S22: 0.0038 S23: -0.0048
REMARK 3 S31: 0.0007 S32: 0.0020 S33: -0.0000
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 304 THROUGH 321 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.9556 -2.9881 -7.0369
REMARK 3 T TENSOR
REMARK 3 T11: 0.0490 T22: 0.0337
REMARK 3 T33: 0.0775 T12: -0.0103
REMARK 3 T13: -0.0814 T23: 0.0155
REMARK 3 L TENSOR
REMARK 3 L11: 0.0001 L22: 0.0006
REMARK 3 L33: -0.0004 L12: 0.0016
REMARK 3 L13: 0.0014 L23: -0.0001
REMARK 3 S TENSOR
REMARK 3 S11: 0.0041 S12: -0.0027 S13: 0.0010
REMARK 3 S21: -0.0043 S22: 0.0042 S23: -0.0006
REMARK 3 S31: -0.0054 S32: -0.0006 S33: 0.0000
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 77 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.7527 -14.7083 8.4360
REMARK 3 T TENSOR
REMARK 3 T11: 0.0476 T22: 0.0280
REMARK 3 T33: 0.0273 T12: 0.0081
REMARK 3 T13: -0.0127 T23: -0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 0.0009 L22: -0.0019
REMARK 3 L33: 0.0005 L12: 0.0009
REMARK 3 L13: -0.0001 L23: -0.0032
REMARK 3 S TENSOR
REMARK 3 S11: -0.0239 S12: 0.0066 S13: -0.0043
REMARK 3 S21: -0.0075 S22: -0.0245 S23: -0.0117
REMARK 3 S31: -0.0112 S32: -0.0052 S33: -0.0000
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 78 THROUGH 96 )
REMARK 3 ORIGIN FOR THE GROUP (A): 38.1567 -8.8538 17.9611
REMARK 3 T TENSOR
REMARK 3 T11: 0.0349 T22: 0.0316
REMARK 3 T33: 0.0537 T12: 0.0161
REMARK 3 T13: -0.0126 T23: -0.0017
REMARK 3 L TENSOR
REMARK 3 L11: -0.0000 L22: 0.0001
REMARK 3 L33: 0.0000 L12: 0.0001
REMARK 3 L13: 0.0000 L23: 0.0001
REMARK 3 S TENSOR
REMARK 3 S11: -0.0063 S12: -0.0014 S13: 0.0003
REMARK 3 S21: 0.0007 S22: -0.0034 S23: -0.0010
REMARK 3 S31: -0.0022 S32: -0.0018 S33: -0.0000
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 97 THROUGH 126 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.6814 -10.1260 18.2595
REMARK 3 T TENSOR
REMARK 3 T11: 0.0405 T22: 0.0392
REMARK 3 T33: 0.0129 T12: 0.0429
REMARK 3 T13: -0.0218 T23: -0.0934
REMARK 3 L TENSOR
REMARK 3 L11: 0.0005 L22: -0.0001
REMARK 3 L33: -0.0001 L12: -0.0005
REMARK 3 L13: -0.0013 L23: 0.0008
REMARK 3 S TENSOR
REMARK 3 S11: 0.0021 S12: 0.0038 S13: 0.0069
REMARK 3 S21: 0.0035 S22: -0.0128 S23: -0.0045
REMARK 3 S31: -0.0048 S32: 0.0018 S33: -0.0000
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 127 THROUGH 161 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.0148 -28.9421 25.9803
REMARK 3 T TENSOR
REMARK 3 T11: 0.0006 T22: 0.0268
REMARK 3 T33: 0.0313 T12: -0.0166
REMARK 3 T13: -0.0317 T23: -0.0439
REMARK 3 L TENSOR
REMARK 3 L11: 0.0010 L22: -0.0001
REMARK 3 L33: -0.0010 L12: -0.0016
REMARK 3 L13: 0.0006 L23: 0.0001
REMARK 3 S TENSOR
REMARK 3 S11: 0.0062 S12: 0.0005 S13: -0.0038
REMARK 3 S21: 0.0026 S22: -0.0011 S23: 0.0047
REMARK 3 S31: -0.0062 S32: 0.0035 S33: -0.0000
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 162 THROUGH 193 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.2087 -35.1271 9.8356
REMARK 3 T TENSOR
REMARK 3 T11: 0.0129 T22: 0.0159
REMARK 3 T33: 0.0466 T12: 0.0118
REMARK 3 T13: -0.0372 T23: -0.0147
REMARK 3 L TENSOR
REMARK 3 L11: -0.0000 L22: 0.0006
REMARK 3 L33: -0.0004 L12: 0.0004
REMARK 3 L13: 0.0009 L23: -0.0002
REMARK 3 S TENSOR
REMARK 3 S11: 0.0031 S12: 0.0058 S13: -0.0056
REMARK 3 S21: -0.0105 S22: 0.0090 S23: 0.0058
REMARK 3 S31: 0.0031 S32: -0.0063 S33: 0.0000
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 194 THROUGH 215 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.3777 -34.9192 6.0741
REMARK 3 T TENSOR
REMARK 3 T11: 0.0706 T22: 0.0410
REMARK 3 T33: 0.0332 T12: -0.0123
REMARK 3 T13: -0.0376 T23: -0.0070
REMARK 3 L TENSOR
REMARK 3 L11: -0.0008 L22: 0.0000
REMARK 3 L33: 0.0008 L12: 0.0017
REMARK 3 L13: 0.0015 L23: 0.0007
REMARK 3 S TENSOR
REMARK 3 S11: -0.0113 S12: -0.0013 S13: -0.0014
REMARK 3 S21: -0.0125 S22: -0.0041 S23: 0.0074
REMARK 3 S31: -0.0037 S32: 0.0012 S33: 0.0000
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 216 THROUGH 231 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.8130 -29.1682 2.1814
REMARK 3 T TENSOR
REMARK 3 T11: 0.0420 T22: 0.0355
REMARK 3 T33: 0.0330 T12: -0.0057
REMARK 3 T13: -0.0043 T23: -0.0010
REMARK 3 L TENSOR
REMARK 3 L11: -0.0000 L22: -0.0002
REMARK 3 L33: 0.0003 L12: -0.0002
REMARK 3 L13: 0.0006 L23: 0.0002
REMARK 3 S TENSOR
REMARK 3 S11: -0.0006 S12: 0.0018 S13: -0.0030
REMARK 3 S21: -0.0048 S22: 0.0031 S23: -0.0059
REMARK 3 S31: 0.0016 S32: -0.0012 S33: -0.0000
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 232 THROUGH 251 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.6711 -22.7562 26.6564
REMARK 3 T TENSOR
REMARK 3 T11: 0.0456 T22: 0.0527
REMARK 3 T33: 0.0298 T12: -0.0352
REMARK 3 T13: -0.0033 T23: -0.0257
REMARK 3 L TENSOR
REMARK 3 L11: 0.0004 L22: 0.0007
REMARK 3 L33: 0.0000 L12: 0.0019
REMARK 3 L13: -0.0014 L23: -0.0003
REMARK 3 S TENSOR
REMARK 3 S11: -0.0069 S12: -0.0033 S13: 0.0019
REMARK 3 S21: -0.0029 S22: -0.0147 S23: -0.0086
REMARK 3 S31: 0.0036 S32: 0.0045 S33: -0.0000
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 252 THROUGH 278 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.8722 -14.1193 19.1918
REMARK 3 T TENSOR
REMARK 3 T11: 0.0126 T22: 0.0434
REMARK 3 T33: 0.0251 T12: 0.0336
REMARK 3 T13: -0.0103 T23: -0.0542
REMARK 3 L TENSOR
REMARK 3 L11: 0.0006 L22: -0.0005
REMARK 3 L33: 0.0000 L12: 0.0005
REMARK 3 L13: -0.0015 L23: 0.0003
REMARK 3 S TENSOR
REMARK 3 S11: 0.0015 S12: 0.0044 S13: -0.0006
REMARK 3 S21: 0.0029 S22: -0.0055 S23: 0.0060
REMARK 3 S31: -0.0080 S32: -0.0008 S33: 0.0000
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 279 THROUGH 303 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.6031 -12.9394 11.9974
REMARK 3 T TENSOR
REMARK 3 T11: -0.0071 T22: 0.0207
REMARK 3 T33: 0.0192 T12: 0.0454
REMARK 3 T13: -0.0268 T23: -0.0653
REMARK 3 L TENSOR
REMARK 3 L11: 0.0012 L22: -0.0008
REMARK 3 L33: -0.0003 L12: -0.0008
REMARK 3 L13: 0.0007 L23: 0.0010
REMARK 3 S TENSOR
REMARK 3 S11: 0.0102 S12: 0.0042 S13: 0.0120
REMARK 3 S21: -0.0039 S22: 0.0098 S23: 0.0175
REMARK 3 S31: 0.0045 S32: 0.0012 S33: 0.0000
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 304 THROUGH 321 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.2331 -2.8382 6.1115
REMARK 3 T TENSOR
REMARK 3 T11: 0.0655 T22: 0.0431
REMARK 3 T33: 0.0664 T12: 0.0203
REMARK 3 T13: -0.0336 T23: -0.0040
REMARK 3 L TENSOR
REMARK 3 L11: -0.0001 L22: 0.0002
REMARK 3 L33: -0.0001 L12: -0.0009
REMARK 3 L13: 0.0010 L23: 0.0001
REMARK 3 S TENSOR
REMARK 3 S11: 0.0021 S12: 0.0035 S13: 0.0020
REMARK 3 S21: 0.0024 S22: 0.0003 S23: -0.0001
REMARK 3 S31: -0.0051 S32: 0.0017 S33: -0.0000
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 3 THROUGH 27 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.8462 -40.9859 -47.5006
REMARK 3 T TENSOR
REMARK 3 T11: -0.0123 T22: 0.0112
REMARK 3 T33: 0.0171 T12: -0.0229
REMARK 3 T13: 0.0020 T23: -0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 0.0006 L22: -0.0003
REMARK 3 L33: -0.0001 L12: 0.0001
REMARK 3 L13: 0.0008 L23: 0.0009
REMARK 3 S TENSOR
REMARK 3 S11: -0.0058 S12: 0.0018 S13: 0.0015
REMARK 3 S21: -0.0069 S22: 0.0004 S23: 0.0018
REMARK 3 S31: 0.0060 S32: -0.0019 S33: -0.0000
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 28 THROUGH 103 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.2645 -37.7790 -42.8190
REMARK 3 T TENSOR
REMARK 3 T11: 0.0088 T22: 0.0188
REMARK 3 T33: -0.0354 T12: 0.0094
REMARK 3 T13: 0.0106 T23: 0.0433
REMARK 3 L TENSOR
REMARK 3 L11: 0.0025 L22: -0.0004
REMARK 3 L33: 0.0004 L12: 0.0027
REMARK 3 L13: 0.0008 L23: 0.0019
REMARK 3 S TENSOR
REMARK 3 S11: -0.0362 S12: -0.0187 S13: 0.0056
REMARK 3 S21: -0.0254 S22: -0.0243 S23: 0.0126
REMARK 3 S31: 0.0192 S32: -0.0066 S33: -0.0000
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 104 THROUGH 161 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.9870 -30.3501 -30.8077
REMARK 3 T TENSOR
REMARK 3 T11: -0.0508 T22: 0.0358
REMARK 3 T33: -0.0467 T12: 0.0365
REMARK 3 T13: -0.0152 T23: 0.0661
REMARK 3 L TENSOR
REMARK 3 L11: -0.0042 L22: -0.0019
REMARK 3 L33: -0.0000 L12: 0.0044
REMARK 3 L13: 0.0038 L23: -0.0005
REMARK 3 S TENSOR
REMARK 3 S11: 0.0118 S12: -0.0117 S13: 0.0292
REMARK 3 S21: -0.0017 S22: 0.0109 S23: -0.0179
REMARK 3 S31: 0.0236 S32: -0.0052 S33: -0.0000
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 162 THROUGH 215 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.6900 -17.0682 -46.2475
REMARK 3 T TENSOR
REMARK 3 T11: 0.0573 T22: 0.0283
REMARK 3 T33: 0.0375 T12: 0.0211
REMARK 3 T13: 0.0125 T23: 0.0278
REMARK 3 L TENSOR
REMARK 3 L11: -0.0006 L22: 0.0001
REMARK 3 L33: 0.0009 L12: 0.0005
REMARK 3 L13: -0.0018 L23: -0.0022
REMARK 3 S TENSOR
REMARK 3 S11: -0.0043 S12: -0.0052 S13: 0.0065
REMARK 3 S21: -0.0269 S22: 0.0038 S23: -0.0070
REMARK 3 S31: -0.0057 S32: 0.0093 S33: 0.0000
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 216 THROUGH 247 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.6942 -24.9574 -40.5520
REMARK 3 T TENSOR
REMARK 3 T11: 0.0291 T22: 0.0729
REMARK 3 T33: 0.0548 T12: 0.0150
REMARK 3 T13: -0.0001 T23: 0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 0.0016 L22: -0.0008
REMARK 3 L33: -0.0002 L12: 0.0018
REMARK 3 L13: 0.0001 L23: -0.0011
REMARK 3 S TENSOR
REMARK 3 S11: 0.0056 S12: -0.0128 S13: -0.0034
REMARK 3 S21: -0.0155 S22: -0.0132 S23: 0.0032
REMARK 3 S31: -0.0084 S32: -0.0059 S33: 0.0000
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 248 THROUGH 303 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.3198 -38.6753 -37.4738
REMARK 3 T TENSOR
REMARK 3 T11: 0.0234 T22: 0.0509
REMARK 3 T33: 0.0195 T12: 0.0792
REMARK 3 T13: 0.0020 T23: 0.0918
REMARK 3 L TENSOR
REMARK 3 L11: 0.0009 L22: -0.0012
REMARK 3 L33: -0.0004 L12: -0.0005
REMARK 3 L13: 0.0008 L23: -0.0007
REMARK 3 S TENSOR
REMARK 3 S11: 0.0065 S12: 0.0024 S13: -0.0078
REMARK 3 S21: -0.0145 S22: 0.0047 S23: -0.0204
REMARK 3 S31: -0.0048 S32: -0.0003 S33: 0.0000
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 304 THROUGH 321 )
REMARK 3 ORIGIN FOR THE GROUP (A): 34.0009 -48.9756 -48.4276
REMARK 3 T TENSOR
REMARK 3 T11: 0.0355 T22: 0.0091
REMARK 3 T33: 0.0498 T12: -0.0016
REMARK 3 T13: 0.0521 T23: 0.0132
REMARK 3 L TENSOR
REMARK 3 L11: -0.0002 L22: 0.0000
REMARK 3 L33: -0.0000 L12: -0.0003
REMARK 3 L13: -0.0006 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0024 S12: 0.0029 S13: -0.0027
REMARK 3 S21: -0.0021 S22: 0.0003 S23: -0.0009
REMARK 3 S31: 0.0035 S32: -0.0039 S33: 0.0000
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 3 THROUGH 21 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.0654 14.6939 -45.8236
REMARK 3 T TENSOR
REMARK 3 T11: -0.0042 T22: 0.0100
REMARK 3 T33: -0.0023 T12: -0.0146
REMARK 3 T13: -0.0291 T23: 0.0381
REMARK 3 L TENSOR
REMARK 3 L11: -0.0002 L22: -0.0002
REMARK 3 L33: 0.0003 L12: -0.0006
REMARK 3 L13: 0.0003 L23: 0.0004
REMARK 3 S TENSOR
REMARK 3 S11: -0.0058 S12: 0.0080 S13: 0.0015
REMARK 3 S21: -0.0050 S22: 0.0027 S23: -0.0001
REMARK 3 S31: 0.0016 S32: 0.0014 S33: 0.0000
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 22 THROUGH 38 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.4381 12.2259 -45.8065
REMARK 3 T TENSOR
REMARK 3 T11: 0.0316 T22: 0.0303
REMARK 3 T33: 0.0240 T12: -0.0523
REMARK 3 T13: 0.0112 T23: 0.0147
REMARK 3 L TENSOR
REMARK 3 L11: 0.0001 L22: 0.0001
REMARK 3 L33: 0.0006 L12: 0.0002
REMARK 3 L13: -0.0004 L23: -0.0000
REMARK 3 S TENSOR
REMARK 3 S11: -0.0120 S12: 0.0046 S13: -0.0057
REMARK 3 S21: 0.0008 S22: -0.0069 S23: 0.0008
REMARK 3 S31: -0.0065 S32: 0.0036 S33: 0.0000
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 39 THROUGH 77 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.7390 16.9490 -44.5488
REMARK 3 T TENSOR
REMARK 3 T11: 0.0284 T22: 0.0313
REMARK 3 T33: 0.0356 T12: -0.0034
REMARK 3 T13: -0.0005 T23: -0.0047
REMARK 3 L TENSOR
REMARK 3 L11: 0.0038 L22: -0.0007
REMARK 3 L33: -0.0005 L12: 0.0032
REMARK 3 L13: -0.0007 L23: 0.0017
REMARK 3 S TENSOR
REMARK 3 S11: -0.0115 S12: 0.0024 S13: 0.0126
REMARK 3 S21: -0.0146 S22: -0.0083 S23: 0.0067
REMARK 3 S31: 0.0069 S32: 0.0004 S33: 0.0000
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 78 THROUGH 96 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.1084 9.5536 -35.5112
REMARK 3 T TENSOR
REMARK 3 T11: 0.0359 T22: 0.0320
REMARK 3 T33: 0.0366 T12: 0.0244
REMARK 3 T13: 0.0080 T23: -0.0186
REMARK 3 L TENSOR
REMARK 3 L11: 0.0002 L22: 0.0001
REMARK 3 L33: 0.0000 L12: -0.0001
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0007 S12: -0.0027 S13: -0.0063
REMARK 3 S21: -0.0018 S22: 0.0005 S23: 0.0016
REMARK 3 S31: 0.0032 S32: 0.0001 S33: -0.0000
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 97 THROUGH 161 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5708 21.3485 -30.9787
REMARK 3 T TENSOR
REMARK 3 T11: -0.0691 T22: -0.0353
REMARK 3 T33: -0.1015 T12: 0.0314
REMARK 3 T13: 0.0468 T23: 0.0540
REMARK 3 L TENSOR
REMARK 3 L11: -0.0039 L22: -0.0017
REMARK 3 L33: -0.0029 L12: 0.0028
REMARK 3 L13: -0.0000 L23: 0.0010
REMARK 3 S TENSOR
REMARK 3 S11: 0.0229 S12: -0.0190 S13: 0.0370
REMARK 3 S21: 0.0007 S22: -0.0024 S23: -0.0062
REMARK 3 S31: 0.0136 S32: 0.0069 S33: 0.0000
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 162 THROUGH 215 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.6902 35.5597 -45.5659
REMARK 3 T TENSOR
REMARK 3 T11: 0.0573 T22: 0.0336
REMARK 3 T33: 0.0743 T12: -0.0030
REMARK 3 T13: 0.0044 T23: 0.0344
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0004
REMARK 3 L33: 0.0009 L12: 0.0021
REMARK 3 L13: -0.0026 L23: -0.0015
REMARK 3 S TENSOR
REMARK 3 S11: -0.0075 S12: 0.0059 S13: 0.0025
REMARK 3 S21: -0.0132 S22: 0.0110 S23: 0.0017
REMARK 3 S31: -0.0093 S32: 0.0034 S33: -0.0000
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 216 THROUGH 247 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.3911 27.6922 -39.8220
REMARK 3 T TENSOR
REMARK 3 T11: 0.0400 T22: 0.0442
REMARK 3 T33: 0.0555 T12: 0.0085
REMARK 3 T13: -0.0103 T23: 0.0286
REMARK 3 L TENSOR
REMARK 3 L11: 0.0013 L22: 0.0001
REMARK 3 L33: -0.0004 L12: 0.0043
REMARK 3 L13: 0.0007 L23: -0.0009
REMARK 3 S TENSOR
REMARK 3 S11: -0.0062 S12: -0.0115 S13: 0.0054
REMARK 3 S21: -0.0098 S22: -0.0025 S23: 0.0063
REMARK 3 S31: -0.0055 S32: -0.0021 S33: 0.0000
REMARK 3 TLS GROUP : 35
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 248 THROUGH 272 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.4286 13.3589 -32.2981
REMARK 3 T TENSOR
REMARK 3 T11: 0.0439 T22: 0.0519
REMARK 3 T33: 0.0337 T12: 0.0094
REMARK 3 T13: 0.0101 T23: 0.0195
REMARK 3 L TENSOR
REMARK 3 L11: 0.0003 L22: 0.0002
REMARK 3 L33: 0.0002 L12: 0.0005
REMARK 3 L13: 0.0001 L23: 0.0005
REMARK 3 S TENSOR
REMARK 3 S11: 0.0037 S12: 0.0102 S13: -0.0075
REMARK 3 S21: -0.0002 S22: -0.0092 S23: -0.0001
REMARK 3 S31: -0.0010 S32: 0.0040 S33: -0.0000
REMARK 3 TLS GROUP : 36
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 273 THROUGH 292 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.3533 11.9072 -33.6630
REMARK 3 T TENSOR
REMARK 3 T11: -0.0327 T22: -0.0372
REMARK 3 T33: 0.0448 T12: 0.0485
REMARK 3 T13: 0.0206 T23: 0.0663
REMARK 3 L TENSOR
REMARK 3 L11: 0.0003 L22: -0.0005
REMARK 3 L33: -0.0004 L12: -0.0005
REMARK 3 L13: 0.0008 L23: -0.0001
REMARK 3 S TENSOR
REMARK 3 S11: 0.0060 S12: -0.0049 S13: -0.0024
REMARK 3 S21: 0.0005 S22: 0.0044 S23: -0.0027
REMARK 3 S31: -0.0052 S32: 0.0025 S33: -0.0000
REMARK 3 TLS GROUP : 37
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 293 THROUGH 321 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.9116 9.7635 -47.8638
REMARK 3 T TENSOR
REMARK 3 T11: 0.0462 T22: 0.0144
REMARK 3 T33: 0.0222 T12: -0.0220
REMARK 3 T13: 0.0936 T23: 0.0302
REMARK 3 L TENSOR
REMARK 3 L11: -0.0007 L22: 0.0005
REMARK 3 L33: 0.0008 L12: -0.0007
REMARK 3 L13: -0.0019 L23: 0.0010
REMARK 3 S TENSOR
REMARK 3 S11: 0.0015 S12: 0.0107 S13: -0.0123
REMARK 3 S21: 0.0010 S22: 0.0036 S23: 0.0027
REMARK 3 S31: 0.0040 S32: 0.0004 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 5CW2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000212271.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-NOV-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : MASSIF-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9752
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 93380
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 47.820
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.11450
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.6800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.52240
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.420
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BISTRIS PH 7.5, 2.15 M (NH4)2SO4,
REMARK 280 4.5% (V/V) PEG 400, 1-3% (V/V) 2,3-BUTANEDIOL, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
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 52.50500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 C -3
REMARK 465 ALA C -2
REMARK 465 MET C -1
REMARK 465 ALA C 0
REMARK 465 MET C 1
REMARK 465 ILE C 2
REMARK 465 GLY A -3
REMARK 465 ALA A -2
REMARK 465 MET A -1
REMARK 465 ALA A 0
REMARK 465 MET A 1
REMARK 465 ILE A 2
REMARK 465 GLY B -3
REMARK 465 ALA B -2
REMARK 465 MET B -1
REMARK 465 ALA B 0
REMARK 465 MET B 1
REMARK 465 ILE B 2
REMARK 465 GLY D -3
REMARK 465 ALA D -2
REMARK 465 MET D -1
REMARK 465 ALA D 0
REMARK 465 MET D 1
REMARK 465 ILE 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 HE22 GLN C 300 O HOH C 501 1.31
REMARK 500 HG SER D 41 HH TYR D 222 1.31
REMARK 500 HE ARG C 176 OE2 GLU C 206 1.34
REMARK 500 C PRO D 36 H GLU D 37 1.37
REMARK 500 C PRO D 36 H GLU D 37 1.39
REMARK 500 HD22 ASN A 12 OD1 ASP A 84 1.46
REMARK 500 HE ARG C 7 OE2 GLU C 20 1.46
REMARK 500 HE ARG B 177 OE1 GLU B 206 1.47
REMARK 500 O ASP D 60 HG SER D 67 1.47
REMARK 500 HG SER A 127 OD2 ASP A 268 1.48
REMARK 500 HH21 ARG A 176 OE2 GLU A 206 1.49
REMARK 500 O PRO B 70 HH TYR B 76 1.51
REMARK 500 HH11 ARG D 137 O HOH D 501 1.52
REMARK 500 HH22 ARG C 43 OE1 GLN C 301 1.54
REMARK 500 HH TYR C 54 O HOH C 503 1.55
REMARK 500 O ASP C 60 HG SER C 67 1.55
REMARK 500 HH TYR C 238 O11 BSU C 401 1.56
REMARK 500 HH12 ARG B 24 O HOH B 503 1.56
REMARK 500 HH12 ARG C 133 O TRP C 245 1.57
REMARK 500 HH12 ARG D 137 O HOH D 501 1.57
REMARK 500 OD1 ASP A 77 HG1 THR A 79 1.58
REMARK 500 OG SER C 41 HH TYR C 222 1.59
REMARK 500 NH1 ARG D 137 O HOH D 501 1.78
REMARK 500 OG SER B 134 O THR B 136 1.95
REMARK 500 NE2 GLN C 300 O HOH C 501 1.97
REMARK 500 NH1 ARG B 62 O ALA B 75 2.08
REMARK 500 O HOH A 581 O HOH A 589 2.09
REMARK 500 NE ARG C 176 OE2 GLU C 206 2.10
REMARK 500 OE1 GLU A 71 O HOH A 501 2.11
REMARK 500 O TRP A 213 O HOH A 502 2.13
REMARK 500 O HOH D 526 O HOH D 564 2.15
REMARK 500 O HOH D 502 O HOH D 539 2.16
REMARK 500 O HOH B 586 O HOH B 590 2.16
REMARK 500 OE2 GLU D 140 O HOH D 501 2.17
REMARK 500 O HOH B 543 O HOH B 585 2.18
REMARK 500 O HOH D 578 O HOH D 596 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 544 O HOH D 546 2545 1.99
REMARK 500 O HOH A 561 O HOH D 561 2645 2.12
REMARK 500 O HOH B 513 O HOH D 520 2644 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 197 C - N - CA ANGL. DEV. = 9.9 DEGREES
REMARK 500 PRO B 207 C - N - CA ANGL. DEV. = -9.7 DEGREES
REMARK 500 GLU D 37 C - N - CA ANGL. DEV. = 15.2 DEGREES
REMARK 500 GLU D 37 C - N - CA ANGL. DEV. = 18.2 DEGREES
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 HIS C 33 -170.95 -65.74
REMARK 500 ALA C 52 1.72 -68.41
REMARK 500 ASP C 91 -36.58 -39.12
REMARK 500 ASP C 103 -132.69 72.23
REMARK 500 SER C 127 -59.19 69.01
REMARK 500 ASP C 170 87.01 -151.44
REMARK 500 MET C 274 55.31 -115.99
REMARK 500 ARG C 303 58.37 -119.36
REMARK 500 HIS A 33 -177.22 -67.56
REMARK 500 ASP A 103 -125.59 74.76
REMARK 500 ALA A 122 148.30 -177.22
REMARK 500 SER A 127 -51.83 74.22
REMARK 500 ASP A 170 82.10 -159.05
REMARK 500 MET A 274 66.21 -112.22
REMARK 500 ASP B 103 -116.30 62.16
REMARK 500 SER B 127 -42.26 77.09
REMARK 500 MET B 274 77.97 -115.16
REMARK 500 TYR B 287 159.29 179.25
REMARK 500 TRP B 298 59.90 -92.34
REMARK 500 PRO D 70 151.10 -46.75
REMARK 500 ASP D 103 -117.29 59.37
REMARK 500 SER D 127 -43.35 76.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 317 LEU A 318 -148.29
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 C 604 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH C 605 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH C 606 DISTANCE = 6.63 ANGSTROMS
REMARK 525 HOH A 600 DISTANCE = 6.03 ANGSTROMS
REMARK 525 HOH A 601 DISTANCE = 6.05 ANGSTROMS
REMARK 525 HOH A 602 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH A 603 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH A 604 DISTANCE = 6.71 ANGSTROMS
REMARK 525 HOH A 605 DISTANCE = 6.81 ANGSTROMS
REMARK 525 HOH A 606 DISTANCE = 6.83 ANGSTROMS
REMARK 525 HOH A 607 DISTANCE = 7.69 ANGSTROMS
REMARK 525 HOH A 608 DISTANCE = 7.87 ANGSTROMS
REMARK 525 HOH A 609 DISTANCE = 8.66 ANGSTROMS
REMARK 525 HOH A 610 DISTANCE = 10.20 ANGSTROMS
REMARK 525 HOH A 611 DISTANCE = 12.38 ANGSTROMS
REMARK 525 HOH B 591 DISTANCE = 8.07 ANGSTROMS
REMARK 525 HOH D 596 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH D 597 DISTANCE = 6.57 ANGSTROMS
REMARK 525 HOH D 598 DISTANCE = 7.11 ANGSTROMS
REMARK 525 HOH D 599 DISTANCE = 8.04 ANGSTROMS
REMARK 525 HOH D 600 DISTANCE = 8.92 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 NA D 402 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU D 210 O
REMARK 620 2 HOH D 506 O 62.3
REMARK 620 3 THR B 183 OG1 113.1 110.6
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BSU C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BSU A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BSU B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BSU D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA D 402
DBREF 5CW2 C 1 321 UNP G7CF24 G7CF24_MYCTH 1 321
DBREF 5CW2 A 1 321 UNP G7CF24 G7CF24_MYCTH 1 321
DBREF 5CW2 B 1 321 UNP G7CF24 G7CF24_MYCTH 1 321
DBREF 5CW2 D 1 321 UNP G7CF24 G7CF24_MYCTH 1 321
SEQADV 5CW2 GLY C -3 UNP G7CF24 EXPRESSION TAG
SEQADV 5CW2 ALA C -2 UNP G7CF24 EXPRESSION TAG
SEQADV 5CW2 MET C -1 UNP G7CF24 EXPRESSION TAG
SEQADV 5CW2 ALA C 0 UNP G7CF24 EXPRESSION TAG
SEQADV 5CW2 GLY A -3 UNP G7CF24 EXPRESSION TAG
SEQADV 5CW2 ALA A -2 UNP G7CF24 EXPRESSION TAG
SEQADV 5CW2 MET A -1 UNP G7CF24 EXPRESSION TAG
SEQADV 5CW2 ALA A 0 UNP G7CF24 EXPRESSION TAG
SEQADV 5CW2 GLY B -3 UNP G7CF24 EXPRESSION TAG
SEQADV 5CW2 ALA B -2 UNP G7CF24 EXPRESSION TAG
SEQADV 5CW2 MET B -1 UNP G7CF24 EXPRESSION TAG
SEQADV 5CW2 ALA B 0 UNP G7CF24 EXPRESSION TAG
SEQADV 5CW2 GLY D -3 UNP G7CF24 EXPRESSION TAG
SEQADV 5CW2 ALA D -2 UNP G7CF24 EXPRESSION TAG
SEQADV 5CW2 MET D -1 UNP G7CF24 EXPRESSION TAG
SEQADV 5CW2 ALA D 0 UNP G7CF24 EXPRESSION TAG
SEQRES 1 C 325 GLY ALA MET ALA MET ILE THR PRO SER GLU ARG SER VAL
SEQRES 2 C 325 GLU THR ASN GLY VAL ARG LEU ARG LEU VAL GLU ALA GLY
SEQRES 3 C 325 GLU ARG GLY ASP PRO LEU VAL VAL LEU ALA HIS GLY PHE
SEQRES 4 C 325 PRO GLU LEU ALA TYR SER TRP ARG HIS GLN ILE PRO ALA
SEQRES 5 C 325 LEU VAL ASP ALA GLY TYR HIS VAL MET ALA PRO ASP GLN
SEQRES 6 C 325 ARG GLY TYR GLY GLY SER SER ALA PRO GLU ALA ILE GLU
SEQRES 7 C 325 ALA TYR ASP ILE THR ARG LEU THR ALA ASP LEU MET GLY
SEQRES 8 C 325 LEU LEU ASP ASP ILE GLY ALA GLU LYS ALA ALA PHE ILE
SEQRES 9 C 325 GLY HIS ASP TRP GLY ALA LEU VAL VAL TRP ASN ALA ALA
SEQRES 10 C 325 LEU LEU TYR PRO ASP ARG VAL ALA ALA VAL ALA GLY LEU
SEQRES 11 C 325 SER VAL PRO PRO VAL PRO ARG SER LEU THR ARG PRO THR
SEQRES 12 C 325 GLU ALA PHE ARG ALA LEU VAL GLY GLU ASP ASN PHE PHE
SEQRES 13 C 325 TYR ILE LEU TYR PHE GLN GLU PRO GLY VAL ALA ASP ALA
SEQRES 14 C 325 GLU LEU ASP GLY ASP PRO ALA ARG THR MET ARG ARG MET
SEQRES 15 C 325 PHE GLY GLY LEU THR SER ASP PRO ASP ALA ALA HIS ARG
SEQRES 16 C 325 MET LEU GLN PRO GLY PRO ALA GLY PHE ILE ASP ARG LEU
SEQRES 17 C 325 PRO GLU PRO GLU ALA LEU PRO ASP TRP LEU THR ALA GLU
SEQRES 18 C 325 GLU LEU ASP HIS TYR ILE ALA GLU PHE THR ARG THR GLY
SEQRES 19 C 325 PHE THR GLY GLY LEU ASN TRP TYR ARG ASN MET ASP ARG
SEQRES 20 C 325 ASN TRP GLU LEU THR GLU HIS LEU ALA GLY ALA THR ILE
SEQRES 21 C 325 THR ALA PRO ALA LEU PHE LEU ALA GLY ALA ALA ASP PRO
SEQRES 22 C 325 VAL LEU GLY PHE MET ARG PRO GLU ARG ALA THR GLU VAL
SEQRES 23 C 325 ALA VAL GLY PRO TYR ARG GLN VAL LEU LEU ASP GLY ALA
SEQRES 24 C 325 GLY HIS TRP VAL GLN GLN GLU ARG PRO GLN GLU VAL ASN
SEQRES 25 C 325 ALA ALA LEU ILE ASP PHE LEU ARG GLY LEU GLU LEU GLN
SEQRES 1 A 325 GLY ALA MET ALA MET ILE THR PRO SER GLU ARG SER VAL
SEQRES 2 A 325 GLU THR ASN GLY VAL ARG LEU ARG LEU VAL GLU ALA GLY
SEQRES 3 A 325 GLU ARG GLY ASP PRO LEU VAL VAL LEU ALA HIS GLY PHE
SEQRES 4 A 325 PRO GLU LEU ALA TYR SER TRP ARG HIS GLN ILE PRO ALA
SEQRES 5 A 325 LEU VAL ASP ALA GLY TYR HIS VAL MET ALA PRO ASP GLN
SEQRES 6 A 325 ARG GLY TYR GLY GLY SER SER ALA PRO GLU ALA ILE GLU
SEQRES 7 A 325 ALA TYR ASP ILE THR ARG LEU THR ALA ASP LEU MET GLY
SEQRES 8 A 325 LEU LEU ASP ASP ILE GLY ALA GLU LYS ALA ALA PHE ILE
SEQRES 9 A 325 GLY HIS ASP TRP GLY ALA LEU VAL VAL TRP ASN ALA ALA
SEQRES 10 A 325 LEU LEU TYR PRO ASP ARG VAL ALA ALA VAL ALA GLY LEU
SEQRES 11 A 325 SER VAL PRO PRO VAL PRO ARG SER LEU THR ARG PRO THR
SEQRES 12 A 325 GLU ALA PHE ARG ALA LEU VAL GLY GLU ASP ASN PHE PHE
SEQRES 13 A 325 TYR ILE LEU TYR PHE GLN GLU PRO GLY VAL ALA ASP ALA
SEQRES 14 A 325 GLU LEU ASP GLY ASP PRO ALA ARG THR MET ARG ARG MET
SEQRES 15 A 325 PHE GLY GLY LEU THR SER ASP PRO ASP ALA ALA HIS ARG
SEQRES 16 A 325 MET LEU GLN PRO GLY PRO ALA GLY PHE ILE ASP ARG LEU
SEQRES 17 A 325 PRO GLU PRO GLU ALA LEU PRO ASP TRP LEU THR ALA GLU
SEQRES 18 A 325 GLU LEU ASP HIS TYR ILE ALA GLU PHE THR ARG THR GLY
SEQRES 19 A 325 PHE THR GLY GLY LEU ASN TRP TYR ARG ASN MET ASP ARG
SEQRES 20 A 325 ASN TRP GLU LEU THR GLU HIS LEU ALA GLY ALA THR ILE
SEQRES 21 A 325 THR ALA PRO ALA LEU PHE LEU ALA GLY ALA ALA ASP PRO
SEQRES 22 A 325 VAL LEU GLY PHE MET ARG PRO GLU ARG ALA THR GLU VAL
SEQRES 23 A 325 ALA VAL GLY PRO TYR ARG GLN VAL LEU LEU ASP GLY ALA
SEQRES 24 A 325 GLY HIS TRP VAL GLN GLN GLU ARG PRO GLN GLU VAL ASN
SEQRES 25 A 325 ALA ALA LEU ILE ASP PHE LEU ARG GLY LEU GLU LEU GLN
SEQRES 1 B 325 GLY ALA MET ALA MET ILE THR PRO SER GLU ARG SER VAL
SEQRES 2 B 325 GLU THR ASN GLY VAL ARG LEU ARG LEU VAL GLU ALA GLY
SEQRES 3 B 325 GLU ARG GLY ASP PRO LEU VAL VAL LEU ALA HIS GLY PHE
SEQRES 4 B 325 PRO GLU LEU ALA TYR SER TRP ARG HIS GLN ILE PRO ALA
SEQRES 5 B 325 LEU VAL ASP ALA GLY TYR HIS VAL MET ALA PRO ASP GLN
SEQRES 6 B 325 ARG GLY TYR GLY GLY SER SER ALA PRO GLU ALA ILE GLU
SEQRES 7 B 325 ALA TYR ASP ILE THR ARG LEU THR ALA ASP LEU MET GLY
SEQRES 8 B 325 LEU LEU ASP ASP ILE GLY ALA GLU LYS ALA ALA PHE ILE
SEQRES 9 B 325 GLY HIS ASP TRP GLY ALA LEU VAL VAL TRP ASN ALA ALA
SEQRES 10 B 325 LEU LEU TYR PRO ASP ARG VAL ALA ALA VAL ALA GLY LEU
SEQRES 11 B 325 SER VAL PRO PRO VAL PRO ARG SER LEU THR ARG PRO THR
SEQRES 12 B 325 GLU ALA PHE ARG ALA LEU VAL GLY GLU ASP ASN PHE PHE
SEQRES 13 B 325 TYR ILE LEU TYR PHE GLN GLU PRO GLY VAL ALA ASP ALA
SEQRES 14 B 325 GLU LEU ASP GLY ASP PRO ALA ARG THR MET ARG ARG MET
SEQRES 15 B 325 PHE GLY GLY LEU THR SER ASP PRO ASP ALA ALA HIS ARG
SEQRES 16 B 325 MET LEU GLN PRO GLY PRO ALA GLY PHE ILE ASP ARG LEU
SEQRES 17 B 325 PRO GLU PRO GLU ALA LEU PRO ASP TRP LEU THR ALA GLU
SEQRES 18 B 325 GLU LEU ASP HIS TYR ILE ALA GLU PHE THR ARG THR GLY
SEQRES 19 B 325 PHE THR GLY GLY LEU ASN TRP TYR ARG ASN MET ASP ARG
SEQRES 20 B 325 ASN TRP GLU LEU THR GLU HIS LEU ALA GLY ALA THR ILE
SEQRES 21 B 325 THR ALA PRO ALA LEU PHE LEU ALA GLY ALA ALA ASP PRO
SEQRES 22 B 325 VAL LEU GLY PHE MET ARG PRO GLU ARG ALA THR GLU VAL
SEQRES 23 B 325 ALA VAL GLY PRO TYR ARG GLN VAL LEU LEU ASP GLY ALA
SEQRES 24 B 325 GLY HIS TRP VAL GLN GLN GLU ARG PRO GLN GLU VAL ASN
SEQRES 25 B 325 ALA ALA LEU ILE ASP PHE LEU ARG GLY LEU GLU LEU GLN
SEQRES 1 D 325 GLY ALA MET ALA MET ILE THR PRO SER GLU ARG SER VAL
SEQRES 2 D 325 GLU THR ASN GLY VAL ARG LEU ARG LEU VAL GLU ALA GLY
SEQRES 3 D 325 GLU ARG GLY ASP PRO LEU VAL VAL LEU ALA HIS GLY PHE
SEQRES 4 D 325 PRO GLU LEU ALA TYR SER TRP ARG HIS GLN ILE PRO ALA
SEQRES 5 D 325 LEU VAL ASP ALA GLY TYR HIS VAL MET ALA PRO ASP GLN
SEQRES 6 D 325 ARG GLY TYR GLY GLY SER SER ALA PRO GLU ALA ILE GLU
SEQRES 7 D 325 ALA TYR ASP ILE THR ARG LEU THR ALA ASP LEU MET GLY
SEQRES 8 D 325 LEU LEU ASP ASP ILE GLY ALA GLU LYS ALA ALA PHE ILE
SEQRES 9 D 325 GLY HIS ASP TRP GLY ALA LEU VAL VAL TRP ASN ALA ALA
SEQRES 10 D 325 LEU LEU TYR PRO ASP ARG VAL ALA ALA VAL ALA GLY LEU
SEQRES 11 D 325 SER VAL PRO PRO VAL PRO ARG SER LEU THR ARG PRO THR
SEQRES 12 D 325 GLU ALA PHE ARG ALA LEU VAL GLY GLU ASP ASN PHE PHE
SEQRES 13 D 325 TYR ILE LEU TYR PHE GLN GLU PRO GLY VAL ALA ASP ALA
SEQRES 14 D 325 GLU LEU ASP GLY ASP PRO ALA ARG THR MET ARG ARG MET
SEQRES 15 D 325 PHE GLY GLY LEU THR SER ASP PRO ASP ALA ALA HIS ARG
SEQRES 16 D 325 MET LEU GLN PRO GLY PRO ALA GLY PHE ILE ASP ARG LEU
SEQRES 17 D 325 PRO GLU PRO GLU ALA LEU PRO ASP TRP LEU THR ALA GLU
SEQRES 18 D 325 GLU LEU ASP HIS TYR ILE ALA GLU PHE THR ARG THR GLY
SEQRES 19 D 325 PHE THR GLY GLY LEU ASN TRP TYR ARG ASN MET ASP ARG
SEQRES 20 D 325 ASN TRP GLU LEU THR GLU HIS LEU ALA GLY ALA THR ILE
SEQRES 21 D 325 THR ALA PRO ALA LEU PHE LEU ALA GLY ALA ALA ASP PRO
SEQRES 22 D 325 VAL LEU GLY PHE MET ARG PRO GLU ARG ALA THR GLU VAL
SEQRES 23 D 325 ALA VAL GLY PRO TYR ARG GLN VAL LEU LEU ASP GLY ALA
SEQRES 24 D 325 GLY HIS TRP VAL GLN GLN GLU ARG PRO GLN GLU VAL ASN
SEQRES 25 D 325 ALA ALA LEU ILE ASP PHE LEU ARG GLY LEU GLU LEU GLN
HET BSU C 401 16
HET BSU A 401 16
HET BSU B 401 16
HET BSU D 401 16
HET NA D 402 1
HETNAM BSU 1,3-DIPHENYLUREA
HETNAM NA SODIUM ION
HETSYN BSU DIPHENYLCARBAMIDE
FORMUL 5 BSU 4(C13 H12 N2 O)
FORMUL 9 NA NA 1+
FORMUL 10 HOH *408(H2 O)
HELIX 1 AA1 LEU C 38 ARG C 43 5 6
HELIX 2 AA2 GLN C 45 ALA C 52 1 8
HELIX 3 AA3 ILE C 73 TYR C 76 5 4
HELIX 4 AA4 ASP C 77 ILE C 92 1 16
HELIX 5 AA5 ASP C 103 TYR C 116 1 14
HELIX 6 AA6 ARG C 137 GLY C 147 1 11
HELIX 7 AA7 PHE C 152 PHE C 157 1 6
HELIX 8 AA8 GLY C 161 ASP C 170 1 10
HELIX 9 AA9 ASP C 170 LEU C 182 1 13
HELIX 10 AB1 ASP C 185 GLN C 194 1 10
HELIX 11 AB2 GLY C 199 LEU C 204 1 6
HELIX 12 AB3 THR C 215 GLY C 230 1 16
HELIX 13 AB4 PHE C 231 ARG C 239 1 9
HELIX 14 AB5 ASN C 240 LEU C 247 1 8
HELIX 15 AB6 THR C 248 ALA C 252 5 5
HELIX 16 AB7 ASP C 268 PHE C 273 5 6
HELIX 17 AB8 ARG C 278 VAL C 282 5 5
HELIX 18 AB9 TRP C 298 ARG C 303 1 6
HELIX 19 AC1 ARG C 303 ARG C 316 1 14
HELIX 20 AC2 LEU A 38 ARG A 43 5 6
HELIX 21 AC3 GLN A 45 ALA A 52 1 8
HELIX 22 AC4 ALA A 72 TYR A 76 5 5
HELIX 23 AC5 ASP A 77 GLY A 93 1 17
HELIX 24 AC6 ASP A 103 TYR A 116 1 14
HELIX 25 AC7 ARG A 137 GLY A 147 1 11
HELIX 26 AC8 PHE A 152 PHE A 157 1 6
HELIX 27 AC9 GLY A 161 ASP A 170 1 10
HELIX 28 AD1 ASP A 170 LEU A 182 1 13
HELIX 29 AD2 ASP A 185 GLN A 194 1 10
HELIX 30 AD3 THR A 215 GLY A 230 1 16
HELIX 31 AD4 PHE A 231 ARG A 239 1 9
HELIX 32 AD5 ASN A 240 LEU A 247 1 8
HELIX 33 AD6 THR A 248 ALA A 252 5 5
HELIX 34 AD7 ASP A 268 PHE A 273 5 6
HELIX 35 AD8 ARG A 278 ALA A 283 1 6
HELIX 36 AD9 TRP A 298 ARG A 303 1 6
HELIX 37 AE1 ARG A 303 LEU A 315 1 13
HELIX 38 AE2 LEU B 38 ARG B 43 5 6
HELIX 39 AE3 HIS B 44 ALA B 52 1 9
HELIX 40 AE4 ALA B 72 TYR B 76 5 5
HELIX 41 AE5 ASP B 77 ILE B 92 1 16
HELIX 42 AE6 ASP B 103 TYR B 116 1 14
HELIX 43 AE7 ARG B 137 GLY B 147 1 11
HELIX 44 AE8 PHE B 152 GLN B 158 1 7
HELIX 45 AE9 GLY B 161 ASP B 170 1 10
HELIX 46 AF1 ASP B 170 LEU B 182 1 13
HELIX 47 AF2 ASP B 185 GLN B 194 1 10
HELIX 48 AF3 GLY B 199 LEU B 204 1 6
HELIX 49 AF4 THR B 215 GLY B 230 1 16
HELIX 50 AF5 PHE B 231 ARG B 239 1 9
HELIX 51 AF6 ASN B 240 THR B 248 1 9
HELIX 52 AF7 GLU B 249 ALA B 252 5 4
HELIX 53 AF8 ASP B 268 PHE B 273 5 6
HELIX 54 AF9 PRO B 276 VAL B 282 5 7
HELIX 55 AG1 TRP B 298 ARG B 303 1 6
HELIX 56 AG2 ARG B 303 ARG B 316 1 14
HELIX 57 AG3 LEU D 38 ARG D 43 5 6
HELIX 58 AG4 HIS D 44 ALA D 52 1 9
HELIX 59 AG5 ALA D 72 TYR D 76 5 5
HELIX 60 AG6 ASP D 77 ILE D 92 1 16
HELIX 61 AG7 ASP D 103 TYR D 116 1 14
HELIX 62 AG8 ARG D 137 GLY D 147 1 11
HELIX 63 AG9 PHE D 152 GLN D 158 1 7
HELIX 64 AH1 GLY D 161 ASP D 170 1 10
HELIX 65 AH2 ASP D 170 GLY D 180 1 11
HELIX 66 AH3 ASP D 185 GLN D 194 1 10
HELIX 67 AH4 PHE D 200 LEU D 204 5 5
HELIX 68 AH5 THR D 215 GLY D 230 1 16
HELIX 69 AH6 PHE D 231 ARG D 239 1 9
HELIX 70 AH7 ASN D 240 THR D 248 1 9
HELIX 71 AH8 GLU D 249 ALA D 252 5 4
HELIX 72 AH9 ASP D 268 PHE D 273 5 6
HELIX 73 AI1 ARG D 275 GLU D 277 5 3
HELIX 74 AI2 ARG D 278 ALA D 283 1 6
HELIX 75 AI3 TRP D 298 ARG D 303 1 6
HELIX 76 AI4 ARG D 303 ARG D 316 1 14
SHEET 1 AA1 8 SER C 5 THR C 11 0
SHEET 2 AA1 8 VAL C 14 ALA C 21 -1 O VAL C 14 N THR C 11
SHEET 3 AA1 8 HIS C 55 ASP C 60 -1 O ALA C 58 N VAL C 19
SHEET 4 AA1 8 LEU C 28 ALA C 32 1 N LEU C 31 O MET C 57
SHEET 5 AA1 8 ALA C 97 HIS C 102 1 O ALA C 98 N VAL C 30
SHEET 6 AA1 8 VAL C 120 LEU C 126 1 O LEU C 126 N GLY C 101
SHEET 7 AA1 8 ALA C 260 GLY C 265 1 O LEU C 261 N GLY C 125
SHEET 8 AA1 8 GLN C 289 LEU C 292 1 O LEU C 292 N ALA C 264
SHEET 1 AA2 8 SER A 5 THR A 11 0
SHEET 2 AA2 8 VAL A 14 ALA A 21 -1 O GLU A 20 N SER A 5
SHEET 3 AA2 8 HIS A 55 PRO A 59 -1 O ALA A 58 N VAL A 19
SHEET 4 AA2 8 LEU A 28 ALA A 32 1 N VAL A 29 O HIS A 55
SHEET 5 AA2 8 ALA A 97 HIS A 102 1 O ALA A 98 N VAL A 30
SHEET 6 AA2 8 VAL A 120 LEU A 126 1 O LEU A 126 N GLY A 101
SHEET 7 AA2 8 ALA A 260 GLY A 265 1 O LEU A 261 N GLY A 125
SHEET 8 AA2 8 TYR A 287 LEU A 292 1 O LEU A 292 N ALA A 264
SHEET 1 AA3 8 SER B 5 THR B 11 0
SHEET 2 AA3 8 VAL B 14 ALA B 21 -1 O LEU B 18 N ARG B 7
SHEET 3 AA3 8 HIS B 55 PRO B 59 -1 O VAL B 56 N ALA B 21
SHEET 4 AA3 8 LEU B 28 ALA B 32 1 N LEU B 31 O MET B 57
SHEET 5 AA3 8 ALA B 97 HIS B 102 1 O ALA B 98 N LEU B 28
SHEET 6 AA3 8 VAL B 120 LEU B 126 1 O ALA B 124 N PHE B 99
SHEET 7 AA3 8 ALA B 260 GLY B 265 1 O LEU B 261 N GLY B 125
SHEET 8 AA3 8 GLN B 289 LEU B 292 1 O VAL B 290 N PHE B 262
SHEET 1 AA4 8 SER D 5 THR D 11 0
SHEET 2 AA4 8 VAL D 14 ALA D 21 -1 O LEU D 18 N ARG D 7
SHEET 3 AA4 8 HIS D 55 ASP D 60 -1 O VAL D 56 N ALA D 21
SHEET 4 AA4 8 LEU D 28 ALA D 32 1 N VAL D 29 O MET D 57
SHEET 5 AA4 8 ALA D 97 HIS D 102 1 O ILE D 100 N VAL D 30
SHEET 6 AA4 8 VAL D 120 LEU D 126 1 O LEU D 126 N GLY D 101
SHEET 7 AA4 8 ALA D 260 GLY D 265 1 O LEU D 261 N GLY D 125
SHEET 8 AA4 8 TYR D 287 LEU D 292 1 O VAL D 290 N PHE D 262
LINK O LEU D 210 NA NA D 402 1555 1555 2.21
LINK NA NA D 402 O HOH D 506 1555 1555 2.41
LINK OG1 THR B 183 NA NA D 402 1555 2644 2.28
CISPEP 1 PHE C 35 PRO C 36 0 -15.09
CISPEP 2 PHE A 35 PRO A 36 0 -16.50
CISPEP 3 PHE B 35 PRO B 36 0 -12.62
CISPEP 4 ARG B 316 GLY B 317 0 -6.72
CISPEP 5 PHE D 35 PRO D 36 0 -14.61
SITE 1 AC1 11 PHE C 35 ASP C 103 TRP C 104 LEU C 107
SITE 2 AC1 11 TYR C 153 ILE C 154 MET C 178 TYR C 238
SITE 3 AC1 11 MET C 241 HIS C 297 TRP C 298
SITE 1 AC2 9 PHE A 35 ASP A 103 TRP A 104 LEU A 107
SITE 2 AC2 9 TYR A 153 MET A 178 TYR A 238 MET A 241
SITE 3 AC2 9 HIS A 297
SITE 1 AC3 7 PHE B 35 ASP B 103 TRP B 104 LEU B 107
SITE 2 AC3 7 TYR B 153 TYR B 238 HIS B 297
SITE 1 AC4 8 PHE D 35 ASP D 103 TRP D 104 LEU D 107
SITE 2 AC4 8 TYR D 153 PHE D 200 TYR D 238 HIS D 297
SITE 1 AC5 2 LEU D 210 HOH D 506
CRYST1 61.800 105.010 108.950 90.00 90.11 90.00 P 1 21 1 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 0.016181 0.000000 0.000030 0.00000
SCALE2 0.000000 0.009523 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009179 0.00000
TER 4846 GLN C 321
TER 9693 GLN A 321
TER 14540 GLN B 321
TER 19399 GLN D 321
MASTER 1019 0 5 76 32 0 11 610365 4 67 100
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