| content |
HEADER HYDROLASE 03-DEC-15 5F4Z
TITLE THE CRYSTAL STRUCTURE OF AN EPOXIDE HYDROLASE FROM STREPTOMYCES
TITLE 2 CARZINOSTATICUS SUBSP. NEOCARZINOSTATICUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPOXIDE HYDROLASE;
COMPND 3 CHAIN: A, B, C, D, E;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES CARZINOSTATICUS SUBSP.
SOURCE 3 NEOCARZINOSTATICUS;
SOURCE 4 ORGANISM_TAXID: 167636;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: BL21(DE3)MAGIC;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMCSG81
KEYWDS EPOXIDE HYDROLASE, STRUCTURAL GENOMICS, PSI-BIOLOGY, MIDWEST CENTER
KEYWDS 2 FOR STRUCTURAL GENOMICS, MCSG, ENZYME DISCOVERY FOR NATURAL PRODUCT
KEYWDS 3 BIOSYNTHESIS, NATPRO, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.TAN,H.LI,R.JEDRZEJCZAK,G.BABNIGG,C.A.BINGMAN,R.YENNAMALLI,J.LOHMAN,
AUTHOR 2 C.Y.CHANG,B.SHEN,G.N.PHILLIPS JR,A.JOACHIMIAK,MIDWEST CENTER FOR
AUTHOR 3 STRUCTURAL GENOMICS (MCSG),ENZYME DISCOVERY FOR NATURAL PRODUCT
AUTHOR 4 BIOSYNTHESIS (NATPRO)
REVDAT 1 17-FEB-16 5F4Z 0
JRNL AUTH K.TAN,H.LI,R.JEDRZEJCZAK,G.BABNIGG,C.A.BINGMAN,R.YENNAMALLI,
JRNL AUTH 2 J.LOHMAN,C.Y.CHANG,B.SHEN,G.N.PHILLIPS JR,A.JOACHIMIAK
JRNL TITL THE CRYSTAL STRUCTURE OF AN EPOXIDE HYDROLASE FROM
JRNL TITL 2 STREPTOMYCES CARZINOSTATICUS SUBSP. NEOCARZINOSTATICUS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.82 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.82
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.27
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 177658
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 8896
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 33.2728 - 5.6463 0.98 5676 310 0.1423 0.1494
REMARK 3 2 5.6463 - 4.4851 0.99 5662 280 0.1292 0.1732
REMARK 3 3 4.4851 - 3.9192 0.99 5635 306 0.1249 0.1553
REMARK 3 4 3.9192 - 3.5613 0.99 5662 281 0.1389 0.1714
REMARK 3 5 3.5613 - 3.3063 0.99 5641 284 0.1521 0.1828
REMARK 3 6 3.3063 - 3.1115 1.00 5635 309 0.1583 0.2034
REMARK 3 7 3.1115 - 2.9558 1.00 5659 274 0.1625 0.2142
REMARK 3 8 2.9558 - 2.8272 1.00 5680 273 0.1657 0.2060
REMARK 3 9 2.8272 - 2.7184 1.00 5601 318 0.1636 0.2189
REMARK 3 10 2.7184 - 2.6246 1.00 5656 284 0.1555 0.2106
REMARK 3 11 2.6246 - 2.5426 1.00 5628 334 0.1654 0.2168
REMARK 3 12 2.5426 - 2.4699 1.00 5586 321 0.1640 0.2123
REMARK 3 13 2.4699 - 2.4049 1.00 5603 310 0.1537 0.2014
REMARK 3 14 2.4049 - 2.3463 1.00 5615 303 0.1576 0.2074
REMARK 3 15 2.3463 - 2.2929 1.00 5636 328 0.1646 0.2245
REMARK 3 16 2.2929 - 2.2442 1.00 5604 298 0.1676 0.1980
REMARK 3 17 2.2442 - 2.1993 1.00 5584 314 0.1629 0.2143
REMARK 3 18 2.1993 - 2.1578 1.00 5633 320 0.1625 0.2076
REMARK 3 19 2.1578 - 2.1192 1.00 5647 275 0.1726 0.2424
REMARK 3 20 2.1192 - 2.0833 1.00 5642 304 0.1809 0.2162
REMARK 3 21 2.0833 - 2.0497 1.00 5609 293 0.1849 0.2213
REMARK 3 22 2.0497 - 2.0182 1.00 5588 273 0.1856 0.2318
REMARK 3 23 2.0182 - 1.9885 1.00 5700 294 0.1894 0.2349
REMARK 3 24 1.9885 - 1.9605 1.00 5631 270 0.2011 0.2344
REMARK 3 25 1.9605 - 1.9340 1.00 5593 298 0.2171 0.2691
REMARK 3 26 1.9340 - 1.9089 1.00 5580 292 0.2337 0.2647
REMARK 3 27 1.9089 - 1.8850 1.00 5638 292 0.2306 0.2986
REMARK 3 28 1.8850 - 1.8623 1.00 5592 283 0.2471 0.2827
REMARK 3 29 1.8623 - 1.8407 0.99 5618 285 0.2612 0.3048
REMARK 3 30 1.8407 - 1.8200 0.98 5528 290 0.2869 0.3367
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.830
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 : 0.008 15988
REMARK 3 ANGLE : 1.082 21933
REMARK 3 CHIRALITY : 0.045 2327
REMARK 3 PLANARITY : 0.006 2881
REMARK 3 DIHEDRAL : 12.422 5724
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 34
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 39 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.1970 4.5968 28.6691
REMARK 3 T TENSOR
REMARK 3 T11: 0.1565 T22: 0.1170
REMARK 3 T33: 0.2356 T12: -0.0373
REMARK 3 T13: 0.0218 T23: -0.0305
REMARK 3 L TENSOR
REMARK 3 L11: 1.4449 L22: 2.1788
REMARK 3 L33: 2.1553 L12: -1.0011
REMARK 3 L13: 0.2484 L23: -1.2653
REMARK 3 S TENSOR
REMARK 3 S11: -0.0679 S12: -0.0495 S13: -0.2644
REMARK 3 S21: 0.1845 S22: 0.0800 S23: 0.2575
REMARK 3 S31: 0.0048 S32: -0.0354 S33: -0.0367
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 40 THROUGH 80 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.0439 -3.6983 29.4481
REMARK 3 T TENSOR
REMARK 3 T11: 0.1966 T22: 0.1272
REMARK 3 T33: 0.1724 T12: -0.0053
REMARK 3 T13: 0.0677 T23: -0.0200
REMARK 3 L TENSOR
REMARK 3 L11: 2.9901 L22: 1.8390
REMARK 3 L33: 0.9356 L12: -0.8829
REMARK 3 L13: 0.6417 L23: -0.7590
REMARK 3 S TENSOR
REMARK 3 S11: -0.0239 S12: -0.1860 S13: -0.4367
REMARK 3 S21: 0.0951 S22: 0.0533 S23: 0.3108
REMARK 3 S31: 0.1690 S32: -0.1323 S33: -0.0644
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 81 THROUGH 215 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.0872 -2.9989 21.8728
REMARK 3 T TENSOR
REMARK 3 T11: 0.1488 T22: 0.1534
REMARK 3 T33: 0.1962 T12: 0.0218
REMARK 3 T13: -0.0035 T23: 0.0121
REMARK 3 L TENSOR
REMARK 3 L11: 0.9571 L22: 0.8077
REMARK 3 L33: 1.3381 L12: -0.1066
REMARK 3 L13: -0.1553 L23: 0.2013
REMARK 3 S TENSOR
REMARK 3 S11: -0.0396 S12: 0.0228 S13: -0.1144
REMARK 3 S21: 0.0644 S22: -0.0148 S23: -0.1060
REMARK 3 S31: 0.1250 S32: 0.1054 S33: 0.0367
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 216 THROUGH 306 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.0350 8.5102 19.3211
REMARK 3 T TENSOR
REMARK 3 T11: 0.1249 T22: 0.1473
REMARK 3 T33: 0.1622 T12: 0.0052
REMARK 3 T13: -0.0139 T23: -0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 1.1695 L22: 0.7571
REMARK 3 L33: 1.2128 L12: -0.5133
REMARK 3 L13: -0.4877 L23: 0.3728
REMARK 3 S TENSOR
REMARK 3 S11: 0.0069 S12: 0.1413 S13: -0.0395
REMARK 3 S21: -0.0202 S22: -0.0291 S23: 0.0791
REMARK 3 S31: 0.0314 S32: -0.0921 S33: 0.0257
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 307 THROUGH 341 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.6299 9.0217 12.5171
REMARK 3 T TENSOR
REMARK 3 T11: 0.1923 T22: 0.1742
REMARK 3 T33: 0.2195 T12: -0.0063
REMARK 3 T13: -0.0096 T23: 0.0540
REMARK 3 L TENSOR
REMARK 3 L11: 2.6075 L22: 2.0406
REMARK 3 L33: 2.6144 L12: -2.1945
REMARK 3 L13: -2.1180 L23: 1.9619
REMARK 3 S TENSOR
REMARK 3 S11: 0.1089 S12: -0.1062 S13: 0.3363
REMARK 3 S21: -0.2055 S22: 0.0585 S23: -0.4160
REMARK 3 S31: -0.3726 S32: 0.1530 S33: -0.1790
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 342 THROUGH 369 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.9992 -0.7146 6.7741
REMARK 3 T TENSOR
REMARK 3 T11: 0.1478 T22: 0.1328
REMARK 3 T33: 0.1070 T12: 0.0063
REMARK 3 T13: -0.0224 T23: -0.0346
REMARK 3 L TENSOR
REMARK 3 L11: 4.0397 L22: 2.1921
REMARK 3 L33: 3.0069 L12: -0.5325
REMARK 3 L13: -1.7761 L23: -0.8478
REMARK 3 S TENSOR
REMARK 3 S11: 0.0345 S12: 0.2604 S13: -0.0406
REMARK 3 S21: -0.1178 S22: -0.0838 S23: -0.0415
REMARK 3 S31: 0.0528 S32: -0.0056 S33: -0.0010
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 370 THROUGH 388 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.2797 -12.2907 11.2361
REMARK 3 T TENSOR
REMARK 3 T11: 0.2273 T22: 0.1471
REMARK 3 T33: 0.1818 T12: 0.0294
REMARK 3 T13: 0.0147 T23: -0.0199
REMARK 3 L TENSOR
REMARK 3 L11: 8.9611 L22: 4.7447
REMARK 3 L33: 4.8241 L12: -1.1344
REMARK 3 L13: -2.6311 L23: -0.7566
REMARK 3 S TENSOR
REMARK 3 S11: -0.0690 S12: 0.0215 S13: -0.3513
REMARK 3 S21: -0.1588 S22: -0.0855 S23: -0.1269
REMARK 3 S31: 0.3733 S32: 0.3642 S33: 0.2705
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 39 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.5799 22.1114 34.5109
REMARK 3 T TENSOR
REMARK 3 T11: 0.1756 T22: 0.1327
REMARK 3 T33: 0.0890 T12: 0.0059
REMARK 3 T13: 0.0279 T23: -0.0291
REMARK 3 L TENSOR
REMARK 3 L11: 3.2635 L22: 2.5222
REMARK 3 L33: 0.8554 L12: -1.0450
REMARK 3 L13: 0.0361 L23: -0.5142
REMARK 3 S TENSOR
REMARK 3 S11: -0.0388 S12: -0.0468 S13: -0.2305
REMARK 3 S21: 0.1566 S22: 0.1005 S23: 0.2983
REMARK 3 S31: 0.0025 S32: -0.1146 S33: -0.0490
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 40 THROUGH 80 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.1022 31.1588 31.8511
REMARK 3 T TENSOR
REMARK 3 T11: 0.1405 T22: 0.1096
REMARK 3 T33: 0.2008 T12: -0.0243
REMARK 3 T13: 0.0272 T23: -0.0127
REMARK 3 L TENSOR
REMARK 3 L11: 2.7927 L22: 2.1430
REMARK 3 L33: 3.0245 L12: -1.6826
REMARK 3 L13: 0.9117 L23: -1.1536
REMARK 3 S TENSOR
REMARK 3 S11: -0.0515 S12: -0.2568 S13: 0.0106
REMARK 3 S21: 0.1988 S22: 0.1536 S23: 0.2554
REMARK 3 S31: -0.1094 S32: -0.3932 S33: -0.0775
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 81 THROUGH 187 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.9209 43.1552 18.1317
REMARK 3 T TENSOR
REMARK 3 T11: 0.1853 T22: 0.1949
REMARK 3 T33: 0.1833 T12: 0.0695
REMARK 3 T13: -0.0105 T23: 0.0292
REMARK 3 L TENSOR
REMARK 3 L11: 0.8952 L22: 2.2507
REMARK 3 L33: 1.4644 L12: 0.0512
REMARK 3 L13: -0.1052 L23: 0.2641
REMARK 3 S TENSOR
REMARK 3 S11: 0.0507 S12: 0.1219 S13: 0.1308
REMARK 3 S21: -0.1289 S22: -0.0235 S23: 0.1429
REMARK 3 S31: -0.2615 S32: -0.1128 S33: -0.0121
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 188 THROUGH 215 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.6762 44.8337 10.8096
REMARK 3 T TENSOR
REMARK 3 T11: 0.2903 T22: 0.3611
REMARK 3 T33: 0.2318 T12: 0.0154
REMARK 3 T13: 0.0870 T23: 0.0358
REMARK 3 L TENSOR
REMARK 3 L11: 3.3478 L22: 1.3869
REMARK 3 L33: 1.1472 L12: 0.6558
REMARK 3 L13: 0.2982 L23: -0.0466
REMARK 3 S TENSOR
REMARK 3 S11: 0.0042 S12: 0.8062 S13: -0.0261
REMARK 3 S21: -0.3695 S22: 0.0254 S23: -0.2265
REMARK 3 S31: -0.2754 S32: 0.2511 S33: -0.0311
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 216 THROUGH 242 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.1532 31.3858 19.2715
REMARK 3 T TENSOR
REMARK 3 T11: 0.1847 T22: 0.1991
REMARK 3 T33: 0.2212 T12: -0.0056
REMARK 3 T13: 0.0233 T23: -0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 4.4567 L22: 8.4653
REMARK 3 L33: 0.0308 L12: 6.1251
REMARK 3 L13: 0.5343 L23: 0.7488
REMARK 3 S TENSOR
REMARK 3 S11: 0.0581 S12: 0.0003 S13: -0.0783
REMARK 3 S21: -0.0097 S22: -0.0081 S23: -0.3317
REMARK 3 S31: -0.0949 S32: 0.0568 S33: -0.1046
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 243 THROUGH 306 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.6382 26.9906 28.7041
REMARK 3 T TENSOR
REMARK 3 T11: 0.1815 T22: 0.1707
REMARK 3 T33: 0.1855 T12: 0.0227
REMARK 3 T13: -0.0049 T23: 0.0077
REMARK 3 L TENSOR
REMARK 3 L11: 1.1475 L22: 1.1325
REMARK 3 L33: 1.1072 L12: 0.1028
REMARK 3 L13: -0.0623 L23: 0.5123
REMARK 3 S TENSOR
REMARK 3 S11: 0.0223 S12: -0.0680 S13: -0.0146
REMARK 3 S21: 0.0834 S22: -0.0083 S23: 0.0579
REMARK 3 S31: -0.0296 S32: -0.0418 S33: -0.0083
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 307 THROUGH 341 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.7884 39.5148 12.5361
REMARK 3 T TENSOR
REMARK 3 T11: 0.2230 T22: 0.2784
REMARK 3 T33: 0.2171 T12: 0.0538
REMARK 3 T13: 0.0704 T23: 0.0470
REMARK 3 L TENSOR
REMARK 3 L11: 1.3745 L22: 4.0624
REMARK 3 L33: 0.7142 L12: 1.0387
REMARK 3 L13: 0.4334 L23: -0.7069
REMARK 3 S TENSOR
REMARK 3 S11: 0.0459 S12: 0.3618 S13: 0.0867
REMARK 3 S21: -0.5745 S22: -0.0023 S23: -0.3481
REMARK 3 S31: -0.0956 S32: 0.0150 S33: -0.0691
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 342 THROUGH 369 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.0314 48.2210 19.7189
REMARK 3 T TENSOR
REMARK 3 T11: 0.1958 T22: 0.1746
REMARK 3 T33: 0.2503 T12: -0.0273
REMARK 3 T13: -0.0211 T23: 0.0314
REMARK 3 L TENSOR
REMARK 3 L11: 4.5352 L22: 3.8946
REMARK 3 L33: 3.8474 L12: -0.6969
REMARK 3 L13: -1.5998 L23: -1.3488
REMARK 3 S TENSOR
REMARK 3 S11: 0.1121 S12: 0.2656 S13: 0.4696
REMARK 3 S21: -0.0212 S22: -0.1097 S23: -0.2597
REMARK 3 S31: -0.3969 S32: 0.1975 S33: -0.0182
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 370 THROUGH 390 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.9244 57.5355 20.0638
REMARK 3 T TENSOR
REMARK 3 T11: 0.4018 T22: 0.1884
REMARK 3 T33: 0.4467 T12: 0.0475
REMARK 3 T13: 0.0546 T23: 0.0871
REMARK 3 L TENSOR
REMARK 3 L11: 2.2256 L22: 3.1943
REMARK 3 L33: 3.4833 L12: -0.3156
REMARK 3 L13: 0.8305 L23: -1.3127
REMARK 3 S TENSOR
REMARK 3 S11: 0.1432 S12: 0.2999 S13: 0.7026
REMARK 3 S21: -0.2034 S22: -0.0738 S23: -0.2001
REMARK 3 S31: -0.7229 S32: 0.2169 S33: -0.0510
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 39 )
REMARK 3 ORIGIN FOR THE GROUP (A): 57.9726 43.1857 15.9175
REMARK 3 T TENSOR
REMARK 3 T11: 0.0765 T22: 0.1779
REMARK 3 T33: 0.2157 T12: -0.0352
REMARK 3 T13: -0.0052 T23: -0.0206
REMARK 3 L TENSOR
REMARK 3 L11: 0.5345 L22: 1.2140
REMARK 3 L33: 3.0746 L12: -0.1390
REMARK 3 L13: -1.1620 L23: -0.1836
REMARK 3 S TENSOR
REMARK 3 S11: 0.0582 S12: -0.0131 S13: 0.0869
REMARK 3 S21: -0.0425 S22: -0.0569 S23: -0.1201
REMARK 3 S31: -0.1678 S32: 0.0598 S33: -0.0022
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 40 THROUGH 80 )
REMARK 3 ORIGIN FOR THE GROUP (A): 58.9268 35.9778 8.7115
REMARK 3 T TENSOR
REMARK 3 T11: 0.1397 T22: 0.1389
REMARK 3 T33: 0.2070 T12: -0.0039
REMARK 3 T13: 0.0154 T23: 0.0162
REMARK 3 L TENSOR
REMARK 3 L11: 1.7048 L22: 1.5980
REMARK 3 L33: 3.8010 L12: 1.0592
REMARK 3 L13: 0.6808 L23: 1.4940
REMARK 3 S TENSOR
REMARK 3 S11: -0.0669 S12: 0.1035 S13: 0.0578
REMARK 3 S21: -0.1054 S22: 0.1176 S23: -0.1231
REMARK 3 S31: -0.1112 S32: 0.3257 S33: -0.0635
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 81 THROUGH 164 )
REMARK 3 ORIGIN FOR THE GROUP (A): 51.6144 21.1079 4.4758
REMARK 3 T TENSOR
REMARK 3 T11: 0.2078 T22: 0.1884
REMARK 3 T33: 0.1436 T12: -0.0204
REMARK 3 T13: 0.0164 T23: -0.0158
REMARK 3 L TENSOR
REMARK 3 L11: 1.9693 L22: 2.6191
REMARK 3 L33: 2.5815 L12: -0.1884
REMARK 3 L13: -0.8989 L23: 0.1526
REMARK 3 S TENSOR
REMARK 3 S11: -0.0878 S12: 0.1031 S13: -0.0803
REMARK 3 S21: -0.1505 S22: -0.0329 S23: -0.1277
REMARK 3 S31: 0.4353 S32: 0.0526 S33: 0.0956
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 165 THROUGH 215 )
REMARK 3 ORIGIN FOR THE GROUP (A): 43.6326 13.3431 15.9943
REMARK 3 T TENSOR
REMARK 3 T11: 0.2479 T22: 0.2375
REMARK 3 T33: 0.2545 T12: -0.0832
REMARK 3 T13: 0.0295 T23: -0.0233
REMARK 3 L TENSOR
REMARK 3 L11: 1.3351 L22: 1.8916
REMARK 3 L33: 3.2661 L12: -0.1608
REMARK 3 L13: 0.3115 L23: -0.2610
REMARK 3 S TENSOR
REMARK 3 S11: -0.0902 S12: 0.0205 S13: -0.2458
REMARK 3 S21: 0.0173 S22: 0.1390 S23: 0.1225
REMARK 3 S31: 0.4314 S32: -0.3837 S33: -0.0225
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 216 THROUGH 242 )
REMARK 3 ORIGIN FOR THE GROUP (A): 45.5969 24.3503 30.7489
REMARK 3 T TENSOR
REMARK 3 T11: 0.2185 T22: 0.2707
REMARK 3 T33: 0.2593 T12: -0.0569
REMARK 3 T13: 0.0126 T23: -0.0257
REMARK 3 L TENSOR
REMARK 3 L11: 1.2253 L22: 3.4763
REMARK 3 L33: 1.4877 L12: -1.8194
REMARK 3 L13: 0.4774 L23: -0.5624
REMARK 3 S TENSOR
REMARK 3 S11: -0.0415 S12: -0.1727 S13: 0.0170
REMARK 3 S21: 0.2003 S22: 0.1089 S23: -0.0196
REMARK 3 S31: 0.1469 S32: -0.0622 S33: -0.0449
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 243 THROUGH 306 )
REMARK 3 ORIGIN FOR THE GROUP (A): 53.8441 35.7326 19.2452
REMARK 3 T TENSOR
REMARK 3 T11: 0.1599 T22: 0.2253
REMARK 3 T33: 0.2084 T12: -0.0340
REMARK 3 T13: 0.0008 T23: -0.0362
REMARK 3 L TENSOR
REMARK 3 L11: 0.3733 L22: 2.2571
REMARK 3 L33: 1.1183 L12: -0.3368
REMARK 3 L13: -0.3616 L23: -0.4873
REMARK 3 S TENSOR
REMARK 3 S11: -0.0164 S12: -0.0079 S13: 0.0406
REMARK 3 S21: 0.0640 S22: -0.0224 S23: -0.1390
REMARK 3 S31: -0.0400 S32: 0.1175 S33: 0.0384
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 307 THROUGH 341 )
REMARK 3 ORIGIN FOR THE GROUP (A): 42.5317 16.7172 22.6639
REMARK 3 T TENSOR
REMARK 3 T11: 0.2562 T22: 0.2968
REMARK 3 T33: 0.2201 T12: -0.0873
REMARK 3 T13: 0.0521 T23: -0.0222
REMARK 3 L TENSOR
REMARK 3 L11: 0.2957 L22: 4.3938
REMARK 3 L33: 1.4009 L12: 0.1166
REMARK 3 L13: 0.4757 L23: -0.0972
REMARK 3 S TENSOR
REMARK 3 S11: 0.0076 S12: -0.0899 S13: 0.0247
REMARK 3 S21: 0.2271 S22: -0.0247 S23: 0.3621
REMARK 3 S31: 0.2567 S32: -0.3338 S33: 0.0720
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 342 THROUGH 387 )
REMARK 3 ORIGIN FOR THE GROUP (A): 54.2602 9.5537 17.5459
REMARK 3 T TENSOR
REMARK 3 T11: 0.3345 T22: 0.1817
REMARK 3 T33: 0.2335 T12: 0.0320
REMARK 3 T13: -0.0105 T23: 0.0232
REMARK 3 L TENSOR
REMARK 3 L11: 4.1453 L22: 3.5691
REMARK 3 L33: 2.4641 L12: 1.9915
REMARK 3 L13: -0.2915 L23: 0.5470
REMARK 3 S TENSOR
REMARK 3 S11: 0.0357 S12: -0.0448 S13: -0.4576
REMARK 3 S21: -0.1049 S22: -0.0491 S23: -0.3126
REMARK 3 S31: 0.6021 S32: 0.0414 S33: 0.0122
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 65 )
REMARK 3 ORIGIN FOR THE GROUP (A): 43.6248 59.3022 24.1425
REMARK 3 T TENSOR
REMARK 3 T11: 0.2441 T22: 0.1438
REMARK 3 T33: 0.2496 T12: 0.0050
REMARK 3 T13: 0.0505 T23: 0.0058
REMARK 3 L TENSOR
REMARK 3 L11: 1.3484 L22: 2.3049
REMARK 3 L33: 2.4279 L12: 0.2679
REMARK 3 L13: -0.1651 L23: 0.7252
REMARK 3 S TENSOR
REMARK 3 S11: 0.0962 S12: 0.0285 S13: 0.2253
REMARK 3 S21: 0.1000 S22: 0.0252 S23: 0.0240
REMARK 3 S31: -0.4226 S32: 0.0330 S33: -0.0635
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 66 THROUGH 187 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.5363 57.1458 49.4939
REMARK 3 T TENSOR
REMARK 3 T11: 0.4877 T22: 0.2810
REMARK 3 T33: 0.2472 T12: -0.0625
REMARK 3 T13: 0.0672 T23: -0.0960
REMARK 3 L TENSOR
REMARK 3 L11: 1.5704 L22: 1.7108
REMARK 3 L33: 1.5445 L12: -0.4225
REMARK 3 L13: -0.3979 L23: 0.1653
REMARK 3 S TENSOR
REMARK 3 S11: 0.1344 S12: -0.2693 S13: 0.2295
REMARK 3 S21: 0.3707 S22: -0.0464 S23: 0.1074
REMARK 3 S31: -0.5170 S32: 0.0104 S33: -0.0914
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 188 THROUGH 231 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.1879 38.0803 44.5890
REMARK 3 T TENSOR
REMARK 3 T11: 0.2681 T22: 0.2370
REMARK 3 T33: 0.2990 T12: 0.0318
REMARK 3 T13: 0.0316 T23: 0.0776
REMARK 3 L TENSOR
REMARK 3 L11: 4.0663 L22: 3.2593
REMARK 3 L33: 2.9089 L12: 2.3402
REMARK 3 L13: 1.6727 L23: 2.0579
REMARK 3 S TENSOR
REMARK 3 S11: 0.2199 S12: -0.2765 S13: -0.5254
REMARK 3 S21: 0.3545 S22: 0.0279 S23: -0.1247
REMARK 3 S31: -0.0497 S32: -0.2739 S33: -0.2447
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 232 THROUGH 325 )
REMARK 3 ORIGIN FOR THE GROUP (A): 40.6509 46.5067 33.0402
REMARK 3 T TENSOR
REMARK 3 T11: 0.2467 T22: 0.2293
REMARK 3 T33: 0.2346 T12: -0.0250
REMARK 3 T13: 0.0214 T23: -0.0450
REMARK 3 L TENSOR
REMARK 3 L11: 1.4534 L22: 0.6276
REMARK 3 L33: 1.0151 L12: 0.1268
REMARK 3 L13: -0.3982 L23: -0.1273
REMARK 3 S TENSOR
REMARK 3 S11: 0.0648 S12: -0.1092 S13: 0.0554
REMARK 3 S21: 0.1612 S22: -0.0025 S23: 0.0616
REMARK 3 S31: -0.1428 S32: -0.0001 S33: -0.0424
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 326 THROUGH 391 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.9659 49.9070 48.5298
REMARK 3 T TENSOR
REMARK 3 T11: 0.3771 T22: 0.2899
REMARK 3 T33: 0.2642 T12: 0.0567
REMARK 3 T13: 0.1139 T23: -0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 2.1043 L22: 2.6554
REMARK 3 L33: 2.2110 L12: 0.3591
REMARK 3 L13: 0.1815 L23: 1.1818
REMARK 3 S TENSOR
REMARK 3 S11: 0.1798 S12: -0.2983 S13: 0.1309
REMARK 3 S21: 0.4008 S22: 0.0078 S23: 0.2212
REMARK 3 S31: -0.3874 S32: -0.4463 S33: -0.1744
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 1 THROUGH 164 )
REMARK 3 ORIGIN FOR THE GROUP (A): 81.2867 7.5290 52.7903
REMARK 3 T TENSOR
REMARK 3 T11: 0.3506 T22: 0.2048
REMARK 3 T33: 0.2954 T12: 0.0644
REMARK 3 T13: 0.0944 T23: 0.0740
REMARK 3 L TENSOR
REMARK 3 L11: 1.4259 L22: 1.5103
REMARK 3 L33: 0.5527 L12: 0.5405
REMARK 3 L13: -0.3495 L23: 0.1656
REMARK 3 S TENSOR
REMARK 3 S11: -0.1822 S12: -0.0350 S13: -0.3341
REMARK 3 S21: -0.1642 S22: -0.0167 S23: -0.4194
REMARK 3 S31: 0.1746 S32: 0.0907 S33: 0.1808
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 165 THROUGH 215 )
REMARK 3 ORIGIN FOR THE GROUP (A): 84.1055 29.1823 53.3608
REMARK 3 T TENSOR
REMARK 3 T11: 0.2454 T22: 0.1482
REMARK 3 T33: 0.1670 T12: 0.0192
REMARK 3 T13: 0.0286 T23: 0.0108
REMARK 3 L TENSOR
REMARK 3 L11: 3.6661 L22: 4.2634
REMARK 3 L33: 3.8723 L12: -0.9636
REMARK 3 L13: 2.3371 L23: -2.3554
REMARK 3 S TENSOR
REMARK 3 S11: -0.2717 S12: -0.2334 S13: 0.1651
REMARK 3 S21: 0.0238 S22: 0.2065 S23: -0.1177
REMARK 3 S31: -0.3763 S32: -0.1331 S33: 0.0218
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 216 THROUGH 306 )
REMARK 3 ORIGIN FOR THE GROUP (A): 68.2505 14.5792 52.8684
REMARK 3 T TENSOR
REMARK 3 T11: 0.2659 T22: 0.1653
REMARK 3 T33: 0.1494 T12: 0.0193
REMARK 3 T13: 0.0240 T23: 0.0120
REMARK 3 L TENSOR
REMARK 3 L11: 1.1351 L22: 1.5995
REMARK 3 L33: 0.5533 L12: 0.0651
REMARK 3 L13: -0.3710 L23: 0.1552
REMARK 3 S TENSOR
REMARK 3 S11: -0.0681 S12: 0.0408 S13: -0.0796
REMARK 3 S21: -0.1483 S22: -0.0909 S23: -0.0369
REMARK 3 S31: 0.1038 S32: 0.0131 S33: 0.1550
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 307 THROUGH 341 )
REMARK 3 ORIGIN FOR THE GROUP (A): 76.9295 30.4920 53.9703
REMARK 3 T TENSOR
REMARK 3 T11: 0.2791 T22: 0.1599
REMARK 3 T33: 0.2210 T12: 0.0270
REMARK 3 T13: 0.0073 T23: -0.0185
REMARK 3 L TENSOR
REMARK 3 L11: 4.5001 L22: 2.4953
REMARK 3 L33: 1.2184 L12: 1.9222
REMARK 3 L13: -1.6069 L23: -1.6649
REMARK 3 S TENSOR
REMARK 3 S11: 0.2993 S12: -0.4918 S13: 0.3952
REMARK 3 S21: 0.1396 S22: -0.0906 S23: 0.0088
REMARK 3 S31: -0.3513 S32: 0.1131 S33: -0.2144
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 342 THROUGH 388 )
REMARK 3 ORIGIN FOR THE GROUP (A): 85.1426 27.2968 42.1365
REMARK 3 T TENSOR
REMARK 3 T11: 0.3327 T22: 0.1760
REMARK 3 T33: 0.1913 T12: 0.0200
REMARK 3 T13: 0.0931 T23: 0.0542
REMARK 3 L TENSOR
REMARK 3 L11: 1.9990 L22: 4.4232
REMARK 3 L33: 0.5893 L12: 0.7410
REMARK 3 L13: -0.2638 L23: -0.0043
REMARK 3 S TENSOR
REMARK 3 S11: -0.1003 S12: 0.0594 S13: -0.0385
REMARK 3 S21: -0.3613 S22: -0.0035 S23: -0.3619
REMARK 3 S31: 0.0886 S32: 0.0543 S33: 0.0911
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 5F4Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1000216025.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-AUG-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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) : 0.97915
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 : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 177945
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.820
REMARK 200 RESOLUTION RANGE LOW (A) : 34.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 31.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.82
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.66100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.320
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.16M MGCL2, 0.08M TRIS:HCL, 24% (W/V)
REMARK 280 PEG 4000, 20% (V/V) GLYCEROL, PH 8.5, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 89.67800
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.53400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 89.67800
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 46.53400
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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 BIOMT1 2 -1.000000 0.000000 0.000000 122.00138
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 121.17039
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 HIS A 389
REMARK 465 HIS A 390
REMARK 465 HIS A 391
REMARK 465 HIS A 392
REMARK 465 HIS A 393
REMARK 465 HIS B 391
REMARK 465 HIS B 392
REMARK 465 HIS B 393
REMARK 465 HIS C 388
REMARK 465 HIS C 389
REMARK 465 HIS C 390
REMARK 465 HIS C 391
REMARK 465 HIS C 392
REMARK 465 HIS C 393
REMARK 465 HIS D 392
REMARK 465 HIS D 393
REMARK 465 HIS E 389
REMARK 465 HIS E 390
REMARK 465 HIS E 391
REMARK 465 HIS E 392
REMARK 465 HIS E 393
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 168 CZ NH1 NH2
REMARK 470 ARG B 168 CD NE CZ NH1 NH2
REMARK 470 ASP C 89 CG OD1 OD2
REMARK 470 HIS D 391 CG ND1 CD2 CE1 NE2
REMARK 470 HIS E 388 CG ND1 CD2 CE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP A 157 CB TRP A 157 CG -0.116
REMARK 500 TRP A 157 CE3 TRP A 157 CZ3 -0.109
REMARK 500 TRP C 157 CB TRP C 157 CG -0.125
REMARK 500 TRP E 157 CB TRP E 157 CG -0.129
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 ASP A 89 5.30 -69.66
REMARK 500 PRO A 100 54.95 -96.25
REMARK 500 ASP A 175 -138.26 52.11
REMARK 500 ASP A 272 -75.52 -122.14
REMARK 500 PHE A 364 63.44 -106.20
REMARK 500 ASP B 89 41.99 -88.92
REMARK 500 PRO B 100 53.58 -96.26
REMARK 500 ASN B 149 -167.14 -102.32
REMARK 500 ASP B 175 -136.23 48.98
REMARK 500 PRO B 208 -2.07 -59.56
REMARK 500 ASP B 272 -53.76 -134.91
REMARK 500 PHE B 364 69.15 -106.61
REMARK 500 ASP C 89 23.52 -77.66
REMARK 500 PRO C 100 51.72 -98.86
REMARK 500 ASP C 175 -138.57 51.34
REMARK 500 GLN C 223 -34.64 -38.65
REMARK 500 ASP C 272 -76.87 -114.07
REMARK 500 PHE C 364 67.15 -104.49
REMARK 500 ASP D 89 30.16 -83.50
REMARK 500 PRO D 100 54.59 -97.26
REMARK 500 HIS D 119 42.34 -141.33
REMARK 500 ASN D 149 -164.11 -102.40
REMARK 500 ASP D 175 -141.10 53.10
REMARK 500 ASP D 272 -45.72 -138.00
REMARK 500 PHE D 364 65.81 -105.96
REMARK 500 HIS D 389 -87.01 -45.22
REMARK 500 HIS D 390 31.44 -59.10
REMARK 500 ASP E 89 43.52 -104.54
REMARK 500 PRO E 100 60.00 -100.35
REMARK 500 ASN E 149 -167.19 -103.19
REMARK 500 ASP E 175 -138.74 53.04
REMARK 500 ASP E 272 -76.10 -123.97
REMARK 500 PHE E 364 67.55 -105.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5V4 A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5V4 B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5V4 C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5V4 D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL E 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5V4 E 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MCSG-APC109148 RELATED DB: TARGETTRACK
REMARK 900 RELATED ID: NATPRO-GO.119842 RELATED DB: TARGETTRACK
DBREF 5F4Z A 1 387 UNP Q84HB1 Q84HB1_STRCZ 1 387
DBREF 5F4Z B 1 387 UNP Q84HB1 Q84HB1_STRCZ 1 387
DBREF 5F4Z C 1 387 UNP Q84HB1 Q84HB1_STRCZ 1 387
DBREF 5F4Z D 1 387 UNP Q84HB1 Q84HB1_STRCZ 1 387
DBREF 5F4Z E 1 387 UNP Q84HB1 Q84HB1_STRCZ 1 387
SEQADV 5F4Z HIS A 388 UNP Q84HB1 EXPRESSION TAG
SEQADV 5F4Z HIS A 389 UNP Q84HB1 EXPRESSION TAG
SEQADV 5F4Z HIS A 390 UNP Q84HB1 EXPRESSION TAG
SEQADV 5F4Z HIS A 391 UNP Q84HB1 EXPRESSION TAG
SEQADV 5F4Z HIS A 392 UNP Q84HB1 EXPRESSION TAG
SEQADV 5F4Z HIS A 393 UNP Q84HB1 EXPRESSION TAG
SEQADV 5F4Z HIS B 388 UNP Q84HB1 EXPRESSION TAG
SEQADV 5F4Z HIS B 389 UNP Q84HB1 EXPRESSION TAG
SEQADV 5F4Z HIS B 390 UNP Q84HB1 EXPRESSION TAG
SEQADV 5F4Z HIS B 391 UNP Q84HB1 EXPRESSION TAG
SEQADV 5F4Z HIS B 392 UNP Q84HB1 EXPRESSION TAG
SEQADV 5F4Z HIS B 393 UNP Q84HB1 EXPRESSION TAG
SEQADV 5F4Z HIS C 388 UNP Q84HB1 EXPRESSION TAG
SEQADV 5F4Z HIS C 389 UNP Q84HB1 EXPRESSION TAG
SEQADV 5F4Z HIS C 390 UNP Q84HB1 EXPRESSION TAG
SEQADV 5F4Z HIS C 391 UNP Q84HB1 EXPRESSION TAG
SEQADV 5F4Z HIS C 392 UNP Q84HB1 EXPRESSION TAG
SEQADV 5F4Z HIS C 393 UNP Q84HB1 EXPRESSION TAG
SEQADV 5F4Z HIS D 388 UNP Q84HB1 EXPRESSION TAG
SEQADV 5F4Z HIS D 389 UNP Q84HB1 EXPRESSION TAG
SEQADV 5F4Z HIS D 390 UNP Q84HB1 EXPRESSION TAG
SEQADV 5F4Z HIS D 391 UNP Q84HB1 EXPRESSION TAG
SEQADV 5F4Z HIS D 392 UNP Q84HB1 EXPRESSION TAG
SEQADV 5F4Z HIS D 393 UNP Q84HB1 EXPRESSION TAG
SEQADV 5F4Z HIS E 388 UNP Q84HB1 EXPRESSION TAG
SEQADV 5F4Z HIS E 389 UNP Q84HB1 EXPRESSION TAG
SEQADV 5F4Z HIS E 390 UNP Q84HB1 EXPRESSION TAG
SEQADV 5F4Z HIS E 391 UNP Q84HB1 EXPRESSION TAG
SEQADV 5F4Z HIS E 392 UNP Q84HB1 EXPRESSION TAG
SEQADV 5F4Z HIS E 393 UNP Q84HB1 EXPRESSION TAG
SEQRES 1 A 393 MSE GLU PRO PHE ARG ILE VAL ILE PRO GLN ALA ASP LEU
SEQRES 2 A 393 ASP ASP LEU HIS ARG ARG LEU ASP ALA THR ARG TRP PRO
SEQRES 3 A 393 SER GLU ILE PRO GLY THR GLY TRP SER ARG GLY VAL PRO
SEQRES 4 A 393 LEU ASP TYR LEU LYS GLU LEU VAL GLY TYR TRP ARG ASP
SEQRES 5 A 393 GLY TYR ASP TRP ARG ALA ALA GLU ASP ARG LEU ASN THR
SEQRES 6 A 393 VAL PRO GLN PHE THR THR GLU ILE ASP GLY THR ASN VAL
SEQRES 7 A 393 HIS PHE MSE HIS ILE ARG SER ALA GLU PRO ASP ALA LEU
SEQRES 8 A 393 PRO MSE ILE ILE THR HIS GLY TRP PRO GLY SER VAL ALA
SEQRES 9 A 393 GLU PHE LEU ASP VAL ILE ASP PRO LEU THR ASN PRO ARG
SEQRES 10 A 393 ALA HIS GLY GLY ASP PRO ALA ASP ALA PHE HIS LEU VAL
SEQRES 11 A 393 ILE PRO SER LEU PRO GLY PHE GLY PHE SER GLY PRO THR
SEQRES 12 A 393 PRO GLU PRO GLY TRP ASN LEU PRO ARG VAL ALA SER ALA
SEQRES 13 A 393 TRP ALA GLU LEU MSE ARG ARG LEU GLY TYR SER ARG TYR
SEQRES 14 A 393 ALA VAL GLN GLY GLY ASP LEU GLY ALA TRP THR SER LEU
SEQRES 15 A 393 THR LEU SER GLY VAL ASP HIS GLU HIS VAL VAL GLY THR
SEQRES 16 A 393 HIS VAL ASN PHE LEU ILE THR PRO PRO SER GLY ASP PRO
SEQRES 17 A 393 ALA ASP LEU ALA GLY LEU GLY GLU GLN ASP LEU ALA ARG
SEQRES 18 A 393 LEU GLN LEU LEU ALA GLU PHE GLY ALA GLU GLY SER GLY
SEQRES 19 A 393 TYR MSE LYS ILE GLN SER THR ARG PRO GLN THR LEU SER
SEQRES 20 A 393 TYR SER LEU THR ASP SER PRO VAL GLY GLN LEU ALA TRP
SEQRES 21 A 393 VAL VAL GLU LYS PHE MSE GLU TRP GLY ASP THR ASP LYS
SEQRES 22 A 393 SER PRO GLU ASP ALA VAL ASP ARG ASP ARG LEU LEU THR
SEQRES 23 A 393 ASN VAL MSE ILE TYR TRP LEU THR ALA THR ALA GLY SER
SEQRES 24 A 393 SER ALA HIS PHE TYR TYR GLU ILE SER ASP VAL LEU PRO
SEQRES 25 A 393 THR ALA PRO THR PRO PRO PRO PRO ALA PRO PRO LEU PRO
SEQRES 26 A 393 THR PRO LEU GLY VAL ALA VAL TYR PRO ALA ASP SER ALA
SEQRES 27 A 393 LYS PRO VAL ARG ARG PHE ALA GLU ARG ALA PHE PRO ASN
SEQRES 28 A 393 ILE VAL HIS TRP ALA GLU LEU GLU ARG GLY GLY HIS PHE
SEQRES 29 A 393 ALA ALA LEU GLU GLN PRO GLY LEU PHE VAL SER ASP LEU
SEQRES 30 A 393 ARG ALA PHE ALA ARG ALA LEU ARG THR SER HIS HIS HIS
SEQRES 31 A 393 HIS HIS HIS
SEQRES 1 B 393 MSE GLU PRO PHE ARG ILE VAL ILE PRO GLN ALA ASP LEU
SEQRES 2 B 393 ASP ASP LEU HIS ARG ARG LEU ASP ALA THR ARG TRP PRO
SEQRES 3 B 393 SER GLU ILE PRO GLY THR GLY TRP SER ARG GLY VAL PRO
SEQRES 4 B 393 LEU ASP TYR LEU LYS GLU LEU VAL GLY TYR TRP ARG ASP
SEQRES 5 B 393 GLY TYR ASP TRP ARG ALA ALA GLU ASP ARG LEU ASN THR
SEQRES 6 B 393 VAL PRO GLN PHE THR THR GLU ILE ASP GLY THR ASN VAL
SEQRES 7 B 393 HIS PHE MSE HIS ILE ARG SER ALA GLU PRO ASP ALA LEU
SEQRES 8 B 393 PRO MSE ILE ILE THR HIS GLY TRP PRO GLY SER VAL ALA
SEQRES 9 B 393 GLU PHE LEU ASP VAL ILE ASP PRO LEU THR ASN PRO ARG
SEQRES 10 B 393 ALA HIS GLY GLY ASP PRO ALA ASP ALA PHE HIS LEU VAL
SEQRES 11 B 393 ILE PRO SER LEU PRO GLY PHE GLY PHE SER GLY PRO THR
SEQRES 12 B 393 PRO GLU PRO GLY TRP ASN LEU PRO ARG VAL ALA SER ALA
SEQRES 13 B 393 TRP ALA GLU LEU MSE ARG ARG LEU GLY TYR SER ARG TYR
SEQRES 14 B 393 ALA VAL GLN GLY GLY ASP LEU GLY ALA TRP THR SER LEU
SEQRES 15 B 393 THR LEU SER GLY VAL ASP HIS GLU HIS VAL VAL GLY THR
SEQRES 16 B 393 HIS VAL ASN PHE LEU ILE THR PRO PRO SER GLY ASP PRO
SEQRES 17 B 393 ALA ASP LEU ALA GLY LEU GLY GLU GLN ASP LEU ALA ARG
SEQRES 18 B 393 LEU GLN LEU LEU ALA GLU PHE GLY ALA GLU GLY SER GLY
SEQRES 19 B 393 TYR MSE LYS ILE GLN SER THR ARG PRO GLN THR LEU SER
SEQRES 20 B 393 TYR SER LEU THR ASP SER PRO VAL GLY GLN LEU ALA TRP
SEQRES 21 B 393 VAL VAL GLU LYS PHE MSE GLU TRP GLY ASP THR ASP LYS
SEQRES 22 B 393 SER PRO GLU ASP ALA VAL ASP ARG ASP ARG LEU LEU THR
SEQRES 23 B 393 ASN VAL MSE ILE TYR TRP LEU THR ALA THR ALA GLY SER
SEQRES 24 B 393 SER ALA HIS PHE TYR TYR GLU ILE SER ASP VAL LEU PRO
SEQRES 25 B 393 THR ALA PRO THR PRO PRO PRO PRO ALA PRO PRO LEU PRO
SEQRES 26 B 393 THR PRO LEU GLY VAL ALA VAL TYR PRO ALA ASP SER ALA
SEQRES 27 B 393 LYS PRO VAL ARG ARG PHE ALA GLU ARG ALA PHE PRO ASN
SEQRES 28 B 393 ILE VAL HIS TRP ALA GLU LEU GLU ARG GLY GLY HIS PHE
SEQRES 29 B 393 ALA ALA LEU GLU GLN PRO GLY LEU PHE VAL SER ASP LEU
SEQRES 30 B 393 ARG ALA PHE ALA ARG ALA LEU ARG THR SER HIS HIS HIS
SEQRES 31 B 393 HIS HIS HIS
SEQRES 1 C 393 MSE GLU PRO PHE ARG ILE VAL ILE PRO GLN ALA ASP LEU
SEQRES 2 C 393 ASP ASP LEU HIS ARG ARG LEU ASP ALA THR ARG TRP PRO
SEQRES 3 C 393 SER GLU ILE PRO GLY THR GLY TRP SER ARG GLY VAL PRO
SEQRES 4 C 393 LEU ASP TYR LEU LYS GLU LEU VAL GLY TYR TRP ARG ASP
SEQRES 5 C 393 GLY TYR ASP TRP ARG ALA ALA GLU ASP ARG LEU ASN THR
SEQRES 6 C 393 VAL PRO GLN PHE THR THR GLU ILE ASP GLY THR ASN VAL
SEQRES 7 C 393 HIS PHE MSE HIS ILE ARG SER ALA GLU PRO ASP ALA LEU
SEQRES 8 C 393 PRO MSE ILE ILE THR HIS GLY TRP PRO GLY SER VAL ALA
SEQRES 9 C 393 GLU PHE LEU ASP VAL ILE ASP PRO LEU THR ASN PRO ARG
SEQRES 10 C 393 ALA HIS GLY GLY ASP PRO ALA ASP ALA PHE HIS LEU VAL
SEQRES 11 C 393 ILE PRO SER LEU PRO GLY PHE GLY PHE SER GLY PRO THR
SEQRES 12 C 393 PRO GLU PRO GLY TRP ASN LEU PRO ARG VAL ALA SER ALA
SEQRES 13 C 393 TRP ALA GLU LEU MSE ARG ARG LEU GLY TYR SER ARG TYR
SEQRES 14 C 393 ALA VAL GLN GLY GLY ASP LEU GLY ALA TRP THR SER LEU
SEQRES 15 C 393 THR LEU SER GLY VAL ASP HIS GLU HIS VAL VAL GLY THR
SEQRES 16 C 393 HIS VAL ASN PHE LEU ILE THR PRO PRO SER GLY ASP PRO
SEQRES 17 C 393 ALA ASP LEU ALA GLY LEU GLY GLU GLN ASP LEU ALA ARG
SEQRES 18 C 393 LEU GLN LEU LEU ALA GLU PHE GLY ALA GLU GLY SER GLY
SEQRES 19 C 393 TYR MSE LYS ILE GLN SER THR ARG PRO GLN THR LEU SER
SEQRES 20 C 393 TYR SER LEU THR ASP SER PRO VAL GLY GLN LEU ALA TRP
SEQRES 21 C 393 VAL VAL GLU LYS PHE MSE GLU TRP GLY ASP THR ASP LYS
SEQRES 22 C 393 SER PRO GLU ASP ALA VAL ASP ARG ASP ARG LEU LEU THR
SEQRES 23 C 393 ASN VAL MSE ILE TYR TRP LEU THR ALA THR ALA GLY SER
SEQRES 24 C 393 SER ALA HIS PHE TYR TYR GLU ILE SER ASP VAL LEU PRO
SEQRES 25 C 393 THR ALA PRO THR PRO PRO PRO PRO ALA PRO PRO LEU PRO
SEQRES 26 C 393 THR PRO LEU GLY VAL ALA VAL TYR PRO ALA ASP SER ALA
SEQRES 27 C 393 LYS PRO VAL ARG ARG PHE ALA GLU ARG ALA PHE PRO ASN
SEQRES 28 C 393 ILE VAL HIS TRP ALA GLU LEU GLU ARG GLY GLY HIS PHE
SEQRES 29 C 393 ALA ALA LEU GLU GLN PRO GLY LEU PHE VAL SER ASP LEU
SEQRES 30 C 393 ARG ALA PHE ALA ARG ALA LEU ARG THR SER HIS HIS HIS
SEQRES 31 C 393 HIS HIS HIS
SEQRES 1 D 393 MSE GLU PRO PHE ARG ILE VAL ILE PRO GLN ALA ASP LEU
SEQRES 2 D 393 ASP ASP LEU HIS ARG ARG LEU ASP ALA THR ARG TRP PRO
SEQRES 3 D 393 SER GLU ILE PRO GLY THR GLY TRP SER ARG GLY VAL PRO
SEQRES 4 D 393 LEU ASP TYR LEU LYS GLU LEU VAL GLY TYR TRP ARG ASP
SEQRES 5 D 393 GLY TYR ASP TRP ARG ALA ALA GLU ASP ARG LEU ASN THR
SEQRES 6 D 393 VAL PRO GLN PHE THR THR GLU ILE ASP GLY THR ASN VAL
SEQRES 7 D 393 HIS PHE MSE HIS ILE ARG SER ALA GLU PRO ASP ALA LEU
SEQRES 8 D 393 PRO MSE ILE ILE THR HIS GLY TRP PRO GLY SER VAL ALA
SEQRES 9 D 393 GLU PHE LEU ASP VAL ILE ASP PRO LEU THR ASN PRO ARG
SEQRES 10 D 393 ALA HIS GLY GLY ASP PRO ALA ASP ALA PHE HIS LEU VAL
SEQRES 11 D 393 ILE PRO SER LEU PRO GLY PHE GLY PHE SER GLY PRO THR
SEQRES 12 D 393 PRO GLU PRO GLY TRP ASN LEU PRO ARG VAL ALA SER ALA
SEQRES 13 D 393 TRP ALA GLU LEU MSE ARG ARG LEU GLY TYR SER ARG TYR
SEQRES 14 D 393 ALA VAL GLN GLY GLY ASP LEU GLY ALA TRP THR SER LEU
SEQRES 15 D 393 THR LEU SER GLY VAL ASP HIS GLU HIS VAL VAL GLY THR
SEQRES 16 D 393 HIS VAL ASN PHE LEU ILE THR PRO PRO SER GLY ASP PRO
SEQRES 17 D 393 ALA ASP LEU ALA GLY LEU GLY GLU GLN ASP LEU ALA ARG
SEQRES 18 D 393 LEU GLN LEU LEU ALA GLU PHE GLY ALA GLU GLY SER GLY
SEQRES 19 D 393 TYR MSE LYS ILE GLN SER THR ARG PRO GLN THR LEU SER
SEQRES 20 D 393 TYR SER LEU THR ASP SER PRO VAL GLY GLN LEU ALA TRP
SEQRES 21 D 393 VAL VAL GLU LYS PHE MSE GLU TRP GLY ASP THR ASP LYS
SEQRES 22 D 393 SER PRO GLU ASP ALA VAL ASP ARG ASP ARG LEU LEU THR
SEQRES 23 D 393 ASN VAL MSE ILE TYR TRP LEU THR ALA THR ALA GLY SER
SEQRES 24 D 393 SER ALA HIS PHE TYR TYR GLU ILE SER ASP VAL LEU PRO
SEQRES 25 D 393 THR ALA PRO THR PRO PRO PRO PRO ALA PRO PRO LEU PRO
SEQRES 26 D 393 THR PRO LEU GLY VAL ALA VAL TYR PRO ALA ASP SER ALA
SEQRES 27 D 393 LYS PRO VAL ARG ARG PHE ALA GLU ARG ALA PHE PRO ASN
SEQRES 28 D 393 ILE VAL HIS TRP ALA GLU LEU GLU ARG GLY GLY HIS PHE
SEQRES 29 D 393 ALA ALA LEU GLU GLN PRO GLY LEU PHE VAL SER ASP LEU
SEQRES 30 D 393 ARG ALA PHE ALA ARG ALA LEU ARG THR SER HIS HIS HIS
SEQRES 31 D 393 HIS HIS HIS
SEQRES 1 E 393 MSE GLU PRO PHE ARG ILE VAL ILE PRO GLN ALA ASP LEU
SEQRES 2 E 393 ASP ASP LEU HIS ARG ARG LEU ASP ALA THR ARG TRP PRO
SEQRES 3 E 393 SER GLU ILE PRO GLY THR GLY TRP SER ARG GLY VAL PRO
SEQRES 4 E 393 LEU ASP TYR LEU LYS GLU LEU VAL GLY TYR TRP ARG ASP
SEQRES 5 E 393 GLY TYR ASP TRP ARG ALA ALA GLU ASP ARG LEU ASN THR
SEQRES 6 E 393 VAL PRO GLN PHE THR THR GLU ILE ASP GLY THR ASN VAL
SEQRES 7 E 393 HIS PHE MSE HIS ILE ARG SER ALA GLU PRO ASP ALA LEU
SEQRES 8 E 393 PRO MSE ILE ILE THR HIS GLY TRP PRO GLY SER VAL ALA
SEQRES 9 E 393 GLU PHE LEU ASP VAL ILE ASP PRO LEU THR ASN PRO ARG
SEQRES 10 E 393 ALA HIS GLY GLY ASP PRO ALA ASP ALA PHE HIS LEU VAL
SEQRES 11 E 393 ILE PRO SER LEU PRO GLY PHE GLY PHE SER GLY PRO THR
SEQRES 12 E 393 PRO GLU PRO GLY TRP ASN LEU PRO ARG VAL ALA SER ALA
SEQRES 13 E 393 TRP ALA GLU LEU MSE ARG ARG LEU GLY TYR SER ARG TYR
SEQRES 14 E 393 ALA VAL GLN GLY GLY ASP LEU GLY ALA TRP THR SER LEU
SEQRES 15 E 393 THR LEU SER GLY VAL ASP HIS GLU HIS VAL VAL GLY THR
SEQRES 16 E 393 HIS VAL ASN PHE LEU ILE THR PRO PRO SER GLY ASP PRO
SEQRES 17 E 393 ALA ASP LEU ALA GLY LEU GLY GLU GLN ASP LEU ALA ARG
SEQRES 18 E 393 LEU GLN LEU LEU ALA GLU PHE GLY ALA GLU GLY SER GLY
SEQRES 19 E 393 TYR MSE LYS ILE GLN SER THR ARG PRO GLN THR LEU SER
SEQRES 20 E 393 TYR SER LEU THR ASP SER PRO VAL GLY GLN LEU ALA TRP
SEQRES 21 E 393 VAL VAL GLU LYS PHE MSE GLU TRP GLY ASP THR ASP LYS
SEQRES 22 E 393 SER PRO GLU ASP ALA VAL ASP ARG ASP ARG LEU LEU THR
SEQRES 23 E 393 ASN VAL MSE ILE TYR TRP LEU THR ALA THR ALA GLY SER
SEQRES 24 E 393 SER ALA HIS PHE TYR TYR GLU ILE SER ASP VAL LEU PRO
SEQRES 25 E 393 THR ALA PRO THR PRO PRO PRO PRO ALA PRO PRO LEU PRO
SEQRES 26 E 393 THR PRO LEU GLY VAL ALA VAL TYR PRO ALA ASP SER ALA
SEQRES 27 E 393 LYS PRO VAL ARG ARG PHE ALA GLU ARG ALA PHE PRO ASN
SEQRES 28 E 393 ILE VAL HIS TRP ALA GLU LEU GLU ARG GLY GLY HIS PHE
SEQRES 29 E 393 ALA ALA LEU GLU GLN PRO GLY LEU PHE VAL SER ASP LEU
SEQRES 30 E 393 ARG ALA PHE ALA ARG ALA LEU ARG THR SER HIS HIS HIS
SEQRES 31 E 393 HIS HIS HIS
MODRES 5F4Z MSE A 1 MET MODIFIED RESIDUE
MODRES 5F4Z MSE A 81 MET MODIFIED RESIDUE
MODRES 5F4Z MSE A 93 MET MODIFIED RESIDUE
MODRES 5F4Z MSE A 161 MET MODIFIED RESIDUE
MODRES 5F4Z MSE A 236 MET MODIFIED RESIDUE
MODRES 5F4Z MSE A 266 MET MODIFIED RESIDUE
MODRES 5F4Z MSE A 289 MET MODIFIED RESIDUE
MODRES 5F4Z MSE B 1 MET MODIFIED RESIDUE
MODRES 5F4Z MSE B 81 MET MODIFIED RESIDUE
MODRES 5F4Z MSE B 93 MET MODIFIED RESIDUE
MODRES 5F4Z MSE B 161 MET MODIFIED RESIDUE
MODRES 5F4Z MSE B 236 MET MODIFIED RESIDUE
MODRES 5F4Z MSE B 266 MET MODIFIED RESIDUE
MODRES 5F4Z MSE B 289 MET MODIFIED RESIDUE
MODRES 5F4Z MSE C 1 MET MODIFIED RESIDUE
MODRES 5F4Z MSE C 81 MET MODIFIED RESIDUE
MODRES 5F4Z MSE C 93 MET MODIFIED RESIDUE
MODRES 5F4Z MSE C 161 MET MODIFIED RESIDUE
MODRES 5F4Z MSE C 236 MET MODIFIED RESIDUE
MODRES 5F4Z MSE C 266 MET MODIFIED RESIDUE
MODRES 5F4Z MSE C 289 MET MODIFIED RESIDUE
MODRES 5F4Z MSE D 1 MET MODIFIED RESIDUE
MODRES 5F4Z MSE D 81 MET MODIFIED RESIDUE
MODRES 5F4Z MSE D 93 MET MODIFIED RESIDUE
MODRES 5F4Z MSE D 161 MET MODIFIED RESIDUE
MODRES 5F4Z MSE D 236 MET MODIFIED RESIDUE
MODRES 5F4Z MSE D 266 MET MODIFIED RESIDUE
MODRES 5F4Z MSE D 289 MET MODIFIED RESIDUE
MODRES 5F4Z MSE E 1 MET MODIFIED RESIDUE
MODRES 5F4Z MSE E 81 MET MODIFIED RESIDUE
MODRES 5F4Z MSE E 93 MET MODIFIED RESIDUE
MODRES 5F4Z MSE E 161 MET MODIFIED RESIDUE
MODRES 5F4Z MSE E 236 MET MODIFIED RESIDUE
MODRES 5F4Z MSE E 266 MET MODIFIED RESIDUE
MODRES 5F4Z MSE E 289 MET MODIFIED RESIDUE
HET MSE A 1 8
HET MSE A 81 8
HET MSE A 93 8
HET MSE A 161 8
HET MSE A 236 8
HET MSE A 266 8
HET MSE A 289 8
HET MSE B 1 8
HET MSE B 81 8
HET MSE B 93 8
HET MSE B 161 8
HET MSE B 236 8
HET MSE B 266 8
HET MSE B 289 8
HET MSE C 1 8
HET MSE C 81 8
HET MSE C 93 8
HET MSE C 161 8
HET MSE C 236 8
HET MSE C 266 8
HET MSE C 289 8
HET MSE D 1 8
HET MSE D 81 8
HET MSE D 93 8
HET MSE D 161 8
HET MSE D 236 8
HET MSE D 266 8
HET MSE D 289 8
HET MSE E 1 8
HET MSE E 81 8
HET MSE E 93 8
HET MSE E 161 8
HET MSE E 236 8
HET MSE E 266 8
HET MSE E 289 8
HET GOL A 401 6
HET GOL A 402 6
HET GOL A 403 6
HET GOL A 404 6
HET GOL A 405 6
HET ACT A 406 4
HET PEG A 407 7
HET 5V4 A 408 22
HET ACT B 401 4
HET PG4 B 402 13
HET TRS B 403 8
HET 5V4 B 404 22
HET GOL C 401 6
HET 5V4 C 402 22
HET 5V4 D 401 22
HET GOL E 401 6
HET 5V4 E 402 22
HETNAM MSE SELENOMETHIONINE
HETNAM GOL GLYCEROL
HETNAM ACT ACETATE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM 5V4 (1~{R},2~{R})-2,3-DIHYDRO-1~{H}-INDENE-1,2-DIOL
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN TRS TRIS BUFFER
FORMUL 1 MSE 35(C5 H11 N O2 SE)
FORMUL 6 GOL 7(C3 H8 O3)
FORMUL 11 ACT 2(C2 H3 O2 1-)
FORMUL 12 PEG C4 H10 O3
FORMUL 13 5V4 5(C9 H10 O2)
FORMUL 15 PG4 C8 H18 O5
FORMUL 16 TRS C4 H12 N O3 1+
FORMUL 23 HOH *1192(H2 O)
HELIX 1 AA1 PRO A 9 ALA A 22 1 14
HELIX 2 AA2 PRO A 39 GLY A 53 1 15
HELIX 3 AA3 ASP A 55 ASN A 64 1 10
HELIX 4 AA4 SER A 102 LEU A 107 5 6
HELIX 5 AA5 VAL A 109 ASN A 115 1 7
HELIX 6 AA6 PRO A 116 HIS A 119 5 4
HELIX 7 AA7 ASP A 122 ASP A 125 5 4
HELIX 8 AA8 ASN A 149 GLY A 165 1 17
HELIX 9 AA9 GLY A 174 ASP A 188 1 15
HELIX 10 AB1 ASP A 207 ALA A 212 5 6
HELIX 11 AB2 GLY A 215 GLY A 232 1 18
HELIX 12 AB3 SER A 233 SER A 240 1 8
HELIX 13 AB4 ARG A 242 SER A 253 1 12
HELIX 14 AB5 SER A 253 GLY A 269 1 17
HELIX 15 AB6 SER A 274 ALA A 278 5 5
HELIX 16 AB7 ASP A 280 ALA A 295 1 16
HELIX 17 AB8 THR A 296 ILE A 307 1 12
HELIX 18 AB9 SER A 308 LEU A 311 5 4
HELIX 19 AC1 VAL A 341 PHE A 349 1 9
HELIX 20 AC2 PHE A 364 GLN A 369 1 6
HELIX 21 AC3 GLN A 369 HIS A 388 1 20
HELIX 22 AC4 PRO B 9 ALA B 22 1 14
HELIX 23 AC5 PRO B 39 ASP B 52 1 14
HELIX 24 AC6 ASP B 55 ASN B 64 1 10
HELIX 25 AC7 SER B 102 LEU B 107 5 6
HELIX 26 AC8 VAL B 109 ASN B 115 1 7
HELIX 27 AC9 PRO B 116 HIS B 119 5 4
HELIX 28 AD1 ASP B 122 ASP B 125 5 4
HELIX 29 AD2 ASN B 149 GLY B 165 1 17
HELIX 30 AD3 GLY B 174 ASP B 188 1 15
HELIX 31 AD4 GLY B 215 GLY B 232 1 18
HELIX 32 AD5 SER B 233 SER B 240 1 8
HELIX 33 AD6 ARG B 242 SER B 253 1 12
HELIX 34 AD7 SER B 253 GLY B 269 1 17
HELIX 35 AD8 SER B 274 ALA B 278 5 5
HELIX 36 AD9 ASP B 280 ALA B 295 1 16
HELIX 37 AE1 THR B 296 ILE B 307 1 12
HELIX 38 AE2 SER B 308 LEU B 311 5 4
HELIX 39 AE3 VAL B 341 PHE B 349 1 9
HELIX 40 AE4 PHE B 364 GLN B 369 1 6
HELIX 41 AE5 GLN B 369 HIS B 390 1 22
HELIX 42 AE6 PRO C 9 ALA C 22 1 14
HELIX 43 AE7 PRO C 39 GLY C 53 1 15
HELIX 44 AE8 ASP C 55 ASN C 64 1 10
HELIX 45 AE9 SER C 102 LEU C 107 5 6
HELIX 46 AF1 VAL C 109 ASN C 115 1 7
HELIX 47 AF2 PRO C 116 HIS C 119 5 4
HELIX 48 AF3 ASP C 122 ASP C 125 5 4
HELIX 49 AF4 ASN C 149 LEU C 164 1 16
HELIX 50 AF5 GLY C 174 ASP C 188 1 15
HELIX 51 AF6 ASP C 207 ALA C 212 5 6
HELIX 52 AF7 GLY C 215 GLY C 232 1 18
HELIX 53 AF8 SER C 233 SER C 240 1 8
HELIX 54 AF9 ARG C 242 SER C 253 1 12
HELIX 55 AG1 SER C 253 GLY C 269 1 17
HELIX 56 AG2 SER C 274 ALA C 278 5 5
HELIX 57 AG3 ASP C 280 ALA C 295 1 16
HELIX 58 AG4 THR C 296 ILE C 307 1 12
HELIX 59 AG5 SER C 308 LEU C 311 5 4
HELIX 60 AG6 VAL C 341 PHE C 349 1 9
HELIX 61 AG7 PHE C 364 GLN C 369 1 6
HELIX 62 AG8 GLN C 369 SER C 387 1 19
HELIX 63 AG9 PRO D 9 ALA D 22 1 14
HELIX 64 AH1 PRO D 39 ASP D 52 1 14
HELIX 65 AH2 ASP D 55 ASN D 64 1 10
HELIX 66 AH3 SER D 102 LEU D 107 5 6
HELIX 67 AH4 VAL D 109 ASN D 115 1 7
HELIX 68 AH5 PRO D 116 GLY D 120 5 5
HELIX 69 AH6 ASP D 122 ASP D 125 5 4
HELIX 70 AH7 ASN D 149 GLY D 165 1 17
HELIX 71 AH8 GLY D 174 ASP D 188 1 15
HELIX 72 AH9 ASP D 207 ALA D 212 5 6
HELIX 73 AI1 GLY D 215 GLY D 232 1 18
HELIX 74 AI2 SER D 233 ARG D 242 1 10
HELIX 75 AI3 ARG D 242 SER D 253 1 12
HELIX 76 AI4 SER D 253 GLY D 269 1 17
HELIX 77 AI5 SER D 274 ALA D 278 5 5
HELIX 78 AI6 ASP D 280 ALA D 295 1 16
HELIX 79 AI7 THR D 296 ILE D 307 1 12
HELIX 80 AI8 SER D 308 LEU D 311 5 4
HELIX 81 AI9 VAL D 341 PHE D 349 1 9
HELIX 82 AJ1 PHE D 364 GLN D 369 1 6
HELIX 83 AJ2 GLN D 369 HIS D 390 1 22
HELIX 84 AJ3 PRO E 9 ALA E 22 1 14
HELIX 85 AJ4 PRO E 39 GLY E 53 1 15
HELIX 86 AJ5 ASP E 55 ASN E 64 1 10
HELIX 87 AJ6 SER E 102 LEU E 107 5 6
HELIX 88 AJ7 VAL E 109 ASN E 115 1 7
HELIX 89 AJ8 PRO E 116 HIS E 119 5 4
HELIX 90 AJ9 ASP E 122 ASP E 125 5 4
HELIX 91 AK1 ASN E 149 GLY E 165 1 17
HELIX 92 AK2 ASP E 175 ASP E 188 1 14
HELIX 93 AK3 ASP E 207 ALA E 212 5 6
HELIX 94 AK4 GLY E 215 GLY E 232 1 18
HELIX 95 AK5 SER E 233 SER E 240 1 8
HELIX 96 AK6 ARG E 242 SER E 253 1 12
HELIX 97 AK7 SER E 253 GLY E 269 1 17
HELIX 98 AK8 SER E 274 ALA E 278 5 5
HELIX 99 AK9 ASP E 280 ALA E 295 1 16
HELIX 100 AL1 THR E 296 ILE E 307 1 12
HELIX 101 AL2 SER E 308 LEU E 311 5 4
HELIX 102 AL3 VAL E 341 PHE E 349 1 9
HELIX 103 AL4 PHE E 364 GLN E 369 1 6
HELIX 104 AL5 GLN E 369 THR E 386 1 18
SHEET 1 AA1 9 GLU A 2 PHE A 4 0
SHEET 2 AA1 9 GLN A 68 ILE A 73 -1 O THR A 70 N GLU A 2
SHEET 3 AA1 9 THR A 76 ILE A 83 -1 O VAL A 78 N THR A 71
SHEET 4 AA1 9 PHE A 127 PRO A 132 -1 O LEU A 129 N ILE A 83
SHEET 5 AA1 9 LEU A 91 THR A 96 1 N MSE A 93 O HIS A 128
SHEET 6 AA1 9 TYR A 169 GLY A 173 1 O ALA A 170 N PRO A 92
SHEET 7 AA1 9 VAL A 192 VAL A 197 1 O HIS A 196 N VAL A 171
SHEET 8 AA1 9 LEU A 328 VAL A 332 1 O GLY A 329 N THR A 195
SHEET 9 AA1 9 ILE A 352 GLU A 357 1 O ALA A 356 N VAL A 332
SHEET 1 AA2 9 GLU B 2 PHE B 4 0
SHEET 2 AA2 9 GLN B 68 ILE B 73 -1 O THR B 70 N GLU B 2
SHEET 3 AA2 9 THR B 76 ILE B 83 -1 O THR B 76 N ILE B 73
SHEET 4 AA2 9 PHE B 127 PRO B 132 -1 O LEU B 129 N ILE B 83
SHEET 5 AA2 9 LEU B 91 THR B 96 1 N MSE B 93 O HIS B 128
SHEET 6 AA2 9 TYR B 169 GLY B 173 1 O ALA B 170 N PRO B 92
SHEET 7 AA2 9 VAL B 192 VAL B 197 1 O HIS B 196 N VAL B 171
SHEET 8 AA2 9 LEU B 328 VAL B 332 1 O GLY B 329 N THR B 195
SHEET 9 AA2 9 ILE B 352 GLU B 357 1 O ALA B 356 N VAL B 332
SHEET 1 AA3 9 GLU C 2 PHE C 4 0
SHEET 2 AA3 9 GLN C 68 ILE C 73 -1 O GLN C 68 N PHE C 4
SHEET 3 AA3 9 THR C 76 ILE C 83 -1 O VAL C 78 N THR C 71
SHEET 4 AA3 9 PHE C 127 PRO C 132 -1 O LEU C 129 N ILE C 83
SHEET 5 AA3 9 LEU C 91 THR C 96 1 N ILE C 95 O VAL C 130
SHEET 6 AA3 9 TYR C 169 GLY C 173 1 O ALA C 170 N PRO C 92
SHEET 7 AA3 9 VAL C 192 VAL C 197 1 O HIS C 196 N VAL C 171
SHEET 8 AA3 9 LEU C 328 VAL C 332 1 O GLY C 329 N THR C 195
SHEET 9 AA3 9 ILE C 352 GLU C 357 1 O ALA C 356 N VAL C 332
SHEET 1 AA4 9 GLU D 2 PHE D 4 0
SHEET 2 AA4 9 GLN D 68 ILE D 73 -1 O THR D 70 N GLU D 2
SHEET 3 AA4 9 THR D 76 ILE D 83 -1 O VAL D 78 N THR D 71
SHEET 4 AA4 9 PHE D 127 PRO D 132 -1 O LEU D 129 N ILE D 83
SHEET 5 AA4 9 LEU D 91 THR D 96 1 N MSE D 93 O HIS D 128
SHEET 6 AA4 9 TYR D 169 GLY D 173 1 O ALA D 170 N PRO D 92
SHEET 7 AA4 9 VAL D 192 VAL D 197 1 O HIS D 196 N VAL D 171
SHEET 8 AA4 9 LEU D 328 VAL D 332 1 O GLY D 329 N THR D 195
SHEET 9 AA4 9 ILE D 352 GLU D 357 1 O ALA D 356 N VAL D 332
SHEET 1 AA5 9 GLU E 2 PHE E 4 0
SHEET 2 AA5 9 GLN E 68 ILE E 73 -1 O GLN E 68 N PHE E 4
SHEET 3 AA5 9 THR E 76 ILE E 83 -1 O VAL E 78 N THR E 71
SHEET 4 AA5 9 PHE E 127 PRO E 132 -1 O LEU E 129 N ILE E 83
SHEET 5 AA5 9 LEU E 91 THR E 96 1 N MSE E 93 O HIS E 128
SHEET 6 AA5 9 TYR E 169 GLY E 173 1 O ALA E 170 N PRO E 92
SHEET 7 AA5 9 VAL E 192 VAL E 197 1 O HIS E 196 N VAL E 171
SHEET 8 AA5 9 LEU E 328 VAL E 332 1 O GLY E 329 N THR E 195
SHEET 9 AA5 9 ILE E 352 GLU E 357 1 O ALA E 356 N VAL E 332
LINK C MSE A 1 N GLU A 2 1555 1555 1.33
LINK C PHE A 80 N MSE A 81 1555 1555 1.33
LINK C MSE A 81 N HIS A 82 1555 1555 1.32
LINK C PRO A 92 N MSE A 93 1555 1555 1.32
LINK C MSE A 93 N ILE A 94 1555 1555 1.33
LINK C LEU A 160 N MSE A 161 1555 1555 1.33
LINK C MSE A 161 N ARG A 162 1555 1555 1.33
LINK C TYR A 235 N MSE A 236 1555 1555 1.33
LINK C MSE A 236 N LYS A 237 1555 1555 1.33
LINK C PHE A 265 N MSE A 266 1555 1555 1.33
LINK C MSE A 266 N GLU A 267 1555 1555 1.33
LINK C VAL A 288 N MSE A 289 1555 1555 1.33
LINK C MSE A 289 N ILE A 290 1555 1555 1.33
LINK C MSE B 1 N GLU B 2 1555 1555 1.33
LINK C PHE B 80 N MSE B 81 1555 1555 1.33
LINK C MSE B 81 N HIS B 82 1555 1555 1.33
LINK C PRO B 92 N MSE B 93 1555 1555 1.32
LINK C MSE B 93 N ILE B 94 1555 1555 1.33
LINK C LEU B 160 N MSE B 161 1555 1555 1.33
LINK C MSE B 161 N ARG B 162 1555 1555 1.33
LINK C TYR B 235 N MSE B 236 1555 1555 1.33
LINK C MSE B 236 N LYS B 237 1555 1555 1.33
LINK C PHE B 265 N MSE B 266 1555 1555 1.33
LINK C MSE B 266 N GLU B 267 1555 1555 1.32
LINK C VAL B 288 N MSE B 289 1555 1555 1.33
LINK C MSE B 289 N ILE B 290 1555 1555 1.33
LINK C MSE C 1 N GLU C 2 1555 1555 1.33
LINK C PHE C 80 N MSE C 81 1555 1555 1.32
LINK C MSE C 81 N HIS C 82 1555 1555 1.33
LINK C PRO C 92 N MSE C 93 1555 1555 1.33
LINK C MSE C 93 N ILE C 94 1555 1555 1.33
LINK C LEU C 160 N MSE C 161 1555 1555 1.33
LINK C MSE C 161 N ARG C 162 1555 1555 1.33
LINK C TYR C 235 N MSE C 236 1555 1555 1.33
LINK C MSE C 236 N LYS C 237 1555 1555 1.33
LINK C PHE C 265 N MSE C 266 1555 1555 1.32
LINK C MSE C 266 N GLU C 267 1555 1555 1.32
LINK C VAL C 288 N MSE C 289 1555 1555 1.34
LINK C MSE C 289 N ILE C 290 1555 1555 1.33
LINK C MSE D 1 N GLU D 2 1555 1555 1.33
LINK C PHE D 80 N MSE D 81 1555 1555 1.33
LINK C MSE D 81 N HIS D 82 1555 1555 1.33
LINK C PRO D 92 N MSE D 93 1555 1555 1.32
LINK C MSE D 93 N ILE D 94 1555 1555 1.33
LINK C LEU D 160 N MSE D 161 1555 1555 1.34
LINK C MSE D 161 N ARG D 162 1555 1555 1.33
LINK C TYR D 235 N MSE D 236 1555 1555 1.33
LINK C MSE D 236 N LYS D 237 1555 1555 1.33
LINK C PHE D 265 N MSE D 266 1555 1555 1.33
LINK C MSE D 266 N GLU D 267 1555 1555 1.33
LINK C VAL D 288 N MSE D 289 1555 1555 1.33
LINK C MSE D 289 N ILE D 290 1555 1555 1.33
LINK C MSE E 1 N GLU E 2 1555 1555 1.33
LINK C PHE E 80 N MSE E 81 1555 1555 1.33
LINK C MSE E 81 N HIS E 82 1555 1555 1.33
LINK C PRO E 92 N MSE E 93 1555 1555 1.33
LINK C MSE E 93 N ILE E 94 1555 1555 1.33
LINK C LEU E 160 N MSE E 161 1555 1555 1.33
LINK C MSE E 161 N ARG E 162 1555 1555 1.33
LINK C TYR E 235 N MSE E 236 1555 1555 1.33
LINK C MSE E 236 N LYS E 237 1555 1555 1.33
LINK C PHE E 265 N MSE E 266 1555 1555 1.33
LINK C MSE E 266 N GLU E 267 1555 1555 1.33
LINK C VAL E 288 N MSE E 289 1555 1555 1.33
LINK C MSE E 289 N ILE E 290 1555 1555 1.33
CISPEP 1 TRP A 99 PRO A 100 0 1.26
CISPEP 2 TRP B 99 PRO B 100 0 1.96
CISPEP 3 TRP C 99 PRO C 100 0 1.00
CISPEP 4 TRP D 99 PRO D 100 0 -1.71
CISPEP 5 TRP E 99 PRO E 100 0 1.96
SITE 1 AC1 5 HIS A 82 ARG A 84 LEU A 164 GLY A 165
SITE 2 AC1 5 TYR A 166
SITE 1 AC2 5 PRO A 92 GLY A 165 TYR A 166 SER A 167
SITE 2 AC2 5 ARG A 168
SITE 1 AC3 2 LEU A 293 HOH A 523
SITE 1 AC4 5 ALA A 58 ALA A 59 ARG A 62 HOH A 511
SITE 2 AC4 5 HOH A 512
SITE 1 AC5 3 HIS A 191 HOH A 505 HOH A 714
SITE 1 AC6 3 ASP A 21 ARG A 51 ASP A 52
SITE 1 AC7 1 ASP A 12
SITE 1 AC8 13 ASP A 175 TRP A 179 PHE A 199 ILE A 201
SITE 2 AC8 13 PHE A 228 TYR A 235 MSE A 236 TRP A 268
SITE 3 AC8 13 PRO A 312 SER A 337 ALA A 338 HIS A 363
SITE 4 AC8 13 HOH A 504
SITE 1 AC9 3 GLU B 267 TRS B 403 HOH D 505
SITE 1 AD1 6 HOH A 568 ILE B 8 PRO B 9 ASP B 12
SITE 2 AD1 6 LEU B 293 HOH B 673
SITE 1 AD2 7 MSE B 266 GLU B 267 TRP B 268 GLY B 269
SITE 2 AD2 7 ALA B 335 ACT B 401 GLU D 216
SITE 1 AD3 13 ASP B 175 TRP B 179 PHE B 199 ILE B 201
SITE 2 AD3 13 PHE B 228 TYR B 235 MSE B 236 TRP B 268
SITE 3 AD3 13 PRO B 312 SER B 337 ALA B 338 HIS B 363
SITE 4 AD3 13 HOH B 502
SITE 1 AD4 5 LEU C 20 ASP C 21 TRP C 25 HOH C 512
SITE 2 AD4 5 HOH C 531
SITE 1 AD5 13 ASP C 175 TRP C 179 PHE C 199 ILE C 201
SITE 2 AD5 13 PHE C 228 TYR C 235 MSE C 236 TRP C 268
SITE 3 AD5 13 PRO C 312 SER C 337 ALA C 338 HIS C 363
SITE 4 AD5 13 HOH C 514
SITE 1 AD6 13 ASP D 175 TRP D 179 PHE D 199 ILE D 201
SITE 2 AD6 13 PHE D 228 TYR D 235 MSE D 236 TRP D 268
SITE 3 AD6 13 PRO D 312 SER D 337 ALA D 338 HIS D 363
SITE 4 AD6 13 HOH D 508
SITE 1 AD7 5 PRO E 92 GLY E 165 TYR E 166 SER E 167
SITE 2 AD7 5 ARG E 168
SITE 1 AD8 12 ASP E 175 TRP E 179 PHE E 199 ILE E 201
SITE 2 AD8 12 PHE E 228 TYR E 235 MSE E 236 TRP E 268
SITE 3 AD8 12 PRO E 312 SER E 337 HIS E 363 HOH E 502
CRYST1 179.356 93.068 134.059 90.00 115.33 90.00 C 1 2 1 20
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 0.005576 0.000000 0.002639 0.00000
SCALE2 0.000000 0.010745 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008253 0.00000
TER 3053 HIS A 388
TER 6105 HIS B 390
TER 9153 SER C 387
TER 12232 HIS D 391
TER 15273 HIS E 388
MASTER 943 0 52 104 45 0 38 616469 5 533 155
END |