HEADER ISOMERASE/DNA/ANTIBIOTIC 25-APR-10 2XCT
TITLE THE TWINNED 3.35A STRUCTURE OF S. AUREUS GYRASE COMPLEX WITH
TITLE 2 CIPROFLOXACIN AND DNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA GYRASE SUBUNIT B, DNA GYRASE SUBUNIT A;
COMPND 3 CHAIN: B, D, S, U;
COMPND 4 FRAGMENT: GYRB- C-TERMINAL 27KDA DOMAIN, RESIDUES 410-543 AND 580-
COMPND 5 644, GYRA- N-TERMINAL 56KDA DOMAIN, RESIDUES 2-491;
COMPND 6 EC: 5.99.1.3;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 OTHER_DETAILS: C-TERMINUS GYRB (644) FUSED TO N-TERMINUS GYRA
COMPND 10 (1002). GREEK KEY DOMAIN (544-579) DELETED AND REPLACED WITH TWO
COMPND 11 RESIDUES, TG;
COMPND 12 MOL_ID: 2;
COMPND 13 MOLECULE: 5'-D(TP*GP*TP*GP*CP*GP*GP*T)-3';
COMPND 14 CHAIN: E, V;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: 5'-D(AP*GP*CP*CP*GP*TP*AP*G)-3';
COMPND 17 CHAIN: F, W;
COMPND 18 MOL_ID: 4;
COMPND 19 MOLECULE: 5'-D(GP*TP*AP*CP*CP*CP*AP*CP*GP*GP*CP*T)-3';
COMPND 20 CHAIN: G, X;
COMPND 21 MOL_ID: 5;
COMPND 22 MOLECULE: 5'-D(GP*TP*AP*CP*AP*CP*CP*GP*CP*AP*CP*A)-3';
COMPND 23 CHAIN: H, Y
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 158879;
SOURCE 4 STRAIN: N315;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 11 ORGANISM_TAXID: 32630;
SOURCE 12 MOL_ID: 3;
SOURCE 13 SYNTHETIC: YES;
SOURCE 14 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 15 ORGANISM_TAXID: 32630;
SOURCE 16 MOL_ID: 4;
SOURCE 17 SYNTHETIC: YES;
SOURCE 18 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 19 ORGANISM_TAXID: 32630;
SOURCE 20 MOL_ID: 5;
SOURCE 21 SYNTHETIC: YES;
SOURCE 22 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 23 ORGANISM_TAXID: 32630
KEYWDS ISOMERASE-DNA-ANTIBIOTIC COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.D.BAX,P.CHAN,D.S.EGGLESTON,A.FOSBERRY,D.R.GENTRY,F.GORREC,
AUTHOR 2 I.GIORDANO,M.M.HANN,A.HENNESSY,M.HIBBS,J.HUANG,E.JONES,J.JONES,
AUTHOR 3 K.K.BROWN,C.J.LEWIS,E.MAY,O.SINGH,C.SPITZFADEN,C.SHEN,A.SHILLINGS,
AUTHOR 4 A.THEOBALD,A.WOHLKONIG,N.D.PEARSON,M.N.GWYNN
REVDAT 1 25-AUG-10 2XCT 0
JRNL AUTH B.D.BAX,P.F.CHAN,D.S.EGGLESTON,A.FOSBERRY,D.R.GENTRY,
JRNL AUTH 2 F.GORREC,I.GIORDANO,M.M.HANN,A.HENNESSY,M.HIBBS,J.HUANG,
JRNL AUTH 3 E.JONES,J.JONES,K.K.BROWN,C.J.LEWIS,E.W.MAY,M.R.SAUNDERS,
JRNL AUTH 4 O.SINGH,C.SPITZFADEN,C.SHEN,A.SHILLINGS,A.F.THEOBALD,
JRNL AUTH 5 A.WOHLKONIG,N.D.PEARSON,M.N.GWYNN
JRNL TITL TYPE IIA TOPOISOMERASE INHIBITION BY A NEW CLASS OF
JRNL TITL 2 ANTIBACTERIAL AGENTS.
JRNL REF NATURE V. 466 935 2010
JRNL REFN ISSN 0028-0836
JRNL PMID 20686482
JRNL DOI 10.1038/NATURE09197
REMARK 2
REMARK 2 RESOLUTION. 3.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT 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) : 3.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.956
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.38
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.47
REMARK 3 NUMBER OF REFLECTIONS : 52173
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1692
REMARK 3 R VALUE (WORKING SET) : 0.1664
REMARK 3 FREE R VALUE : 0.2363
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.1
REMARK 3 FREE R VALUE TEST SET COUNT : 2148
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 24.9566 - 8.9582 0.98 2539 141 0.1767 0.1763
REMARK 3 2 8.9582 - 7.1658 0.98 2516 141 0.1552 0.2383
REMARK 3 3 7.1658 - 6.2765 0.98 2637 0 0.1809 0.0000
REMARK 3 4 6.2765 - 5.7101 0.98 2475 141 0.1682 0.2968
REMARK 3 5 5.7101 - 5.3051 0.98 2464 141 0.1626 0.2887
REMARK 3 6 5.3051 - 4.9949 0.98 2483 141 0.1477 0.2214
REMARK 3 7 4.9949 - 4.7465 0.98 2581 0 0.1440 0.0000
REMARK 3 8 4.7465 - 4.5412 0.98 2501 141 0.1439 0.2274
REMARK 3 9 4.5412 - 4.3674 0.98 2448 141 0.1424 0.2045
REMARK 3 10 4.3674 - 4.2174 0.98 2445 141 0.1497 0.2214
REMARK 3 11 4.2174 - 4.0861 0.98 2597 0 0.1544 0.0000
REMARK 3 12 4.0861 - 3.9698 0.98 2475 141 0.1652 0.2281
REMARK 3 13 3.9698 - 3.8657 0.98 2417 141 0.1677 0.2449
REMARK 3 14 3.8657 - 3.7717 0.98 2494 141 0.1759 0.2032
REMARK 3 15 3.7717 - 3.6862 0.98 2558 0 0.1812 0.0000
REMARK 3 16 3.6862 - 3.6080 0.98 2475 141 0.1828 0.2570
REMARK 3 17 3.6080 - 3.5360 0.98 2444 141 0.1959 0.2874
REMARK 3 18 3.5360 - 3.4695 0.98 2504 86 0.1984 0.2556
REMARK 3 19 3.4695 - 3.4077 0.98 2518 55 0.2005 0.2875
REMARK 3 20 3.4077 - 3.3500 0.98 2487 141 0.2114 0.3288
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 : 0.291
REMARK 3 B_SOL : 35.369
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 37.56
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 76.3
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 73.7
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.1570
REMARK 3 B22 (A**2) : 15.7485
REMARK 3 B33 (A**2) : -24.7844
REMARK 3 B12 (A**2) : 0.0000
REMARK 3 B13 (A**2) : 5.3898
REMARK 3 B23 (A**2) : -0.0000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: 0.324
REMARK 3 OPERATOR: H,-K,-L
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.024 22861
REMARK 3 ANGLE : 1.442 31150
REMARK 3 CHIRALITY : 0.082 3550
REMARK 3 PLANARITY : 0.005 3859
REMARK 3 DIHEDRAL : 20.472 8689
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 16
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ((CHAIN B AND (RESID 1029:1374 OR RESID 1451:1491))
REMARK 3 OR (CHAIN E) OR (CHAIN F) OR CHAIN G) OR (CHAIN H))
REMARK 3 ORIGIN FOR THE GROUP (A): 13.8303 30.4628 81.7539
REMARK 3 T TENSOR
REMARK 3 T11: 0.3065 T22: 0.3247
REMARK 3 T33: 0.3598 T12: 0.0282
REMARK 3 T13: -0.0383 T23: -0.0268
REMARK 3 L TENSOR
REMARK 3 L11: 0.9306 L22: 0.1593
REMARK 3 L33: -0.1528 L12: -0.1717
REMARK 3 L13: -0.0791 L23: -0.1299
REMARK 3 S TENSOR
REMARK 3 S11: 0.0484 S12: 0.1751 S13: -0.0667
REMARK 3 S21: -0.0529 S22: -0.0047 S23: -0.0022
REMARK 3 S31: 0.0301 S32: -0.0153 S33: -0.0349
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ((CHAIN B AND (RESID 417:545 OR RESID 580:606)))
REMARK 3 ORIGIN FOR THE GROUP (A): 4.8182 62.4552 64.0615
REMARK 3 T TENSOR
REMARK 3 T11: 0.1651 T22: 0.1761
REMARK 3 T33: 0.3215 T12: 0.0067
REMARK 3 T13: -0.0415 T23: 0.1026
REMARK 3 L TENSOR
REMARK 3 L11: 0.4404 L22: 0.2400
REMARK 3 L33: 0.6484 L12: 0.1010
REMARK 3 L13: 0.3511 L23: -0.2218
REMARK 3 S TENSOR
REMARK 3 S11: 0.0208 S12: 0.1688 S13: 0.1346
REMARK 3 S21: -0.0052 S22: 0.0215 S23: 0.1235
REMARK 3 S31: -0.0110 S32: -0.0769 S33: -0.0430
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ((CHAIN B AND (RESID 1375:1450)))
REMARK 3 ORIGIN FOR THE GROUP (A): 1.0299 42.1024 132.9771
REMARK 3 T TENSOR
REMARK 3 T11: 0.3100 T22: 0.2625
REMARK 3 T33: 0.1750 T12: 0.0751
REMARK 3 T13: -0.0651 T23: -0.0484
REMARK 3 L TENSOR
REMARK 3 L11: 0.1366 L22: 0.3624
REMARK 3 L33: 0.2254 L12: 0.2695
REMARK 3 L13: 0.1620 L23: 0.1048
REMARK 3 S TENSOR
REMARK 3 S11: 0.1599 S12: 0.0612 S13: -0.0447
REMARK 3 S21: -0.1003 S22: -0.1850 S23: 0.1474
REMARK 3 S31: 0.0495 S32: 0.0155 S33: 0.0438
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: ((CHAIN B AND (RESID 1019:1028)) OR (CHAIN B AND
REMARK 3 (RESID 609:637)))
REMARK 3 ORIGIN FOR THE GROUP (A): 23.5957 59.8005 72.2793
REMARK 3 T TENSOR
REMARK 3 T11: 0.2531 T22: 0.4383
REMARK 3 T33: 0.5869 T12: -0.0284
REMARK 3 T13: -0.0291 T23: 0.1131
REMARK 3 L TENSOR
REMARK 3 L11: 0.1111 L22: 0.4482
REMARK 3 L33: 0.2157 L12: -0.0409
REMARK 3 L13: 0.2257 L23: -0.1094
REMARK 3 S TENSOR
REMARK 3 S11: -0.0103 S12: 0.2428 S13: -0.3556
REMARK 3 S21: -0.0195 S22: 0.0306 S23: 0.2320
REMARK 3 S31: 0.0030 S32: 0.2067 S33: -0.0690
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: ((CHAIN D AND (RESID 1030:1374 OR RESID 1451:1491)))
REMARK 3 ORIGIN FOR THE GROUP (A): -29.7788 51.9111 82.2621
REMARK 3 T TENSOR
REMARK 3 T11: 0.2475 T22: 0.4002
REMARK 3 T33: 0.3754 T12: -0.0119
REMARK 3 T13: -0.0960 T23: -0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 0.2712 L22: 0.7820
REMARK 3 L33: 0.8966 L12: -0.1024
REMARK 3 L13: 0.2324 L23: -0.4833
REMARK 3 S TENSOR
REMARK 3 S11: -0.1512 S12: -0.1006 S13: 0.0915
REMARK 3 S21: 0.0456 S22: 0.0608 S23: 0.0005
REMARK 3 S31: -0.0540 S32: -0.1943 S33: 0.0605
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: ((CHAIN D AND (RESID 417:545 OR RESID 580:606)))
REMARK 3 ORIGIN FOR THE GROUP (A): -14.0594 17.0340 63.1686
REMARK 3 T TENSOR
REMARK 3 T11: 0.3629 T22: 0.2472
REMARK 3 T33: 0.2559 T12: 0.1225
REMARK 3 T13: -0.1026 T23: -0.0976
REMARK 3 L TENSOR
REMARK 3 L11: 0.4959 L22: 0.4866
REMARK 3 L33: -0.2508 L12: -0.1105
REMARK 3 L13: -0.2882 L23: -0.0770
REMARK 3 S TENSOR
REMARK 3 S11: 0.2332 S12: 0.2913 S13: -0.2184
REMARK 3 S21: -0.1534 S22: -0.0536 S23: -0.0765
REMARK 3 S31: 0.1083 S32: 0.2080 S33: -0.1169
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: ((CHAIN D AND (RESID 1375:1450)))
REMARK 3 ORIGIN FOR THE GROUP (A): -19.1548 38.2380 131.8792
REMARK 3 T TENSOR
REMARK 3 T11: 0.3405 T22: 0.4251
REMARK 3 T33: 0.1678 T12: 0.0611
REMARK 3 T13: 0.0287 T23: 0.0316
REMARK 3 L TENSOR
REMARK 3 L11: 0.2545 L22: 0.0850
REMARK 3 L33: 0.0655 L12: 0.0336
REMARK 3 L13: -0.1366 L23: -0.0124
REMARK 3 S TENSOR
REMARK 3 S11: -0.0895 S12: -0.0543 S13: -0.0858
REMARK 3 S21: 0.1676 S22: -0.0302 S23: 0.0239
REMARK 3 S31: -0.1399 S32: -0.4961 S33: 0.0506
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: ((CHAIN D AND (RESID 1010:1028)) OR (CHAIN D AND
REMARK 3 (RESID 607:639)))
REMARK 3 ORIGIN FOR THE GROUP (A): -33.8843 20.0079 69.0069
REMARK 3 T TENSOR
REMARK 3 T11: 0.2539 T22: 0.1691
REMARK 3 T33: 0.2030 T12: -0.1125
REMARK 3 T13: -0.1239 T23: 0.0379
REMARK 3 L TENSOR
REMARK 3 L11: -0.1375 L22: 0.8620
REMARK 3 L33: 0.9370 L12: 0.6644
REMARK 3 L13: 0.0417 L23: 0.4969
REMARK 3 S TENSOR
REMARK 3 S11: -0.0032 S12: 0.0319 S13: -0.1057
REMARK 3 S21: -0.1507 S22: 0.2564 S23: -0.2364
REMARK 3 S31: 0.0870 S32: -0.2747 S33: -0.1946
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: ((CHAIN S AND (RESID 1029:1374 OR RESID 1451:1491))
REMARK 3 OR (CHAIN V) OR (CHAIN W) OR CHAIN X) OR (CHAIN Y))
REMARK 3 ORIGIN FOR THE GROUP (A): 57.2887 30.0654 -5.7269
REMARK 3 T TENSOR
REMARK 3 T11: 0.6006 T22: 0.4066
REMARK 3 T33: 0.4877 T12: 0.0327
REMARK 3 T13: 0.1363 T23: -0.0087
REMARK 3 L TENSOR
REMARK 3 L11: 0.8404 L22: -0.1115
REMARK 3 L33: 0.5083 L12: -0.2442
REMARK 3 L13: -0.6778 L23: 0.0369
REMARK 3 S TENSOR
REMARK 3 S11: -0.2579 S12: 0.0373 S13: -0.2607
REMARK 3 S21: 0.0267 S22: 0.0804 S23: 0.1030
REMARK 3 S31: 0.1207 S32: 0.1164 S33: 0.1081
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: ((CHAIN S AND (RESID 417:545 OR RESID 580:606)))
REMARK 3 ORIGIN FOR THE GROUP (A): 27.9663 16.7370 -20.8361
REMARK 3 T TENSOR
REMARK 3 T11: 0.8043 T22: 0.6111
REMARK 3 T33: 0.5626 T12: -0.0077
REMARK 3 T13: 0.0077 T23: -0.0773
REMARK 3 L TENSOR
REMARK 3 L11: 0.4629 L22: 0.2416
REMARK 3 L33: 0.2925 L12: 0.1534
REMARK 3 L13: -0.6633 L23: 0.0477
REMARK 3 S TENSOR
REMARK 3 S11: 0.1010 S12: 0.0785 S13: -0.1081
REMARK 3 S21: -0.1572 S22: -0.0007 S23: -0.0715
REMARK 3 S31: 0.0820 S32: 0.0171 S33: -0.0594
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: ((CHAIN S AND (RESID 1375:1450)))
REMARK 3 ORIGIN FOR THE GROUP (A): 50.8904 41.4310 46.6307
REMARK 3 T TENSOR
REMARK 3 T11: 0.3488 T22: 0.4227
REMARK 3 T33: 0.1548 T12: 0.0841
REMARK 3 T13: -0.0435 T23: 0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 0.1490 L22: 0.1009
REMARK 3 L33: 0.3383 L12: 0.0342
REMARK 3 L13: 0.1622 L23: -0.0444
REMARK 3 S TENSOR
REMARK 3 S11: 0.0311 S12: 0.0257 S13: -0.0229
REMARK 3 S21: -0.0186 S22: -0.1480 S23: 0.0658
REMARK 3 S31: 0.1327 S32: 0.3027 S33: 0.0691
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: ((CHAIN S AND (RESID 1012:1028)) OR (CHAIN U AND
REMARK 3 (RESID 609:639)))
REMARK 3 ORIGIN FOR THE GROUP (A): 67.0846 58.4173 -15.9857
REMARK 3 T TENSOR
REMARK 3 T11: 0.7044 T22: 0.4511
REMARK 3 T33: 0.5927 T12: -0.1300
REMARK 3 T13: 0.1786 T23: 0.0132
REMARK 3 L TENSOR
REMARK 3 L11: 0.3818 L22: 0.0109
REMARK 3 L33: 1.1373 L12: 0.1821
REMARK 3 L13: -0.1222 L23: -0.6112
REMARK 3 S TENSOR
REMARK 3 S11: 0.1293 S12: -0.0136 S13: 0.0216
REMARK 3 S21: 0.2183 S22: -0.0331 S23: -0.1302
REMARK 3 S31: -0.5768 S32: 0.1700 S33: -0.0931
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: ((CHAIN U AND (RESID 1029:1374 OR RESID 1451:1491)))
REMARK 3 ORIGIN FOR THE GROUP (A): 13.8319 51.5275 0.0035
REMARK 3 T TENSOR
REMARK 3 T11: 0.2124 T22: 0.2026
REMARK 3 T33: 0.1874 T12: 0.0763
REMARK 3 T13: 0.0174 T23: 0.0267
REMARK 3 L TENSOR
REMARK 3 L11: 0.2732 L22: 0.4769
REMARK 3 L33: 0.9825 L12: -0.0365
REMARK 3 L13: -0.2229 L23: 0.3036
REMARK 3 S TENSOR
REMARK 3 S11: 0.0503 S12: 0.0078 S13: 0.1025
REMARK 3 S21: -0.0657 S22: -0.0047 S23: -0.0172
REMARK 3 S31: -0.2148 S32: -0.1392 S33: -0.0122
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: ((CHAIN U AND (RESID 418:544 OR RESID 581:608)))
REMARK 3 ORIGIN FOR THE GROUP (A): 46.9071 62.4124 -22.5056
REMARK 3 T TENSOR
REMARK 3 T11: 0.5135 T22: 0.2477
REMARK 3 T33: 0.3803 T12: 0.1171
REMARK 3 T13: 0.1771 T23: 0.1036
REMARK 3 L TENSOR
REMARK 3 L11: 0.2810 L22: -0.0428
REMARK 3 L33: 0.3301 L12: -0.3059
REMARK 3 L13: -0.1360 L23: 0.2260
REMARK 3 S TENSOR
REMARK 3 S11: 0.4161 S12: 0.2216 S13: 0.3796
REMARK 3 S21: -0.0831 S22: -0.2045 S23: -0.1740
REMARK 3 S31: -0.6316 S32: -0.0913 S33: -0.1037
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: ((CHAIN U AND (RESID 1375:1450)))
REMARK 3 ORIGIN FOR THE GROUP (A): 30.6748 37.7366 48.1567
REMARK 3 T TENSOR
REMARK 3 T11: 0.2821 T22: 0.2434
REMARK 3 T33: 0.1697 T12: -0.0266
REMARK 3 T13: 0.0428 T23: 0.0198
REMARK 3 L TENSOR
REMARK 3 L11: 0.7138 L22: 0.8001
REMARK 3 L33: 0.1366 L12: -0.3821
REMARK 3 L13: -0.2670 L23: -0.0024
REMARK 3 S TENSOR
REMARK 3 S11: -0.3674 S12: 0.2092 S13: -0.0352
REMARK 3 S21: 0.3658 S22: 0.2052 S23: 0.0702
REMARK 3 S31: 0.0353 S32: 0.1231 S33: 0.0732
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: ((CHAIN U AND (RESID 1013:1028)) OR (CHAIN S AND
REMARK 3 (RESID 609:639)))
REMARK 3 ORIGIN FOR THE GROUP (A): 7.8046 20.7355 -12.5674
REMARK 3 T TENSOR
REMARK 3 T11: 0.4805 T22: 0.4646
REMARK 3 T33: 0.4470 T12: 0.0364
REMARK 3 T13: 0.0548 T23: 0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 0.9635 L22: 1.3542
REMARK 3 L33: 1.2318 L12: 1.3892
REMARK 3 L13: 1.3992 L23: -0.2461
REMARK 3 S TENSOR
REMARK 3 S11: 0.3087 S12: -0.2344 S13: -0.3162
REMARK 3 S21: 0.2435 S22: -0.0708 S23: -0.4464
REMARK 3 S31: -0.2132 S32: -0.2522 S33: -0.1355
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE DATA ARE IN P21, BUT WITH A BETA
REMARK 3 ANGLE OF 90 DEGREES.BECAUSE THE DATA ARE PSEUDO ORTHORHOMBIC.
REMARK 3 AUTHOR SELECTED THE R-FREE IN THE ABOVE MENTIONED RESOLUTION
REMARK 3 SHELLS. THIS IS NOT A STANDARD SPACE GROUP FOR A TWIN OPERATOR.
REMARK 4
REMARK 4 2XCT COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-APR-10.
REMARK 100 THE PDBE ID CODE IS EBI-43722.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52713
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.35
REMARK 200 RESOLUTION RANGE LOW (A) : 25.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 3.8
REMARK 200 R MERGE (I) : 0.14
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.10
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.8
REMARK 200 R MERGE FOR SHELL (I) : 0.47
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.70
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: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 11% PEG 3350, 0.15M BIS TRIS PH 6.2
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 61.58300
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
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 57690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, G, H, E, F
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 18550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 57280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -105.3 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: S, U, V, X, Y, W
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, TYR 1123 TO PHE
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, TYR 1123 TO PHE
REMARK 400 ENGINEERED RESIDUE IN CHAIN S, TYR 1123 TO PHE
REMARK 400 ENGINEERED RESIDUE IN CHAIN U, TYR 1123 TO PHE
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET B 409
REMARK 465 ASP B 410
REMARK 465 VAL B 411
REMARK 465 ALA B 412
REMARK 465 SER B 413
REMARK 465 LEU B 414
REMARK 465 PRO B 415
REMARK 465 GLY B 416
REMARK 465 VAL B 638
REMARK 465 TYR B 639
REMARK 465 ALA B 640
REMARK 465 ASN B 641
REMARK 465 LEU B 642
REMARK 465 ASP B 643
REMARK 465 PHE B 644
REMARK 465 ALA B 1002
REMARK 465 GLU B 1003
REMARK 465 LEU B 1004
REMARK 465 PRO B 1005
REMARK 465 GLN B 1006
REMARK 465 SER B 1007
REMARK 465 ARG B 1008
REMARK 465 ILE B 1009
REMARK 465 MET D 409
REMARK 465 ASP D 410
REMARK 465 VAL D 411
REMARK 465 ALA D 412
REMARK 465 SER D 413
REMARK 465 LEU D 414
REMARK 465 PRO D 415
REMARK 465 GLY D 416
REMARK 465 GLY D 545
REMARK 465 TYR D 580
REMARK 465 ALA D 640
REMARK 465 ASN D 641
REMARK 465 LEU D 642
REMARK 465 ASP D 643
REMARK 465 PHE D 644
REMARK 465 ALA D 1002
REMARK 465 GLU D 1003
REMARK 465 LEU D 1004
REMARK 465 PRO D 1005
REMARK 465 GLN D 1006
REMARK 465 SER D 1007
REMARK 465 ARG D 1008
REMARK 465 ILE D 1009
REMARK 465 DT E 1
REMARK 465 DA F 1
REMARK 465 DT G 20
REMARK 465 MET S 409
REMARK 465 ASP S 410
REMARK 465 VAL S 411
REMARK 465 ALA S 412
REMARK 465 SER S 413
REMARK 465 LEU S 414
REMARK 465 PRO S 415
REMARK 465 GLY S 416
REMARK 465 GLY S 545
REMARK 465 TYR S 580
REMARK 465 LYS S 581
REMARK 465 ASN S 641
REMARK 465 LEU S 642
REMARK 465 ASP S 643
REMARK 465 PHE S 644
REMARK 465 ALA S 1002
REMARK 465 GLU S 1003
REMARK 465 LEU S 1004
REMARK 465 PRO S 1005
REMARK 465 GLN S 1006
REMARK 465 SER S 1007
REMARK 465 ARG S 1008
REMARK 465 ILE S 1009
REMARK 465 ASN S 1010
REMARK 465 GLU S 1011
REMARK 465 MET U 409
REMARK 465 ASP U 410
REMARK 465 VAL U 411
REMARK 465 ALA U 412
REMARK 465 SER U 413
REMARK 465 LEU U 414
REMARK 465 PRO U 415
REMARK 465 GLY U 416
REMARK 465 LYS U 417
REMARK 465 GLY U 545
REMARK 465 TYR U 580
REMARK 465 ALA U 640
REMARK 465 ASN U 641
REMARK 465 LEU U 642
REMARK 465 ASP U 643
REMARK 465 PHE U 644
REMARK 465 ALA U 1002
REMARK 465 GLU U 1003
REMARK 465 LEU U 1004
REMARK 465 PRO U 1005
REMARK 465 GLN U 1006
REMARK 465 SER U 1007
REMARK 465 ARG U 1008
REMARK 465 ILE U 1009
REMARK 465 ASN U 1010
REMARK 465 GLU U 1011
REMARK 465 ARG U 1012
REMARK 465 DT V 1
REMARK 465 DA W 1
REMARK 465 DG W 2
REMARK 465 DT X 20
REMARK 465 DA Y 20
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 LYS B 417 CG CD CE NZ
REMARK 470 LYS B 424 CG CD CE NZ
REMARK 470 LYS B 444 CG CD CE NZ
REMARK 470 TYR B 580 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 581 CG CD CE NZ
REMARK 470 GLU B 585 CG CD OE1 OE2
REMARK 470 ARG B1299 CG CD NE CZ NH1 NH2
REMARK 470 LYS B1310 CG CD CE NZ
REMARK 470 GLU B1393 CG CD OE1 OE2
REMARK 470 ARG B1414 CG CD NE CZ NH1 NH2
REMARK 470 ARG B1438 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 417 CG CD CE NZ
REMARK 470 LYS D 424 CG CD CE NZ
REMARK 470 GLU D 427 CG CD OE1 OE2
REMARK 470 ASP D 437 CG OD1 OD2
REMARK 470 LYS D 460 CG CD CE NZ
REMARK 470 LYS D 502 CG CD CE NZ
REMARK 470 ARG D 529 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 581 CG CD CE NZ
REMARK 470 GLU D 599 CG CD OE1 OE2
REMARK 470 LYS D 607 CG CD CE NZ
REMARK 470 GLU D 609 CG CD OE1 OE2
REMARK 470 TYR D 639 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASN D1010 CG OD1 ND2
REMARK 470 LYS D1062 CG CD CE NZ
REMARK 470 LYS D1065 CG CD CE NZ
REMARK 470 LYS D1066 CG CD CE NZ
REMARK 470 ARG D1069 CG CD NE CZ NH1 NH2
REMARK 470 GLU D1208 CG CD OE1 OE2
REMARK 470 GLU D1211 CG CD OE1 OE2
REMARK 470 LYS D1227 CG CD CE NZ
REMARK 470 ARG D1232 CG CD NE CZ NH1 NH2
REMARK 470 GLU D1251 CG CD OE1 OE2
REMARK 470 ARG D1252 CG CD NE CZ NH1 NH2
REMARK 470 ARG D1256 CG CD NE CZ NH1 NH2
REMARK 470 LYS D1276 CG CD CE NZ
REMARK 470 ARG D1309 CG CD NE CZ NH1 NH2
REMARK 470 LYS D1310 CG CD CE NZ
REMARK 470 ARG D1342 CG CD NE CZ NH1 NH2
REMARK 470 LYS D1405 CG CD CE NZ
REMARK 470 GLU D1409 CG CD OE1 OE2
REMARK 470 LYS D1416 CG CD CE NZ
REMARK 470 LYS D1420 CG CD CE NZ
REMARK 470 ARG D1429 CG CD NE CZ NH1 NH2
REMARK 470 ARG D1438 CG CD NE CZ NH1 NH2
REMARK 470 LYS D1440 CG CD CE NZ
REMARK 470 LYS S 417 CG CD CE NZ
REMARK 470 LYS S 466 CG CD CE NZ
REMARK 470 ARG S 468 CG CD NE CZ NH1 NH2
REMARK 470 ARG S 529 CG CD NE CZ NH1 NH2
REMARK 470 ALA S 640 CA C O CB
REMARK 470 ARG S1012 CG CD NE CZ NH1 NH2
REMARK 470 ARG S1019 CG CD NE CZ NH1 NH2
REMARK 470 LYS S1062 CG CD CE NZ
REMARK 470 LYS S1066 CG CD CE NZ
REMARK 470 ARG S1069 CG CD NE CZ NH1 NH2
REMARK 470 GLN S1107 CG CD OE1 NE2
REMARK 470 ARG S1238 CG CD NE CZ NH1 NH2
REMARK 470 ARG S1244 CG CD NE CZ NH1 NH2
REMARK 470 ARG S1252 CG CD NE CZ NH1 NH2
REMARK 470 GLU S1393 CG CD OE1 OE2
REMARK 470 ARG S1429 CG CD NE CZ NH1 NH2
REMARK 470 LYS U 424 CG CD CE NZ
REMARK 470 ARG U 450 CG CD NE CZ NH1 NH2
REMARK 470 LYS U 581 CG CD CE NZ
REMARK 470 GLU U 585 CG CD OE1 OE2
REMARK 470 GLU U 619 CG CD OE1 OE2
REMARK 470 LYS U1062 CG CD CE NZ
REMARK 470 LYS U1065 CG CD CE NZ
REMARK 470 LYS U1227 CG CD CE NZ
REMARK 470 GLU U1251 CG CD OE1 OE2
REMARK 470 ARG U1252 CG CD NE CZ NH1 NH2
REMARK 470 ARG U1256 CG CD NE CZ NH1 NH2
REMARK 470 LYS U1284 CG CD CE NZ
REMARK 470 LYS U1373 CG CD CE NZ
REMARK 470 LYS U1375 CG CD CE NZ
REMARK 470 LYS U1405 CG CD CE NZ
REMARK 470 ARG U1429 CG CD NE CZ NH1 NH2
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 N1 DA X 11 O4 DT Y 10 1.78
REMARK 500 N3 DC G 12 N2 DG H 9 1.82
REMARK 500 N2 DG X 9 O2 DC Y 12 1.91
REMARK 500 OG SER S 1067 O THR S 1124 2.13
REMARK 500 O LEU D 1196 OG SER D 1199 2.16
REMARK 500 O GLY U 535 OE1 GLN U 605 2.17
REMARK 500 OG SER U 1112 OD1 ASP U 1116 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 DG H 16 O3' DG H 16 C3' -0.055
REMARK 500 DC H 17 O3' DC H 17 C3' -0.056
REMARK 500 DC Y 17 O3' DC Y 17 C3' -0.038
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 B1326 C - N - CA ANGL. DEV. = 10.5 DEGREES
REMARK 500 PRO D1161 C - N - CA ANGL. DEV. = 9.1 DEGREES
REMARK 500 DT E 3 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DG E 6 C4' - C3' - C2' ANGL. DEV. = -6.4 DEGREES
REMARK 500 DG E 6 O4' - C1' - N9 ANGL. DEV. = 7.6 DEGREES
REMARK 500 DG E 7 O4' - C1' - N9 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DC F 3 O4' - C1' - N1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 DC F 4 O4' - C4' - C3' ANGL. DEV. = -4.4 DEGREES
REMARK 500 DT F 6 O4' - C1' - C2' ANGL. DEV. = -5.2 DEGREES
REMARK 500 DT F 6 O4' - C1' - N1 ANGL. DEV. = 7.3 DEGREES
REMARK 500 DT F 6 N3 - C4 - O4 ANGL. DEV. = 5.3 DEGREES
REMARK 500 DG F 8 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DG G 9 O4' - C1' - N9 ANGL. DEV. = 5.5 DEGREES
REMARK 500 DT G 10 C1' - O4' - C4' ANGL. DEV. = -6.2 DEGREES
REMARK 500 DT G 10 O4' - C1' - N1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 DC G 12 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DC G 13 O4' - C1' - N1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 DC G 16 O4' - C4' - C3' ANGL. DEV. = -2.7 DEGREES
REMARK 500 DC G 19 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DG H 9 C4' - C3' - O3' ANGL. DEV. = 13.6 DEGREES
REMARK 500 DG H 9 O4' - C1' - N9 ANGL. DEV. = 9.2 DEGREES
REMARK 500 DG H 9 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 DG H 9 N9 - C4 - C5 ANGL. DEV. = 4.1 DEGREES
REMARK 500 DG H 9 N3 - C4 - N9 ANGL. DEV. = -6.0 DEGREES
REMARK 500 DG H 9 C6 - C5 - N7 ANGL. DEV. = 4.4 DEGREES
REMARK 500 DG H 9 N3 - C2 - N2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 DG H 9 C8 - N9 - C1' ANGL. DEV. = 7.9 DEGREES
REMARK 500 DT H 10 O4' - C1' - N1 ANGL. DEV. = 9.1 DEGREES
REMARK 500 DT H 10 C5 - C4 - O4 ANGL. DEV. = -4.8 DEGREES
REMARK 500 DG H 9 C3' - O3' - P ANGL. DEV. = 11.9 DEGREES
REMARK 500 DA H 13 C3' - C2' - C1' ANGL. DEV. = -7.7 DEGREES
REMARK 500 DA H 13 O4' - C1' - N9 ANGL. DEV. = 3.2 DEGREES
REMARK 500 DC H 14 O4' - C4' - C3' ANGL. DEV. = -3.6 DEGREES
REMARK 500 DG H 16 O4' - C4' - C3' ANGL. DEV. = -4.1 DEGREES
REMARK 500 DG H 16 C1' - O4' - C4' ANGL. DEV. = -9.0 DEGREES
REMARK 500 DG H 16 O4' - C1' - N9 ANGL. DEV. = -4.4 DEGREES
REMARK 500 DG H 16 C8 - N9 - C4 ANGL. DEV. = 2.6 DEGREES
REMARK 500 DC H 17 O4' - C1' - N1 ANGL. DEV. = -9.6 DEGREES
REMARK 500 DC H 17 C6 - N1 - C2 ANGL. DEV. = 3.0 DEGREES
REMARK 500 DA H 18 C3' - C2' - C1' ANGL. DEV. = -7.3 DEGREES
REMARK 500 DC H 19 O4' - C1' - N1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 PRO S1036 C - N - CA ANGL. DEV. = 9.2 DEGREES
REMARK 500 PRO S1165 C - N - CA ANGL. DEV. = 10.0 DEGREES
REMARK 500 LEU U 608 CA - CB - CG ANGL. DEV. = 15.7 DEGREES
REMARK 500 DC V 5 C3' - C2' - C1' ANGL. DEV. = -6.9 DEGREES
REMARK 500 DG V 6 O5' - C5' - C4' ANGL. DEV. = -8.4 DEGREES
REMARK 500 DT V 8 O5' - C5' - C4' ANGL. DEV. = -4.8 DEGREES
REMARK 500 DT W 6 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DT W 6 N3 - C2 - O2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 DG X 9 O4' - C1' - N9 ANGL. DEV. = 4.4 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 76 ANGLE DEVIATIONS.
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 ILE B 461 -152.96 -106.29
REMARK 500 ILE B 478 -70.10 -77.19
REMARK 500 THR B 487 -71.75 -115.46
REMARK 500 THR B 522 -63.83 -29.31
REMARK 500 LYS B 581 173.02 168.07
REMARK 500 ILE B 633 -70.92 -42.75
REMARK 500 ASP B1024 -36.33 -38.53
REMARK 500 ILE B1030 -72.17 -96.63
REMARK 500 ALA B1032 54.52 -111.35
REMARK 500 ARG B1033 -87.80 -152.38
REMARK 500 MET B1058 70.19 -119.49
REMARK 500 TYR B1078 -52.50 -136.36
REMARK 500 TYR B1087 -71.57 -63.07
REMARK 500 PHE B1110 62.49 -105.71
REMARK 500 SER B1112 167.79 179.81
REMARK 500 ASP B1114 -7.46 -59.50
REMARK 500 MET B1121 -7.88 -53.59
REMARK 500 ASP B1142 71.23 44.21
REMARK 500 TYR B1150 -23.60 -33.00
REMARK 500 ALA B1162 73.33 49.90
REMARK 500 LEU B1167 -76.36 -37.49
REMARK 500 ALA B1169 -70.36 -73.48
REMARK 500 ALA B1172 148.86 165.37
REMARK 500 SER B1173 90.11 -168.88
REMARK 500 ALA B1176 -137.89 -103.76
REMARK 500 ALA B1180 132.13 -170.30
REMARK 500 ASN B1201 76.48 -108.88
REMARK 500 PRO B1202 14.48 -66.34
REMARK 500 ASP B1217 98.05 -160.73
REMARK 500 ALA B1221 -127.71 77.98
REMARK 500 LEU B1225 79.69 -114.12
REMARK 500 ARG B1244 -166.87 -103.95
REMARK 500 GLN B1267 -10.34 80.11
REMARK 500 LYS B1276 16.29 -66.93
REMARK 500 GLU B1279 -6.55 -52.05
REMARK 500 LYS B1284 51.62 36.16
REMARK 500 ILE B1286 116.88 -160.07
REMARK 500 THR B1290 62.06 -119.18
REMARK 500 ASP B1291 143.97 119.00
REMARK 500 LEU B1292 91.08 -161.27
REMARK 500 ARG B1303 105.29 -168.85
REMARK 500 ARG B1309 100.02 -48.12
REMARK 500 LYS B1310 155.13 -20.43
REMARK 500 ASN B1313 100.67 -59.40
REMARK 500 PRO B1326 6.21 -61.87
REMARK 500 MET B1335 86.66 -60.54
REMARK 500 LEU B1338 104.98 -55.44
REMARK 500 ASN B1340 33.90 33.43
REMARK 500 LYS B1349 -77.28 -58.15
REMARK 500 HIS B1379 -57.11 -27.14
REMARK 500
REMARK 500 THIS ENTRY HAS 280 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 LEU B 469 24.9 L L OUTSIDE RANGE
REMARK 500 ILE B1391 23.9 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
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 MN D2492 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 508 OD2
REMARK 620 2 ASP D 510 OD2 91.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN S2492 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP S 508 OD2
REMARK 620 2 ASP S 510 OD1 93.3
REMARK 620 3 ASP S 510 OD2 66.6 52.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN F2000 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CPF H1020 O2
REMARK 620 2 CPF H1020 O3 76.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN G2000 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CPF G1020 O3
REMARK 620 2 CPF G1020 O2 70.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN W2000 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CPF X1020 O2
REMARK 620 2 CPF X1020 O3 71.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN W2001 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CPF Y1020 O2
REMARK 620 2 CPF Y1020 O3 72.9
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B2492
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D2492
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CPF G1020
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CPF H1020
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G2000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN F2000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN W2000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN W2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN S2492
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN U2492
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CPF X1020
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CPF Y1020
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2XCS RELATED DB: PDB
REMARK 900 THE 2.1A CRYSTAL STRUCTURE OF S. AUREUS GYRASE COMPLEX WITH
REMARK 900 GSK299423 AND DNA
REMARK 900 RELATED ID: 2XCO RELATED DB: PDB
REMARK 900 THE 3.1A CRYSTAL STRUCTURE OF THE CATALYTIC CORE (B'A'
REMARK 900 REGION) OF STAPHYLOCOCCUS AUREUS DNA GYRASE
REMARK 900 RELATED ID: 2XCQ RELATED DB: PDB
REMARK 900 THE 2.98A CRYSTAL STRUCTURE OF THE CATALYTIC CORE (B'A'
REMARK 900 REGION) OF STAPHYLOCOCCUS AUREUS DNA GYRASE
REMARK 900 RELATED ID: 2XCR RELATED DB: PDB
REMARK 900 THE 3.5A CRYSTAL STRUCTURE OF THE CATALYTIC CORE (B'A' REGION)
REMARK 900 OF STAPHYLOCOCCUS AUREUS DNA GYRASE COMPLEXED
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES 544-579 DELETED AND REPLACED WITH TWO AMINO ACIDS,
REMARK 999 TG. THE C-TERMINUS OF GYRB (6B44) IS FUSED TO THE N-
REMARK 999 TERMINUS OF GYRA (A2)
REMARK 999 CATALYTIC TYROSINE (A123/B1123) MUTATED TO PHENYLALANINE.
REMARK 999 DNA (8MER, 12MER ON TOP 5'-3', 12MER, 8MER UNDER 3'-5')
REMARK 999 DNA CALLED 8-3NN - FOUR STRANDS (CALLED 8-3,12-3,12-4,8-4)
REMARK 999 CAN ANNEAL TO GIVE 3 DIFFERENT DUPLEXES 5' TGTGCGGT GTAC-
REMARK 999 CTACGGCT 8-3 12-3 3' ACACGCCA-CATG GATGCCGA 12-4 8-4 5'
REMARK 999 TGTGCGGT GTAC-ACCGCACA 8-3 12-3 3' ACACGCCA-CATG TGGCGTGT
REMARK 999 12-3 8-3 5' AGCCGTAG GTAC-CTACGGCT 8-4 12-3 3' TCGGCATC-
REMARK 999 CATG GATGCCGA 12-3 8-4
DBREF 2XCT B 410 545 UNP P66937 GYRB_STAAN 410 545
DBREF 2XCT B 580 644 UNP P66937 GYRB_STAAN 580 644
DBREF 2XCT B 1002 1491 UNP Q99XG5 GYRA_STAAN 2 491
DBREF 2XCT D 410 545 UNP P66937 GYRB_STAAN 410 545
DBREF 2XCT D 580 644 UNP P66937 GYRB_STAAN 580 644
DBREF 2XCT D 1002 1491 UNP Q99XG5 GYRA_STAAN 2 491
DBREF 2XCT S 410 545 UNP P66937 GYRB_STAAN 410 545
DBREF 2XCT S 580 644 UNP P66937 GYRB_STAAN 580 644
DBREF 2XCT S 1002 1491 UNP Q99XG5 GYRA_STAAN 2 491
DBREF 2XCT U 410 545 UNP P66937 GYRB_STAAN 410 545
DBREF 2XCT U 580 644 UNP P66937 GYRB_STAAN 580 644
DBREF 2XCT U 1002 1491 UNP Q99XG5 GYRA_STAAN 2 491
DBREF 2XCT E 1 8 PDB 2XCT 2XCT 1 8
DBREF 2XCT G 9 12 PDB 2XCT 2XCT 9 12
DBREF 2XCT F 1 8 PDB 2XCT 2XCT 1 8
DBREF 2XCT H 9 12 PDB 2XCT 2XCT 9 12
DBREF 2XCT W 1 8 PDB 2XCT 2XCT 1 8
DBREF 2XCT Y 9 12 PDB 2XCT 2XCT 9 12
DBREF 2XCT V 1 8 PDB 2XCT 2XCT 1 8
DBREF 2XCT X 9 12 PDB 2XCT 2XCT 9 12
SEQADV 2XCT MET B 409 UNP P66937 EXPRESSION TAG
SEQADV 2XCT THR B 544 UNP P66937 INSERTION
SEQADV 2XCT GLY B 545 UNP P66937 INSERTION
SEQADV 2XCT PHE B 1123 UNP Q99XG5 TYR 123 ENGINEERED MUTATION
SEQADV 2XCT MET D 409 UNP P66937 EXPRESSION TAG
SEQADV 2XCT THR D 544 UNP P66937 INSERTION
SEQADV 2XCT GLY D 545 UNP P66937 INSERTION
SEQADV 2XCT PHE D 1123 UNP Q99XG5 TYR 123 ENGINEERED MUTATION
SEQADV 2XCT MET S 409 UNP P66937 EXPRESSION TAG
SEQADV 2XCT THR S 544 UNP P66937 INSERTION
SEQADV 2XCT GLY S 545 UNP P66937 INSERTION
SEQADV 2XCT PHE S 1123 UNP Q99XG5 TYR 123 ENGINEERED MUTATION
SEQADV 2XCT MET U 409 UNP P66937 EXPRESSION TAG
SEQADV 2XCT THR U 544 UNP P66937 INSERTION
SEQADV 2XCT GLY U 545 UNP P66937 INSERTION
SEQADV 2XCT PHE U 1123 UNP Q99XG5 TYR 123 ENGINEERED MUTATION
SEQRES 1 B 692 MET ASP VAL ALA SER LEU PRO GLY LYS LEU ALA ASP CYS
SEQRES 2 B 692 SER SER LYS SER PRO GLU GLU CYS GLU ILE PHE LEU VAL
SEQRES 3 B 692 GLU GLY ASP SER ALA GLY GLY SER THR LYS SER GLY ARG
SEQRES 4 B 692 ASP SER ARG THR GLN ALA ILE LEU PRO LEU ARG GLY LYS
SEQRES 5 B 692 ILE LEU ASN VAL GLU LYS ALA ARG LEU ASP ARG ILE LEU
SEQRES 6 B 692 ASN ASN ASN GLU ILE ARG GLN MET ILE THR ALA PHE GLY
SEQRES 7 B 692 THR GLY ILE GLY GLY ASP PHE ASP LEU ALA LYS ALA ARG
SEQRES 8 B 692 TYR HIS LYS ILE VAL ILE MET THR ASP ALA ASP VAL ASP
SEQRES 9 B 692 GLY ALA HIS ILE ARG THR LEU LEU LEU THR PHE PHE TYR
SEQRES 10 B 692 ARG PHE MET ARG PRO LEU ILE GLU ALA GLY TYR VAL TYR
SEQRES 11 B 692 ILE ALA GLN PRO PRO THR GLY TYR LYS GLY LEU GLY GLU
SEQRES 12 B 692 MET ASN ALA ASP GLN LEU TRP GLU THR THR MET ASN PRO
SEQRES 13 B 692 GLU HIS ARG ALA LEU LEU GLN VAL LYS LEU GLU ASP ALA
SEQRES 14 B 692 ILE GLU ALA ASP GLN THR PHE GLU MET LEU MET GLY ASP
SEQRES 15 B 692 VAL VAL GLU ASN ARG ARG GLN PHE ILE GLU ASP ASN ALA
SEQRES 16 B 692 VAL TYR ALA ASN LEU ASP PHE ALA GLU LEU PRO GLN SER
SEQRES 17 B 692 ARG ILE ASN GLU ARG ASN ILE THR SER GLU MET ARG GLU
SEQRES 18 B 692 SER PHE LEU ASP TYR ALA MET SER VAL ILE VAL ALA ARG
SEQRES 19 B 692 ALA LEU PRO ASP VAL ARG ASP GLY LEU LYS PRO VAL HIS
SEQRES 20 B 692 ARG ARG ILE LEU TYR GLY LEU ASN GLU GLN GLY MET THR
SEQRES 21 B 692 PRO ASP LYS SER TYR LYS LYS SER ALA ARG ILE VAL GLY
SEQRES 22 B 692 ASP VAL MET GLY LYS TYR HIS PRO HIS GLY ASP SER SER
SEQRES 23 B 692 ILE TYR GLU ALA MET VAL ARG MET ALA GLN ASP PHE SER
SEQRES 24 B 692 TYR ARG TYR PRO LEU VAL ASP GLY GLN GLY ASN PHE GLY
SEQRES 25 B 692 SER MET ASP GLY ASP GLY ALA ALA ALA MET ARG PHE THR
SEQRES 26 B 692 GLU ALA ARG MET THR LYS ILE THR LEU GLU LEU LEU ARG
SEQRES 27 B 692 ASP ILE ASN LYS ASP THR ILE ASP PHE ILE ASP ASN TYR
SEQRES 28 B 692 ASP GLY ASN GLU ARG GLU PRO SER VAL LEU PRO ALA ARG
SEQRES 29 B 692 PHE PRO ASN LEU LEU ALA ASN GLY ALA SER GLY ILE ALA
SEQRES 30 B 692 VAL GLY MET ALA THR ASN ILE PRO PRO HIS ASN LEU THR
SEQRES 31 B 692 GLU LEU ILE ASN GLY VAL LEU SER LEU SER LYS ASN PRO
SEQRES 32 B 692 ASP ILE SER ILE ALA GLU LEU MET GLU ASP ILE GLU GLY
SEQRES 33 B 692 PRO ASP PHE PRO THR ALA GLY LEU ILE LEU GLY LYS SER
SEQRES 34 B 692 GLY ILE ARG ARG ALA TYR GLU THR GLY ARG GLY SER ILE
SEQRES 35 B 692 GLN MET ARG SER ARG ALA VAL ILE GLU GLU ARG GLY GLY
SEQRES 36 B 692 GLY ARG GLN ARG ILE VAL VAL THR GLU ILE PRO PHE GLN
SEQRES 37 B 692 VAL ASN LYS ALA ARG MET ILE GLU LYS ILE ALA GLU LEU
SEQRES 38 B 692 VAL ARG ASP LYS LYS ILE ASP GLY ILE THR ASP LEU ARG
SEQRES 39 B 692 ASP GLU THR SER LEU ARG THR GLY VAL ARG VAL VAL ILE
SEQRES 40 B 692 ASP VAL ARG LYS ASP ALA ASN ALA SER VAL ILE LEU ASN
SEQRES 41 B 692 ASN LEU TYR LYS GLN THR PRO LEU GLN THR SER PHE GLY
SEQRES 42 B 692 VAL ASN MET ILE ALA LEU VAL ASN GLY ARG PRO LYS LEU
SEQRES 43 B 692 ILE ASN LEU LYS GLU ALA LEU VAL HIS TYR LEU GLU HIS
SEQRES 44 B 692 GLN LYS THR VAL VAL ARG ARG ARG THR GLN TYR ASN LEU
SEQRES 45 B 692 ARG LYS ALA LYS ASP ARG ALA HIS ILE LEU GLU GLY LEU
SEQRES 46 B 692 ARG ILE ALA LEU ASP HIS ILE ASP GLU ILE ILE SER THR
SEQRES 47 B 692 ILE ARG GLU SER ASP THR ASP LYS VAL ALA MET GLU SER
SEQRES 48 B 692 LEU GLN GLN ARG PHE LYS LEU SER GLU LYS GLN ALA GLN
SEQRES 49 B 692 ALA ILE LEU ASP MET ARG LEU ARG ARG LEU THR GLY LEU
SEQRES 50 B 692 GLU ARG ASP LYS ILE GLU ALA GLU TYR ASN GLU LEU LEU
SEQRES 51 B 692 ASN TYR ILE SER GLU LEU GLU THR ILE LEU ALA ASP GLU
SEQRES 52 B 692 GLU VAL LEU LEU GLN LEU VAL ARG ASP GLU LEU THR GLU
SEQRES 53 B 692 ILE ARG ASP ARG PHE GLY ASP ASP ARG ARG THR GLU ILE
SEQRES 54 B 692 GLN LEU GLY
SEQRES 1 D 692 MET ASP VAL ALA SER LEU PRO GLY LYS LEU ALA ASP CYS
SEQRES 2 D 692 SER SER LYS SER PRO GLU GLU CYS GLU ILE PHE LEU VAL
SEQRES 3 D 692 GLU GLY ASP SER ALA GLY GLY SER THR LYS SER GLY ARG
SEQRES 4 D 692 ASP SER ARG THR GLN ALA ILE LEU PRO LEU ARG GLY LYS
SEQRES 5 D 692 ILE LEU ASN VAL GLU LYS ALA ARG LEU ASP ARG ILE LEU
SEQRES 6 D 692 ASN ASN ASN GLU ILE ARG GLN MET ILE THR ALA PHE GLY
SEQRES 7 D 692 THR GLY ILE GLY GLY ASP PHE ASP LEU ALA LYS ALA ARG
SEQRES 8 D 692 TYR HIS LYS ILE VAL ILE MET THR ASP ALA ASP VAL ASP
SEQRES 9 D 692 GLY ALA HIS ILE ARG THR LEU LEU LEU THR PHE PHE TYR
SEQRES 10 D 692 ARG PHE MET ARG PRO LEU ILE GLU ALA GLY TYR VAL TYR
SEQRES 11 D 692 ILE ALA GLN PRO PRO THR GLY TYR LYS GLY LEU GLY GLU
SEQRES 12 D 692 MET ASN ALA ASP GLN LEU TRP GLU THR THR MET ASN PRO
SEQRES 13 D 692 GLU HIS ARG ALA LEU LEU GLN VAL LYS LEU GLU ASP ALA
SEQRES 14 D 692 ILE GLU ALA ASP GLN THR PHE GLU MET LEU MET GLY ASP
SEQRES 15 D 692 VAL VAL GLU ASN ARG ARG GLN PHE ILE GLU ASP ASN ALA
SEQRES 16 D 692 VAL TYR ALA ASN LEU ASP PHE ALA GLU LEU PRO GLN SER
SEQRES 17 D 692 ARG ILE ASN GLU ARG ASN ILE THR SER GLU MET ARG GLU
SEQRES 18 D 692 SER PHE LEU ASP TYR ALA MET SER VAL ILE VAL ALA ARG
SEQRES 19 D 692 ALA LEU PRO ASP VAL ARG ASP GLY LEU LYS PRO VAL HIS
SEQRES 20 D 692 ARG ARG ILE LEU TYR GLY LEU ASN GLU GLN GLY MET THR
SEQRES 21 D 692 PRO ASP LYS SER TYR LYS LYS SER ALA ARG ILE VAL GLY
SEQRES 22 D 692 ASP VAL MET GLY LYS TYR HIS PRO HIS GLY ASP SER SER
SEQRES 23 D 692 ILE TYR GLU ALA MET VAL ARG MET ALA GLN ASP PHE SER
SEQRES 24 D 692 TYR ARG TYR PRO LEU VAL ASP GLY GLN GLY ASN PHE GLY
SEQRES 25 D 692 SER MET ASP GLY ASP GLY ALA ALA ALA MET ARG PHE THR
SEQRES 26 D 692 GLU ALA ARG MET THR LYS ILE THR LEU GLU LEU LEU ARG
SEQRES 27 D 692 ASP ILE ASN LYS ASP THR ILE ASP PHE ILE ASP ASN TYR
SEQRES 28 D 692 ASP GLY ASN GLU ARG GLU PRO SER VAL LEU PRO ALA ARG
SEQRES 29 D 692 PHE PRO ASN LEU LEU ALA ASN GLY ALA SER GLY ILE ALA
SEQRES 30 D 692 VAL GLY MET ALA THR ASN ILE PRO PRO HIS ASN LEU THR
SEQRES 31 D 692 GLU LEU ILE ASN GLY VAL LEU SER LEU SER LYS ASN PRO
SEQRES 32 D 692 ASP ILE SER ILE ALA GLU LEU MET GLU ASP ILE GLU GLY
SEQRES 33 D 692 PRO ASP PHE PRO THR ALA GLY LEU ILE LEU GLY LYS SER
SEQRES 34 D 692 GLY ILE ARG ARG ALA TYR GLU THR GLY ARG GLY SER ILE
SEQRES 35 D 692 GLN MET ARG SER ARG ALA VAL ILE GLU GLU ARG GLY GLY
SEQRES 36 D 692 GLY ARG GLN ARG ILE VAL VAL THR GLU ILE PRO PHE GLN
SEQRES 37 D 692 VAL ASN LYS ALA ARG MET ILE GLU LYS ILE ALA GLU LEU
SEQRES 38 D 692 VAL ARG ASP LYS LYS ILE ASP GLY ILE THR ASP LEU ARG
SEQRES 39 D 692 ASP GLU THR SER LEU ARG THR GLY VAL ARG VAL VAL ILE
SEQRES 40 D 692 ASP VAL ARG LYS ASP ALA ASN ALA SER VAL ILE LEU ASN
SEQRES 41 D 692 ASN LEU TYR LYS GLN THR PRO LEU GLN THR SER PHE GLY
SEQRES 42 D 692 VAL ASN MET ILE ALA LEU VAL ASN GLY ARG PRO LYS LEU
SEQRES 43 D 692 ILE ASN LEU LYS GLU ALA LEU VAL HIS TYR LEU GLU HIS
SEQRES 44 D 692 GLN LYS THR VAL VAL ARG ARG ARG THR GLN TYR ASN LEU
SEQRES 45 D 692 ARG LYS ALA LYS ASP ARG ALA HIS ILE LEU GLU GLY LEU
SEQRES 46 D 692 ARG ILE ALA LEU ASP HIS ILE ASP GLU ILE ILE SER THR
SEQRES 47 D 692 ILE ARG GLU SER ASP THR ASP LYS VAL ALA MET GLU SER
SEQRES 48 D 692 LEU GLN GLN ARG PHE LYS LEU SER GLU LYS GLN ALA GLN
SEQRES 49 D 692 ALA ILE LEU ASP MET ARG LEU ARG ARG LEU THR GLY LEU
SEQRES 50 D 692 GLU ARG ASP LYS ILE GLU ALA GLU TYR ASN GLU LEU LEU
SEQRES 51 D 692 ASN TYR ILE SER GLU LEU GLU THR ILE LEU ALA ASP GLU
SEQRES 52 D 692 GLU VAL LEU LEU GLN LEU VAL ARG ASP GLU LEU THR GLU
SEQRES 53 D 692 ILE ARG ASP ARG PHE GLY ASP ASP ARG ARG THR GLU ILE
SEQRES 54 D 692 GLN LEU GLY
SEQRES 1 E 8 DT DG DT DG DC DG DG DT
SEQRES 1 F 8 DA DG DC DC DG DT DA DG
SEQRES 1 G 12 DG DT DA DC DC DC DA DC DG DG DC DT
SEQRES 1 H 12 DG DT DA DC DA DC DC DG DC DA DC DA
SEQRES 1 S 692 MET ASP VAL ALA SER LEU PRO GLY LYS LEU ALA ASP CYS
SEQRES 2 S 692 SER SER LYS SER PRO GLU GLU CYS GLU ILE PHE LEU VAL
SEQRES 3 S 692 GLU GLY ASP SER ALA GLY GLY SER THR LYS SER GLY ARG
SEQRES 4 S 692 ASP SER ARG THR GLN ALA ILE LEU PRO LEU ARG GLY LYS
SEQRES 5 S 692 ILE LEU ASN VAL GLU LYS ALA ARG LEU ASP ARG ILE LEU
SEQRES 6 S 692 ASN ASN ASN GLU ILE ARG GLN MET ILE THR ALA PHE GLY
SEQRES 7 S 692 THR GLY ILE GLY GLY ASP PHE ASP LEU ALA LYS ALA ARG
SEQRES 8 S 692 TYR HIS LYS ILE VAL ILE MET THR ASP ALA ASP VAL ASP
SEQRES 9 S 692 GLY ALA HIS ILE ARG THR LEU LEU LEU THR PHE PHE TYR
SEQRES 10 S 692 ARG PHE MET ARG PRO LEU ILE GLU ALA GLY TYR VAL TYR
SEQRES 11 S 692 ILE ALA GLN PRO PRO THR GLY TYR LYS GLY LEU GLY GLU
SEQRES 12 S 692 MET ASN ALA ASP GLN LEU TRP GLU THR THR MET ASN PRO
SEQRES 13 S 692 GLU HIS ARG ALA LEU LEU GLN VAL LYS LEU GLU ASP ALA
SEQRES 14 S 692 ILE GLU ALA ASP GLN THR PHE GLU MET LEU MET GLY ASP
SEQRES 15 S 692 VAL VAL GLU ASN ARG ARG GLN PHE ILE GLU ASP ASN ALA
SEQRES 16 S 692 VAL TYR ALA ASN LEU ASP PHE ALA GLU LEU PRO GLN SER
SEQRES 17 S 692 ARG ILE ASN GLU ARG ASN ILE THR SER GLU MET ARG GLU
SEQRES 18 S 692 SER PHE LEU ASP TYR ALA MET SER VAL ILE VAL ALA ARG
SEQRES 19 S 692 ALA LEU PRO ASP VAL ARG ASP GLY LEU LYS PRO VAL HIS
SEQRES 20 S 692 ARG ARG ILE LEU TYR GLY LEU ASN GLU GLN GLY MET THR
SEQRES 21 S 692 PRO ASP LYS SER TYR LYS LYS SER ALA ARG ILE VAL GLY
SEQRES 22 S 692 ASP VAL MET GLY LYS TYR HIS PRO HIS GLY ASP SER SER
SEQRES 23 S 692 ILE TYR GLU ALA MET VAL ARG MET ALA GLN ASP PHE SER
SEQRES 24 S 692 TYR ARG TYR PRO LEU VAL ASP GLY GLN GLY ASN PHE GLY
SEQRES 25 S 692 SER MET ASP GLY ASP GLY ALA ALA ALA MET ARG PHE THR
SEQRES 26 S 692 GLU ALA ARG MET THR LYS ILE THR LEU GLU LEU LEU ARG
SEQRES 27 S 692 ASP ILE ASN LYS ASP THR ILE ASP PHE ILE ASP ASN TYR
SEQRES 28 S 692 ASP GLY ASN GLU ARG GLU PRO SER VAL LEU PRO ALA ARG
SEQRES 29 S 692 PHE PRO ASN LEU LEU ALA ASN GLY ALA SER GLY ILE ALA
SEQRES 30 S 692 VAL GLY MET ALA THR ASN ILE PRO PRO HIS ASN LEU THR
SEQRES 31 S 692 GLU LEU ILE ASN GLY VAL LEU SER LEU SER LYS ASN PRO
SEQRES 32 S 692 ASP ILE SER ILE ALA GLU LEU MET GLU ASP ILE GLU GLY
SEQRES 33 S 692 PRO ASP PHE PRO THR ALA GLY LEU ILE LEU GLY LYS SER
SEQRES 34 S 692 GLY ILE ARG ARG ALA TYR GLU THR GLY ARG GLY SER ILE
SEQRES 35 S 692 GLN MET ARG SER ARG ALA VAL ILE GLU GLU ARG GLY GLY
SEQRES 36 S 692 GLY ARG GLN ARG ILE VAL VAL THR GLU ILE PRO PHE GLN
SEQRES 37 S 692 VAL ASN LYS ALA ARG MET ILE GLU LYS ILE ALA GLU LEU
SEQRES 38 S 692 VAL ARG ASP LYS LYS ILE ASP GLY ILE THR ASP LEU ARG
SEQRES 39 S 692 ASP GLU THR SER LEU ARG THR GLY VAL ARG VAL VAL ILE
SEQRES 40 S 692 ASP VAL ARG LYS ASP ALA ASN ALA SER VAL ILE LEU ASN
SEQRES 41 S 692 ASN LEU TYR LYS GLN THR PRO LEU GLN THR SER PHE GLY
SEQRES 42 S 692 VAL ASN MET ILE ALA LEU VAL ASN GLY ARG PRO LYS LEU
SEQRES 43 S 692 ILE ASN LEU LYS GLU ALA LEU VAL HIS TYR LEU GLU HIS
SEQRES 44 S 692 GLN LYS THR VAL VAL ARG ARG ARG THR GLN TYR ASN LEU
SEQRES 45 S 692 ARG LYS ALA LYS ASP ARG ALA HIS ILE LEU GLU GLY LEU
SEQRES 46 S 692 ARG ILE ALA LEU ASP HIS ILE ASP GLU ILE ILE SER THR
SEQRES 47 S 692 ILE ARG GLU SER ASP THR ASP LYS VAL ALA MET GLU SER
SEQRES 48 S 692 LEU GLN GLN ARG PHE LYS LEU SER GLU LYS GLN ALA GLN
SEQRES 49 S 692 ALA ILE LEU ASP MET ARG LEU ARG ARG LEU THR GLY LEU
SEQRES 50 S 692 GLU ARG ASP LYS ILE GLU ALA GLU TYR ASN GLU LEU LEU
SEQRES 51 S 692 ASN TYR ILE SER GLU LEU GLU THR ILE LEU ALA ASP GLU
SEQRES 52 S 692 GLU VAL LEU LEU GLN LEU VAL ARG ASP GLU LEU THR GLU
SEQRES 53 S 692 ILE ARG ASP ARG PHE GLY ASP ASP ARG ARG THR GLU ILE
SEQRES 54 S 692 GLN LEU GLY
SEQRES 1 U 692 MET ASP VAL ALA SER LEU PRO GLY LYS LEU ALA ASP CYS
SEQRES 2 U 692 SER SER LYS SER PRO GLU GLU CYS GLU ILE PHE LEU VAL
SEQRES 3 U 692 GLU GLY ASP SER ALA GLY GLY SER THR LYS SER GLY ARG
SEQRES 4 U 692 ASP SER ARG THR GLN ALA ILE LEU PRO LEU ARG GLY LYS
SEQRES 5 U 692 ILE LEU ASN VAL GLU LYS ALA ARG LEU ASP ARG ILE LEU
SEQRES 6 U 692 ASN ASN ASN GLU ILE ARG GLN MET ILE THR ALA PHE GLY
SEQRES 7 U 692 THR GLY ILE GLY GLY ASP PHE ASP LEU ALA LYS ALA ARG
SEQRES 8 U 692 TYR HIS LYS ILE VAL ILE MET THR ASP ALA ASP VAL ASP
SEQRES 9 U 692 GLY ALA HIS ILE ARG THR LEU LEU LEU THR PHE PHE TYR
SEQRES 10 U 692 ARG PHE MET ARG PRO LEU ILE GLU ALA GLY TYR VAL TYR
SEQRES 11 U 692 ILE ALA GLN PRO PRO THR GLY TYR LYS GLY LEU GLY GLU
SEQRES 12 U 692 MET ASN ALA ASP GLN LEU TRP GLU THR THR MET ASN PRO
SEQRES 13 U 692 GLU HIS ARG ALA LEU LEU GLN VAL LYS LEU GLU ASP ALA
SEQRES 14 U 692 ILE GLU ALA ASP GLN THR PHE GLU MET LEU MET GLY ASP
SEQRES 15 U 692 VAL VAL GLU ASN ARG ARG GLN PHE ILE GLU ASP ASN ALA
SEQRES 16 U 692 VAL TYR ALA ASN LEU ASP PHE ALA GLU LEU PRO GLN SER
SEQRES 17 U 692 ARG ILE ASN GLU ARG ASN ILE THR SER GLU MET ARG GLU
SEQRES 18 U 692 SER PHE LEU ASP TYR ALA MET SER VAL ILE VAL ALA ARG
SEQRES 19 U 692 ALA LEU PRO ASP VAL ARG ASP GLY LEU LYS PRO VAL HIS
SEQRES 20 U 692 ARG ARG ILE LEU TYR GLY LEU ASN GLU GLN GLY MET THR
SEQRES 21 U 692 PRO ASP LYS SER TYR LYS LYS SER ALA ARG ILE VAL GLY
SEQRES 22 U 692 ASP VAL MET GLY LYS TYR HIS PRO HIS GLY ASP SER SER
SEQRES 23 U 692 ILE TYR GLU ALA MET VAL ARG MET ALA GLN ASP PHE SER
SEQRES 24 U 692 TYR ARG TYR PRO LEU VAL ASP GLY GLN GLY ASN PHE GLY
SEQRES 25 U 692 SER MET ASP GLY ASP GLY ALA ALA ALA MET ARG PHE THR
SEQRES 26 U 692 GLU ALA ARG MET THR LYS ILE THR LEU GLU LEU LEU ARG
SEQRES 27 U 692 ASP ILE ASN LYS ASP THR ILE ASP PHE ILE ASP ASN TYR
SEQRES 28 U 692 ASP GLY ASN GLU ARG GLU PRO SER VAL LEU PRO ALA ARG
SEQRES 29 U 692 PHE PRO ASN LEU LEU ALA ASN GLY ALA SER GLY ILE ALA
SEQRES 30 U 692 VAL GLY MET ALA THR ASN ILE PRO PRO HIS ASN LEU THR
SEQRES 31 U 692 GLU LEU ILE ASN GLY VAL LEU SER LEU SER LYS ASN PRO
SEQRES 32 U 692 ASP ILE SER ILE ALA GLU LEU MET GLU ASP ILE GLU GLY
SEQRES 33 U 692 PRO ASP PHE PRO THR ALA GLY LEU ILE LEU GLY LYS SER
SEQRES 34 U 692 GLY ILE ARG ARG ALA TYR GLU THR GLY ARG GLY SER ILE
SEQRES 35 U 692 GLN MET ARG SER ARG ALA VAL ILE GLU GLU ARG GLY GLY
SEQRES 36 U 692 GLY ARG GLN ARG ILE VAL VAL THR GLU ILE PRO PHE GLN
SEQRES 37 U 692 VAL ASN LYS ALA ARG MET ILE GLU LYS ILE ALA GLU LEU
SEQRES 38 U 692 VAL ARG ASP LYS LYS ILE ASP GLY ILE THR ASP LEU ARG
SEQRES 39 U 692 ASP GLU THR SER LEU ARG THR GLY VAL ARG VAL VAL ILE
SEQRES 40 U 692 ASP VAL ARG LYS ASP ALA ASN ALA SER VAL ILE LEU ASN
SEQRES 41 U 692 ASN LEU TYR LYS GLN THR PRO LEU GLN THR SER PHE GLY
SEQRES 42 U 692 VAL ASN MET ILE ALA LEU VAL ASN GLY ARG PRO LYS LEU
SEQRES 43 U 692 ILE ASN LEU LYS GLU ALA LEU VAL HIS TYR LEU GLU HIS
SEQRES 44 U 692 GLN LYS THR VAL VAL ARG ARG ARG THR GLN TYR ASN LEU
SEQRES 45 U 692 ARG LYS ALA LYS ASP ARG ALA HIS ILE LEU GLU GLY LEU
SEQRES 46 U 692 ARG ILE ALA LEU ASP HIS ILE ASP GLU ILE ILE SER THR
SEQRES 47 U 692 ILE ARG GLU SER ASP THR ASP LYS VAL ALA MET GLU SER
SEQRES 48 U 692 LEU GLN GLN ARG PHE LYS LEU SER GLU LYS GLN ALA GLN
SEQRES 49 U 692 ALA ILE LEU ASP MET ARG LEU ARG ARG LEU THR GLY LEU
SEQRES 50 U 692 GLU ARG ASP LYS ILE GLU ALA GLU TYR ASN GLU LEU LEU
SEQRES 51 U 692 ASN TYR ILE SER GLU LEU GLU THR ILE LEU ALA ASP GLU
SEQRES 52 U 692 GLU VAL LEU LEU GLN LEU VAL ARG ASP GLU LEU THR GLU
SEQRES 53 U 692 ILE ARG ASP ARG PHE GLY ASP ASP ARG ARG THR GLU ILE
SEQRES 54 U 692 GLN LEU GLY
SEQRES 1 V 8 DT DG DT DG DC DG DG DT
SEQRES 1 W 8 DA DG DC DC DG DT DA DG
SEQRES 1 X 12 DG DT DA DC DC DC DA DC DG DG DC DT
SEQRES 1 Y 12 DG DT DA DC DA DC DC DG DC DA DC DA
HET MN B2492 1
HET MN D2492 1
HET MN F2000 1
HET CPF G1020 24
HET MN G2000 1
HET CPF H1020 24
HET MN S2492 1
HET MN U2492 1
HET MN W2000 1
HET MN W2001 1
HET CPF X1020 24
HET CPF Y1020 24
HETNAM MN MANGANESE (II) ION
HETNAM CPF 1-CYCLOPROPYL-6-FLUORO-4-OXO-7-PIPERAZIN-1-
HETNAM 2 CPF YL-1,4-DIHYDROQUINOLINE-3-CARBOXYLIC ACID
HETSYN CPF CIPROFLOXACIN
FORMUL 13 MN 8(MN 2+)
FORMUL 14 CPF 4(C17 H18 F N3 O3)
HELIX 1 1 SER B 425 GLU B 428 5 4
HELIX 2 2 ASP B 437 ARG B 447 1 11
HELIX 3 3 ARG B 468 ASN B 474 1 7
HELIX 4 4 ASN B 475 GLY B 486 1 12
HELIX 5 5 ILE B 489 PHE B 493 5 5
HELIX 6 6 ASP B 510 MET B 528 1 19
HELIX 7 7 MET B 528 GLY B 535 1 8
HELIX 8 8 GLY B 582 MET B 586 5 5
HELIX 9 9 ASN B 587 THR B 595 1 9
HELIX 10 10 ASP B 610 GLY B 623 1 14
HELIX 11 11 VAL B 625 ALA B 637 1 13
HELIX 12 12 ILE B 1014 ALA B 1032 1 19
HELIX 13 13 LYS B 1043 GLY B 1057 1 15
HELIX 14 14 SER B 1067 TYR B 1078 1 12
HELIX 15 15 GLY B 1082 MET B 1093 1 12
HELIX 16 16 THR B 1129 LEU B 1136 5 8
HELIX 17 17 PRO B 1165 GLY B 1171 1 7
HELIX 18 18 ASN B 1187 ASN B 1201 1 15
HELIX 19 19 SER B 1205 LEU B 1209 5 5
HELIX 20 20 GLY B 1226 ARG B 1232 1 7
HELIX 21 21 ARG B 1232 GLY B 1237 1 6
HELIX 22 22 ASN B 1269 ARG B 1282 1 14
HELIX 23 23 ASN B 1313 THR B 1325 1 13
HELIX 24 24 ASN B 1347 HIS B 1390 1 44
HELIX 25 25 HIS B 1390 GLU B 1400 1 11
HELIX 26 26 THR B 1403 ARG B 1414 1 12
HELIX 27 27 SER B 1418 ASP B 1427 1 10
HELIX 28 28 LEU B 1430 THR B 1434 5 5
HELIX 29 29 GLY B 1435 ALA B 1460 1 26
HELIX 30 30 GLU B 1463 GLY B 1481 1 19
HELIX 31 31 SER D 425 CYS D 429 5 5
HELIX 32 32 SER D 442 ARG D 447 1 6
HELIX 33 33 ARG D 468 LEU D 473 1 6
HELIX 34 34 ASN D 475 GLY D 486 1 12
HELIX 35 35 ILE D 489 PHE D 493 5 5
HELIX 36 36 ASP D 510 ARG D 526 1 17
HELIX 37 37 MET D 528 GLY D 535 1 8
HELIX 38 38 ALA D 588 MET D 596 1 9
HELIX 39 39 ASP D 610 GLY D 623 1 14
HELIX 40 40 VAL D 625 ASN D 636 1 12
HELIX 41 41 ILE D 1014 PHE D 1022 1 9
HELIX 42 42 PHE D 1022 ARG D 1033 1 12
HELIX 43 43 LYS D 1043 GLN D 1056 1 14
HELIX 44 44 SER D 1067 TYR D 1078 1 12
HELIX 45 45 GLY D 1082 MET D 1093 1 12
HELIX 46 46 ALA D 1120 PHE D 1123 5 4
HELIX 47 47 THR D 1129 ARG D 1137 1 9
HELIX 48 48 PRO D 1165 GLY D 1171 1 7
HELIX 49 49 ASN D 1187 LYS D 1200 1 14
HELIX 50 50 SER D 1205 MET D 1210 1 6
HELIX 51 51 GLY D 1226 GLY D 1237 1 12
HELIX 52 52 ASN D 1269 ASP D 1283 1 15
HELIX 53 53 ASN D 1313 THR D 1325 1 13
HELIX 54 54 ASN D 1347 HIS D 1390 1 44
HELIX 55 55 HIS D 1390 GLU D 1400 1 11
HELIX 56 56 THR D 1403 LYS D 1416 1 14
HELIX 57 57 SER D 1418 LEU D 1426 1 9
HELIX 58 58 LEU D 1430 LEU D 1433 5 4
HELIX 59 59 THR D 1434 ALA D 1460 1 27
HELIX 60 60 ASP D 1461 PHE D 1480 1 20
HELIX 61 61 ASP S 437 SER S 445 1 9
HELIX 62 62 ASN S 463 ALA S 467 5 5
HELIX 63 63 ARG S 468 LEU S 473 1 6
HELIX 64 64 ASN S 475 ILE S 482 1 8
HELIX 65 65 ILE S 489 PHE S 493 5 5
HELIX 66 66 ASP S 512 PHE S 527 1 16
HELIX 67 67 MET S 528 ALA S 534 1 7
HELIX 68 68 ALA S 588 MET S 596 1 9
HELIX 69 69 ASP S 610 MET S 622 1 13
HELIX 70 70 VAL S 626 ASN S 636 1 11
HELIX 71 71 ASN S 1013 ALA S 1032 1 20
HELIX 72 72 LYS S 1043 GLU S 1055 1 13
HELIX 73 73 SER S 1067 LYS S 1077 1 11
HELIX 74 74 GLY S 1082 ARG S 1092 1 11
HELIX 75 75 THR S 1132 ARG S 1137 1 6
HELIX 76 76 PRO S 1165 GLY S 1171 1 7
HELIX 77 77 ASN S 1187 SER S 1199 1 13
HELIX 78 78 SER S 1205 ILE S 1213 1 9
HELIX 79 79 LYS S 1227 THR S 1236 1 10
HELIX 80 80 ASN S 1269 LYS S 1284 1 16
HELIX 81 81 ASN S 1313 ASN S 1320 1 8
HELIX 82 82 ASN S 1347 HIS S 1390 1 44
HELIX 83 83 HIS S 1390 GLU S 1400 1 11
HELIX 84 84 THR S 1403 ARG S 1414 1 12
HELIX 85 85 SER S 1418 MET S 1428 1 11
HELIX 86 86 LEU S 1430 THR S 1434 5 5
HELIX 87 87 THR S 1434 ARG S 1438 5 5
HELIX 88 88 ASP S 1439 ILE S 1458 1 20
HELIX 89 89 ASP S 1461 GLY S 1481 1 21
HELIX 90 90 ASP U 437 GLY U 446 1 10
HELIX 91 91 ARG U 468 LEU U 473 1 6
HELIX 92 92 ASN U 475 GLY U 486 1 12
HELIX 93 93 ILE U 489 PHE U 493 5 5
HELIX 94 94 ASP U 494 ALA U 498 5 5
HELIX 95 95 ASP U 510 MET U 528 1 19
HELIX 96 96 MET U 528 GLY U 535 1 8
HELIX 97 97 ASN U 587 ASN U 597 1 11
HELIX 98 98 ALA U 611 LEU U 621 1 11
HELIX 99 99 VAL U 625 ASN U 636 1 12
HELIX 100 100 THR U 1015 ALA U 1032 1 18
HELIX 101 101 LYS U 1043 GLN U 1056 1 14
HELIX 102 102 SER U 1067 TYR U 1078 1 12
HELIX 103 103 GLY U 1082 VAL U 1091 1 10
HELIX 104 104 THR U 1129 ARG U 1137 1 9
HELIX 105 105 PRO U 1165 GLY U 1171 1 7
HELIX 106 106 ASN U 1187 SER U 1199 1 13
HELIX 107 107 SER U 1205 ILE U 1213 1 9
HELIX 108 108 LYS U 1227 GLY U 1237 1 11
HELIX 109 109 ASN U 1269 ASP U 1283 1 15
HELIX 110 110 ASN U 1313 LEU U 1318 1 6
HELIX 111 111 LEU U 1318 GLN U 1324 1 7
HELIX 112 112 ASN U 1347 HIS U 1390 1 44
HELIX 113 113 HIS U 1390 GLU U 1400 1 11
HELIX 114 114 THR U 1403 LYS U 1416 1 14
HELIX 115 115 SER U 1418 ASP U 1427 1 10
HELIX 116 116 LEU U 1430 THR U 1434 5 5
HELIX 117 117 LEU U 1436 ASP U 1461 1 26
HELIX 118 118 ASP U 1461 PHE U 1480 1 20
SHEET 1 BA 6 GLN B 452 PRO B 456 0
SHEET 2 BA 6 GLU B 430 VAL B 434 1 O GLU B 430 N ALA B 453
SHEET 3 BA 6 LYS B 502 MET B 506 1 O LYS B 502 N ILE B 431
SHEET 4 BA 6 VAL B 537 ALA B 540 1 O TYR B 538 N ILE B 505
SHEET 5 BA 6 LEU B 603 LYS B 607 -1 O LEU B 604 N ILE B 539
SHEET 6 BA 6 GLU B1011 ASN B1013 1 O ARG B1012 N LYS B 607
SHEET 1 BB 3 LYS B1065 LYS B1066 0
SHEET 2 BB 3 GLU B1125 ARG B1127 -1 O ALA B1126 N LYS B1065
SHEET 3 BB 3 ASP B1105 GLN B1107 -1 O ASP B1105 N ARG B1127
SHEET 1 BC 2 PHE B1146 ASP B1148 0
SHEET 2 BC 2 ARG B1155 PRO B1157 -1 O GLU B1156 N ILE B1147
SHEET 1 BD 4 THR B1329 ASN B1334 0
SHEET 2 BD 4 ARG B1238 ARG B1244 -1 O GLY B1239 N VAL B1333
SHEET 3 BD 4 GLY B1222 LEU B1225 -1 O LEU B1223 N ARG B1244
SHEET 4 BD 4 THR B1486 GLN B1489 1 O GLU B1487 N ILE B1224
SHEET 1 BE 4 ALA B1247 GLU B1251 0
SHEET 2 BE 4 GLN B1257 VAL B1261 -1 O ARG B1258 N GLU B1250
SHEET 3 BE 4 VAL B1304 VAL B1308 -1 O VAL B1304 N VAL B1261
SHEET 4 BE 4 ILE B1289 ASP B1294 -1 N THR B1290 O ASP B1307
SHEET 1 BF 2 ILE B1336 VAL B1339 0
SHEET 2 BF 2 ARG B1342 LEU B1345 -1 O ARG B1342 N VAL B1339
SHEET 1 DA 4 ALA D 453 PRO D 456 0
SHEET 2 DA 4 ILE D 431 VAL D 434 1 O PHE D 432 N LEU D 455
SHEET 3 DA 4 ILE D 503 MET D 506 1 O VAL D 504 N LEU D 433
SHEET 4 DA 4 VAL D 537 TYR D 538 1 O TYR D 538 N ILE D 505
SHEET 1 DB 2 GLN D 605 LYS D 607 0
SHEET 2 DB 2 GLU D1011 ASN D1013 1 O ARG D1012 N LYS D 607
SHEET 1 DC 2 LYS D1065 LYS D1066 0
SHEET 2 DC 2 GLU D1125 ALA D1126 -1 O ALA D1126 N LYS D1065
SHEET 1 DD 2 PHE D1146 ASP D1148 0
SHEET 2 DD 2 ARG D1155 PRO D1157 -1 O GLU D1156 N ILE D1147
SHEET 1 DE 2 ALA D1172 ILE D1175 0
SHEET 2 DE 2 ALA D1180 ILE D1183 -1 O THR D1181 N GLY D1174
SHEET 1 DF 4 GLN D1328 PHE D1331 0
SHEET 2 DF 4 ILE D1241 ARG D1244 -1 O ILE D1241 N PHE D1331
SHEET 3 DF 4 LEU D1223 LEU D1225 -1 O LEU D1223 N ARG D1244
SHEET 4 DF 4 GLU D1487 GLN D1489 1 O GLU D1487 N ILE D1224
SHEET 1 DG 4 ARG D1246 GLY D1253 0
SHEET 2 DG 4 ARG D1256 GLU D1263 -1 O ARG D1256 N ARG D1252
SHEET 3 DG 4 VAL D1304 VAL D1308 -1 O VAL D1304 N VAL D1261
SHEET 4 DG 4 ILE D1289 ASP D1294 -1 N THR D1290 O ASP D1307
SHEET 1 DH 2 ILE D1336 VAL D1339 0
SHEET 2 DH 2 ARG D1342 LEU D1345 -1 O ARG D1342 N VAL D1339
SHEET 1 SA 5 GLN S 452 LEU S 455 0
SHEET 2 SA 5 GLU S 430 VAL S 434 1 O GLU S 430 N ALA S 453
SHEET 3 SA 5 LYS S 502 MET S 506 1 O LYS S 502 N ILE S 431
SHEET 4 SA 5 VAL S 537 ILE S 539 1 O TYR S 538 N ILE S 505
SHEET 5 SA 5 LEU S 604 GLN S 605 -1 O LEU S 604 N ILE S 539
SHEET 1 SB 3 LYS S1065 LYS S1066 0
SHEET 2 SB 3 GLU S1125 ARG S1127 -1 O ALA S1126 N LYS S1065
SHEET 3 SB 3 ASP S1105 GLY S1106 -1 O ASP S1105 N ARG S1127
SHEET 1 SC 2 PHE S1146 ASP S1148 0
SHEET 2 SC 2 ARG S1155 PRO S1157 -1 O GLU S1156 N ILE S1147
SHEET 1 SD 4 GLN S1328 ASN S1334 0
SHEET 2 SD 4 ARG S1238 ARG S1244 -1 O GLY S1239 N VAL S1333
SHEET 3 SD 4 GLY S1222 ILE S1224 -1 O LEU S1223 N ARG S1244
SHEET 4 SD 4 THR S1486 ILE S1488 1 O GLU S1487 N ILE S1224
SHEET 1 SE 3 GLU S1250 GLY S1253 0
SHEET 2 SE 3 ARG S1256 VAL S1261 -1 O ARG S1256 N ARG S1252
SHEET 3 SE 3 VAL S1304 VAL S1308 -1 O VAL S1304 N VAL S1261
SHEET 1 SF 2 LEU S1338 VAL S1339 0
SHEET 2 SF 2 ARG S1342 PRO S1343 -1 O ARG S1342 N VAL S1339
SHEET 1 UA 5 GLN U 452 PRO U 456 0
SHEET 2 UA 5 GLU U 430 VAL U 434 1 O GLU U 430 N ALA U 453
SHEET 3 UA 5 LYS U 502 ILE U 505 1 O LYS U 502 N ILE U 431
SHEET 4 UA 5 VAL U 537 ILE U 539 1 O TYR U 538 N ILE U 505
SHEET 5 UA 5 LEU U 604 GLN U 605 -1 O LEU U 604 N ILE U 539
SHEET 1 UB 3 LYS U1065 LYS U1066 0
SHEET 2 UB 3 GLU U1125 ARG U1127 -1 O ALA U1126 N LYS U1065
SHEET 3 UB 3 ASP U1105 GLN U1107 -1 O ASP U1105 N ARG U1127
SHEET 1 UC 2 PHE U1146 ASP U1148 0
SHEET 2 UC 2 ARG U1155 PRO U1157 -1 O GLU U1156 N ILE U1147
SHEET 1 UD 2 ALA U1172 ILE U1175 0
SHEET 2 UD 2 ALA U1180 ILE U1183 -1 O THR U1181 N GLY U1174
SHEET 1 UE 2 GLY U1222 LEU U1223 0
SHEET 2 UE 2 THR U1486 GLU U1487 1 N GLU U1487 O GLY U1222
SHEET 1 UF 4 ARG U1246 GLU U1250 0
SHEET 2 UF 4 ARG U1258 GLU U1263 -1 O ARG U1258 N GLU U1250
SHEET 3 UF 4 VAL U1304 VAL U1308 -1 O VAL U1304 N VAL U1261
SHEET 4 UF 4 ILE U1289 ASP U1294 -1 N THR U1290 O ASP U1307
LINK MN MN B2492 OD2 ASP B 510 1555 1555 1.72
LINK MN MN D2492 OD2 ASP D 508 1555 1555 2.55
LINK MN MN D2492 OD2 ASP D 510 1555 1555 2.02
LINK MN MN F2000 O2 CPF H1020 1555 1555 2.11
LINK MN MN F2000 O3 CPF H1020 1555 1555 2.10
LINK MN MN G2000 O2 CPF G1020 1555 1555 2.10
LINK MN MN G2000 O3 CPF G1020 1555 1555 2.11
LINK MN MN S2492 OD1 ASP S 510 1555 1555 2.65
LINK MN MN S2492 OD2 ASP S 508 1555 1555 2.10
LINK MN MN S2492 OD2 ASP S 510 1555 1555 2.25
LINK MN MN U2492 OD2 ASP U 510 1555 1555 2.62
LINK MN MN W2000 O3 CPF X1020 1555 1555 2.10
LINK MN MN W2000 O2 CPF X1020 1555 1555 2.10
LINK MN MN W2001 O3 CPF Y1020 1555 1555 2.08
LINK MN MN W2001 O2 CPF Y1020 1555 1555 2.12
SITE 1 AC1 2 ASP B 508 ASP B 510
SITE 1 AC2 2 ASP D 508 ASP D 510
SITE 1 AC3 7 ARG B 458 SER B1084 DT E 8 DG G 9
SITE 2 AC3 7 MN G2000 DC H 12 DA H 13
SITE 1 AC4 8 ARG D 458 GLU D 477 SER D1084 DG F 8
SITE 2 AC4 8 MN F2000 DC G 12 DC G 13 DG H 9
SITE 1 AC5 1 CPF G1020
SITE 1 AC6 1 CPF H1020
SITE 1 AC7 2 CPF X1020 DG Y 9
SITE 1 AC8 1 CPF Y1020
SITE 1 AC9 2 ASP S 508 ASP S 510
SITE 1 BC1 2 ASP U 508 ASP U 510
SITE 1 BC2 7 ARG S 458 GLY S 459 DG W 8 MN W2000
SITE 2 BC2 7 DC X 12 DC X 13 DG Y 9
SITE 1 BC3 7 SER S1084 ARG U 458 DT V 8 MN W2001
SITE 2 BC3 7 DG X 9 DC Y 12 DA Y 13
CRYST1 88.984 123.166 170.418 90.00 90.25 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 0.011238 0.000000 0.000049 0.00000
SCALE2 0.000000 0.008119 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005868 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
