HEADER ISOMERASE/DNA/ANTIBIOTIC 08-JUL-10 2XKK
TITLE CRYSTAL STRUCTURE OF MOXIFLOXACIN, DNA, AND A. BAUMANNII TOPO IV
TITLE 2 (PARE-PARC FUSION TRUNCATE)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TOPOISOMERASE IV;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: PARE SUBUNIT C-TERMINAL 28KDA DOMAIN, RESIDUES 370-627,
COMPND 5 PARC SUBUNIT N-TERMINAL 58KDA DOMAIN, RESIDUES 1 TO 503;
COMPND 6 EC: 5.99.1.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: THE CONSTRUCT IS A FUSION OF THE TOPO IV, PARE AND
COMPND 9 PARC SUBUNITS. RESIDUE 604 OF PARE IS LINKED TO RESIDUES 996 OF PARC;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: DNA;
COMPND 12 CHAIN: E;
COMPND 13 ENGINEERED: YES;
COMPND 14 OTHER_DETAILS: DNA CLEAVED INTO 2, COMPLEX TRAPPED BY MFX;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: DNA;
COMPND 17 CHAIN: F;
COMPND 18 ENGINEERED: YES;
COMPND 19 OTHER_DETAILS: DNA CLEAVED INTO 2, COMPLEX TRAPPED BY MFX
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ACINETOBACTER BAUMANNII;
SOURCE 3 ORGANISM_TAXID: 470;
SOURCE 4 STRAIN: EUROFINS MEDINET;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET22B;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 13 ORGANISM_TAXID: 32630;
SOURCE 14 MOL_ID: 3;
SOURCE 15 SYNTHETIC: YES;
SOURCE 16 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 17 ORGANISM_TAXID: 32630
KEYWDS ISOMERASE-DNA-ANTIBIOTIC COMPLEX, TYPE IIA TOPOISOMERASE, QUINOLONE,
KEYWDS 2 ANTIBACTERIAL AGENT
EXPDTA X-RAY DIFFRACTION
AUTHOR A.WOHLKONIG,P.F.CHAN,A.P.FOSBERRY,P.HOMES,J.HUANG,M.KRANZ,V.R.LEYDON,
AUTHOR 2 T.J.MILES,N.D.PEARSON,R.L.PERERA,A.J.SHILLINGS,M.N.GWYNN,B.D.BAX
REVDAT 4 20-DEC-23 2XKK 1 REMARK LINK
REVDAT 3 12-OCT-11 2XKK 1 JRNL REMARK VERSN
REVDAT 2 08-SEP-10 2XKK 1 JRNL
REVDAT 1 01-SEP-10 2XKK 0
JRNL AUTH A.WOHLKONIG,P.F.CHAN,A.P.FOSBERRY,P.HOMES,J.HUANG,M.KRANZ,
JRNL AUTH 2 V.R.LEYDON,T.J.MILES,N.D.PEARSON,R.L.PERERA,A.J.SHILLINGS,
JRNL AUTH 3 M.N.GWYNN,B.D.BAX
JRNL TITL STRUCTURAL BASIS OF QUINOLONE INHIBITION OF TYPE IIA
JRNL TITL 2 TOPOISOMERASES AND TARGET-MEDIATED RESISTANCE
JRNL REF NAT.STRUCT.MOL.BIOL. V. 17 1152 2010
JRNL REFN ISSN 1545-9993
JRNL PMID 20802486
JRNL DOI 10.1038/NSMB.1892
REMARK 2
REMARK 2 RESOLUTION. 3.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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) : 3.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.17
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 32221
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1316
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 36.1678 - 6.7585 0.90 3266 153 0.1866 0.2418
REMARK 3 2 6.7585 - 5.3701 0.99 3501 167 0.1836 0.2743
REMARK 3 3 5.3701 - 4.6929 0.99 3536 145 0.1537 0.2213
REMARK 3 4 4.6929 - 4.2645 0.99 3529 122 0.1552 0.2464
REMARK 3 5 4.2645 - 3.9593 0.94 3329 136 0.1782 0.2530
REMARK 3 6 3.9593 - 3.7261 0.99 3515 137 0.1978 0.2758
REMARK 3 7 3.7261 - 3.5397 0.99 3467 158 0.2303 0.3563
REMARK 3 8 3.5397 - 3.3857 0.99 3498 157 0.2443 0.3059
REMARK 3 9 3.3857 - 3.2554 0.93 3264 141 0.2658 0.3444
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 : 0.29
REMARK 3 B_SOL : 96.77
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.400
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 109.0
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 133.6
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -29.25450
REMARK 3 B22 (A**2) : 18.70980
REMARK 3 B33 (A**2) : 10.54470
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -17.98420
REMARK 3 B23 (A**2) : 0.00000
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 : 0.013 12185
REMARK 3 ANGLE : 1.493 16775
REMARK 3 CHIRALITY : 0.074 1942
REMARK 3 PLANARITY : 0.005 2002
REMARK 3 DIHEDRAL : 19.435 4548
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 15
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ((CHAIN A AND (RESID 385:503 OR RESID 539:567)))
REMARK 3 ORIGIN FOR THE GROUP (A): -16.2141 64.2109 -17.8156
REMARK 3 T TENSOR
REMARK 3 T11: 1.7952 T22: 0.9982
REMARK 3 T33: 2.1077 T12: -0.3526
REMARK 3 T13: -0.2160 T23: -0.0585
REMARK 3 L TENSOR
REMARK 3 L11: 1.1184 L22: 0.3513
REMARK 3 L33: 1.8057 L12: -0.6231
REMARK 3 L13: -0.9530 L23: -0.3505
REMARK 3 S TENSOR
REMARK 3 S11: -0.2384 S12: 0.3447 S13: 0.9872
REMARK 3 S21: -0.2074 S22: 0.0718 S23: -0.2792
REMARK 3 S31: -0.8104 S32: 0.7256 S33: -0.0001
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ((CHAIN A AND (RESID 504:538)))
REMARK 3 ORIGIN FOR THE GROUP (A): -41.0069 67.7118 -28.6754
REMARK 3 T TENSOR
REMARK 3 T11: 2.2738 T22: 1.6924
REMARK 3 T33: 2.5535 T12: -0.1615
REMARK 3 T13: -0.4512 T23: 0.2308
REMARK 3 L TENSOR
REMARK 3 L11: 0.0742 L22: 0.1033
REMARK 3 L33: 0.0561 L12: -0.0065
REMARK 3 L13: -0.0402 L23: -0.0820
REMARK 3 S TENSOR
REMARK 3 S11: 0.7741 S12: 0.7043 S13: -0.0648
REMARK 3 S21: -0.1627 S22: -0.9099 S23: 1.7363
REMARK 3 S31: -0.7513 S32: -0.1885 S33: 0.0002
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ((CHAIN A AND (RESID 569:596)) OR ((CHAIN A) AND
REMARK 3 (RESID 1013:1026)))
REMARK 3 ORIGIN FOR THE GROUP (A): -26.8610 66.3100 -0.0976
REMARK 3 T TENSOR
REMARK 3 T11: 1.9867 T22: 1.2280
REMARK 3 T33: 1.9101 T12: -0.0823
REMARK 3 T13: -0.0811 T23: -0.5266
REMARK 3 L TENSOR
REMARK 3 L11: 0.1660 L22: 0.1477
REMARK 3 L33: 0.2249 L12: -0.0343
REMARK 3 L13: -0.2325 L23: 0.2111
REMARK 3 S TENSOR
REMARK 3 S11: 0.4951 S12: -0.5597 S13: 1.1415
REMARK 3 S21: 0.1886 S22: -0.5320 S23: 0.0676
REMARK 3 S31: -0.1819 S32: 0.3413 S33: 0.0006
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: ((CHAIN A AND (RESID 1027:1246 OR RESID 1326:1367 OR
REMARK 3 RESID 1457:1486)))
REMARK 3 ORIGIN FOR THE GROUP (A): -43.8528 38.9538 -1.2371
REMARK 3 T TENSOR
REMARK 3 T11: 0.9547 T22: 0.7305
REMARK 3 T33: 0.8357 T12: 0.1698
REMARK 3 T13: -0.0390 T23: -0.3903
REMARK 3 L TENSOR
REMARK 3 L11: 3.4780 L22: 0.4824
REMARK 3 L33: 3.7261 L12: -0.3269
REMARK 3 L13: -1.2056 L23: 0.5194
REMARK 3 S TENSOR
REMARK 3 S11: -0.2240 S12: -0.6637 S13: 0.7316
REMARK 3 S21: 0.1536 S22: -0.0189 S23: -0.0746
REMARK 3 S31: -0.4835 S32: -0.2942 S33: -0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: ((CHAIN A AND (RESID 1247:1325)))
REMARK 3 ORIGIN FOR THE GROUP (A): -19.3744 20.7827 12.3293
REMARK 3 T TENSOR
REMARK 3 T11: 1.1019 T22: 1.5935
REMARK 3 T33: 1.0560 T12: 0.0970
REMARK 3 T13: -0.0002 T23: 0.0582
REMARK 3 L TENSOR
REMARK 3 L11: 0.6373 L22: 0.4729
REMARK 3 L33: 0.8263 L12: -0.5588
REMARK 3 L13: -0.5062 L23: 0.4066
REMARK 3 S TENSOR
REMARK 3 S11: 0.0220 S12: -1.0265 S13: -0.3279
REMARK 3 S21: 0.2113 S22: -0.3497 S23: -0.2348
REMARK 3 S31: 0.3204 S32: 0.3943 S33: 0.0004
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: ((CHAIN A AND (RESID 1368:1378)) OR (CHAIN A AND
REMARK 3 (RESID 1439:1455)))
REMARK 3 ORIGIN FOR THE GROUP (A): -75.0223 40.5350 -12.0109
REMARK 3 T TENSOR
REMARK 3 T11: 1.1704 T22: 1.3636
REMARK 3 T33: 1.6026 T12: 0.2740
REMARK 3 T13: 0.0017 T23: -0.2804
REMARK 3 L TENSOR
REMARK 3 L11: 0.0814 L22: 0.0402
REMARK 3 L33: 0.0935 L12: 0.0791
REMARK 3 L13: 0.0934 L23: 0.0589
REMARK 3 S TENSOR
REMARK 3 S11: -0.5197 S12: -0.8185 S13: -0.1744
REMARK 3 S21: -0.4569 S22: 0.5079 S23: 0.3099
REMARK 3 S31: -0.3583 S32: -1.0668 S33: 0.0001
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: ((CHAIN A AND (RESID 1379:1434)))
REMARK 3 ORIGIN FOR THE GROUP (A): -83.8578 43.4856 -32.6780
REMARK 3 T TENSOR
REMARK 3 T11: 1.2418 T22: 1.4477
REMARK 3 T33: 1.4507 T12: 0.0976
REMARK 3 T13: -0.1700 T23: -0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 0.4498 L22: 0.2510
REMARK 3 L33: 0.9113 L12: -0.0887
REMARK 3 L13: -0.0356 L23: 0.4341
REMARK 3 S TENSOR
REMARK 3 S11: 0.0223 S12: 0.0312 S13: 0.0332
REMARK 3 S21: -0.4561 S22: -0.2277 S23: 1.1267
REMARK 3 S31: 0.0563 S32: -0.7235 S33: 0.0006
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: ((CHAIN C AND (RESID 1368:1378)) OR (CHAIN C AND
REMARK 3 (RESID 1439:1455)))
REMARK 3 ORIGIN FOR THE GROUP (A): -61.2413 34.5442 -56.5010
REMARK 3 T TENSOR
REMARK 3 T11: 1.2518 T22: 1.6912
REMARK 3 T33: 1.0692 T12: -0.2033
REMARK 3 T13: -0.2480 T23: 0.2963
REMARK 3 L TENSOR
REMARK 3 L11: 0.1620 L22: 0.0815
REMARK 3 L33: 0.2063 L12: 0.0519
REMARK 3 L13: -0.0465 L23: 0.0341
REMARK 3 S TENSOR
REMARK 3 S11: -0.2506 S12: 0.6930 S13: 0.0552
REMARK 3 S21: 0.3254 S22: -0.2219 S23: 0.0039
REMARK 3 S31: -0.2785 S32: 0.6230 S33: -0.0008
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: ((CHAIN C AND (RESID 1379:1434)))
REMARK 3 ORIGIN FOR THE GROUP (A): -80.0810 30.7741 -44.8506
REMARK 3 T TENSOR
REMARK 3 T11: 1.1760 T22: 1.4725
REMARK 3 T33: 1.3949 T12: -0.1249
REMARK 3 T13: -0.2435 T23: 0.0738
REMARK 3 L TENSOR
REMARK 3 L11: 0.7669 L22: 0.2622
REMARK 3 L33: 0.9967 L12: -0.0499
REMARK 3 L13: 0.1488 L23: 0.4487
REMARK 3 S TENSOR
REMARK 3 S11: -0.5578 S12: 0.6291 S13: 0.2206
REMARK 3 S21: -0.5809 S22: 0.4105 S23: 1.1243
REMARK 3 S31: -0.0223 S32: -1.1906 S33: -0.0001
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: ((CHAIN E) OR (CHAIN F))
REMARK 3 ORIGIN FOR THE GROUP (A): -13.4855 38.1383 -19.3872
REMARK 3 T TENSOR
REMARK 3 T11: 1.1763 T22: 1.2561
REMARK 3 T33: 1.4212 T12: -0.2853
REMARK 3 T13: -0.1039 T23: 0.0330
REMARK 3 L TENSOR
REMARK 3 L11: 2.1383 L22: 0.2836
REMARK 3 L33: 0.7544 L12: -0.6524
REMARK 3 L13: 0.7610 L23: -0.6968
REMARK 3 S TENSOR
REMARK 3 S11: -0.4521 S12: -0.1721 S13: 0.7158
REMARK 3 S21: 0.2424 S22: 0.0525 S23: -0.7030
REMARK 3 S31: -0.2707 S32: 0.7406 S33: -0.0001
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: ((CHAIN C AND (RESID 385:503 OR RESID 539:567)))
REMARK 3 ORIGIN FOR THE GROUP (A): -15.0056 12.9001 -19.3375
REMARK 3 T TENSOR
REMARK 3 T11: 0.9202 T22: 0.8775
REMARK 3 T33: 0.9405 T12: 0.0171
REMARK 3 T13: 0.1241 T23: 0.1305
REMARK 3 L TENSOR
REMARK 3 L11: 2.2263 L22: 2.1517
REMARK 3 L33: 3.6782 L12: 0.7839
REMARK 3 L13: 1.0405 L23: 0.6942
REMARK 3 S TENSOR
REMARK 3 S11: -0.0169 S12: -0.2140 S13: -0.1342
REMARK 3 S21: -0.0216 S22: 0.0158 S23: -0.2540
REMARK 3 S31: 0.2894 S32: 0.2648 S33: 0.0001
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: ((CHAIN C AND (RESID 504:538)))
REMARK 3 ORIGIN FOR THE GROUP (A): -41.2886 9.2443 -24.7110
REMARK 3 T TENSOR
REMARK 3 T11: 1.2692 T22: 1.3565
REMARK 3 T33: 1.5547 T12: -0.2073
REMARK 3 T13: -0.1142 T23: 0.1383
REMARK 3 L TENSOR
REMARK 3 L11: 0.1736 L22: 0.0624
REMARK 3 L33: 0.3473 L12: -0.0874
REMARK 3 L13: 0.2416 L23: -0.2095
REMARK 3 S TENSOR
REMARK 3 S11: 0.2341 S12: -0.4872 S13: 0.2119
REMARK 3 S21: -0.4087 S22: 0.2141 S23: 0.7740
REMARK 3 S31: 0.9030 S32: -1.1927 S33: 0.0012
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: ((CHAIN C AND (RESID 569:596)) OR ((CHAIN C) AND
REMARK 3 (RESID 1013:1026)))
REMARK 3 ORIGIN FOR THE GROUP (A): -13.8556 11.0979 -40.2908
REMARK 3 T TENSOR
REMARK 3 T11: 1.0173 T22: 0.9960
REMARK 3 T33: 0.9204 T12: -0.1644
REMARK 3 T13: 0.2833 T23: 0.0492
REMARK 3 L TENSOR
REMARK 3 L11: 0.2292 L22: 0.6814
REMARK 3 L33: 0.5057 L12: -0.2364
REMARK 3 L13: -0.1054 L23: 0.5289
REMARK 3 S TENSOR
REMARK 3 S11: 0.1910 S12: 0.8937 S13: -0.7211
REMARK 3 S21: -0.6000 S22: -0.6197 S23: 0.2316
REMARK 3 S31: -0.0288 S32: -0.1596 S33: -0.0006
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: ((CHAIN C AND (RESID 1027:1246 OR RESID 1326:1367 OR
REMARK 3 RESID 1457:1486)))
REMARK 3 ORIGIN FOR THE GROUP (A): -29.3864 37.4957 -48.5872
REMARK 3 T TENSOR
REMARK 3 T11: 1.0537 T22: 1.0711
REMARK 3 T33: 0.8412 T12: -0.1790
REMARK 3 T13: 0.0010 T23: 0.3242
REMARK 3 L TENSOR
REMARK 3 L11: 2.9245 L22: 0.4501
REMARK 3 L33: 3.5553 L12: -0.0088
REMARK 3 L13: -0.3879 L23: -0.1639
REMARK 3 S TENSOR
REMARK 3 S11: -0.0738 S12: 0.8963 S13: 0.4810
REMARK 3 S21: -0.2966 S22: 0.0366 S23: -0.0686
REMARK 3 S31: -0.3220 S32: 0.0525 S33: 0.0003
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: ((CHAIN C AND (RESID 1247:1325)))
REMARK 3 ORIGIN FOR THE GROUP (A): -2.0658 56.8288 -46.6072
REMARK 3 T TENSOR
REMARK 3 T11: 1.6262 T22: 1.6281
REMARK 3 T33: 2.0021 T12: -0.5419
REMARK 3 T13: 0.1369 T23: 0.5817
REMARK 3 L TENSOR
REMARK 3 L11: 0.1727 L22: 0.3953
REMARK 3 L33: 0.3075 L12: 0.4447
REMARK 3 L13: 0.0620 L23: 0.2195
REMARK 3 S TENSOR
REMARK 3 S11: 0.2142 S12: -0.0137 S13: 0.6069
REMARK 3 S21: -0.2937 S22: -0.2664 S23: -0.7801
REMARK 3 S31: -0.3391 S32: 0.3315 S33: -0.0000
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2XKK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-JUL-10.
REMARK 100 THE DEPOSITION ID IS D_1290044569.
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 : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9395
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32221
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.270
REMARK 200 RESOLUTION RANGE LOW (A) : 36.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.27
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : 0.46000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
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: PDB ENTRY 2XKJ
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 5000MME, 200 MM TRIS PH 8.5,
REMARK 280 100 MM MGCL2
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 99.88750
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.78300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 99.88750
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 47.78300
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 62960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -102.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 346
REMARK 465 GLU A 347
REMARK 465 MET A 348
REMARK 465 ALA A 349
REMARK 465 ILE A 350
REMARK 465 SER A 351
REMARK 465 LYS A 352
REMARK 465 ALA A 353
REMARK 465 GLY A 354
REMARK 465 ARG A 355
REMARK 465 ARG A 356
REMARK 465 LEU A 357
REMARK 465 LYS A 358
REMARK 465 ALA A 359
REMARK 465 ALA A 360
REMARK 465 LYS A 361
REMARK 465 LYS A 362
REMARK 465 VAL A 363
REMARK 465 GLU A 364
REMARK 465 ARG A 365
REMARK 465 LYS A 366
REMARK 465 LYS A 367
REMARK 465 ILE A 368
REMARK 465 VAL A 369
REMARK 465 SER A 370
REMARK 465 GLY A 371
REMARK 465 PRO A 372
REMARK 465 ALA A 379
REMARK 465 ASP A 380
REMARK 465 CYS A 381
REMARK 465 VAL A 382
REMARK 465 GLY A 383
REMARK 465 GLN A 384
REMARK 465 LYS A 529
REMARK 465 GLY A 530
REMARK 465 ASN A 531
REMARK 465 GLY A 597
REMARK 465 ASN A 598
REMARK 465 LEU A 599
REMARK 465 ALA A 600
REMARK 465 ASP A 601
REMARK 465 ILE A 602
REMARK 465 THR A 603
REMARK 465 VAL A 604
REMARK 465 GLU A 996
REMARK 465 ASP A 997
REMARK 465 LYS A 998
REMARK 465 LEU A 999
REMARK 465 THR A 1000
REMARK 465 MET A 1001
REMARK 465 THR A 1002
REMARK 465 SER A 1003
REMARK 465 LEU A 1004
REMARK 465 ALA A 1005
REMARK 465 HIS A 1006
REMARK 465 HIS A 1007
REMARK 465 ALA A 1008
REMARK 465 THR A 1009
REMARK 465 ARG A 1487
REMARK 465 ALA A 1488
REMARK 465 GLU A 1489
REMARK 465 ALA A 1490
REMARK 465 VAL A 1491
REMARK 465 GLN A 1492
REMARK 465 ILE A 1493
REMARK 465 LYS A 1494
REMARK 465 GLU A 1495
REMARK 465 GLN A 1496
REMARK 465 ASP A 1497
REMARK 465 LEU A 1498
REMARK 465 MET A 1499
REMARK 465 PRO A 1500
REMARK 465 ALA A 1501
REMARK 465 GLU A 1502
REMARK 465 THR A 1503
REMARK 465 MET C 346
REMARK 465 GLU C 347
REMARK 465 MET C 348
REMARK 465 ALA C 349
REMARK 465 ILE C 350
REMARK 465 SER C 351
REMARK 465 LYS C 352
REMARK 465 ALA C 353
REMARK 465 GLY C 354
REMARK 465 ARG C 355
REMARK 465 ARG C 356
REMARK 465 LEU C 357
REMARK 465 LYS C 358
REMARK 465 ALA C 359
REMARK 465 ALA C 360
REMARK 465 LYS C 361
REMARK 465 LYS C 362
REMARK 465 VAL C 363
REMARK 465 LYS C 529
REMARK 465 GLY C 530
REMARK 465 ASN C 531
REMARK 465 ASN C 598
REMARK 465 LEU C 599
REMARK 465 ALA C 600
REMARK 465 ASP C 601
REMARK 465 ILE C 602
REMARK 465 THR C 603
REMARK 465 VAL C 604
REMARK 465 GLU C 996
REMARK 465 ASP C 997
REMARK 465 LYS C 998
REMARK 465 LEU C 999
REMARK 465 THR C 1000
REMARK 465 MET C 1001
REMARK 465 THR C 1002
REMARK 465 SER C 1003
REMARK 465 LEU C 1004
REMARK 465 ALA C 1005
REMARK 465 HIS C 1006
REMARK 465 HIS C 1007
REMARK 465 ALA C 1488
REMARK 465 GLU C 1489
REMARK 465 ALA C 1490
REMARK 465 VAL C 1491
REMARK 465 GLN C 1492
REMARK 465 ILE C 1493
REMARK 465 LYS C 1494
REMARK 465 GLU C 1495
REMARK 465 GLN C 1496
REMARK 465 ASP C 1497
REMARK 465 LEU C 1498
REMARK 465 MET C 1499
REMARK 465 PRO C 1500
REMARK 465 ALA C 1501
REMARK 465 GLU C 1502
REMARK 465 THR C 1503
REMARK 465 DA E 1
REMARK 465 DC E 2
REMARK 465 DC E 3
REMARK 465 DA E 4
REMARK 465 DA E 5
REMARK 465 DC E 32
REMARK 465 DA E 33
REMARK 465 DG E 34
REMARK 465 DC F 1
REMARK 465 DT F 2
REMARK 465 DG F 3
REMARK 465 DT F 4
REMARK 465 DT F 31
REMARK 465 DG F 32
REMARK 465 DG F 33
REMARK 465 DT F 34
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 386 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 387 CG CD OE1 OE2
REMARK 470 SER A 389 OG
REMARK 470 ASP A 408 CG OD1 OD2
REMARK 470 LYS A 409 CG CD CE NZ
REMARK 470 ASP A 430 CG OD1 OD2
REMARK 470 GLU A 431 CG CD OE1 OE2
REMARK 470 ARG A 458 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 461 CG CD CE NZ
REMARK 470 LEU A 482 CG CD1 CD2
REMARK 470 LEU A 490 CG CD1 CD2
REMARK 470 VAL A 491 CG1 CG2
REMARK 470 GLU A 492 CG CD OE1 OE2
REMARK 470 GLU A 493 CG CD OE1 OE2
REMARK 470 VAL A 498 CG1 CG2
REMARK 470 LYS A 510 CG CD CE NZ
REMARK 470 ASP A 511 CG OD1 OD2
REMARK 470 LYS A 532 CG CD CE NZ
REMARK 470 LYS A 540 CG CD CE NZ
REMARK 470 LEU A 542 CG CD1 CD2
REMARK 470 ILE A 548 CG1 CG2 CD1
REMARK 470 ARG A 561 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 565 CG CD1 CD2
REMARK 470 LYS A 584 CG CD CE NZ
REMARK 470 ARG A 585 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 594 CG CD OE1 OE2
REMARK 470 LYS A 596 CG CD CE NZ
REMARK 470 GLU A1010 CG CD OE1 OE2
REMARK 470 ARG A1012 CG CD NE CZ NH1 NH2
REMARK 470 LYS A1065 CG CD CE NZ
REMARK 470 ASP A1149 N
REMARK 470 LYS A1156 CG CD CE NZ
REMARK 470 LYS A1194 CG CD CE NZ
REMARK 470 GLU A1212 CG CD OE1 OE2
REMARK 470 GLU A1230 CG CD OE1 OE2
REMARK 470 LYS A1234 CG CD CE NZ
REMARK 470 LYS A1253 CG CD CE NZ
REMARK 470 GLN A1279 CG CD OE1 NE2
REMARK 470 ARG A1290 CG CD NE CZ NH1 NH2
REMARK 470 LEU A1305 CG CD1 CD2
REMARK 470 ARG A1306 CG CD NE CZ NH1 NH2
REMARK 470 ASN A1308 CG OD1 ND2
REMARK 470 ARG A1309 CG CD NE CZ NH1 NH2
REMARK 470 GLU A1326 CG CD OE1 OE2
REMARK 470 ARG A1341 CG CD NE CZ NH1 NH2
REMARK 470 LYS A1375 CG CD CE NZ
REMARK 470 ARG A1395 CG CD NE CZ NH1 NH2
REMARK 470 ILE A1396 CG1 CG2 CD1
REMARK 470 ASP A1401 CG OD1 OD2
REMARK 470 GLN A1402 CG CD OE1 NE2
REMARK 470 LYS A1404 CG CD CE NZ
REMARK 470 ILE A1413 CG1 CG2 CD1
REMARK 470 GLU A1415 CG CD OE1 OE2
REMARK 470 LYS A1431 CG CD CE NZ
REMARK 470 GLU A1433 CG CD OE1 OE2
REMARK 470 MET A1435 CG SD CE
REMARK 470 GLU A1436 CG CD OE1 OE2
REMARK 470 ARG A1438 CG CD NE CZ NH1 NH2
REMARK 470 LYS A1447 CG CD CE NZ
REMARK 470 LYS A1470 CG CD CE NZ
REMARK 470 LYS A1474 CG CD CE NZ
REMARK 470 GLU C 387 CG CD OE1 OE2
REMARK 470 GLU C 388 CG CD OE1 OE2
REMARK 470 GLU C 431 CG CD OE1 OE2
REMARK 470 GLU C 456 CG CD OE1 OE2
REMARK 470 GLU C 522 CG CD OE1 OE2
REMARK 470 ASN C 527 CG OD1 ND2
REMARK 470 VAL C 528 CG1 CG2
REMARK 470 LYS C 532 CG CD CE NZ
REMARK 470 HIS C 571 CG ND1 CD2 CE1 NE2
REMARK 470 LEU C 572 CG CD1 CD2
REMARK 470 LYS C 583 CG CD CE NZ
REMARK 470 LYS C1059 CG CD CE NZ
REMARK 470 LYS C1209 CG CD CE NZ
REMARK 470 GLU C1224 CG CD OE1 OE2
REMARK 470 LEU C1233 CG CD1 CD2
REMARK 470 LYS C1234 CG CD CE NZ
REMARK 470 GLU C1255 CG CD OE1 OE2
REMARK 470 LYS C1269 CG CD CE NZ
REMARK 470 GLN C1279 CG CD OE1 NE2
REMARK 470 LYS C1281 CG CD CE NZ
REMARK 470 LYS C1282 CG CD CE NZ
REMARK 470 VAL C1287 CG1 CG2
REMARK 470 ARG C1290 CG CD NE CZ NH1 NH2
REMARK 470 GLU C1296 CG CD OE1 OE2
REMARK 470 ARG C1300 CG CD NE CZ NH1 NH2
REMARK 470 ARG C1306 CG CD NE CZ NH1 NH2
REMARK 470 ARG C1309 CG CD NE CZ NH1 NH2
REMARK 470 ILE C1397 CG1 CG2 CD1
REMARK 470 ARG C1398 CG CD NE CZ NH1 NH2
REMARK 470 ASP C1401 CG OD1 OD2
REMARK 470 LYS C1404 CG CD CE NZ
REMARK 470 GLU C1415 CG CD OE1 OE2
REMARK 470 LYS C1425 CG CD CE NZ
REMARK 470 LYS C1431 CG CD CE NZ
REMARK 470 MET C1435 CG SD CE
REMARK 470 ARG C1438 CG CD NE CZ NH1 NH2
REMARK 470 LYS C1447 CG CD CE NZ
REMARK 470 LYS C1470 CG CD CE NZ
REMARK 470 LYS C1474 CG CD CE NZ
REMARK 470 LYS C1475 CG CD CE NZ
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 OH TYR A 1132 ND2 ASN A 1167 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 E 16 O3' DG E 16 C3' -0.040
REMARK 500 DA E 20 O3' DA E 20 C3' -0.049
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 A1096 C - N - CA ANGL. DEV. = 9.3 DEGREES
REMARK 500 PRO C1229 C - N - CA ANGL. DEV. = 10.4 DEGREES
REMARK 500 PRO C1403 C - N - CA ANGL. DEV. = 9.8 DEGREES
REMARK 500 DG E 6 O4' - C1' - N9 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DT E 11 C3' - O3' - P ANGL. DEV. = 9.6 DEGREES
REMARK 500 DG E 12 O4' - C4' - C3' ANGL. DEV. = -6.3 DEGREES
REMARK 500 DG E 12 C4' - C3' - C2' ANGL. DEV. = -5.6 DEGREES
REMARK 500 DC E 18 O4' - C1' - N1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 DT E 19 O4' - C1' - N1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 DA E 20 C3' - C2' - C1' ANGL. DEV. = -6.7 DEGREES
REMARK 500 DA E 20 O4' - C1' - N9 ANGL. DEV. = 2.6 DEGREES
REMARK 500 DT E 21 O4' - C4' - C3' ANGL. DEV. = -3.4 DEGREES
REMARK 500 DT E 21 C1' - O4' - C4' ANGL. DEV. = -11.6 DEGREES
REMARK 500 DT E 21 O4' - C1' - N1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 DG E 22 O4' - C1' - N9 ANGL. DEV. = -5.5 DEGREES
REMARK 500 DC E 23 O4' - C4' - C3' ANGL. DEV. = -8.4 DEGREES
REMARK 500 DC E 25 O4' - C1' - N1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 DG E 26 O4' - C1' - N9 ANGL. DEV. = 4.2 DEGREES
REMARK 500 DA E 28 O4' - C1' - N9 ANGL. DEV. = 2.8 DEGREES
REMARK 500 DA E 29 O4' - C1' - N9 ANGL. DEV. = 3.0 DEGREES
REMARK 500 DA E 31 O4' - C1' - N9 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DT F 7 O4' - C1' - N1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 DG F 10 O4' - C4' - C3' ANGL. DEV. = -3.2 DEGREES
REMARK 500 DG F 10 O4' - C1' - N9 ANGL. DEV. = -4.5 DEGREES
REMARK 500 DT F 11 O4' - C1' - N1 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DC F 13 C3' - C2' - C1' ANGL. DEV. = -6.7 DEGREES
REMARK 500 DT F 15 N3 - C4 - O4 ANGL. DEV. = 4.0 DEGREES
REMARK 500 DT F 18 C3' - O3' - P ANGL. DEV. = 7.8 DEGREES
REMARK 500 DA F 20 C3' - C2' - C1' ANGL. DEV. = -5.0 DEGREES
REMARK 500 DA F 20 O4' - C1' - N9 ANGL. DEV. = 3.5 DEGREES
REMARK 500 DT F 21 C3' - C2' - C1' ANGL. DEV. = -7.7 DEGREES
REMARK 500 DT F 21 O4' - C1' - N1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 DC F 23 C1' - O4' - C4' ANGL. DEV. = -6.9 DEGREES
REMARK 500 DA F 24 O4' - C4' - C3' ANGL. DEV. = -2.6 DEGREES
REMARK 500 DT F 25 O4' - C1' - N1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 DC F 28 O4' - C4' - C3' ANGL. DEV. = -2.8 DEGREES
REMARK 500 DC F 29 O4' - C1' - N1 ANGL. DEV. = 5.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 398 -71.07 -68.88
REMARK 500 PHE A 483 -73.69 -81.04
REMARK 500 PHE A 487 58.90 -145.91
REMARK 500 LYS A 510 -5.15 -143.75
REMARK 500 ASP A 511 86.43 -67.25
REMARK 500 ASP A 517 -160.83 -166.04
REMARK 500 THR A 554 -12.01 -144.50
REMARK 500 MET A 555 -71.15 -103.58
REMARK 500 THR A 559 0.12 -159.96
REMARK 500 LEU A 562 113.87 -165.98
REMARK 500 ASP A 568 -143.95 73.45
REMARK 500 THR A 573 -82.79 -62.01
REMARK 500 ALA A 586 -28.08 -39.08
REMARK 500 GLN A 591 -73.83 -38.48
REMARK 500 TRP A 592 -50.90 -25.27
REMARK 500 TYR A1025 -70.58 -55.61
REMARK 500 ASP A1032 44.28 -100.16
REMARK 500 ARG A1033 -74.37 -164.33
REMARK 500 LEU A1058 42.99 -92.18
REMARK 500 LYS A1066 147.48 -32.96
REMARK 500 LYS A1077 -4.65 -145.97
REMARK 500 TYR A1078 -37.10 -139.97
REMARK 500 HIS A1081 -150.70 -143.75
REMARK 500 LYS A1128 -162.38 -122.95
REMARK 500 LEU A1135 -19.98 -48.05
REMARK 500 GLU A1139 33.23 -99.91
REMARK 500 GLN A1142 45.97 -92.04
REMARK 500 ALA A1177 -110.42 -105.88
REMARK 500 PRO A1220 1.21 -60.96
REMARK 500 LYS A1253 -116.16 70.41
REMARK 500 LYS A1269 -35.42 -38.48
REMARK 500 SER A1293 152.18 167.64
REMARK 500 ASP A1294 173.96 177.88
REMARK 500 ARG A1300 70.01 -170.73
REMARK 500 ARG A1306 -77.48 -80.14
REMARK 500 ASN A1308 23.16 -70.91
REMARK 500 THR A1322 -13.51 -150.40
REMARK 500 LEU A1333 63.76 -67.40
REMARK 500 MET A1335 153.62 171.71
REMARK 500 THR A1363 -72.59 -59.66
REMARK 500 ASN A1371 -2.24 -53.47
REMARK 500 GLU A1374 -77.24 -68.63
REMARK 500 LYS A1375 -26.57 -39.06
REMARK 500 ALA A1381 -70.01 -32.72
REMARK 500 LEU A1383 -70.68 -52.27
REMARK 500 LEU A1388 -80.27 -67.35
REMARK 500 ASP A1401 -74.96 -66.42
REMARK 500 GLU A1433 -3.12 -58.15
REMARK 500 PRO A1458 -38.63 -39.81
REMARK 500 GLU A1479 172.03 -58.21
REMARK 500
REMARK 500 THIS ENTRY HAS 102 RAMACHANDRAN OUTLIERS.
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 MG A2487 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 467 OD2
REMARK 620 2 ASP A 469 OD2 99.3
REMARK 620 3 HOH A2001 O 66.2 139.2
REMARK 620 4 HOH A2002 O 134.8 83.7 82.2
REMARK 620 5 HOH E2001 O 104.7 139.2 81.2 101.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1504 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2003 O
REMARK 620 2 MFX F1100 O03 107.2
REMARK 620 3 MFX F1100 O02 161.3 91.0
REMARK 620 4 HOH F2003 O 84.5 168.2 77.3
REMARK 620 5 HOH F2004 O 99.0 86.4 86.1 91.3
REMARK 620 6 HOH F2005 O 84.2 84.8 93.5 97.2 171.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C2488 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 467 OD2
REMARK 620 2 ASP C 469 OD1 112.1
REMARK 620 3 ASP C 469 OD2 116.9 50.5
REMARK 620 4 HOH C2002 O 80.5 128.8 162.2
REMARK 620 5 HOH C2006 O 65.2 141.3 94.5 89.7
REMARK 620 6 HOH C2009 O 141.2 102.0 71.8 92.4 76.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C1504 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C2014 O
REMARK 620 2 MFX E1100 O03 107.5
REMARK 620 3 MFX E1100 O02 169.6 80.9
REMARK 620 4 HOH E2003 O 83.1 168.9 88.2
REMARK 620 5 HOH E2004 O 85.4 86.1 89.2 91.7
REMARK 620 6 HOH F2001 O 87.7 100.5 96.8 82.7 171.6
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 2487
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 1504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 2488
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MFX E 1100
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2XKJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CATALYTIC CORE OF A. BAUMANNII TOPO IV (PARE-
REMARK 900 PARC FUSION TRUNCATE)
DBREF 2XKK A 347 604 UNP B0V9T6 B0V9T6_ACIBY 370 627
DBREF 2XKK A 996 1000 PDB 2XKK 2XKK 996 1000
DBREF 2XKK A 1001 1503 UNP B0VP98 B0VP98_ACIBS 1 503
DBREF 2XKK C 347 604 UNP B0V9T6 B0V9T6_ACIBY 370 627
DBREF 2XKK C 996 1000 PDB 2XKK 2XKK 996 1000
DBREF 2XKK C 1001 1503 UNP B0VP98 B0VP98_ACIBS 1 503
DBREF 2XKK E 1 34 PDB 2XKK 2XKK 1 34
DBREF 2XKK F 1 34 PDB 2XKK 2XKK 1 34
SEQADV 2XKK MET A 346 UNP B0V9T6 EXPRESSION TAG
SEQADV 2XKK MET C 346 UNP B0V9T6 EXPRESSION TAG
SEQRES 1 A 767 MET GLU MET ALA ILE SER LYS ALA GLY ARG ARG LEU LYS
SEQRES 2 A 767 ALA ALA LYS LYS VAL GLU ARG LYS LYS ILE VAL SER GLY
SEQRES 3 A 767 PRO ALA LEU PRO GLY LYS LEU ALA ASP CYS VAL GLY GLN
SEQRES 4 A 767 THR ARG GLU GLU SER GLU LEU PHE ILE VAL GLU GLY ASP
SEQRES 5 A 767 SER ALA GLY GLY SER ALA LYS GLN ALA ARG ASP LYS ASN
SEQRES 6 A 767 PHE GLN ALA ILE MET PRO ILE ARG GLY LYS ILE LEU ASN
SEQRES 7 A 767 THR TRP GLU VAL SER SER ASP GLU VAL LEU ALA SER GLN
SEQRES 8 A 767 GLU VAL HIS ASP ILE ALA ILE ALA ILE GLY VAL ASP PRO
SEQRES 9 A 767 GLY SER ASP ASP LEU SER GLU LEU ARG TYR GLY LYS ILE
SEQRES 10 A 767 CYS ILE LEU ALA ASP ALA ASP SER ASP GLY LEU HIS ILE
SEQRES 11 A 767 ALA THR LEU LEU CYS ALA LEU PHE VAL LYS HIS PHE PRO
SEQRES 12 A 767 ALA LEU VAL GLU GLU GLY HIS LEU TYR VAL ALA MET PRO
SEQRES 13 A 767 PRO LEU PHE ARG ILE ASP ILE GLY LYS ASP VAL HIS TYR
SEQRES 14 A 767 ALA LEU ASP ASP GLU GLU LEU GLU THR ILE LEU LYS ASN
SEQRES 15 A 767 VAL LYS GLY ASN LYS ASN PRO GLN ILE THR ARG PHE LYS
SEQRES 16 A 767 GLY LEU GLY GLU MET ASN ALA ILE GLN LEU ARG GLU THR
SEQRES 17 A 767 THR MET ASP PRO ASN THR ARG ARG LEU VAL GLN LEU ASP
SEQRES 18 A 767 LEU ASP ASP ALA HIS LEU THR ALA GLY LEU LEU ASP LYS
SEQRES 19 A 767 LEU LEU ALA LYS LYS ARG ALA ALA ASP ARG LYS GLN TRP
SEQRES 20 A 767 LEU GLU GLN LYS GLY ASN LEU ALA ASP ILE THR VAL GLU
SEQRES 21 A 767 ASP LYS LEU THR MET THR SER LEU ALA HIS HIS ALA THR
SEQRES 22 A 767 GLU ASN ARG SER VAL ALA GLU PHE THR GLU GLN ALA TYR
SEQRES 23 A 767 LEU ASN TYR ALA MET TYR VAL ILE MET ASP ARG ALA LEU
SEQRES 24 A 767 PRO HIS ILE SER ASP GLY LEU LYS PRO VAL GLN ARG ARG
SEQRES 25 A 767 ILE VAL TYR ALA MET SER GLU LEU GLY LEU LYS SER SER
SEQRES 26 A 767 GLY LYS PRO LYS LYS SER ALA ARG THR VAL GLY ASP VAL
SEQRES 27 A 767 LEU GLY LYS TYR HIS PRO HIS GLY ASP SER ALA CYS TYR
SEQRES 28 A 767 GLU ALA MET VAL LEU MET ALA GLN PRO PHE SER TYR ARG
SEQRES 29 A 767 TYR PRO LEU ILE GLU GLY GLN GLY ASN TRP GLY SER PRO
SEQRES 30 A 767 ASP ASP PRO LYS SER PHE ALA ALA MET ARG PTR THR GLU
SEQRES 31 A 767 ALA LYS LEU SER ALA TYR SER GLU LEU LEU LEU SER GLU
SEQRES 32 A 767 LEU GLY GLN GLY THR SER GLU TRP GLN ASP ASN PHE ASP
SEQRES 33 A 767 GLY SER LEU LYS GLU PRO ILE THR LEU PRO ALA ARG VAL
SEQRES 34 A 767 PRO ASN ILE LEU LEU ASN GLY THR THR GLY ILE ALA VAL
SEQRES 35 A 767 GLY MET ALA THR ASP ILE PRO PRO HIS ASN LEU ARG GLU
SEQRES 36 A 767 VAL VAL LYS GLY THR ILE ALA LEU ILE ARG ASN PRO GLN
SEQRES 37 A 767 THR SER ASP GLU LYS LEU ALA GLU TYR ILE PRO ALA PRO
SEQRES 38 A 767 ASP LEU PRO THR LYS ALA GLU ILE ILE THR PRO PRO GLU
SEQRES 39 A 767 GLU LEU LEU LYS ILE GLN THR THR GLY ARG GLY SER TYR
SEQRES 40 A 767 ARG MET ARG ALA VAL TYR THR ILE GLU LYS ASN GLU ILE
SEQRES 41 A 767 VAL ILE THR GLU LEU PRO TYR GLN VAL SER GLY SER LYS
SEQRES 42 A 767 VAL ILE THR GLN ILE ALA ASP GLN MET GLN ALA LYS LYS
SEQRES 43 A 767 LEU PRO LEU VAL VAL ASP VAL ARG ASP GLU SER ASP HIS
SEQRES 44 A 767 GLU ASN PRO THR ARG LEU VAL ILE VAL LEU ARG SER ASN
SEQRES 45 A 767 ARG ILE ASP ALA GLU ALA VAL MET SER HIS LEU PHE ALA
SEQRES 46 A 767 THR THR ASP LEU GLU SER SER TYR ARG VAL ASN LEU ASN
SEQRES 47 A 767 MET ILE GLY GLU ASP GLY ARG PRO GLN VAL LYS SER ILE
SEQRES 48 A 767 ARG ARG ILE LEU LEU GLU TRP ILE GLU ILE ARG LYS LYS
SEQRES 49 A 767 THR VAL THR ARG ARG LEU GLN TYR HIS LEU ASN ARG ILE
SEQRES 50 A 767 GLU LYS ARG LEU HIS ILE LEU ALA GLY LEU LEU ILE ALA
SEQRES 51 A 767 TYR LEU ASP ILE ASP THR VAL ILE ARG ILE ILE ARG GLU
SEQRES 52 A 767 GLU ASP GLN PRO LYS PRO VAL LEU MET GLU HIS PHE ASN
SEQRES 53 A 767 ILE ASP GLU ILE GLN ALA GLU ALA ILE LEU GLU LEU LYS
SEQRES 54 A 767 LEU ARG HIS LEU ALA LYS LEU GLU GLU MET GLU ILE ARG
SEQRES 55 A 767 HIS GLU GLN ASP GLU LEU SER ALA LYS ALA ALA ILE ILE
SEQRES 56 A 767 ARG GLU GLN LEU GLU ASN PRO GLU SER LEU LYS ASN LEU
SEQRES 57 A 767 ILE ILE SER GLU LEU LYS GLU ASP ALA LYS LYS PHE GLY
SEQRES 58 A 767 ASP GLU ARG ARG SER PRO ILE VAL ALA ARG ALA GLU ALA
SEQRES 59 A 767 VAL GLN ILE LYS GLU GLN ASP LEU MET PRO ALA GLU THR
SEQRES 1 C 767 MET GLU MET ALA ILE SER LYS ALA GLY ARG ARG LEU LYS
SEQRES 2 C 767 ALA ALA LYS LYS VAL GLU ARG LYS LYS ILE VAL SER GLY
SEQRES 3 C 767 PRO ALA LEU PRO GLY LYS LEU ALA ASP CYS VAL GLY GLN
SEQRES 4 C 767 THR ARG GLU GLU SER GLU LEU PHE ILE VAL GLU GLY ASP
SEQRES 5 C 767 SER ALA GLY GLY SER ALA LYS GLN ALA ARG ASP LYS ASN
SEQRES 6 C 767 PHE GLN ALA ILE MET PRO ILE ARG GLY LYS ILE LEU ASN
SEQRES 7 C 767 THR TRP GLU VAL SER SER ASP GLU VAL LEU ALA SER GLN
SEQRES 8 C 767 GLU VAL HIS ASP ILE ALA ILE ALA ILE GLY VAL ASP PRO
SEQRES 9 C 767 GLY SER ASP ASP LEU SER GLU LEU ARG TYR GLY LYS ILE
SEQRES 10 C 767 CYS ILE LEU ALA ASP ALA ASP SER ASP GLY LEU HIS ILE
SEQRES 11 C 767 ALA THR LEU LEU CYS ALA LEU PHE VAL LYS HIS PHE PRO
SEQRES 12 C 767 ALA LEU VAL GLU GLU GLY HIS LEU TYR VAL ALA MET PRO
SEQRES 13 C 767 PRO LEU PHE ARG ILE ASP ILE GLY LYS ASP VAL HIS TYR
SEQRES 14 C 767 ALA LEU ASP ASP GLU GLU LEU GLU THR ILE LEU LYS ASN
SEQRES 15 C 767 VAL LYS GLY ASN LYS ASN PRO GLN ILE THR ARG PHE LYS
SEQRES 16 C 767 GLY LEU GLY GLU MET ASN ALA ILE GLN LEU ARG GLU THR
SEQRES 17 C 767 THR MET ASP PRO ASN THR ARG ARG LEU VAL GLN LEU ASP
SEQRES 18 C 767 LEU ASP ASP ALA HIS LEU THR ALA GLY LEU LEU ASP LYS
SEQRES 19 C 767 LEU LEU ALA LYS LYS ARG ALA ALA ASP ARG LYS GLN TRP
SEQRES 20 C 767 LEU GLU GLN LYS GLY ASN LEU ALA ASP ILE THR VAL GLU
SEQRES 21 C 767 ASP LYS LEU THR MET THR SER LEU ALA HIS HIS ALA THR
SEQRES 22 C 767 GLU ASN ARG SER VAL ALA GLU PHE THR GLU GLN ALA TYR
SEQRES 23 C 767 LEU ASN TYR ALA MET TYR VAL ILE MET ASP ARG ALA LEU
SEQRES 24 C 767 PRO HIS ILE SER ASP GLY LEU LYS PRO VAL GLN ARG ARG
SEQRES 25 C 767 ILE VAL TYR ALA MET SER GLU LEU GLY LEU LYS SER SER
SEQRES 26 C 767 GLY LYS PRO LYS LYS SER ALA ARG THR VAL GLY ASP VAL
SEQRES 27 C 767 LEU GLY LYS TYR HIS PRO HIS GLY ASP SER ALA CYS TYR
SEQRES 28 C 767 GLU ALA MET VAL LEU MET ALA GLN PRO PHE SER TYR ARG
SEQRES 29 C 767 TYR PRO LEU ILE GLU GLY GLN GLY ASN TRP GLY SER PRO
SEQRES 30 C 767 ASP ASP PRO LYS SER PHE ALA ALA MET ARG PTR THR GLU
SEQRES 31 C 767 ALA LYS LEU SER ALA TYR SER GLU LEU LEU LEU SER GLU
SEQRES 32 C 767 LEU GLY GLN GLY THR SER GLU TRP GLN ASP ASN PHE ASP
SEQRES 33 C 767 GLY SER LEU LYS GLU PRO ILE THR LEU PRO ALA ARG VAL
SEQRES 34 C 767 PRO ASN ILE LEU LEU ASN GLY THR THR GLY ILE ALA VAL
SEQRES 35 C 767 GLY MET ALA THR ASP ILE PRO PRO HIS ASN LEU ARG GLU
SEQRES 36 C 767 VAL VAL LYS GLY THR ILE ALA LEU ILE ARG ASN PRO GLN
SEQRES 37 C 767 THR SER ASP GLU LYS LEU ALA GLU TYR ILE PRO ALA PRO
SEQRES 38 C 767 ASP LEU PRO THR LYS ALA GLU ILE ILE THR PRO PRO GLU
SEQRES 39 C 767 GLU LEU LEU LYS ILE GLN THR THR GLY ARG GLY SER TYR
SEQRES 40 C 767 ARG MET ARG ALA VAL TYR THR ILE GLU LYS ASN GLU ILE
SEQRES 41 C 767 VAL ILE THR GLU LEU PRO TYR GLN VAL SER GLY SER LYS
SEQRES 42 C 767 VAL ILE THR GLN ILE ALA ASP GLN MET GLN ALA LYS LYS
SEQRES 43 C 767 LEU PRO LEU VAL VAL ASP VAL ARG ASP GLU SER ASP HIS
SEQRES 44 C 767 GLU ASN PRO THR ARG LEU VAL ILE VAL LEU ARG SER ASN
SEQRES 45 C 767 ARG ILE ASP ALA GLU ALA VAL MET SER HIS LEU PHE ALA
SEQRES 46 C 767 THR THR ASP LEU GLU SER SER TYR ARG VAL ASN LEU ASN
SEQRES 47 C 767 MET ILE GLY GLU ASP GLY ARG PRO GLN VAL LYS SER ILE
SEQRES 48 C 767 ARG ARG ILE LEU LEU GLU TRP ILE GLU ILE ARG LYS LYS
SEQRES 49 C 767 THR VAL THR ARG ARG LEU GLN TYR HIS LEU ASN ARG ILE
SEQRES 50 C 767 GLU LYS ARG LEU HIS ILE LEU ALA GLY LEU LEU ILE ALA
SEQRES 51 C 767 TYR LEU ASP ILE ASP THR VAL ILE ARG ILE ILE ARG GLU
SEQRES 52 C 767 GLU ASP GLN PRO LYS PRO VAL LEU MET GLU HIS PHE ASN
SEQRES 53 C 767 ILE ASP GLU ILE GLN ALA GLU ALA ILE LEU GLU LEU LYS
SEQRES 54 C 767 LEU ARG HIS LEU ALA LYS LEU GLU GLU MET GLU ILE ARG
SEQRES 55 C 767 HIS GLU GLN ASP GLU LEU SER ALA LYS ALA ALA ILE ILE
SEQRES 56 C 767 ARG GLU GLN LEU GLU ASN PRO GLU SER LEU LYS ASN LEU
SEQRES 57 C 767 ILE ILE SER GLU LEU LYS GLU ASP ALA LYS LYS PHE GLY
SEQRES 58 C 767 ASP GLU ARG ARG SER PRO ILE VAL ALA ARG ALA GLU ALA
SEQRES 59 C 767 VAL GLN ILE LYS GLU GLN ASP LEU MET PRO ALA GLU THR
SEQRES 1 E 34 DA DC DC DA DA DG DG DT DC DA DT DG DA
SEQRES 2 E 34 DA DT DG DA DC DT DA DT DG DC DA DC DG
SEQRES 3 E 34 DT DA DA DA DA DC DA DG
SEQRES 1 F 34 DC DT DG DT DT DT DT DA DC DG DT DG DC
SEQRES 2 F 34 DA DT DA DG DT DC DA DT DT DC DA DT DG
SEQRES 3 F 34 DA DC DC DT DT DG DG DT
MODRES 2XKK PTR A 1124 TYR O-PHOSPHOTYROSINE
MODRES 2XKK PTR C 1124 TYR O-PHOSPHOTYROSINE
HET PTR A1124 16
HET PTR C1124 16
HET MG A1504 1
HET MG A2487 1
HET MG C1504 1
HET MG C2488 1
HET MFX E1100 29
HET MFX F1100 29
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM MG MAGNESIUM ION
HETNAM MFX 1-CYCLOPROPYL-6-FLUORO-8-METHOXY-7-[(4AS,7AS)-
HETNAM 2 MFX OCTAHYDRO-6H-PYRROLO[3,4-B]PYRIDIN-6-YL]-4-OXO-1,4-
HETNAM 3 MFX DIHYDROQUINOLINE-3-CARBOXYLIC ACID
HETSYN PTR PHOSPHONOTYROSINE
HETSYN MFX MOXIFLOXACIN
FORMUL 1 PTR 2(C9 H12 N O6 P)
FORMUL 5 MG 4(MG 2+)
FORMUL 9 MFX 2(C21 H24 F N3 O4)
FORMUL 11 HOH *40(H2 O)
HELIX 1 1 GLY A 396 ARG A 407 1 12
HELIX 2 2 SER A 428 LEU A 433 1 6
HELIX 3 3 SER A 435 GLY A 446 1 12
HELIX 4 4 ASP A 453 LEU A 457 5 5
HELIX 5 5 ASP A 469 PHE A 487 1 19
HELIX 6 6 PHE A 487 GLY A 494 1 8
HELIX 7 7 ASP A 517 LYS A 526 1 10
HELIX 8 8 GLY A 541 MET A 545 5 5
HELIX 9 9 ASN A 546 MET A 555 1 10
HELIX 10 10 ASP A 569 ALA A 582 1 14
HELIX 11 11 ARG A 585 LYS A 596 1 12
HELIX 12 12 SER A 1013 ASP A 1032 1 20
HELIX 13 13 LYS A 1043 GLU A 1055 1 13
HELIX 14 14 SER A 1067 TYR A 1078 1 12
HELIX 15 15 ASP A 1083 GLN A 1095 1 13
HELIX 16 16 ASP A 1115 PHE A 1119 5 5
HELIX 17 17 SER A 1133 SER A 1138 1 6
HELIX 18 18 PRO A 1166 ASN A 1171 1 6
HELIX 19 19 ASN A 1188 ASN A 1202 1 15
HELIX 20 20 SER A 1206 ALA A 1211 1 6
HELIX 21 21 PRO A 1228 GLY A 1239 1 12
HELIX 22 22 SER A 1266 LYS A 1281 1 16
HELIX 23 23 ASP A 1311 ALA A 1321 1 11
HELIX 24 24 SER A 1346 TYR A 1387 1 42
HELIX 25 25 ASP A 1389 GLU A 1400 1 12
HELIX 26 26 PRO A 1403 ASN A 1412 1 10
HELIX 27 27 ASP A 1414 GLU A 1423 1 10
HELIX 28 28 LEU A 1426 LEU A 1429 5 4
HELIX 29 29 ALA A 1430 ASN A 1457 1 28
HELIX 30 30 ASN A 1457 PHE A 1476 1 20
HELIX 31 31 GLY C 396 ARG C 407 1 12
HELIX 32 32 SER C 428 LEU C 433 1 6
HELIX 33 33 SER C 435 GLY C 446 1 12
HELIX 34 34 ASP C 453 LEU C 457 5 5
HELIX 35 35 ASP C 469 PHE C 487 1 19
HELIX 36 36 PHE C 487 GLU C 493 1 7
HELIX 37 37 ASP C 518 LYS C 526 1 9
HELIX 38 38 GLY C 541 MET C 545 5 5
HELIX 39 39 ASN C 546 THR C 554 1 9
HELIX 40 40 ASP C 556 ARG C 560 5 5
HELIX 41 41 ASP C 569 ALA C 582 1 14
HELIX 42 42 ARG C 585 LYS C 596 1 12
HELIX 43 43 VAL C 1014 ASP C 1032 1 19
HELIX 44 44 LYS C 1043 GLU C 1055 1 13
HELIX 45 45 SER C 1067 TYR C 1078 1 12
HELIX 46 46 GLY C 1082 GLN C 1095 1 14
HELIX 47 47 ASP C 1115 PHE C 1119 5 5
HELIX 48 48 SER C 1133 SER C 1138 1 6
HELIX 49 49 PRO C 1166 ASN C 1171 1 6
HELIX 50 50 ASN C 1188 ASN C 1202 1 15
HELIX 51 51 SER C 1206 ILE C 1214 1 9
HELIX 52 52 PRO C 1228 GLY C 1239 1 12
HELIX 53 53 SER C 1266 ALA C 1280 1 15
HELIX 54 54 ASP C 1311 PHE C 1320 1 10
HELIX 55 55 SER C 1346 ASP C 1389 1 44
HELIX 56 56 ASP C 1389 GLU C 1400 1 12
HELIX 57 57 PRO C 1403 ASN C 1412 1 10
HELIX 58 58 ASP C 1414 GLU C 1423 1 10
HELIX 59 59 LEU C 1426 LEU C 1429 5 4
HELIX 60 60 ALA C 1430 ASN C 1457 1 28
HELIX 61 61 ASN C 1457 PHE C 1476 1 20
SHEET 1 AA 5 GLN A 412 ILE A 417 0
SHEET 2 AA 5 GLU A 390 GLU A 395 1 O GLU A 390 N ALA A 413
SHEET 3 AA 5 LYS A 461 LEU A 465 1 O LYS A 461 N LEU A 391
SHEET 4 AA 5 LEU A 496 ALA A 499 1 O TYR A 497 N ILE A 464
SHEET 5 AA 5 LEU A 562 GLN A 564 -1 O VAL A 563 N VAL A 498
SHEET 1 AB 3 ASP A 511 ALA A 515 0
SHEET 2 AB 3 PHE A 504 ILE A 508 -1 O PHE A 504 N ALA A 515
SHEET 3 AB 3 THR A 537 ARG A 538 -1 O THR A 537 N ARG A 505
SHEET 1 AC 3 LYS A1065 LYS A1066 0
SHEET 2 AC 3 GLU A1126 LEU A1129 -1 O ALA A1127 N LYS A1065
SHEET 3 AC 3 ILE A1104 GLN A1107 -1 O GLU A1105 N LYS A1128
SHEET 1 AD 2 TRP A1147 GLN A1148 0
SHEET 2 AD 2 GLU A1157 PRO A1158 -1 O GLU A1157 N GLN A1148
SHEET 1 AE 2 THR A1174 ILE A1176 0
SHEET 2 AE 2 ALA A1181 ASP A1183 -1 O THR A1182 N GLY A1175
SHEET 1 AF 3 GLU A1224 ILE A1225 0
SHEET 2 AF 3 ARG A1240 ARG A1246 -1 O ARG A1246 N GLU A1224
SHEET 3 AF 3 GLU A1326 ASN A1332 -1 O SER A1327 N MET A1245
SHEET 1 AG 4 VAL A1248 GLU A1252 0
SHEET 2 AG 4 GLU A1255 GLU A1260 -1 O GLU A1255 N GLU A1252
SHEET 3 AG 4 LEU A1301 LEU A1305 -1 O LEU A1301 N ILE A1258
SHEET 4 AG 4 VAL A1286 ASP A1291 -1 N VAL A1287 O VAL A1304
SHEET 1 AH 2 ASN A1334 ILE A1336 0
SHEET 2 AH 2 PRO A1342 VAL A1344 -1 N GLN A1343 O MET A1335
SHEET 1 CA 6 GLN C 412 ILE C 417 0
SHEET 2 CA 6 GLU C 390 GLU C 395 1 O GLU C 390 N ALA C 413
SHEET 3 CA 6 ILE C 462 LEU C 465 1 O CYS C 463 N ILE C 393
SHEET 4 CA 6 LEU C 496 ALA C 499 1 O TYR C 497 N ILE C 464
SHEET 5 CA 6 LEU C 562 ASP C 566 -1 O VAL C 563 N VAL C 498
SHEET 6 CA 6 ASN C1011 SER C1013 1 O ARG C1012 N ASP C 566
SHEET 1 CB 3 VAL C 512 ALA C 515 0
SHEET 2 CB 3 PHE C 504 ASP C 507 -1 O PHE C 504 N ALA C 515
SHEET 3 CB 3 GLN C 535 ARG C 538 -1 O GLN C 535 N ASP C 507
SHEET 1 CC 3 LYS C1065 LYS C1066 0
SHEET 2 CC 3 GLU C1126 LEU C1129 -1 O ALA C1127 N LYS C1065
SHEET 3 CC 3 ILE C1104 GLN C1107 -1 O GLU C1105 N LYS C1128
SHEET 1 CD 2 TRP C1147 ASP C1149 0
SHEET 2 CD 2 LYS C1156 PRO C1158 -1 O GLU C1157 N GLN C1148
SHEET 1 CE 2 THR C1174 ILE C1176 0
SHEET 2 CE 2 ALA C1181 ASP C1183 -1 O THR C1182 N GLY C1175
SHEET 1 CF 3 GLU C1224 ILE C1225 0
SHEET 2 CF 3 ARG C1240 ARG C1246 -1 O ARG C1246 N GLU C1224
SHEET 3 CF 3 GLU C1326 ASN C1332 -1 O SER C1327 N MET C1245
SHEET 1 CG 4 VAL C1248 GLU C1252 0
SHEET 2 CG 4 GLU C1255 GLU C1260 -1 O GLU C1255 N GLU C1252
SHEET 3 CG 4 LEU C1301 LEU C1305 -1 O LEU C1301 N ILE C1258
SHEET 4 CG 4 VAL C1286 ASP C1291 -1 N VAL C1287 O VAL C1304
SHEET 1 CH 2 ASN C1334 ILE C1336 0
SHEET 2 CH 2 PRO C1342 VAL C1344 -1 O GLN C1343 N MET C1335
LINK C AARG A1123 N PTR A1124 1555 1555 1.33
LINK C BARG A1123 N PTR A1124 1555 1555 1.33
LINK C PTR A1124 N THR A1125 1555 1555 1.32
LINK O1P PTR A1124 C5' DA F 16 1555 1555 1.41
LINK C AARG C1123 N PTR C1124 1555 1555 1.33
LINK C BARG C1123 N PTR C1124 1555 1555 1.33
LINK C PTR C1124 N THR C1125 1555 1555 1.33
LINK O1P PTR C1124 C5' DG E 16 1555 1555 1.43
LINK OD2 ASP A 467 MG MG A2487 1555 1555 2.02
LINK OD2 ASP A 469 MG MG A2487 1555 1555 2.09
LINK MG MG A1504 O HOH A2003 1555 1555 2.05
LINK MG MG A1504 O03 MFX F1100 1555 1555 1.95
LINK MG MG A1504 O02 MFX F1100 1555 1555 1.95
LINK MG MG A1504 O HOH F2003 1555 1555 2.01
LINK MG MG A1504 O HOH F2004 1555 1555 2.13
LINK MG MG A1504 O HOH F2005 1555 1555 2.11
LINK O HOH A2001 MG MG A2487 1555 1555 2.05
LINK O HOH A2002 MG MG A2487 1555 1555 2.10
LINK MG MG A2487 O HOH E2001 1555 1555 1.99
LINK OD2 ASP C 467 MG MG C2488 1555 1555 2.12
LINK OD1 ASP C 469 MG MG C2488 1555 1555 2.79
LINK OD2 ASP C 469 MG MG C2488 1555 1555 2.07
LINK MG MG C1504 O HOH C2014 1555 1555 2.00
LINK MG MG C1504 O03 MFX E1100 1555 1555 1.99
LINK MG MG C1504 O02 MFX E1100 1555 1555 1.91
LINK MG MG C1504 O HOH E2003 1555 1555 1.99
LINK MG MG C1504 O HOH E2004 1555 1555 2.11
LINK MG MG C1504 O HOH F2001 1555 1555 2.09
LINK O HOH C2002 MG MG C2488 1555 1555 2.09
LINK O HOH C2006 MG MG C2488 1555 1555 2.10
LINK O HOH C2009 MG MG C2488 1555 1555 1.99
SITE 1 AC1 5 HOH A2003 MFX F1100 HOH F2003 HOH F2004
SITE 2 AC1 5 HOH F2005
SITE 1 AC2 5 ASP A 467 ASP A 469 HOH A2001 HOH A2002
SITE 2 AC2 5 HOH E2001
SITE 1 AC3 5 HOH C2014 MFX E1100 HOH E2003 HOH E2004
SITE 2 AC3 5 HOH F2001
SITE 1 AC4 5 ASP C 467 ASP C 469 HOH C2002 HOH C2006
SITE 2 AC4 5 HOH C2009
SITE 1 AC5 9 PTR A1124 MG C1504 DT E 19 DA E 20
SITE 2 AC5 9 HOH E2003 HOH E2004 DT F 15 DA F 16
SITE 3 AC5 9 HOH F2001
CRYST1 199.775 95.566 118.092 90.00 108.27 90.00 C 1 2 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 0.005006 0.000000 0.001653 0.00000
SCALE2 0.000000 0.010464 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008918 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
