HEADER OXIDOREDUCTASE/INHIBITOR 20-MAY-16 5K4L
TITLE CRYSTAL STRUCTURE OF KDM5A IN COMPLEX WITH A NAPHTHYRIDONE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSINE-SPECIFIC DEMETHYLASE 5A;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 12-797;
COMPND 5 SYNONYM: HISTONE DEMETHYLASE JARID1A,JUMONJI/ARID DOMAIN-CONTAINING
COMPND 6 PROTEIN 1A,RETINOBLASTOMA-BINDING PROTEIN 2,RBBP-2;
COMPND 7 EC: 1.14.11.-;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: UNKNOWN PEPTIDE;
COMPND 11 CHAIN: F, G;
COMPND 12 ENGINEERED: YES;
COMPND 13 OTHER_DETAILS: A LARGE SECTION OF MOLECULE 1 IS MISSING IN THE
COMPND 14 COORDINATES AND MOLECULE 2 IS PROBABLY A PART OF MOLECULE 1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: KDM5A, JARID1A, RBBP2, RBP2;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: KDM5A, JARID1A, RBBP2, RBP2;
SOURCE 14 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: SF9
KEYWDS EPIGENETICS, DEMETHYLASE, JUMONJI, INHIBITOR, CANCER, OXIDOREDUCTASE-
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.KIEFER,M.V.VINOGRADOVA
REVDAT 3 07-SEP-16 5K4L 1 JRNL
REVDAT 2 24-AUG-16 5K4L 1 JRNL
REVDAT 1 10-AUG-16 5K4L 0
JRNL AUTH S.S.LABADIE,P.S.DRAGOVICH,R.T.CUMMINGS,G.DESHMUKH,
JRNL AUTH 2 A.GUSTAFSON,N.HAN,J.C.HARMANGE,J.R.KIEFER,Y.LI,J.LIANG,
JRNL AUTH 3 B.M.LIEDERER,Y.LIU,W.MANIERI,W.MAO,L.MURRAY,D.F.ORTWINE,
JRNL AUTH 4 P.TROJER,E.VANDERPORTEN,M.VINOGRADOVA,L.WEN
JRNL TITL DESIGN AND EVALUATION OF 1,7-NAPHTHYRIDONES AS NOVEL KDM5
JRNL TITL 2 INHIBITORS.
JRNL REF BIOORG.MED.CHEM.LETT. V. 26 4492 2016
JRNL REFN ESSN 1464-3405
JRNL PMID 27499454
JRNL DOI 10.1016/J.BMCL.2016.07.070
REMARK 2
REMARK 2 RESOLUTION. 3.18 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.2_1309
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.18
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.50
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.9
REMARK 3 NUMBER OF REFLECTIONS : 40747
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.224
REMARK 3 R VALUE (WORKING SET) : 0.222
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.350
REMARK 3 FREE R VALUE TEST SET COUNT : 2181
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 30.0762 - 7.7984 0.93 2734 166 0.1886 0.2003
REMARK 3 2 7.7984 - 6.2077 0.92 2703 145 0.2108 0.2453
REMARK 3 3 6.2077 - 5.4282 0.94 2706 144 0.2252 0.2525
REMARK 3 4 5.4282 - 4.9343 0.93 2751 141 0.2003 0.2237
REMARK 3 5 4.9343 - 4.5819 0.92 2686 140 0.1993 0.2494
REMARK 3 6 4.5819 - 4.3126 0.92 2708 145 0.1992 0.2548
REMARK 3 7 4.3126 - 4.0972 0.83 2422 148 0.2102 0.2720
REMARK 3 8 4.0972 - 3.9192 0.76 2238 104 0.2137 0.2497
REMARK 3 9 3.9192 - 3.7686 0.84 2457 122 0.2335 0.2799
REMARK 3 10 3.7686 - 3.6388 0.93 2723 136 0.2841 0.3118
REMARK 3 11 3.6388 - 3.5252 0.90 2617 157 0.2488 0.3026
REMARK 3 12 3.5252 - 3.4246 0.88 2538 118 0.2453 0.3127
REMARK 3 13 3.4246 - 3.3346 0.87 2561 140 0.2672 0.3188
REMARK 3 14 3.3346 - 3.2533 0.86 2512 129 0.2717 0.3442
REMARK 3 15 3.2533 - 3.1794 0.80 2315 127 0.2988 0.3337
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.350
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 105.0
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: 0.5000
REMARK 3 OPERATOR: K,H,-L
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.011 9602
REMARK 3 ANGLE : 0.965 13055
REMARK 3 CHIRALITY : 0.055 1402
REMARK 3 PLANARITY : 0.005 1713
REMARK 3 DIHEDRAL : 15.835 3499
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 14
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 12 THROUGH 62 )
REMARK 3 ORIGIN FOR THE GROUP (A): 188.1395 14.5627 -4.9661
REMARK 3 T TENSOR
REMARK 3 T11: 0.8223 T22: 0.5190
REMARK 3 T33: 0.2519 T12: 0.1540
REMARK 3 T13: 0.1795 T23: -0.0153
REMARK 3 L TENSOR
REMARK 3 L11: 0.6428 L22: 0.4668
REMARK 3 L33: 1.2251 L12: 0.0763
REMARK 3 L13: -0.5252 L23: -0.6664
REMARK 3 S TENSOR
REMARK 3 S11: -0.0133 S12: -0.1643 S13: -0.0113
REMARK 3 S21: 0.2289 S22: 0.0265 S23: -0.0356
REMARK 3 S31: -0.2221 S32: 0.3105 S33: -0.0348
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 63 THROUGH 173 )
REMARK 3 ORIGIN FOR THE GROUP (A): 182.2669 -17.2061 -30.6563
REMARK 3 T TENSOR
REMARK 3 T11: 0.4072 T22: 0.8212
REMARK 3 T33: 1.4937 T12: 0.0709
REMARK 3 T13: -0.1004 T23: -0.0215
REMARK 3 L TENSOR
REMARK 3 L11: 0.7064 L22: 0.8237
REMARK 3 L33: 0.3972 L12: 0.7534
REMARK 3 L13: 0.2966 L23: 0.2446
REMARK 3 S TENSOR
REMARK 3 S11: 0.1404 S12: 0.0717 S13: -0.0416
REMARK 3 S21: -0.0402 S22: 0.1903 S23: -0.2801
REMARK 3 S31: 0.0695 S32: -0.0957 S33: -0.1946
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 174 THROUGH 498 )
REMARK 3 ORIGIN FOR THE GROUP (A): 193.1631 2.8297 -17.6765
REMARK 3 T TENSOR
REMARK 3 T11: 0.5479 T22: 0.7703
REMARK 3 T33: 1.1707 T12: 0.0765
REMARK 3 T13: 0.2226 T23: -0.2281
REMARK 3 L TENSOR
REMARK 3 L11: 1.0990 L22: 0.9683
REMARK 3 L33: 0.8110 L12: 0.1841
REMARK 3 L13: 0.2035 L23: 0.3592
REMARK 3 S TENSOR
REMARK 3 S11: 0.2682 S12: 0.2879 S13: -0.0051
REMARK 3 S21: 0.0463 S22: 0.1480 S23: -0.0970
REMARK 3 S31: -0.1900 S32: -0.1289 S33: -0.2960
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 499 THROUGH 547 )
REMARK 3 ORIGIN FOR THE GROUP (A): 172.8947 -2.0328 -16.7871
REMARK 3 T TENSOR
REMARK 3 T11: 0.5381 T22: 0.7730
REMARK 3 T33: 1.2813 T12: 0.0687
REMARK 3 T13: 0.2594 T23: -0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 0.2203 L22: 0.7026
REMARK 3 L33: 0.6638 L12: 0.1982
REMARK 3 L13: 0.3244 L23: 0.6042
REMARK 3 S TENSOR
REMARK 3 S11: 0.1817 S12: 0.3200 S13: -0.1873
REMARK 3 S21: 0.0094 S22: 0.0265 S23: -0.1252
REMARK 3 S31: 0.0578 S32: -0.0447 S33: -0.2386
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 548 THROUGH 723 )
REMARK 3 ORIGIN FOR THE GROUP (A): 183.1115 -14.1411 0.8828
REMARK 3 T TENSOR
REMARK 3 T11: 0.6811 T22: 0.5037
REMARK 3 T33: 0.7151 T12: 0.1016
REMARK 3 T13: 0.1003 T23: -0.0792
REMARK 3 L TENSOR
REMARK 3 L11: 1.3391 L22: 1.1934
REMARK 3 L33: 1.0472 L12: 0.1873
REMARK 3 L13: -0.3062 L23: -0.3435
REMARK 3 S TENSOR
REMARK 3 S11: -0.0632 S12: -0.2372 S13: -0.3471
REMARK 3 S21: 0.1661 S22: 0.1619 S23: 0.1486
REMARK 3 S31: 0.2818 S32: 0.0500 S33: -0.1080
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 724 THROUGH 785 )
REMARK 3 ORIGIN FOR THE GROUP (A): 191.8846 2.7431 22.4344
REMARK 3 T TENSOR
REMARK 3 T11: 1.5317 T22: 1.4356
REMARK 3 T33: 1.3431 T12: 0.2019
REMARK 3 T13: 0.0105 T23: 0.2728
REMARK 3 L TENSOR
REMARK 3 L11: 0.5859 L22: 1.2876
REMARK 3 L33: 0.0521 L12: 0.6124
REMARK 3 L13: -0.1060 L23: -0.0529
REMARK 3 S TENSOR
REMARK 3 S11: -0.0104 S12: -0.0060 S13: 0.0294
REMARK 3 S21: 0.0188 S22: 0.1118 S23: -0.1363
REMARK 3 S31: -0.0326 S32: 0.0387 S33: -0.1020
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 12 THROUGH 62 )
REMARK 3 ORIGIN FOR THE GROUP (A): 236.9094 -13.7211 -19.1397
REMARK 3 T TENSOR
REMARK 3 T11: 0.7152 T22: 0.8415
REMARK 3 T33: 0.9327 T12: 0.0462
REMARK 3 T13: 0.2058 T23: 0.1641
REMARK 3 L TENSOR
REMARK 3 L11: 1.0289 L22: 0.5629
REMARK 3 L33: 0.5449 L12: -0.4975
REMARK 3 L13: 0.1187 L23: 0.1044
REMARK 3 S TENSOR
REMARK 3 S11: -0.0877 S12: 0.0550 S13: 0.1110
REMARK 3 S21: -0.1147 S22: -0.1207 S23: -0.0978
REMARK 3 S31: 0.1529 S32: 0.1764 S33: 0.1111
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 63 THROUGH 173 )
REMARK 3 ORIGIN FOR THE GROUP (A): 212.2305 -34.5456 6.5173
REMARK 3 T TENSOR
REMARK 3 T11: 0.8495 T22: 0.7865
REMARK 3 T33: 0.1128 T12: 0.1373
REMARK 3 T13: -0.0398 T23: 0.0776
REMARK 3 L TENSOR
REMARK 3 L11: 0.2161 L22: 0.1772
REMARK 3 L33: 0.2026 L12: 0.0681
REMARK 3 L13: 0.1384 L23: 0.0496
REMARK 3 S TENSOR
REMARK 3 S11: 0.0075 S12: -0.0569 S13: 0.0770
REMARK 3 S21: 0.0510 S22: -0.1151 S23: -0.0109
REMARK 3 S31: -0.0845 S32: -0.0486 S33: -0.0908
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 174 THROUGH 378 )
REMARK 3 ORIGIN FOR THE GROUP (A): 220.6549 -21.3640 8.8079
REMARK 3 T TENSOR
REMARK 3 T11: 0.7708 T22: 0.8354
REMARK 3 T33: 0.4098 T12: 0.1647
REMARK 3 T13: -0.2411 T23: -0.1684
REMARK 3 L TENSOR
REMARK 3 L11: 0.3077 L22: 1.5777
REMARK 3 L33: 0.5260 L12: 0.2193
REMARK 3 L13: -0.3471 L23: -0.6861
REMARK 3 S TENSOR
REMARK 3 S11: 0.0126 S12: -0.0913 S13: -0.0786
REMARK 3 S21: 0.1153 S22: -0.0938 S23: 0.0717
REMARK 3 S31: 0.0252 S32: 0.0653 S33: 0.0276
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 379 THROUGH 462 )
REMARK 3 ORIGIN FOR THE GROUP (A): 225.5038 -11.5575 -9.3853
REMARK 3 T TENSOR
REMARK 3 T11: 0.6613 T22: 0.8174
REMARK 3 T33: 0.3363 T12: -0.0228
REMARK 3 T13: -0.3085 T23: -0.0184
REMARK 3 L TENSOR
REMARK 3 L11: 0.5195 L22: 0.6932
REMARK 3 L33: 0.5278 L12: -0.0805
REMARK 3 L13: 0.2370 L23: -0.1519
REMARK 3 S TENSOR
REMARK 3 S11: -0.0403 S12: -0.0361 S13: 0.0545
REMARK 3 S21: 0.0770 S22: 0.0417 S23: -0.0334
REMARK 3 S31: -0.0375 S32: 0.0511 S33: 0.2265
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 463 THROUGH 557 )
REMARK 3 ORIGIN FOR THE GROUP (A): 228.6233 -27.7492 -8.9927
REMARK 3 T TENSOR
REMARK 3 T11: 0.5865 T22: 0.7408
REMARK 3 T33: 0.2003 T12: 0.1167
REMARK 3 T13: -0.1961 T23: 0.0795
REMARK 3 L TENSOR
REMARK 3 L11: 0.2038 L22: 0.6701
REMARK 3 L33: 0.3786 L12: -0.0396
REMARK 3 L13: 0.0147 L23: -0.0379
REMARK 3 S TENSOR
REMARK 3 S11: 0.0084 S12: -0.0360 S13: -0.0646
REMARK 3 S21: -0.0492 S22: -0.0312 S23: 0.0720
REMARK 3 S31: 0.0671 S32: -0.1019 S33: -0.2195
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 558 THROUGH 655 )
REMARK 3 ORIGIN FOR THE GROUP (A): 220.4750 -27.7607 -25.0540
REMARK 3 T TENSOR
REMARK 3 T11: 0.5618 T22: 0.6597
REMARK 3 T33: 0.4873 T12: 0.0933
REMARK 3 T13: -0.3022 T23: -0.2044
REMARK 3 L TENSOR
REMARK 3 L11: 0.7440 L22: 0.4407
REMARK 3 L33: 1.9290 L12: 0.2155
REMARK 3 L13: 0.5413 L23: 0.2571
REMARK 3 S TENSOR
REMARK 3 S11: 0.0513 S12: 0.2969 S13: -0.3753
REMARK 3 S21: -0.2582 S22: 0.0532 S23: 0.3148
REMARK 3 S31: 0.2642 S32: -0.0454 S33: -0.1453
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 656 THROUGH 699 )
REMARK 3 ORIGIN FOR THE GROUP (A): 201.3224 -37.8825 -25.7727
REMARK 3 T TENSOR
REMARK 3 T11: 0.6244 T22: 0.8096
REMARK 3 T33: 1.2133 T12: -0.1027
REMARK 3 T13: -0.2647 T23: -0.0226
REMARK 3 L TENSOR
REMARK 3 L11: 2.1471 L22: 3.3660
REMARK 3 L33: 1.2423 L12: 0.6064
REMARK 3 L13: 0.5185 L23: -1.2775
REMARK 3 S TENSOR
REMARK 3 S11: 0.0442 S12: 0.0817 S13: -0.3937
REMARK 3 S21: -0.2450 S22: 0.0279 S23: 0.5143
REMARK 3 S31: 0.2882 S32: -0.2035 S33: -0.0554
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 700 THROUGH 785 )
REMARK 3 ORIGIN FOR THE GROUP (A): 216.4186 -26.1900 -40.6031
REMARK 3 T TENSOR
REMARK 3 T11: 1.0800 T22: 1.2141
REMARK 3 T33: 1.2838 T12: -0.1519
REMARK 3 T13: -0.2201 T23: 0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 1.3608 L22: 0.2971
REMARK 3 L33: 0.9548 L12: 0.5973
REMARK 3 L13: -0.7200 L23: -0.4396
REMARK 3 S TENSOR
REMARK 3 S11: 0.0679 S12: 0.3666 S13: -0.0744
REMARK 3 S21: -0.2228 S22: 0.0494 S23: -0.0058
REMARK 3 S31: -0.0014 S32: 0.1563 S33: -0.0780
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 5K4L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1000221729.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JUN-14
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 7.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97950
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40754
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.179
REMARK 200 RESOLUTION RANGE LOW (A) : 35.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.3
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.18
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.50200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 0.1 M HEPES, PH 7.3, AND
REMARK 280 12% GLYCEROL, VAPOR DIFFUSION, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 30.70300
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 61.40600
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS DIMER. CHAINS F,G ARE PARTS OF
REMARK 300 MOLECULE 1
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, F, G
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 SER A 11
REMARK 465 PRO A 184
REMARK 465 ASN A 185
REMARK 465 LEU A 186
REMARK 465 ASP A 187
REMARK 465 LEU A 188
REMARK 465 LYS A 189
REMARK 465 GLU A 190
REMARK 465 LYS A 191
REMARK 465 VAL A 192
REMARK 465 GLU A 193
REMARK 465 PRO A 194
REMARK 465 GLU A 195
REMARK 465 VAL A 196
REMARK 465 LEU A 197
REMARK 465 SER A 198
REMARK 465 THR A 199
REMARK 465 ASP A 200
REMARK 465 THR A 201
REMARK 465 GLN A 202
REMARK 465 THR A 203
REMARK 465 SER A 204
REMARK 465 PRO A 205
REMARK 465 GLU A 206
REMARK 465 PRO A 207
REMARK 465 GLY A 208
REMARK 465 THR A 209
REMARK 465 ARG A 210
REMARK 465 MET A 211
REMARK 465 ASN A 212
REMARK 465 ILE A 213
REMARK 465 LEU A 214
REMARK 465 PRO A 215
REMARK 465 LYS A 216
REMARK 465 ARG A 217
REMARK 465 THR A 218
REMARK 465 ARG A 219
REMARK 465 ARG A 220
REMARK 465 VAL A 221
REMARK 465 LYS A 222
REMARK 465 THR A 223
REMARK 465 GLN A 224
REMARK 465 SER A 225
REMARK 465 GLU A 226
REMARK 465 SER A 227
REMARK 465 GLY A 228
REMARK 465 ASP A 229
REMARK 465 VAL A 230
REMARK 465 SER A 231
REMARK 465 ARG A 232
REMARK 465 ASN A 233
REMARK 465 THR A 234
REMARK 465 GLU A 235
REMARK 465 LEU A 236
REMARK 465 LYS A 237
REMARK 465 LYS A 238
REMARK 465 LEU A 239
REMARK 465 GLN A 240
REMARK 465 ILE A 241
REMARK 465 PHE A 242
REMARK 465 GLY A 243
REMARK 465 ALA A 244
REMARK 465 GLY A 245
REMARK 465 PRO A 246
REMARK 465 LYS A 247
REMARK 465 VAL A 248
REMARK 465 VAL A 249
REMARK 465 GLY A 250
REMARK 465 LEU A 251
REMARK 465 ALA A 252
REMARK 465 MET A 253
REMARK 465 GLY A 254
REMARK 465 THR A 255
REMARK 465 LYS A 256
REMARK 465 ASP A 257
REMARK 465 LYS A 258
REMARK 465 GLU A 259
REMARK 465 ASP A 260
REMARK 465 GLU A 261
REMARK 465 VAL A 262
REMARK 465 THR A 263
REMARK 465 ARG A 264
REMARK 465 ARG A 265
REMARK 465 ARG A 266
REMARK 465 LYS A 267
REMARK 465 VAL A 268
REMARK 465 THR A 269
REMARK 465 ASN A 270
REMARK 465 ARG A 271
REMARK 465 SER A 272
REMARK 465 ASP A 273
REMARK 465 ALA A 274
REMARK 465 PHE A 275
REMARK 465 ASN A 276
REMARK 465 MET A 277
REMARK 465 GLN A 278
REMARK 465 MET A 279
REMARK 465 ARG A 280
REMARK 465 GLN A 281
REMARK 465 ARG A 282
REMARK 465 LYS A 283
REMARK 465 GLY A 284
REMARK 465 THR A 285
REMARK 465 LEU A 286
REMARK 465 SER A 287
REMARK 465 VAL A 288
REMARK 465 ASN A 289
REMARK 465 PHE A 290
REMARK 465 VAL A 291
REMARK 465 ASP A 292
REMARK 465 LEU A 293
REMARK 465 TYR A 294
REMARK 465 VAL A 295
REMARK 465 CYS A 296
REMARK 465 MET A 297
REMARK 465 PHE A 298
REMARK 465 CYS A 299
REMARK 465 GLY A 300
REMARK 465 ARG A 301
REMARK 465 GLY A 302
REMARK 465 ASN A 303
REMARK 465 ASN A 304
REMARK 465 GLU A 305
REMARK 465 ASP A 306
REMARK 465 LYS A 307
REMARK 465 LEU A 308
REMARK 465 LEU A 309
REMARK 465 LEU A 310
REMARK 465 CYS A 311
REMARK 465 ASP A 312
REMARK 465 GLY A 313
REMARK 465 CYS A 314
REMARK 465 ASP A 315
REMARK 465 ASP A 316
REMARK 465 SER A 317
REMARK 465 TYR A 318
REMARK 465 HIS A 319
REMARK 465 THR A 320
REMARK 465 PHE A 321
REMARK 465 CYS A 322
REMARK 465 LEU A 323
REMARK 465 ILE A 324
REMARK 465 PRO A 325
REMARK 465 PRO A 326
REMARK 465 LEU A 327
REMARK 465 PRO A 328
REMARK 465 ASP A 329
REMARK 465 VAL A 330
REMARK 465 PRO A 331
REMARK 465 LYS A 332
REMARK 465 GLY A 333
REMARK 465 ASP A 334
REMARK 465 TRP A 335
REMARK 465 ARG A 336
REMARK 465 CYS A 337
REMARK 465 PRO A 338
REMARK 465 LYS A 339
REMARK 465 CYS A 340
REMARK 465 VAL A 341
REMARK 465 ALA A 342
REMARK 465 GLU A 343
REMARK 465 GLU A 344
REMARK 465 CYS A 345
REMARK 465 SER A 346
REMARK 465 LYS A 347
REMARK 465 PRO A 348
REMARK 465 ARG A 349
REMARK 465 GLU A 350
REMARK 465 ALA A 351
REMARK 465 PHE A 352
REMARK 465 GLY A 353
REMARK 465 PHE A 354
REMARK 465 GLU A 355
REMARK 465 GLN A 356
REMARK 465 ALA A 357
REMARK 465 VAL A 358
REMARK 465 ARG A 359
REMARK 465 GLU A 360
REMARK 465 ARG A 745
REMARK 465 VAL A 746
REMARK 465 THR A 747
REMARK 465 GLU A 748
REMARK 465 ALA A 749
REMARK 465 LEU A 750
REMARK 465 SER A 751
REMARK 465 ALA A 752
REMARK 465 ASN A 753
REMARK 465 PHE A 754
REMARK 465 ASN A 755
REMARK 465 HIS A 756
REMARK 465 LYS A 757
REMARK 465 LYS A 758
REMARK 465 ASP A 759
REMARK 465 LEU A 760
REMARK 465 ILE A 761
REMARK 465 GLU A 762
REMARK 465 LEU A 763
REMARK 465 ARG A 764
REMARK 465 ASP A 786
REMARK 465 ALA A 787
REMARK 465 VAL A 788
REMARK 465 LYS A 789
REMARK 465 GLU A 790
REMARK 465 ALA A 791
REMARK 465 GLU A 792
REMARK 465 THR A 793
REMARK 465 CYS A 794
REMARK 465 ALA A 795
REMARK 465 SER A 796
REMARK 465 VAL A 797
REMARK 465 GLY A 798
REMARK 465 ASN A 799
REMARK 465 SER A 800
REMARK 465 SER B 11
REMARK 465 PRO B 184
REMARK 465 ASN B 185
REMARK 465 LEU B 186
REMARK 465 ASP B 187
REMARK 465 LEU B 188
REMARK 465 LYS B 189
REMARK 465 GLU B 190
REMARK 465 LYS B 191
REMARK 465 VAL B 192
REMARK 465 GLU B 193
REMARK 465 PRO B 194
REMARK 465 GLU B 195
REMARK 465 VAL B 196
REMARK 465 LEU B 197
REMARK 465 SER B 198
REMARK 465 THR B 199
REMARK 465 ASP B 200
REMARK 465 THR B 201
REMARK 465 GLN B 202
REMARK 465 THR B 203
REMARK 465 SER B 204
REMARK 465 PRO B 205
REMARK 465 GLU B 206
REMARK 465 PRO B 207
REMARK 465 GLY B 208
REMARK 465 THR B 209
REMARK 465 ARG B 210
REMARK 465 MET B 211
REMARK 465 ASN B 212
REMARK 465 ILE B 213
REMARK 465 LEU B 214
REMARK 465 PRO B 215
REMARK 465 LYS B 216
REMARK 465 ARG B 217
REMARK 465 THR B 218
REMARK 465 ARG B 219
REMARK 465 ARG B 220
REMARK 465 VAL B 221
REMARK 465 LYS B 222
REMARK 465 THR B 223
REMARK 465 GLN B 224
REMARK 465 SER B 225
REMARK 465 GLU B 226
REMARK 465 SER B 227
REMARK 465 GLY B 228
REMARK 465 ASP B 229
REMARK 465 VAL B 230
REMARK 465 SER B 231
REMARK 465 ARG B 232
REMARK 465 ASN B 233
REMARK 465 THR B 234
REMARK 465 GLU B 235
REMARK 465 LEU B 236
REMARK 465 LYS B 237
REMARK 465 LYS B 238
REMARK 465 LEU B 239
REMARK 465 GLN B 240
REMARK 465 ILE B 241
REMARK 465 PHE B 242
REMARK 465 GLY B 243
REMARK 465 ALA B 244
REMARK 465 GLY B 245
REMARK 465 PRO B 246
REMARK 465 LYS B 247
REMARK 465 VAL B 248
REMARK 465 VAL B 249
REMARK 465 GLY B 250
REMARK 465 LEU B 251
REMARK 465 ALA B 252
REMARK 465 MET B 253
REMARK 465 GLY B 254
REMARK 465 THR B 255
REMARK 465 LYS B 256
REMARK 465 ASP B 257
REMARK 465 LYS B 258
REMARK 465 GLU B 259
REMARK 465 ASP B 260
REMARK 465 GLU B 261
REMARK 465 VAL B 262
REMARK 465 THR B 263
REMARK 465 ARG B 264
REMARK 465 ARG B 265
REMARK 465 ARG B 266
REMARK 465 LYS B 267
REMARK 465 VAL B 268
REMARK 465 THR B 269
REMARK 465 ASN B 270
REMARK 465 ARG B 271
REMARK 465 SER B 272
REMARK 465 ASP B 273
REMARK 465 ALA B 274
REMARK 465 PHE B 275
REMARK 465 ASN B 276
REMARK 465 MET B 277
REMARK 465 GLN B 278
REMARK 465 MET B 279
REMARK 465 ARG B 280
REMARK 465 GLN B 281
REMARK 465 ARG B 282
REMARK 465 LYS B 283
REMARK 465 GLY B 284
REMARK 465 THR B 285
REMARK 465 LEU B 286
REMARK 465 SER B 287
REMARK 465 VAL B 288
REMARK 465 ASN B 289
REMARK 465 PHE B 290
REMARK 465 VAL B 291
REMARK 465 ASP B 292
REMARK 465 LEU B 293
REMARK 465 TYR B 294
REMARK 465 VAL B 295
REMARK 465 CYS B 296
REMARK 465 MET B 297
REMARK 465 PHE B 298
REMARK 465 CYS B 299
REMARK 465 GLY B 300
REMARK 465 ARG B 301
REMARK 465 GLY B 302
REMARK 465 ASN B 303
REMARK 465 ASN B 304
REMARK 465 GLU B 305
REMARK 465 ASP B 306
REMARK 465 LYS B 307
REMARK 465 LEU B 308
REMARK 465 LEU B 309
REMARK 465 LEU B 310
REMARK 465 CYS B 311
REMARK 465 ASP B 312
REMARK 465 GLY B 313
REMARK 465 CYS B 314
REMARK 465 ASP B 315
REMARK 465 ASP B 316
REMARK 465 SER B 317
REMARK 465 TYR B 318
REMARK 465 HIS B 319
REMARK 465 THR B 320
REMARK 465 PHE B 321
REMARK 465 CYS B 322
REMARK 465 LEU B 323
REMARK 465 ILE B 324
REMARK 465 PRO B 325
REMARK 465 PRO B 326
REMARK 465 LEU B 327
REMARK 465 PRO B 328
REMARK 465 ASP B 329
REMARK 465 VAL B 330
REMARK 465 PRO B 331
REMARK 465 LYS B 332
REMARK 465 GLY B 333
REMARK 465 ASP B 334
REMARK 465 TRP B 335
REMARK 465 ARG B 336
REMARK 465 CYS B 337
REMARK 465 PRO B 338
REMARK 465 LYS B 339
REMARK 465 CYS B 340
REMARK 465 VAL B 341
REMARK 465 ALA B 342
REMARK 465 GLU B 343
REMARK 465 GLU B 344
REMARK 465 CYS B 345
REMARK 465 SER B 346
REMARK 465 LYS B 347
REMARK 465 PRO B 348
REMARK 465 ARG B 349
REMARK 465 GLU B 350
REMARK 465 ALA B 351
REMARK 465 PHE B 352
REMARK 465 GLY B 353
REMARK 465 PHE B 354
REMARK 465 GLU B 355
REMARK 465 GLN B 356
REMARK 465 ALA B 357
REMARK 465 VAL B 358
REMARK 465 ARG B 359
REMARK 465 GLU B 360
REMARK 465 ARG B 745
REMARK 465 VAL B 746
REMARK 465 THR B 747
REMARK 465 GLU B 748
REMARK 465 ALA B 749
REMARK 465 LEU B 750
REMARK 465 SER B 751
REMARK 465 ALA B 752
REMARK 465 ASN B 753
REMARK 465 PHE B 754
REMARK 465 ASN B 755
REMARK 465 HIS B 756
REMARK 465 LYS B 757
REMARK 465 LYS B 758
REMARK 465 ASP B 759
REMARK 465 LEU B 760
REMARK 465 ILE B 761
REMARK 465 GLU B 762
REMARK 465 LEU B 763
REMARK 465 ARG B 764
REMARK 465 ASP B 786
REMARK 465 ALA B 787
REMARK 465 VAL B 788
REMARK 465 LYS B 789
REMARK 465 GLU B 790
REMARK 465 ALA B 791
REMARK 465 GLU B 792
REMARK 465 THR B 793
REMARK 465 CYS B 794
REMARK 465 ALA B 795
REMARK 465 SER B 796
REMARK 465 VAL B 797
REMARK 465 GLY B 798
REMARK 465 ASN B 799
REMARK 465 SER B 800
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 GLU A 64 CG CD OE1 OE2
REMARK 470 ARG A 69 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 76 CG CD NE CZ NH1 NH2
REMARK 470 MET A 179 CG SD CE
REMARK 470 VAL A 181 CG1 CG2
REMARK 470 GLU A 402 CG CD OE1 OE2
REMARK 470 LYS A 430 CG CD CE NZ
REMARK 470 ASN A 460 CG OD1 ND2
REMARK 470 VAL A 461 CG1 CG2
REMARK 470 ASP A 462 CG OD1 OD2
REMARK 470 LYS A 637 CG CD CE NZ
REMARK 470 ARG A 650 CG CD NE CZ NH1 NH2
REMARK 470 MET A 711 CG SD CE
REMARK 470 GLN A 712 CG CD OE1 NE2
REMARK 470 LYS A 713 CG CD CE NZ
REMARK 470 LYS A 714 CG CD CE NZ
REMARK 470 ARG A 717 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 733 CG CD CE NZ
REMARK 470 GLU A 777 CG CD OE1 OE2
REMARK 470 ASN A 778 CG OD1 ND2
REMARK 470 ARG A 782 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 784 CG CD1 CD2
REMARK 470 ARG A 785 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 64 CG CD OE1 OE2
REMARK 470 ARG B 69 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 76 CG CD NE CZ NH1 NH2
REMARK 470 MET B 179 CG SD CE
REMARK 470 VAL B 181 CG1 CG2
REMARK 470 GLU B 402 CG CD OE1 OE2
REMARK 470 LYS B 430 CG CD CE NZ
REMARK 470 ASN B 460 CG OD1 ND2
REMARK 470 VAL B 461 CG1 CG2
REMARK 470 ASP B 462 CG OD1 OD2
REMARK 470 LYS B 637 CG CD CE NZ
REMARK 470 ARG B 650 CG CD NE CZ NH1 NH2
REMARK 470 MET B 711 CG SD CE
REMARK 470 GLN B 712 CG CD OE1 NE2
REMARK 470 LYS B 713 CG CD CE NZ
REMARK 470 LYS B 714 CG CD CE NZ
REMARK 470 LYS B 733 CG CD CE NZ
REMARK 470 GLU B 777 CG CD OE1 OE2
REMARK 470 ASN B 778 CG OD1 ND2
REMARK 470 ARG B 782 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 784 CG CD1 CD2
REMARK 470 ARG B 785 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 HB3 CYS B 709 ZN ZN B 903 1.14
REMARK 500 HE2 HIS B 571 NI NI B 901 1.17
REMARK 500 HE2 HIS A 571 NI NI A 901 1.21
REMARK 500 HB3 CYS A 699 ZN ZN A 902 1.24
REMARK 500 HE2 HIS A 483 NI NI A 901 1.29
REMARK 500 SG CYS B 692 HG CYS B 707 1.36
REMARK 500 HG CYS B 692 SG CYS B 707 1.46
REMARK 500 HB2 CYS A 679 ZN ZN A 902 1.56
REMARK 500 O GLU B 170 H SER B 174 1.57
REMARK 500 H CYS A 19 O ARG A 554 1.59
REMARK 500 OE2 GLU A 646 OG SER A 686 2.16
REMARK 500 O ALA B 457 N ILE B 459 2.16
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 GLU A 23 74.04 -117.53
REMARK 500 LEU A 42 -62.61 -96.04
REMARK 500 ARG A 112 -10.01 77.27
REMARK 500 PHE A 130 -70.69 -57.30
REMARK 500 LYS A 152 -6.66 -58.25
REMARK 500 ILE A 165 -61.09 -129.27
REMARK 500 VAL A 176 -121.33 47.97
REMARK 500 SER A 177 -142.04 59.98
REMARK 500 LEU A 178 72.84 56.93
REMARK 500 MET A 179 -79.02 -102.69
REMARK 500 ALA A 411 -177.33 -171.90
REMARK 500 ALA A 457 -154.40 -68.79
REMARK 500 HIS A 458 -22.44 -33.71
REMARK 500 VAL A 461 -68.98 -133.63
REMARK 500 PHE A 477 -8.37 76.72
REMARK 500 SER A 489 -82.70 -119.97
REMARK 500 LEU A 659 -69.82 -120.07
REMARK 500 SER A 677 -71.19 -49.19
REMARK 500 CYS A 679 -61.23 -133.31
REMARK 500 PHE A 684 -64.07 -129.45
REMARK 500 GLN A 712 -113.31 52.04
REMARK 500 LYS A 714 -149.46 56.55
REMARK 500 LEU A 722 0.80 92.53
REMARK 500 GLU A 777 -84.25 -126.27
REMARK 500 ASN A 778 -143.11 42.32
REMARK 500 ASP A 779 -119.19 36.66
REMARK 500 LEU B 42 -62.73 -97.34
REMARK 500 VAL B 65 -57.78 -129.14
REMARK 500 ARG B 112 -4.46 75.19
REMARK 500 LYS B 152 -6.65 -57.61
REMARK 500 ILE B 165 -61.28 -126.02
REMARK 500 VAL B 176 -125.68 46.71
REMARK 500 SER B 177 -141.19 60.59
REMARK 500 LEU B 178 73.94 57.17
REMARK 500 MET B 179 -78.58 -102.00
REMARK 500 ALA B 411 -177.31 -171.51
REMARK 500 ALA B 457 -153.89 -68.44
REMARK 500 HIS B 458 -21.77 -32.05
REMARK 500 VAL B 461 -68.64 -132.84
REMARK 500 PHE B 477 -7.91 66.88
REMARK 500 TRP B 488 -117.21 54.72
REMARK 500 SER B 489 -148.84 55.45
REMARK 500 LEU B 659 -65.87 -123.74
REMARK 500 CYS B 679 -66.06 -135.70
REMARK 500 PHE B 684 -63.33 -130.38
REMARK 500 GLN B 712 -113.63 51.50
REMARK 500 LYS B 714 -151.07 52.09
REMARK 500 LEU B 722 -2.42 91.74
REMARK 500 GLU B 777 -84.45 -128.03
REMARK 500 ASN B 778 -144.12 44.92
REMARK 500
REMARK 500 THIS ENTRY HAS 53 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS A 425 ASP A 426 149.18
REMARK 500 ALA A 457 HIS A 458 -144.31
REMARK 500 MET A 466 LYS A 467 142.04
REMARK 500 ASN A 778 ASP A 779 135.29
REMARK 500 ALA B 457 HIS B 458 -145.10
REMARK 500 MET B 466 LYS B 467 143.16
REMARK 500 ASN B 778 ASP B 779 136.15
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 NI A 901 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 483 NE2
REMARK 620 2 GLU A 485 OE1 122.8
REMARK 620 3 GLU A 485 OE2 77.0 63.9
REMARK 620 4 HIS A 571 NE2 83.0 140.1 98.6
REMARK 620 5 6QN A 904 N11 79.8 106.3 141.9 108.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 902 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 676 SG
REMARK 620 2 CYS A 679 SG 122.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 903 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 690 SG
REMARK 620 2 CYS A 709 SG 82.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI B 901 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 483 NE2
REMARK 620 2 GLU B 485 OE2 102.4
REMARK 620 3 HIS B 571 NE2 87.5 93.7
REMARK 620 4 6QN B 904 N11 112.5 142.7 100.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 902 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 676 SG
REMARK 620 2 CYS B 679 SG 107.1
REMARK 620 3 CYS B 699 SG 95.8 87.3
REMARK 620 4 HIS B 702 ND1 140.8 108.8 101.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 903 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 707 SG
REMARK 620 2 CYS B 709 O 135.1
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 NI A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6QN A 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NI B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6QN B 904
DBREF 5K4L A 12 797 UNP P29375 KDM5A_HUMAN 12 797
DBREF 5K4L B 12 797 UNP P29375 KDM5A_HUMAN 12 797
DBREF 5K4L F 219 228 PDB 5K4L 5K4L 219 228
DBREF 5K4L G 219 228 PDB 5K4L 5K4L 219 228
SEQADV 5K4L SER A 11 UNP P29375 EXPRESSION TAG
SEQADV 5K4L GLY A 798 UNP P29375 EXPRESSION TAG
SEQADV 5K4L ASN A 799 UNP P29375 EXPRESSION TAG
SEQADV 5K4L SER A 800 UNP P29375 EXPRESSION TAG
SEQADV 5K4L SER B 11 UNP P29375 EXPRESSION TAG
SEQADV 5K4L GLY B 798 UNP P29375 EXPRESSION TAG
SEQADV 5K4L ASN B 799 UNP P29375 EXPRESSION TAG
SEQADV 5K4L SER B 800 UNP P29375 EXPRESSION TAG
SEQRES 1 A 790 SER GLU PHE VAL PRO PRO PRO GLU CYS PRO VAL PHE GLU
SEQRES 2 A 790 PRO SER TRP GLU GLU PHE THR ASP PRO LEU SER PHE ILE
SEQRES 3 A 790 GLY ARG ILE ARG PRO LEU ALA GLU LYS THR GLY ILE CYS
SEQRES 4 A 790 LYS ILE ARG PRO PRO LYS ASP TRP GLN PRO PRO PHE ALA
SEQRES 5 A 790 CYS GLU VAL LYS SER PHE ARG PHE THR PRO ARG VAL GLN
SEQRES 6 A 790 ARG LEU ASN GLU LEU GLU ALA MET THR ARG VAL ARG LEU
SEQRES 7 A 790 ASP PHE LEU ASP GLN LEU ALA LYS PHE TRP GLU LEU GLN
SEQRES 8 A 790 GLY SER THR LEU LYS ILE PRO VAL VAL GLU ARG LYS ILE
SEQRES 9 A 790 LEU ASP LEU TYR ALA LEU SER LYS ILE VAL ALA SER LYS
SEQRES 10 A 790 GLY GLY PHE GLU MET VAL THR LYS GLU LYS LYS TRP SER
SEQRES 11 A 790 LYS VAL GLY SER ARG LEU GLY TYR LEU PRO GLY LYS GLY
SEQRES 12 A 790 THR GLY SER LEU LEU LYS SER HIS TYR GLU ARG ILE LEU
SEQRES 13 A 790 TYR PRO TYR GLU LEU PHE GLN SER GLY VAL SER LEU MET
SEQRES 14 A 790 GLY VAL GLN MET PRO ASN LEU ASP LEU LYS GLU LYS VAL
SEQRES 15 A 790 GLU PRO GLU VAL LEU SER THR ASP THR GLN THR SER PRO
SEQRES 16 A 790 GLU PRO GLY THR ARG MET ASN ILE LEU PRO LYS ARG THR
SEQRES 17 A 790 ARG ARG VAL LYS THR GLN SER GLU SER GLY ASP VAL SER
SEQRES 18 A 790 ARG ASN THR GLU LEU LYS LYS LEU GLN ILE PHE GLY ALA
SEQRES 19 A 790 GLY PRO LYS VAL VAL GLY LEU ALA MET GLY THR LYS ASP
SEQRES 20 A 790 LYS GLU ASP GLU VAL THR ARG ARG ARG LYS VAL THR ASN
SEQRES 21 A 790 ARG SER ASP ALA PHE ASN MET GLN MET ARG GLN ARG LYS
SEQRES 22 A 790 GLY THR LEU SER VAL ASN PHE VAL ASP LEU TYR VAL CYS
SEQRES 23 A 790 MET PHE CYS GLY ARG GLY ASN ASN GLU ASP LYS LEU LEU
SEQRES 24 A 790 LEU CYS ASP GLY CYS ASP ASP SER TYR HIS THR PHE CYS
SEQRES 25 A 790 LEU ILE PRO PRO LEU PRO ASP VAL PRO LYS GLY ASP TRP
SEQRES 26 A 790 ARG CYS PRO LYS CYS VAL ALA GLU GLU CYS SER LYS PRO
SEQRES 27 A 790 ARG GLU ALA PHE GLY PHE GLU GLN ALA VAL ARG GLU TYR
SEQRES 28 A 790 THR LEU GLN SER PHE GLY GLU MET ALA ASP ASN PHE LYS
SEQRES 29 A 790 SER ASP TYR PHE ASN MET PRO VAL HIS MET VAL PRO THR
SEQRES 30 A 790 GLU LEU VAL GLU LYS GLU PHE TRP ARG LEU VAL SER SER
SEQRES 31 A 790 ILE GLU GLU ASP VAL ILE VAL GLU TYR GLY ALA ASP ILE
SEQRES 32 A 790 SER SER LYS ASP PHE GLY SER GLY PHE PRO VAL LYS ASP
SEQRES 33 A 790 GLY ARG ARG LYS ILE LEU PRO GLU GLU GLU GLU TYR ALA
SEQRES 34 A 790 LEU SER GLY TRP ASN LEU ASN ASN MET PRO VAL LEU GLU
SEQRES 35 A 790 GLN SER VAL LEU ALA HIS ILE ASN VAL ASP ILE SER GLY
SEQRES 36 A 790 MET LYS VAL PRO TRP LEU TYR VAL GLY MET CYS PHE SER
SEQRES 37 A 790 SER PHE CYS TRP HIS ILE GLU ASP HIS TRP SER TYR SER
SEQRES 38 A 790 ILE ASN TYR LEU HIS TRP GLY GLU PRO LYS THR TRP TYR
SEQRES 39 A 790 GLY VAL PRO SER HIS ALA ALA GLU GLN LEU GLU GLU VAL
SEQRES 40 A 790 MET ARG GLU LEU ALA PRO GLU LEU PHE GLU SER GLN PRO
SEQRES 41 A 790 ASP LEU LEU HIS GLN LEU VAL THR ILE MET ASN PRO ASN
SEQRES 42 A 790 VAL LEU MET GLU HIS GLY VAL PRO VAL TYR ARG THR ASN
SEQRES 43 A 790 GLN CYS ALA GLY GLU PHE VAL VAL THR PHE PRO ARG ALA
SEQRES 44 A 790 TYR HIS SER GLY PHE ASN GLN GLY TYR ASN PHE ALA GLU
SEQRES 45 A 790 ALA VAL ASN PHE CYS THR ALA ASP TRP LEU PRO ILE GLY
SEQRES 46 A 790 ARG GLN CYS VAL ASN HIS TYR ARG ARG LEU ARG ARG HIS
SEQRES 47 A 790 CYS VAL PHE SER HIS GLU GLU LEU ILE PHE LYS MET ALA
SEQRES 48 A 790 ALA ASP PRO GLU CYS LEU ASP VAL GLY LEU ALA ALA MET
SEQRES 49 A 790 VAL CYS LYS GLU LEU THR LEU MET THR GLU GLU GLU THR
SEQRES 50 A 790 ARG LEU ARG GLU SER VAL VAL GLN MET GLY VAL LEU MET
SEQRES 51 A 790 SER GLU GLU GLU VAL PHE GLU LEU VAL PRO ASP ASP GLU
SEQRES 52 A 790 ARG GLN CYS SER ALA CYS ARG THR THR CYS PHE LEU SER
SEQRES 53 A 790 ALA LEU THR CYS SER CYS ASN PRO GLU ARG LEU VAL CYS
SEQRES 54 A 790 LEU TYR HIS PRO THR ASP LEU CYS PRO CYS PRO MET GLN
SEQRES 55 A 790 LYS LYS CYS LEU ARG TYR ARG TYR PRO LEU GLU ASP LEU
SEQRES 56 A 790 PRO SER LEU LEU TYR GLY VAL LYS VAL ARG ALA GLN SER
SEQRES 57 A 790 TYR ASP THR TRP VAL SER ARG VAL THR GLU ALA LEU SER
SEQRES 58 A 790 ALA ASN PHE ASN HIS LYS LYS ASP LEU ILE GLU LEU ARG
SEQRES 59 A 790 VAL MET LEU GLU ASP ALA GLU ASP ARG LYS TYR PRO GLU
SEQRES 60 A 790 ASN ASP LEU PHE ARG LYS LEU ARG ASP ALA VAL LYS GLU
SEQRES 61 A 790 ALA GLU THR CYS ALA SER VAL GLY ASN SER
SEQRES 1 B 790 SER GLU PHE VAL PRO PRO PRO GLU CYS PRO VAL PHE GLU
SEQRES 2 B 790 PRO SER TRP GLU GLU PHE THR ASP PRO LEU SER PHE ILE
SEQRES 3 B 790 GLY ARG ILE ARG PRO LEU ALA GLU LYS THR GLY ILE CYS
SEQRES 4 B 790 LYS ILE ARG PRO PRO LYS ASP TRP GLN PRO PRO PHE ALA
SEQRES 5 B 790 CYS GLU VAL LYS SER PHE ARG PHE THR PRO ARG VAL GLN
SEQRES 6 B 790 ARG LEU ASN GLU LEU GLU ALA MET THR ARG VAL ARG LEU
SEQRES 7 B 790 ASP PHE LEU ASP GLN LEU ALA LYS PHE TRP GLU LEU GLN
SEQRES 8 B 790 GLY SER THR LEU LYS ILE PRO VAL VAL GLU ARG LYS ILE
SEQRES 9 B 790 LEU ASP LEU TYR ALA LEU SER LYS ILE VAL ALA SER LYS
SEQRES 10 B 790 GLY GLY PHE GLU MET VAL THR LYS GLU LYS LYS TRP SER
SEQRES 11 B 790 LYS VAL GLY SER ARG LEU GLY TYR LEU PRO GLY LYS GLY
SEQRES 12 B 790 THR GLY SER LEU LEU LYS SER HIS TYR GLU ARG ILE LEU
SEQRES 13 B 790 TYR PRO TYR GLU LEU PHE GLN SER GLY VAL SER LEU MET
SEQRES 14 B 790 GLY VAL GLN MET PRO ASN LEU ASP LEU LYS GLU LYS VAL
SEQRES 15 B 790 GLU PRO GLU VAL LEU SER THR ASP THR GLN THR SER PRO
SEQRES 16 B 790 GLU PRO GLY THR ARG MET ASN ILE LEU PRO LYS ARG THR
SEQRES 17 B 790 ARG ARG VAL LYS THR GLN SER GLU SER GLY ASP VAL SER
SEQRES 18 B 790 ARG ASN THR GLU LEU LYS LYS LEU GLN ILE PHE GLY ALA
SEQRES 19 B 790 GLY PRO LYS VAL VAL GLY LEU ALA MET GLY THR LYS ASP
SEQRES 20 B 790 LYS GLU ASP GLU VAL THR ARG ARG ARG LYS VAL THR ASN
SEQRES 21 B 790 ARG SER ASP ALA PHE ASN MET GLN MET ARG GLN ARG LYS
SEQRES 22 B 790 GLY THR LEU SER VAL ASN PHE VAL ASP LEU TYR VAL CYS
SEQRES 23 B 790 MET PHE CYS GLY ARG GLY ASN ASN GLU ASP LYS LEU LEU
SEQRES 24 B 790 LEU CYS ASP GLY CYS ASP ASP SER TYR HIS THR PHE CYS
SEQRES 25 B 790 LEU ILE PRO PRO LEU PRO ASP VAL PRO LYS GLY ASP TRP
SEQRES 26 B 790 ARG CYS PRO LYS CYS VAL ALA GLU GLU CYS SER LYS PRO
SEQRES 27 B 790 ARG GLU ALA PHE GLY PHE GLU GLN ALA VAL ARG GLU TYR
SEQRES 28 B 790 THR LEU GLN SER PHE GLY GLU MET ALA ASP ASN PHE LYS
SEQRES 29 B 790 SER ASP TYR PHE ASN MET PRO VAL HIS MET VAL PRO THR
SEQRES 30 B 790 GLU LEU VAL GLU LYS GLU PHE TRP ARG LEU VAL SER SER
SEQRES 31 B 790 ILE GLU GLU ASP VAL ILE VAL GLU TYR GLY ALA ASP ILE
SEQRES 32 B 790 SER SER LYS ASP PHE GLY SER GLY PHE PRO VAL LYS ASP
SEQRES 33 B 790 GLY ARG ARG LYS ILE LEU PRO GLU GLU GLU GLU TYR ALA
SEQRES 34 B 790 LEU SER GLY TRP ASN LEU ASN ASN MET PRO VAL LEU GLU
SEQRES 35 B 790 GLN SER VAL LEU ALA HIS ILE ASN VAL ASP ILE SER GLY
SEQRES 36 B 790 MET LYS VAL PRO TRP LEU TYR VAL GLY MET CYS PHE SER
SEQRES 37 B 790 SER PHE CYS TRP HIS ILE GLU ASP HIS TRP SER TYR SER
SEQRES 38 B 790 ILE ASN TYR LEU HIS TRP GLY GLU PRO LYS THR TRP TYR
SEQRES 39 B 790 GLY VAL PRO SER HIS ALA ALA GLU GLN LEU GLU GLU VAL
SEQRES 40 B 790 MET ARG GLU LEU ALA PRO GLU LEU PHE GLU SER GLN PRO
SEQRES 41 B 790 ASP LEU LEU HIS GLN LEU VAL THR ILE MET ASN PRO ASN
SEQRES 42 B 790 VAL LEU MET GLU HIS GLY VAL PRO VAL TYR ARG THR ASN
SEQRES 43 B 790 GLN CYS ALA GLY GLU PHE VAL VAL THR PHE PRO ARG ALA
SEQRES 44 B 790 TYR HIS SER GLY PHE ASN GLN GLY TYR ASN PHE ALA GLU
SEQRES 45 B 790 ALA VAL ASN PHE CYS THR ALA ASP TRP LEU PRO ILE GLY
SEQRES 46 B 790 ARG GLN CYS VAL ASN HIS TYR ARG ARG LEU ARG ARG HIS
SEQRES 47 B 790 CYS VAL PHE SER HIS GLU GLU LEU ILE PHE LYS MET ALA
SEQRES 48 B 790 ALA ASP PRO GLU CYS LEU ASP VAL GLY LEU ALA ALA MET
SEQRES 49 B 790 VAL CYS LYS GLU LEU THR LEU MET THR GLU GLU GLU THR
SEQRES 50 B 790 ARG LEU ARG GLU SER VAL VAL GLN MET GLY VAL LEU MET
SEQRES 51 B 790 SER GLU GLU GLU VAL PHE GLU LEU VAL PRO ASP ASP GLU
SEQRES 52 B 790 ARG GLN CYS SER ALA CYS ARG THR THR CYS PHE LEU SER
SEQRES 53 B 790 ALA LEU THR CYS SER CYS ASN PRO GLU ARG LEU VAL CYS
SEQRES 54 B 790 LEU TYR HIS PRO THR ASP LEU CYS PRO CYS PRO MET GLN
SEQRES 55 B 790 LYS LYS CYS LEU ARG TYR ARG TYR PRO LEU GLU ASP LEU
SEQRES 56 B 790 PRO SER LEU LEU TYR GLY VAL LYS VAL ARG ALA GLN SER
SEQRES 57 B 790 TYR ASP THR TRP VAL SER ARG VAL THR GLU ALA LEU SER
SEQRES 58 B 790 ALA ASN PHE ASN HIS LYS LYS ASP LEU ILE GLU LEU ARG
SEQRES 59 B 790 VAL MET LEU GLU ASP ALA GLU ASP ARG LYS TYR PRO GLU
SEQRES 60 B 790 ASN ASP LEU PHE ARG LYS LEU ARG ASP ALA VAL LYS GLU
SEQRES 61 B 790 ALA GLU THR CYS ALA SER VAL GLY ASN SER
SEQRES 1 F 10 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 1 G 10 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
HET NI A 901 1
HET ZN A 902 1
HET ZN A 903 1
HET 6QN A 904 28
HET NI B 901 1
HET ZN B 902 1
HET ZN B 903 1
HET 6QN B 904 28
HETNAM NI NICKEL (II) ION
HETNAM ZN ZINC ION
HETNAM 6QN ~{N}-ETHYL-4-OXIDANYL-2-OXIDANYLIDENE-1~{H}-1,7-
HETNAM 2 6QN NAPHTHYRIDINE-3-CARBOXAMIDE
FORMUL 5 NI 2(NI 2+)
FORMUL 6 ZN 4(ZN 2+)
FORMUL 8 6QN 2(C11 H11 N3 O3)
FORMUL 13 HOH *20(H2 O)
HELIX 1 AA1 GLU A 27 THR A 30 5 4
HELIX 2 AA2 ASP A 31 GLU A 44 1 14
HELIX 3 AA3 THR A 84 GLY A 102 1 19
HELIX 4 AA4 ASP A 116 LYS A 127 1 12
HELIX 5 AA5 GLY A 129 LYS A 137 1 9
HELIX 6 AA6 LYS A 138 LEU A 146 1 9
HELIX 7 AA7 GLY A 153 SER A 174 1 22
HELIX 8 AA8 THR A 362 ASN A 379 1 18
HELIX 9 AA9 PRO A 381 VAL A 385 5 5
HELIX 10 AB1 PRO A 386 SER A 399 1 14
HELIX 11 AB2 SER A 415 GLY A 419 1 5
HELIX 12 AB3 LEU A 432 SER A 441 1 10
HELIX 13 AB4 ASN A 447 LEU A 451 5 5
HELIX 14 AB5 PRO A 507 HIS A 509 5 3
HELIX 15 AB6 ALA A 510 GLU A 520 1 11
HELIX 16 AB7 ALA A 522 GLN A 529 1 8
HELIX 17 AB8 ASP A 531 LEU A 536 1 6
HELIX 18 AB9 ASN A 541 HIS A 548 1 8
HELIX 19 AC1 THR A 588 ASP A 590 5 3
HELIX 20 AC2 TRP A 591 LEU A 605 1 15
HELIX 21 AC3 SER A 612 ALA A 622 1 11
HELIX 22 AC4 ASP A 628 MET A 656 1 29
HELIX 23 AC5 HIS A 702 LEU A 706 5 5
HELIX 24 AC6 GLU A 723 SER A 744 1 22
HELIX 25 AC7 MET A 766 ARG A 773 1 8
HELIX 26 AC8 ASN A 778 ARG A 785 1 8
HELIX 27 AC9 ASP B 31 GLU B 44 1 14
HELIX 28 AD1 THR B 84 GLN B 101 1 18
HELIX 29 AD2 ASP B 116 LYS B 127 1 12
HELIX 30 AD3 GLY B 129 LYS B 137 1 9
HELIX 31 AD4 LYS B 138 LEU B 146 1 9
HELIX 32 AD5 GLY B 153 ILE B 165 1 13
HELIX 33 AD6 ILE B 165 SER B 174 1 10
HELIX 34 AD7 THR B 362 ASN B 379 1 18
HELIX 35 AD8 PRO B 381 VAL B 385 5 5
HELIX 36 AD9 PRO B 386 SER B 400 1 15
HELIX 37 AE1 SER B 414 GLY B 419 1 6
HELIX 38 AE2 LEU B 432 SER B 441 1 10
HELIX 39 AE3 ASN B 444 MET B 448 5 5
HELIX 40 AE4 ALA B 510 GLU B 520 1 11
HELIX 41 AE5 ALA B 522 GLN B 529 1 8
HELIX 42 AE6 ASP B 531 LEU B 536 1 6
HELIX 43 AE7 ASN B 541 HIS B 548 1 8
HELIX 44 AE8 ASP B 590 LEU B 605 1 16
HELIX 45 AE9 SER B 612 ALA B 622 1 11
HELIX 46 AF1 ASP B 628 MET B 656 1 29
HELIX 47 AF2 HIS B 702 LEU B 706 5 5
HELIX 48 AF3 GLU B 723 SER B 744 1 22
HELIX 49 AF4 MET B 766 ARG B 773 1 8
HELIX 50 AF5 ASN B 778 ARG B 785 1 8
HELIX 51 AF6 UNK F 221 UNK F 226 1 6
HELIX 52 AF7 UNK G 221 UNK G 226 1 6
SHEET 1 AA1 8 VAL A 21 PHE A 22 0
SHEET 2 AA1 8 ILE A 48 ILE A 51 1 O LYS A 50 N PHE A 22
SHEET 3 AA1 8 PHE A 562 THR A 565 -1 O PHE A 562 N ILE A 51
SHEET 4 AA1 8 SER A 491 GLY A 498 -1 N ASN A 493 O VAL A 563
SHEET 5 AA1 8 ASN A 579 ASN A 585 -1 O GLU A 582 N TYR A 494
SHEET 6 AA1 8 TRP A 470 GLY A 474 -1 N TRP A 470 O ALA A 583
SHEET 7 AA1 8 ILE A 406 SER A 414 -1 N ILE A 413 O LEU A 471
SHEET 8 AA1 8 ARG A 73 ARG A 76 -1 N GLN A 75 O VAL A 407
SHEET 1 AA2 2 VAL A 109 VAL A 110 0
SHEET 2 AA2 2 LYS A 113 ILE A 114 -1 O LYS A 113 N VAL A 110
SHEET 1 AA3 4 SER A 479 HIS A 483 0
SHEET 2 AA3 4 HIS A 571 ASN A 575 -1 O GLY A 573 N PHE A 480
SHEET 3 AA3 4 LYS A 501 GLY A 505 -1 N TYR A 504 O SER A 572
SHEET 4 AA3 4 TYR A 553 GLN A 557 -1 O GLN A 557 N LYS A 501
SHEET 1 AA4 3 SER A 661 GLU A 663 0
SHEET 2 AA4 3 LEU A 716 TYR A 718 1 O TYR A 718 N GLU A 662
SHEET 3 AA4 3 SER A 686 LEU A 688 -1 N ALA A 687 O ARG A 717
SHEET 1 AA5 6 VAL B 21 PHE B 22 0
SHEET 2 AA5 6 ILE B 48 ILE B 51 1 O LYS B 50 N PHE B 22
SHEET 3 AA5 6 PHE B 562 THR B 565 -1 O VAL B 564 N CYS B 49
SHEET 4 AA5 6 TYR B 490 GLY B 498 -1 N SER B 491 O THR B 565
SHEET 5 AA5 6 ASN B 579 PHE B 586 -1 O GLU B 582 N TYR B 494
SHEET 6 AA5 6 TRP B 470 GLY B 474 -1 N TRP B 470 O ALA B 583
SHEET 1 AA6 2 ARG B 73 ARG B 76 0
SHEET 2 AA6 2 ILE B 406 TYR B 409 -1 O TYR B 409 N ARG B 73
SHEET 1 AA7 2 VAL B 109 VAL B 110 0
SHEET 2 AA7 2 LYS B 113 ILE B 114 -1 O LYS B 113 N VAL B 110
SHEET 1 AA8 4 SER B 479 HIS B 483 0
SHEET 2 AA8 4 HIS B 571 ASN B 575 -1 O GLY B 573 N PHE B 480
SHEET 3 AA8 4 LYS B 501 GLY B 505 -1 N THR B 502 O PHE B 574
SHEET 4 AA8 4 TYR B 553 GLN B 557 -1 O GLN B 557 N LYS B 501
SHEET 1 AA9 3 SER B 661 GLU B 663 0
SHEET 2 AA9 3 LEU B 716 TYR B 718 1 O TYR B 718 N GLU B 662
SHEET 3 AA9 3 SER B 686 LEU B 688 -1 N ALA B 687 O ARG B 717
SSBOND 1 CYS B 692 CYS B 707 1555 1555 2.04
LINK NE2 HIS A 483 NI NI A 901 1555 1555 2.06
LINK OE1 GLU A 485 NI NI A 901 1555 1555 2.02
LINK OE2 GLU A 485 NI NI A 901 1555 1555 2.05
LINK NE2 HIS A 571 NI NI A 901 1555 1555 2.00
LINK SG CYS A 676 ZN ZN A 902 1555 1555 2.29
LINK SG CYS A 679 ZN ZN A 902 1555 1555 2.70
LINK SG CYS A 690 ZN ZN A 903 1555 1555 2.25
LINK SG CYS A 709 ZN ZN A 903 1555 1555 2.46
LINK NE2 HIS B 483 NI NI B 901 1555 1555 1.99
LINK OE2 GLU B 485 NI NI B 901 1555 1555 1.99
LINK NE2 HIS B 571 NI NI B 901 1555 1555 2.01
LINK SG CYS B 676 ZN ZN B 902 1555 1555 2.43
LINK SG CYS B 679 ZN ZN B 902 1555 1555 2.11
LINK SG CYS B 699 ZN ZN B 902 1555 1555 2.28
LINK ND1 HIS B 702 ZN ZN B 902 1555 1555 2.01
LINK SG CYS B 707 ZN ZN B 903 1555 1555 2.29
LINK O CYS B 709 ZN ZN B 903 1555 1555 2.58
LINK NI NI A 901 N11 6QN A 904 1555 1555 2.04
LINK NI NI B 901 N11 6QN B 904 1555 1555 1.96
CISPEP 1 PRO A 150 GLY A 151 0 -7.78
CISPEP 2 GLY A 180 VAL A 181 0 -14.64
CISPEP 3 CYS A 679 ARG A 680 0 -6.61
CISPEP 4 LYS A 714 CYS A 715 0 -24.90
CISPEP 5 PRO B 150 GLY B 151 0 -5.73
CISPEP 6 GLY B 180 VAL B 181 0 -13.50
CISPEP 7 CYS B 679 ARG B 680 0 -2.91
CISPEP 8 LYS B 714 CYS B 715 0 -28.76
SITE 1 AC1 4 HIS A 483 GLU A 485 HIS A 571 6QN A 904
SITE 1 AC2 3 CYS A 676 CYS A 679 CYS A 699
SITE 1 AC3 4 CYS A 690 SER A 691 CYS A 692 CYS A 709
SITE 1 AC4 11 TYR A 472 SER A 478 PHE A 480 HIS A 483
SITE 2 AC4 11 GLU A 485 ASN A 493 LYS A 501 TRP A 503
SITE 3 AC4 11 HIS A 571 ASN A 575 NI A 901
SITE 1 AC5 4 HIS B 483 GLU B 485 HIS B 571 6QN B 904
SITE 1 AC6 5 CYS B 676 ALA B 678 CYS B 679 CYS B 699
SITE 2 AC6 5 HIS B 702
SITE 1 AC7 4 CYS B 690 CYS B 692 CYS B 707 CYS B 709
SITE 1 AC8 11 TYR B 472 VAL B 473 SER B 479 PHE B 480
SITE 2 AC8 11 HIS B 483 ASN B 493 LYS B 501 TRP B 503
SITE 3 AC8 11 HIS B 571 ASN B 575 NI B 901
CRYST1 159.141 159.141 92.109 90.00 90.00 120.00 P 31 6
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 0.006284 0.003628 0.000000 0.00000
SCALE2 0.000000 0.007256 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010857 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
