HEADER DNA BINDING PROTEIN/DNA 07-MAR-17 5V3M
TITLE MOUSEZFP568-ZNF1-11 IN COMPLEX WITH DNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (28-MER);
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: DNA (28-MER);
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: ZINC FINGER PROTEIN 568;
COMPND 11 CHAIN: C;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 MOL_ID: 2;
SOURCE 6 SYNTHETIC: YES;
SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 8 ORGANISM_TAXID: 10090;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 11 ORGANISM_COMMON: MOUSE;
SOURCE 12 ORGANISM_TAXID: 10090;
SOURCE 13 GENE: ZNF568, CHATO, ZFP568;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 866768
KEYWDS C2H2 TYPE ZINC FINGERS, DNA BINDING, TRANSFERASE-DNA COMPLEX, DNA
KEYWDS 2 BINDING PROTEIN-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.PATEL,X.CHENG
REVDAT 2 18-SEP-19 5V3M 1 JRNL
REVDAT 1 07-MAR-18 5V3M 0
JRNL AUTH A.PATEL,P.YANG,M.TINKHAM,M.PRADHAN,M.A.SUN,Y.WANG,D.HOANG,
JRNL AUTH 2 G.WOLF,J.R.HORTON,X.ZHANG,T.MACFARLAN,X.CHENG
JRNL TITL DNA CONFORMATION INDUCES ADAPTABLE BINDING BY TANDEM ZINC
JRNL TITL 2 FINGER PROTEINS.
JRNL REF CELL V. 173 221 2018
JRNL REFN ISSN 1097-4172
JRNL PMID 29551271
JRNL DOI 10.1016/J.CELL.2018.02.058
REMARK 2
REMARK 2 RESOLUTION. 2.09 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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) : 2.09
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.25
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 78.8
REMARK 3 NUMBER OF REFLECTIONS : 53174
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2661
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 32.2492 - 5.5717 0.99 3341 171 0.1670 0.1883
REMARK 3 2 5.5717 - 4.4261 1.00 3357 176 0.1772 0.2016
REMARK 3 3 4.4261 - 3.8676 0.98 3326 177 0.1708 0.1840
REMARK 3 4 3.8676 - 3.5145 0.96 3258 170 0.1845 0.2572
REMARK 3 5 3.5145 - 3.2628 0.96 3176 171 0.2021 0.2411
REMARK 3 6 3.2628 - 3.0706 0.93 3174 173 0.2295 0.2624
REMARK 3 7 3.0706 - 2.9170 0.96 3244 172 0.2698 0.3254
REMARK 3 8 2.9170 - 2.7901 0.98 3303 176 0.2663 0.3448
REMARK 3 9 2.7901 - 2.6827 0.95 3249 168 0.2783 0.3110
REMARK 3 10 2.6827 - 2.5902 0.95 3138 168 0.2712 0.3047
REMARK 3 11 2.5902 - 2.5092 0.91 3117 164 0.2707 0.3150
REMARK 3 12 2.5092 - 2.4375 0.89 3000 160 0.2732 0.3393
REMARK 3 13 2.4375 - 2.3734 0.80 2639 142 0.2767 0.3436
REMARK 3 14 2.3734 - 2.3155 0.69 2437 119 0.2621 0.3180
REMARK 3 15 2.3155 - 2.2629 0.58 1907 101 0.2865 0.3674
REMARK 3 16 2.2629 - 2.2147 0.50 1727 88 0.2804 0.3871
REMARK 3 17 2.2147 - 2.1704 0.38 1259 68 0.2959 0.2773
REMARK 3 18 2.1704 - 2.1295 0.33 1087 60 0.3135 0.4071
REMARK 3 19 2.1295 - 2.0914 0.23 774 37 0.3364 0.5048
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.970
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.025 3441
REMARK 3 ANGLE : 1.095 4827
REMARK 3 CHIRALITY : 0.055 516
REMARK 3 PLANARITY : 0.008 435
REMARK 3 DIHEDRAL : 23.939 1825
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 16
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 362 THROUGH 388 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.7694 -14.8552 -38.0945
REMARK 3 T TENSOR
REMARK 3 T11: 0.8108 T22: 0.7576
REMARK 3 T33: 1.0667 T12: -0.1684
REMARK 3 T13: 0.1084 T23: -0.0206
REMARK 3 L TENSOR
REMARK 3 L11: 5.1965 L22: 4.1859
REMARK 3 L33: 6.8996 L12: 3.9071
REMARK 3 L13: -5.2967 L23: -2.8177
REMARK 3 S TENSOR
REMARK 3 S11: -0.1421 S12: -0.0179 S13: 0.3818
REMARK 3 S21: 0.0820 S22: 0.1652 S23: 2.3021
REMARK 3 S31: 1.0151 S32: -1.2490 S33: -0.0379
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 389 THROUGH 413 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.9466 -12.3972 -25.7044
REMARK 3 T TENSOR
REMARK 3 T11: 0.5053 T22: 0.2584
REMARK 3 T33: 0.4638 T12: 0.0481
REMARK 3 T13: 0.0288 T23: -0.1258
REMARK 3 L TENSOR
REMARK 3 L11: 3.4726 L22: 7.2646
REMARK 3 L33: 2.0399 L12: -0.6510
REMARK 3 L13: 0.5803 L23: -2.7625
REMARK 3 S TENSOR
REMARK 3 S11: -0.1666 S12: 0.4110 S13: -0.7119
REMARK 3 S21: -0.2390 S22: 0.3610 S23: -0.2534
REMARK 3 S31: 1.2124 S32: 0.2905 S33: -0.1893
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 414 THROUGH 430 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.2499 -10.2295 -14.2596
REMARK 3 T TENSOR
REMARK 3 T11: 0.5815 T22: 0.1984
REMARK 3 T33: 0.3862 T12: -0.0312
REMARK 3 T13: 0.0349 T23: -0.0250
REMARK 3 L TENSOR
REMARK 3 L11: 1.9867 L22: 2.1858
REMARK 3 L33: 4.6548 L12: 0.0495
REMARK 3 L13: -2.1382 L23: 2.2101
REMARK 3 S TENSOR
REMARK 3 S11: 0.0903 S12: 0.1379 S13: -0.7102
REMARK 3 S21: 0.2749 S22: 0.1105 S23: -0.1838
REMARK 3 S31: 1.3914 S32: 0.1467 S33: -0.2050
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 431 THROUGH 452 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.8982 3.5603 -14.4485
REMARK 3 T TENSOR
REMARK 3 T11: 0.2884 T22: 0.2256
REMARK 3 T33: 0.2821 T12: 0.0776
REMARK 3 T13: 0.0424 T23: -0.0538
REMARK 3 L TENSOR
REMARK 3 L11: 3.1752 L22: 1.9745
REMARK 3 L33: 1.2044 L12: -0.0482
REMARK 3 L13: 0.3795 L23: -1.2095
REMARK 3 S TENSOR
REMARK 3 S11: -0.0568 S12: -0.2447 S13: 0.2441
REMARK 3 S21: 0.3369 S22: 0.1486 S23: 0.5048
REMARK 3 S31: -0.4607 S32: -0.5000 S33: -0.0449
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 453 THROUGH 468 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.9005 13.5254 -17.0157
REMARK 3 T TENSOR
REMARK 3 T11: 0.6348 T22: 0.2763
REMARK 3 T33: 0.4269 T12: 0.1542
REMARK 3 T13: -0.1291 T23: -0.0257
REMARK 3 L TENSOR
REMARK 3 L11: 1.8852 L22: 2.2513
REMARK 3 L33: 1.1824 L12: -1.7762
REMARK 3 L13: -1.4246 L23: 1.5862
REMARK 3 S TENSOR
REMARK 3 S11: -0.1276 S12: -0.0215 S13: 0.4545
REMARK 3 S21: -0.0782 S22: 0.0704 S23: 0.6254
REMARK 3 S31: -0.7949 S32: -0.4459 S33: 0.0063
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 469 THROUGH 564 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.6028 8.0248 -33.9261
REMARK 3 T TENSOR
REMARK 3 T11: 0.7977 T22: 0.5345
REMARK 3 T33: 0.3059 T12: -0.3914
REMARK 3 T13: 0.0858 T23: 0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 1.4876 L22: 2.0433
REMARK 3 L33: 1.1751 L12: 0.1826
REMARK 3 L13: 0.6164 L23: 0.7647
REMARK 3 S TENSOR
REMARK 3 S11: -0.4342 S12: 0.6371 S13: 0.1286
REMARK 3 S21: -0.3903 S22: 0.4739 S23: -0.1269
REMARK 3 S31: -0.6434 S32: 0.5456 S33: -0.0414
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 565 THROUGH 580 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.5112 11.6556 -49.1375
REMARK 3 T TENSOR
REMARK 3 T11: 1.0004 T22: 0.8173
REMARK 3 T33: 0.1823 T12: -0.3270
REMARK 3 T13: 0.0278 T23: 0.1584
REMARK 3 L TENSOR
REMARK 3 L11: 5.0938 L22: 7.0174
REMARK 3 L33: 6.1485 L12: 0.9367
REMARK 3 L13: -2.0158 L23: -6.2880
REMARK 3 S TENSOR
REMARK 3 S11: -0.1462 S12: 0.5610 S13: 0.3420
REMARK 3 S21: -0.0428 S22: -0.0193 S23: -0.1428
REMARK 3 S31: -0.8817 S32: -0.2015 S33: 0.0855
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 581 THROUGH 598 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.2804 24.6159 -55.4182
REMARK 3 T TENSOR
REMARK 3 T11: 1.7930 T22: 1.2446
REMARK 3 T33: 0.8649 T12: -0.4502
REMARK 3 T13: 0.0150 T23: 0.5720
REMARK 3 L TENSOR
REMARK 3 L11: 2.8244 L22: 0.4553
REMARK 3 L33: 0.7340 L12: -0.5845
REMARK 3 L13: -1.2919 L23: 0.0469
REMARK 3 S TENSOR
REMARK 3 S11: 0.6575 S12: 0.6700 S13: 1.1222
REMARK 3 S21: 0.1940 S22: -0.3997 S23: -0.3431
REMARK 3 S31: -0.9966 S32: 0.0810 S33: -0.4021
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 599 THROUGH 638 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.6836 11.4458 -68.3257
REMARK 3 T TENSOR
REMARK 3 T11: 1.2322 T22: 2.2142
REMARK 3 T33: 0.5369 T12: -0.5277
REMARK 3 T13: 0.1071 T23: 0.1026
REMARK 3 L TENSOR
REMARK 3 L11: 2.1346 L22: 1.4791
REMARK 3 L33: 2.9746 L12: -0.0725
REMARK 3 L13: -1.7781 L23: -0.0837
REMARK 3 S TENSOR
REMARK 3 S11: 0.0874 S12: 0.7213 S13: 0.0318
REMARK 3 S21: -0.8177 S22: -0.2010 S23: -0.6050
REMARK 3 S31: -0.6672 S32: 0.7271 S33: 0.0991
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 5 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.9767 9.1036 -80.6795
REMARK 3 T TENSOR
REMARK 3 T11: 1.9685 T22: 2.1270
REMARK 3 T33: 0.3362 T12: -0.0355
REMARK 3 T13: -0.1541 T23: -0.0892
REMARK 3 L TENSOR
REMARK 3 L11: 1.2366 L22: 1.9781
REMARK 3 L33: 2.1384 L12: 0.8677
REMARK 3 L13: 0.6889 L23: 1.4594
REMARK 3 S TENSOR
REMARK 3 S11: 0.0804 S12: 0.5138 S13: -0.1314
REMARK 3 S21: -0.9698 S22: -0.1876 S23: 0.2626
REMARK 3 S31: 0.2875 S32: -0.1608 S33: 0.0271
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 6 THROUGH 15 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.2688 9.1992 -56.4762
REMARK 3 T TENSOR
REMARK 3 T11: 0.8963 T22: 1.3156
REMARK 3 T33: 0.2902 T12: -0.5200
REMARK 3 T13: 0.1155 T23: 0.0577
REMARK 3 L TENSOR
REMARK 3 L11: 2.0120 L22: 1.8373
REMARK 3 L33: 2.7161 L12: -1.8588
REMARK 3 L13: -0.9975 L23: 0.7539
REMARK 3 S TENSOR
REMARK 3 S11: 0.0751 S12: 0.9532 S13: 0.3576
REMARK 3 S21: -0.6136 S22: -0.1722 S23: -0.0833
REMARK 3 S31: -0.6608 S32: -0.1473 S33: -0.1139
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 16 THROUGH 28 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.7305 7.7963 -19.9468
REMARK 3 T TENSOR
REMARK 3 T11: 0.5196 T22: 0.2017
REMARK 3 T33: 0.2730 T12: -0.1559
REMARK 3 T13: -0.0194 T23: 0.0137
REMARK 3 L TENSOR
REMARK 3 L11: 2.0412 L22: 1.5624
REMARK 3 L33: 3.1275 L12: 0.9110
REMARK 3 L13: -2.1428 L23: -1.9357
REMARK 3 S TENSOR
REMARK 3 S11: -0.4071 S12: 0.4272 S13: 0.0521
REMARK 3 S21: -0.4392 S22: 0.3569 S23: 0.0915
REMARK 3 S31: -0.9344 S32: 0.4642 S33: 0.0680
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 10 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.6391 6.0896 -13.9297
REMARK 3 T TENSOR
REMARK 3 T11: 0.3321 T22: 0.2253
REMARK 3 T33: 0.2565 T12: -0.0903
REMARK 3 T13: 0.0083 T23: -0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 0.5001 L22: 2.1525
REMARK 3 L33: 6.1654 L12: 1.0175
REMARK 3 L13: 0.2609 L23: -0.0874
REMARK 3 S TENSOR
REMARK 3 S11: -0.0084 S12: 0.0882 S13: 0.0332
REMARK 3 S21: -0.0330 S22: 0.2178 S23: -0.1491
REMARK 3 S31: -0.9310 S32: 0.5262 S33: -0.2145
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 11 THROUGH 20 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.3327 9.3140 -47.2080
REMARK 3 T TENSOR
REMARK 3 T11: 0.9848 T22: 0.9897
REMARK 3 T33: 0.3716 T12: -0.4508
REMARK 3 T13: -0.0472 T23: 0.1113
REMARK 3 L TENSOR
REMARK 3 L11: 0.4423 L22: 0.9911
REMARK 3 L33: 2.6287 L12: 0.2017
REMARK 3 L13: 1.0626 L23: 0.7208
REMARK 3 S TENSOR
REMARK 3 S11: -0.0260 S12: 1.1875 S13: 0.1032
REMARK 3 S21: -0.2705 S22: 0.4486 S23: -0.1209
REMARK 3 S31: -0.7262 S32: 0.5001 S33: -0.2267
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 21 THROUGH 25 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.9538 11.8059 -70.0867
REMARK 3 T TENSOR
REMARK 3 T11: 1.5326 T22: 2.2028
REMARK 3 T33: 0.6653 T12: -0.4068
REMARK 3 T13: -0.3313 T23: 0.1376
REMARK 3 L TENSOR
REMARK 3 L11: 2.3734 L22: 0.4726
REMARK 3 L33: 8.9300 L12: -0.2293
REMARK 3 L13: -0.4395 L23: -0.2062
REMARK 3 S TENSOR
REMARK 3 S11: 0.0448 S12: 0.8268 S13: -0.1164
REMARK 3 S21: 0.2546 S22: 0.5608 S23: 0.1427
REMARK 3 S31: -0.7655 S32: -1.2086 S33: -0.5225
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 26 THROUGH 28 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.6050 16.6048 -83.8078
REMARK 3 T TENSOR
REMARK 3 T11: 2.0454 T22: 3.1114
REMARK 3 T33: 0.7788 T12: -0.3788
REMARK 3 T13: 0.0887 T23: 0.1315
REMARK 3 L TENSOR
REMARK 3 L11: 0.6120 L22: 1.9632
REMARK 3 L33: 2.1211 L12: -0.6469
REMARK 3 L13: 1.0598 L23: -0.5154
REMARK 3 S TENSOR
REMARK 3 S11: 0.1710 S12: -0.6118 S13: 0.2136
REMARK 3 S21: -1.0923 S22: 0.4733 S23: -0.5276
REMARK 3 S31: -1.4152 S32: 1.8579 S33: -0.5911
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 5V3M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1000226829.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-AUG-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300-HS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53292
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.090
REMARK 200 RESOLUTION RANGE LOW (A) : 32.245
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 81.7
REMARK 200 DATA REDUNDANCY : 13.90
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.09
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 32.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 0.47900
REMARK 200 R SYM FOR SHELL (I) : 0.15900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% ISOPROPANOL, 0.1M BICINE(PH 8.5)
REMARK 280 AND 30% (W/V) PEG1500, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 176.83350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 176.83350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 17.97700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 46.37900
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 17.97700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 46.37900
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 176.83350
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 17.97700
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 46.37900
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 176.83350
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 17.97700
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 46.37900
REMARK 290 SMTRY3 8 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8690 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 131 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY C 358
REMARK 465 PRO C 359
REMARK 465 GLY C 360
REMARK 465 SER C 361
REMARK 465 GLY C 639
REMARK 465 GLU C 640
REMARK 465 LYS C 641
REMARK 465 PRO C 642
REMARK 465 TYR C 643
REMARK 465 LYS C 644
REMARK 465 CYS C 645
REMARK 465 GLN C 646
REMARK 465 GLN C 647
REMARK 465 CYS C 648
REMARK 465 GLY C 649
REMARK 465 LYS C 650
REMARK 465 ALA C 651
REMARK 465 PHE C 652
REMARK 465 ILE C 653
REMARK 465 ARG C 654
REMARK 465 GLY C 655
REMARK 465 SER C 656
REMARK 465 HIS C 657
REMARK 465 LEU C 658
REMARK 465 THR C 659
REMARK 465 GLN C 660
REMARK 465 HIS C 661
REMARK 465 GLN C 662
REMARK 465 ARG C 663
REMARK 465 ILE C 664
REMARK 465 HIS C 665
REMARK 465 THR C 666
REMARK 465 GLY C 667
REMARK 465 ARG C 668
REMARK 465 ARG C 669
REMARK 465 LEU C 670
REMARK 465 GLU C 671
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 HIS C 363 CG ND1 CD2 CE1 NE2
REMARK 470 LYS C 364 CG CD CE NZ
REMARK 470 LYS C 370 CG CD CE NZ
REMARK 470 PHE C 372 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 THR C 374 OG1 CG2
REMARK 470 GLN C 377 CG CD OE1 NE2
REMARK 470 HIS C 380 CG ND1 CD2 CE1 NE2
REMARK 470 LYS C 383 CG CD CE NZ
REMARK 470 GLN C 394 CD OE1 NE2
REMARK 470 LYS C 448 CD CE NZ
REMARK 470 ASP C 481 CG OD1 OD2
REMARK 470 LYS C 482 CG CD CE NZ
REMARK 470 LYS C 506 CG CD CE NZ
REMARK 470 GLU C 528 CG CD OE1 OE2
REMARK 470 LYS C 538 CG CD CE NZ
REMARK 470 LYS C 562 CG CD CE NZ
REMARK 470 GLU C 563 CG CD OE1 OE2
REMARK 470 LYS C 566 CG CD CE NZ
REMARK 470 THR C 582 OG1 CG2
REMARK 470 ASP C 584 CG OD1 OD2
REMARK 470 LYS C 588 CG CD CE NZ
REMARK 470 LYS C 590 CG CD CE NZ
REMARK 470 GLU C 591 CG CD OE1 OE2
REMARK 470 LYS C 594 CG CD CE NZ
REMARK 470 ARG C 599 CG CD NE CZ NH1 NH2
REMARK 470 LEU C 602 CG CD1 CD2
REMARK 470 HIS C 604 CG ND1 CD2 CE1 NE2
REMARK 470 GLU C 606 CG CD OE1 OE2
REMARK 470 ARG C 607 CG CD NE CZ NH1 NH2
REMARK 470 SER C 608 OG
REMARK 470 SER C 610 OG
REMARK 470 GLU C 612 CG CD OE1 OE2
REMARK 470 LYS C 613 CG CD CE NZ
REMARK 470 TYR C 615 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU C 616 CG CD OE1 OE2
REMARK 470 LYS C 618 CG CD CE NZ
REMARK 470 GLU C 619 CG CD OE1 OE2
REMARK 470 LYS C 622 CG CD CE NZ
REMARK 470 LEU C 630 CG CD1 CD2
REMARK 470 SER C 631 OG
REMARK 470 GLN C 634 CG CD OE1 NE2
REMARK 470 LYS C 635 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 SG CYS C 452 ZN ZN C 1004 1.70
REMARK 500 NE2 HIS C 465 ZN ZN C 1004 1.70
REMARK 500 SG CYS C 505 NE2 HIS C 525 1.90
REMARK 500 SG CYS C 620 CE1 HIS C 633 2.05
REMARK 500 OP1 DA A 21 O HOH A 101 2.07
REMARK 500 OP2 DC A 12 O HOH A 102 2.12
REMARK 500 O HOH A 124 O HOH A 128 2.15
REMARK 500 O HOH A 126 O HOH A 127 2.16
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 DA A 20 O3' DA A 20 C3' -0.080
REMARK 500 DA A 22 O3' DA A 22 C3' -0.037
REMARK 500 DT B 1 O3' DT B 1 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 DG A 4 C3' - C2' - C1' ANGL. DEV. = -4.9 DEGREES
REMARK 500 DG A 4 O4' - C1' - N9 ANGL. DEV. = 2.6 DEGREES
REMARK 500 DC A 7 O4' - C1' - N1 ANGL. DEV. = 2.9 DEGREES
REMARK 500 CYS C 508 CA - CB - SG ANGL. DEV. = 8.9 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 GLU C 367 -67.28 -92.73
REMARK 500 LYS C 506 -19.71 -49.18
REMARK 500 LYS C 579 3.35 -68.76
REMARK 500 HIS C 587 62.89 65.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLU C 507 16.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 133 DISTANCE = 8.57 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C1001 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 365 SG
REMARK 620 2 CYS C 368 SG 98.9
REMARK 620 3 HIS C 381 NE2 87.5 104.7
REMARK 620 4 HIS C 385 NE2 104.4 130.0 119.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C1002 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 393 SG
REMARK 620 2 CYS C 396 SG 115.5
REMARK 620 3 HIS C 409 NE2 110.4 97.5
REMARK 620 4 HIS C 413 NE2 79.9 144.9 106.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C1003 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 421 SG
REMARK 620 2 CYS C 424 SG 111.3
REMARK 620 3 HIS C 437 NE2 113.1 97.9
REMARK 620 4 HIS C 441 NE2 103.4 123.2 108.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C1004 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 449 SG
REMARK 620 2 HIS C 469 NE2 94.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C1005 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 477 SG
REMARK 620 2 CYS C 480 SG 102.2
REMARK 620 3 HIS C 493 NE2 106.5 104.4
REMARK 620 4 HIS C 497 NE2 107.6 135.9 97.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C1006 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 505 SG
REMARK 620 2 CYS C 508 SG 143.2
REMARK 620 3 HIS C 521 NE2 103.6 111.5
REMARK 620 4 HIS C 525 NE2 49.7 126.9 104.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C1007 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 533 SG
REMARK 620 2 CYS C 536 SG 92.0
REMARK 620 3 HIS C 549 NE2 100.7 84.2
REMARK 620 4 HIS C 553 NE2 113.5 154.3 87.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C1008 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 561 SG
REMARK 620 2 CYS C 564 SG 82.5
REMARK 620 3 HIS C 577 NE2 91.5 69.4
REMARK 620 4 HIS C 581 NE2 120.0 142.9 132.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C1009 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 589 SG
REMARK 620 2 CYS C 592 SG 93.1
REMARK 620 3 HIS C 605 NE2 140.2 91.0
REMARK 620 4 HIS C 609 NE2 125.3 125.7 81.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C1010 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 617 SG
REMARK 620 2 CYS C 620 N 69.8
REMARK 620 3 CYS C 620 SG 90.6 77.9
REMARK 620 4 HIS C 633 NE2 78.4 109.0 40.2
REMARK 620 5 HIS C 637 NE2 116.1 145.1 133.7 105.8
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 1006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 1007
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 1008
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 1009
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 1010
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5V3G RELATED DB: PDB
REMARK 900 RELATED ID: 5V3J RELATED DB: PDB
DBREF 5V3M A 1 28 PDB 5V3M 5V3M 1 28
DBREF 5V3M B 1 28 PDB 5V3M 5V3M 1 28
DBREF 5V3M C 362 669 UNP E9PYI1 ZN568_MOUSE 362 669
SEQADV 5V3M GLY C 358 UNP E9PYI1 EXPRESSION TAG
SEQADV 5V3M PRO C 359 UNP E9PYI1 EXPRESSION TAG
SEQADV 5V3M GLY C 360 UNP E9PYI1 EXPRESSION TAG
SEQADV 5V3M SER C 361 UNP E9PYI1 EXPRESSION TAG
SEQADV 5V3M LEU C 670 UNP E9PYI1 EXPRESSION TAG
SEQADV 5V3M GLU C 671 UNP E9PYI1 EXPRESSION TAG
SEQRES 1 A 28 DT DG DT DG DG DG DC DG DT DG DG DC DA
SEQRES 2 A 28 DC DA DG DG DT DA DA DA DA DA DG DG DG
SEQRES 3 A 28 DC DA
SEQRES 1 B 28 DT DG DC DC DC DT DT DT DT DT DA DC DC
SEQRES 2 B 28 DT DG DT DG DC DC DA DC DG DC DC DC DA
SEQRES 3 B 28 DC DA
SEQRES 1 C 314 GLY PRO GLY SER PRO HIS LYS CYS LYS GLU CYS GLY LYS
SEQRES 2 C 314 ALA PHE HIS THR PRO SER GLN LEU SER HIS HIS GLN LYS
SEQRES 3 C 314 LEU HIS VAL GLY GLU LYS PRO TYR LYS CYS GLN GLU CYS
SEQRES 4 C 314 GLY LYS ALA PHE PRO SER ASN ALA GLN LEU SER LEU HIS
SEQRES 5 C 314 HIS ARG VAL HIS THR ASP GLU LYS CYS PHE GLU CYS LYS
SEQRES 6 C 314 GLU CYS GLY LYS ALA PHE MET ARG PRO SER HIS LEU LEU
SEQRES 7 C 314 ARG HIS GLN ARG ILE HIS THR GLY GLU LYS PRO HIS LYS
SEQRES 8 C 314 CYS LYS GLU CYS GLY LYS ALA PHE ARG TYR ASP THR GLN
SEQRES 9 C 314 LEU SER LEU HIS LEU LEU THR HIS ALA GLY ALA ARG ARG
SEQRES 10 C 314 PHE GLU CYS LYS ASP CYS ASP LYS VAL TYR SER CYS ALA
SEQRES 11 C 314 SER GLN LEU ALA LEU HIS GLN MET SER HIS THR GLY GLU
SEQRES 12 C 314 LYS PRO HIS LYS CYS LYS GLU CYS GLY LYS GLY PHE ILE
SEQRES 13 C 314 SER ASP SER HIS LEU LEU ARG HIS GLN SER VAL HIS THR
SEQRES 14 C 314 GLY GLU THR PRO TYR LYS CYS LYS GLU CYS GLY LYS GLY
SEQRES 15 C 314 PHE ARG ARG GLY SER GLU LEU ALA ARG HIS GLN ARG ALA
SEQRES 16 C 314 HIS SER GLY ASP LYS PRO TYR LYS CYS LYS GLU CYS GLY
SEQRES 17 C 314 LYS SER PHE THR CYS THR THR GLU LEU PHE ARG HIS GLN
SEQRES 18 C 314 LYS VAL HIS THR GLY ASP ARG PRO HIS LYS CYS LYS GLU
SEQRES 19 C 314 CYS GLY LYS ALA PHE ILE ARG ARG SER GLU LEU THR HIS
SEQRES 20 C 314 HIS GLU ARG SER HIS SER GLY GLU LYS PRO TYR GLU CYS
SEQRES 21 C 314 LYS GLU CYS GLY LYS THR PHE GLY ARG GLY SER GLU LEU
SEQRES 22 C 314 SER ARG HIS GLN LYS ILE HIS THR GLY GLU LYS PRO TYR
SEQRES 23 C 314 LYS CYS GLN GLN CYS GLY LYS ALA PHE ILE ARG GLY SER
SEQRES 24 C 314 HIS LEU THR GLN HIS GLN ARG ILE HIS THR GLY ARG ARG
SEQRES 25 C 314 LEU GLU
HET ZN C1001 1
HET ZN C1002 1
HET ZN C1003 1
HET ZN C1004 1
HET ZN C1005 1
HET ZN C1006 1
HET ZN C1007 1
HET ZN C1008 1
HET ZN C1009 1
HET ZN C1010 1
HETNAM ZN ZINC ION
FORMUL 4 ZN 10(ZN 2+)
FORMUL 14 HOH *139(H2 O)
HELIX 1 AA1 THR C 374 LYS C 383 1 10
HELIX 2 AA2 LEU C 384 LYS C 389 5 6
HELIX 3 AA3 SER C 402 ASP C 415 1 14
HELIX 4 AA4 ARG C 430 GLN C 438 1 9
HELIX 5 AA5 GLN C 438 GLY C 443 1 6
HELIX 6 AA6 TYR C 458 LEU C 467 1 10
HELIX 7 AA7 CYS C 486 GLY C 499 1 14
HELIX 8 AA8 SER C 514 GLN C 522 1 9
HELIX 9 AA9 GLN C 522 GLY C 527 1 6
HELIX 10 AB1 ARG C 542 GLY C 555 1 14
HELIX 11 AB2 CYS C 570 GLN C 578 1 9
HELIX 12 AB3 ARG C 598 SER C 610 1 13
HELIX 13 AB4 ARG C 626 GLN C 634 1 9
SHEET 1 AA1 2 TYR C 391 LYS C 392 0
SHEET 2 AA1 2 ALA C 399 PHE C 400 -1 O PHE C 400 N TYR C 391
SHEET 1 AA2 2 PHE C 419 GLU C 420 0
SHEET 2 AA2 2 ALA C 427 PHE C 428 -1 O PHE C 428 N PHE C 419
SHEET 1 AA3 2 HIS C 447 LYS C 448 0
SHEET 2 AA3 2 ALA C 455 PHE C 456 -1 O PHE C 456 N HIS C 447
SHEET 1 AA4 2 PHE C 475 GLU C 476 0
SHEET 2 AA4 2 VAL C 483 TYR C 484 -1 O TYR C 484 N PHE C 475
SHEET 1 AA5 2 HIS C 503 LYS C 504 0
SHEET 2 AA5 2 GLY C 511 PHE C 512 -1 O PHE C 512 N HIS C 503
SHEET 1 AA6 2 TYR C 531 LYS C 532 0
SHEET 2 AA6 2 GLY C 539 PHE C 540 -1 O PHE C 540 N TYR C 531
SHEET 1 AA7 2 TYR C 559 LYS C 560 0
SHEET 2 AA7 2 SER C 567 PHE C 568 -1 O PHE C 568 N TYR C 559
SHEET 1 AA8 2 TYR C 615 GLU C 616 0
SHEET 2 AA8 2 THR C 623 PHE C 624 -1 O PHE C 624 N TYR C 615
LINK SG CYS C 365 ZN ZN C1001 1555 1555 2.41
LINK SG CYS C 368 ZN ZN C1001 1555 1555 2.01
LINK NE2 HIS C 381 ZN ZN C1001 1555 1555 2.03
LINK NE2 HIS C 385 ZN ZN C1001 1555 1555 2.04
LINK SG CYS C 393 ZN ZN C1002 1555 1555 2.26
LINK SG CYS C 396 ZN ZN C1002 1555 1555 2.14
LINK NE2 HIS C 409 ZN ZN C1002 1555 1555 2.07
LINK NE2 HIS C 413 ZN ZN C1002 1555 1555 1.99
LINK SG CYS C 421 ZN ZN C1003 1555 1555 2.27
LINK SG CYS C 424 ZN ZN C1003 1555 1555 2.16
LINK NE2 HIS C 437 ZN ZN C1003 1555 1555 2.04
LINK NE2 HIS C 441 ZN ZN C1003 1555 1555 1.93
LINK SG CYS C 449 ZN ZN C1004 1555 1555 2.40
LINK NE2 HIS C 469 ZN ZN C1004 1555 1555 2.28
LINK SG CYS C 477 ZN ZN C1005 1555 1555 2.33
LINK SG CYS C 480 ZN ZN C1005 1555 1555 2.28
LINK NE2 HIS C 493 ZN ZN C1005 1555 1555 2.03
LINK NE2 HIS C 497 ZN ZN C1005 1555 1555 1.94
LINK SG CYS C 505 ZN ZN C1006 1555 1555 2.44
LINK SG CYS C 508 ZN ZN C1006 1555 1555 2.88
LINK NE2 HIS C 521 ZN ZN C1006 1555 1555 2.11
LINK NE2 HIS C 525 ZN ZN C1006 1555 1555 1.98
LINK SG CYS C 533 ZN ZN C1007 1555 1555 2.41
LINK SG CYS C 536 ZN ZN C1007 1555 1555 2.22
LINK NE2 HIS C 549 ZN ZN C1007 1555 1555 2.10
LINK NE2 HIS C 553 ZN ZN C1007 1555 1555 1.91
LINK SG CYS C 561 ZN ZN C1008 1555 1555 2.51
LINK SG CYS C 564 ZN ZN C1008 1555 1555 2.14
LINK NE2 HIS C 577 ZN ZN C1008 1555 1555 1.96
LINK NE2 HIS C 581 ZN ZN C1008 1555 1555 2.12
LINK SG CYS C 589 ZN ZN C1009 1555 1555 2.33
LINK SG CYS C 592 ZN ZN C1009 1555 1555 2.24
LINK NE2 HIS C 605 ZN ZN C1009 1555 1555 2.08
LINK NE2 HIS C 609 ZN ZN C1009 1555 1555 1.96
LINK SG CYS C 617 ZN ZN C1010 1555 1555 2.60
LINK N CYS C 620 ZN ZN C1010 1555 1555 2.53
LINK SG CYS C 620 NE2 HIS C 633 1555 1555 1.72
LINK SG CYS C 620 ZN ZN C1010 1555 1555 2.39
LINK NE2 HIS C 633 ZN ZN C1010 1555 1555 2.58
LINK NE2 HIS C 637 ZN ZN C1010 1555 1555 2.11
SITE 1 AC1 4 CYS C 365 CYS C 368 HIS C 381 HIS C 385
SITE 1 AC2 4 CYS C 393 CYS C 396 HIS C 409 HIS C 413
SITE 1 AC3 4 CYS C 421 CYS C 424 HIS C 437 HIS C 441
SITE 1 AC4 4 CYS C 449 CYS C 452 HIS C 465 HIS C 469
SITE 1 AC5 4 CYS C 477 CYS C 480 HIS C 493 HIS C 497
SITE 1 AC6 4 CYS C 505 CYS C 508 HIS C 521 HIS C 525
SITE 1 AC7 4 CYS C 533 CYS C 536 HIS C 549 HIS C 553
SITE 1 AC8 4 CYS C 561 CYS C 564 HIS C 577 HIS C 581
SITE 1 AC9 4 CYS C 589 CYS C 592 HIS C 605 HIS C 609
SITE 1 AD1 5 CYS C 617 GLU C 619 CYS C 620 HIS C 633
SITE 2 AD1 5 HIS C 637
CRYST1 35.954 92.758 353.667 90.00 90.00 90.00 C 2 2 21 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 0.027813 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010781 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002828 0.00000
(ATOM LINES ARE NOT SHOWN.)
END