HEADER TRANSFERASE 05-JUL-12 4FYV
TITLE ASPARTATE TRANSCARBAMOYLASE COMPLEXED WITH DCTP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ASPARTATE CARBAMOYLTRANSFERASE CATALYTIC CHAIN;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: ASPARTATE TRANSCARBAMYLASE, ATCASE;
COMPND 5 EC: 2.1.3.2;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: ASPARTATE CARBAMOYLTRANSFERASE REGULATORY CHAIN;
COMPND 8 CHAIN: B, D
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 7 ORGANISM_TAXID: 83333;
SOURCE 8 STRAIN: K12
KEYWDS ALLOSTERIC REGULATION, ASPARTATE CARBAMOYLTRANSFERASE, ESCHERICHIA
KEYWDS 2 COLI, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.M.COCKRELL,E.R.KANTROWITZ
REVDAT 3 28-FEB-24 4FYV 1 REMARK LINK
REVDAT 2 15-NOV-17 4FYV 1 REMARK
REVDAT 1 10-OCT-12 4FYV 0
JRNL AUTH G.M.COCKRELL,E.R.KANTROWITZ
JRNL TITL METAL ION INVOLVEMENT IN THE ALLOSTERIC MECHANISM OF
JRNL TITL 2 ESCHERICHIA COLI ASPARTATE TRANSCARBAMOYLASE.
JRNL REF BIOCHEMISTRY V. 51 7128 2012
JRNL REFN ISSN 0006-2960
JRNL PMID 22906065
JRNL DOI 10.1021/BI300920M
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.06
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 70565
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 3564
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 49.0756 - 6.1295 1.00 2902 136 0.1674 0.1671
REMARK 3 2 6.1295 - 4.8666 1.00 2764 135 0.1668 0.1911
REMARK 3 3 4.8666 - 4.2518 1.00 2720 167 0.1417 0.1716
REMARK 3 4 4.2518 - 3.8632 1.00 2717 139 0.1478 0.1950
REMARK 3 5 3.8632 - 3.5864 1.00 2715 130 0.1699 0.2114
REMARK 3 6 3.5864 - 3.3750 1.00 2679 153 0.1759 0.2049
REMARK 3 7 3.3750 - 3.2060 1.00 2708 141 0.1867 0.2395
REMARK 3 8 3.2060 - 3.0665 1.00 2662 141 0.1914 0.2313
REMARK 3 9 3.0665 - 2.9485 1.00 2654 159 0.1885 0.2488
REMARK 3 10 2.9485 - 2.8467 1.00 2702 140 0.1974 0.2693
REMARK 3 11 2.8467 - 2.7577 1.00 2653 148 0.1950 0.2572
REMARK 3 12 2.7577 - 2.6789 1.00 2683 134 0.1879 0.2394
REMARK 3 13 2.6789 - 2.6084 1.00 2672 145 0.1865 0.2499
REMARK 3 14 2.6084 - 2.5447 1.00 2668 134 0.1882 0.2087
REMARK 3 15 2.5447 - 2.4869 1.00 2685 133 0.1785 0.2473
REMARK 3 16 2.4869 - 2.4340 1.00 2635 150 0.1881 0.2552
REMARK 3 17 2.4340 - 2.3853 1.00 2681 143 0.1890 0.2376
REMARK 3 18 2.3853 - 2.3403 1.00 2643 138 0.1919 0.2394
REMARK 3 19 2.3403 - 2.2985 1.00 2657 132 0.1977 0.2447
REMARK 3 20 2.2985 - 2.2595 1.00 2667 144 0.1933 0.2592
REMARK 3 21 2.2595 - 2.2231 1.00 2630 132 0.1945 0.2354
REMARK 3 22 2.2231 - 2.1889 1.00 2684 152 0.1949 0.2499
REMARK 3 23 2.1889 - 2.1567 1.00 2622 157 0.2053 0.2756
REMARK 3 24 2.1567 - 2.1263 1.00 2648 146 0.2129 0.2907
REMARK 3 25 2.1263 - 2.0976 0.96 2550 135 0.2158 0.2451
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.30
REMARK 3 SHRINKAGE RADIUS : 1.10
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.460
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.72
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 7270
REMARK 3 ANGLE : 1.122 9870
REMARK 3 CHIRALITY : 0.076 1144
REMARK 3 PLANARITY : 0.005 1274
REMARK 3 DIHEDRAL : 15.069 2710
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 22
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 1:66)
REMARK 3 ORIGIN FOR THE GROUP (A): 43.0142 36.2077 2.8460
REMARK 3 T TENSOR
REMARK 3 T11: 0.3251 T22: 0.4207
REMARK 3 T33: 0.2742 T12: 0.0252
REMARK 3 T13: -0.0409 T23: 0.0244
REMARK 3 L TENSOR
REMARK 3 L11: 0.2083 L22: 0.2045
REMARK 3 L33: 0.1552 L12: 0.0909
REMARK 3 L13: -0.1535 L23: 0.1061
REMARK 3 S TENSOR
REMARK 3 S11: -0.0615 S12: 0.1993 S13: -0.0413
REMARK 3 S21: -0.1728 S22: 0.1437 S23: 0.0921
REMARK 3 S31: -0.0986 S32: -0.1349 S33: 0.0005
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 67:87)
REMARK 3 ORIGIN FOR THE GROUP (A): 54.5015 43.2931 19.4348
REMARK 3 T TENSOR
REMARK 3 T11: 0.3750 T22: 0.3824
REMARK 3 T33: 0.2408 T12: 0.0617
REMARK 3 T13: -0.0518 T23: 0.0810
REMARK 3 L TENSOR
REMARK 3 L11: 0.2204 L22: 0.0748
REMARK 3 L33: 0.0049 L12: 0.1302
REMARK 3 L13: -0.0134 L23: -0.0129
REMARK 3 S TENSOR
REMARK 3 S11: -0.1162 S12: -0.0132 S13: -0.2181
REMARK 3 S21: 0.0722 S22: 0.0804 S23: -0.1938
REMARK 3 S31: -0.3600 S32: -0.0987 S33: -0.0039
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 88:187)
REMARK 3 ORIGIN FOR THE GROUP (A): 35.4717 36.0137 12.5245
REMARK 3 T TENSOR
REMARK 3 T11: 0.2686 T22: 0.4383
REMARK 3 T33: 0.2473 T12: 0.0089
REMARK 3 T13: -0.0347 T23: 0.0121
REMARK 3 L TENSOR
REMARK 3 L11: 0.3216 L22: 0.0502
REMARK 3 L33: 0.1591 L12: 0.0964
REMARK 3 L13: -0.0208 L23: 0.0290
REMARK 3 S TENSOR
REMARK 3 S11: 0.0145 S12: 0.1170 S13: 0.1049
REMARK 3 S21: 0.0082 S22: 0.0417 S23: 0.0872
REMARK 3 S31: -0.1158 S32: -0.2945 S33: 0.0003
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 188:236)
REMARK 3 ORIGIN FOR THE GROUP (A): 25.0448 25.5641 22.2165
REMARK 3 T TENSOR
REMARK 3 T11: 0.3445 T22: 0.5481
REMARK 3 T33: 0.3779 T12: 0.0116
REMARK 3 T13: -0.0088 T23: 0.0176
REMARK 3 L TENSOR
REMARK 3 L11: 0.0868 L22: 0.3129
REMARK 3 L33: 0.1406 L12: -0.0246
REMARK 3 L13: -0.0563 L23: -0.0328
REMARK 3 S TENSOR
REMARK 3 S11: -0.1770 S12: -0.2245 S13: -0.0951
REMARK 3 S21: 0.3516 S22: 0.2799 S23: 0.2776
REMARK 3 S31: 0.0382 S32: -0.4388 S33: -0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 237:265)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.8585 14.4080 22.4179
REMARK 3 T TENSOR
REMARK 3 T11: 0.4623 T22: 0.3618
REMARK 3 T33: 0.4638 T12: -0.1715
REMARK 3 T13: 0.0422 T23: -0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 0.4569 L22: 0.7816
REMARK 3 L33: 0.2390 L12: -0.5672
REMARK 3 L13: 0.0920 L23: -0.2373
REMARK 3 S TENSOR
REMARK 3 S11: -0.3702 S12: -0.1355 S13: -0.3146
REMARK 3 S21: 0.2345 S22: 0.2078 S23: 0.0694
REMARK 3 S31: 0.1333 S32: -0.3371 S33: -0.1220
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 266:310)
REMARK 3 ORIGIN FOR THE GROUP (A): 40.2187 24.2335 7.4632
REMARK 3 T TENSOR
REMARK 3 T11: 0.3695 T22: 0.3822
REMARK 3 T33: 0.2653 T12: -0.0516
REMARK 3 T13: -0.0541 T23: -0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 0.4337 L22: 0.2162
REMARK 3 L33: 0.1462 L12: -0.1754
REMARK 3 L13: -0.2485 L23: 0.1947
REMARK 3 S TENSOR
REMARK 3 S11: -0.1659 S12: 0.2401 S13: -0.0573
REMARK 3 S21: -0.1663 S22: 0.0676 S23: -0.0803
REMARK 3 S31: 0.1473 S32: -0.2228 S33: -0.0003
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 10:25)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.7581 78.3023 28.2748
REMARK 3 T TENSOR
REMARK 3 T11: 1.0283 T22: 0.7281
REMARK 3 T33: 0.7996 T12: 0.8543
REMARK 3 T13: -0.4160 T23: -0.5067
REMARK 3 L TENSOR
REMARK 3 L11: 0.0976 L22: 0.0213
REMARK 3 L33: 0.0989 L12: 0.0060
REMARK 3 L13: -0.0503 L23: -0.0485
REMARK 3 S TENSOR
REMARK 3 S11: 0.1580 S12: 0.1708 S13: 0.0912
REMARK 3 S21: -0.3530 S22: -0.2130 S23: 0.2132
REMARK 3 S31: -0.3107 S32: -0.1623 S33: -0.1227
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 26:32)
REMARK 3 ORIGIN FOR THE GROUP (A): 27.4494 69.3552 32.2569
REMARK 3 T TENSOR
REMARK 3 T11: 0.7789 T22: 0.6063
REMARK 3 T33: 0.5808 T12: 0.9487
REMARK 3 T13: -0.2407 T23: -0.4628
REMARK 3 L TENSOR
REMARK 3 L11: 0.0139 L22: 0.0755
REMARK 3 L33: 0.0740 L12: 0.0096
REMARK 3 L13: -0.0294 L23: 0.0189
REMARK 3 S TENSOR
REMARK 3 S11: -0.0362 S12: -0.0689 S13: 0.0060
REMARK 3 S21: -0.0761 S22: -0.0442 S23: -0.0114
REMARK 3 S31: -0.0693 S32: -0.0602 S33: -0.0539
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 33:42)
REMARK 3 ORIGIN FOR THE GROUP (A): 31.1332 78.2855 25.6164
REMARK 3 T TENSOR
REMARK 3 T11: 1.4333 T22: 0.6350
REMARK 3 T33: 0.6383 T12: 0.6672
REMARK 3 T13: -0.3339 T23: 0.0213
REMARK 3 L TENSOR
REMARK 3 L11: 0.1176 L22: 0.0848
REMARK 3 L33: 0.1229 L12: -0.0352
REMARK 3 L13: -0.0699 L23: 0.1001
REMARK 3 S TENSOR
REMARK 3 S11: -0.0039 S12: 0.1261 S13: 0.1575
REMARK 3 S21: -0.0745 S22: 0.0036 S23: -0.0072
REMARK 3 S31: -0.3042 S32: 0.0376 S33: 0.0742
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 43:62)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.1411 76.7262 35.1916
REMARK 3 T TENSOR
REMARK 3 T11: 0.9814 T22: 1.0660
REMARK 3 T33: 1.0358 T12: 0.9400
REMARK 3 T13: -0.2790 T23: -0.5659
REMARK 3 L TENSOR
REMARK 3 L11: 0.0059 L22: 0.0351
REMARK 3 L33: 0.0192 L12: -0.0199
REMARK 3 L13: 0.0068 L23: -0.0143
REMARK 3 S TENSOR
REMARK 3 S11: -0.0976 S12: -0.0674 S13: 0.0839
REMARK 3 S21: -0.1891 S22: -0.0279 S23: -0.0694
REMARK 3 S31: -0.0348 S32: -0.1289 S33: -0.0907
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 63:101)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.2060 72.5104 20.6010
REMARK 3 T TENSOR
REMARK 3 T11: 1.1321 T22: 0.9045
REMARK 3 T33: 1.0034 T12: 0.9462
REMARK 3 T13: -0.6066 T23: -0.4316
REMARK 3 L TENSOR
REMARK 3 L11: 0.3519 L22: 0.1617
REMARK 3 L33: 0.0209 L12: -0.1373
REMARK 3 L13: -0.0540 L23: -0.0460
REMARK 3 S TENSOR
REMARK 3 S11: -0.1216 S12: 0.2885 S13: -0.2678
REMARK 3 S21: -0.2572 S22: 0.0041 S23: 0.1249
REMARK 3 S31: -0.3116 S32: -0.2343 S33: 0.0140
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 102:129)
REMARK 3 ORIGIN FOR THE GROUP (A): 32.7121 53.7452 23.4863
REMARK 3 T TENSOR
REMARK 3 T11: 0.3350 T22: 0.3782
REMARK 3 T33: 0.2881 T12: 0.1536
REMARK 3 T13: -0.0445 T23: -0.1167
REMARK 3 L TENSOR
REMARK 3 L11: 0.5286 L22: 0.8138
REMARK 3 L33: 0.3343 L12: 0.4126
REMARK 3 L13: -0.2958 L23: -0.4736
REMARK 3 S TENSOR
REMARK 3 S11: 0.1077 S12: -0.0818 S13: -0.0545
REMARK 3 S21: -0.2450 S22: -0.3538 S23: 0.1604
REMARK 3 S31: -0.3024 S32: -0.2648 S33: -0.1360
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 130:153)
REMARK 3 ORIGIN FOR THE GROUP (A): 25.5340 49.5740 26.5364
REMARK 3 T TENSOR
REMARK 3 T11: 0.2320 T22: 0.5580
REMARK 3 T33: 0.6466 T12: 0.0458
REMARK 3 T13: -0.0037 T23: -0.2650
REMARK 3 L TENSOR
REMARK 3 L11: 0.1923 L22: 0.1280
REMARK 3 L33: 0.0003 L12: -0.1584
REMARK 3 L13: -0.0199 L23: -0.0231
REMARK 3 S TENSOR
REMARK 3 S11: 0.1700 S12: -0.3055 S13: 0.2916
REMARK 3 S21: -0.0441 S22: -0.4254 S23: 0.7297
REMARK 3 S31: 0.0374 S32: -0.3561 S33: -0.1812
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 1:66)
REMARK 3 ORIGIN FOR THE GROUP (A): 63.1546 52.0084 67.2396
REMARK 3 T TENSOR
REMARK 3 T11: 0.2858 T22: 0.2433
REMARK 3 T33: 0.2698 T12: -0.0176
REMARK 3 T13: 0.0146 T23: -0.0297
REMARK 3 L TENSOR
REMARK 3 L11: 0.4401 L22: 0.2980
REMARK 3 L33: 0.3705 L12: 0.1676
REMARK 3 L13: 0.3457 L23: -0.1663
REMARK 3 S TENSOR
REMARK 3 S11: 0.1308 S12: -0.1505 S13: 0.0934
REMARK 3 S21: 0.1130 S22: -0.0193 S23: -0.0168
REMARK 3 S31: -0.1190 S32: -0.0267 S33: -0.0000
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 67:134)
REMARK 3 ORIGIN FOR THE GROUP (A): 52.7328 49.4615 55.5340
REMARK 3 T TENSOR
REMARK 3 T11: 0.2623 T22: 0.2388
REMARK 3 T33: 0.3019 T12: -0.0094
REMARK 3 T13: -0.0134 T23: -0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 0.2462 L22: 0.1857
REMARK 3 L33: 0.0562 L12: 0.0187
REMARK 3 L13: -0.0519 L23: -0.0381
REMARK 3 S TENSOR
REMARK 3 S11: -0.0411 S12: 0.0015 S13: -0.0131
REMARK 3 S21: 0.0315 S22: 0.0420 S23: 0.0399
REMARK 3 S31: -0.0039 S32: -0.0889 S33: 0.0000
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 135:217)
REMARK 3 ORIGIN FOR THE GROUP (A): 75.8735 67.2375 54.6561
REMARK 3 T TENSOR
REMARK 3 T11: 0.3178 T22: 0.2488
REMARK 3 T33: 0.3253 T12: -0.0386
REMARK 3 T13: -0.0520 T23: 0.0319
REMARK 3 L TENSOR
REMARK 3 L11: 0.4725 L22: 0.3797
REMARK 3 L33: 0.2921 L12: -0.1746
REMARK 3 L13: -0.2811 L23: -0.0022
REMARK 3 S TENSOR
REMARK 3 S11: 0.0598 S12: 0.0948 S13: 0.2471
REMARK 3 S21: -0.1799 S22: -0.0710 S23: 0.0277
REMARK 3 S31: -0.2105 S32: -0.0238 S33: -0.0000
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 218:242)
REMARK 3 ORIGIN FOR THE GROUP (A): 80.2758 58.9031 44.6016
REMARK 3 T TENSOR
REMARK 3 T11: 0.3634 T22: 0.2798
REMARK 3 T33: 0.3095 T12: 0.0108
REMARK 3 T13: 0.0172 T23: -0.0001
REMARK 3 L TENSOR
REMARK 3 L11: 0.0734 L22: 0.1063
REMARK 3 L33: 0.1111 L12: -0.0458
REMARK 3 L13: -0.0792 L23: -0.1002
REMARK 3 S TENSOR
REMARK 3 S11: 0.2006 S12: -0.0091 S13: 0.0578
REMARK 3 S21: -0.3612 S22: -0.1690 S23: -0.2828
REMARK 3 S31: 0.0014 S32: -0.0178 S33: -0.0012
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 243:310)
REMARK 3 ORIGIN FOR THE GROUP (A): 80.0372 54.1796 59.0980
REMARK 3 T TENSOR
REMARK 3 T11: 0.2235 T22: 0.2341
REMARK 3 T33: 0.2834 T12: -0.0264
REMARK 3 T13: -0.0014 T23: -0.0171
REMARK 3 L TENSOR
REMARK 3 L11: 0.2380 L22: 0.7804
REMARK 3 L33: 0.1826 L12: -0.1830
REMARK 3 L13: 0.1344 L23: -0.1768
REMARK 3 S TENSOR
REMARK 3 S11: -0.0312 S12: -0.0281 S13: -0.0524
REMARK 3 S21: 0.0265 S22: -0.1356 S23: -0.2045
REMARK 3 S31: 0.0033 S32: 0.0618 S33: 0.0000
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 10:32)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.4607 82.8826 40.6546
REMARK 3 T TENSOR
REMARK 3 T11: 1.2087 T22: 0.1872
REMARK 3 T33: 0.4208 T12: 0.7728
REMARK 3 T13: -0.1422 T23: -0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 0.0282 L22: 0.3523
REMARK 3 L33: 0.2823 L12: -0.1002
REMARK 3 L13: 0.0274 L23: 0.0652
REMARK 3 S TENSOR
REMARK 3 S11: -0.2695 S12: -0.3026 S13: 0.3021
REMARK 3 S21: -0.3921 S22: 0.0195 S23: 0.1684
REMARK 3 S31: -0.4529 S32: -0.5310 S33: -0.1889
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 33:67)
REMARK 3 ORIGIN FOR THE GROUP (A): 28.3646 82.3875 40.7523
REMARK 3 T TENSOR
REMARK 3 T11: 1.0125 T22: 0.4134
REMARK 3 T33: 0.5836 T12: 0.3776
REMARK 3 T13: -0.1395 T23: -0.1434
REMARK 3 L TENSOR
REMARK 3 L11: 1.3265 L22: 0.0537
REMARK 3 L33: 0.3339 L12: 0.1955
REMARK 3 L13: 0.6823 L23: 0.1014
REMARK 3 S TENSOR
REMARK 3 S11: 0.1010 S12: -0.5593 S13: 0.1773
REMARK 3 S21: -0.2636 S22: -0.1414 S23: 0.1943
REMARK 3 S31: -0.4416 S32: -0.5396 S33: -0.1093
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 68:101)
REMARK 3 ORIGIN FOR THE GROUP (A): 35.4976 85.9711 49.1733
REMARK 3 T TENSOR
REMARK 3 T11: 0.8932 T22: 0.4767
REMARK 3 T33: 0.6948 T12: 0.2992
REMARK 3 T13: -0.1365 T23: -0.1582
REMARK 3 L TENSOR
REMARK 3 L11: 0.0341 L22: 0.8712
REMARK 3 L33: 0.3956 L12: -0.0775
REMARK 3 L13: 0.0372 L23: -0.2702
REMARK 3 S TENSOR
REMARK 3 S11: -0.3481 S12: -0.3498 S13: 0.2352
REMARK 3 S21: -0.2255 S22: -0.2732 S23: -0.2008
REMARK 3 S31: -0.4619 S32: -0.5366 S33: -0.3979
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 102:153)
REMARK 3 ORIGIN FOR THE GROUP (A): 51.3286 69.2825 45.4841
REMARK 3 T TENSOR
REMARK 3 T11: 0.3555 T22: 0.2790
REMARK 3 T33: 0.4174 T12: 0.0367
REMARK 3 T13: 0.0086 T23: 0.0885
REMARK 3 L TENSOR
REMARK 3 L11: 0.1731 L22: 0.1542
REMARK 3 L33: 0.1736 L12: -0.1588
REMARK 3 L13: -0.0514 L23: 0.0118
REMARK 3 S TENSOR
REMARK 3 S11: 0.1610 S12: 0.3504 S13: 0.1914
REMARK 3 S21: -0.1638 S22: -0.0476 S23: 0.0320
REMARK 3 S31: -0.0782 S32: -0.0448 S33: 0.0001
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 4FYV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUL-12.
REMARK 100 THE DEPOSITION ID IS D_1000073524.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JAN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.075
REMARK 200 MONOCHROMATOR : ROSENBAUM-ROCK DOUBLE CRYSTAL
REMARK 200 SAGITTAL FOCUSING MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70569
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.098
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 23.10
REMARK 200 R MERGE (I) : 0.10700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 21.10
REMARK 200 R MERGE FOR SHELL (I) : 0.56200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
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 (%): 57.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 40 MM SODIUM CITRATE, 1 MM 2
REMARK 280 -MERCAPTOETHANOL, 0.2 MM EDTA, 1.0 MM DCTP, PH 5.7,
REMARK 280 MICRODIALYSIS, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-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 -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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 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: DODECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 30540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 106730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -92.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -0.500000 -0.866025 0.000000 120.68000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 60.34000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 104.51195
REMARK 350 BIOMT3 3 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 A 597 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C 559 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C 606 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 MET B 1
REMARK 465 THR B 2
REMARK 465 HIS B 3
REMARK 465 ASP B 4
REMARK 465 ASN B 5
REMARK 465 LYS B 6
REMARK 465 LEU B 7
REMARK 465 GLN B 8
REMARK 465 VAL B 9
REMARK 465 MET D 1
REMARK 465 THR D 2
REMARK 465 HIS D 3
REMARK 465 ASP D 4
REMARK 465 ASN D 5
REMARK 465 LYS D 6
REMARK 465 LEU D 7
REMARK 465 GLN D 8
REMARK 465 VAL D 9
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 O HOH C 557 O HOH C 603 2.04
REMARK 500 OE1 GLN D 24 O HOH D 369 2.08
REMARK 500 ND2 ASN D 47 O HOH D 369 2.08
REMARK 500 OE1 GLU B 62 O HOH B 346 2.09
REMARK 500 O HOH A 541 O HOH A 645 2.10
REMARK 500 OH TYR C 98 O HOH C 599 2.11
REMARK 500 OD2 ASP A 153 O HOH A 634 2.11
REMARK 500 O THR B 38 O HOH D 369 2.14
REMARK 500 O HOH A 599 O HOH A 630 2.14
REMARK 500 O LYS D 56 O HOH D 337 2.16
REMARK 500 O2 PO4 A 401 O HOH A 646 2.16
REMARK 500 O HOH B 330 O HOH B 348 2.16
REMARK 500 OE2 GLU A 204 O HOH A 622 2.17
REMARK 500 O HOH C 517 O HOH C 526 2.18
REMARK 500 O ASN C 121 O HOH C 528 2.18
REMARK 500 OE2 GLU B 144 O HOH B 330 2.19
REMARK 500 O HOH A 610 O HOH A 617 2.19
REMARK 500 O LYS B 60 O HOH B 346 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH C 514 O HOH C 522 3665 2.15
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 52 91.00 -161.57
REMARK 500 ASP A 75 -111.71 -92.30
REMARK 500 SER A 76 -15.25 68.50
REMARK 500 THR A 79 -66.75 -137.99
REMARK 500 SER A 80 0.88 -151.70
REMARK 500 LYS A 83 -98.51 49.12
REMARK 500 ASN A 132 -90.93 -91.28
REMARK 500 HIS A 134 62.14 -158.88
REMARK 500 GLN A 231 81.77 -55.74
REMARK 500 LEU A 267 152.25 72.25
REMARK 500 VAL A 270 -35.90 -38.06
REMARK 500 GLU B 37 38.68 -95.34
REMARK 500 SER B 50 -48.51 -138.62
REMARK 500 ARG B 55 -136.73 62.08
REMARK 500 ALA B 81 -169.15 -71.19
REMARK 500 THR B 82 117.29 -160.48
REMARK 500 ASN B 88 -66.69 -126.57
REMARK 500 TYR B 89 -41.52 -138.00
REMARK 500 VAL B 91 171.80 -57.53
REMARK 500 VAL B 92 -60.78 -127.73
REMARK 500 ASN B 105 -39.35 74.03
REMARK 500 ASN B 132 -10.54 78.08
REMARK 500 SER C 76 -106.05 -89.15
REMARK 500 ASN C 78 -155.04 -134.18
REMARK 500 THR C 79 150.60 157.51
REMARK 500 SER C 80 -151.78 -84.17
REMARK 500 ASN C 132 -88.92 -89.84
REMARK 500 HIS C 134 65.85 -153.97
REMARK 500 GLN C 231 69.65 -68.40
REMARK 500 LEU C 267 154.61 72.71
REMARK 500 ASP C 271 -5.82 73.08
REMARK 500 TRP C 284 20.64 -140.92
REMARK 500 ALA D 11 172.66 -59.11
REMARK 500 PRO D 49 98.78 -39.74
REMARK 500 GLU D 52 27.47 -76.47
REMARK 500 MET D 53 -175.69 -172.02
REMARK 500 ALA D 78 61.30 -160.49
REMARK 500 TYR D 89 -5.74 68.62
REMARK 500 ASN D 105 -45.37 77.34
REMARK 500 ASN D 132 -9.25 92.14
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 ZN B 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 109 SG
REMARK 620 2 CYS B 114 SG 116.8
REMARK 620 3 CYS B 138 SG 112.1 106.1
REMARK 620 4 CYS B 141 SG 101.5 114.4 105.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 109 SG
REMARK 620 2 CYS D 114 SG 116.1
REMARK 620 3 CYS D 138 SG 112.0 107.6
REMARK 620 4 CYS D 141 SG 101.8 113.1 105.9
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DCP B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DCP D 202
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4FYW RELATED DB: PDB
REMARK 900 ATCASE COMPLEXED WITH CTP
REMARK 900 RELATED ID: 4FYX RELATED DB: PDB
REMARK 900 ATCASE COMPLEXED WITH DCTP, UTP, AND MG2+
REMARK 900 RELATED ID: 4FYY RELATED DB: PDB
REMARK 900 ATCASE COMPLEXED WITH CTP, UTP, AND MG2+
DBREF 4FYV A 1 310 UNP P0A786 PYRB_ECOLI 2 311
DBREF 4FYV B 1 153 UNP P0A7F3 PYRI_ECOLI 1 153
DBREF 4FYV C 1 310 UNP P0A786 PYRB_ECOLI 2 311
DBREF 4FYV D 1 153 UNP P0A7F3 PYRI_ECOLI 1 153
SEQRES 1 A 310 ALA ASN PRO LEU TYR GLN LYS HIS ILE ILE SER ILE ASN
SEQRES 2 A 310 ASP LEU SER ARG ASP ASP LEU ASN LEU VAL LEU ALA THR
SEQRES 3 A 310 ALA ALA LYS LEU LYS ALA ASN PRO GLN PRO GLU LEU LEU
SEQRES 4 A 310 LYS HIS LYS VAL ILE ALA SER CYS PHE PHE GLU ALA SER
SEQRES 5 A 310 THR ARG THR ARG LEU SER PHE GLU THR SER MET HIS ARG
SEQRES 6 A 310 LEU GLY ALA SER VAL VAL GLY PHE SER ASP SER ALA ASN
SEQRES 7 A 310 THR SER LEU GLY LYS LYS GLY GLU THR LEU ALA ASP THR
SEQRES 8 A 310 ILE SER VAL ILE SER THR TYR VAL ASP ALA ILE VAL MET
SEQRES 9 A 310 ARG HIS PRO GLN GLU GLY ALA ALA ARG LEU ALA THR GLU
SEQRES 10 A 310 PHE SER GLY ASN VAL PRO VAL LEU ASN ALA GLY ASP GLY
SEQRES 11 A 310 SER ASN GLN HIS PRO THR GLN THR LEU LEU ASP LEU PHE
SEQRES 12 A 310 THR ILE GLN GLU THR GLN GLY ARG LEU ASP ASN LEU HIS
SEQRES 13 A 310 VAL ALA MET VAL GLY ASP LEU LYS TYR GLY ARG THR VAL
SEQRES 14 A 310 HIS SER LEU THR GLN ALA LEU ALA LYS PHE ASP GLY ASN
SEQRES 15 A 310 ARG PHE TYR PHE ILE ALA PRO ASP ALA LEU ALA MET PRO
SEQRES 16 A 310 GLN TYR ILE LEU ASP MET LEU ASP GLU LYS GLY ILE ALA
SEQRES 17 A 310 TRP SER LEU HIS SER SER ILE GLU GLU VAL MET ALA GLU
SEQRES 18 A 310 VAL ASP ILE LEU TYR MET THR ARG VAL GLN LYS GLU ARG
SEQRES 19 A 310 LEU ASP PRO SER GLU TYR ALA ASN VAL LYS ALA GLN PHE
SEQRES 20 A 310 VAL LEU ARG ALA SER ASP LEU HIS ASN ALA LYS ALA ASN
SEQRES 21 A 310 MET LYS VAL LEU HIS PRO LEU PRO ARG VAL ASP GLU ILE
SEQRES 22 A 310 ALA THR ASP VAL ASP LYS THR PRO HIS ALA TRP TYR PHE
SEQRES 23 A 310 GLN GLN ALA GLY ASN GLY ILE PHE ALA ARG GLN ALA LEU
SEQRES 24 A 310 LEU ALA LEU VAL LEU ASN ARG ASP LEU VAL LEU
SEQRES 1 B 153 MET THR HIS ASP ASN LYS LEU GLN VAL GLU ALA ILE LYS
SEQRES 2 B 153 ARG GLY THR VAL ILE ASP HIS ILE PRO ALA GLN ILE GLY
SEQRES 3 B 153 PHE LYS LEU LEU SER LEU PHE LYS LEU THR GLU THR ASP
SEQRES 4 B 153 GLN ARG ILE THR ILE GLY LEU ASN LEU PRO SER GLY GLU
SEQRES 5 B 153 MET GLY ARG LYS ASP LEU ILE LYS ILE GLU ASN THR PHE
SEQRES 6 B 153 LEU SER GLU ASP GLN VAL ASP GLN LEU ALA LEU TYR ALA
SEQRES 7 B 153 PRO GLN ALA THR VAL ASN ARG ILE ASP ASN TYR GLU VAL
SEQRES 8 B 153 VAL GLY LYS SER ARG PRO SER LEU PRO GLU ARG ILE ASP
SEQRES 9 B 153 ASN VAL LEU VAL CYS PRO ASN SER ASN CYS ILE SER HIS
SEQRES 10 B 153 ALA GLU PRO VAL SER SER SER PHE ALA VAL ARG LYS ARG
SEQRES 11 B 153 ALA ASN ASP ILE ALA LEU LYS CYS LYS TYR CYS GLU LYS
SEQRES 12 B 153 GLU PHE SER HIS ASN VAL VAL LEU ALA ASN
SEQRES 1 C 310 ALA ASN PRO LEU TYR GLN LYS HIS ILE ILE SER ILE ASN
SEQRES 2 C 310 ASP LEU SER ARG ASP ASP LEU ASN LEU VAL LEU ALA THR
SEQRES 3 C 310 ALA ALA LYS LEU LYS ALA ASN PRO GLN PRO GLU LEU LEU
SEQRES 4 C 310 LYS HIS LYS VAL ILE ALA SER CYS PHE PHE GLU ALA SER
SEQRES 5 C 310 THR ARG THR ARG LEU SER PHE GLU THR SER MET HIS ARG
SEQRES 6 C 310 LEU GLY ALA SER VAL VAL GLY PHE SER ASP SER ALA ASN
SEQRES 7 C 310 THR SER LEU GLY LYS LYS GLY GLU THR LEU ALA ASP THR
SEQRES 8 C 310 ILE SER VAL ILE SER THR TYR VAL ASP ALA ILE VAL MET
SEQRES 9 C 310 ARG HIS PRO GLN GLU GLY ALA ALA ARG LEU ALA THR GLU
SEQRES 10 C 310 PHE SER GLY ASN VAL PRO VAL LEU ASN ALA GLY ASP GLY
SEQRES 11 C 310 SER ASN GLN HIS PRO THR GLN THR LEU LEU ASP LEU PHE
SEQRES 12 C 310 THR ILE GLN GLU THR GLN GLY ARG LEU ASP ASN LEU HIS
SEQRES 13 C 310 VAL ALA MET VAL GLY ASP LEU LYS TYR GLY ARG THR VAL
SEQRES 14 C 310 HIS SER LEU THR GLN ALA LEU ALA LYS PHE ASP GLY ASN
SEQRES 15 C 310 ARG PHE TYR PHE ILE ALA PRO ASP ALA LEU ALA MET PRO
SEQRES 16 C 310 GLN TYR ILE LEU ASP MET LEU ASP GLU LYS GLY ILE ALA
SEQRES 17 C 310 TRP SER LEU HIS SER SER ILE GLU GLU VAL MET ALA GLU
SEQRES 18 C 310 VAL ASP ILE LEU TYR MET THR ARG VAL GLN LYS GLU ARG
SEQRES 19 C 310 LEU ASP PRO SER GLU TYR ALA ASN VAL LYS ALA GLN PHE
SEQRES 20 C 310 VAL LEU ARG ALA SER ASP LEU HIS ASN ALA LYS ALA ASN
SEQRES 21 C 310 MET LYS VAL LEU HIS PRO LEU PRO ARG VAL ASP GLU ILE
SEQRES 22 C 310 ALA THR ASP VAL ASP LYS THR PRO HIS ALA TRP TYR PHE
SEQRES 23 C 310 GLN GLN ALA GLY ASN GLY ILE PHE ALA ARG GLN ALA LEU
SEQRES 24 C 310 LEU ALA LEU VAL LEU ASN ARG ASP LEU VAL LEU
SEQRES 1 D 153 MET THR HIS ASP ASN LYS LEU GLN VAL GLU ALA ILE LYS
SEQRES 2 D 153 ARG GLY THR VAL ILE ASP HIS ILE PRO ALA GLN ILE GLY
SEQRES 3 D 153 PHE LYS LEU LEU SER LEU PHE LYS LEU THR GLU THR ASP
SEQRES 4 D 153 GLN ARG ILE THR ILE GLY LEU ASN LEU PRO SER GLY GLU
SEQRES 5 D 153 MET GLY ARG LYS ASP LEU ILE LYS ILE GLU ASN THR PHE
SEQRES 6 D 153 LEU SER GLU ASP GLN VAL ASP GLN LEU ALA LEU TYR ALA
SEQRES 7 D 153 PRO GLN ALA THR VAL ASN ARG ILE ASP ASN TYR GLU VAL
SEQRES 8 D 153 VAL GLY LYS SER ARG PRO SER LEU PRO GLU ARG ILE ASP
SEQRES 9 D 153 ASN VAL LEU VAL CYS PRO ASN SER ASN CYS ILE SER HIS
SEQRES 10 D 153 ALA GLU PRO VAL SER SER SER PHE ALA VAL ARG LYS ARG
SEQRES 11 D 153 ALA ASN ASP ILE ALA LEU LYS CYS LYS TYR CYS GLU LYS
SEQRES 12 D 153 GLU PHE SER HIS ASN VAL VAL LEU ALA ASN
HET PO4 A 401 5
HET ZN B 201 1
HET DCP B 202 28
HET ZN D 201 1
HET DCP D 202 28
HETNAM PO4 PHOSPHATE ION
HETNAM ZN ZINC ION
HETNAM DCP 2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE
FORMUL 5 PO4 O4 P 3-
FORMUL 6 ZN 2(ZN 2+)
FORMUL 7 DCP 2(C9 H16 N3 O13 P3)
FORMUL 10 HOH *496(H2 O)
HELIX 1 1 SER A 11 LEU A 15 5 5
HELIX 2 2 SER A 16 ASN A 33 1 18
HELIX 3 3 SER A 52 LEU A 66 1 15
HELIX 4 4 THR A 87 SER A 96 1 10
HELIX 5 5 GLY A 110 GLU A 117 1 8
HELIX 6 6 HIS A 134 GLY A 150 1 17
HELIX 7 7 GLY A 166 ALA A 177 1 12
HELIX 8 8 PRO A 189 ALA A 193 5 5
HELIX 9 9 PRO A 195 LYS A 205 1 11
HELIX 10 10 SER A 214 VAL A 218 5 5
HELIX 11 11 ASP A 236 LYS A 244 1 9
HELIX 12 12 ALA A 245 VAL A 248 5 4
HELIX 13 13 ARG A 250 HIS A 255 5 6
HELIX 14 14 ALA A 274 ASP A 278 5 5
HELIX 15 15 TRP A 284 ASN A 305 1 22
HELIX 16 16 ILE B 25 PHE B 33 1 9
HELIX 17 17 SER B 67 GLN B 73 1 7
HELIX 18 18 HIS B 147 LEU B 151 1 5
HELIX 19 19 SER C 11 LEU C 15 5 5
HELIX 20 20 SER C 16 ASN C 33 1 18
HELIX 21 21 SER C 52 LEU C 66 1 15
HELIX 22 22 THR C 87 SER C 96 1 10
HELIX 23 23 GLY C 110 GLU C 117 1 8
HELIX 24 24 HIS C 134 GLY C 150 1 17
HELIX 25 25 GLY C 166 ALA C 177 1 12
HELIX 26 26 PRO C 189 ALA C 193 5 5
HELIX 27 27 PRO C 195 LYS C 205 1 11
HELIX 28 28 SER C 214 VAL C 218 5 5
HELIX 29 29 GLN C 231 LEU C 235 5 5
HELIX 30 30 ASP C 236 VAL C 243 1 8
HELIX 31 31 ARG C 250 HIS C 255 5 6
HELIX 32 32 ALA C 274 ASP C 278 5 5
HELIX 33 33 TRP C 284 ASN C 305 1 22
HELIX 34 34 ILE D 25 PHE D 33 1 9
HELIX 35 35 SER D 67 GLN D 73 1 7
HELIX 36 36 HIS D 147 ALA D 152 1 6
SHEET 1 A 4 SER A 69 SER A 74 0
SHEET 2 A 4 VAL A 43 PHE A 48 1 N SER A 46 O VAL A 71
SHEET 3 A 4 ALA A 101 HIS A 106 1 O VAL A 103 N CYS A 47
SHEET 4 A 4 VAL A 124 ASP A 129 1 O ALA A 127 N MET A 104
SHEET 1 B 5 TRP A 209 HIS A 212 0
SHEET 2 B 5 ARG A 183 ILE A 187 1 N PHE A 186 O SER A 210
SHEET 3 B 5 HIS A 156 VAL A 160 1 N VAL A 157 O ARG A 183
SHEET 4 B 5 ILE A 224 MET A 227 1 O TYR A 226 N ALA A 158
SHEET 5 B 5 LYS A 262 LEU A 264 1 O LEU A 264 N MET A 227
SHEET 1 C10 VAL B 91 SER B 95 0
SHEET 2 C10 THR B 82 ILE B 86 -1 N VAL B 83 O SER B 95
SHEET 3 C10 GLY B 15 PRO B 22 -1 N ASP B 19 O THR B 82
SHEET 4 C10 LYS B 56 GLU B 62 -1 O ILE B 61 N THR B 16
SHEET 5 C10 ILE B 42 LEU B 48 -1 N GLY B 45 O LEU B 58
SHEET 6 C10 ILE D 42 LEU D 46 -1 O LEU D 46 N ILE B 42
SHEET 7 C10 LYS D 56 GLU D 62 -1 O LYS D 60 N THR D 43
SHEET 8 C10 GLY D 15 PRO D 22 -1 N ILE D 21 O ASP D 57
SHEET 9 C10 THR D 82 ASP D 87 -1 O THR D 82 N ASP D 19
SHEET 10 C10 GLU D 90 SER D 95 -1 O GLY D 93 N ARG D 85
SHEET 1 D 4 ARG B 102 ASP B 104 0
SHEET 2 D 4 SER B 124 LYS B 129 -1 O PHE B 125 N ILE B 103
SHEET 3 D 4 ILE B 134 CYS B 138 -1 O ALA B 135 N ARG B 128
SHEET 4 D 4 GLU B 144 SER B 146 -1 O PHE B 145 N LEU B 136
SHEET 1 E 4 SER C 69 SER C 74 0
SHEET 2 E 4 VAL C 43 PHE C 48 1 N SER C 46 O VAL C 71
SHEET 3 E 4 ALA C 101 HIS C 106 1 O VAL C 103 N CYS C 47
SHEET 4 E 4 VAL C 124 ASP C 129 1 O LEU C 125 N ILE C 102
SHEET 1 F 5 TRP C 209 LEU C 211 0
SHEET 2 F 5 ARG C 183 ILE C 187 1 N PHE C 186 O SER C 210
SHEET 3 F 5 HIS C 156 GLY C 161 1 N MET C 159 O TYR C 185
SHEET 4 F 5 ILE C 224 THR C 228 1 O TYR C 226 N ALA C 158
SHEET 5 F 5 LYS C 262 LEU C 264 1 O LEU C 264 N MET C 227
SHEET 1 G 4 ARG D 102 ASP D 104 0
SHEET 2 G 4 SER D 124 ARG D 130 -1 O PHE D 125 N ILE D 103
SHEET 3 G 4 ASP D 133 CYS D 138 -1 O ALA D 135 N ARG D 128
SHEET 4 G 4 GLU D 144 SER D 146 -1 O PHE D 145 N LEU D 136
LINK SG CYS B 109 ZN ZN B 201 1555 1555 2.36
LINK SG CYS B 114 ZN ZN B 201 1555 1555 2.31
LINK SG CYS B 138 ZN ZN B 201 1555 1555 2.37
LINK SG CYS B 141 ZN ZN B 201 1555 1555 2.26
LINK SG CYS D 109 ZN ZN D 201 1555 1555 2.35
LINK SG CYS D 114 ZN ZN D 201 1555 1555 2.28
LINK SG CYS D 138 ZN ZN D 201 1555 1555 2.33
LINK SG CYS D 141 ZN ZN D 201 1555 1555 2.38
CISPEP 1 LEU A 267 PRO A 268 0 -0.83
CISPEP 2 LEU C 81 GLY C 82 0 -2.60
CISPEP 3 LEU C 267 PRO C 268 0 -0.50
SITE 1 AC1 7 ARG A 54 THR A 55 ARG A 105 HIS A 134
SITE 2 AC1 7 LEU A 267 HOH A 625 HOH A 646
SITE 1 AC2 4 CYS B 109 CYS B 114 CYS B 138 CYS B 141
SITE 1 AC3 8 ALA B 11 ILE B 12 VAL B 17 LYS B 60
SITE 2 AC3 8 ILE B 86 TYR B 89 HOH B 323 HOH B 328
SITE 1 AC4 4 CYS D 109 CYS D 114 CYS D 138 CYS D 141
SITE 1 AC5 11 ILE D 12 VAL D 17 ASP D 19 HIS D 20
SITE 2 AC5 11 GLU D 52 LYS D 60 ASN D 84 ILE D 86
SITE 3 AC5 11 TYR D 89 VAL D 91 LYS D 94
CRYST1 120.680 120.680 142.523 90.00 90.00 120.00 P 3 2 1 12
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 0.008286 0.004784 0.000000 0.00000
SCALE2 0.000000 0.009568 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007016 0.00000
(ATOM LINES ARE NOT SHOWN.)
END