HEADER TRANSFERASE 29-APR-13 4KH1
TITLE THE R STATE STRUCTURE OF E. COLI ATCASE WITH CTP,UTP, AND MAGNESIUM
TITLE 2 BOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ASPARTATE CARBAMOYLTRANSFERASE;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: ASPARTATE TRANSCARBAMYLASE;
COMPND 5 EC: 2.1.3.2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: ASPARTATE CARBAMOYLTRANSFERASE REGULATORY CHAIN;
COMPND 9 CHAIN: B, D;
COMPND 10 EC: 2.1.3.2;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 595495;
SOURCE 4 STRAIN: ATCC 55124 / KO11;
SOURCE 5 GENE: PYRB, EKO11_4066, KO11_22860;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 10 ORGANISM_TAXID: 595495;
SOURCE 11 STRAIN: ATCC 55124 / KO11;
SOURCE 12 GENE: PYRI, EKO11_4067, KO11_22855;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PYRIMIDINE NUCLEOTIDE BIOSYNTHESIS, FEEDBACK INHIBITION, COMPETING
KEYWDS 2 PATHWAY PRODUCT ACTIVATION, ALLOSTERY, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.M.COCKRELL,Y.ZHENG,W.GUO,A.W.PETERSON,E.R.KANTROWITZ
REVDAT 2 20-SEP-23 4KH1 1 REMARK LINK
REVDAT 1 27-NOV-13 4KH1 0
JRNL AUTH G.M.COCKRELL,Y.ZHENG,W.GUO,A.W.PETERSON,J.K.TRUONG,
JRNL AUTH 2 E.R.KANTROWITZ
JRNL TITL NEW PARADIGM FOR ALLOSTERIC REGULATION OF ESCHERICHIA COLI
JRNL TITL 2 ASPARTATE TRANSCARBAMOYLASE.
JRNL REF BIOCHEMISTRY V. 52 8036 2013
JRNL REFN ISSN 0006-2960
JRNL PMID 24138583
JRNL DOI 10.1021/BI401205N
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.1_1168
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.81
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 66361
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 3366
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 31.8102 - 6.3303 0.95 2703 136 0.1482 0.1715
REMARK 3 2 6.3303 - 5.0310 0.98 2668 119 0.1685 0.1570
REMARK 3 3 5.0310 - 4.3969 0.98 2648 151 0.1253 0.1435
REMARK 3 4 4.3969 - 3.9957 0.99 2631 137 0.1301 0.1599
REMARK 3 5 3.9957 - 3.7098 0.99 2637 132 0.1425 0.1762
REMARK 3 6 3.7098 - 3.4913 0.99 2627 146 0.1501 0.1834
REMARK 3 7 3.4913 - 3.3167 0.99 2619 149 0.1676 0.1957
REMARK 3 8 3.3167 - 3.1724 0.99 2596 145 0.1844 0.2473
REMARK 3 9 3.1724 - 3.0504 1.00 2657 139 0.1817 0.2349
REMARK 3 10 3.0504 - 2.9452 1.00 2610 141 0.1847 0.2444
REMARK 3 11 2.9452 - 2.8532 1.00 2638 137 0.1806 0.2276
REMARK 3 12 2.8532 - 2.7717 1.00 2624 124 0.1849 0.2331
REMARK 3 13 2.7717 - 2.6988 1.00 2625 153 0.1830 0.2212
REMARK 3 14 2.6988 - 2.6330 1.00 2606 133 0.1862 0.2358
REMARK 3 15 2.6330 - 2.5731 1.00 2594 151 0.1893 0.2417
REMARK 3 16 2.5731 - 2.5184 1.00 2604 143 0.1893 0.2370
REMARK 3 17 2.5184 - 2.4680 1.00 2668 135 0.1960 0.2501
REMARK 3 18 2.4680 - 2.4215 1.00 2595 145 0.2073 0.2415
REMARK 3 19 2.4215 - 2.3782 1.00 2633 120 0.2161 0.3273
REMARK 3 20 2.3782 - 2.3379 1.00 2596 140 0.2168 0.2682
REMARK 3 21 2.3379 - 2.3002 1.00 2627 142 0.2170 0.2578
REMARK 3 22 2.3002 - 2.2649 1.00 2585 147 0.2152 0.2698
REMARK 3 23 2.2649 - 2.2316 1.00 2597 160 0.2328 0.2714
REMARK 3 24 2.2316 - 2.2000 1.00 2607 141 0.2308 0.2846
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) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.890
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 60.16
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 : 0.009 7432
REMARK 3 ANGLE : 1.061 10122
REMARK 3 CHIRALITY : 0.073 1164
REMARK 3 PLANARITY : 0.005 1294
REMARK 3 DIHEDRAL : 14.418 2788
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 28
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 16 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.3662 43.8975 3.0733
REMARK 3 T TENSOR
REMARK 3 T11: 0.3685 T22: 0.4289
REMARK 3 T33: 0.4834 T12: 0.0293
REMARK 3 T13: -0.0907 T23: 0.1231
REMARK 3 L TENSOR
REMARK 3 L11: 0.0827 L22: 0.2627
REMARK 3 L33: 0.0588 L12: -0.2916
REMARK 3 L13: 0.0714 L23: -0.0281
REMARK 3 S TENSOR
REMARK 3 S11: 0.0635 S12: 0.1943 S13: 0.2150
REMARK 3 S21: 0.0800 S22: -0.1458 S23: 0.5246
REMARK 3 S31: -0.5893 S32: -0.1213 S33: -0.0046
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 17 THROUGH 32 )
REMARK 3 ORIGIN FOR THE GROUP (A): 34.0103 32.4208 -3.0314
REMARK 3 T TENSOR
REMARK 3 T11: 0.3887 T22: 0.4771
REMARK 3 T33: 0.4446 T12: 0.0374
REMARK 3 T13: -0.1533 T23: 0.0547
REMARK 3 L TENSOR
REMARK 3 L11: 0.1141 L22: 0.1801
REMARK 3 L33: 0.1717 L12: 0.2296
REMARK 3 L13: 0.1067 L23: 0.1093
REMARK 3 S TENSOR
REMARK 3 S11: 0.1174 S12: 0.5209 S13: -0.0108
REMARK 3 S21: -0.5612 S22: 0.0250 S23: 0.3852
REMARK 3 S31: -0.0580 S32: -0.6004 S33: 0.0003
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 33 THROUGH 53 )
REMARK 3 ORIGIN FOR THE GROUP (A): 50.4741 36.6571 2.3218
REMARK 3 T TENSOR
REMARK 3 T11: 0.3204 T22: 0.3340
REMARK 3 T33: 0.2167 T12: -0.0077
REMARK 3 T13: 0.0544 T23: 0.0554
REMARK 3 L TENSOR
REMARK 3 L11: 0.8673 L22: 0.9536
REMARK 3 L33: 0.0087 L12: 0.3700
REMARK 3 L13: -0.1199 L23: -0.0539
REMARK 3 S TENSOR
REMARK 3 S11: -0.0633 S12: 0.1611 S13: 0.1571
REMARK 3 S21: -0.1088 S22: 0.1370 S23: -0.2123
REMARK 3 S31: -0.0689 S32: 0.0398 S33: 0.0233
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 54 THROUGH 134 )
REMARK 3 ORIGIN FOR THE GROUP (A): 48.8911 42.7755 12.1359
REMARK 3 T TENSOR
REMARK 3 T11: 0.2449 T22: 0.2615
REMARK 3 T33: 0.2744 T12: 0.0289
REMARK 3 T13: 0.0150 T23: 0.0321
REMARK 3 L TENSOR
REMARK 3 L11: 1.1033 L22: 1.6335
REMARK 3 L33: 1.1168 L12: 0.2982
REMARK 3 L13: -0.0436 L23: 0.1409
REMARK 3 S TENSOR
REMARK 3 S11: 0.0843 S12: -0.0100 S13: 0.1202
REMARK 3 S21: -0.0454 S22: 0.0487 S23: 0.1130
REMARK 3 S31: -0.0716 S32: -0.0357 S33: -0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 135 THROUGH 187 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.3211 28.2229 11.7240
REMARK 3 T TENSOR
REMARK 3 T11: 0.1871 T22: 0.3822
REMARK 3 T33: 0.4860 T12: -0.0325
REMARK 3 T13: -0.0367 T23: 0.1067
REMARK 3 L TENSOR
REMARK 3 L11: 0.5800 L22: 1.9425
REMARK 3 L33: 1.0978 L12: -0.3542
REMARK 3 L13: -0.5716 L23: -0.1214
REMARK 3 S TENSOR
REMARK 3 S11: -0.0519 S12: -0.0573 S13: -0.1839
REMARK 3 S21: -0.1012 S22: 0.1042 S23: 0.4892
REMARK 3 S31: -0.1168 S32: -0.1900 S33: 0.0034
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 188 THROUGH 214 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.8413 32.2306 21.5072
REMARK 3 T TENSOR
REMARK 3 T11: 0.2850 T22: 0.5354
REMARK 3 T33: 0.7034 T12: 0.0086
REMARK 3 T13: 0.1144 T23: 0.1849
REMARK 3 L TENSOR
REMARK 3 L11: 0.1194 L22: 0.1006
REMARK 3 L33: 0.9826 L12: 0.0999
REMARK 3 L13: 0.0656 L23: 0.2569
REMARK 3 S TENSOR
REMARK 3 S11: 0.0336 S12: -0.6093 S13: 0.1921
REMARK 3 S21: 0.2977 S22: 0.1704 S23: 0.6602
REMARK 3 S31: -0.3002 S32: -0.6150 S33: -0.0027
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 215 THROUGH 236 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.3246 23.1041 21.4347
REMARK 3 T TENSOR
REMARK 3 T11: 0.2263 T22: 0.3240
REMARK 3 T33: 0.7277 T12: -0.0103
REMARK 3 T13: 0.0833 T23: 0.2196
REMARK 3 L TENSOR
REMARK 3 L11: 1.2288 L22: 1.3805
REMARK 3 L33: 2.5703 L12: 0.6483
REMARK 3 L13: 1.0734 L23: 0.8046
REMARK 3 S TENSOR
REMARK 3 S11: -0.3089 S12: 0.4055 S13: -0.4610
REMARK 3 S21: 0.6609 S22: 0.6604 S23: 0.7125
REMARK 3 S31: 0.1679 S32: 0.7575 S33: 0.2196
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 237 THROUGH 261 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.6984 17.6748 24.3810
REMARK 3 T TENSOR
REMARK 3 T11: 0.1334 T22: 0.3891
REMARK 3 T33: 0.8067 T12: -0.2768
REMARK 3 T13: 0.1372 T23: 0.3066
REMARK 3 L TENSOR
REMARK 3 L11: 1.2519 L22: 3.0776
REMARK 3 L33: 0.3552 L12: 0.0989
REMARK 3 L13: -0.5159 L23: 0.2219
REMARK 3 S TENSOR
REMARK 3 S11: -0.8061 S12: -0.6981 S13: -0.9549
REMARK 3 S21: 1.8842 S22: 0.9306 S23: 1.3686
REMARK 3 S31: 0.5843 S32: 0.4585 S33: 0.0396
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 262 THROUGH 284 )
REMARK 3 ORIGIN FOR THE GROUP (A): 37.7332 15.7032 16.1450
REMARK 3 T TENSOR
REMARK 3 T11: 0.2996 T22: 0.2980
REMARK 3 T33: 0.6630 T12: -0.0103
REMARK 3 T13: -0.0583 T23: 0.1440
REMARK 3 L TENSOR
REMARK 3 L11: 0.2355 L22: 0.2386
REMARK 3 L33: 0.0988 L12: -0.4713
REMARK 3 L13: 0.1590 L23: -0.1067
REMARK 3 S TENSOR
REMARK 3 S11: 0.0351 S12: -0.1784 S13: -0.4240
REMARK 3 S21: -0.0370 S22: 0.1518 S23: 0.6437
REMARK 3 S31: -0.1166 S32: -0.2689 S33: 0.0006
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 285 THROUGH 310 )
REMARK 3 ORIGIN FOR THE GROUP (A): 41.4577 31.7305 -0.0247
REMARK 3 T TENSOR
REMARK 3 T11: 0.2892 T22: 0.3533
REMARK 3 T33: 0.3249 T12: -0.0167
REMARK 3 T13: -0.1010 T23: -0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 1.6926 L22: 0.3501
REMARK 3 L33: 0.5756 L12: -0.3142
REMARK 3 L13: 0.0457 L23: 0.7344
REMARK 3 S TENSOR
REMARK 3 S11: 0.0423 S12: 0.2782 S13: -0.0708
REMARK 3 S21: -0.4609 S22: 0.2457 S23: 0.4161
REMARK 3 S31: 0.0394 S32: -0.2151 S33: 0.0003
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 10 THROUGH 19 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.1197 81.8766 26.4284
REMARK 3 T TENSOR
REMARK 3 T11: 0.5913 T22: 0.5855
REMARK 3 T33: 0.6694 T12: 0.2414
REMARK 3 T13: -0.0303 T23: -0.1216
REMARK 3 L TENSOR
REMARK 3 L11: 0.1790 L22: 0.1442
REMARK 3 L33: 0.9281 L12: 0.0294
REMARK 3 L13: 0.2756 L23: 0.1157
REMARK 3 S TENSOR
REMARK 3 S11: 0.0473 S12: -0.2519 S13: 0.0934
REMARK 3 S21: 0.5680 S22: -0.7407 S23: 0.0008
REMARK 3 S31: -1.1813 S32: -0.2439 S33: -0.0178
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 20 THROUGH 45 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.5099 72.0869 32.5476
REMARK 3 T TENSOR
REMARK 3 T11: 0.5935 T22: 0.5284
REMARK 3 T33: 0.5610 T12: 0.1830
REMARK 3 T13: 0.0155 T23: -0.1300
REMARK 3 L TENSOR
REMARK 3 L11: 0.5585 L22: 0.3518
REMARK 3 L33: 0.6958 L12: 0.0555
REMARK 3 L13: 0.2401 L23: 0.3629
REMARK 3 S TENSOR
REMARK 3 S11: -0.4628 S12: 0.3039 S13: -0.1648
REMARK 3 S21: 0.1719 S22: 0.1058 S23: -0.3206
REMARK 3 S31: 0.0908 S32: 0.0800 S33: -0.0039
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 46 THROUGH 57 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.9246 71.1218 36.7370
REMARK 3 T TENSOR
REMARK 3 T11: 0.7235 T22: 0.8339
REMARK 3 T33: 0.8617 T12: -0.0231
REMARK 3 T13: 0.1829 T23: -0.3585
REMARK 3 L TENSOR
REMARK 3 L11: 0.0922 L22: 0.0843
REMARK 3 L33: 0.1504 L12: 0.0267
REMARK 3 L13: -0.0064 L23: -0.1224
REMARK 3 S TENSOR
REMARK 3 S11: -0.4945 S12: -0.1678 S13: -0.0489
REMARK 3 S21: 0.0749 S22: -0.4508 S23: 1.0758
REMARK 3 S31: 0.8453 S32: -0.1858 S33: -0.0185
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 58 THROUGH 76 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.2550 72.1351 23.0874
REMARK 3 T TENSOR
REMARK 3 T11: 0.6019 T22: 0.6329
REMARK 3 T33: 0.3705 T12: 0.2632
REMARK 3 T13: 0.0295 T23: -0.1614
REMARK 3 L TENSOR
REMARK 3 L11: 0.4583 L22: 0.3907
REMARK 3 L33: 0.2253 L12: -0.0560
REMARK 3 L13: 0.2005 L23: -0.2350
REMARK 3 S TENSOR
REMARK 3 S11: 0.4519 S12: 0.5635 S13: -0.1809
REMARK 3 S21: -0.6291 S22: -0.5591 S23: -0.1109
REMARK 3 S31: -0.2986 S32: -0.7121 S33: -0.0003
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 77 THROUGH 89 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.1457 75.2595 23.5372
REMARK 3 T TENSOR
REMARK 3 T11: 0.5470 T22: 0.8417
REMARK 3 T33: 0.7110 T12: 0.2129
REMARK 3 T13: -0.0058 T23: -0.1660
REMARK 3 L TENSOR
REMARK 3 L11: 0.3402 L22: 0.0486
REMARK 3 L33: 0.1197 L12: 0.0971
REMARK 3 L13: -0.1900 L23: -0.0107
REMARK 3 S TENSOR
REMARK 3 S11: -0.0555 S12: 0.1697 S13: -0.0865
REMARK 3 S21: 0.0738 S22: -0.3101 S23: 0.5340
REMARK 3 S31: -0.3363 S32: -0.8657 S33: -0.0016
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 90 THROUGH 104 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.3222 67.1524 18.9883
REMARK 3 T TENSOR
REMARK 3 T11: 0.4787 T22: 0.5609
REMARK 3 T33: 0.6476 T12: 0.2006
REMARK 3 T13: -0.1137 T23: -0.1515
REMARK 3 L TENSOR
REMARK 3 L11: 0.1125 L22: 0.4351
REMARK 3 L33: 0.3636 L12: 0.0476
REMARK 3 L13: 0.0877 L23: -0.2975
REMARK 3 S TENSOR
REMARK 3 S11: 0.4484 S12: 0.4818 S13: 0.0478
REMARK 3 S21: -1.7327 S22: -0.4926 S23: -0.4679
REMARK 3 S31: -0.0024 S32: -0.4702 S33: -0.0033
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 105 THROUGH 130 )
REMARK 3 ORIGIN FOR THE GROUP (A): 33.2461 51.8596 24.2343
REMARK 3 T TENSOR
REMARK 3 T11: 0.3214 T22: 0.5301
REMARK 3 T33: 0.4859 T12: 0.0542
REMARK 3 T13: 0.0402 T23: -0.0154
REMARK 3 L TENSOR
REMARK 3 L11: 0.3785 L22: 0.7751
REMARK 3 L33: 0.2957 L12: -0.5325
REMARK 3 L13: -0.0448 L23: 0.0009
REMARK 3 S TENSOR
REMARK 3 S11: -0.4056 S12: -0.5036 S13: 0.0321
REMARK 3 S21: 0.0251 S22: 0.2479 S23: -0.0741
REMARK 3 S31: 0.1073 S32: -0.2698 S33: 0.0000
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 131 THROUGH 143 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.8245 48.5473 22.3250
REMARK 3 T TENSOR
REMARK 3 T11: 0.2553 T22: 0.4619
REMARK 3 T33: 0.6441 T12: -0.0053
REMARK 3 T13: 0.0750 T23: -0.0346
REMARK 3 L TENSOR
REMARK 3 L11: 0.1520 L22: 0.4097
REMARK 3 L33: 0.4264 L12: -0.0820
REMARK 3 L13: 0.0444 L23: 0.3984
REMARK 3 S TENSOR
REMARK 3 S11: 0.1356 S12: -0.3606 S13: -0.4006
REMARK 3 S21: -0.1541 S22: -0.4367 S23: 0.6836
REMARK 3 S31: 0.2670 S32: 0.0249 S33: -0.0013
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 144 THROUGH 153 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.9422 51.7654 29.9522
REMARK 3 T TENSOR
REMARK 3 T11: 0.5251 T22: 0.8063
REMARK 3 T33: 0.5829 T12: -0.0171
REMARK 3 T13: 0.0972 T23: -0.0440
REMARK 3 L TENSOR
REMARK 3 L11: 0.0878 L22: 0.1182
REMARK 3 L33: 0.1611 L12: -0.0991
REMARK 3 L13: -0.0194 L23: -0.0441
REMARK 3 S TENSOR
REMARK 3 S11: -0.4277 S12: -0.8264 S13: 0.4041
REMARK 3 S21: 0.5788 S22: 0.3528 S23: 0.4508
REMARK 3 S31: -0.1119 S32: -0.0732 S33: 0.0001
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 53 )
REMARK 3 ORIGIN FOR THE GROUP (A): 59.5336 54.5048 78.2347
REMARK 3 T TENSOR
REMARK 3 T11: 0.3285 T22: 0.3369
REMARK 3 T33: 0.2644 T12: 0.0257
REMARK 3 T13: 0.0315 T23: -0.0499
REMARK 3 L TENSOR
REMARK 3 L11: 1.2269 L22: 1.3381
REMARK 3 L33: 0.9935 L12: 0.2596
REMARK 3 L13: 0.2859 L23: 0.0388
REMARK 3 S TENSOR
REMARK 3 S11: 0.0246 S12: -0.2390 S13: 0.0949
REMARK 3 S21: 0.1475 S22: 0.0268 S23: 0.1326
REMARK 3 S31: -0.0995 S32: -0.1429 S33: 0.0000
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 54 THROUGH 134 )
REMARK 3 ORIGIN FOR THE GROUP (A): 53.6512 47.1539 67.1279
REMARK 3 T TENSOR
REMARK 3 T11: 0.3204 T22: 0.3407
REMARK 3 T33: 0.2408 T12: 0.0237
REMARK 3 T13: 0.0352 T23: 0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 1.3422 L22: 0.8080
REMARK 3 L33: 0.1480 L12: 1.1406
REMARK 3 L13: 1.2311 L23: 0.2595
REMARK 3 S TENSOR
REMARK 3 S11: -0.0236 S12: 0.0413 S13: 0.0611
REMARK 3 S21: -0.0471 S22: 0.0485 S23: 0.0998
REMARK 3 S31: -0.0142 S32: 0.0235 S33: -0.0000
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 135 THROUGH 187 )
REMARK 3 ORIGIN FOR THE GROUP (A): 70.0538 66.2908 67.6890
REMARK 3 T TENSOR
REMARK 3 T11: 0.4636 T22: 0.3471
REMARK 3 T33: 0.3742 T12: -0.0347
REMARK 3 T13: 0.0356 T23: 0.0259
REMARK 3 L TENSOR
REMARK 3 L11: 1.7613 L22: 0.3838
REMARK 3 L33: 0.7459 L12: -0.2792
REMARK 3 L13: -0.9784 L23: -0.5394
REMARK 3 S TENSOR
REMARK 3 S11: 0.1000 S12: -0.0976 S13: 0.3348
REMARK 3 S21: 0.0416 S22: -0.0699 S23: -0.0769
REMARK 3 S31: -0.2378 S32: 0.0780 S33: -0.0011
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 188 THROUGH 215 )
REMARK 3 ORIGIN FOR THE GROUP (A): 67.3793 72.9640 57.8024
REMARK 3 T TENSOR
REMARK 3 T11: 0.6435 T22: 0.3901
REMARK 3 T33: 0.5422 T12: -0.0010
REMARK 3 T13: -0.0098 T23: 0.1179
REMARK 3 L TENSOR
REMARK 3 L11: 0.3865 L22: 0.2540
REMARK 3 L33: 0.6559 L12: -0.0210
REMARK 3 L13: 0.1367 L23: 0.0941
REMARK 3 S TENSOR
REMARK 3 S11: -0.3377 S12: 0.3352 S13: 0.6277
REMARK 3 S21: -0.9717 S22: 0.1922 S23: 0.4532
REMARK 3 S31: -0.8333 S32: 0.2626 S33: -0.0237
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 216 THROUGH 236 )
REMARK 3 ORIGIN FOR THE GROUP (A): 74.5708 62.5514 57.9311
REMARK 3 T TENSOR
REMARK 3 T11: 0.5137 T22: 0.4334
REMARK 3 T33: 0.3932 T12: -0.0723
REMARK 3 T13: 0.0802 T23: 0.0368
REMARK 3 L TENSOR
REMARK 3 L11: -0.0068 L22: 0.3052
REMARK 3 L33: 0.5221 L12: -0.0506
REMARK 3 L13: -0.2325 L23: 0.0098
REMARK 3 S TENSOR
REMARK 3 S11: -0.0681 S12: 0.3282 S13: 0.2726
REMARK 3 S21: -0.2481 S22: 0.1165 S23: 0.0734
REMARK 3 S31: -0.0064 S32: 0.2569 S33: 0.0001
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 237 THROUGH 261 )
REMARK 3 ORIGIN FOR THE GROUP (A): 80.2992 61.8787 54.9917
REMARK 3 T TENSOR
REMARK 3 T11: 0.4963 T22: 0.6242
REMARK 3 T33: 0.4043 T12: -0.1135
REMARK 3 T13: 0.2283 T23: -0.0096
REMARK 3 L TENSOR
REMARK 3 L11: 0.2686 L22: 2.2754
REMARK 3 L33: 1.2989 L12: -0.4168
REMARK 3 L13: -0.4154 L23: 0.2094
REMARK 3 S TENSOR
REMARK 3 S11: -0.0504 S12: 0.5920 S13: -0.0018
REMARK 3 S21: -0.3714 S22: 0.3196 S23: -0.4432
REMARK 3 S31: -0.1124 S32: 0.2754 S33: 0.2906
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 262 THROUGH 310 )
REMARK 3 ORIGIN FOR THE GROUP (A): 73.0639 54.4829 71.7017
REMARK 3 T TENSOR
REMARK 3 T11: 0.3706 T22: 0.3229
REMARK 3 T33: 0.3064 T12: -0.0129
REMARK 3 T13: 0.0347 T23: -0.0319
REMARK 3 L TENSOR
REMARK 3 L11: 0.9101 L22: 1.3074
REMARK 3 L33: 0.6201 L12: 0.0687
REMARK 3 L13: 0.8517 L23: 0.0489
REMARK 3 S TENSOR
REMARK 3 S11: 0.0281 S12: -0.1126 S13: 0.1539
REMARK 3 S21: 0.0976 S22: -0.0347 S23: -0.0949
REMARK 3 S31: -0.1250 S32: 0.0900 S33: 0.0000
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 11 THROUGH 95 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.8593 79.6814 47.7201
REMARK 3 T TENSOR
REMARK 3 T11: 0.7904 T22: 0.5952
REMARK 3 T33: 0.4409 T12: 0.2202
REMARK 3 T13: -0.0214 T23: -0.0964
REMARK 3 L TENSOR
REMARK 3 L11: 1.8369 L22: 1.8831
REMARK 3 L33: 2.1855 L12: -0.2550
REMARK 3 L13: 1.2789 L23: 1.3759
REMARK 3 S TENSOR
REMARK 3 S11: -0.2996 S12: -0.3464 S13: 0.0713
REMARK 3 S21: 0.6073 S22: -0.0469 S23: 0.0767
REMARK 3 S31: 0.0722 S32: -0.0286 S33: -0.0032
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 96 THROUGH 153 )
REMARK 3 ORIGIN FOR THE GROUP (A): 45.9635 68.2788 54.8473
REMARK 3 T TENSOR
REMARK 3 T11: 0.7648 T22: 0.3799
REMARK 3 T33: 0.4591 T12: 0.0755
REMARK 3 T13: -0.2546 T23: 0.0778
REMARK 3 L TENSOR
REMARK 3 L11: 0.6964 L22: 0.9055
REMARK 3 L33: 1.0808 L12: -0.4312
REMARK 3 L13: 0.6281 L23: -0.2592
REMARK 3 S TENSOR
REMARK 3 S11: -0.4530 S12: -0.0157 S13: -0.1396
REMARK 3 S21: -0.4846 S22: -0.0734 S23: 0.0308
REMARK 3 S31: -0.8069 S32: -0.1084 S33: -0.2337
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 4KH1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAY-13.
REMARK 100 THE DEPOSITION ID IS D_1000079328.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.542
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK 9.9.8.8D
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66369
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 31.810
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 5.680
REMARK 200 R MERGE (I) : 0.03900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.58
REMARK 200 R MERGE FOR SHELL (I) : 0.40900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: PDB ENTRY 1D09
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM MALEIC ACID, 1 MM PALA, 3 MM
REMARK 280 SODIUM AZIDE, PH 5.9, MICRODIALYSIS, TEMPERATURE 293K
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: 42780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 98390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -218.0 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 120.87000
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 60.43500
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 104.67649
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 581 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 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 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 OE1 GLU B 37 O HOH B 340 2.19
REMARK 500 O ASP B 39 NH1 ARG D 55 2.19
REMARK 500 OD1 ASP A 271 O HOH A 634 2.19
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 ASN A 132 -87.66 -82.86
REMARK 500 LEU A 267 159.84 68.32
REMARK 500 VAL A 270 -94.41 -99.35
REMARK 500 ASN B 105 -52.31 76.86
REMARK 500 ALA B 131 -126.95 50.09
REMARK 500 ASN C 132 -85.32 -85.65
REMARK 500 LEU C 267 159.28 74.58
REMARK 500 VAL C 270 -91.26 -100.01
REMARK 500 TRP C 284 17.01 -144.93
REMARK 500 ASP D 69 -30.71 67.57
REMARK 500 ALA D 78 75.77 -154.50
REMARK 500 ASN D 105 -38.70 74.19
REMARK 500 ALA D 131 -42.87 80.75
REMARK 500 ALA D 152 38.24 -163.30
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 111.8 105.9
REMARK 620 4 CYS B 141 SG 100.1 116.2 105.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 204 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CTP B 202 O2B
REMARK 620 2 CTP B 202 O1G 87.7
REMARK 620 3 UTP B 203 O1B 93.1 176.9
REMARK 620 4 UTP B 203 O2G 169.9 93.2 86.5
REMARK 620 5 HOH B 301 O 83.6 88.5 94.5 86.4
REMARK 620 6 HOH B 302 O 100.1 98.2 78.7 89.7 172.4
REMARK 620 N 1 2 3 4 5
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 119.3
REMARK 620 3 CYS D 138 SG 115.3 105.6
REMARK 620 4 CYS D 141 SG 99.6 113.3 102.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 204 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CTP D 202 O2G
REMARK 620 2 CTP D 202 O2B 83.5
REMARK 620 3 UTP D 203 O1B 157.2 105.4
REMARK 620 4 UTP D 203 O1G 87.9 163.2 77.9
REMARK 620 5 HOH D 301 O 106.3 92.3 94.5 104.0
REMARK 620 6 HOH D 302 O 75.0 80.4 85.7 83.4 172.4
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PAL 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 CTP B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UTP B 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PAL C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CTP D 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UTP D 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 204
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4KGV RELATED DB: PDB
REMARK 900 RELATED ID: 4KGX RELATED DB: PDB
REMARK 900 RELATED ID: 4KGZ RELATED DB: PDB
REMARK 900 RELATED ID: 4KH0 RELATED DB: PDB
DBREF 4KH1 A 1 310 UNP E8Y328 E8Y328_ECOKO 2 311
DBREF 4KH1 B 1 153 UNP E8Y329 E8Y329_ECOKO 1 153
DBREF 4KH1 C 1 310 UNP E8Y328 E8Y328_ECOKO 2 311
DBREF 4KH1 D 1 153 UNP E8Y329 E8Y329_ECOKO 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 PAL A 401 16
HET ZN B 201 1
HET CTP B 202 29
HET UTP B 203 29
HET MG B 204 1
HET PO4 B 205 5
HET PAL C 401 16
HET ZN D 201 1
HET CTP D 202 29
HET UTP D 203 29
HET MG D 204 1
HETNAM PAL N-(PHOSPHONACETYL)-L-ASPARTIC ACID
HETNAM ZN ZINC ION
HETNAM CTP CYTIDINE-5'-TRIPHOSPHATE
HETNAM UTP URIDINE 5'-TRIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM PO4 PHOSPHATE ION
FORMUL 5 PAL 2(C6 H10 N O8 P)
FORMUL 6 ZN 2(ZN 2+)
FORMUL 7 CTP 2(C9 H16 N3 O14 P3)
FORMUL 8 UTP 2(C9 H15 N2 O15 P3)
FORMUL 9 MG 2(MG 2+)
FORMUL 10 PO4 O4 P 3-
FORMUL 16 HOH *458(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 THR A 53 LEU A 66 1 14
HELIX 4 4 ASP A 75 ASN A 78 5 4
HELIX 5 5 THR A 79 LYS A 84 1 6
HELIX 6 6 THR A 87 SER A 96 1 10
HELIX 7 7 GLY A 110 GLU A 117 1 8
HELIX 8 8 HIS A 134 GLY A 150 1 17
HELIX 9 9 GLY A 166 ALA A 177 1 12
HELIX 10 10 PRO A 189 ALA A 193 5 5
HELIX 11 11 PRO A 195 LYS A 205 1 11
HELIX 12 12 ILE A 215 ALA A 220 1 6
HELIX 13 13 GLN A 231 LEU A 235 5 5
HELIX 14 14 ASP A 236 VAL A 243 5 8
HELIX 15 15 ARG A 250 HIS A 255 5 6
HELIX 16 16 ALA A 274 ASP A 278 5 5
HELIX 17 17 TRP A 284 ASN A 305 1 22
HELIX 18 18 ILE B 25 PHE B 33 1 9
HELIX 19 19 SER B 67 GLN B 73 1 7
HELIX 20 20 LEU B 74 TYR B 77 5 4
HELIX 21 21 CYS B 114 ALA B 118 5 5
HELIX 22 22 ASN B 148 VAL B 150 5 3
HELIX 23 23 SER C 11 LEU C 15 5 5
HELIX 24 24 SER C 16 ASN C 33 1 18
HELIX 25 25 THR C 53 LEU C 66 1 14
HELIX 26 26 THR C 79 LYS C 84 1 6
HELIX 27 27 THR C 87 SER C 96 1 10
HELIX 28 28 GLY C 110 GLU C 117 1 8
HELIX 29 29 HIS C 134 GLY C 150 1 17
HELIX 30 30 GLY C 166 ALA C 177 1 12
HELIX 31 31 PRO C 189 ALA C 193 5 5
HELIX 32 32 PRO C 195 LYS C 205 1 11
HELIX 33 33 ILE C 215 ALA C 220 1 6
HELIX 34 34 ASP C 236 VAL C 243 5 8
HELIX 35 35 ARG C 250 HIS C 255 5 6
HELIX 36 36 ALA C 274 ASP C 278 5 5
HELIX 37 37 TRP C 284 ASN C 291 1 8
HELIX 38 38 ASN C 291 ASN C 305 1 15
HELIX 39 39 ILE D 25 PHE D 33 1 9
HELIX 40 40 ASP D 69 ALA D 78 1 10
HELIX 41 41 HIS D 147 LEU D 151 1 5
SHEET 1 A 4 SER A 69 PHE A 73 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 LEU A 211 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 GLU B 90 SER B 95 0
SHEET 2 C10 THR B 82 ASP B 87 -1 N ASP B 87 O GLU B 90
SHEET 3 C10 GLY B 15 PRO B 22 -1 N GLY B 15 O ILE B 86
SHEET 4 C10 GLY B 54 GLU B 62 -1 O ASP B 57 N ILE B 21
SHEET 5 C10 ILE B 42 SER B 50 -1 N SER B 50 O GLY B 54
SHEET 6 C10 ILE D 42 SER D 50 -1 O ILE D 42 N LEU B 46
SHEET 7 C10 GLY D 54 GLU D 62 -1 O LYS D 56 N LEU D 48
SHEET 8 C10 GLY D 15 ILE D 21 -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 ARG B 130 -1 O PHE B 125 N ILE B 103
SHEET 3 D 4 ASP B 133 CYS B 138 -1 O ASP B 133 N ARG B 130
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 PHE C 73 0
SHEET 2 E 4 VAL C 43 PHE C 48 1 N PHE C 48 O PHE C 73
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 ALA C 127 N MET C 104
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 VAL C 160 1 N MET C 159 O TYR C 185
SHEET 4 F 5 ILE C 224 MET C 227 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 LYS D 129 -1 O PHE D 125 N ILE D 103
SHEET 3 G 4 ILE D 134 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 2.37
LINK SG CYS B 114 ZN ZN B 201 1555 1555 2.36
LINK SG CYS B 138 ZN ZN B 201 1555 1555 2.38
LINK SG CYS B 141 ZN ZN B 201 1555 1555 2.25
LINK O2B CTP B 202 MG MG B 204 1555 1555 2.02
LINK O1G CTP B 202 MG MG B 204 1555 1555 2.16
LINK O1B UTP B 203 MG MG B 204 1555 1555 2.02
LINK O2G UTP B 203 MG MG B 204 1555 1555 2.08
LINK MG MG B 204 O HOH B 301 1555 1555 2.09
LINK MG MG B 204 O HOH B 302 1555 1555 2.07
LINK SG CYS D 109 ZN ZN D 201 1555 1555 2.42
LINK SG CYS D 114 ZN ZN D 201 1555 1555 2.31
LINK SG CYS D 138 ZN ZN D 201 1555 1555 2.32
LINK SG CYS D 141 ZN ZN D 201 1555 1555 2.28
LINK O2G CTP D 202 MG MG D 204 1555 1555 1.99
LINK O2B CTP D 202 MG MG D 204 1555 1555 2.07
LINK O1B UTP D 203 MG MG D 204 1555 1555 1.85
LINK O1G UTP D 203 MG MG D 204 1555 1555 2.43
LINK MG MG D 204 O HOH D 301 1555 1555 2.09
LINK MG MG D 204 O HOH D 302 1555 1555 2.05
CISPEP 1 LEU A 267 PRO A 268 0 -0.74
CISPEP 2 LEU C 267 PRO C 268 0 -3.09
SITE 1 AC1 14 SER A 52 THR A 53 ARG A 54 THR A 55
SITE 2 AC1 14 SER A 80 LYS A 84 ARG A 105 HIS A 134
SITE 3 AC1 14 ARG A 167 ARG A 229 GLN A 231 LEU A 267
SITE 4 AC1 14 HOH A 510 HOH A 532
SITE 1 AC2 4 CYS B 109 CYS B 114 CYS B 138 CYS B 141
SITE 1 AC3 13 ALA B 11 ILE B 12 VAL B 17 ASP B 19
SITE 2 AC3 13 HIS B 20 LYS B 60 ASN B 84 TYR B 89
SITE 3 AC3 13 VAL B 91 LYS B 94 UTP B 203 MG B 204
SITE 4 AC3 13 HOH B 301
SITE 1 AC4 14 LEU B 7 GLN B 8 VAL B 9 HIS B 20
SITE 2 AC4 14 PRO B 49 SER B 50 GLU B 52 LYS B 56
SITE 3 AC4 14 LEU B 58 LYS B 60 CTP B 202 MG B 204
SITE 4 AC4 14 HOH B 301 HOH B 302
SITE 1 AC5 4 CTP B 202 UTP B 203 HOH B 301 HOH B 302
SITE 1 AC6 4 ARG B 130 GLU B 144 SER B 146 HOH B 320
SITE 1 AC7 16 SER C 52 THR C 53 ARG C 54 THR C 55
SITE 2 AC7 16 SER C 80 LYS C 84 ARG C 105 HIS C 134
SITE 3 AC7 16 ARG C 167 THR C 168 ARG C 229 GLN C 231
SITE 4 AC7 16 LEU C 267 HOH C 503 HOH C 507 HOH C 649
SITE 1 AC8 4 CYS D 109 CYS D 114 CYS D 138 CYS D 141
SITE 1 AC9 16 ALA D 11 ILE D 12 VAL D 17 ASP D 19
SITE 2 AC9 16 HIS D 20 LYS D 60 ASN D 84 ILE D 86
SITE 3 AC9 16 TYR D 89 VAL D 91 LYS D 94 UTP D 203
SITE 4 AC9 16 MG D 204 HOH D 301 HOH D 302 HOH D 323
SITE 1 BC1 15 LEU D 7 GLN D 8 VAL D 9 HIS D 20
SITE 2 BC1 15 PRO D 49 SER D 50 GLY D 51 GLU D 52
SITE 3 BC1 15 LYS D 56 LEU D 58 LYS D 60 CTP D 202
SITE 4 BC1 15 MG D 204 HOH D 301 HOH D 302
SITE 1 BC2 4 CTP D 202 UTP D 203 HOH D 301 HOH D 302
CRYST1 120.870 120.870 154.730 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 0.008273 0.004777 0.000000 0.00000
SCALE2 0.000000 0.009553 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006463 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
