HEADER LYASE 04-FEB-10 3LP6
TITLE CRYSTAL STRUCTURE OF RV3275C-E60A FROM MYCOBACTERIUM TUBERCULOSIS AT
TITLE 2 1.7A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE CATALYTIC SUBUNIT;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: AIR CARBOXYLASE, AIRC;
COMPND 5 EC: 4.1.1.21;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: MT3375, MTCY71.15C, PURE, RV3275C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: CUSTOM
KEYWDS ALPHA AND BETA PROTEIN, STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, INTEGRATED CENTER FOR STRUCTURE AND FUNCTION INNOVATION,
KEYWDS 3 ISFI, TB STRUCTURAL GENOMICS CONSORTIUM, TBSGC, DECARBOXYLASE,
KEYWDS 4 LYASE, PURINE BIOSYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR H.KIM,M.YU,L.-W.HUNG,T.C.TERWILLIGER,C.-Y.KIM,INTEGRATED CENTER FOR
AUTHOR 2 STRUCTURE AND FUNCTION INNOVATION (ISFI),TB STRUCTURAL GENOMICS
AUTHOR 3 CONSORTIUM (TBSGC)
REVDAT 4 03-APR-24 3LP6 1 REMARK
REVDAT 3 21-FEB-24 3LP6 1 REMARK
REVDAT 2 13-OCT-21 3LP6 1 REMARK SEQADV
REVDAT 1 16-JUN-10 3LP6 0
JRNL AUTH H.KIM,M.YU,L.-W.HUNG,T.C.TERWILLIGER,C.-Y.KIM
JRNL TITL CRYSTAL STRUCTURE OF RV3275C-E60A FROM MYCOBACTERIUM
JRNL TITL 2 TUBERCULOSIS AT 1.7A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6_292)
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.56
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.0
REMARK 3 NUMBER OF REFLECTIONS : 62961
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.220
REMARK 3 FREE R VALUE TEST SET COUNT : 2029
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 45.5743 - 3.6663 0.98 6955 230 0.1565 0.1703
REMARK 3 2 3.6663 - 2.9102 0.95 6434 216 0.1570 0.1640
REMARK 3 3 2.9102 - 2.5424 0.93 6271 208 0.1779 0.2546
REMARK 3 4 2.5424 - 2.3099 0.92 6112 208 0.1734 0.2083
REMARK 3 5 2.3099 - 2.1444 0.92 6134 200 0.1670 0.1974
REMARK 3 6 2.1444 - 2.0179 0.92 6099 200 0.1689 0.2403
REMARK 3 7 2.0179 - 1.9169 0.92 6067 205 0.1801 0.2494
REMARK 3 8 1.9169 - 1.8334 0.86 5696 190 0.1762 0.2212
REMARK 3 9 1.8334 - 1.7628 0.84 5573 186 0.1815 0.2355
REMARK 3 10 1.7628 - 1.7020 0.85 5591 186 0.1962 0.2522
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.38
REMARK 3 B_SOL : 41.67
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.310
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.75720
REMARK 3 B22 (A**2) : -5.75720
REMARK 3 B33 (A**2) : 11.51430
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 4934
REMARK 3 ANGLE : 0.993 6694
REMARK 3 CHIRALITY : 0.064 794
REMARK 3 PLANARITY : 0.004 890
REMARK 3 DIHEDRAL : 13.058 1784
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 24
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 6:31)
REMARK 3 ORIGIN FOR THE GROUP (A): 56.2859 19.8637 13.5725
REMARK 3 T TENSOR
REMARK 3 T11: 0.2319 T22: 0.1948
REMARK 3 T33: 0.2199 T12: -0.0112
REMARK 3 T13: -0.0067 T23: -0.0410
REMARK 3 L TENSOR
REMARK 3 L11: 0.1528 L22: 1.4672
REMARK 3 L33: 0.2929 L12: 0.3745
REMARK 3 L13: 0.0339 L23: 0.4815
REMARK 3 S TENSOR
REMARK 3 S11: -0.1160 S12: 0.2331 S13: -0.1716
REMARK 3 S21: -0.4294 S22: 0.1815 S23: -0.0924
REMARK 3 S31: -0.0345 S32: 0.0585 S33: -0.0414
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 32:45)
REMARK 3 ORIGIN FOR THE GROUP (A): 56.5998 17.0028 15.2091
REMARK 3 T TENSOR
REMARK 3 T11: 0.2304 T22: 0.2174
REMARK 3 T33: 0.2120 T12: -0.0084
REMARK 3 T13: 0.0320 T23: -0.1092
REMARK 3 L TENSOR
REMARK 3 L11: 1.0835 L22: 0.3882
REMARK 3 L33: 0.0644 L12: 0.0706
REMARK 3 L13: -0.0128 L23: -0.0264
REMARK 3 S TENSOR
REMARK 3 S11: 0.0749 S12: 0.1749 S13: -0.2777
REMARK 3 S21: -0.2658 S22: 0.0235 S23: -0.1075
REMARK 3 S31: -0.0095 S32: 0.0132 S33: -0.0538
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 46:64)
REMARK 3 ORIGIN FOR THE GROUP (A): 51.2209 9.7187 22.5192
REMARK 3 T TENSOR
REMARK 3 T11: 0.1542 T22: 0.1352
REMARK 3 T33: 0.2872 T12: -0.0028
REMARK 3 T13: -0.0426 T23: -0.0288
REMARK 3 L TENSOR
REMARK 3 L11: 0.7407 L22: 0.5086
REMARK 3 L33: 0.5571 L12: -0.5056
REMARK 3 L13: 0.2114 L23: 0.0143
REMARK 3 S TENSOR
REMARK 3 S11: -0.0173 S12: -0.1257 S13: -0.0424
REMARK 3 S21: -0.1135 S22: 0.1142 S23: 0.0139
REMARK 3 S31: 0.1603 S32: -0.0096 S33: -0.1003
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 65:133)
REMARK 3 ORIGIN FOR THE GROUP (A): 51.7369 25.3870 24.7943
REMARK 3 T TENSOR
REMARK 3 T11: 0.1188 T22: 0.1412
REMARK 3 T33: 0.1500 T12: 0.0021
REMARK 3 T13: -0.0031 T23: -0.0156
REMARK 3 L TENSOR
REMARK 3 L11: 0.7811 L22: 0.3204
REMARK 3 L33: 0.2939 L12: -0.1285
REMARK 3 L13: 0.1310 L23: 0.2310
REMARK 3 S TENSOR
REMARK 3 S11: 0.0209 S12: -0.0032 S13: -0.0889
REMARK 3 S21: -0.0790 S22: 0.0156 S23: 0.0533
REMARK 3 S31: -0.0246 S32: -0.0277 S33: -0.0307
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 134:150)
REMARK 3 ORIGIN FOR THE GROUP (A): 73.9923 23.0464 20.9916
REMARK 3 T TENSOR
REMARK 3 T11: 0.1635 T22: 0.2057
REMARK 3 T33: 0.3242 T12: 0.0181
REMARK 3 T13: 0.0411 T23: -0.0672
REMARK 3 L TENSOR
REMARK 3 L11: 0.1088 L22: 2.4549
REMARK 3 L33: 0.3100 L12: 0.4556
REMARK 3 L13: -0.1593 L23: -0.6176
REMARK 3 S TENSOR
REMARK 3 S11: -0.2091 S12: 0.0358 S13: -0.1310
REMARK 3 S21: -0.2294 S22: 0.1725 S23: -0.7381
REMARK 3 S31: 0.1855 S32: -0.0202 S33: 0.0303
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 151:169)
REMARK 3 ORIGIN FOR THE GROUP (A): 71.4235 44.5994 8.8710
REMARK 3 T TENSOR
REMARK 3 T11: 0.2146 T22: 0.2778
REMARK 3 T33: 0.2509 T12: -0.0060
REMARK 3 T13: 0.0391 T23: -0.0361
REMARK 3 L TENSOR
REMARK 3 L11: 2.8896 L22: 3.4414
REMARK 3 L33: 0.0980 L12: -2.6984
REMARK 3 L13: 0.1284 L23: -0.2675
REMARK 3 S TENSOR
REMARK 3 S11: 0.0391 S12: 0.6106 S13: -0.1146
REMARK 3 S21: -0.2010 S22: -0.2407 S23: 0.0913
REMARK 3 S31: -0.0505 S32: -0.0196 S33: 0.1730
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN B AND RESID 7:31)
REMARK 3 ORIGIN FOR THE GROUP (A): 64.8482 56.1777 13.9790
REMARK 3 T TENSOR
REMARK 3 T11: 0.2219 T22: 0.1949
REMARK 3 T33: 0.1952 T12: -0.0027
REMARK 3 T13: 0.0578 T23: 0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 1.3684 L22: 0.2488
REMARK 3 L33: 0.3464 L12: 0.0298
REMARK 3 L13: -0.2903 L23: -0.2371
REMARK 3 S TENSOR
REMARK 3 S11: 0.2232 S12: 0.2895 S13: 0.0847
REMARK 3 S21: -0.2314 S22: -0.0683 S23: -0.0171
REMARK 3 S31: -0.0132 S32: -0.0007 S33: -0.1056
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN B AND RESID 32:42)
REMARK 3 ORIGIN FOR THE GROUP (A): 68.4561 60.6814 14.5510
REMARK 3 T TENSOR
REMARK 3 T11: 0.2257 T22: 0.1903
REMARK 3 T33: 0.3254 T12: -0.0169
REMARK 3 T13: 0.1094 T23: 0.0448
REMARK 3 L TENSOR
REMARK 3 L11: 1.6979 L22: 3.5779
REMARK 3 L33: 0.1927 L12: -2.3465
REMARK 3 L13: -0.0391 L23: 0.3068
REMARK 3 S TENSOR
REMARK 3 S11: 0.1002 S12: 0.2392 S13: 0.5159
REMARK 3 S21: -0.4786 S22: -0.0192 S23: -0.7116
REMARK 3 S31: -0.1233 S32: -0.0644 S33: -0.0757
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN B AND RESID 43:64)
REMARK 3 ORIGIN FOR THE GROUP (A): 74.4881 49.4681 22.9868
REMARK 3 T TENSOR
REMARK 3 T11: 0.1528 T22: 0.1834
REMARK 3 T33: 0.3173 T12: -0.0076
REMARK 3 T13: 0.0420 T23: -0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 0.2540 L22: 0.5979
REMARK 3 L33: 0.4118 L12: 0.0459
REMARK 3 L13: -0.2840 L23: 0.0501
REMARK 3 S TENSOR
REMARK 3 S11: 0.1267 S12: -0.0298 S13: 0.0466
REMARK 3 S21: 0.0217 S22: -0.0907 S23: -0.2041
REMARK 3 S31: -0.0082 S32: 0.0524 S33: -0.0388
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN B AND RESID 65:133)
REMARK 3 ORIGIN FOR THE GROUP (A): 59.9882 51.9166 25.2710
REMARK 3 T TENSOR
REMARK 3 T11: 0.1456 T22: 0.1273
REMARK 3 T33: 0.1782 T12: -0.0135
REMARK 3 T13: 0.0165 T23: -0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 0.1950 L22: 0.2585
REMARK 3 L33: 0.3860 L12: -0.2117
REMARK 3 L13: -0.1203 L23: 0.1298
REMARK 3 S TENSOR
REMARK 3 S11: 0.0213 S12: 0.0637 S13: 0.0427
REMARK 3 S21: -0.0769 S22: 0.0200 S23: -0.0734
REMARK 3 S31: 0.0418 S32: -0.0151 S33: -0.0396
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN B AND RESID 134:153)
REMARK 3 ORIGIN FOR THE GROUP (A): 60.6200 74.4830 21.2426
REMARK 3 T TENSOR
REMARK 3 T11: 0.2448 T22: 0.1470
REMARK 3 T33: 0.4142 T12: -0.0204
REMARK 3 T13: 0.0069 T23: 0.0631
REMARK 3 L TENSOR
REMARK 3 L11: 1.1332 L22: 0.5980
REMARK 3 L33: 0.1208 L12: -0.7521
REMARK 3 L13: 0.0571 L23: -0.1467
REMARK 3 S TENSOR
REMARK 3 S11: 0.0591 S12: 0.0933 S13: 0.6616
REMARK 3 S21: 0.1869 S22: -0.1535 S23: -0.5342
REMARK 3 S31: -0.1443 S32: 0.1231 S33: 0.0953
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN B AND RESID 154:173)
REMARK 3 ORIGIN FOR THE GROUP (A): 35.1649 73.0994 8.4001
REMARK 3 T TENSOR
REMARK 3 T11: 0.2653 T22: 0.2504
REMARK 3 T33: 0.3474 T12: 0.0046
REMARK 3 T13: -0.0029 T23: 0.1033
REMARK 3 L TENSOR
REMARK 3 L11: 1.0366 L22: 2.1462
REMARK 3 L33: 0.0894 L12: 1.4580
REMARK 3 L13: 0.0488 L23: 0.0291
REMARK 3 S TENSOR
REMARK 3 S11: -0.0072 S12: 0.3397 S13: 0.3212
REMARK 3 S21: -0.1406 S22: 0.0043 S23: 0.4508
REMARK 3 S31: 0.2708 S32: -0.0585 S33: -0.0183
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN C AND RESID 4:31)
REMARK 3 ORIGIN FOR THE GROUP (A): 66.8863 28.3536 43.4071
REMARK 3 T TENSOR
REMARK 3 T11: 0.1671 T22: 0.2058
REMARK 3 T33: 0.1817 T12: 0.0037
REMARK 3 T13: -0.0484 T23: 0.0132
REMARK 3 L TENSOR
REMARK 3 L11: 0.8106 L22: 0.9736
REMARK 3 L33: 1.0533 L12: -0.3988
REMARK 3 L13: 0.8245 L23: -0.7671
REMARK 3 S TENSOR
REMARK 3 S11: 0.0671 S12: -0.2883 S13: -0.0447
REMARK 3 S21: 0.3226 S22: 0.0252 S23: -0.2135
REMARK 3 S31: 0.0194 S32: -0.0479 S33: -0.0536
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN C AND RESID 32:41)
REMARK 3 ORIGIN FOR THE GROUP (A): 68.9732 23.4487 42.8385
REMARK 3 T TENSOR
REMARK 3 T11: 0.1922 T22: 0.2025
REMARK 3 T33: 0.2523 T12: 0.0215
REMARK 3 T13: -0.0751 T23: 0.0376
REMARK 3 L TENSOR
REMARK 3 L11: 0.2284 L22: 0.5686
REMARK 3 L33: 0.0817 L12: -0.0896
REMARK 3 L13: -0.0896 L23: 0.0130
REMARK 3 S TENSOR
REMARK 3 S11: -0.0495 S12: -0.2933 S13: -0.1413
REMARK 3 S21: 0.2525 S22: 0.0709 S23: -0.2028
REMARK 3 S31: 0.0456 S32: -0.0318 S33: -0.0135
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN C AND RESID 42:64)
REMARK 3 ORIGIN FOR THE GROUP (A): 74.6380 35.9979 33.9202
REMARK 3 T TENSOR
REMARK 3 T11: 0.1334 T22: 0.1787
REMARK 3 T33: 0.3135 T12: 0.0037
REMARK 3 T13: -0.0133 T23: -0.0253
REMARK 3 L TENSOR
REMARK 3 L11: 0.2367 L22: 1.1173
REMARK 3 L33: 0.4592 L12: 0.2658
REMARK 3 L13: 0.1618 L23: -0.0093
REMARK 3 S TENSOR
REMARK 3 S11: 0.0348 S12: 0.0050 S13: 0.0189
REMARK 3 S21: 0.0464 S22: -0.0595 S23: -0.2947
REMARK 3 S31: -0.0341 S32: 0.1824 S33: 0.0176
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN C AND RESID 65:133)
REMARK 3 ORIGIN FOR THE GROUP (A): 60.1303 33.4875 32.2737
REMARK 3 T TENSOR
REMARK 3 T11: 0.1185 T22: 0.1293
REMARK 3 T33: 0.1315 T12: 0.0040
REMARK 3 T13: -0.0011 T23: -0.0099
REMARK 3 L TENSOR
REMARK 3 L11: 0.4256 L22: 0.5188
REMARK 3 L33: 0.2100 L12: 0.0175
REMARK 3 L13: 0.2365 L23: 0.0801
REMARK 3 S TENSOR
REMARK 3 S11: -0.0112 S12: -0.1039 S13: 0.0012
REMARK 3 S21: 0.0336 S22: 0.0329 S23: -0.0428
REMARK 3 S31: -0.0761 S32: 0.0038 S33: -0.0178
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (CHAIN C AND RESID 134:152)
REMARK 3 ORIGIN FOR THE GROUP (A): 61.4389 10.6803 35.9582
REMARK 3 T TENSOR
REMARK 3 T11: 0.1768 T22: 0.1710
REMARK 3 T33: 0.3056 T12: 0.0298
REMARK 3 T13: -0.0254 T23: 0.0493
REMARK 3 L TENSOR
REMARK 3 L11: 0.8182 L22: 0.1129
REMARK 3 L33: 0.2411 L12: 0.1126
REMARK 3 L13: 0.0248 L23: 0.1272
REMARK 3 S TENSOR
REMARK 3 S11: 0.1679 S12: -0.2069 S13: -0.3991
REMARK 3 S21: 0.0512 S22: -0.0977 S23: -0.1521
REMARK 3 S31: 0.0561 S32: 0.1570 S33: -0.0451
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (CHAIN C AND RESID 153:173)
REMARK 3 ORIGIN FOR THE GROUP (A): 36.3790 12.0884 49.3532
REMARK 3 T TENSOR
REMARK 3 T11: 0.2579 T22: 0.2699
REMARK 3 T33: 0.3260 T12: 0.0224
REMARK 3 T13: 0.0452 T23: 0.1110
REMARK 3 L TENSOR
REMARK 3 L11: 0.3720 L22: 1.0144
REMARK 3 L33: 1.0819 L12: -0.2153
REMARK 3 L13: -0.5510 L23: 0.2077
REMARK 3 S TENSOR
REMARK 3 S11: 0.0476 S12: -0.0679 S13: -0.0926
REMARK 3 S21: 0.3102 S22: -0.1278 S23: 0.3367
REMARK 3 S31: -0.1784 S32: -0.3002 S33: 0.0304
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: (CHAIN D AND RESID 1:24)
REMARK 3 ORIGIN FOR THE GROUP (A): 28.7147 16.9252 44.4044
REMARK 3 T TENSOR
REMARK 3 T11: 0.1932 T22: 0.2056
REMARK 3 T33: 0.2595 T12: 0.0015
REMARK 3 T13: 0.0314 T23: 0.0930
REMARK 3 L TENSOR
REMARK 3 L11: 0.2641 L22: 1.2472
REMARK 3 L33: 0.5480 L12: -0.5319
REMARK 3 L13: 0.0777 L23: -0.4624
REMARK 3 S TENSOR
REMARK 3 S11: -0.1232 S12: -0.1758 S13: -0.1068
REMARK 3 S21: 0.2703 S22: 0.2477 S23: 0.3912
REMARK 3 S31: -0.0650 S32: -0.1095 S33: -0.1068
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: (CHAIN D AND RESID 25:41)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.9236 18.2665 44.0370
REMARK 3 T TENSOR
REMARK 3 T11: 0.1914 T22: 0.2125
REMARK 3 T33: 0.2573 T12: 0.0085
REMARK 3 T13: 0.0589 T23: 0.1359
REMARK 3 L TENSOR
REMARK 3 L11: 2.8002 L22: 0.2821
REMARK 3 L33: 1.1112 L12: -0.5881
REMARK 3 L13: 0.1057 L23: -0.1476
REMARK 3 S TENSOR
REMARK 3 S11: -0.0642 S12: -0.3070 S13: -0.5279
REMARK 3 S21: 0.2286 S22: 0.1993 S23: 0.3688
REMARK 3 S31: -0.1371 S32: -0.1510 S33: -0.0313
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: (CHAIN D AND RESID 42:64)
REMARK 3 ORIGIN FOR THE GROUP (A): 36.7207 11.0214 34.2092
REMARK 3 T TENSOR
REMARK 3 T11: 0.1556 T22: 0.1201
REMARK 3 T33: 0.3049 T12: -0.0022
REMARK 3 T13: -0.0276 T23: 0.0373
REMARK 3 L TENSOR
REMARK 3 L11: 0.4953 L22: 0.9775
REMARK 3 L33: 0.8353 L12: -0.4798
REMARK 3 L13: 0.4004 L23: -0.8980
REMARK 3 S TENSOR
REMARK 3 S11: -0.0040 S12: 0.0695 S13: -0.2372
REMARK 3 S21: -0.1837 S22: 0.0213 S23: 0.0836
REMARK 3 S31: 0.1947 S32: 0.0265 S33: -0.0214
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: (CHAIN D AND RESID 65:133)
REMARK 3 ORIGIN FOR THE GROUP (A): 33.6699 25.1701 32.6302
REMARK 3 T TENSOR
REMARK 3 T11: 0.1168 T22: 0.1382
REMARK 3 T33: 0.1683 T12: -0.0133
REMARK 3 T13: -0.0153 T23: 0.0246
REMARK 3 L TENSOR
REMARK 3 L11: 0.2527 L22: 0.4573
REMARK 3 L33: 0.3706 L12: -0.3279
REMARK 3 L13: 0.1226 L23: -0.2646
REMARK 3 S TENSOR
REMARK 3 S11: 0.0277 S12: -0.0059 S13: -0.1257
REMARK 3 S21: -0.0418 S22: 0.0410 S23: 0.0300
REMARK 3 S31: 0.0008 S32: 0.0397 S33: -0.0608
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: (CHAIN D AND RESID 134:149)
REMARK 3 ORIGIN FOR THE GROUP (A): 11.3261 21.9885 36.2399
REMARK 3 T TENSOR
REMARK 3 T11: 0.1407 T22: 0.2215
REMARK 3 T33: 0.5369 T12: -0.0514
REMARK 3 T13: 0.0206 T23: 0.1585
REMARK 3 L TENSOR
REMARK 3 L11: 0.0477 L22: 0.9082
REMARK 3 L33: 0.0776 L12: -0.0316
REMARK 3 L13: 0.0188 L23: -0.1986
REMARK 3 S TENSOR
REMARK 3 S11: -0.2433 S12: -0.0526 S13: -0.3085
REMARK 3 S21: 0.0679 S22: 0.3752 S23: 0.7800
REMARK 3 S31: 0.2719 S32: -0.0091 S33: -0.1432
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: (CHAIN D AND RESID 150:168)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.6274 42.8273 48.6350
REMARK 3 T TENSOR
REMARK 3 T11: 0.2322 T22: 0.3555
REMARK 3 T33: 0.2753 T12: -0.0446
REMARK 3 T13: 0.0493 T23: 0.0222
REMARK 3 L TENSOR
REMARK 3 L11: 3.2715 L22: 0.8110
REMARK 3 L33: 0.2103 L12: 1.2219
REMARK 3 L13: -0.7059 L23: -0.3511
REMARK 3 S TENSOR
REMARK 3 S11: 0.0643 S12: -0.7618 S13: 0.0971
REMARK 3 S21: 0.2266 S22: -0.1475 S23: 0.2268
REMARK 3 S31: 0.1815 S32: 0.1340 S33: 0.0586
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 3LP6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-FEB-10.
REMARK 100 THE DEPOSITION ID IS D_1000057556.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-JAN-09
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.4
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63825
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.1
REMARK 200 DATA REDUNDANCY : 18.60
REMARK 200 R MERGE (I) : 0.10800
REMARK 200 R SYM (I) : 0.10800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.00
REMARK 200 R MERGE FOR SHELL (I) : 0.46300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
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 1O4VA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NA ACETATE PH5.4, 1.7M NA
REMARK 280 FORMATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 72.84800
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 72.84800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 29.19200
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 72.84800
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 72.84800
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 29.19200
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 72.84800
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 72.84800
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 29.19200
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 72.84800
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 72.84800
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 29.19200
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 42310 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -239.0 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 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 58.38400
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 58.38400
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 PRO A 3
REMARK 465 ALA A 4
REMARK 465 GLY A 5
REMARK 465 LYS A 170
REMARK 465 LEU A 171
REMARK 465 THR A 172
REMARK 465 ARG A 173
REMARK 465 ASP A 174
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 PRO B 3
REMARK 465 ALA B 4
REMARK 465 GLY B 5
REMARK 465 GLU B 6
REMARK 465 ASP B 174
REMARK 465 MET C 1
REMARK 465 THR C 2
REMARK 465 PRO C 3
REMARK 465 ASP C 174
REMARK 465 GLY D 169
REMARK 465 LYS D 170
REMARK 465 LEU D 171
REMARK 465 THR D 172
REMARK 465 ARG D 173
REMARK 465 ASP D 174
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 LEU A 98 -0.53 82.09
REMARK 500 GLN A 109 37.90 -81.17
REMARK 500 ALA A 168 21.75 -76.71
REMARK 500 LEU B 95 -159.87 -101.47
REMARK 500 LEU B 98 -1.77 81.27
REMARK 500 GLN B 109 35.32 -83.79
REMARK 500 LEU C 95 -162.04 -102.49
REMARK 500 LEU C 98 -0.79 83.65
REMARK 500 GLN C 109 35.61 -79.74
REMARK 500 LEU D 98 -1.98 84.28
REMARK 500 GLN D 109 39.02 -79.23
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 175
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 176
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 177
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 178
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 175
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 176
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 177
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 178
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 179
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 180
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 181
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 182
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 175
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 176
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 177
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 178
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 179
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 175
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 176
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 177
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 178
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 179
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 180
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 181
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: RV3275C RELATED DB: TARGETDB
DBREF 3LP6 A 1 174 UNP P96880 PUR6_MYCTU 1 174
DBREF 3LP6 B 1 174 UNP P96880 PUR6_MYCTU 1 174
DBREF 3LP6 C 1 174 UNP P96880 PUR6_MYCTU 1 174
DBREF 3LP6 D 1 174 UNP P96880 PUR6_MYCTU 1 174
SEQADV 3LP6 ALA A 60 UNP P96880 GLU 60 ENGINEERED MUTATION
SEQADV 3LP6 ALA B 60 UNP P96880 GLU 60 ENGINEERED MUTATION
SEQADV 3LP6 ALA C 60 UNP P96880 GLU 60 ENGINEERED MUTATION
SEQADV 3LP6 ALA D 60 UNP P96880 GLU 60 ENGINEERED MUTATION
SEQRES 1 A 174 MET THR PRO ALA GLY GLU ARG PRO ARG VAL GLY VAL ILE
SEQRES 2 A 174 MET GLY SER ASP SER ASP TRP PRO VAL MET ALA ASP ALA
SEQRES 3 A 174 ALA ALA ALA LEU ALA GLU PHE ASP ILE PRO ALA GLU VAL
SEQRES 4 A 174 ARG VAL VAL SER ALA HIS ARG THR PRO GLU ALA MET PHE
SEQRES 5 A 174 SER TYR ALA ARG GLY ALA ALA ALA ARG GLY LEU GLU VAL
SEQRES 6 A 174 ILE ILE ALA GLY ALA GLY GLY ALA ALA HIS LEU PRO GLY
SEQRES 7 A 174 MET VAL ALA ALA ALA THR PRO LEU PRO VAL ILE GLY VAL
SEQRES 8 A 174 PRO VAL PRO LEU GLY ARG LEU ASP GLY LEU ASP SER LEU
SEQRES 9 A 174 LEU SER ILE VAL GLN MET PRO ALA GLY VAL PRO VAL ALA
SEQRES 10 A 174 THR VAL SER ILE GLY GLY ALA GLY ASN ALA GLY LEU LEU
SEQRES 11 A 174 ALA VAL ARG MET LEU GLY ALA ALA ASN PRO GLN LEU ARG
SEQRES 12 A 174 ALA ARG ILE VAL ALA PHE GLN ASP ARG LEU ALA ASP VAL
SEQRES 13 A 174 VAL ALA ALA LYS ASP ALA GLU LEU GLN ARG LEU ALA GLY
SEQRES 14 A 174 LYS LEU THR ARG ASP
SEQRES 1 B 174 MET THR PRO ALA GLY GLU ARG PRO ARG VAL GLY VAL ILE
SEQRES 2 B 174 MET GLY SER ASP SER ASP TRP PRO VAL MET ALA ASP ALA
SEQRES 3 B 174 ALA ALA ALA LEU ALA GLU PHE ASP ILE PRO ALA GLU VAL
SEQRES 4 B 174 ARG VAL VAL SER ALA HIS ARG THR PRO GLU ALA MET PHE
SEQRES 5 B 174 SER TYR ALA ARG GLY ALA ALA ALA ARG GLY LEU GLU VAL
SEQRES 6 B 174 ILE ILE ALA GLY ALA GLY GLY ALA ALA HIS LEU PRO GLY
SEQRES 7 B 174 MET VAL ALA ALA ALA THR PRO LEU PRO VAL ILE GLY VAL
SEQRES 8 B 174 PRO VAL PRO LEU GLY ARG LEU ASP GLY LEU ASP SER LEU
SEQRES 9 B 174 LEU SER ILE VAL GLN MET PRO ALA GLY VAL PRO VAL ALA
SEQRES 10 B 174 THR VAL SER ILE GLY GLY ALA GLY ASN ALA GLY LEU LEU
SEQRES 11 B 174 ALA VAL ARG MET LEU GLY ALA ALA ASN PRO GLN LEU ARG
SEQRES 12 B 174 ALA ARG ILE VAL ALA PHE GLN ASP ARG LEU ALA ASP VAL
SEQRES 13 B 174 VAL ALA ALA LYS ASP ALA GLU LEU GLN ARG LEU ALA GLY
SEQRES 14 B 174 LYS LEU THR ARG ASP
SEQRES 1 C 174 MET THR PRO ALA GLY GLU ARG PRO ARG VAL GLY VAL ILE
SEQRES 2 C 174 MET GLY SER ASP SER ASP TRP PRO VAL MET ALA ASP ALA
SEQRES 3 C 174 ALA ALA ALA LEU ALA GLU PHE ASP ILE PRO ALA GLU VAL
SEQRES 4 C 174 ARG VAL VAL SER ALA HIS ARG THR PRO GLU ALA MET PHE
SEQRES 5 C 174 SER TYR ALA ARG GLY ALA ALA ALA ARG GLY LEU GLU VAL
SEQRES 6 C 174 ILE ILE ALA GLY ALA GLY GLY ALA ALA HIS LEU PRO GLY
SEQRES 7 C 174 MET VAL ALA ALA ALA THR PRO LEU PRO VAL ILE GLY VAL
SEQRES 8 C 174 PRO VAL PRO LEU GLY ARG LEU ASP GLY LEU ASP SER LEU
SEQRES 9 C 174 LEU SER ILE VAL GLN MET PRO ALA GLY VAL PRO VAL ALA
SEQRES 10 C 174 THR VAL SER ILE GLY GLY ALA GLY ASN ALA GLY LEU LEU
SEQRES 11 C 174 ALA VAL ARG MET LEU GLY ALA ALA ASN PRO GLN LEU ARG
SEQRES 12 C 174 ALA ARG ILE VAL ALA PHE GLN ASP ARG LEU ALA ASP VAL
SEQRES 13 C 174 VAL ALA ALA LYS ASP ALA GLU LEU GLN ARG LEU ALA GLY
SEQRES 14 C 174 LYS LEU THR ARG ASP
SEQRES 1 D 174 MET THR PRO ALA GLY GLU ARG PRO ARG VAL GLY VAL ILE
SEQRES 2 D 174 MET GLY SER ASP SER ASP TRP PRO VAL MET ALA ASP ALA
SEQRES 3 D 174 ALA ALA ALA LEU ALA GLU PHE ASP ILE PRO ALA GLU VAL
SEQRES 4 D 174 ARG VAL VAL SER ALA HIS ARG THR PRO GLU ALA MET PHE
SEQRES 5 D 174 SER TYR ALA ARG GLY ALA ALA ALA ARG GLY LEU GLU VAL
SEQRES 6 D 174 ILE ILE ALA GLY ALA GLY GLY ALA ALA HIS LEU PRO GLY
SEQRES 7 D 174 MET VAL ALA ALA ALA THR PRO LEU PRO VAL ILE GLY VAL
SEQRES 8 D 174 PRO VAL PRO LEU GLY ARG LEU ASP GLY LEU ASP SER LEU
SEQRES 9 D 174 LEU SER ILE VAL GLN MET PRO ALA GLY VAL PRO VAL ALA
SEQRES 10 D 174 THR VAL SER ILE GLY GLY ALA GLY ASN ALA GLY LEU LEU
SEQRES 11 D 174 ALA VAL ARG MET LEU GLY ALA ALA ASN PRO GLN LEU ARG
SEQRES 12 D 174 ALA ARG ILE VAL ALA PHE GLN ASP ARG LEU ALA ASP VAL
SEQRES 13 D 174 VAL ALA ALA LYS ASP ALA GLU LEU GLN ARG LEU ALA GLY
SEQRES 14 D 174 LYS LEU THR ARG ASP
HET FMT A 175 3
HET FMT A 176 3
HET FMT A 177 3
HET FMT A 178 3
HET GOL B 175 6
HET FMT B 176 3
HET FMT B 177 3
HET FMT B 178 3
HET FMT B 179 3
HET FMT B 180 3
HET FMT B 181 3
HET FMT B 182 3
HET GOL C 175 6
HET FMT C 176 3
HET FMT C 177 3
HET FMT C 178 3
HET FMT C 179 3
HET FMT D 175 3
HET FMT D 176 3
HET FMT D 177 3
HET FMT D 178 3
HET FMT D 179 3
HET FMT D 180 3
HET FMT D 181 3
HETNAM FMT FORMIC ACID
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 FMT 22(C H2 O2)
FORMUL 9 GOL 2(C3 H8 O3)
FORMUL 29 HOH *408(H2 O)
HELIX 1 1 SER A 16 SER A 18 5 3
HELIX 2 2 ASP A 19 PHE A 33 1 15
HELIX 3 3 THR A 47 GLY A 62 1 16
HELIX 4 4 HIS A 75 THR A 84 1 10
HELIX 5 5 ARG A 97 ASP A 99 5 3
HELIX 6 6 GLY A 100 GLN A 109 1 10
HELIX 7 7 GLY A 123 ALA A 137 1 15
HELIX 8 8 ASN A 139 ALA A 168 1 30
HELIX 9 9 SER B 16 SER B 18 5 3
HELIX 10 10 ASP B 19 PHE B 33 1 15
HELIX 11 11 THR B 47 ALA B 58 1 12
HELIX 12 12 HIS B 75 THR B 84 1 10
HELIX 13 13 ARG B 97 ASP B 99 5 3
HELIX 14 14 GLY B 100 GLN B 109 1 10
HELIX 15 15 GLY B 123 ALA B 137 1 15
HELIX 16 16 ASN B 139 ARG B 173 1 35
HELIX 17 17 SER C 16 SER C 18 5 3
HELIX 18 18 ASP C 19 PHE C 33 1 15
HELIX 19 19 THR C 47 ALA C 58 1 12
HELIX 20 20 ALA C 59 GLY C 62 5 4
HELIX 21 21 HIS C 75 ALA C 83 1 9
HELIX 22 22 ARG C 97 ASP C 99 5 3
HELIX 23 23 GLY C 100 GLN C 109 1 10
HELIX 24 24 GLY C 123 ALA C 137 1 15
HELIX 25 25 ASN C 139 ARG C 173 1 35
HELIX 26 26 SER D 16 SER D 18 5 3
HELIX 27 27 ASP D 19 PHE D 33 1 15
HELIX 28 28 THR D 47 ALA D 58 1 12
HELIX 29 29 ALA D 59 GLY D 62 5 4
HELIX 30 30 HIS D 75 ALA D 82 1 8
HELIX 31 31 ARG D 97 ASP D 99 5 3
HELIX 32 32 GLY D 100 GLN D 109 1 10
HELIX 33 33 GLY D 123 ALA D 137 1 15
HELIX 34 34 ASN D 139 ALA D 168 1 30
SHEET 1 A 5 ALA A 37 VAL A 41 0
SHEET 2 A 5 VAL A 10 MET A 14 1 N VAL A 12 O GLU A 38
SHEET 3 A 5 VAL A 65 GLY A 71 1 O ILE A 67 N GLY A 11
SHEET 4 A 5 VAL A 88 VAL A 93 1 O ILE A 89 N ALA A 68
SHEET 5 A 5 ALA A 117 THR A 118 1 O ALA A 117 N VAL A 88
SHEET 1 B 5 ALA B 37 VAL B 41 0
SHEET 2 B 5 VAL B 10 MET B 14 1 N VAL B 12 O GLU B 38
SHEET 3 B 5 VAL B 65 GLY B 71 1 O ILE B 67 N GLY B 11
SHEET 4 B 5 VAL B 88 VAL B 93 1 O ILE B 89 N ALA B 68
SHEET 5 B 5 ALA B 117 THR B 118 1 O ALA B 117 N GLY B 90
SHEET 1 C 5 ALA C 37 VAL C 41 0
SHEET 2 C 5 VAL C 10 MET C 14 1 N VAL C 12 O GLU C 38
SHEET 3 C 5 VAL C 65 GLY C 71 1 O ILE C 67 N GLY C 11
SHEET 4 C 5 VAL C 88 VAL C 93 1 O ILE C 89 N ALA C 68
SHEET 5 C 5 ALA C 117 THR C 118 1 O ALA C 117 N VAL C 88
SHEET 1 D 5 ALA D 37 VAL D 41 0
SHEET 2 D 5 VAL D 10 MET D 14 1 N VAL D 12 O GLU D 38
SHEET 3 D 5 VAL D 65 GLY D 71 1 O ILE D 67 N GLY D 11
SHEET 4 D 5 VAL D 88 VAL D 93 1 O ILE D 89 N ALA D 68
SHEET 5 D 5 ALA D 117 THR D 118 1 O ALA D 117 N GLY D 90
SITE 1 AC1 2 ASP A 19 GLY A 71
SITE 1 AC2 4 ARG A 56 ALA A 82 HOH C 325 FMT D 175
SITE 1 AC3 7 GLY A 15 SER A 43 ALA A 44 HIS A 45
SITE 2 AC3 7 ARG A 46 HOH A 188 HOH A 400
SITE 1 AC4 5 THR A 47 PRO A 48 GLU A 49 ALA A 50
SITE 2 AC4 5 HOH A 224
SITE 1 AC5 5 GLY B 15 ASP B 19 ALA B 70 GLY B 71
SITE 2 AC5 5 LEU B 95
SITE 1 AC6 5 FMT B 178 THR C 47 PRO C 48 GLU C 49
SITE 2 AC6 5 ALA C 50
SITE 1 AC7 7 THR B 47 PRO B 48 GLU B 49 ALA B 50
SITE 2 AC7 7 GOL C 175 HOH C 238 HOH C 355
SITE 1 AC8 3 ARG B 56 ALA B 82 FMT B 176
SITE 1 AC9 1 VAL B 41
SITE 1 BC1 7 GLY B 15 SER B 43 ALA B 44 HIS B 45
SITE 2 BC1 7 ARG B 46 FMT B 182 HOH B 187
SITE 1 BC2 5 LYS A 160 SER B 16 ASP B 17 ARG B 46
SITE 2 BC2 5 HOH B 349
SITE 1 BC3 6 HIS B 45 ARG B 46 FMT B 180 HOH B 209
SITE 2 BC3 6 PRO C 111 HOH C 211
SITE 1 BC4 11 GLN A 150 ASP A 151 HOH A 192 HOH A 285
SITE 2 BC4 11 PRO B 48 FMT B 177 ARG C 56 ALA C 82
SITE 3 BC4 11 ALA C 83 HOH C 204 HOH C 332
SITE 1 BC5 3 ASP C 19 ALA C 70 GLY C 71
SITE 1 BC6 5 GLU C 32 PHE C 33 ARG C 145 ARG C 152
SITE 2 BC6 5 HOH C 209
SITE 1 BC7 4 LYS B 160 SER C 16 ASP C 17 ARG C 46
SITE 1 BC8 6 GLY C 15 SER C 43 ALA C 44 HIS C 45
SITE 2 BC8 6 HOH C 193 HOH C 407
SITE 1 BC9 5 FMT A 176 THR D 47 PRO D 48 GLU D 49
SITE 2 BC9 5 ALA D 50
SITE 1 CC1 5 GLY D 15 SER D 43 ALA D 44 HIS D 45
SITE 2 CC1 5 HOH D 202
SITE 1 CC2 3 VAL A 41 HOH A 323 HOH D 329
SITE 1 CC3 5 HIS A 45 HOH A 210 ALA D 82 GLN D 150
SITE 2 CC3 5 HOH D 243
SITE 1 CC4 2 ASP D 19 GLY D 71
SITE 1 CC5 2 GLU D 32 ARG D 145
SITE 1 CC6 3 GLY D 5 HOH D 233 HOH D 408
CRYST1 145.696 145.696 58.384 90.00 90.00 90.00 P 42 21 2 32
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 0.006864 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006864 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017128 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
