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HEADER HYDROLASE 23-OCT-18 6MUH
TITLE FLUOROACETATE DEHALOGENASE, ROOM TEMPERATURE STRUCTURE SOLVED BY
TITLE 2 SERIAL 1 DEGREE OSCILLATION CRYSTALLOGRAPHY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLUOROACETATE DEHALOGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.8.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOPSEUDOMONAS PALUSTRIS (STRAIN ATCC BAA-98
SOURCE 3 / CGA009);
SOURCE 4 ORGANISM_TAXID: 258594;
SOURCE 5 STRAIN: ATCC BAA-98 / CGA009;
SOURCE 6 GENE: RPA1163;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS DEHALOGENASE, DEFLUORINASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.D.FINKE,J.L.WIERMAN,O.PARE-LABROSSE,A.SARRACHINI,J.BESAW,P.MEHRABI,
AUTHOR 2 S.M.GRUNER,R.J.D.MILLER
REVDAT 1 27-MAR-19 6MUH 0
JRNL AUTH J.L.WIERMAN,O.PARE-LABROSSE,A.SARRACINI,J.E.BESAW,M.J.COOK,
JRNL AUTH 2 S.OGHBAEY,H.DAOUD,P.MEHRABI,I.KRIKSUNOV,A.KUO,D.J.SCHULLER,
JRNL AUTH 3 S.SMITH,O.P.ERNST,D.M.E.SZEBENYI,S.M.GRUNER,R.J.D.MILLER,
JRNL AUTH 4 A.D.FINKE
JRNL TITL FIXED-TARGET SERIAL OSCILLATION CRYSTALLOGRAPHY AT ROOM
JRNL TITL 2 TEMPERATURE.
JRNL REF IUCRJ V. 6 305 2019
JRNL REFN ESSN 2052-2525
JRNL PMID 30867928
JRNL DOI 10.1107/S2052252519001453
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.13_2998: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.83
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 48271
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.153
REMARK 3 R VALUE (WORKING SET) : 0.152
REMARK 3 FREE R VALUE : 0.181
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2413
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 40.8366 - 4.6263 0.99 2762 145 0.1261 0.1491
REMARK 3 2 4.6263 - 3.6728 0.99 2775 146 0.1043 0.1095
REMARK 3 3 3.6728 - 3.2087 0.99 2706 143 0.1165 0.1579
REMARK 3 4 3.2087 - 2.9154 1.00 2767 146 0.1388 0.1455
REMARK 3 5 2.9154 - 2.7065 0.99 2725 143 0.1525 0.2043
REMARK 3 6 2.7065 - 2.5470 0.99 2714 143 0.1499 0.2030
REMARK 3 7 2.5470 - 2.4194 0.99 2697 142 0.1556 0.2041
REMARK 3 8 2.4194 - 2.3141 0.99 2715 143 0.1513 0.1860
REMARK 3 9 2.3141 - 2.2250 0.99 2736 144 0.1665 0.2174
REMARK 3 10 2.2250 - 2.1483 0.99 2699 142 0.1714 0.1951
REMARK 3 11 2.1483 - 2.0811 0.99 2653 140 0.1977 0.2665
REMARK 3 12 2.0811 - 2.0216 0.99 2740 144 0.2224 0.2607
REMARK 3 13 2.0216 - 1.9684 0.98 2660 140 0.2343 0.2693
REMARK 3 14 1.9684 - 1.9204 0.98 2682 141 0.2469 0.3138
REMARK 3 15 1.9204 - 1.8767 0.97 2678 140 0.2760 0.3006
REMARK 3 16 1.8767 - 1.8368 0.97 2629 138 0.3221 0.3231
REMARK 3 17 1.8368 - 1.8000 0.93 2520 133 0.3850 0.4176
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.980
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 4924
REMARK 3 ANGLE : 0.960 6713
REMARK 3 CHIRALITY : 0.051 688
REMARK 3 PLANARITY : 0.006 884
REMARK 3 DIHEDRAL : 16.005 3978
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 15
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 4 THROUGH 63 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.9274 -72.7836 102.8325
REMARK 3 T TENSOR
REMARK 3 T11: 0.2204 T22: 0.2315
REMARK 3 T33: 0.1913 T12: 0.0275
REMARK 3 T13: 0.0028 T23: 0.0514
REMARK 3 L TENSOR
REMARK 3 L11: 1.8434 L22: 3.2586
REMARK 3 L33: 4.3817 L12: -0.1826
REMARK 3 L13: -0.2157 L23: 0.7752
REMARK 3 S TENSOR
REMARK 3 S11: -0.0293 S12: -0.3939 S13: -0.1214
REMARK 3 S21: 0.3097 S22: 0.0491 S23: -0.0787
REMARK 3 S31: 0.4238 S32: 0.1151 S33: -0.0383
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 64 THROUGH 104 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.1513 -64.0500 95.0776
REMARK 3 T TENSOR
REMARK 3 T11: 0.1178 T22: 0.2126
REMARK 3 T33: 0.2446 T12: 0.0167
REMARK 3 T13: 0.0100 T23: -0.0102
REMARK 3 L TENSOR
REMARK 3 L11: 1.5945 L22: 2.3043
REMARK 3 L33: 7.3975 L12: 0.1229
REMARK 3 L13: -0.1507 L23: 0.6494
REMARK 3 S TENSOR
REMARK 3 S11: 0.0464 S12: -0.1315 S13: 0.0192
REMARK 3 S21: 0.0187 S22: -0.0233 S23: 0.1539
REMARK 3 S31: -0.0777 S32: -0.4254 S33: -0.0246
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 105 THROUGH 137 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.6208 -58.2942 96.5973
REMARK 3 T TENSOR
REMARK 3 T11: 0.1545 T22: 0.1841
REMARK 3 T33: 0.1941 T12: 0.0008
REMARK 3 T13: 0.0028 T23: -0.0156
REMARK 3 L TENSOR
REMARK 3 L11: 2.4776 L22: 3.5391
REMARK 3 L33: 5.5206 L12: -0.0167
REMARK 3 L13: 0.1383 L23: 0.5443
REMARK 3 S TENSOR
REMARK 3 S11: 0.0303 S12: -0.2620 S13: 0.2283
REMARK 3 S21: 0.1902 S22: -0.0201 S23: -0.0977
REMARK 3 S31: -0.1634 S32: 0.0143 S33: -0.0096
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 138 THROUGH 164 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.6484 -59.9483 77.5797
REMARK 3 T TENSOR
REMARK 3 T11: 0.2326 T22: 0.1995
REMARK 3 T33: 0.2461 T12: 0.0016
REMARK 3 T13: 0.0014 T23: 0.0130
REMARK 3 L TENSOR
REMARK 3 L11: 0.9795 L22: 0.8265
REMARK 3 L33: 3.9710 L12: -0.4059
REMARK 3 L13: -0.7732 L23: 1.1566
REMARK 3 S TENSOR
REMARK 3 S11: 0.0421 S12: 0.0596 S13: 0.1281
REMARK 3 S21: -0.0279 S22: 0.1732 S23: -0.1073
REMARK 3 S31: -0.0990 S32: 0.4213 S33: -0.2167
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 165 THROUGH 208 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.2901 -77.9560 83.6558
REMARK 3 T TENSOR
REMARK 3 T11: 0.2400 T22: 0.1596
REMARK 3 T33: 0.2683 T12: 0.0313
REMARK 3 T13: 0.0258 T23: -0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 4.0493 L22: 2.2147
REMARK 3 L33: 4.5958 L12: -1.4615
REMARK 3 L13: 2.4370 L23: -0.9387
REMARK 3 S TENSOR
REMARK 3 S11: 0.0178 S12: 0.1869 S13: -0.1468
REMARK 3 S21: -0.0583 S22: 0.0429 S23: -0.1612
REMARK 3 S31: 0.4376 S32: 0.2954 S33: -0.0930
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 209 THROUGH 235 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.6251 -60.6111 83.6430
REMARK 3 T TENSOR
REMARK 3 T11: 0.1811 T22: 0.1598
REMARK 3 T33: 0.2010 T12: 0.0388
REMARK 3 T13: 0.0055 T23: 0.0105
REMARK 3 L TENSOR
REMARK 3 L11: 1.6968 L22: 2.4532
REMARK 3 L33: 2.1216 L12: 1.0003
REMARK 3 L13: 0.6343 L23: 1.3997
REMARK 3 S TENSOR
REMARK 3 S11: -0.0237 S12: 0.0247 S13: 0.1853
REMARK 3 S21: -0.0603 S22: -0.0301 S23: 0.1428
REMARK 3 S31: -0.2130 S32: -0.0704 S33: 0.0421
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 236 THROUGH 276 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.9522 -54.1966 94.0968
REMARK 3 T TENSOR
REMARK 3 T11: 0.2436 T22: 0.3089
REMARK 3 T33: 0.3244 T12: -0.0621
REMARK 3 T13: -0.0077 T23: -0.0416
REMARK 3 L TENSOR
REMARK 3 L11: 6.3840 L22: 7.6337
REMARK 3 L33: 3.3641 L12: -4.2920
REMARK 3 L13: -1.3346 L23: 0.5255
REMARK 3 S TENSOR
REMARK 3 S11: 0.1090 S12: -0.0124 S13: 0.2608
REMARK 3 S21: -0.2144 S22: -0.0681 S23: -0.4332
REMARK 3 S31: -0.2357 S32: 0.5725 S33: -0.0815
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 277 THROUGH 300 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.1993 -67.5644 99.9673
REMARK 3 T TENSOR
REMARK 3 T11: 0.2025 T22: 0.4264
REMARK 3 T33: 0.3033 T12: 0.0415
REMARK 3 T13: -0.0494 T23: 0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 2.8708 L22: 5.1445
REMARK 3 L33: 2.5261 L12: -1.7054
REMARK 3 L13: -1.2936 L23: 2.1769
REMARK 3 S TENSOR
REMARK 3 S11: -0.0175 S12: -0.4427 S13: -0.0314
REMARK 3 S21: 0.5647 S22: 0.2887 S23: -0.4947
REMARK 3 S31: 0.3025 S32: 0.7275 S33: -0.2376
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 4 THROUGH 63 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.3670 -67.8732 41.0846
REMARK 3 T TENSOR
REMARK 3 T11: 0.2772 T22: 0.3525
REMARK 3 T33: 0.1957 T12: -0.0386
REMARK 3 T13: -0.0097 T23: -0.0503
REMARK 3 L TENSOR
REMARK 3 L11: 3.6058 L22: 1.4856
REMARK 3 L33: 4.7310 L12: 0.2100
REMARK 3 L13: -1.3566 L23: -0.3194
REMARK 3 S TENSOR
REMARK 3 S11: 0.0233 S12: 0.5900 S13: -0.1330
REMARK 3 S21: -0.2759 S22: -0.0222 S23: 0.0964
REMARK 3 S31: 0.2701 S32: -0.4742 S33: -0.0142
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 64 THROUGH 104 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.0327 -69.6794 48.8844
REMARK 3 T TENSOR
REMARK 3 T11: 0.1986 T22: 0.2233
REMARK 3 T33: 0.2312 T12: 0.0438
REMARK 3 T13: 0.0298 T23: -0.0284
REMARK 3 L TENSOR
REMARK 3 L11: 2.6831 L22: 3.1491
REMARK 3 L33: 8.3339 L12: 1.3459
REMARK 3 L13: -1.1067 L23: -1.8312
REMARK 3 S TENSOR
REMARK 3 S11: 0.0325 S12: 0.0163 S13: -0.2042
REMARK 3 S21: 0.0458 S22: -0.1161 S23: -0.0963
REMARK 3 S31: 0.4655 S32: 0.4177 S33: 0.0935
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 105 THROUGH 137 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.9848 -57.2613 49.3631
REMARK 3 T TENSOR
REMARK 3 T11: 0.2340 T22: 0.2163
REMARK 3 T33: 0.2014 T12: -0.0246
REMARK 3 T13: 0.0068 T23: 0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 6.2753 L22: 1.8038
REMARK 3 L33: 4.3914 L12: 0.3540
REMARK 3 L13: -1.9289 L23: -0.1966
REMARK 3 S TENSOR
REMARK 3 S11: 0.0685 S12: 0.3084 S13: 0.3663
REMARK 3 S21: -0.0561 S22: 0.0446 S23: -0.0321
REMARK 3 S31: -0.3062 S32: -0.0462 S33: -0.1175
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 138 THROUGH 164 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.9441 -59.6563 67.9584
REMARK 3 T TENSOR
REMARK 3 T11: 0.2262 T22: 0.1827
REMARK 3 T33: 0.1719 T12: -0.0092
REMARK 3 T13: -0.0113 T23: -0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 2.8508 L22: 0.2197
REMARK 3 L33: 4.3118 L12: 0.0350
REMARK 3 L13: -2.2092 L23: 0.7312
REMARK 3 S TENSOR
REMARK 3 S11: 0.1115 S12: 0.1511 S13: 0.2341
REMARK 3 S21: 0.0340 S22: 0.1289 S23: 0.0289
REMARK 3 S31: -0.3891 S32: -0.0164 S33: -0.2509
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 165 THROUGH 208 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.2692 -71.2294 59.3535
REMARK 3 T TENSOR
REMARK 3 T11: 0.2615 T22: 0.2504
REMARK 3 T33: 0.2327 T12: -0.0814
REMARK 3 T13: 0.0358 T23: 0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 8.4093 L22: 1.6077
REMARK 3 L33: 5.5623 L12: -2.4649
REMARK 3 L13: 4.1368 L23: -1.4106
REMARK 3 S TENSOR
REMARK 3 S11: -0.1170 S12: -0.1200 S13: -0.2489
REMARK 3 S21: 0.0262 S22: 0.2445 S23: 0.1269
REMARK 3 S31: 0.2547 S32: -0.4183 S33: -0.1543
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 209 THROUGH 249 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.8668 -60.2617 57.4374
REMARK 3 T TENSOR
REMARK 3 T11: 0.2428 T22: 0.2211
REMARK 3 T33: 0.1803 T12: -0.0113
REMARK 3 T13: 0.0301 T23: -0.0697
REMARK 3 L TENSOR
REMARK 3 L11: 2.2595 L22: 2.2511
REMARK 3 L33: 2.6260 L12: 0.5688
REMARK 3 L13: -0.4827 L23: -1.6746
REMARK 3 S TENSOR
REMARK 3 S11: -0.0062 S12: -0.1845 S13: 0.1257
REMARK 3 S21: 0.0342 S22: -0.0574 S23: -0.1893
REMARK 3 S31: -0.1995 S32: 0.1617 S33: 0.0907
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 250 THROUGH 300 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.2532 -50.9653 50.4122
REMARK 3 T TENSOR
REMARK 3 T11: 0.3394 T22: 0.3301
REMARK 3 T33: 0.3231 T12: 0.0728
REMARK 3 T13: 0.0395 T23: 0.0528
REMARK 3 L TENSOR
REMARK 3 L11: 6.9400 L22: 5.1093
REMARK 3 L33: 2.0429 L12: 3.3319
REMARK 3 L13: 0.2615 L23: 1.2963
REMARK 3 S TENSOR
REMARK 3 S11: 0.2339 S12: -0.0120 S13: 0.5981
REMARK 3 S21: -0.0547 S22: -0.1974 S23: 0.3230
REMARK 3 S31: -0.4138 S32: -0.3891 S33: -0.0228
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 6MUH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-OCT-18.
REMARK 100 THE DEPOSITION ID IS D_1000237576.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-MAR-18
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.2155
REMARK 200 MONOCHROMATOR : W/B4C MULTILAYER
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 1M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48288
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 40.826
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.3300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 6FSX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.5 MM DEFLUORINASE WITH A MOTHER
REMARK 280 LIQUOR OF 16-20% PEG 3350, 100MM TRIS-CL PH 8.5, AND 200MM CACL2,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 39.55000
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 PRO A 2
REMARK 465 ALA A 301
REMARK 465 PRO A 302
REMARK 465 GLY A 303
REMARK 465 SER A 304
REMARK 465 GLY B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 PRO B 2
REMARK 465 ALA B 301
REMARK 465 PRO B 302
REMARK 465 GLY B 303
REMARK 465 SER B 304
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 OE2 GLU A 277 O HOH A 401 2.04
REMARK 500 OE1 GLU A 140 NH2 ARG A 144 2.05
REMARK 500 OE1 GLU B 140 NH2 ARG B 144 2.17
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 PRO A 41 67.08 -102.85
REMARK 500 ASP A 110 -127.74 58.64
REMARK 500 SER A 123 58.77 -143.29
REMARK 500 MET A 145 96.39 -69.47
REMARK 500 ILE A 153 50.77 -112.93
REMARK 500 ASP A 173 69.86 -156.59
REMARK 500 TYR A 224 -91.96 -121.12
REMARK 500 GLU A 277 99.74 -65.72
REMARK 500 ASP B 110 -127.31 57.53
REMARK 500 ILE B 153 50.47 -109.48
REMARK 500 ASP B 173 69.99 -166.52
REMARK 500 TYR B 224 -96.49 -123.62
REMARK 500 GLU B 277 92.62 -67.33
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6MUH A 1 302 UNP Q6NAM1 DEHA_RHOPA 1 302
DBREF 6MUH B 1 302 UNP Q6NAM1 DEHA_RHOPA 1 302
SEQADV 6MUH GLY A -1 UNP Q6NAM1 EXPRESSION TAG
SEQADV 6MUH HIS A 0 UNP Q6NAM1 EXPRESSION TAG
SEQADV 6MUH GLY A 303 UNP Q6NAM1 EXPRESSION TAG
SEQADV 6MUH SER A 304 UNP Q6NAM1 EXPRESSION TAG
SEQADV 6MUH GLY B -1 UNP Q6NAM1 EXPRESSION TAG
SEQADV 6MUH HIS B 0 UNP Q6NAM1 EXPRESSION TAG
SEQADV 6MUH GLY B 303 UNP Q6NAM1 EXPRESSION TAG
SEQADV 6MUH SER B 304 UNP Q6NAM1 EXPRESSION TAG
SEQRES 1 A 306 GLY HIS MET PRO ASP LEU ALA ASP LEU PHE PRO GLY PHE
SEQRES 2 A 306 GLY SER GLU TRP ILE ASN THR SER SER GLY ARG ILE PHE
SEQRES 3 A 306 ALA ARG VAL GLY GLY ASP GLY PRO PRO LEU LEU LEU LEU
SEQRES 4 A 306 HIS GLY PHE PRO GLN THR HIS VAL MET TRP HIS ARG VAL
SEQRES 5 A 306 ALA PRO LYS LEU ALA GLU ARG PHE LYS VAL ILE VAL ALA
SEQRES 6 A 306 ASP LEU PRO GLY TYR GLY TRP SER ASP MET PRO GLU SER
SEQRES 7 A 306 ASP GLU GLN HIS THR PRO TYR THR LYS ARG ALA MET ALA
SEQRES 8 A 306 LYS GLN LEU ILE GLU ALA MET GLU GLN LEU GLY HIS VAL
SEQRES 9 A 306 HIS PHE ALA LEU ALA GLY HIS ASP ARG GLY ALA ARG VAL
SEQRES 10 A 306 SER TYR ARG LEU ALA LEU ASP SER PRO GLY ARG LEU SER
SEQRES 11 A 306 LYS LEU ALA VAL LEU ASP ILE LEU PRO THR TYR GLU TYR
SEQRES 12 A 306 TRP GLN ARG MET ASN ARG ALA TYR ALA LEU LYS ILE TYR
SEQRES 13 A 306 HIS TRP SER PHE LEU ALA GLN PRO ALA PRO LEU PRO GLU
SEQRES 14 A 306 ASN LEU LEU GLY GLY ASP PRO ASP PHE TYR VAL LYS ALA
SEQRES 15 A 306 LYS LEU ALA SER TRP THR ARG ALA GLY ASP LEU SER ALA
SEQRES 16 A 306 PHE ASP PRO ARG ALA VAL GLU HIS TYR ARG ILE ALA PHE
SEQRES 17 A 306 ALA ASP PRO MET ARG ARG HIS VAL MET CYS GLU ASP TYR
SEQRES 18 A 306 ARG ALA GLY ALA TYR ALA ASP PHE GLU HIS ASP LYS ILE
SEQRES 19 A 306 ASP VAL GLU ALA GLY ASN LYS ILE PRO VAL PRO MET LEU
SEQRES 20 A 306 ALA LEU TRP GLY ALA SER GLY ILE ALA GLN SER ALA ALA
SEQRES 21 A 306 THR PRO LEU ASP VAL TRP ARG LYS TRP ALA SER ASP VAL
SEQRES 22 A 306 GLN GLY ALA PRO ILE GLU SER GLY HIS PHE LEU PRO GLU
SEQRES 23 A 306 GLU ALA PRO ASP GLN THR ALA GLU ALA LEU VAL ARG PHE
SEQRES 24 A 306 PHE SER ALA ALA PRO GLY SER
SEQRES 1 B 306 GLY HIS MET PRO ASP LEU ALA ASP LEU PHE PRO GLY PHE
SEQRES 2 B 306 GLY SER GLU TRP ILE ASN THR SER SER GLY ARG ILE PHE
SEQRES 3 B 306 ALA ARG VAL GLY GLY ASP GLY PRO PRO LEU LEU LEU LEU
SEQRES 4 B 306 HIS GLY PHE PRO GLN THR HIS VAL MET TRP HIS ARG VAL
SEQRES 5 B 306 ALA PRO LYS LEU ALA GLU ARG PHE LYS VAL ILE VAL ALA
SEQRES 6 B 306 ASP LEU PRO GLY TYR GLY TRP SER ASP MET PRO GLU SER
SEQRES 7 B 306 ASP GLU GLN HIS THR PRO TYR THR LYS ARG ALA MET ALA
SEQRES 8 B 306 LYS GLN LEU ILE GLU ALA MET GLU GLN LEU GLY HIS VAL
SEQRES 9 B 306 HIS PHE ALA LEU ALA GLY HIS ASP ARG GLY ALA ARG VAL
SEQRES 10 B 306 SER TYR ARG LEU ALA LEU ASP SER PRO GLY ARG LEU SER
SEQRES 11 B 306 LYS LEU ALA VAL LEU ASP ILE LEU PRO THR TYR GLU TYR
SEQRES 12 B 306 TRP GLN ARG MET ASN ARG ALA TYR ALA LEU LYS ILE TYR
SEQRES 13 B 306 HIS TRP SER PHE LEU ALA GLN PRO ALA PRO LEU PRO GLU
SEQRES 14 B 306 ASN LEU LEU GLY GLY ASP PRO ASP PHE TYR VAL LYS ALA
SEQRES 15 B 306 LYS LEU ALA SER TRP THR ARG ALA GLY ASP LEU SER ALA
SEQRES 16 B 306 PHE ASP PRO ARG ALA VAL GLU HIS TYR ARG ILE ALA PHE
SEQRES 17 B 306 ALA ASP PRO MET ARG ARG HIS VAL MET CYS GLU ASP TYR
SEQRES 18 B 306 ARG ALA GLY ALA TYR ALA ASP PHE GLU HIS ASP LYS ILE
SEQRES 19 B 306 ASP VAL GLU ALA GLY ASN LYS ILE PRO VAL PRO MET LEU
SEQRES 20 B 306 ALA LEU TRP GLY ALA SER GLY ILE ALA GLN SER ALA ALA
SEQRES 21 B 306 THR PRO LEU ASP VAL TRP ARG LYS TRP ALA SER ASP VAL
SEQRES 22 B 306 GLN GLY ALA PRO ILE GLU SER GLY HIS PHE LEU PRO GLU
SEQRES 23 B 306 GLU ALA PRO ASP GLN THR ALA GLU ALA LEU VAL ARG PHE
SEQRES 24 B 306 PHE SER ALA ALA PRO GLY SER
FORMUL 3 HOH *211(H2 O)
HELIX 1 AA1 THR A 43 HIS A 48 5 6
HELIX 2 AA2 VAL A 50 GLU A 56 1 7
HELIX 3 AA3 HIS A 80 TYR A 83 5 4
HELIX 4 AA4 THR A 84 LEU A 99 1 16
HELIX 5 AA5 ASP A 110 SER A 123 1 14
HELIX 6 AA6 PRO A 137 ARG A 144 1 8
HELIX 7 AA7 ASN A 146 ILE A 153 1 8
HELIX 8 AA8 ILE A 153 LEU A 159 1 7
HELIX 9 AA9 PRO A 164 GLY A 171 1 8
HELIX 10 AB1 ASP A 173 TRP A 185 1 13
HELIX 11 AB2 ASP A 195 ALA A 207 1 13
HELIX 12 AB3 ASP A 208 TYR A 224 1 17
HELIX 13 AB4 TYR A 224 ALA A 236 1 13
HELIX 14 AB5 ILE A 253 ALA A 257 5 5
HELIX 15 AB6 THR A 259 ALA A 268 1 10
HELIX 16 AB7 PHE A 281 ALA A 286 1 6
HELIX 17 AB8 ALA A 286 ALA A 300 1 15
HELIX 18 AB9 THR B 43 HIS B 48 5 6
HELIX 19 AC1 VAL B 50 ALA B 55 1 6
HELIX 20 AC2 HIS B 80 TYR B 83 5 4
HELIX 21 AC3 THR B 84 LEU B 99 1 16
HELIX 22 AC4 ASP B 110 SER B 123 1 14
HELIX 23 AC5 PRO B 137 ARG B 144 1 8
HELIX 24 AC6 ASN B 146 ILE B 153 1 8
HELIX 25 AC7 ILE B 153 LEU B 159 1 7
HELIX 26 AC8 PRO B 164 GLY B 171 1 8
HELIX 27 AC9 ASP B 173 TRP B 185 1 13
HELIX 28 AD1 ASP B 195 ASP B 208 1 14
HELIX 29 AD2 ASP B 208 TYR B 224 1 17
HELIX 30 AD3 TYR B 224 GLY B 237 1 14
HELIX 31 AD4 ILE B 253 ALA B 258 1 6
HELIX 32 AD5 THR B 259 ALA B 268 1 10
HELIX 33 AD6 PHE B 281 ALA B 286 1 6
HELIX 34 AD7 ALA B 286 ALA B 300 1 15
SHEET 1 AA1 8 GLY A 12 ILE A 16 0
SHEET 2 AA1 8 ILE A 23 GLY A 29 -1 O VAL A 27 N GLY A 12
SHEET 3 AA1 8 LYS A 59 ALA A 63 -1 O VAL A 62 N ARG A 26
SHEET 4 AA1 8 PRO A 33 LEU A 37 1 N LEU A 34 O LYS A 59
SHEET 5 AA1 8 PHE A 104 HIS A 109 1 O ALA A 105 N LEU A 35
SHEET 6 AA1 8 LEU A 127 LEU A 133 1 O ALA A 131 N LEU A 106
SHEET 7 AA1 8 MET A 244 GLY A 249 1 O LEU A 247 N VAL A 132
SHEET 8 AA1 8 VAL A 271 ILE A 276 1 O GLN A 272 N ALA A 246
SHEET 1 AA2 8 GLY B 12 ILE B 16 0
SHEET 2 AA2 8 ILE B 23 GLY B 28 -1 O ALA B 25 N GLU B 14
SHEET 3 AA2 8 LYS B 59 ALA B 63 -1 O VAL B 62 N ARG B 26
SHEET 4 AA2 8 PRO B 33 LEU B 37 1 N LEU B 34 O ILE B 61
SHEET 5 AA2 8 PHE B 104 HIS B 109 1 O ALA B 105 N PRO B 33
SHEET 6 AA2 8 LEU B 127 LEU B 133 1 O ALA B 131 N LEU B 106
SHEET 7 AA2 8 MET B 244 GLY B 249 1 O LEU B 245 N VAL B 132
SHEET 8 AA2 8 VAL B 271 ILE B 276 1 O GLN B 272 N ALA B 246
CISPEP 1 PHE A 40 PRO A 41 0 -2.98
CISPEP 2 ALA A 163 PRO A 164 0 4.70
CISPEP 3 PHE B 40 PRO B 41 0 -7.61
CISPEP 4 ALA B 163 PRO B 164 0 3.33
CRYST1 41.600 79.100 83.800 90.00 103.00 90.00 P 1 21 1 4
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 0.024038 0.000000 0.005550 0.00000
SCALE2 0.000000 0.012642 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012247 0.00000
TER 2388 ALA A 300
TER 4767 ALA B 300
MASTER 491 0 0 34 16 0 0 6 4923 2 0 48
END |