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HEADER HYDROLASE 24-OCT-18 6MUY
TITLE FLUOROACETATE DEHALOGENASE, ROOM TEMPERATURE STRUCTURE SOLVED BY
TITLE 2 SERIAL 3 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;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
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 6MUY 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) : 39.55
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 48560
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 2422
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 - 4.6264 0.99 2771 146 0.1414 0.1637
REMARK 3 2 4.6264 - 3.6729 1.00 2789 144 0.1099 0.1223
REMARK 3 3 3.6729 - 3.2088 1.00 2717 144 0.1271 0.1771
REMARK 3 4 3.2088 - 2.9155 1.00 2773 146 0.1501 0.1820
REMARK 3 5 2.9155 - 2.7066 1.00 2731 143 0.1586 0.2179
REMARK 3 6 2.7066 - 2.5470 1.00 2727 142 0.1566 0.2337
REMARK 3 7 2.5470 - 2.4195 0.99 2699 141 0.1595 0.1876
REMARK 3 8 2.4195 - 2.3142 0.99 2717 144 0.1645 0.2028
REMARK 3 9 2.3142 - 2.2251 1.00 2754 144 0.1866 0.2420
REMARK 3 10 2.2251 - 2.1483 0.99 2717 142 0.2106 0.2588
REMARK 3 11 2.1483 - 2.0812 0.99 2658 134 0.2336 0.3104
REMARK 3 12 2.0812 - 2.0217 0.99 2764 146 0.2469 0.3003
REMARK 3 13 2.0217 - 1.9685 0.99 2667 142 0.2642 0.3098
REMARK 3 14 1.9685 - 1.9204 0.99 2715 141 0.2942 0.3378
REMARK 3 15 1.9204 - 1.8768 0.99 2707 144 0.3644 0.3687
REMARK 3 16 1.8768 - 1.8368 0.98 2670 141 0.3997 0.4802
REMARK 3 17 1.8368 - 1.8001 0.95 2562 138 0.5046 0.5241
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) : 0.350
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.420
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 4914
REMARK 3 ANGLE : 0.966 6698
REMARK 3 CHIRALITY : 0.050 684
REMARK 3 PLANARITY : 0.006 879
REMARK 3 DIHEDRAL : 16.095 3964
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 17
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 4 THROUGH 37 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.0297 -73.4325 103.4640
REMARK 3 T TENSOR
REMARK 3 T11: 0.4182 T22: 0.3760
REMARK 3 T33: 0.2758 T12: 0.0236
REMARK 3 T13: 0.0159 T23: 0.0635
REMARK 3 L TENSOR
REMARK 3 L11: 2.0732 L22: 1.7706
REMARK 3 L33: 1.4185 L12: 0.0222
REMARK 3 L13: -0.0031 L23: 1.0248
REMARK 3 S TENSOR
REMARK 3 S11: -0.0876 S12: -0.3680 S13: 0.0100
REMARK 3 S21: 0.3331 S22: -0.0732 S23: 0.0305
REMARK 3 S31: 0.5789 S32: -0.2078 S33: 0.1063
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 38 THROUGH 63 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.1825 -72.0373 101.7020
REMARK 3 T TENSOR
REMARK 3 T11: 0.3427 T22: 0.3821
REMARK 3 T33: 0.2952 T12: 0.1315
REMARK 3 T13: -0.0128 T23: 0.0257
REMARK 3 L TENSOR
REMARK 3 L11: 0.2431 L22: 1.0998
REMARK 3 L33: 3.1554 L12: 0.1764
REMARK 3 L13: -0.7696 L23: 0.3455
REMARK 3 S TENSOR
REMARK 3 S11: -0.1703 S12: -0.2648 S13: -0.0439
REMARK 3 S21: 0.1019 S22: 0.1023 S23: -0.0463
REMARK 3 S31: 0.3464 S32: 0.4872 S33: 0.0166
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 64 THROUGH 104 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.1781 -64.1580 95.1316
REMARK 3 T TENSOR
REMARK 3 T11: 0.2021 T22: 0.2551
REMARK 3 T33: 0.2759 T12: 0.0263
REMARK 3 T13: 0.0043 T23: -0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 1.4178 L22: 1.1788
REMARK 3 L33: 3.0325 L12: 0.2123
REMARK 3 L13: -0.5245 L23: 0.1147
REMARK 3 S TENSOR
REMARK 3 S11: 0.0252 S12: -0.0609 S13: 0.0808
REMARK 3 S21: 0.0045 S22: -0.0089 S23: 0.1265
REMARK 3 S31: 0.0383 S32: -0.3816 S33: -0.0009
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 105 THROUGH 137 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.6761 -58.2830 96.6174
REMARK 3 T TENSOR
REMARK 3 T11: 0.2376 T22: 0.2430
REMARK 3 T33: 0.2611 T12: 0.0381
REMARK 3 T13: 0.0006 T23: -0.0198
REMARK 3 L TENSOR
REMARK 3 L11: 1.3661 L22: 1.0476
REMARK 3 L33: 1.3807 L12: 0.1355
REMARK 3 L13: 0.4537 L23: 0.2773
REMARK 3 S TENSOR
REMARK 3 S11: 0.0171 S12: -0.2522 S13: 0.2290
REMARK 3 S21: 0.1146 S22: 0.1481 S23: -0.1116
REMARK 3 S31: -0.1202 S32: 0.0230 S33: -0.1535
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 138 THROUGH 164 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.7148 -59.9932 77.6024
REMARK 3 T TENSOR
REMARK 3 T11: 0.2670 T22: 0.2204
REMARK 3 T33: 0.2605 T12: 0.0003
REMARK 3 T13: -0.0013 T23: -0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 0.4089 L22: 1.2814
REMARK 3 L33: 1.7396 L12: -0.2890
REMARK 3 L13: -0.5057 L23: 0.1516
REMARK 3 S TENSOR
REMARK 3 S11: -0.0053 S12: 0.1181 S13: 0.0342
REMARK 3 S21: -0.0771 S22: 0.1865 S23: -0.0603
REMARK 3 S31: -0.1399 S32: 0.2929 S33: -0.1930
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 165 THROUGH 208 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.8719 -77.5674 83.7083
REMARK 3 T TENSOR
REMARK 3 T11: 0.3463 T22: 0.2168
REMARK 3 T33: 0.3228 T12: 0.0683
REMARK 3 T13: 0.0069 T23: 0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 1.7458 L22: 1.1820
REMARK 3 L33: 2.2901 L12: -0.9375
REMARK 3 L13: 0.2149 L23: -0.2994
REMARK 3 S TENSOR
REMARK 3 S11: -0.1560 S12: 0.0150 S13: -0.3185
REMARK 3 S21: 0.1371 S22: 0.1880 S23: -0.1416
REMARK 3 S31: 0.5415 S32: 0.3032 S33: -0.0605
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 209 THROUGH 235 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.4028 -60.0749 83.6428
REMARK 3 T TENSOR
REMARK 3 T11: 0.2710 T22: 0.2206
REMARK 3 T33: 0.2762 T12: 0.0269
REMARK 3 T13: -0.0021 T23: 0.0149
REMARK 3 L TENSOR
REMARK 3 L11: 1.1090 L22: 2.1971
REMARK 3 L33: 1.6836 L12: 0.0335
REMARK 3 L13: -0.0172 L23: 0.8139
REMARK 3 S TENSOR
REMARK 3 S11: 0.0047 S12: 0.0881 S13: 0.1919
REMARK 3 S21: 0.1009 S22: -0.0372 S23: 0.1454
REMARK 3 S31: -0.1996 S32: -0.1521 S33: 0.0218
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 236 THROUGH 259 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.7625 -55.4738 93.0666
REMARK 3 T TENSOR
REMARK 3 T11: 0.3230 T22: 0.4013
REMARK 3 T33: 0.3777 T12: 0.0256
REMARK 3 T13: -0.0074 T23: -0.0845
REMARK 3 L TENSOR
REMARK 3 L11: 1.7744 L22: 2.0649
REMARK 3 L33: 1.1809 L12: -0.6973
REMARK 3 L13: -0.3461 L23: 0.1737
REMARK 3 S TENSOR
REMARK 3 S11: 0.2371 S12: -0.1075 S13: -0.1218
REMARK 3 S21: -0.3819 S22: -0.0433 S23: -0.1492
REMARK 3 S31: -0.2593 S32: 0.5628 S33: -0.1683
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 260 THROUGH 300 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.1461 -61.1984 98.0956
REMARK 3 T TENSOR
REMARK 3 T11: 0.2851 T22: 0.5580
REMARK 3 T33: 0.3634 T12: 0.0662
REMARK 3 T13: -0.0463 T23: -0.0651
REMARK 3 L TENSOR
REMARK 3 L11: 1.8436 L22: 1.7580
REMARK 3 L33: 2.0812 L12: -0.0740
REMARK 3 L13: -0.0452 L23: 0.8052
REMARK 3 S TENSOR
REMARK 3 S11: -0.0926 S12: -0.4018 S13: 0.0813
REMARK 3 S21: 0.2724 S22: 0.3179 S23: -0.4694
REMARK 3 S31: 0.0796 S32: 0.7873 S33: -0.1820
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 3 THROUGH 84 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.6097 -69.6914 44.9126
REMARK 3 T TENSOR
REMARK 3 T11: 0.3397 T22: 0.3461
REMARK 3 T33: 0.2880 T12: -0.0327
REMARK 3 T13: -0.0051 T23: -0.0551
REMARK 3 L TENSOR
REMARK 3 L11: 2.9890 L22: 1.8180
REMARK 3 L33: 3.1870 L12: -0.0586
REMARK 3 L13: -1.2620 L23: -0.0936
REMARK 3 S TENSOR
REMARK 3 S11: 0.0371 S12: 0.3524 S13: -0.1767
REMARK 3 S21: -0.1208 S22: -0.0748 S23: 0.0424
REMARK 3 S31: 0.3698 S32: -0.2878 S33: 0.0206
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 85 THROUGH 137 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.8236 -60.6108 46.7293
REMARK 3 T TENSOR
REMARK 3 T11: 0.2636 T22: 0.2778
REMARK 3 T33: 0.2602 T12: 0.0064
REMARK 3 T13: 0.0099 T23: 0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 1.8875 L22: 0.8024
REMARK 3 L33: 1.9799 L12: 0.2059
REMARK 3 L13: 0.2694 L23: -0.2736
REMARK 3 S TENSOR
REMARK 3 S11: 0.1032 S12: 0.3066 S13: 0.2141
REMARK 3 S21: -0.0775 S22: -0.0705 S23: -0.0400
REMARK 3 S31: -0.1546 S32: 0.1141 S33: -0.0148
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 138 THROUGH 164 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.2269 -59.2185 67.9131
REMARK 3 T TENSOR
REMARK 3 T11: 0.3425 T22: 0.2987
REMARK 3 T33: 0.3066 T12: -0.0033
REMARK 3 T13: -0.0013 T23: -0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 1.3320 L22: 0.4544
REMARK 3 L33: 1.9503 L12: -0.1919
REMARK 3 L13: -0.9729 L23: 0.2377
REMARK 3 S TENSOR
REMARK 3 S11: 0.1238 S12: 0.0255 S13: 0.1857
REMARK 3 S21: -0.1143 S22: 0.0643 S23: 0.0235
REMARK 3 S31: -0.3047 S32: -0.0046 S33: -0.1787
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 165 THROUGH 185 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.2727 -72.0964 64.9834
REMARK 3 T TENSOR
REMARK 3 T11: 0.3116 T22: 0.3594
REMARK 3 T33: 0.3093 T12: -0.0098
REMARK 3 T13: 0.0030 T23: 0.0221
REMARK 3 L TENSOR
REMARK 3 L11: 3.4611 L22: 2.0692
REMARK 3 L33: 2.6475 L12: -2.0561
REMARK 3 L13: 1.8547 L23: -1.2371
REMARK 3 S TENSOR
REMARK 3 S11: 0.0017 S12: -0.2617 S13: -0.1425
REMARK 3 S21: -0.0078 S22: 0.2280 S23: 0.2823
REMARK 3 S31: 0.2691 S32: -0.4031 S33: -0.1997
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 186 THROUGH 208 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.0131 -70.4349 54.3352
REMARK 3 T TENSOR
REMARK 3 T11: 0.3164 T22: 0.3569
REMARK 3 T33: 0.3254 T12: -0.0847
REMARK 3 T13: 0.0167 T23: -0.0627
REMARK 3 L TENSOR
REMARK 3 L11: 3.5606 L22: 0.7540
REMARK 3 L33: 2.9508 L12: -0.2371
REMARK 3 L13: 0.0521 L23: 0.1252
REMARK 3 S TENSOR
REMARK 3 S11: 0.1052 S12: 0.3573 S13: -0.1734
REMARK 3 S21: -0.2402 S22: -0.0620 S23: -0.0117
REMARK 3 S31: 0.3226 S32: -0.4517 S33: -0.0311
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 209 THROUGH 235 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.1212 -65.3911 61.2324
REMARK 3 T TENSOR
REMARK 3 T11: 0.2878 T22: 0.3138
REMARK 3 T33: 0.2490 T12: 0.0053
REMARK 3 T13: -0.0000 T23: -0.0466
REMARK 3 L TENSOR
REMARK 3 L11: 2.1619 L22: 2.0371
REMARK 3 L33: 1.4774 L12: 0.8598
REMARK 3 L13: -0.6601 L23: -1.4732
REMARK 3 S TENSOR
REMARK 3 S11: 0.0373 S12: -0.2424 S13: 0.0493
REMARK 3 S21: 0.1863 S22: -0.0878 S23: -0.1584
REMARK 3 S31: -0.1113 S32: 0.1405 S33: 0.0750
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 236 THROUGH 259 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.6829 -49.4065 53.8742
REMARK 3 T TENSOR
REMARK 3 T11: 0.4517 T22: 0.3601
REMARK 3 T33: 0.4615 T12: -0.0263
REMARK 3 T13: 0.0594 T23: 0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 5.3636 L22: 1.0251
REMARK 3 L33: 0.5586 L12: 1.3340
REMARK 3 L13: 0.3049 L23: -0.5368
REMARK 3 S TENSOR
REMARK 3 S11: 0.3582 S12: -0.5788 S13: 0.4606
REMARK 3 S21: 0.2079 S22: -0.1928 S23: 0.2163
REMARK 3 S31: -0.6447 S32: -0.1061 S33: -0.1898
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 260 THROUGH 300 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.0710 -51.1461 48.4718
REMARK 3 T TENSOR
REMARK 3 T11: 0.3949 T22: 0.3744
REMARK 3 T33: 0.3834 T12: 0.0696
REMARK 3 T13: 0.0207 T23: 0.0934
REMARK 3 L TENSOR
REMARK 3 L11: 1.8546 L22: 1.8077
REMARK 3 L33: 2.0974 L12: 0.2252
REMARK 3 L13: -1.1482 L23: 0.2251
REMARK 3 S TENSOR
REMARK 3 S11: 0.1286 S12: 0.4544 S13: 0.5881
REMARK 3 S21: -0.1065 S22: 0.0790 S23: 0.2105
REMARK 3 S31: -0.5228 S32: -0.4943 S33: -0.1697
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 6MUY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-OCT-18.
REMARK 100 THE DEPOSITION ID IS D_1000237616.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-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 : F1
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 : BE COMPOUND REFRACTIVE LENS
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 : 48608
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 39.550
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 12.60
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.6500
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: 2370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 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 ASP A 3
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 B 277 O HOH B 501 2.10
REMARK 500 OE1 GLU A 140 NH2 ARG A 144 2.10
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 63.81 -103.66
REMARK 500 ASP A 110 -125.23 60.00
REMARK 500 ILE A 153 50.82 -116.52
REMARK 500 ASP A 173 69.82 -154.98
REMARK 500 TYR A 224 -92.46 -117.60
REMARK 500 SER A 278 157.89 177.32
REMARK 500 PRO B 41 61.83 -102.69
REMARK 500 ASP B 110 -127.33 58.11
REMARK 500 ASP B 173 73.86 -163.15
REMARK 500 TYR B 224 -100.00 -119.75
REMARK 500 SER B 256 -94.60 -158.28
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 CA B 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 173 OD2
REMARK 620 2 HOH A 402 O 106.9
REMARK 620 3 HOH A 415 O 91.9 73.6
REMARK 620 4 ALA A 236 O 70.8 41.4 56.0
REMARK 620 5 HOH A 416 O 85.1 146.1 74.4 122.6
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6MUH RELATED DB: PDB
REMARK 900 SERIAL EXPERIMENT ON THE SAME SAMPLE, BUT WITH 1 DEGREE OSCILLATION
DBREF 6MUY A 1 302 UNP Q6NAM1 DEHA_RHOPA 1 302
DBREF 6MUY B 1 302 UNP Q6NAM1 DEHA_RHOPA 1 302
SEQADV 6MUY GLY A -1 UNP Q6NAM1 EXPRESSION TAG
SEQADV 6MUY HIS A 0 UNP Q6NAM1 EXPRESSION TAG
SEQADV 6MUY GLY A 303 UNP Q6NAM1 EXPRESSION TAG
SEQADV 6MUY SER A 304 UNP Q6NAM1 EXPRESSION TAG
SEQADV 6MUY GLY B -1 UNP Q6NAM1 EXPRESSION TAG
SEQADV 6MUY HIS B 0 UNP Q6NAM1 EXPRESSION TAG
SEQADV 6MUY GLY B 303 UNP Q6NAM1 EXPRESSION TAG
SEQADV 6MUY 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
HET CA B 401 1
HETNAM CA CALCIUM ION
FORMUL 3 CA CA 2+
FORMUL 4 HOH *217(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 TYR A 154 LEU A 159 1 6
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 GLY A 237 1 14
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 TYR B 154 LEU B 159 1 6
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 ALA B 207 1 13
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 THR B 259 LYS B 266 1 8
HELIX 32 AD5 PHE B 281 ALA B 286 1 6
HELIX 33 AD6 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 ILE A 61
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 245 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 ILE B 23 N ILE B 16
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 LYS B 59
SHEET 5 AA2 8 PHE B 104 HIS B 109 1 O ALA B 105 N LEU B 35
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
LINK OD2 ASP B 173 CA CA B 401 1555 1555 2.38
LINK CA CA B 401 O HOH A 402 1555 1555 2.83
LINK CA CA B 401 O HOH A 415 1555 1555 3.00
LINK O ALA A 236 CA CA B 401 1555 2557 2.49
LINK CA CA B 401 O HOH A 416 1555 2547 2.51
CISPEP 1 PHE A 40 PRO A 41 0 -1.27
CISPEP 2 ALA A 163 PRO A 164 0 1.58
CISPEP 3 PHE B 40 PRO B 41 0 -4.23
CISPEP 4 ALA B 163 PRO B 164 0 -0.74
SITE 1 AC1 3 HOH A 402 HOH A 415 ASP B 173
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 2387 ALA A 300
TER 4756 ALA B 300
MASTER 542 0 1 33 16 0 1 6 4922 2 4 48
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