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HEADER LYASE 26-SEP-13 4MXD
TITLE 1.45 ANGSTRONM CRYSTAL STRUCTURE OF E.COLI 2-SUCCINYL-6-HYDROXY-2,4-
TITLE 2 CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE (MENH)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE
COMPND 3 SYNTHASE;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: SHCHC SYNTHASE;
COMPND 6 EC: 4.2.99.20;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: B2263, JW2258, MENH, YFBB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PETM
KEYWDS OPEN CONFORMATION, ALPHA/BETA HYDROLASE FOLD, 2-SUCCINYL-6-HYDROXY-2,
KEYWDS 2 4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.SUN,S.YIN,Y.FENG,J.LI,J.ZHOU,C.LIU,G.ZHU,Z.GUO
REVDAT 1 23-APR-14 4MXD 0
JRNL AUTH Y.SUN,S.YIN,Y.FENG,J.LI,J.ZHOU,C.LIU,G.ZHU,Z.GUO
JRNL TITL MOLECULAR BASIS OF THE GENERAL BASE CATALYSIS OF AN
JRNL TITL 2 ALPHA/BETA-HYDROLASE CATALYTIC TRIAD
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.83
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 59422
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.155
REMARK 3 R VALUE (WORKING SET) : 0.155
REMARK 3 FREE R VALUE : 0.168
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.340
REMARK 3 FREE R VALUE TEST SET COUNT : 1983
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 41.8432 - 3.4945 0.99 4381 154 0.1503 0.1569
REMARK 3 2 3.4945 - 2.7738 1.00 4257 143 0.1625 0.1719
REMARK 3 3 2.7738 - 2.4232 1.00 4245 147 0.1592 0.2224
REMARK 3 4 2.4232 - 2.2017 1.00 4182 145 0.1522 0.1586
REMARK 3 5 2.2017 - 2.0439 1.00 4186 145 0.1491 0.1569
REMARK 3 6 2.0439 - 1.9234 0.99 4138 146 0.1495 0.1405
REMARK 3 7 1.9234 - 1.8271 0.99 4118 141 0.1513 0.1527
REMARK 3 8 1.8271 - 1.7475 0.98 4077 141 0.1547 0.1797
REMARK 3 9 1.7475 - 1.6802 0.98 4057 139 0.1514 0.1740
REMARK 3 10 1.6802 - 1.6223 0.98 4081 138 0.1492 0.1771
REMARK 3 11 1.6223 - 1.5715 0.97 3999 134 0.1518 0.1471
REMARK 3 12 1.5715 - 1.5266 0.96 3956 139 0.1607 0.1498
REMARK 3 13 1.5266 - 1.4864 0.94 3899 135 0.1748 0.2076
REMARK 3 14 1.4864 - 1.4502 0.93 3863 136 0.1895 0.2031
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) : 0.100
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.330
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.47
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.99
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 : 0.006 2162
REMARK 3 ANGLE : 1.110 2947
REMARK 3 CHIRALITY : 0.080 307
REMARK 3 PLANARITY : 0.004 398
REMARK 3 DIHEDRAL : 15.062 781
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 20
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (chain A and resid -2:3)
REMARK 3 ORIGIN FOR THE GROUP (A): 39.2323 18.3020 21.5319
REMARK 3 T TENSOR
REMARK 3 T11: 0.3289 T22: 0.3076
REMARK 3 T33: 0.1809 T12: 0.0249
REMARK 3 T13: 0.0088 T23: 0.0595
REMARK 3 L TENSOR
REMARK 3 L11: 1.7312 L22: 2.0313
REMARK 3 L33: 4.1381 L12: 0.2029
REMARK 3 L13: 1.6880 L23: -0.6682
REMARK 3 S TENSOR
REMARK 3 S11: 0.3087 S12: -0.5873 S13: -0.2576
REMARK 3 S21: 0.4229 S22: -0.0007 S23: -0.5534
REMARK 3 S31: 0.2957 S32: 0.7924 S33: 0.2197
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (chain A and resid 4:14)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.5590 23.0520 12.4231
REMARK 3 T TENSOR
REMARK 3 T11: 0.2270 T22: 0.2505
REMARK 3 T33: 0.1502 T12: -0.0364
REMARK 3 T13: 0.0337 T23: 0.0584
REMARK 3 L TENSOR
REMARK 3 L11: 4.3642 L22: 0.5854
REMARK 3 L33: 3.3724 L12: -0.7755
REMARK 3 L13: 3.7356 L23: -0.3599
REMARK 3 S TENSOR
REMARK 3 S11: 0.1431 S12: -0.6602 S13: -0.3486
REMARK 3 S21: 0.1717 S22: 0.0721 S23: 0.2099
REMARK 3 S31: 0.2910 S32: -0.5258 S33: -0.0942
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (chain A and resid 15:49)
REMARK 3 ORIGIN FOR THE GROUP (A): 29.6267 28.3148 7.8773
REMARK 3 T TENSOR
REMARK 3 T11: 0.1230 T22: 0.1207
REMARK 3 T33: 0.0600 T12: 0.0027
REMARK 3 T13: 0.0079 T23: 0.0108
REMARK 3 L TENSOR
REMARK 3 L11: 2.5168 L22: 0.5477
REMARK 3 L33: 1.1800 L12: -0.1594
REMARK 3 L13: 0.9284 L23: -0.0401
REMARK 3 S TENSOR
REMARK 3 S11: 0.0033 S12: -0.1654 S13: 0.0097
REMARK 3 S21: 0.0882 S22: 0.0199 S23: 0.0212
REMARK 3 S31: 0.0541 S32: -0.0613 S33: -0.0247
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (chain A and resid 50:56)
REMARK 3 ORIGIN FOR THE GROUP (A): 41.8510 27.4839 17.0235
REMARK 3 T TENSOR
REMARK 3 T11: 0.1779 T22: 0.2015
REMARK 3 T33: 0.0816 T12: 0.0222
REMARK 3 T13: -0.0245 T23: -0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 2.4863 L22: 3.6079
REMARK 3 L33: 3.2298 L12: -0.5062
REMARK 3 L13: 2.1953 L23: -2.5087
REMARK 3 S TENSOR
REMARK 3 S11: 0.0515 S12: -0.1985 S13: -0.2441
REMARK 3 S21: 0.1673 S22: -0.1306 S23: -0.2436
REMARK 3 S31: 0.4611 S32: 0.3832 S33: -0.0184
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (chain A and resid 57:74)
REMARK 3 ORIGIN FOR THE GROUP (A): 40.9823 16.2327 11.5146
REMARK 3 T TENSOR
REMARK 3 T11: 0.2596 T22: 0.1540
REMARK 3 T33: 0.0990 T12: 0.0633
REMARK 3 T13: -0.0387 T23: 0.0221
REMARK 3 L TENSOR
REMARK 3 L11: 5.3153 L22: 2.1112
REMARK 3 L33: 3.4815 L12: 1.7986
REMARK 3 L13: -2.1766 L23: -0.8588
REMARK 3 S TENSOR
REMARK 3 S11: -0.0939 S12: -0.1953 S13: -0.3808
REMARK 3 S21: 0.0798 S22: 0.0383 S23: -0.1677
REMARK 3 S31: 0.5169 S32: 0.2291 S33: 0.0013
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (chain A and resid 75:82)
REMARK 3 ORIGIN FOR THE GROUP (A): 26.8208 15.7698 7.9890
REMARK 3 T TENSOR
REMARK 3 T11: 0.3152 T22: 0.1722
REMARK 3 T33: 0.1392 T12: -0.0678
REMARK 3 T13: -0.0136 T23: 0.0604
REMARK 3 L TENSOR
REMARK 3 L11: 0.3642 L22: 0.1646
REMARK 3 L33: 3.5480 L12: -0.1804
REMARK 3 L13: 0.0851 L23: -0.5715
REMARK 3 S TENSOR
REMARK 3 S11: 0.0795 S12: -0.1659 S13: -0.2556
REMARK 3 S21: -0.0707 S22: 0.0650 S23: 0.1064
REMARK 3 S31: 0.9153 S32: -0.3003 S33: 0.0558
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (chain A and resid 83:99)
REMARK 3 ORIGIN FOR THE GROUP (A): 39.6877 21.6755 1.1630
REMARK 3 T TENSOR
REMARK 3 T11: 0.1367 T22: 0.1324
REMARK 3 T33: 0.0576 T12: 0.0305
REMARK 3 T13: -0.0005 T23: 0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 4.0553 L22: 2.1733
REMARK 3 L33: 2.4679 L12: -0.7091
REMARK 3 L13: 0.2640 L23: 0.6815
REMARK 3 S TENSOR
REMARK 3 S11: 0.0614 S12: -0.0267 S13: -0.1466
REMARK 3 S21: -0.0320 S22: 0.0114 S23: -0.0096
REMARK 3 S31: 0.3061 S32: 0.2084 S33: -0.0887
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (chain A and resid 100:108)
REMARK 3 ORIGIN FOR THE GROUP (A): 31.3482 17.1012 0.1322
REMARK 3 T TENSOR
REMARK 3 T11: 0.2624 T22: 0.1251
REMARK 3 T33: 0.1665 T12: -0.0246
REMARK 3 T13: -0.0192 T23: 0.0185
REMARK 3 L TENSOR
REMARK 3 L11: 4.4048 L22: 4.1997
REMARK 3 L33: 7.5668 L12: 0.7040
REMARK 3 L13: -0.9491 L23: -5.6353
REMARK 3 S TENSOR
REMARK 3 S11: 0.0414 S12: -0.1199 S13: -0.6213
REMARK 3 S21: -0.2476 S22: -0.0358 S23: -0.0150
REMARK 3 S31: 0.7483 S32: -0.2889 S33: 0.0724
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (chain A and resid 109:116)
REMARK 3 ORIGIN FOR THE GROUP (A): 43.8976 26.2876 -6.0544
REMARK 3 T TENSOR
REMARK 3 T11: 0.1128 T22: 0.1885
REMARK 3 T33: 0.0888 T12: 0.0070
REMARK 3 T13: 0.0091 T23: -0.0195
REMARK 3 L TENSOR
REMARK 3 L11: 2.2512 L22: 3.7177
REMARK 3 L33: 2.2049 L12: -1.7014
REMARK 3 L13: 1.8663 L23: -0.7461
REMARK 3 S TENSOR
REMARK 3 S11: 0.0077 S12: 0.2659 S13: -0.0849
REMARK 3 S21: -0.1125 S22: 0.0574 S23: -0.2628
REMARK 3 S31: -0.0244 S32: 0.4776 S33: -0.1619
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (chain A and resid 117:129)
REMARK 3 ORIGIN FOR THE GROUP (A): 57.4145 27.9050 -2.8039
REMARK 3 T TENSOR
REMARK 3 T11: 0.2144 T22: 0.6730
REMARK 3 T33: 0.3796 T12: -0.0892
REMARK 3 T13: 0.0304 T23: -0.1682
REMARK 3 L TENSOR
REMARK 3 L11: 1.7477 L22: 4.4047
REMARK 3 L33: 4.7777 L12: -0.4235
REMARK 3 L13: -1.3792 L23: 4.3157
REMARK 3 S TENSOR
REMARK 3 S11: -0.2175 S12: 1.4165 S13: -0.4205
REMARK 3 S21: -0.4965 S22: 0.5845 S23: -0.2203
REMARK 3 S31: -0.1517 S32: 0.9331 S33: -0.1520
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (chain A and resid 130:143)
REMARK 3 ORIGIN FOR THE GROUP (A): 54.6439 38.6689 10.7135
REMARK 3 T TENSOR
REMARK 3 T11: 0.2176 T22: 0.2657
REMARK 3 T33: 0.1727 T12: -0.0723
REMARK 3 T13: -0.0352 T23: -0.0212
REMARK 3 L TENSOR
REMARK 3 L11: 3.8191 L22: 4.8581
REMARK 3 L33: 0.4428 L12: -1.4368
REMARK 3 L13: 0.4015 L23: 0.9717
REMARK 3 S TENSOR
REMARK 3 S11: -0.0168 S12: 0.1394 S13: 0.0025
REMARK 3 S21: 0.4264 S22: -0.1661 S23: -0.0395
REMARK 3 S31: -0.3499 S32: 0.2499 S33: 0.0651
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (chain A and resid 144:156)
REMARK 3 ORIGIN FOR THE GROUP (A): 46.3606 42.9825 1.5361
REMARK 3 T TENSOR
REMARK 3 T11: 0.3484 T22: 0.4248
REMARK 3 T33: 0.2952 T12: -0.1004
REMARK 3 T13: -0.0303 T23: 0.0967
REMARK 3 L TENSOR
REMARK 3 L11: 2.5349 L22: 1.9198
REMARK 3 L33: 3.6193 L12: -0.1961
REMARK 3 L13: 2.9080 L23: -0.9669
REMARK 3 S TENSOR
REMARK 3 S11: -0.4025 S12: 1.0720 S13: 0.6803
REMARK 3 S21: -0.5890 S22: 0.2710 S23: 0.2640
REMARK 3 S31: -0.5233 S32: 0.4255 S33: 0.0648
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (chain A and resid 157:176)
REMARK 3 ORIGIN FOR THE GROUP (A): 42.3176 43.2831 10.1213
REMARK 3 T TENSOR
REMARK 3 T11: 0.3275 T22: 0.2263
REMARK 3 T33: 0.2942 T12: -0.0281
REMARK 3 T13: -0.0351 T23: 0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 3.9104 L22: 2.8603
REMARK 3 L33: 2.6609 L12: -1.1241
REMARK 3 L13: 0.1937 L23: 1.4621
REMARK 3 S TENSOR
REMARK 3 S11: -0.2154 S12: -0.2096 S13: 0.7523
REMARK 3 S21: -0.0507 S22: 0.1869 S23: -0.1468
REMARK 3 S31: -0.7477 S32: 0.0215 S33: 0.0081
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (chain A and resid 177:193)
REMARK 3 ORIGIN FOR THE GROUP (A): 49.5526 22.9658 1.4046
REMARK 3 T TENSOR
REMARK 3 T11: 0.1229 T22: 0.2606
REMARK 3 T33: 0.1179 T12: 0.0494
REMARK 3 T13: -0.0031 T23: -0.0228
REMARK 3 L TENSOR
REMARK 3 L11: 0.2926 L22: 1.5638
REMARK 3 L33: 2.5927 L12: 0.5926
REMARK 3 L13: 0.1995 L23: 1.3744
REMARK 3 S TENSOR
REMARK 3 S11: -0.0278 S12: 0.0744 S13: -0.1164
REMARK 3 S21: 0.0719 S22: 0.2051 S23: -0.2078
REMARK 3 S31: 0.1172 S32: 0.6240 S33: -0.1838
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (chain A and resid 194:201)
REMARK 3 ORIGIN FOR THE GROUP (A): 36.8184 13.6594 -8.1835
REMARK 3 T TENSOR
REMARK 3 T11: 0.2280 T22: 0.1307
REMARK 3 T33: 0.1080 T12: 0.0385
REMARK 3 T13: -0.0080 T23: -0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 2.3064 L22: 3.3591
REMARK 3 L33: 4.7264 L12: -0.7239
REMARK 3 L13: -2.9814 L23: 2.5804
REMARK 3 S TENSOR
REMARK 3 S11: -0.2202 S12: -0.1388 S13: -0.3561
REMARK 3 S21: 0.0009 S22: 0.1231 S23: 0.0940
REMARK 3 S31: 0.2619 S32: 0.1325 S33: -0.0212
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (chain A and resid 202:210)
REMARK 3 ORIGIN FOR THE GROUP (A): 34.1636 31.5187 -9.4407
REMARK 3 T TENSOR
REMARK 3 T11: 0.1505 T22: 0.1321
REMARK 3 T33: 0.0743 T12: 0.0200
REMARK 3 T13: 0.0304 T23: 0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 2.4357 L22: 6.2305
REMARK 3 L33: 2.6863 L12: 0.0783
REMARK 3 L13: -1.1841 L23: 0.5306
REMARK 3 S TENSOR
REMARK 3 S11: 0.1033 S12: 0.1043 S13: 0.1513
REMARK 3 S21: -0.2187 S22: -0.0283 S23: -0.0120
REMARK 3 S31: -0.1530 S32: 0.1141 S33: -0.0970
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (chain A and resid 211:222)
REMARK 3 ORIGIN FOR THE GROUP (A): 40.3992 28.2315 -12.6775
REMARK 3 T TENSOR
REMARK 3 T11: 0.1563 T22: 0.2007
REMARK 3 T33: 0.0751 T12: 0.0155
REMARK 3 T13: 0.0386 T23: -0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 1.0839 L22: 6.7112
REMARK 3 L33: 2.9821 L12: -0.1161
REMARK 3 L13: -0.4249 L23: 1.9464
REMARK 3 S TENSOR
REMARK 3 S11: 0.1056 S12: 0.1181 S13: 0.1026
REMARK 3 S21: -0.1294 S22: 0.0003 S23: -0.1597
REMARK 3 S31: -0.0706 S32: 0.2134 S33: -0.1215
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (chain A and resid 223:229)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.0148 32.9808 -11.5326
REMARK 3 T TENSOR
REMARK 3 T11: 0.1674 T22: 0.1544
REMARK 3 T33: 0.0719 T12: 0.0433
REMARK 3 T13: 0.0039 T23: 0.0274
REMARK 3 L TENSOR
REMARK 3 L11: 3.1652 L22: 2.0198
REMARK 3 L33: 3.3424 L12: 0.1869
REMARK 3 L13: 0.1447 L23: 2.4364
REMARK 3 S TENSOR
REMARK 3 S11: 0.0607 S12: 0.2627 S13: 0.1404
REMARK 3 S21: -0.4573 S22: -0.0060 S23: 0.0585
REMARK 3 S31: -0.1500 S32: -0.0696 S33: -0.0665
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: (chain A and resid 230:244)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.9699 37.1790 -2.8084
REMARK 3 T TENSOR
REMARK 3 T11: 0.0937 T22: 0.0961
REMARK 3 T33: 0.0767 T12: 0.0082
REMARK 3 T13: 0.0125 T23: 0.0197
REMARK 3 L TENSOR
REMARK 3 L11: 1.4195 L22: 1.8680
REMARK 3 L33: 4.0425 L12: -0.4194
REMARK 3 L13: 0.2224 L23: 0.1113
REMARK 3 S TENSOR
REMARK 3 S11: 0.0551 S12: 0.0030 S13: 0.1604
REMARK 3 S21: -0.0212 S22: -0.1087 S23: -0.2227
REMARK 3 S31: -0.1554 S32: 0.2565 S33: 0.0350
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: (chain A and resid 245:252)
REMARK 3 ORIGIN FOR THE GROUP (A): 21.2361 25.0849 -5.5777
REMARK 3 T TENSOR
REMARK 3 T11: 0.1547 T22: 0.1272
REMARK 3 T33: 0.0920 T12: 0.0162
REMARK 3 T13: -0.0150 T23: -0.0262
REMARK 3 L TENSOR
REMARK 3 L11: 7.3300 L22: 3.1922
REMARK 3 L33: 3.9174 L12: -1.7268
REMARK 3 L13: -1.2844 L23: -1.9045
REMARK 3 S TENSOR
REMARK 3 S11: 0.1399 S12: 0.1510 S13: -0.3166
REMARK 3 S21: -0.3216 S22: -0.0861 S23: 0.1209
REMARK 3 S31: 0.3046 S32: -0.0128 S33: 0.0046
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 4MXD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-OCT-13.
REMARK 100 THE RCSB ID CODE IS RCSB082484.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
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 : 60673
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 10.800
REMARK 200 R MERGE (I) : 0.09100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.90
REMARK 200 R MERGE FOR SHELL (I) : 0.59200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: 1R3D
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M LI2SO4, 0.1M TRIS BUFFER (PH 9.0)
REMARK 280 , 30% V/V GLYCEROL, 17% PEG 3350, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 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+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 37.52767
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 75.05533
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 75.05533
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 37.52767
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 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 638 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 742 LIES ON A SPECIAL POSITION.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 523 O HOH A 749 1.86
REMARK 500 O HOH A 555 O HOH A 736 1.96
REMARK 500 O1 SO4 A 301 O HOH A 736 2.04
REMARK 500 O2 GOL A 305 O HOH A 736 2.05
REMARK 500 O3 SO4 A 301 O HOH A 736 2.12
REMARK 500 O HOH A 698 O HOH A 749 2.12
REMARK 500 O HOH A 740 O HOH A 741 2.13
REMARK 500 S SO4 A 301 O HOH A 736 2.13
REMARK 500 OE2 GLU A 181 O HOH A 593 2.17
REMARK 500 O HOH A 546 O HOH A 743 2.17
REMARK 500 OE2 GLU A 181 O HOH A 606 2.18
REMARK 500 O HOH A 531 O HOH A 731 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 SER A 24 -12.36 77.87
REMARK 500 SER A 86 -119.15 54.94
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 SO4 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 306
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4MYD RELATED DB: PDB
REMARK 900 RELATED ID: 4MYS RELATED DB: PDB
DBREF 4MXD A 1 252 UNP P37355 MENH_ECOLI 1 252
SEQADV 4MXD SER A -2 UNP P37355 EXPRESSION TAG
SEQADV 4MXD GLY A -1 UNP P37355 EXPRESSION TAG
SEQADV 4MXD SER A 0 UNP P37355 EXPRESSION TAG
SEQRES 1 A 255 SER GLY SER MET ILE LEU HIS ALA GLN ALA LYS HIS GLY
SEQRES 2 A 255 LYS PRO GLY LEU PRO TRP LEU VAL PHE LEU HIS GLY PHE
SEQRES 3 A 255 SER GLY ASP CYS HIS GLU TRP GLN GLU VAL GLY GLU ALA
SEQRES 4 A 255 PHE ALA ASP TYR SER ARG LEU TYR VAL ASP LEU PRO GLY
SEQRES 5 A 255 HIS GLY GLY SER ALA ALA ILE SER VAL ASP GLY PHE ASP
SEQRES 6 A 255 ASP VAL THR ASP LEU LEU ARG LYS THR LEU VAL SER TYR
SEQRES 7 A 255 ASN ILE LEU ASP PHE TRP LEU VAL GLY TYR SER LEU GLY
SEQRES 8 A 255 GLY ARG VAL ALA MET MET ALA ALA CYS GLN GLY LEU ALA
SEQRES 9 A 255 GLY LEU CYS GLY VAL ILE VAL GLU GLY GLY HIS PRO GLY
SEQRES 10 A 255 LEU GLN ASN ALA GLU GLN ARG ALA GLU ARG GLN ARG SER
SEQRES 11 A 255 ASP ARG GLN TRP VAL GLN ARG PHE LEU THR GLU PRO LEU
SEQRES 12 A 255 THR ALA VAL PHE ALA ASP TRP TYR GLN GLN PRO VAL PHE
SEQRES 13 A 255 ALA SER LEU ASN ASP ASP GLN ARG ARG GLU LEU VAL ALA
SEQRES 14 A 255 LEU ARG SER ASN ASN ASN GLY ALA THR LEU ALA ALA MET
SEQRES 15 A 255 LEU GLU ALA THR SER LEU ALA VAL GLN PRO ASP LEU ARG
SEQRES 16 A 255 ALA ASN LEU SER ALA ARG THR PHE ALA PHE TYR TYR LEU
SEQRES 17 A 255 CYS GLY GLU ARG ASP SER LYS PHE ARG ALA LEU ALA ALA
SEQRES 18 A 255 GLU LEU ALA ALA ASP CYS HIS VAL ILE PRO ARG ALA GLY
SEQRES 19 A 255 HIS ASN ALA HIS ARG GLU ASN PRO ALA GLY VAL ILE ALA
SEQRES 20 A 255 SER LEU ALA GLN ILE LEU ARG PHE
HET SO4 A 301 5
HET SO4 A 302 5
HET SO4 A 303 5
HET PEG A 304 7
HET GOL A 305 6
HET PGE A 306 10
HETNAM SO4 SULFATE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM GOL GLYCEROL
HETNAM PGE TRIETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 SO4 3(O4 S 2-)
FORMUL 5 PEG C4 H10 O3
FORMUL 6 GOL C3 H8 O3
FORMUL 7 PGE C6 H14 O4
FORMUL 8 HOH *349(H2 O)
HELIX 1 1 TRP A 30 GLU A 35 1 6
HELIX 2 2 HIS A 50 ALA A 54 5 5
HELIX 3 3 GLY A 60 TYR A 75 1 16
HELIX 4 4 SER A 86 GLY A 99 1 14
HELIX 5 5 ASN A 117 GLU A 138 1 22
HELIX 6 6 PRO A 139 TYR A 148 1 10
HELIX 7 7 GLN A 149 ALA A 154 5 6
HELIX 8 8 ASN A 157 SER A 169 1 13
HELIX 9 9 ASN A 172 THR A 183 1 12
HELIX 10 10 SER A 184 GLN A 188 5 5
HELIX 11 11 LEU A 191 ALA A 197 1 7
HELIX 12 12 ASP A 210 LEU A 220 1 11
HELIX 13 13 ASN A 233 ASN A 238 1 6
HELIX 14 14 ASN A 238 ARG A 251 1 14
SHEET 1 A 7 ALA A 5 LYS A 8 0
SHEET 2 A 7 SER A 41 VAL A 45 -1 O TYR A 44 N GLN A 6
SHEET 3 A 7 TRP A 16 LEU A 20 1 N LEU A 17 O LEU A 43
SHEET 4 A 7 PHE A 80 TYR A 85 1 O VAL A 83 N LEU A 20
SHEET 5 A 7 LEU A 103 GLU A 109 1 O CYS A 104 N PHE A 80
SHEET 6 A 7 ALA A 201 GLY A 207 1 O LEU A 205 N VAL A 108
SHEET 7 A 7 HIS A 225 ILE A 227 1 O ILE A 227 N CYS A 206
SSBOND 1 CYS A 206 CYS A 224 1555 1555 2.07
SITE 1 AC1 11 TYR A 148 PHE A 153 LEU A 164 ARG A 168
SITE 2 AC1 11 ARG A 236 GOL A 305 HOH A 410 HOH A 443
SITE 3 AC1 11 HOH A 555 HOH A 599 HOH A 736
SITE 1 AC2 9 HIS A 112 ARG A 124 LYS A 212 PHE A 213
SITE 2 AC2 9 HOH A 433 HOH A 435 HOH A 587 HOH A 590
SITE 3 AC2 9 HOH A 664
SITE 1 AC3 5 MET A 94 CYS A 97 PRO A 189 ASN A 194
SITE 2 AC3 5 HOH A 678
SITE 1 AC4 6 GLU A 32 ARG A 229 HOH A 463 HOH A 655
SITE 2 AC4 6 HOH A 675 HOH A 702
SITE 1 AC5 10 TYR A 85 SER A 86 VAL A 152 HIS A 232
SITE 2 AC5 10 SO4 A 301 HOH A 405 HOH A 410 HOH A 444
SITE 3 AC5 10 HOH A 555 HOH A 736
SITE 1 AC6 8 GLU A 163 ARG A 236 HOH A 502 HOH A 537
SITE 2 AC6 8 HOH A 562 HOH A 695 HOH A 729 HOH A 738
CRYST1 72.163 72.163 112.583 90.00 90.00 120.00 P 31 2 1 6
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 0.013858 0.008001 0.000000 0.00000
SCALE2 0.000000 0.016001 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008882 0.00000
TER 2070 PHE A 252
MASTER 590 0 6 14 7 0 15 6 2356 1 40 20
END |