| content |
HEADER HYDROLASE 13-AUG-12 4B6G
TITLE THE CRYSTAL STRUCTURE OF THE NEISSERIAL ESTERASE D.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: S-FORMYLGLUTATHIONE HYDROLASE PROTEIN;
COMPND 5 EC: 3.1.2.12;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NEISSERIA MENINGITIDIS MC58;
SOURCE 3 ORGANISM_TAXID: 122586;
SOURCE 4 STRAIN: C311;
SOURCE 5 VARIANT: NUMBER 3;
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: PMSGC7
KEYWDS HYDROLASE, FORMALDEHYDE DETOXIFICATION, ALPHA/BETA SERINE HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.M.COUNAGO,B.KOBE
REVDAT 1 14-NOV-12 4B6G 0
JRNL AUTH N.H.CHEN,R.M.COUNAGO,K.Y.DJOKO,M.P.JENNINGS,M.A.APICELLA,
JRNL AUTH 2 B.KOBE,A.G.MCEWAN
JRNL TITL A GLUTATHIONE-DEPENDENT DETOXIFICATION SYSTEM IS REQUIRED
JRNL TITL 2 FOR FORMALDEHYDE RESISTANCE AND OPTIMAL SURVIVAL OF
JRNL TITL 3 NEISSERIA MENINGITIDIS IN BIOFILMS.
JRNL REF ANTIOXID.REDOX SIGNAL. 2012
JRNL REFN ESSN 1557-7716
JRNL PMID 22937752
JRNL DOI 10.1089/ARS.2012.4749
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT 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) : 1.400
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.842
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.00
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.65
REMARK 3 NUMBER OF REFLECTIONS : 121215
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1434
REMARK 3 R VALUE (WORKING SET) : 0.1431
REMARK 3 FREE R VALUE : 0.1539
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.0
REMARK 3 FREE R VALUE TEST SET COUNT : 3610
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 19.8436 - 4.1355 0.96 4749 139 0.1429 0.1552
REMARK 3 2 4.1355 - 3.2873 0.98 4592 180 0.1337 0.1479
REMARK 3 3 3.2873 - 2.8732 0.99 4603 143 0.1428 0.1549
REMARK 3 4 2.8732 - 2.6111 1.00 4593 142 0.1383 0.1518
REMARK 3 5 2.6111 - 2.4243 1.00 4575 134 0.1329 0.1478
REMARK 3 6 2.4243 - 2.2816 1.00 4553 156 0.1230 0.1300
REMARK 3 7 2.2816 - 2.1675 1.00 4542 146 0.1288 0.1347
REMARK 3 8 2.1675 - 2.0732 1.00 4532 140 0.1281 0.1348
REMARK 3 9 2.0732 - 1.9935 1.00 4563 121 0.1310 0.1503
REMARK 3 10 1.9935 - 1.9248 1.00 4537 131 0.1295 0.1278
REMARK 3 11 1.9248 - 1.8646 1.00 4523 138 0.1320 0.1433
REMARK 3 12 1.8646 - 1.8114 1.00 4511 143 0.1324 0.1372
REMARK 3 13 1.8114 - 1.7637 1.00 4490 145 0.1379 0.1553
REMARK 3 14 1.7637 - 1.7207 1.00 4492 153 0.1462 0.1665
REMARK 3 15 1.7207 - 1.6816 1.00 4500 139 0.1489 0.1712
REMARK 3 16 1.6816 - 1.6458 1.00 4499 127 0.1482 0.1580
REMARK 3 17 1.6458 - 1.6129 1.00 4477 135 0.1442 0.1512
REMARK 3 18 1.6129 - 1.5825 1.00 4505 132 0.1544 0.1563
REMARK 3 19 1.5825 - 1.5542 1.00 4493 122 0.1589 0.1772
REMARK 3 20 1.5542 - 1.5279 1.00 4474 147 0.1645 0.1627
REMARK 3 21 1.5279 - 1.5033 1.00 4444 132 0.1783 0.1762
REMARK 3 22 1.5033 - 1.4801 1.00 4516 126 0.1840 0.1897
REMARK 3 23 1.4801 - 1.4584 1.00 4469 133 0.1915 0.1958
REMARK 3 24 1.4584 - 1.4379 1.00 4471 134 0.2018 0.2566
REMARK 3 25 1.4379 - 1.4184 1.00 4469 111 0.2190 0.2222
REMARK 3 26 1.4184 - 1.4000 1.00 4433 161 0.2209 0.2448
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.70
REMARK 3 K_SOL : 0
REMARK 3 B_SOL : 0
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.09
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 13.36
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.91
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.023
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 : 0.011 4651
REMARK 3 ANGLE : 1.222 6315
REMARK 3 CHIRALITY : 0.077 641
REMARK 3 PLANARITY : 0.007 839
REMARK 3 DIHEDRAL : 14.519 1690
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 14
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESID -7 THROUGH 11 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.0100 102.0605 30.4042
REMARK 3 T TENSOR
REMARK 3 T11: 0.1826 T22: 0.1404
REMARK 3 T33: 0.1437 T12: -0.0092
REMARK 3 T13: 0.0013 T23: -0.0038
REMARK 3 L TENSOR
REMARK 3 L11: 0.0347 L22: 0.1193
REMARK 3 L33: 0.0182 L12: 0.0627
REMARK 3 L13: -0.0218 L23: -0.0446
REMARK 3 S TENSOR
REMARK 3 S11: 0.0187 S12: -0.1132 S13: 0.0164
REMARK 3 S21: 0.0339 S22: -0.0025 S23: 0.0283
REMARK 3 S31: -0.0328 S32: 0.0467 S33: 0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESID 12 THROUGH 34 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.4846 99.6806 21.7720
REMARK 3 T TENSOR
REMARK 3 T11: 0.1563 T22: 0.1252
REMARK 3 T33: 0.1543 T12: -0.0006
REMARK 3 T13: -0.0031 T23: -0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 0.0880 L22: 0.0649
REMARK 3 L33: 0.1368 L12: 0.0705
REMARK 3 L13: -0.0655 L23: -0.0250
REMARK 3 S TENSOR
REMARK 3 S11: -0.0017 S12: 0.0049 S13: 0.0635
REMARK 3 S21: 0.0427 S22: -0.0324 S23: 0.0395
REMARK 3 S31: -0.0623 S32: 0.0261 S33: -0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESID 35 THROUGH 99 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.6055 90.4300 21.0711
REMARK 3 T TENSOR
REMARK 3 T11: 0.1286 T22: 0.1141
REMARK 3 T33: 0.1257 T12: -0.0013
REMARK 3 T13: 0.0021 T23: 0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 0.2427 L22: 0.4232
REMARK 3 L33: 0.7290 L12: 0.0107
REMARK 3 L13: 0.0643 L23: -0.0662
REMARK 3 S TENSOR
REMARK 3 S11: -0.0272 S12: -0.0215 S13: -0.0122
REMARK 3 S21: 0.0290 S22: -0.0096 S23: 0.0119
REMARK 3 S31: -0.0387 S32: 0.0144 S33: -0.0001
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESID 100 THROUGH 177 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.9932 91.7852 9.7404
REMARK 3 T TENSOR
REMARK 3 T11: 0.1362 T22: 0.1268
REMARK 3 T33: 0.1338 T12: 0.0017
REMARK 3 T13: 0.0015 T23: 0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 0.2993 L22: 0.2539
REMARK 3 L33: 0.5666 L12: 0.0182
REMARK 3 L13: 0.0351 L23: 0.0412
REMARK 3 S TENSOR
REMARK 3 S11: -0.0221 S12: 0.0174 S13: -0.0078
REMARK 3 S21: -0.0355 S22: 0.0013 S23: 0.0401
REMARK 3 S31: -0.0492 S32: -0.0260 S33: 0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND (RESID 178 THROUGH 229 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.4016 79.8831 5.6104
REMARK 3 T TENSOR
REMARK 3 T11: 0.1499 T22: 0.1645
REMARK 3 T33: 0.1645 T12: -0.0047
REMARK 3 T13: -0.0043 T23: -0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 0.1786 L22: 0.3604
REMARK 3 L33: 0.5099 L12: -0.0880
REMARK 3 L13: -0.0543 L23: 0.1719
REMARK 3 S TENSOR
REMARK 3 S11: 0.0078 S12: 0.0682 S13: -0.0744
REMARK 3 S21: -0.0645 S22: -0.0354 S23: 0.0532
REMARK 3 S31: 0.0532 S32: -0.0969 S33: -0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN A AND (RESID 230 THROUGH 275 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.9752 75.7497 11.1054
REMARK 3 T TENSOR
REMARK 3 T11: 0.1649 T22: 0.1379
REMARK 3 T33: 0.1418 T12: 0.0061
REMARK 3 T13: 0.0077 T23: 0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 0.2236 L22: 0.1147
REMARK 3 L33: 0.2849 L12: -0.1251
REMARK 3 L13: 0.0021 L23: 0.1123
REMARK 3 S TENSOR
REMARK 3 S11: 0.0063 S12: 0.0274 S13: -0.0402
REMARK 3 S21: 0.0028 S22: -0.0320 S23: 0.0105
REMARK 3 S31: 0.0940 S32: 0.0622 S33: -0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN B AND (RESID 1 THROUGH 21 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.6979 66.8211 34.6417
REMARK 3 T TENSOR
REMARK 3 T11: 0.2238 T22: 0.1287
REMARK 3 T33: 0.1785 T12: -0.0308
REMARK 3 T13: 0.0350 T23: -0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 0.4677 L22: 0.4099
REMARK 3 L33: 0.3501 L12: -0.0448
REMARK 3 L13: 0.3421 L23: -0.0952
REMARK 3 S TENSOR
REMARK 3 S11: -0.0653 S12: 0.0657 S13: -0.0964
REMARK 3 S21: 0.0179 S22: -0.0440 S23: 0.0285
REMARK 3 S31: 0.3181 S32: -0.0987 S33: 0.0223
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN B AND (RESID 22 THROUGH 145 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.4694 72.5514 45.6658
REMARK 3 T TENSOR
REMARK 3 T11: 0.1691 T22: 0.1241
REMARK 3 T33: 0.1571 T12: 0.0080
REMARK 3 T13: 0.0297 T23: 0.0138
REMARK 3 L TENSOR
REMARK 3 L11: 0.5138 L22: 0.3772
REMARK 3 L33: 0.8673 L12: -0.1566
REMARK 3 L13: -0.2186 L23: 0.4403
REMARK 3 S TENSOR
REMARK 3 S11: -0.0679 S12: -0.0171 S13: -0.0674
REMARK 3 S21: 0.0401 S22: -0.0203 S23: 0.0795
REMARK 3 S31: 0.1715 S32: -0.0421 S33: -0.0012
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN B AND (RESID 146 THROUGH 168 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.6977 75.2712 53.7751
REMARK 3 T TENSOR
REMARK 3 T11: 0.1804 T22: 0.1792
REMARK 3 T33: 0.1535 T12: 0.0436
REMARK 3 T13: 0.0139 T23: 0.0243
REMARK 3 L TENSOR
REMARK 3 L11: 0.0747 L22: 0.0884
REMARK 3 L33: 0.0961 L12: 0.0372
REMARK 3 L13: -0.0166 L23: 0.0714
REMARK 3 S TENSOR
REMARK 3 S11: -0.0512 S12: -0.1029 S13: -0.0740
REMARK 3 S21: 0.1058 S22: 0.0348 S23: 0.0540
REMARK 3 S31: 0.1021 S32: 0.0719 S33: -0.0000
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN B AND (RESID 169 THROUGH 188 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.4948 88.4764 57.4932
REMARK 3 T TENSOR
REMARK 3 T11: 0.1777 T22: 0.1690
REMARK 3 T33: 0.1731 T12: 0.0012
REMARK 3 T13: 0.0177 T23: -0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 0.0333 L22: 0.0677
REMARK 3 L33: 0.0424 L12: -0.0397
REMARK 3 L13: 0.0005 L23: -0.0302
REMARK 3 S TENSOR
REMARK 3 S11: 0.0453 S12: -0.0578 S13: 0.0708
REMARK 3 S21: 0.0835 S22: -0.0357 S23: 0.0483
REMARK 3 S31: -0.0460 S32: 0.0154 S33: -0.0000
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN B AND (RESID 189 THROUGH 213 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.2404 82.3406 63.8736
REMARK 3 T TENSOR
REMARK 3 T11: 0.2068 T22: 0.2413
REMARK 3 T33: 0.1486 T12: 0.0231
REMARK 3 T13: 0.0025 T23: 0.0146
REMARK 3 L TENSOR
REMARK 3 L11: 0.2820 L22: 0.2861
REMARK 3 L33: 0.0785 L12: 0.2515
REMARK 3 L13: 0.0287 L23: -0.0211
REMARK 3 S TENSOR
REMARK 3 S11: 0.0520 S12: -0.2715 S13: -0.0029
REMARK 3 S21: 0.1771 S22: -0.0500 S23: 0.0471
REMARK 3 S31: 0.0660 S32: 0.2094 S33: 0.0015
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN B AND (RESID 214 THROUGH 229 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.0555 93.2504 46.8353
REMARK 3 T TENSOR
REMARK 3 T11: 0.1900 T22: 0.1638
REMARK 3 T33: 0.1674 T12: -0.0012
REMARK 3 T13: 0.0180 T23: 0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 0.0975 L22: 0.1175
REMARK 3 L33: 0.0979 L12: 0.1072
REMARK 3 L13: -0.0071 L23: -0.0092
REMARK 3 S TENSOR
REMARK 3 S11: 0.0924 S12: -0.0496 S13: 0.0438
REMARK 3 S21: -0.0287 S22: -0.0385 S23: 0.0156
REMARK 3 S31: -0.1455 S32: 0.1241 S33: -0.0000
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN B AND (RESID 230 THROUGH 255 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.1722 90.0560 51.0750
REMARK 3 T TENSOR
REMARK 3 T11: 0.1738 T22: 0.2356
REMARK 3 T33: 0.1617 T12: -0.0244
REMARK 3 T13: -0.0237 T23: 0.0050
REMARK 3 L TENSOR
REMARK 3 L11: 0.1447 L22: 0.1775
REMARK 3 L33: 0.1928 L12: -0.0846
REMARK 3 L13: -0.1643 L23: 0.0656
REMARK 3 S TENSOR
REMARK 3 S11: -0.0201 S12: -0.0746 S13: 0.1277
REMARK 3 S21: 0.0448 S22: -0.0282 S23: -0.1094
REMARK 3 S31: -0.1248 S32: 0.3079 S33: 0.0004
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN B AND (RESID 256 THROUGH 275 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.9212 79.9926 39.3469
REMARK 3 T TENSOR
REMARK 3 T11: 0.1493 T22: 0.1596
REMARK 3 T33: 0.1462 T12: 0.0216
REMARK 3 T13: 0.0067 T23: 0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 0.0612 L22: 0.0410
REMARK 3 L33: 0.1441 L12: -0.0336
REMARK 3 L13: -0.0840 L23: 0.0194
REMARK 3 S TENSOR
REMARK 3 S11: -0.0703 S12: -0.0278 S13: -0.0428
REMARK 3 S21: 0.0187 S22: 0.0592 S23: 0.0493
REMARK 3 S31: 0.0050 S32: 0.1258 S33: -0.0031
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 4B6G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-OCT-11.
REMARK 100 THE PDBE ID CODE IS EBI-49945.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-OCT-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95369
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 MONOCHROMATOR (SI111)
REMARK 200 OPTICS : SILICON MIRRORS (ADAPTIVE
REMARK 200 AND U-BENT)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (QUANTUM 315R)
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 151514
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.30
REMARK 200 RESOLUTION RANGE LOW (A) : 19.84
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 5.2
REMARK 200 R MERGE (I) : 0.06
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.30
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.1
REMARK 200 R MERGE FOR SHELL (I) : 0.68
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.30
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: PDB ENTRY 3FCX
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25 MM BIS-TRIS (PH 6.5), 200 MM
REMARK 280 LITHIUM SULFATE AND 25% PEG 3350.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 113.24067
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 56.62033
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 84.93050
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 28.31017
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 141.55083
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 113.24067
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 56.62033
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 28.31017
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 84.93050
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 141.55083
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 AUTHOR DETERMINED QUATERNARY STRUCTURE: 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 GLU B -7
REMARK 465 ASN B -6
REMARK 465 LEU B -5
REMARK 465 TYR B -4
REMARK 465 PHE B -3
REMARK 465 GLN B -2
REMARK 465 GLY B -1
REMARK 465 ALA B 0
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 37 62.89 -163.10
REMARK 500 THR A 53 -4.31 74.15
REMARK 500 THR A 55 -162.52 -112.79
REMARK 500 ALA A 100 48.74 -148.14
REMARK 500 SER A 145 -117.03 64.61
REMARK 500 GLN A 159 -107.63 48.91
REMARK 500 ASP A 253 -155.96 -105.73
REMARK 500 ASN B 37 65.64 -160.47
REMARK 500 THR B 53 -6.14 76.69
REMARK 500 THR B 55 -160.68 -112.54
REMARK 500 ALA B 100 47.69 -149.42
REMARK 500 SER B 145 -114.69 66.58
REMARK 500 ASP B 253 -155.26 -107.28
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4B6G A 3 275 UNP Q9JZ43 Q9JZ43_NEIMB 3 275
DBREF 4B6G B 3 275 UNP Q9JZ43 Q9JZ43_NEIMB 3 275
SEQADV 4B6G GLU A -7 UNP Q9JZ43 EXPRESSION TAG
SEQADV 4B6G ASN A -6 UNP Q9JZ43 EXPRESSION TAG
SEQADV 4B6G LEU A -5 UNP Q9JZ43 EXPRESSION TAG
SEQADV 4B6G TYR A -4 UNP Q9JZ43 EXPRESSION TAG
SEQADV 4B6G PHE A -3 UNP Q9JZ43 EXPRESSION TAG
SEQADV 4B6G GLN A -2 UNP Q9JZ43 EXPRESSION TAG
SEQADV 4B6G GLY A -1 UNP Q9JZ43 EXPRESSION TAG
SEQADV 4B6G ALA A 0 UNP Q9JZ43 EXPRESSION TAG
SEQADV 4B6G MET A 1 UNP Q9JZ43 EXPRESSION TAG
SEQADV 4B6G GLU A 2 UNP Q9JZ43 EXPRESSION TAG
SEQADV 4B6G GLU B -7 UNP Q9JZ43 EXPRESSION TAG
SEQADV 4B6G ASN B -6 UNP Q9JZ43 EXPRESSION TAG
SEQADV 4B6G LEU B -5 UNP Q9JZ43 EXPRESSION TAG
SEQADV 4B6G TYR B -4 UNP Q9JZ43 EXPRESSION TAG
SEQADV 4B6G PHE B -3 UNP Q9JZ43 EXPRESSION TAG
SEQADV 4B6G GLN B -2 UNP Q9JZ43 EXPRESSION TAG
SEQADV 4B6G GLY B -1 UNP Q9JZ43 EXPRESSION TAG
SEQADV 4B6G ALA B 0 UNP Q9JZ43 EXPRESSION TAG
SEQADV 4B6G MET B 1 UNP Q9JZ43 EXPRESSION TAG
SEQADV 4B6G GLU B 2 UNP Q9JZ43 EXPRESSION TAG
SEQRES 1 A 283 GLU ASN LEU TYR PHE GLN GLY ALA MET GLU LEU ILE GLU
SEQRES 2 A 283 GLN HIS GLN ILE PHE GLY GLY SER GLN GLN VAL TRP ALA
SEQRES 3 A 283 HIS HIS ALA GLN THR LEU GLN CYS GLU MET LYS PHE ALA
SEQRES 4 A 283 VAL TYR LEU PRO ASN ASN PRO GLU ASN ARG PRO LEU GLY
SEQRES 5 A 283 VAL ILE TYR TRP LEU SER GLY LEU THR CYS THR GLU GLN
SEQRES 6 A 283 ASN PHE ILE THR LYS SER GLY PHE GLN ARG TYR ALA ALA
SEQRES 7 A 283 GLU HIS GLN VAL ILE VAL VAL ALA PRO ASP THR SER PRO
SEQRES 8 A 283 ARG GLY GLU GLN VAL PRO ASN ASP ASP ALA TYR ASP LEU
SEQRES 9 A 283 GLY GLN SER ALA GLY PHE TYR LEU ASN ALA THR GLU GLN
SEQRES 10 A 283 PRO TRP ALA ALA ASN TYR GLN MET TYR ASP TYR ILE LEU
SEQRES 11 A 283 ASN GLU LEU PRO ARG LEU ILE GLU LYS HIS PHE PRO THR
SEQRES 12 A 283 ASN GLY LYS ARG SER ILE MET GLY HIS SER MET GLY GLY
SEQRES 13 A 283 HIS GLY ALA LEU VAL LEU ALA LEU ARG ASN GLN GLU ARG
SEQRES 14 A 283 TYR GLN SER VAL SER ALA PHE SER PRO ILE LEU SER PRO
SEQRES 15 A 283 SER LEU VAL PRO TRP GLY GLU LYS ALA PHE THR ALA TYR
SEQRES 16 A 283 LEU GLY LYS ASP ARG GLU LYS TRP GLN GLN TYR ASP ALA
SEQRES 17 A 283 ASN SER LEU ILE GLN GLN GLY TYR LYS VAL GLN GLY MET
SEQRES 18 A 283 ARG ILE ASP GLN GLY LEU GLU ASP GLU PHE LEU PRO THR
SEQRES 19 A 283 GLN LEU ARG THR GLU ASP PHE ILE GLU THR CYS ARG ALA
SEQRES 20 A 283 ALA ASN GLN PRO VAL ASP VAL ARG PHE HIS LYS GLY TYR
SEQRES 21 A 283 ASP HIS SER TYR TYR PHE ILE ALA SER PHE ILE GLY GLU
SEQRES 22 A 283 HIS ILE ALA TYR HIS ALA ALA PHE LEU LYS
SEQRES 1 B 283 GLU ASN LEU TYR PHE GLN GLY ALA MET GLU LEU ILE GLU
SEQRES 2 B 283 GLN HIS GLN ILE PHE GLY GLY SER GLN GLN VAL TRP ALA
SEQRES 3 B 283 HIS HIS ALA GLN THR LEU GLN CYS GLU MET LYS PHE ALA
SEQRES 4 B 283 VAL TYR LEU PRO ASN ASN PRO GLU ASN ARG PRO LEU GLY
SEQRES 5 B 283 VAL ILE TYR TRP LEU SER GLY LEU THR CYS THR GLU GLN
SEQRES 6 B 283 ASN PHE ILE THR LYS SER GLY PHE GLN ARG TYR ALA ALA
SEQRES 7 B 283 GLU HIS GLN VAL ILE VAL VAL ALA PRO ASP THR SER PRO
SEQRES 8 B 283 ARG GLY GLU GLN VAL PRO ASN ASP ASP ALA TYR ASP LEU
SEQRES 9 B 283 GLY GLN SER ALA GLY PHE TYR LEU ASN ALA THR GLU GLN
SEQRES 10 B 283 PRO TRP ALA ALA ASN TYR GLN MET TYR ASP TYR ILE LEU
SEQRES 11 B 283 ASN GLU LEU PRO ARG LEU ILE GLU LYS HIS PHE PRO THR
SEQRES 12 B 283 ASN GLY LYS ARG SER ILE MET GLY HIS SER MET GLY GLY
SEQRES 13 B 283 HIS GLY ALA LEU VAL LEU ALA LEU ARG ASN GLN GLU ARG
SEQRES 14 B 283 TYR GLN SER VAL SER ALA PHE SER PRO ILE LEU SER PRO
SEQRES 15 B 283 SER LEU VAL PRO TRP GLY GLU LYS ALA PHE THR ALA TYR
SEQRES 16 B 283 LEU GLY LYS ASP ARG GLU LYS TRP GLN GLN TYR ASP ALA
SEQRES 17 B 283 ASN SER LEU ILE GLN GLN GLY TYR LYS VAL GLN GLY MET
SEQRES 18 B 283 ARG ILE ASP GLN GLY LEU GLU ASP GLU PHE LEU PRO THR
SEQRES 19 B 283 GLN LEU ARG THR GLU ASP PHE ILE GLU THR CYS ARG ALA
SEQRES 20 B 283 ALA ASN GLN PRO VAL ASP VAL ARG PHE HIS LYS GLY TYR
SEQRES 21 B 283 ASP HIS SER TYR TYR PHE ILE ALA SER PHE ILE GLY GLU
SEQRES 22 B 283 HIS ILE ALA TYR HIS ALA ALA PHE LEU LYS
FORMUL 2 HOH *726(H2 O)
HELIX 1 1 GLU A 56 SER A 63 1 8
HELIX 2 2 PHE A 65 GLN A 73 1 9
HELIX 3 3 PRO A 110 ASN A 114 5 5
HELIX 4 4 GLN A 116 ASN A 123 1 8
HELIX 5 5 ASN A 123 PHE A 133 1 11
HELIX 6 6 SER A 145 GLN A 159 1 15
HELIX 7 7 GLU A 160 TYR A 162 5 3
HELIX 8 8 SER A 173 LEU A 176 5 4
HELIX 9 9 VAL A 177 GLY A 189 1 13
HELIX 10 10 ASP A 191 TYR A 198 5 8
HELIX 11 11 ASP A 199 GLY A 207 1 9
HELIX 12 12 PHE A 223 LEU A 228 1 6
HELIX 13 13 ARG A 229 ASN A 241 1 13
HELIX 14 14 SER A 255 ALA A 272 1 18
HELIX 15 15 GLU B 56 SER B 63 1 8
HELIX 16 16 PHE B 65 GLN B 73 1 9
HELIX 17 17 PRO B 110 ASN B 114 5 5
HELIX 18 18 GLN B 116 ASN B 123 1 8
HELIX 19 19 ASN B 123 PHE B 133 1 11
HELIX 20 20 SER B 145 ASN B 158 1 14
HELIX 21 21 GLN B 159 TYR B 162 5 4
HELIX 22 22 SER B 173 LEU B 176 5 4
HELIX 23 23 VAL B 177 GLY B 189 1 13
HELIX 24 24 ASP B 191 TYR B 198 5 8
HELIX 25 25 ASP B 199 GLN B 206 1 8
HELIX 26 26 PHE B 223 LEU B 228 1 6
HELIX 27 27 ARG B 229 ASN B 241 1 13
HELIX 28 28 SER B 255 LEU B 274 1 20
SHEET 1 AA10 PHE A -3 GLN A -2 0
SHEET 2 AA10 MET A 1 ILE A 9 -1 O MET A 1 N GLN A -2
SHEET 3 AA10 GLY A 12 ALA A 21 -1 O GLY A 12 N ILE A 9
SHEET 4 AA10 CYS A 26 LEU A 34 -1 O CYS A 26 N ALA A 21
SHEET 5 AA10 ILE A 75 PRO A 79 -1 O VAL A 76 N TYR A 33
SHEET 6 AA10 LEU A 43 LEU A 49 1 O GLY A 44 N ILE A 75
SHEET 7 AA10 THR A 135 HIS A 144 1 N ASN A 136 O LEU A 43
SHEET 8 AA10 VAL A 165 PHE A 168 1 O SER A 166 N GLY A 143
SHEET 9 AA10 ARG A 214 GLY A 218 1 O ARG A 214 N ALA A 167
SHEET 10 AA10 ASP A 245 HIS A 249 1 O ASP A 245 N ILE A 215
SHEET 1 BA 9 GLU B 2 ILE B 9 0
SHEET 2 BA 9 GLY B 12 ALA B 21 -1 O GLY B 12 N ILE B 9
SHEET 3 BA 9 CYS B 26 LEU B 34 -1 O CYS B 26 N ALA B 21
SHEET 4 BA 9 ILE B 75 PRO B 79 -1 O VAL B 76 N TYR B 33
SHEET 5 BA 9 LEU B 43 LEU B 49 1 O GLY B 44 N ILE B 75
SHEET 6 BA 9 THR B 135 HIS B 144 1 N ASN B 136 O LEU B 43
SHEET 7 BA 9 VAL B 165 PHE B 168 1 O SER B 166 N GLY B 143
SHEET 8 BA 9 ARG B 214 GLY B 218 1 O ARG B 214 N ALA B 167
SHEET 9 BA 9 ASP B 245 HIS B 249 1 O ASP B 245 N ILE B 215
CISPEP 1 GLN A 109 PRO A 110 0 6.77
CISPEP 2 GLN B 109 PRO B 110 0 3.44
CRYST1 111.268 111.268 169.861 90.00 90.00 120.00 P 65 2 2 24
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 0.008987 0.005189 0.000000 0.00000
SCALE2 0.000000 0.010378 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005887 0.00000
TER 4494 LYS A 275
TER 8844 LYS B 275
MASTER 512 0 0 28 19 0 0 6 9568 2 0 44
END |