HEADER LIGASE/LIGASE INHIBITOR 08-NOV-12 4HWO
TITLE CRYSTAL STRUCTURE OF E. COLI THREONYL-TRNA SYNTHETASE BOUND TO A NOVEL
TITLE 2 INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THREONINE--TRNA LIGASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 242-642;
COMPND 5 SYNONYM: THREONYL-TRNA SYNTHETASE, THRRS;
COMPND 6 EC: 6.1.1.3;
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: THRS, B1719, JW1709;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-AI;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS AMINOACYL-TRNA SYNTHETASE, PROTEIN-INHIBITOR COMPLEX, ANTIBACTERIAL,
KEYWDS 2 LIGASE-LIGASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.T.HILGERS
REVDAT 2 28-FEB-24 4HWO 1 REMARK SEQADV LINK
REVDAT 1 18-SEP-13 4HWO 0
JRNL AUTH M.TENG,M.T.HILGERS,M.L.CUNNINGHAM,A.BORCHARDT,J.B.LOCKE,
JRNL AUTH 2 S.ABRAHAM,G.HALEY,B.P.KWAN,C.HALL,G.W.HOUGH,K.J.SHAW,J.FINN
JRNL TITL IDENTIFICATION OF BACTERIA-SELECTIVE THREONYL-TRNA
JRNL TITL 2 SYNTHETASE SUBSTRATE INHIBITORS BY STRUCTURE-BASED DESIGN.
JRNL REF J.MED.CHEM. V. 56 1748 2013
JRNL REFN ISSN 0022-2623
JRNL PMID 23362938
JRNL DOI 10.1021/JM301756M
REMARK 2
REMARK 2 RESOLUTION. 1.91 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.91
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.78
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 3 NUMBER OF REFLECTIONS : 82237
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4111
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.91
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.96
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5065
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.40
REMARK 3 BIN R VALUE (WORKING SET) : 0.3060
REMARK 3 BIN FREE R VALUE SET COUNT : 242
REMARK 3 BIN FREE R VALUE : 0.3620
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6605
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 58
REMARK 3 SOLVENT ATOMS : 545
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.03000
REMARK 3 B22 (A**2) : -0.09000
REMARK 3 B33 (A**2) : 0.12000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.138
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.119
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.073
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.802
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6813 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9182 ; 1.527 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 805 ; 6.208 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 357 ;32.696 ;23.501
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1230 ;15.447 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 62 ;16.930 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 953 ; 0.106 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5238 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 242 638 B 242 638 486 0.120 0.050
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 24
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 242 A 357
REMARK 3 ORIGIN FOR THE GROUP (A): -18.0503 -27.9927 17.3104
REMARK 3 T TENSOR
REMARK 3 T11: 0.1264 T22: 0.1232
REMARK 3 T33: 0.1114 T12: 0.0020
REMARK 3 T13: -0.0040 T23: 0.0124
REMARK 3 L TENSOR
REMARK 3 L11: 0.9735 L22: 0.4884
REMARK 3 L33: 0.3495 L12: 0.0736
REMARK 3 L13: -0.2117 L23: 0.0186
REMARK 3 S TENSOR
REMARK 3 S11: 0.0239 S12: 0.1043 S13: 0.0417
REMARK 3 S21: -0.0018 S22: -0.0024 S23: -0.0302
REMARK 3 S31: 0.0224 S32: 0.0122 S33: -0.0215
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 358 A 373
REMARK 3 ORIGIN FOR THE GROUP (A): -23.6810 -36.6436 13.1039
REMARK 3 T TENSOR
REMARK 3 T11: 0.1137 T22: 0.1406
REMARK 3 T33: 0.1255 T12: 0.0071
REMARK 3 T13: -0.0216 T23: -0.0285
REMARK 3 L TENSOR
REMARK 3 L11: 2.0687 L22: 0.7967
REMARK 3 L33: 2.5080 L12: 1.1311
REMARK 3 L13: -0.7782 L23: 0.1988
REMARK 3 S TENSOR
REMARK 3 S11: -0.1452 S12: 0.2281 S13: -0.1016
REMARK 3 S21: -0.0811 S22: 0.1209 S23: -0.0635
REMARK 3 S31: 0.0731 S32: -0.1582 S33: 0.0243
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 374 A 389
REMARK 3 ORIGIN FOR THE GROUP (A): -14.6023 -32.5912 19.1859
REMARK 3 T TENSOR
REMARK 3 T11: 0.1237 T22: 0.1236
REMARK 3 T33: 0.1277 T12: 0.0138
REMARK 3 T13: -0.0072 T23: 0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 4.1017 L22: 0.7398
REMARK 3 L33: 0.5281 L12: 1.1838
REMARK 3 L13: 0.9219 L23: 0.4596
REMARK 3 S TENSOR
REMARK 3 S11: -0.0159 S12: 0.0074 S13: -0.0786
REMARK 3 S21: -0.0355 S22: -0.0128 S23: -0.0454
REMARK 3 S31: -0.0003 S32: 0.0485 S33: 0.0287
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 390 A 418
REMARK 3 ORIGIN FOR THE GROUP (A): -8.0630 -38.8830 32.1223
REMARK 3 T TENSOR
REMARK 3 T11: 0.1306 T22: 0.1669
REMARK 3 T33: 0.1266 T12: 0.0204
REMARK 3 T13: -0.0306 T23: 0.0350
REMARK 3 L TENSOR
REMARK 3 L11: 1.5552 L22: 1.1522
REMARK 3 L33: 0.8417 L12: 1.1139
REMARK 3 L13: -1.0186 L23: -0.4951
REMARK 3 S TENSOR
REMARK 3 S11: 0.0494 S12: -0.2236 S13: -0.0901
REMARK 3 S21: 0.1326 S22: -0.0936 S23: -0.1166
REMARK 3 S31: 0.0234 S32: 0.1535 S33: 0.0442
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 419 A 432
REMARK 3 ORIGIN FOR THE GROUP (A): -1.2705 -44.6280 11.5161
REMARK 3 T TENSOR
REMARK 3 T11: 0.1617 T22: 0.1000
REMARK 3 T33: 0.1445 T12: 0.0325
REMARK 3 T13: 0.0081 T23: 0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 3.1989 L22: 1.6736
REMARK 3 L33: 2.9943 L12: 0.9786
REMARK 3 L13: -0.2409 L23: -0.8546
REMARK 3 S TENSOR
REMARK 3 S11: -0.0911 S12: 0.2169 S13: -0.1664
REMARK 3 S21: -0.2428 S22: 0.1120 S23: -0.0383
REMARK 3 S31: 0.1683 S32: -0.0275 S33: -0.0209
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 433 A 465
REMARK 3 ORIGIN FOR THE GROUP (A): -1.9144 -44.9925 21.4060
REMARK 3 T TENSOR
REMARK 3 T11: 0.1261 T22: 0.1270
REMARK 3 T33: 0.1365 T12: 0.0525
REMARK 3 T13: -0.0107 T23: 0.0301
REMARK 3 L TENSOR
REMARK 3 L11: 0.8986 L22: 1.3372
REMARK 3 L33: 2.4406 L12: 0.0830
REMARK 3 L13: -1.1497 L23: 0.2653
REMARK 3 S TENSOR
REMARK 3 S11: -0.0256 S12: -0.0672 S13: -0.0633
REMARK 3 S21: -0.0404 S22: 0.0303 S23: -0.0009
REMARK 3 S31: -0.0864 S32: 0.0710 S33: -0.0047
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 466 A 499
REMARK 3 ORIGIN FOR THE GROUP (A): -9.1747 -38.3296 19.7514
REMARK 3 T TENSOR
REMARK 3 T11: 0.1258 T22: 0.1323
REMARK 3 T33: 0.1482 T12: 0.0177
REMARK 3 T13: 0.0012 T23: 0.0176
REMARK 3 L TENSOR
REMARK 3 L11: 0.7730 L22: 0.6480
REMARK 3 L33: 0.3934 L12: 0.3144
REMARK 3 L13: -0.3306 L23: -0.0285
REMARK 3 S TENSOR
REMARK 3 S11: -0.0143 S12: 0.0359 S13: -0.0667
REMARK 3 S21: -0.0185 S22: -0.0333 S23: -0.0792
REMARK 3 S31: 0.1088 S32: 0.0719 S33: 0.0476
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 500 A 507
REMARK 3 ORIGIN FOR THE GROUP (A): 11.6745 -22.6772 19.2435
REMARK 3 T TENSOR
REMARK 3 T11: 0.0544 T22: 0.2448
REMARK 3 T33: 0.2266 T12: 0.0293
REMARK 3 T13: 0.0224 T23: 0.0338
REMARK 3 L TENSOR
REMARK 3 L11: 12.6464 L22: 4.0327
REMARK 3 L33: 10.8086 L12: 6.8103
REMARK 3 L13: -0.8867 L23: 1.5033
REMARK 3 S TENSOR
REMARK 3 S11: -0.2218 S12: -0.2301 S13: -0.4071
REMARK 3 S21: -0.1229 S22: 0.0880 S23: -0.1968
REMARK 3 S31: 0.0198 S32: 1.1162 S33: 0.1338
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 508 A 582
REMARK 3 ORIGIN FOR THE GROUP (A): -36.9375 -31.8797 36.7429
REMARK 3 T TENSOR
REMARK 3 T11: 0.1674 T22: 0.1089
REMARK 3 T33: 0.1416 T12: -0.0049
REMARK 3 T13: 0.0311 T23: -0.0117
REMARK 3 L TENSOR
REMARK 3 L11: 0.6595 L22: 0.4548
REMARK 3 L33: 0.3694 L12: -0.0296
REMARK 3 L13: -0.4705 L23: 0.0101
REMARK 3 S TENSOR
REMARK 3 S11: 0.0251 S12: -0.0262 S13: -0.0091
REMARK 3 S21: 0.1237 S22: -0.0454 S23: 0.1129
REMARK 3 S31: -0.0254 S32: 0.0343 S33: 0.0203
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 583 A 601
REMARK 3 ORIGIN FOR THE GROUP (A): -45.6214 -35.2354 43.0325
REMARK 3 T TENSOR
REMARK 3 T11: 0.1789 T22: 0.0941
REMARK 3 T33: 0.2023 T12: -0.0093
REMARK 3 T13: 0.1101 T23: 0.0202
REMARK 3 L TENSOR
REMARK 3 L11: 2.2796 L22: 3.1722
REMARK 3 L33: 3.7411 L12: 0.1880
REMARK 3 L13: -1.4639 L23: 2.0604
REMARK 3 S TENSOR
REMARK 3 S11: -0.0252 S12: -0.0106 S13: -0.0912
REMARK 3 S21: 0.3578 S22: -0.0902 S23: 0.5504
REMARK 3 S31: 0.0307 S32: -0.1212 S33: 0.1154
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 602 A 619
REMARK 3 ORIGIN FOR THE GROUP (A): -42.6595 -36.5951 50.5913
REMARK 3 T TENSOR
REMARK 3 T11: 0.6116 T22: 0.1600
REMARK 3 T33: 0.2626 T12: 0.1407
REMARK 3 T13: 0.3920 T23: 0.1153
REMARK 3 L TENSOR
REMARK 3 L11: 3.7808 L22: 8.0085
REMARK 3 L33: 8.5351 L12: -2.4703
REMARK 3 L13: -4.2585 L23: 7.5440
REMARK 3 S TENSOR
REMARK 3 S11: -0.4977 S12: -0.5223 S13: -0.4920
REMARK 3 S21: 0.3793 S22: 0.1383 S23: 0.3744
REMARK 3 S31: 0.2491 S32: 0.4168 S33: 0.3595
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 620 A 642
REMARK 3 ORIGIN FOR THE GROUP (A): -30.9891 -32.2764 48.3900
REMARK 3 T TENSOR
REMARK 3 T11: 0.2462 T22: 0.1589
REMARK 3 T33: 0.0574 T12: -0.0167
REMARK 3 T13: 0.0005 T23: -0.0116
REMARK 3 L TENSOR
REMARK 3 L11: 3.8765 L22: 4.4643
REMARK 3 L33: 2.1476 L12: -2.4297
REMARK 3 L13: -1.2055 L23: 0.3036
REMARK 3 S TENSOR
REMARK 3 S11: -0.1844 S12: -0.4434 S13: -0.1183
REMARK 3 S21: 0.5934 S22: 0.1167 S23: 0.1256
REMARK 3 S31: 0.0034 S32: 0.2821 S33: 0.0677
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 242 B 312
REMARK 3 ORIGIN FOR THE GROUP (A): -23.8488 -15.0415 17.4423
REMARK 3 T TENSOR
REMARK 3 T11: 0.1203 T22: 0.1013
REMARK 3 T33: 0.1136 T12: 0.0077
REMARK 3 T13: 0.0139 T23: -0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 1.0164 L22: 0.4442
REMARK 3 L33: 0.6506 L12: -0.0122
REMARK 3 L13: 0.2419 L23: -0.1204
REMARK 3 S TENSOR
REMARK 3 S11: 0.0581 S12: 0.0583 S13: -0.0293
REMARK 3 S21: 0.0348 S22: -0.0325 S23: -0.0716
REMARK 3 S31: 0.0091 S32: 0.0141 S33: -0.0257
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 313 B 326
REMARK 3 ORIGIN FOR THE GROUP (A): -29.2887 -24.7718 0.1677
REMARK 3 T TENSOR
REMARK 3 T11: 0.1829 T22: 0.2219
REMARK 3 T33: 0.0807 T12: -0.0064
REMARK 3 T13: 0.0017 T23: -0.0305
REMARK 3 L TENSOR
REMARK 3 L11: 2.1251 L22: 5.5494
REMARK 3 L33: 1.6914 L12: -0.1465
REMARK 3 L13: 0.6622 L23: 1.2981
REMARK 3 S TENSOR
REMARK 3 S11: 0.1069 S12: 0.2885 S13: -0.1340
REMARK 3 S21: -0.5402 S22: -0.0846 S23: -0.0220
REMARK 3 S31: 0.0009 S32: -0.0880 S33: -0.0223
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 327 B 360
REMARK 3 ORIGIN FOR THE GROUP (A): -40.9319 -22.6659 17.8695
REMARK 3 T TENSOR
REMARK 3 T11: 0.1279 T22: 0.1197
REMARK 3 T33: 0.1246 T12: -0.0083
REMARK 3 T13: 0.0043 T23: 0.0047
REMARK 3 L TENSOR
REMARK 3 L11: 2.4538 L22: 0.2936
REMARK 3 L33: 1.3857 L12: 0.1397
REMARK 3 L13: -0.7521 L23: -0.2100
REMARK 3 S TENSOR
REMARK 3 S11: 0.0154 S12: 0.0831 S13: -0.0254
REMARK 3 S21: 0.0297 S22: 0.0233 S23: 0.0782
REMARK 3 S31: 0.0967 S32: -0.1209 S33: -0.0386
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 361 B 380
REMARK 3 ORIGIN FOR THE GROUP (A): -22.3330 -10.1866 8.1912
REMARK 3 T TENSOR
REMARK 3 T11: 0.1134 T22: 0.1476
REMARK 3 T33: 0.1200 T12: 0.0160
REMARK 3 T13: 0.0301 T23: 0.0227
REMARK 3 L TENSOR
REMARK 3 L11: 3.0336 L22: 2.5888
REMARK 3 L33: 3.3552 L12: 2.0823
REMARK 3 L13: 1.2051 L23: 0.4994
REMARK 3 S TENSOR
REMARK 3 S11: -0.1246 S12: 0.2552 S13: 0.1259
REMARK 3 S21: -0.0765 S22: 0.1337 S23: -0.0316
REMARK 3 S31: -0.1739 S32: 0.1087 S33: -0.0090
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 381 B 418
REMARK 3 ORIGIN FOR THE GROUP (A): -39.3212 -5.7127 23.8036
REMARK 3 T TENSOR
REMARK 3 T11: 0.1682 T22: 0.1464
REMARK 3 T33: 0.1212 T12: 0.0348
REMARK 3 T13: 0.0280 T23: -0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 0.7319 L22: 1.0199
REMARK 3 L33: 0.0836 L12: 0.2211
REMARK 3 L13: -0.1587 L23: -0.1719
REMARK 3 S TENSOR
REMARK 3 S11: 0.0094 S12: -0.0363 S13: 0.0500
REMARK 3 S21: 0.1399 S22: 0.0179 S23: 0.0800
REMARK 3 S31: -0.0737 S32: -0.0503 S33: -0.0273
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 419 B 445
REMARK 3 ORIGIN FOR THE GROUP (A): -47.3788 -3.6979 8.1666
REMARK 3 T TENSOR
REMARK 3 T11: 0.1301 T22: 0.1435
REMARK 3 T33: 0.0861 T12: 0.0663
REMARK 3 T13: 0.0001 T23: 0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 1.3645 L22: 3.6890
REMARK 3 L33: 5.7279 L12: 1.0027
REMARK 3 L13: 0.8434 L23: 3.6242
REMARK 3 S TENSOR
REMARK 3 S11: 0.0488 S12: 0.0668 S13: 0.0735
REMARK 3 S21: -0.2306 S22: -0.1849 S23: 0.1355
REMARK 3 S31: -0.2337 S32: -0.3684 S33: 0.1361
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 446 B 466
REMARK 3 ORIGIN FOR THE GROUP (A): -41.8854 0.4511 13.1152
REMARK 3 T TENSOR
REMARK 3 T11: 0.1274 T22: 0.1108
REMARK 3 T33: 0.1157 T12: 0.0329
REMARK 3 T13: 0.0276 T23: 0.0070
REMARK 3 L TENSOR
REMARK 3 L11: 0.3367 L22: 4.5412
REMARK 3 L33: 5.4073 L12: -0.4432
REMARK 3 L13: -0.2876 L23: 3.6237
REMARK 3 S TENSOR
REMARK 3 S11: 0.0235 S12: 0.0133 S13: -0.0102
REMARK 3 S21: -0.1608 S22: 0.0204 S23: -0.0674
REMARK 3 S31: -0.1528 S32: 0.0570 S33: -0.0439
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 467 B 498
REMARK 3 ORIGIN FOR THE GROUP (A): -37.4423 -7.5852 13.9017
REMARK 3 T TENSOR
REMARK 3 T11: 0.1208 T22: 0.1510
REMARK 3 T33: 0.1297 T12: 0.0130
REMARK 3 T13: 0.0176 T23: 0.0158
REMARK 3 L TENSOR
REMARK 3 L11: 0.7731 L22: 1.0371
REMARK 3 L33: 0.3871 L12: 0.2908
REMARK 3 L13: -0.0813 L23: -0.2813
REMARK 3 S TENSOR
REMARK 3 S11: 0.0073 S12: 0.1459 S13: 0.1791
REMARK 3 S21: -0.0253 S22: -0.0005 S23: 0.0787
REMARK 3 S31: -0.0795 S32: -0.1051 S33: -0.0068
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 499 B 505
REMARK 3 ORIGIN FOR THE GROUP (A): -60.8051 -22.3215 19.6731
REMARK 3 T TENSOR
REMARK 3 T11: 0.1951 T22: 1.2423
REMARK 3 T33: 0.4588 T12: 0.3377
REMARK 3 T13: 0.1708 T23: 0.5361
REMARK 3 L TENSOR
REMARK 3 L11: 53.2307 L22: 35.9481
REMARK 3 L33: 34.8916 L12: -18.5380
REMARK 3 L13: -38.0357 L23: 0.4969
REMARK 3 S TENSOR
REMARK 3 S11: 0.4033 S12: 0.6275 S13: -0.0338
REMARK 3 S21: -0.9065 S22: 1.2035 S23: 1.9793
REMARK 3 S31: -0.5890 S32: -2.6457 S33: -1.6068
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 506 B 531
REMARK 3 ORIGIN FOR THE GROUP (A): -29.0675 -7.2209 20.1079
REMARK 3 T TENSOR
REMARK 3 T11: 0.1506 T22: 0.1123
REMARK 3 T33: 0.1333 T12: 0.0175
REMARK 3 T13: 0.0142 T23: 0.0050
REMARK 3 L TENSOR
REMARK 3 L11: 2.3580 L22: 0.6691
REMARK 3 L33: 0.2610 L12: 0.7644
REMARK 3 L13: -0.0581 L23: -0.1031
REMARK 3 S TENSOR
REMARK 3 S11: 0.0173 S12: -0.0183 S13: 0.1292
REMARK 3 S21: -0.0045 S22: -0.0422 S23: 0.0141
REMARK 3 S31: -0.0904 S32: -0.0385 S33: 0.0249
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 532 B 632
REMARK 3 ORIGIN FOR THE GROUP (A): -5.3678 -7.3776 41.5731
REMARK 3 T TENSOR
REMARK 3 T11: 0.1606 T22: 0.1100
REMARK 3 T33: 0.1222 T12: -0.0284
REMARK 3 T13: -0.0311 T23: -0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 0.6967 L22: 1.4370
REMARK 3 L33: 0.7253 L12: -0.0086
REMARK 3 L13: 0.1700 L23: 0.1803
REMARK 3 S TENSOR
REMARK 3 S11: -0.0148 S12: -0.0193 S13: 0.0487
REMARK 3 S21: 0.1558 S22: 0.0050 S23: -0.1073
REMARK 3 S31: 0.0484 S32: -0.0317 S33: 0.0098
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 633 B 639
REMARK 3 ORIGIN FOR THE GROUP (A): -22.0881 -2.8963 38.6953
REMARK 3 T TENSOR
REMARK 3 T11: 0.2417 T22: 0.1768
REMARK 3 T33: 0.1787 T12: -0.0776
REMARK 3 T13: 0.0663 T23: -0.0761
REMARK 3 L TENSOR
REMARK 3 L11: 8.1616 L22: 4.4829
REMARK 3 L33: 12.9806 L12: -1.7585
REMARK 3 L13: 5.3281 L23: 5.0854
REMARK 3 S TENSOR
REMARK 3 S11: -0.4413 S12: -0.6127 S13: -0.0867
REMARK 3 S21: -0.3592 S22: 0.3010 S23: 0.2017
REMARK 3 S31: -1.0116 S32: -0.1021 S33: 0.1403
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT U VALUES: RESIDUAL ONLY
REMARK 4
REMARK 4 4HWO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-NOV-12.
REMARK 100 THE DEPOSITION ID IS D_1000076013.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 5.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MAR345
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.16
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 82308
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.907
REMARK 200 RESOLUTION RANGE LOW (A) : 79.390
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.91
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.7
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : 0.22600
REMARK 200 R SYM FOR SHELL (I) : 0.22600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, MPD, SODIUM CITRATE, PH 5.9,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 42.95000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 57.18000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.15000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 57.18000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.95000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.15000
REMARK 290 SMTRY3 4 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: 4030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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 MET A 240
REMARK 465 ALA A 241
REMARK 465 MET B 240
REMARK 465 ALA B 241
REMARK 465 LEU B 640
REMARK 465 GLU B 641
REMARK 465 GLU B 642
REMARK 465 LEU B 643
REMARK 465 GLU B 644
REMARK 465 HIS B 645
REMARK 465 HIS B 646
REMARK 465 HIS B 647
REMARK 465 HIS B 648
REMARK 465 HIS B 649
REMARK 465 HIS B 650
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 OE1 GLN A 639 O HOH A 1060 1.97
REMARK 500 O HOH A 973 O HOH A 1059 1.99
REMARK 500 O HOH B 1078 O HOH B 1079 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP A 266 CE2 TRP A 266 CD2 0.074
REMARK 500 HIS A 337 CG HIS A 337 CD2 0.060
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 611 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A 611 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 MET B 518 CG - SD - CE ANGL. DEV. = -9.7 DEGREES
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 ALA A 260 68.75 -156.91
REMARK 500 TYR A 313 11.89 -143.03
REMARK 500 CYS A 480 -88.13 -116.72
REMARK 500 ALA B 260 73.02 -159.80
REMARK 500 TYR B 313 13.54 -146.45
REMARK 500 CYS B 480 -88.40 -114.83
REMARK 500 ASN B 502 -8.87 73.29
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 ZN A 701 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 334 SG
REMARK 620 2 HIS A 385 NE2 99.0
REMARK 620 3 HIS A 511 ND1 104.8 92.1
REMARK 620 4 409 A 702 N7 90.2 153.8 109.3
REMARK 620 5 409 A 702 O6 149.7 82.6 105.3 77.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 701 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 334 SG
REMARK 620 2 HIS B 385 NE2 97.8
REMARK 620 3 HIS B 511 ND1 103.5 96.7
REMARK 620 4 409 B 702 O6 145.1 85.1 110.7
REMARK 620 5 409 B 702 N7 88.2 152.5 108.0 75.1
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 ZN A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 409 A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 409 B 702
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4HWP RELATED DB: PDB
REMARK 900 RELATED ID: 4HWR RELATED DB: PDB
REMARK 900 RELATED ID: 4HWS RELATED DB: PDB
REMARK 900 RELATED ID: 4HWT RELATED DB: PDB
DBREF 4HWO A 242 642 UNP P0A8M3 SYT_ECOLI 242 642
DBREF 4HWO B 242 642 UNP P0A8M3 SYT_ECOLI 242 642
SEQADV 4HWO MET A 240 UNP P0A8M3 EXPRESSION TAG
SEQADV 4HWO ALA A 241 UNP P0A8M3 EXPRESSION TAG
SEQADV 4HWO LEU A 643 UNP P0A8M3 EXPRESSION TAG
SEQADV 4HWO GLU A 644 UNP P0A8M3 EXPRESSION TAG
SEQADV 4HWO HIS A 645 UNP P0A8M3 EXPRESSION TAG
SEQADV 4HWO HIS A 646 UNP P0A8M3 EXPRESSION TAG
SEQADV 4HWO HIS A 647 UNP P0A8M3 EXPRESSION TAG
SEQADV 4HWO HIS A 648 UNP P0A8M3 EXPRESSION TAG
SEQADV 4HWO HIS A 649 UNP P0A8M3 EXPRESSION TAG
SEQADV 4HWO HIS A 650 UNP P0A8M3 EXPRESSION TAG
SEQADV 4HWO MET B 240 UNP P0A8M3 EXPRESSION TAG
SEQADV 4HWO ALA B 241 UNP P0A8M3 EXPRESSION TAG
SEQADV 4HWO LEU B 643 UNP P0A8M3 EXPRESSION TAG
SEQADV 4HWO GLU B 644 UNP P0A8M3 EXPRESSION TAG
SEQADV 4HWO HIS B 645 UNP P0A8M3 EXPRESSION TAG
SEQADV 4HWO HIS B 646 UNP P0A8M3 EXPRESSION TAG
SEQADV 4HWO HIS B 647 UNP P0A8M3 EXPRESSION TAG
SEQADV 4HWO HIS B 648 UNP P0A8M3 EXPRESSION TAG
SEQADV 4HWO HIS B 649 UNP P0A8M3 EXPRESSION TAG
SEQADV 4HWO HIS B 650 UNP P0A8M3 EXPRESSION TAG
SEQRES 1 A 411 MET ALA ARG ASP HIS ARG LYS ILE GLY LYS GLN LEU ASP
SEQRES 2 A 411 LEU TYR HIS MET GLN GLU GLU ALA PRO GLY MET VAL PHE
SEQRES 3 A 411 TRP HIS ASN ASP GLY TRP THR ILE PHE ARG GLU LEU GLU
SEQRES 4 A 411 VAL PHE VAL ARG SER LYS LEU LYS GLU TYR GLN TYR GLN
SEQRES 5 A 411 GLU VAL LYS GLY PRO PHE MET MET ASP ARG VAL LEU TRP
SEQRES 6 A 411 GLU LYS THR GLY HIS TRP ASP ASN TYR LYS ASP ALA MET
SEQRES 7 A 411 PHE THR THR SER SER GLU ASN ARG GLU TYR CYS ILE LYS
SEQRES 8 A 411 PRO MET ASN CYS PRO GLY HIS VAL GLN ILE PHE ASN GLN
SEQRES 9 A 411 GLY LEU LYS SER TYR ARG ASP LEU PRO LEU ARG MET ALA
SEQRES 10 A 411 GLU PHE GLY SER CYS HIS ARG ASN GLU PRO SER GLY SER
SEQRES 11 A 411 LEU HIS GLY LEU MET ARG VAL ARG GLY PHE THR GLN ASP
SEQRES 12 A 411 ASP ALA HIS ILE PHE CYS THR GLU GLU GLN ILE ARG ASP
SEQRES 13 A 411 GLU VAL ASN GLY CYS ILE ARG LEU VAL TYR ASP MET TYR
SEQRES 14 A 411 SER THR PHE GLY PHE GLU LYS ILE VAL VAL LYS LEU SER
SEQRES 15 A 411 THR ARG PRO GLU LYS ARG ILE GLY SER ASP GLU MET TRP
SEQRES 16 A 411 ASP ARG ALA GLU ALA ASP LEU ALA VAL ALA LEU GLU GLU
SEQRES 17 A 411 ASN ASN ILE PRO PHE GLU TYR GLN LEU GLY GLU GLY ALA
SEQRES 18 A 411 PHE TYR GLY PRO LYS ILE GLU PHE THR LEU TYR ASP CYS
SEQRES 19 A 411 LEU ASP ARG ALA TRP GLN CYS GLY THR VAL GLN LEU ASP
SEQRES 20 A 411 PHE SER LEU PRO SER ARG LEU SER ALA SER TYR VAL GLY
SEQRES 21 A 411 GLU ASP ASN GLU ARG LYS VAL PRO VAL MET ILE HIS ARG
SEQRES 22 A 411 ALA ILE LEU GLY SER MET GLU ARG PHE ILE GLY ILE LEU
SEQRES 23 A 411 THR GLU GLU PHE ALA GLY PHE PHE PRO THR TRP LEU ALA
SEQRES 24 A 411 PRO VAL GLN VAL VAL ILE MET ASN ILE THR ASP SER GLN
SEQRES 25 A 411 SER GLU TYR VAL ASN GLU LEU THR GLN LYS LEU SER ASN
SEQRES 26 A 411 ALA GLY ILE ARG VAL LYS ALA ASP LEU ARG ASN GLU LYS
SEQRES 27 A 411 ILE GLY PHE LYS ILE ARG GLU HIS THR LEU ARG ARG VAL
SEQRES 28 A 411 PRO TYR MET LEU VAL CYS GLY ASP LYS GLU VAL GLU SER
SEQRES 29 A 411 GLY LYS VAL ALA VAL ARG THR ARG ARG GLY LYS ASP LEU
SEQRES 30 A 411 GLY SER MET ASP VAL ASN GLU VAL ILE GLU LYS LEU GLN
SEQRES 31 A 411 GLN GLU ILE ARG SER ARG SER LEU LYS GLN LEU GLU GLU
SEQRES 32 A 411 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 411 MET ALA ARG ASP HIS ARG LYS ILE GLY LYS GLN LEU ASP
SEQRES 2 B 411 LEU TYR HIS MET GLN GLU GLU ALA PRO GLY MET VAL PHE
SEQRES 3 B 411 TRP HIS ASN ASP GLY TRP THR ILE PHE ARG GLU LEU GLU
SEQRES 4 B 411 VAL PHE VAL ARG SER LYS LEU LYS GLU TYR GLN TYR GLN
SEQRES 5 B 411 GLU VAL LYS GLY PRO PHE MET MET ASP ARG VAL LEU TRP
SEQRES 6 B 411 GLU LYS THR GLY HIS TRP ASP ASN TYR LYS ASP ALA MET
SEQRES 7 B 411 PHE THR THR SER SER GLU ASN ARG GLU TYR CYS ILE LYS
SEQRES 8 B 411 PRO MET ASN CYS PRO GLY HIS VAL GLN ILE PHE ASN GLN
SEQRES 9 B 411 GLY LEU LYS SER TYR ARG ASP LEU PRO LEU ARG MET ALA
SEQRES 10 B 411 GLU PHE GLY SER CYS HIS ARG ASN GLU PRO SER GLY SER
SEQRES 11 B 411 LEU HIS GLY LEU MET ARG VAL ARG GLY PHE THR GLN ASP
SEQRES 12 B 411 ASP ALA HIS ILE PHE CYS THR GLU GLU GLN ILE ARG ASP
SEQRES 13 B 411 GLU VAL ASN GLY CYS ILE ARG LEU VAL TYR ASP MET TYR
SEQRES 14 B 411 SER THR PHE GLY PHE GLU LYS ILE VAL VAL LYS LEU SER
SEQRES 15 B 411 THR ARG PRO GLU LYS ARG ILE GLY SER ASP GLU MET TRP
SEQRES 16 B 411 ASP ARG ALA GLU ALA ASP LEU ALA VAL ALA LEU GLU GLU
SEQRES 17 B 411 ASN ASN ILE PRO PHE GLU TYR GLN LEU GLY GLU GLY ALA
SEQRES 18 B 411 PHE TYR GLY PRO LYS ILE GLU PHE THR LEU TYR ASP CYS
SEQRES 19 B 411 LEU ASP ARG ALA TRP GLN CYS GLY THR VAL GLN LEU ASP
SEQRES 20 B 411 PHE SER LEU PRO SER ARG LEU SER ALA SER TYR VAL GLY
SEQRES 21 B 411 GLU ASP ASN GLU ARG LYS VAL PRO VAL MET ILE HIS ARG
SEQRES 22 B 411 ALA ILE LEU GLY SER MET GLU ARG PHE ILE GLY ILE LEU
SEQRES 23 B 411 THR GLU GLU PHE ALA GLY PHE PHE PRO THR TRP LEU ALA
SEQRES 24 B 411 PRO VAL GLN VAL VAL ILE MET ASN ILE THR ASP SER GLN
SEQRES 25 B 411 SER GLU TYR VAL ASN GLU LEU THR GLN LYS LEU SER ASN
SEQRES 26 B 411 ALA GLY ILE ARG VAL LYS ALA ASP LEU ARG ASN GLU LYS
SEQRES 27 B 411 ILE GLY PHE LYS ILE ARG GLU HIS THR LEU ARG ARG VAL
SEQRES 28 B 411 PRO TYR MET LEU VAL CYS GLY ASP LYS GLU VAL GLU SER
SEQRES 29 B 411 GLY LYS VAL ALA VAL ARG THR ARG ARG GLY LYS ASP LEU
SEQRES 30 B 411 GLY SER MET ASP VAL ASN GLU VAL ILE GLU LYS LEU GLN
SEQRES 31 B 411 GLN GLU ILE ARG SER ARG SER LEU LYS GLN LEU GLU GLU
SEQRES 32 B 411 LEU GLU HIS HIS HIS HIS HIS HIS
HET ZN A 701 1
HET 409 A 702 28
HET ZN B 701 1
HET 409 B 702 28
HETNAM ZN ZINC ION
HETNAM 409 N-{[3-(4-AMINOQUINAZOLIN-7-YL)PHENYL]SULFONYL}-L-
HETNAM 2 409 THREONINAMIDE
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 409 2(C18 H19 N5 O4 S)
FORMUL 7 HOH *545(H2 O)
HELIX 1 1 ASP A 243 LEU A 251 1 9
HELIX 2 2 HIS A 267 TYR A 288 1 22
HELIX 3 3 ARG A 301 THR A 307 1 7
HELIX 4 4 GLY A 308 LYS A 314 1 7
HELIX 5 5 ASP A 315 MET A 317 5 3
HELIX 6 6 ASN A 333 ASN A 342 1 10
HELIX 7 7 SER A 347 LEU A 351 5 5
HELIX 8 8 PRO A 366 LEU A 370 5 5
HELIX 9 9 THR A 389 GLU A 391 5 3
HELIX 10 10 GLN A 392 PHE A 411 1 20
HELIX 11 11 SER A 430 ASN A 448 1 19
HELIX 12 12 SER A 488 LEU A 493 1 6
HELIX 13 13 MET A 518 PHE A 529 1 12
HELIX 14 14 PRO A 534 ALA A 538 5 5
HELIX 15 15 THR A 548 SER A 550 5 3
HELIX 16 16 GLN A 551 ALA A 565 1 15
HELIX 17 17 LYS A 577 ARG A 588 1 12
HELIX 18 18 GLY A 597 GLY A 604 1 8
HELIX 19 19 VAL A 621 SER A 634 1 14
HELIX 20 20 ASP B 243 LEU B 251 1 9
HELIX 21 21 HIS B 267 TYR B 288 1 22
HELIX 22 22 ARG B 301 THR B 307 1 7
HELIX 23 23 GLY B 308 LYS B 314 1 7
HELIX 24 24 ASP B 315 MET B 317 5 3
HELIX 25 25 ASN B 333 ASN B 342 1 10
HELIX 26 26 SER B 347 LEU B 351 5 5
HELIX 27 27 PRO B 366 LEU B 370 5 5
HELIX 28 28 THR B 389 GLU B 391 5 3
HELIX 29 29 GLN B 392 PHE B 411 1 20
HELIX 30 30 SER B 430 ASN B 448 1 19
HELIX 31 31 SER B 488 LEU B 493 1 6
HELIX 32 32 MET B 518 ALA B 530 1 13
HELIX 33 33 PRO B 534 ALA B 538 5 5
HELIX 34 34 THR B 548 SER B 550 5 3
HELIX 35 35 GLN B 551 ALA B 565 1 15
HELIX 36 36 LYS B 577 ARG B 588 1 12
HELIX 37 37 GLY B 597 GLY B 604 1 8
HELIX 38 38 VAL B 621 SER B 634 1 14
SHEET 1 A 2 TYR A 254 HIS A 255 0
SHEET 2 A 2 PHE A 265 TRP A 266 -1 O PHE A 265 N HIS A 255
SHEET 1 B 8 GLN A 291 GLU A 292 0
SHEET 2 B 8 LEU A 353 HIS A 362 1 O ARG A 354 N GLN A 291
SHEET 3 B 8 GLY A 378 CYS A 388 -1 O PHE A 379 N CYS A 361
SHEET 4 B 8 VAL A 508 SER A 517 -1 O VAL A 508 N CYS A 388
SHEET 5 B 8 ALA A 477 ASP A 486 -1 N ASP A 486 O MET A 509
SHEET 6 B 8 LYS A 465 TYR A 471 -1 N ILE A 466 O VAL A 483
SHEET 7 B 8 VAL A 417 SER A 421 -1 N SER A 421 O LYS A 465
SHEET 8 B 8 GLU A 453 GLN A 455 1 O GLN A 455 N LEU A 420
SHEET 1 C 3 MET A 298 ASP A 300 0
SHEET 2 C 3 ARG A 325 ILE A 329 -1 O CYS A 328 N MET A 299
SHEET 3 C 3 THR A 319 SER A 322 -1 N THR A 320 O TYR A 327
SHEET 1 D 2 TYR A 497 VAL A 498 0
SHEET 2 D 2 ARG A 504 LYS A 505 -1 O LYS A 505 N TYR A 497
SHEET 1 E 5 VAL A 569 ASP A 572 0
SHEET 2 E 5 VAL A 542 ASN A 546 1 N ILE A 544 O ASP A 572
SHEET 3 E 5 TYR A 592 CYS A 596 1 O LEU A 594 N MET A 545
SHEET 4 E 5 LYS A 605 THR A 610 -1 O ALA A 607 N VAL A 595
SHEET 5 E 5 ASP A 615 ASP A 620 -1 O GLY A 617 N VAL A 608
SHEET 1 F 2 TYR B 254 HIS B 255 0
SHEET 2 F 2 PHE B 265 TRP B 266 -1 O PHE B 265 N HIS B 255
SHEET 1 G 8 GLN B 291 GLU B 292 0
SHEET 2 G 8 LEU B 353 HIS B 362 1 O ARG B 354 N GLN B 291
SHEET 3 G 8 GLY B 378 CYS B 388 -1 O PHE B 379 N CYS B 361
SHEET 4 G 8 VAL B 508 SER B 517 -1 O VAL B 508 N CYS B 388
SHEET 5 G 8 ALA B 477 ASP B 486 -1 N GLN B 484 O HIS B 511
SHEET 6 G 8 LYS B 465 TYR B 471 -1 N ILE B 466 O VAL B 483
SHEET 7 G 8 VAL B 417 SER B 421 -1 N SER B 421 O LYS B 465
SHEET 8 G 8 GLU B 453 GLN B 455 1 O GLN B 455 N LEU B 420
SHEET 1 H 3 MET B 298 ASP B 300 0
SHEET 2 H 3 ARG B 325 ILE B 329 -1 O CYS B 328 N MET B 299
SHEET 3 H 3 THR B 319 SER B 322 -1 N THR B 320 O TYR B 327
SHEET 1 I 2 TYR B 497 VAL B 498 0
SHEET 2 I 2 ARG B 504 LYS B 505 -1 O LYS B 505 N TYR B 497
SHEET 1 J 5 VAL B 569 ASP B 572 0
SHEET 2 J 5 VAL B 542 ASN B 546 1 N ILE B 544 O ASP B 572
SHEET 3 J 5 TYR B 592 CYS B 596 1 O LEU B 594 N MET B 545
SHEET 4 J 5 LYS B 605 THR B 610 -1 O ARG B 609 N MET B 593
SHEET 5 J 5 ASP B 615 ASP B 620 -1 O MET B 619 N VAL B 606
LINK SG CYS A 334 ZN ZN A 701 1555 1555 2.38
LINK NE2 HIS A 385 ZN ZN A 701 1555 1555 2.13
LINK ND1 HIS A 511 ZN ZN A 701 1555 1555 2.18
LINK ZN ZN A 701 N7 409 A 702 1555 1555 2.12
LINK ZN ZN A 701 O6 409 A 702 1555 1555 2.16
LINK SG CYS B 334 ZN ZN B 701 1555 1555 2.40
LINK NE2 HIS B 385 ZN ZN B 701 1555 1555 2.09
LINK ND1 HIS B 511 ZN ZN B 701 1555 1555 2.16
LINK ZN ZN B 701 O6 409 B 702 1555 1555 2.15
LINK ZN ZN B 701 N7 409 B 702 1555 1555 2.20
CISPEP 1 LEU A 351 PRO A 352 0 4.48
CISPEP 2 LEU B 351 PRO B 352 0 -1.26
SITE 1 AC1 4 CYS A 334 HIS A 385 HIS A 511 409 A 702
SITE 1 AC2 21 MET A 332 CYS A 334 ARG A 363 GLU A 365
SITE 2 AC2 21 MET A 374 ARG A 375 VAL A 376 PHE A 379
SITE 3 AC2 21 GLN A 381 ASP A 383 HIS A 385 TYR A 462
SITE 4 AC2 21 LYS A 465 GLN A 479 GLN A 484 HIS A 511
SITE 5 AC2 21 GLY A 516 SER A 517 ARG A 520 ZN A 701
SITE 6 AC2 21 HOH A 829
SITE 1 AC3 4 CYS B 334 HIS B 385 HIS B 511 409 B 702
SITE 1 AC4 21 MET B 332 CYS B 334 ARG B 363 GLU B 365
SITE 2 AC4 21 MET B 374 ARG B 375 VAL B 376 PHE B 379
SITE 3 AC4 21 GLN B 381 ASP B 383 HIS B 385 TYR B 462
SITE 4 AC4 21 LYS B 465 GLN B 479 GLN B 484 HIS B 511
SITE 5 AC4 21 GLY B 516 SER B 517 ZN B 701 HOH B 826
SITE 6 AC4 21 HOH B1081
CRYST1 85.900 110.300 114.360 90.00 90.00 90.00 P 21 21 21 8
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 0.011641 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009066 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008744 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
