HEADER ISOMERASE 08-JAN-13 4IOT
TITLE HIGH-RESOLUTION STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE FROM E. COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRIOSEPHOSPHATE ISOMERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TIM, TRIOSE-PHOSPHATE ISOMERASE;
COMPND 5 EC: 5.3.1.1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 316385;
SOURCE 4 STRAIN: K12 / DH10B
KEYWDS STRUCTURAL GENOMICS, MONTREAL-KINGSTON BACTERIAL STRUCTURAL GENOMICS
KEYWDS 2 INITIATIVE, BSGI, TIM BARREL, CONVERSION OF DIHYDROXYACETONE
KEYWDS 3 PHOSPHATE TO D-GLYCERALDEHYDE-3-PHOSPHATE, CYTOSOL, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.VINAIK,G.KOZLOV,K.GEHRING,MONTREAL-KINGSTON BACTERIAL STRUCTURAL
AUTHOR 2 GENOMICS INITIATIVE (BSGI)
REVDAT 3 20-SEP-23 4IOT 1 REMARK
REVDAT 2 05-JUN-13 4IOT 1 JRNL
REVDAT 1 23-JAN-13 4IOT 0
JRNL AUTH G.KOZLOV,R.VINAIK,K.GEHRING
JRNL TITL TRIOSEPHOSPHATE ISOMERASE IS A COMMON CRYSTALLIZATION
JRNL TITL 2 CONTAMINANT OF SOLUBLE HIS-TAGGED PROTEINS PRODUCED IN
JRNL TITL 3 ESCHERICHIA COLI.
JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 69 499 2013
JRNL REFN ESSN 1744-3091
JRNL PMID 23695562
JRNL DOI 10.1107/S1744309113010841
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 75.16
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 38754
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) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2049
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) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2612
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.06
REMARK 3 BIN R VALUE (WORKING SET) : 0.2020
REMARK 3 BIN FREE R VALUE SET COUNT : 135
REMARK 3 BIN FREE R VALUE : 0.2000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3774
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 474
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.45000
REMARK 3 B22 (A**2) : 1.01000
REMARK 3 B33 (A**2) : -0.56000
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): 0.145
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.130
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.082
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.195
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3899 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5286 ; 1.037 ; 1.951
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 526 ; 4.698 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 163 ;38.879 ;25.337
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 676 ;12.912 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;18.431 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 606 ; 0.067 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2921 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1877 ; 0.182 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2686 ; 0.297 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 398 ; 0.120 ; 0.200
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): 56 ; 0.161 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 31 ; 0.131 ; 0.200
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): 2634 ; 0.426 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4038 ; 0.656 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1443 ; 1.273 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1238 ; 2.056 ; 4.500
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 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 14
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 1 A 36
REMARK 3 ORIGIN FOR THE GROUP (A): -1.8250 4.9710 -6.5240
REMARK 3 T TENSOR
REMARK 3 T11: 0.0854 T22: 0.0287
REMARK 3 T33: 0.0428 T12: -0.0220
REMARK 3 T13: -0.0096 T23: 0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 1.3937 L22: 1.9630
REMARK 3 L33: 1.9693 L12: -0.8764
REMARK 3 L13: 0.3618 L23: -0.1762
REMARK 3 S TENSOR
REMARK 3 S11: -0.0311 S12: -0.1268 S13: -0.1497
REMARK 3 S21: 0.1576 S22: 0.0845 S23: 0.0085
REMARK 3 S31: 0.1143 S32: 0.0591 S33: -0.0534
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 37 A 57
REMARK 3 ORIGIN FOR THE GROUP (A): -1.0430 14.2640 -6.7230
REMARK 3 T TENSOR
REMARK 3 T11: 0.0785 T22: 0.0576
REMARK 3 T33: 0.0428 T12: -0.0103
REMARK 3 T13: 0.0116 T23: 0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 3.4401 L22: 4.4684
REMARK 3 L33: 0.8076 L12: -2.5249
REMARK 3 L13: 0.8123 L23: -0.7213
REMARK 3 S TENSOR
REMARK 3 S11: -0.1369 S12: -0.1673 S13: 0.1872
REMARK 3 S21: 0.2051 S22: 0.1473 S23: -0.0856
REMARK 3 S31: -0.0765 S32: 0.0291 S33: -0.0105
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 58 A 85
REMARK 3 ORIGIN FOR THE GROUP (A): -0.7040 20.7680 -18.7010
REMARK 3 T TENSOR
REMARK 3 T11: 0.0338 T22: 0.0491
REMARK 3 T33: 0.0385 T12: -0.0147
REMARK 3 T13: 0.0020 T23: 0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 0.4416 L22: 3.3110
REMARK 3 L33: 0.9483 L12: -0.2873
REMARK 3 L13: -0.4151 L23: -1.0503
REMARK 3 S TENSOR
REMARK 3 S11: -0.0315 S12: 0.0283 S13: 0.0783
REMARK 3 S21: -0.0303 S22: 0.0724 S23: -0.1152
REMARK 3 S31: 0.0102 S32: -0.0327 S33: -0.0409
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 86 A 144
REMARK 3 ORIGIN FOR THE GROUP (A): -3.8260 9.0440 -28.4390
REMARK 3 T TENSOR
REMARK 3 T11: 0.0987 T22: 0.0695
REMARK 3 T33: 0.0375 T12: -0.0088
REMARK 3 T13: 0.0014 T23: 0.0117
REMARK 3 L TENSOR
REMARK 3 L11: 1.3404 L22: 1.9347
REMARK 3 L33: 1.5599 L12: -0.1347
REMARK 3 L13: 0.1619 L23: 0.5210
REMARK 3 S TENSOR
REMARK 3 S11: 0.0213 S12: 0.1228 S13: -0.1151
REMARK 3 S21: -0.1732 S22: -0.0067 S23: 0.0769
REMARK 3 S31: 0.0674 S32: -0.1713 S33: -0.0146
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 145 A 201
REMARK 3 ORIGIN FOR THE GROUP (A): 1.6320 -0.0990 -30.6050
REMARK 3 T TENSOR
REMARK 3 T11: 0.1354 T22: 0.0785
REMARK 3 T33: 0.0232 T12: -0.0102
REMARK 3 T13: -0.0098 T23: -0.0300
REMARK 3 L TENSOR
REMARK 3 L11: 1.9273 L22: 2.8141
REMARK 3 L33: 1.8181 L12: 0.3619
REMARK 3 L13: -0.8860 L23: -0.7511
REMARK 3 S TENSOR
REMARK 3 S11: -0.0034 S12: 0.1100 S13: -0.0691
REMARK 3 S21: -0.1668 S22: 0.0191 S23: 0.0362
REMARK 3 S31: 0.2425 S32: -0.0050 S33: -0.0156
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 202 A 239
REMARK 3 ORIGIN FOR THE GROUP (A): -0.4780 -4.0170 -18.2400
REMARK 3 T TENSOR
REMARK 3 T11: 0.0938 T22: 0.0011
REMARK 3 T33: 0.0314 T12: -0.0101
REMARK 3 T13: -0.0323 T23: 0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 0.6230 L22: 1.7173
REMARK 3 L33: 3.4283 L12: -0.1230
REMARK 3 L13: 0.1498 L23: -0.4322
REMARK 3 S TENSOR
REMARK 3 S11: -0.0079 S12: -0.0449 S13: -0.1515
REMARK 3 S21: -0.0771 S22: 0.1059 S23: 0.0631
REMARK 3 S31: 0.4769 S32: -0.0056 S33: -0.0980
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 240 A 254
REMARK 3 ORIGIN FOR THE GROUP (A): 2.2450 -5.9640 -9.1150
REMARK 3 T TENSOR
REMARK 3 T11: 0.1369 T22: 0.0105
REMARK 3 T33: 0.0325 T12: -0.0124
REMARK 3 T13: -0.0514 T23: 0.0176
REMARK 3 L TENSOR
REMARK 3 L11: 8.1140 L22: 7.0935
REMARK 3 L33: 8.8075 L12: -3.6440
REMARK 3 L13: -4.4629 L23: 1.7360
REMARK 3 S TENSOR
REMARK 3 S11: -0.2422 S12: -0.4359 S13: -0.2820
REMARK 3 S21: 0.3207 S22: 0.2349 S23: -0.1002
REMARK 3 S31: 0.5718 S32: 0.3743 S33: 0.0073
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 : B 1 B 17
REMARK 3 ORIGIN FOR THE GROUP (A): -10.5140 36.6380 -11.9420
REMARK 3 T TENSOR
REMARK 3 T11: 0.0869 T22: 0.0698
REMARK 3 T33: 0.0904 T12: -0.0237
REMARK 3 T13: -0.0048 T23: 0.0356
REMARK 3 L TENSOR
REMARK 3 L11: 2.5838 L22: 3.1413
REMARK 3 L33: 1.0510 L12: -1.4903
REMARK 3 L13: 0.2567 L23: 0.6264
REMARK 3 S TENSOR
REMARK 3 S11: 0.0213 S12: -0.0933 S13: 0.0123
REMARK 3 S21: 0.0673 S22: 0.0159 S23: 0.0721
REMARK 3 S31: -0.0646 S32: -0.0608 S33: -0.0373
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 : B 18 B 51
REMARK 3 ORIGIN FOR THE GROUP (A): -5.5350 35.3920 -6.2720
REMARK 3 T TENSOR
REMARK 3 T11: 0.0290 T22: 0.0245
REMARK 3 T33: 0.0252 T12: -0.0108
REMARK 3 T13: -0.0206 T23: 0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 2.5157 L22: 3.9841
REMARK 3 L33: 0.9751 L12: -1.1029
REMARK 3 L13: -0.3959 L23: 0.6679
REMARK 3 S TENSOR
REMARK 3 S11: -0.0721 S12: -0.1595 S13: 0.1782
REMARK 3 S21: 0.2514 S22: 0.1134 S23: -0.2488
REMARK 3 S31: -0.0589 S32: 0.1417 S33: -0.0413
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 : B 52 B 87
REMARK 3 ORIGIN FOR THE GROUP (A): -13.4890 23.3680 -9.4590
REMARK 3 T TENSOR
REMARK 3 T11: 0.0180 T22: 0.0440
REMARK 3 T33: 0.0474 T12: -0.0010
REMARK 3 T13: -0.0029 T23: 0.0137
REMARK 3 L TENSOR
REMARK 3 L11: 0.6533 L22: 3.1378
REMARK 3 L33: 0.7462 L12: -0.1421
REMARK 3 L13: -0.4312 L23: 0.6597
REMARK 3 S TENSOR
REMARK 3 S11: -0.0632 S12: -0.0565 S13: -0.0498
REMARK 3 S21: 0.1694 S22: 0.1053 S23: -0.0042
REMARK 3 S31: 0.0335 S32: 0.0659 S33: -0.0420
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 : B 88 B 125
REMARK 3 ORIGIN FOR THE GROUP (A): -20.3940 27.2210 -19.7040
REMARK 3 T TENSOR
REMARK 3 T11: 0.0329 T22: 0.0680
REMARK 3 T33: 0.0683 T12: -0.0058
REMARK 3 T13: -0.0145 T23: 0.0125
REMARK 3 L TENSOR
REMARK 3 L11: 2.5416 L22: 1.8913
REMARK 3 L33: 2.5815 L12: 0.0906
REMARK 3 L13: 0.4086 L23: 0.3891
REMARK 3 S TENSOR
REMARK 3 S11: 0.0097 S12: 0.2364 S13: -0.0592
REMARK 3 S21: -0.0818 S22: 0.0242 S23: 0.0330
REMARK 3 S31: 0.0085 S32: -0.0251 S33: -0.0339
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 : B 126 B 138
REMARK 3 ORIGIN FOR THE GROUP (A): -22.1590 40.3300 -33.9990
REMARK 3 T TENSOR
REMARK 3 T11: 0.0681 T22: 0.1128
REMARK 3 T33: 0.0460 T12: -0.0453
REMARK 3 T13: -0.0140 T23: 0.0827
REMARK 3 L TENSOR
REMARK 3 L11: 2.7114 L22: 4.9253
REMARK 3 L33: 12.4296 L12: -1.0295
REMARK 3 L13: 1.4384 L23: -5.5147
REMARK 3 S TENSOR
REMARK 3 S11: -0.0204 S12: 0.4050 S13: 0.2342
REMARK 3 S21: -0.4122 S22: 0.1024 S23: -0.0270
REMARK 3 S31: -0.0191 S32: -0.1694 S33: -0.0820
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 139 B 229
REMARK 3 ORIGIN FOR THE GROUP (A): -25.6430 41.9060 -20.9820
REMARK 3 T TENSOR
REMARK 3 T11: 0.0287 T22: 0.0830
REMARK 3 T33: 0.0788 T12: 0.0084
REMARK 3 T13: -0.0040 T23: 0.0649
REMARK 3 L TENSOR
REMARK 3 L11: 1.8565 L22: 2.4022
REMARK 3 L33: 1.4932 L12: 0.5001
REMARK 3 L13: 0.3745 L23: 0.4105
REMARK 3 S TENSOR
REMARK 3 S11: -0.0593 S12: 0.1706 S13: 0.2442
REMARK 3 S21: -0.0958 S22: 0.0315 S23: 0.0492
REMARK 3 S31: -0.1309 S32: 0.0450 S33: 0.0279
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 230 B 254
REMARK 3 ORIGIN FOR THE GROUP (A): -11.0090 46.3720 -11.1550
REMARK 3 T TENSOR
REMARK 3 T11: 0.0899 T22: 0.0516
REMARK 3 T33: 0.1113 T12: -0.0310
REMARK 3 T13: 0.0172 T23: 0.0398
REMARK 3 L TENSOR
REMARK 3 L11: 3.6953 L22: 4.7279
REMARK 3 L33: 3.0784 L12: -1.2567
REMARK 3 L13: 0.7265 L23: 1.2722
REMARK 3 S TENSOR
REMARK 3 S11: -0.1232 S12: -0.0691 S13: 0.2575
REMARK 3 S21: 0.1421 S22: 0.1203 S23: -0.1575
REMARK 3 S31: -0.1786 S32: -0.0243 S33: 0.0029
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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: NULL
REMARK 4
REMARK 4 4IOT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JAN-13.
REMARK 100 THE DEPOSITION ID IS D_1000077020.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-MAR-12
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 : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97670
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38754
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 75.160
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.5600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.40400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.290
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: 1TRE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS AND 20% PEG5000 MME, PH
REMARK 280 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K
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 23.23500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.17700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.72600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 75.17700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.23500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.72600
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: 3480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 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 ALA A 255
REMARK 465 ALA B 255
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 NH1 ARG B 16 O HOH B 444 2.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LYS A 11 -144.23 54.28
REMARK 500 LYS B 11 -145.74 51.09
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
DBREF 4IOT A 1 255 UNP B1XB85 TPIS_ECODH 1 255
DBREF 4IOT B 1 255 UNP B1XB85 TPIS_ECODH 1 255
SEQRES 1 A 255 MET ARG HIS PRO LEU VAL MET GLY ASN TRP LYS LEU ASN
SEQRES 2 A 255 GLY SER ARG HIS MET VAL HIS GLU LEU VAL SER ASN LEU
SEQRES 3 A 255 ARG LYS GLU LEU ALA GLY VAL ALA GLY CYS ALA VAL ALA
SEQRES 4 A 255 ILE ALA PRO PRO GLU MET TYR ILE ASP MET ALA LYS ARG
SEQRES 5 A 255 GLU ALA GLU GLY SER HIS ILE MET LEU GLY ALA GLN ASN
SEQRES 6 A 255 VAL ASP LEU ASN LEU SER GLY ALA PHE THR GLY GLU THR
SEQRES 7 A 255 SER ALA ALA MET LEU LYS ASP ILE GLY ALA GLN TYR ILE
SEQRES 8 A 255 ILE ILE GLY HIS SER GLU ARG ARG THR TYR HIS LYS GLU
SEQRES 9 A 255 SER ASP GLU LEU ILE ALA LYS LYS PHE ALA VAL LEU LYS
SEQRES 10 A 255 GLU GLN GLY LEU THR PRO VAL LEU CYS ILE GLY GLU THR
SEQRES 11 A 255 GLU ALA GLU ASN GLU ALA GLY LYS THR GLU GLU VAL CYS
SEQRES 12 A 255 ALA ARG GLN ILE ASP ALA VAL LEU LYS THR GLN GLY ALA
SEQRES 13 A 255 ALA ALA PHE GLU GLY ALA VAL ILE ALA TYR GLU PRO VAL
SEQRES 14 A 255 TRP ALA ILE GLY THR GLY LYS SER ALA THR PRO ALA GLN
SEQRES 15 A 255 ALA GLN ALA VAL HIS LYS PHE ILE ARG ASP HIS ILE ALA
SEQRES 16 A 255 LYS VAL ASP ALA ASN ILE ALA GLU GLN VAL ILE ILE GLN
SEQRES 17 A 255 TYR GLY GLY SER VAL ASN ALA SER ASN ALA ALA GLU LEU
SEQRES 18 A 255 PHE ALA GLN PRO ASP ILE ASP GLY ALA LEU VAL GLY GLY
SEQRES 19 A 255 ALA SER LEU LYS ALA ASP ALA PHE ALA VAL ILE VAL LYS
SEQRES 20 A 255 ALA ALA GLU ALA ALA LYS GLN ALA
SEQRES 1 B 255 MET ARG HIS PRO LEU VAL MET GLY ASN TRP LYS LEU ASN
SEQRES 2 B 255 GLY SER ARG HIS MET VAL HIS GLU LEU VAL SER ASN LEU
SEQRES 3 B 255 ARG LYS GLU LEU ALA GLY VAL ALA GLY CYS ALA VAL ALA
SEQRES 4 B 255 ILE ALA PRO PRO GLU MET TYR ILE ASP MET ALA LYS ARG
SEQRES 5 B 255 GLU ALA GLU GLY SER HIS ILE MET LEU GLY ALA GLN ASN
SEQRES 6 B 255 VAL ASP LEU ASN LEU SER GLY ALA PHE THR GLY GLU THR
SEQRES 7 B 255 SER ALA ALA MET LEU LYS ASP ILE GLY ALA GLN TYR ILE
SEQRES 8 B 255 ILE ILE GLY HIS SER GLU ARG ARG THR TYR HIS LYS GLU
SEQRES 9 B 255 SER ASP GLU LEU ILE ALA LYS LYS PHE ALA VAL LEU LYS
SEQRES 10 B 255 GLU GLN GLY LEU THR PRO VAL LEU CYS ILE GLY GLU THR
SEQRES 11 B 255 GLU ALA GLU ASN GLU ALA GLY LYS THR GLU GLU VAL CYS
SEQRES 12 B 255 ALA ARG GLN ILE ASP ALA VAL LEU LYS THR GLN GLY ALA
SEQRES 13 B 255 ALA ALA PHE GLU GLY ALA VAL ILE ALA TYR GLU PRO VAL
SEQRES 14 B 255 TRP ALA ILE GLY THR GLY LYS SER ALA THR PRO ALA GLN
SEQRES 15 B 255 ALA GLN ALA VAL HIS LYS PHE ILE ARG ASP HIS ILE ALA
SEQRES 16 B 255 LYS VAL ASP ALA ASN ILE ALA GLU GLN VAL ILE ILE GLN
SEQRES 17 B 255 TYR GLY GLY SER VAL ASN ALA SER ASN ALA ALA GLU LEU
SEQRES 18 B 255 PHE ALA GLN PRO ASP ILE ASP GLY ALA LEU VAL GLY GLY
SEQRES 19 B 255 ALA SER LEU LYS ALA ASP ALA PHE ALA VAL ILE VAL LYS
SEQRES 20 B 255 ALA ALA GLU ALA ALA LYS GLN ALA
HET SO4 A 301 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 O4 S 2-
FORMUL 4 HOH *474(H2 O)
HELIX 1 1 SER A 15 ALA A 31 1 17
HELIX 2 2 PRO A 43 MET A 45 5 3
HELIX 3 3 TYR A 46 GLU A 55 1 10
HELIX 4 4 SER A 79 GLY A 87 1 9
HELIX 5 5 HIS A 95 HIS A 102 1 8
HELIX 6 6 SER A 105 GLN A 119 1 15
HELIX 7 7 THR A 130 ALA A 136 1 7
HELIX 8 8 LYS A 138 GLY A 155 1 18
HELIX 9 9 ALA A 156 GLU A 160 5 5
HELIX 10 10 PRO A 168 ILE A 172 5 5
HELIX 11 11 THR A 179 LYS A 196 1 18
HELIX 12 12 ASP A 198 VAL A 205 1 8
HELIX 13 13 ASN A 217 ALA A 223 1 7
HELIX 14 14 GLY A 233 LEU A 237 5 5
HELIX 15 15 LYS A 238 GLN A 254 1 17
HELIX 16 16 SER B 15 LEU B 30 1 16
HELIX 17 17 PRO B 43 MET B 45 5 3
HELIX 18 18 TYR B 46 ALA B 54 1 9
HELIX 19 19 SER B 79 GLY B 87 1 9
HELIX 20 20 HIS B 95 HIS B 102 1 8
HELIX 21 21 SER B 105 GLY B 120 1 16
HELIX 22 22 THR B 130 ALA B 136 1 7
HELIX 23 23 LYS B 138 GLY B 155 1 18
HELIX 24 24 ALA B 156 GLU B 160 5 5
HELIX 25 25 PRO B 168 ILE B 172 5 5
HELIX 26 26 THR B 179 LYS B 196 1 18
HELIX 27 27 ASP B 198 VAL B 205 1 8
HELIX 28 28 ASN B 217 ALA B 223 1 7
HELIX 29 29 GLY B 233 LEU B 237 5 5
HELIX 30 30 LYS B 238 GLN B 254 1 17
SHEET 1 A 9 LEU A 5 ASN A 9 0
SHEET 2 A 9 ALA A 37 ALA A 41 1 O ALA A 41 N GLY A 8
SHEET 3 A 9 ILE A 59 ALA A 63 1 O MET A 60 N VAL A 38
SHEET 4 A 9 ALA A 88 ILE A 93 1 O ILE A 92 N ALA A 63
SHEET 5 A 9 THR A 122 ILE A 127 1 O THR A 122 N GLN A 89
SHEET 6 A 9 VAL A 163 TYR A 166 1 O ALA A 165 N LEU A 125
SHEET 7 A 9 ILE A 206 TYR A 209 1 O GLN A 208 N ILE A 164
SHEET 8 A 9 GLY A 229 VAL A 232 1 O GLY A 229 N TYR A 209
SHEET 9 A 9 LEU A 5 ASN A 9 1 N MET A 7 O VAL A 232
SHEET 1 B 9 LEU B 5 ASN B 9 0
SHEET 2 B 9 ALA B 37 ALA B 41 1 O ALA B 39 N GLY B 8
SHEET 3 B 9 MET B 60 ALA B 63 1 O MET B 60 N VAL B 38
SHEET 4 B 9 TYR B 90 ILE B 93 1 O ILE B 92 N ALA B 63
SHEET 5 B 9 THR B 122 ILE B 127 1 O CYS B 126 N ILE B 93
SHEET 6 B 9 VAL B 163 TYR B 166 1 O VAL B 163 N LEU B 125
SHEET 7 B 9 ILE B 206 TYR B 209 1 O GLN B 208 N ILE B 164
SHEET 8 B 9 GLY B 229 VAL B 232 1 O GLY B 229 N TYR B 209
SHEET 9 B 9 LEU B 5 ASN B 9 1 N MET B 7 O VAL B 232
SITE 1 AC1 5 SER A 212 GLY A 234 HOH A 432 HOH A 541
SITE 2 AC1 5 HOH A 642
CRYST1 46.470 67.452 150.354 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 0.021519 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014825 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006651 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
