HEADER OXIDOREDUCTASE 20-JUL-11 3T0G
TITLE ISPH:HMBPP (SUBSTRATE) STRUCTURE OF THE T167C MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 4-HYDROXY-3-METHYLBUT-2-ENYL DIPHOSPHATE REDUCTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ISPH;
COMPND 5 EC: 1.17.1.2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: ISPH, LYTB, YAAE, B0029, JW0027;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS 3FE-4S IRON-SULFUR CLUSTER, CONSERVED CYSTEINE, IPP AND DMAPP
KEYWDS 2 PRODUCTION FINAL STEP, NON-MEVALONATE PATHWAY, SUBSTRATE HMBPP, LOW
KEYWDS 3 ACTIVITY, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.SPAN,T.GRAEWERT,A.BACHER,W.EISENREICH,M.GROLL
REVDAT 4 13-SEP-23 3T0G 1 REMARK SEQADV LINK
REVDAT 3 15-FEB-12 3T0G 1 JRNL
REVDAT 2 11-JAN-12 3T0G 1 JRNL
REVDAT 1 30-NOV-11 3T0G 0
JRNL AUTH I.SPAN,T.GRAWERT,A.BACHER,W.EISENREICH,M.GROLL
JRNL TITL CRYSTAL STRUCTURES OF MUTANT ISPH PROTEINS REVEAL A ROTATION
JRNL TITL 2 OF THE SUBSTRATE'S HYDROXYMETHYL GROUP DURING CATALYSIS.
JRNL REF J.MOL.BIOL. V. 416 1 2012
JRNL REFN ISSN 0022-2836
JRNL PMID 22137895
JRNL DOI 10.1016/J.JMB.2011.11.033
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 35246
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) : 0.218
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : 0.278
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1855
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2399
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2820
REMARK 3 BIN FREE R VALUE SET COUNT : 127
REMARK 3 BIN FREE R VALUE : 0.3320
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4771
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 44
REMARK 3 SOLVENT ATOMS : 141
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.76
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.98000
REMARK 3 B22 (A**2) : -3.28000
REMARK 3 B33 (A**2) : 1.30000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.222
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.169
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.661
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.913
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4894 ; 0.021 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6631 ; 1.871 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 617 ; 6.250 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 226 ;40.681 ;24.159
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 854 ;16.588 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 44 ;20.467 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 761 ; 0.126 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3674 ; 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): 3079 ; 0.968 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4968 ; 1.665 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1815 ; 2.845 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1651 ; 4.331 ; 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 309 4
REMARK 3 1 B 1 B 309 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 2389 ; 0.39 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 2389 ; 0.39 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 2389 ; 1.22 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 2389 ; 1.22 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 40
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 7
REMARK 3 RESIDUE RANGE : A 997 A 997
REMARK 3 ORIGIN FOR THE GROUP (A): -8.9788 -7.9518 -7.4654
REMARK 3 T TENSOR
REMARK 3 T11: 0.0418 T22: 0.0374
REMARK 3 T33: 0.1102 T12: -0.0131
REMARK 3 T13: -0.0063 T23: -0.0182
REMARK 3 L TENSOR
REMARK 3 L11: 0.6007 L22: 1.7163
REMARK 3 L33: 0.7177 L12: -0.8745
REMARK 3 L13: 0.0034 L23: 0.5566
REMARK 3 S TENSOR
REMARK 3 S11: 0.0356 S12: -0.0991 S13: 0.2153
REMARK 3 S21: 0.0666 S22: 0.0958 S23: -0.4078
REMARK 3 S31: 0.1574 S32: -0.0563 S33: -0.1315
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 8 A 24
REMARK 3 ORIGIN FOR THE GROUP (A): -29.6165 -10.1267 -10.6140
REMARK 3 T TENSOR
REMARK 3 T11: 0.0261 T22: 0.0832
REMARK 3 T33: 0.0227 T12: 0.0086
REMARK 3 T13: -0.0031 T23: 0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 0.1462 L22: 0.4389
REMARK 3 L33: 0.0031 L12: -0.2289
REMARK 3 L13: -0.0089 L23: 0.0001
REMARK 3 S TENSOR
REMARK 3 S11: 0.0517 S12: -0.0170 S13: -0.0085
REMARK 3 S21: -0.1021 S22: -0.0527 S23: -0.0022
REMARK 3 S31: -0.0006 S32: 0.0131 S33: 0.0010
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 25 A 37
REMARK 3 ORIGIN FOR THE GROUP (A): -40.2438 -13.4406 -21.5898
REMARK 3 T TENSOR
REMARK 3 T11: 0.1065 T22: 0.0344
REMARK 3 T33: 0.0513 T12: 0.0173
REMARK 3 T13: -0.0714 T23: -0.0204
REMARK 3 L TENSOR
REMARK 3 L11: 1.6534 L22: 5.6674
REMARK 3 L33: 0.7998 L12: 0.6329
REMARK 3 L13: 1.1032 L23: 0.9824
REMARK 3 S TENSOR
REMARK 3 S11: 0.2579 S12: 0.0364 S13: -0.1352
REMARK 3 S21: -0.2477 S22: -0.2194 S23: 0.2341
REMARK 3 S31: 0.1131 S32: -0.0005 S33: -0.0385
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 38 A 49
REMARK 3 ORIGIN FOR THE GROUP (A): -26.7017 -10.4350 -21.5539
REMARK 3 T TENSOR
REMARK 3 T11: 0.0589 T22: 0.0528
REMARK 3 T33: 0.0313 T12: 0.0078
REMARK 3 T13: -0.0087 T23: -0.0268
REMARK 3 L TENSOR
REMARK 3 L11: 4.2813 L22: 1.2952
REMARK 3 L33: 1.1475 L12: -1.2586
REMARK 3 L13: -0.2374 L23: -0.9534
REMARK 3 S TENSOR
REMARK 3 S11: 0.2307 S12: 0.2305 S13: -0.3297
REMARK 3 S21: -0.1308 S22: -0.1987 S23: 0.1437
REMARK 3 S31: 0.0479 S32: 0.1419 S33: -0.0321
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 50 A 64
REMARK 3 ORIGIN FOR THE GROUP (A): -37.4840 -9.9984 -27.4885
REMARK 3 T TENSOR
REMARK 3 T11: 0.1138 T22: 0.1881
REMARK 3 T33: 0.0412 T12: 0.0204
REMARK 3 T13: 0.0382 T23: -0.0279
REMARK 3 L TENSOR
REMARK 3 L11: 5.6626 L22: 4.5783
REMARK 3 L33: 1.5440 L12: -2.0860
REMARK 3 L13: 1.7820 L23: 0.9996
REMARK 3 S TENSOR
REMARK 3 S11: 0.2366 S12: 0.9909 S13: -0.0212
REMARK 3 S21: -0.5829 S22: -0.2475 S23: -0.1627
REMARK 3 S31: -0.0686 S32: 0.3151 S33: 0.0109
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 65 A 77
REMARK 3 ORIGIN FOR THE GROUP (A): -41.1832 -4.6925 -20.6953
REMARK 3 T TENSOR
REMARK 3 T11: 0.1305 T22: 0.0857
REMARK 3 T33: 0.0341 T12: 0.0346
REMARK 3 T13: 0.0011 T23: -0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 0.0634 L22: 2.3187
REMARK 3 L33: 0.4871 L12: -0.1628
REMARK 3 L13: -0.1607 L23: 0.1849
REMARK 3 S TENSOR
REMARK 3 S11: 0.0627 S12: 0.0504 S13: -0.0020
REMARK 3 S21: -0.1275 S22: -0.0657 S23: 0.2436
REMARK 3 S31: -0.0282 S32: -0.1350 S33: 0.0030
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 78 A 89
REMARK 3 ORIGIN FOR THE GROUP (A): -48.5854 -0.4793 -22.3764
REMARK 3 T TENSOR
REMARK 3 T11: 0.1283 T22: 0.0907
REMARK 3 T33: 0.1338 T12: 0.0115
REMARK 3 T13: -0.0761 T23: -0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 1.3911 L22: 3.9185
REMARK 3 L33: 3.0655 L12: 0.6235
REMARK 3 L13: -0.4470 L23: 2.8666
REMARK 3 S TENSOR
REMARK 3 S11: 0.0289 S12: 0.0797 S13: 0.2472
REMARK 3 S21: -0.1250 S22: -0.2143 S23: 0.5504
REMARK 3 S31: 0.0790 S32: -0.2580 S33: 0.1854
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 90 A 103
REMARK 3 ORIGIN FOR THE GROUP (A): -38.8040 -0.4756 -11.5937
REMARK 3 T TENSOR
REMARK 3 T11: 0.0309 T22: 0.0591
REMARK 3 T33: 0.0146 T12: 0.0105
REMARK 3 T13: -0.0078 T23: -0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 0.2347 L22: 1.2321
REMARK 3 L33: 0.1616 L12: 0.0738
REMARK 3 L13: -0.1928 L23: -0.1212
REMARK 3 S TENSOR
REMARK 3 S11: 0.0611 S12: 0.0061 S13: -0.0062
REMARK 3 S21: -0.1080 S22: -0.0605 S23: 0.0554
REMARK 3 S31: -0.0460 S32: -0.0045 S33: -0.0005
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 104 A 114
REMARK 3 ORIGIN FOR THE GROUP (A): -43.6425 15.5043 -9.0890
REMARK 3 T TENSOR
REMARK 3 T11: 0.1559 T22: 0.0833
REMARK 3 T33: 0.2146 T12: 0.0377
REMARK 3 T13: 0.1373 T23: 0.0560
REMARK 3 L TENSOR
REMARK 3 L11: 6.9653 L22: 4.0090
REMARK 3 L33: 2.2320 L12: 2.6219
REMARK 3 L13: 0.5781 L23: 2.4384
REMARK 3 S TENSOR
REMARK 3 S11: 0.2744 S12: -0.2417 S13: 0.2292
REMARK 3 S21: 0.6111 S22: -0.1811 S23: 0.3226
REMARK 3 S31: 0.2148 S32: -0.2670 S33: -0.0934
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 115 A 127
REMARK 3 ORIGIN FOR THE GROUP (A): -30.9542 11.7670 -17.7106
REMARK 3 T TENSOR
REMARK 3 T11: 0.0263 T22: 0.0471
REMARK 3 T33: 0.0227 T12: 0.0121
REMARK 3 T13: -0.0176 T23: 0.0116
REMARK 3 L TENSOR
REMARK 3 L11: 0.3217 L22: 6.5256
REMARK 3 L33: 1.3688 L12: -0.8942
REMARK 3 L13: -0.6634 L23: 1.8039
REMARK 3 S TENSOR
REMARK 3 S11: -0.0174 S12: -0.0065 S13: 0.0322
REMARK 3 S21: -0.2393 S22: 0.0888 S23: 0.1827
REMARK 3 S31: 0.0339 S32: 0.0157 S33: -0.0714
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 128 A 162
REMARK 3 ORIGIN FOR THE GROUP (A): -34.4218 20.8701 -16.4872
REMARK 3 T TENSOR
REMARK 3 T11: 0.0344 T22: 0.0297
REMARK 3 T33: 0.0426 T12: -0.0003
REMARK 3 T13: -0.0170 T23: 0.0306
REMARK 3 L TENSOR
REMARK 3 L11: 2.0612 L22: 2.1285
REMARK 3 L33: 0.7357 L12: 0.8878
REMARK 3 L13: 0.3261 L23: 0.0024
REMARK 3 S TENSOR
REMARK 3 S11: -0.1414 S12: 0.1290 S13: 0.1523
REMARK 3 S21: -0.2106 S22: 0.1276 S23: 0.2569
REMARK 3 S31: -0.0478 S32: -0.0169 S33: 0.0138
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 163 A 181
REMARK 3 ORIGIN FOR THE GROUP (A): -23.6006 14.2227 -10.3343
REMARK 3 T TENSOR
REMARK 3 T11: 0.0295 T22: 0.0365
REMARK 3 T33: 0.0252 T12: 0.0103
REMARK 3 T13: 0.0163 T23: -0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 0.2663 L22: 2.1431
REMARK 3 L33: 0.2256 L12: -0.7258
REMARK 3 L13: 0.2387 L23: -0.6933
REMARK 3 S TENSOR
REMARK 3 S11: -0.0165 S12: -0.0030 S13: -0.0041
REMARK 3 S21: 0.0588 S22: 0.0065 S23: -0.0294
REMARK 3 S31: -0.0150 S32: 0.0008 S33: 0.0100
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 : A 182 A 193
REMARK 3 ORIGIN FOR THE GROUP (A): -29.2930 22.5851 -5.3559
REMARK 3 T TENSOR
REMARK 3 T11: 0.0865 T22: 0.0136
REMARK 3 T33: 0.0211 T12: -0.0034
REMARK 3 T13: 0.0126 T23: -0.0148
REMARK 3 L TENSOR
REMARK 3 L11: 1.7686 L22: 2.7691
REMARK 3 L33: 5.0403 L12: 1.6123
REMARK 3 L13: -0.7908 L23: -3.1691
REMARK 3 S TENSOR
REMARK 3 S11: 0.0654 S12: -0.0244 S13: 0.1117
REMARK 3 S21: 0.2227 S22: -0.0020 S23: 0.1048
REMARK 3 S31: -0.2612 S32: -0.0380 S33: -0.0635
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 : A 194 A 210
REMARK 3 ORIGIN FOR THE GROUP (A): -19.2614 2.7764 -6.0288
REMARK 3 T TENSOR
REMARK 3 T11: 0.0315 T22: 0.0517
REMARK 3 T33: 0.0183 T12: 0.0072
REMARK 3 T13: 0.0044 T23: -0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 1.5837 L22: 0.3468
REMARK 3 L33: 0.1801 L12: -0.4459
REMARK 3 L13: 0.0053 L23: -0.1993
REMARK 3 S TENSOR
REMARK 3 S11: 0.0570 S12: -0.1021 S13: 0.0904
REMARK 3 S21: -0.0628 S22: -0.0128 S23: 0.0164
REMARK 3 S31: 0.0373 S32: 0.0228 S33: -0.0442
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 : A 211 A 246
REMARK 3 ORIGIN FOR THE GROUP (A): -11.4595 0.1612 -16.1130
REMARK 3 T TENSOR
REMARK 3 T11: 0.0182 T22: 0.0362
REMARK 3 T33: 0.0272 T12: 0.0035
REMARK 3 T13: 0.0210 T23: 0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 0.4998 L22: 0.6742
REMARK 3 L33: 0.1863 L12: 0.1250
REMARK 3 L13: -0.1916 L23: 0.2201
REMARK 3 S TENSOR
REMARK 3 S11: 0.0077 S12: 0.0409 S13: 0.0159
REMARK 3 S21: -0.0087 S22: 0.0115 S23: -0.0485
REMARK 3 S31: -0.0010 S32: -0.0165 S33: -0.0192
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 : A 247 A 261
REMARK 3 ORIGIN FOR THE GROUP (A): -2.7758 -8.6424 -21.0433
REMARK 3 T TENSOR
REMARK 3 T11: 0.0732 T22: 0.0309
REMARK 3 T33: 0.1141 T12: -0.0090
REMARK 3 T13: 0.0905 T23: -0.0114
REMARK 3 L TENSOR
REMARK 3 L11: 2.6761 L22: 0.0410
REMARK 3 L33: 5.1328 L12: -0.0467
REMARK 3 L13: -0.2323 L23: -0.0403
REMARK 3 S TENSOR
REMARK 3 S11: -0.0696 S12: 0.1572 S13: -0.0261
REMARK 3 S21: -0.0522 S22: 0.0040 S23: -0.0671
REMARK 3 S31: 0.1024 S32: 0.3059 S33: 0.0656
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 : A 262 A 280
REMARK 3 ORIGIN FOR THE GROUP (A): -14.7064 -12.0026 -13.7944
REMARK 3 T TENSOR
REMARK 3 T11: 0.0315 T22: 0.0352
REMARK 3 T33: 0.0128 T12: 0.0122
REMARK 3 T13: 0.0090 T23: 0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 1.6050 L22: 2.0070
REMARK 3 L33: 0.0056 L12: 0.2952
REMARK 3 L13: 0.0892 L23: 0.0482
REMARK 3 S TENSOR
REMARK 3 S11: 0.0441 S12: -0.0798 S13: -0.1087
REMARK 3 S21: 0.0667 S22: -0.0360 S23: -0.0031
REMARK 3 S31: 0.0031 S32: -0.0068 S33: -0.0081
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 : A 281 A 297
REMARK 3 ORIGIN FOR THE GROUP (A): -7.6419 -11.9865 -7.7052
REMARK 3 T TENSOR
REMARK 3 T11: 0.0304 T22: 0.0326
REMARK 3 T33: 0.0859 T12: -0.0027
REMARK 3 T13: -0.0350 T23: 0.0335
REMARK 3 L TENSOR
REMARK 3 L11: 2.6871 L22: 1.5413
REMARK 3 L33: 4.2676 L12: -1.3116
REMARK 3 L13: -2.5542 L23: 2.2071
REMARK 3 S TENSOR
REMARK 3 S11: 0.0364 S12: -0.1859 S13: -0.1550
REMARK 3 S21: 0.1159 S22: 0.0163 S23: -0.1763
REMARK 3 S31: 0.1233 S32: 0.0756 S33: -0.0527
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 : A 298 A 304
REMARK 3 ORIGIN FOR THE GROUP (A): -31.2907 -7.3296 -1.8958
REMARK 3 T TENSOR
REMARK 3 T11: 0.0326 T22: 0.0383
REMARK 3 T33: 0.0452 T12: -0.0125
REMARK 3 T13: 0.0200 T23: -0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 5.0563 L22: 0.6376
REMARK 3 L33: 2.1182 L12: 1.7067
REMARK 3 L13: 2.7103 L23: 1.1104
REMARK 3 S TENSOR
REMARK 3 S11: 0.0816 S12: -0.0893 S13: -0.1412
REMARK 3 S21: 0.0589 S22: -0.0467 S23: -0.0495
REMARK 3 S31: 0.1689 S32: -0.1265 S33: -0.0349
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 : A 305 A 309
REMARK 3 ORIGIN FOR THE GROUP (A): -44.0100 -13.5126 -7.5579
REMARK 3 T TENSOR
REMARK 3 T11: 0.0271 T22: 0.0400
REMARK 3 T33: 0.0252 T12: -0.0027
REMARK 3 T13: 0.0136 T23: 0.0054
REMARK 3 L TENSOR
REMARK 3 L11: 4.8400 L22: 8.0392
REMARK 3 L33: 6.9746 L12: -2.4158
REMARK 3 L13: -2.0464 L23: 2.5886
REMARK 3 S TENSOR
REMARK 3 S11: 0.0408 S12: -0.0336 S13: -0.0680
REMARK 3 S21: 0.3982 S22: 0.0269 S23: 0.3130
REMARK 3 S31: 0.1265 S32: -0.4087 S33: -0.0676
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 7
REMARK 3 RESIDUE RANGE : B 997 B 997
REMARK 3 ORIGIN FOR THE GROUP (A): -56.5756 -7.5308 8.2066
REMARK 3 T TENSOR
REMARK 3 T11: 0.0418 T22: 0.0541
REMARK 3 T33: 0.0647 T12: -0.0228
REMARK 3 T13: -0.0272 T23: -0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 1.1274 L22: 0.5646
REMARK 3 L33: 0.6440 L12: 0.1327
REMARK 3 L13: 0.5064 L23: -0.2510
REMARK 3 S TENSOR
REMARK 3 S11: -0.0710 S12: 0.1152 S13: -0.0620
REMARK 3 S21: -0.1274 S22: 0.1129 S23: 0.1350
REMARK 3 S31: 0.0609 S32: -0.0535 S33: -0.0419
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 8 B 49
REMARK 3 ORIGIN FOR THE GROUP (A): -33.3292 -10.9286 17.9870
REMARK 3 T TENSOR
REMARK 3 T11: 0.0388 T22: 0.0371
REMARK 3 T33: 0.0177 T12: 0.0002
REMARK 3 T13: -0.0231 T23: 0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 0.5397 L22: 0.4450
REMARK 3 L33: 0.4139 L12: -0.3141
REMARK 3 L13: 0.3991 L23: -0.2477
REMARK 3 S TENSOR
REMARK 3 S11: 0.0113 S12: 0.0574 S13: -0.0011
REMARK 3 S21: 0.0502 S22: 0.0277 S23: -0.0190
REMARK 3 S31: 0.0409 S32: -0.0028 S33: -0.0391
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 50 B 54
REMARK 3 ORIGIN FOR THE GROUP (A): -33.1718 -17.5494 25.7322
REMARK 3 T TENSOR
REMARK 3 T11: 0.0332 T22: 0.0472
REMARK 3 T33: 0.0189 T12: -0.0340
REMARK 3 T13: -0.0205 T23: 0.0256
REMARK 3 L TENSOR
REMARK 3 L11: 3.5208 L22: 5.4952
REMARK 3 L33: 0.8891 L12: 0.8954
REMARK 3 L13: -0.2977 L23: 0.5875
REMARK 3 S TENSOR
REMARK 3 S11: 0.2467 S12: -0.1124 S13: -0.1177
REMARK 3 S21: 0.1109 S22: -0.1565 S23: -0.2335
REMARK 3 S31: 0.0948 S32: -0.1844 S33: -0.0902
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 55 B 76
REMARK 3 ORIGIN FOR THE GROUP (A): -24.3715 -5.4335 24.7875
REMARK 3 T TENSOR
REMARK 3 T11: 0.0352 T22: 0.0601
REMARK 3 T33: 0.0223 T12: 0.0060
REMARK 3 T13: -0.0229 T23: -0.0218
REMARK 3 L TENSOR
REMARK 3 L11: 1.0605 L22: 0.3883
REMARK 3 L33: 0.3244 L12: 0.0462
REMARK 3 L13: 0.2778 L23: -0.2978
REMARK 3 S TENSOR
REMARK 3 S11: 0.0476 S12: -0.0097 S13: 0.0017
REMARK 3 S21: -0.0342 S22: -0.0059 S23: 0.0442
REMARK 3 S31: 0.0430 S32: 0.0133 S33: -0.0417
REMARK 3
REMARK 3 TLS GROUP : 25
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 77 B 86
REMARK 3 ORIGIN FOR THE GROUP (A): -17.8105 2.2725 20.8108
REMARK 3 T TENSOR
REMARK 3 T11: 0.0188 T22: 0.0342
REMARK 3 T33: 0.1676 T12: -0.0087
REMARK 3 T13: -0.0402 T23: 0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 2.3890 L22: 1.3252
REMARK 3 L33: 5.6113 L12: -0.4008
REMARK 3 L13: 2.9408 L23: -2.0065
REMARK 3 S TENSOR
REMARK 3 S11: -0.0648 S12: 0.0714 S13: 0.2890
REMARK 3 S21: 0.0294 S22: -0.1427 S23: -0.0577
REMARK 3 S31: -0.0547 S32: 0.2218 S33: 0.2076
REMARK 3
REMARK 3 TLS GROUP : 26
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 87 B 100
REMARK 3 ORIGIN FOR THE GROUP (A): -22.7375 -4.0321 15.8390
REMARK 3 T TENSOR
REMARK 3 T11: 0.0433 T22: 0.0480
REMARK 3 T33: 0.0271 T12: -0.0045
REMARK 3 T13: -0.0201 T23: -0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 1.6941 L22: 0.6917
REMARK 3 L33: 1.9438 L12: -0.9933
REMARK 3 L13: 1.6974 L23: -0.8343
REMARK 3 S TENSOR
REMARK 3 S11: 0.0513 S12: 0.0482 S13: -0.0146
REMARK 3 S21: -0.0359 S22: 0.0168 S23: -0.0292
REMARK 3 S31: 0.0328 S32: 0.0961 S33: -0.0681
REMARK 3
REMARK 3 TLS GROUP : 27
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 101 B 112
REMARK 3 ORIGIN FOR THE GROUP (A): -23.1743 12.4005 8.7720
REMARK 3 T TENSOR
REMARK 3 T11: 0.0546 T22: 0.0288
REMARK 3 T33: 0.1044 T12: 0.0309
REMARK 3 T13: 0.0294 T23: 0.0390
REMARK 3 L TENSOR
REMARK 3 L11: 5.7801 L22: 5.6720
REMARK 3 L33: 1.5836 L12: 4.1691
REMARK 3 L13: 0.3721 L23: 2.3071
REMARK 3 S TENSOR
REMARK 3 S11: 0.1861 S12: 0.3191 S13: 0.3173
REMARK 3 S21: -0.1801 S22: 0.0634 S23: -0.1291
REMARK 3 S31: -0.2253 S32: -0.1109 S33: -0.2495
REMARK 3
REMARK 3 TLS GROUP : 28
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 113 B 127
REMARK 3 ORIGIN FOR THE GROUP (A): -32.4823 13.4748 16.8976
REMARK 3 T TENSOR
REMARK 3 T11: 0.0351 T22: 0.0485
REMARK 3 T33: 0.0546 T12: 0.0112
REMARK 3 T13: -0.0299 T23: 0.0155
REMARK 3 L TENSOR
REMARK 3 L11: 0.0994 L22: 3.0921
REMARK 3 L33: 0.1091 L12: -0.5540
REMARK 3 L13: -0.0359 L23: 0.1835
REMARK 3 S TENSOR
REMARK 3 S11: -0.0327 S12: -0.0128 S13: 0.0290
REMARK 3 S21: 0.1648 S22: 0.0796 S23: -0.1506
REMARK 3 S31: -0.0012 S32: -0.0606 S33: -0.0469
REMARK 3
REMARK 3 TLS GROUP : 29
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 128 B 140
REMARK 3 ORIGIN FOR THE GROUP (A): -23.2419 15.0530 17.8675
REMARK 3 T TENSOR
REMARK 3 T11: 0.0386 T22: 0.0760
REMARK 3 T33: 0.1330 T12: -0.0038
REMARK 3 T13: -0.0593 T23: -0.0444
REMARK 3 L TENSOR
REMARK 3 L11: 2.4655 L22: 1.5644
REMARK 3 L33: 1.0290 L12: 0.6664
REMARK 3 L13: -0.0090 L23: -0.1277
REMARK 3 S TENSOR
REMARK 3 S11: 0.0044 S12: -0.3875 S13: 0.2442
REMARK 3 S21: 0.0675 S22: -0.0041 S23: -0.1808
REMARK 3 S31: 0.0202 S32: 0.0643 S33: -0.0003
REMARK 3
REMARK 3 TLS GROUP : 30
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 141 B 181
REMARK 3 ORIGIN FOR THE GROUP (A): -37.5397 19.9629 13.4453
REMARK 3 T TENSOR
REMARK 3 T11: 0.0214 T22: 0.0255
REMARK 3 T33: 0.0397 T12: 0.0084
REMARK 3 T13: -0.0021 T23: 0.0029
REMARK 3 L TENSOR
REMARK 3 L11: 1.4659 L22: 1.7778
REMARK 3 L33: 0.2817 L12: 0.6647
REMARK 3 L13: -0.0290 L23: -0.0218
REMARK 3 S TENSOR
REMARK 3 S11: 0.0162 S12: -0.0349 S13: 0.1674
REMARK 3 S21: 0.1146 S22: 0.0255 S23: -0.0633
REMARK 3 S31: -0.0258 S32: -0.0806 S33: -0.0417
REMARK 3
REMARK 3 TLS GROUP : 31
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 182 B 193
REMARK 3 ORIGIN FOR THE GROUP (A): -36.0501 22.6066 5.4211
REMARK 3 T TENSOR
REMARK 3 T11: 0.0789 T22: 0.0259
REMARK 3 T33: 0.1129 T12: -0.0128
REMARK 3 T13: 0.0246 T23: 0.0366
REMARK 3 L TENSOR
REMARK 3 L11: 1.5639 L22: 6.8361
REMARK 3 L33: 2.1126 L12: 1.4143
REMARK 3 L13: 1.0041 L23: 3.7631
REMARK 3 S TENSOR
REMARK 3 S11: 0.0281 S12: 0.1118 S13: 0.3958
REMARK 3 S21: -0.1191 S22: -0.1549 S23: 0.1090
REMARK 3 S31: -0.0470 S32: -0.0620 S33: 0.1268
REMARK 3
REMARK 3 TLS GROUP : 32
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 194 B 207
REMARK 3 ORIGIN FOR THE GROUP (A): -43.8218 3.2684 6.2212
REMARK 3 T TENSOR
REMARK 3 T11: 0.0187 T22: 0.0553
REMARK 3 T33: 0.0101 T12: 0.0037
REMARK 3 T13: -0.0104 T23: 0.0114
REMARK 3 L TENSOR
REMARK 3 L11: 2.7221 L22: 1.1691
REMARK 3 L33: 0.3639 L12: 1.5640
REMARK 3 L13: -0.7013 L23: -0.1812
REMARK 3 S TENSOR
REMARK 3 S11: 0.0228 S12: 0.0425 S13: 0.0390
REMARK 3 S21: -0.0069 S22: -0.0094 S23: 0.0191
REMARK 3 S31: -0.0224 S32: -0.0287 S33: -0.0133
REMARK 3
REMARK 3 TLS GROUP : 33
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 208 B 216
REMARK 3 ORIGIN FOR THE GROUP (A): -60.1843 0.4854 8.5394
REMARK 3 T TENSOR
REMARK 3 T11: 0.0134 T22: 0.0079
REMARK 3 T33: 0.1121 T12: 0.0031
REMARK 3 T13: -0.0178 T23: -0.0107
REMARK 3 L TENSOR
REMARK 3 L11: 8.0607 L22: 0.0014
REMARK 3 L33: 4.0998 L12: 0.0847
REMARK 3 L13: -3.4571 L23: -0.0315
REMARK 3 S TENSOR
REMARK 3 S11: 0.0982 S12: 0.0436 S13: 0.3657
REMARK 3 S21: -0.0005 S22: -0.0027 S23: 0.0104
REMARK 3 S31: -0.1888 S32: -0.0447 S33: -0.0954
REMARK 3
REMARK 3 TLS GROUP : 34
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 217 B 235
REMARK 3 ORIGIN FOR THE GROUP (A): -48.9158 0.5898 17.6255
REMARK 3 T TENSOR
REMARK 3 T11: 0.0660 T22: 0.0411
REMARK 3 T33: 0.0339 T12: 0.0060
REMARK 3 T13: 0.0123 T23: 0.0099
REMARK 3 L TENSOR
REMARK 3 L11: 0.7249 L22: 0.5834
REMARK 3 L33: 1.0765 L12: -0.1345
REMARK 3 L13: -0.4224 L23: -0.6008
REMARK 3 S TENSOR
REMARK 3 S11: -0.0679 S12: -0.0299 S13: -0.0760
REMARK 3 S21: 0.1899 S22: 0.0493 S23: 0.0449
REMARK 3 S31: -0.1741 S32: -0.0157 S33: 0.0185
REMARK 3
REMARK 3 TLS GROUP : 35
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 236 B 248
REMARK 3 ORIGIN FOR THE GROUP (A): -56.1005 -0.6697 18.8150
REMARK 3 T TENSOR
REMARK 3 T11: 0.0239 T22: 0.0447
REMARK 3 T33: 0.0333 T12: -0.0021
REMARK 3 T13: 0.0214 T23: -0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 0.7992 L22: 4.4549
REMARK 3 L33: 0.9600 L12: -1.2789
REMARK 3 L13: 0.7598 L23: -0.4730
REMARK 3 S TENSOR
REMARK 3 S11: -0.0901 S12: -0.0682 S13: 0.0000
REMARK 3 S21: 0.2246 S22: 0.0497 S23: 0.1659
REMARK 3 S31: -0.0624 S32: -0.0657 S33: 0.0404
REMARK 3
REMARK 3 TLS GROUP : 36
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 249 B 261
REMARK 3 ORIGIN FOR THE GROUP (A): -63.5521 -7.8101 21.7719
REMARK 3 T TENSOR
REMARK 3 T11: 0.0491 T22: 0.0748
REMARK 3 T33: 0.1070 T12: -0.0156
REMARK 3 T13: 0.0671 T23: -0.0097
REMARK 3 L TENSOR
REMARK 3 L11: 5.6176 L22: 2.8908
REMARK 3 L33: 5.9344 L12: -1.9355
REMARK 3 L13: 0.9239 L23: -0.5769
REMARK 3 S TENSOR
REMARK 3 S11: -0.0912 S12: -0.4252 S13: -0.0181
REMARK 3 S21: 0.3299 S22: 0.1112 S23: 0.4932
REMARK 3 S31: 0.1581 S32: -0.5575 S33: -0.0200
REMARK 3
REMARK 3 TLS GROUP : 37
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 262 B 280
REMARK 3 ORIGIN FOR THE GROUP (A): -50.5492 -11.4391 14.3489
REMARK 3 T TENSOR
REMARK 3 T11: 0.0266 T22: 0.0367
REMARK 3 T33: 0.0136 T12: -0.0103
REMARK 3 T13: -0.0086 T23: 0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 1.3307 L22: 1.7226
REMARK 3 L33: 0.2059 L12: 0.0949
REMARK 3 L13: -0.3832 L23: 0.3772
REMARK 3 S TENSOR
REMARK 3 S11: 0.0225 S12: 0.0625 S13: -0.0368
REMARK 3 S21: 0.0900 S22: -0.0444 S23: 0.0605
REMARK 3 S31: 0.0137 S32: -0.0266 S33: 0.0219
REMARK 3
REMARK 3 TLS GROUP : 38
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 281 B 297
REMARK 3 ORIGIN FOR THE GROUP (A): -57.6718 -11.4248 8.6176
REMARK 3 T TENSOR
REMARK 3 T11: 0.0401 T22: 0.0347
REMARK 3 T33: 0.0814 T12: 0.0014
REMARK 3 T13: -0.0389 T23: -0.0146
REMARK 3 L TENSOR
REMARK 3 L11: 2.1898 L22: 4.1304
REMARK 3 L33: 4.2041 L12: 1.3550
REMARK 3 L13: -2.1252 L23: -1.2705
REMARK 3 S TENSOR
REMARK 3 S11: -0.0037 S12: 0.2704 S13: -0.0438
REMARK 3 S21: -0.1406 S22: 0.1031 S23: 0.4531
REMARK 3 S31: 0.2738 S32: -0.2689 S33: -0.0994
REMARK 3
REMARK 3 TLS GROUP : 39
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 298 B 305
REMARK 3 ORIGIN FOR THE GROUP (A): -32.9204 -7.7092 3.1076
REMARK 3 T TENSOR
REMARK 3 T11: 0.0734 T22: 0.0684
REMARK 3 T33: 0.0119 T12: 0.0010
REMARK 3 T13: 0.0240 T23: -0.0112
REMARK 3 L TENSOR
REMARK 3 L11: 4.4463 L22: 0.3777
REMARK 3 L33: 2.4401 L12: -1.2514
REMARK 3 L13: 2.8485 L23: -0.9261
REMARK 3 S TENSOR
REMARK 3 S11: -0.0259 S12: 0.1857 S13: -0.0215
REMARK 3 S21: -0.0334 S22: -0.0402 S23: -0.0099
REMARK 3 S31: 0.1904 S32: 0.0989 S33: 0.0661
REMARK 3
REMARK 3 TLS GROUP : 40
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 306 B 310
REMARK 3 ORIGIN FOR THE GROUP (A): -22.2258 -15.4829 7.9667
REMARK 3 T TENSOR
REMARK 3 T11: 0.0277 T22: 0.0442
REMARK 3 T33: 0.0147 T12: 0.0112
REMARK 3 T13: 0.0047 T23: -0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 7.3486 L22: 1.4867
REMARK 3 L33: 2.5149 L12: -0.5575
REMARK 3 L13: -1.7045 L23: 0.8188
REMARK 3 S TENSOR
REMARK 3 S11: -0.0256 S12: 0.3239 S13: 0.1460
REMARK 3 S21: -0.0616 S22: 0.1250 S23: -0.1408
REMARK 3 S31: 0.1862 S32: 0.1570 S33: -0.0994
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES : RESIDUAL ONLY
REMARK 4
REMARK 4 3T0G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUL-11.
REMARK 100 THE DEPOSITION ID IS D_1000066880.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-APR-11
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 : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : FIXED-EXIT LN2 COOLED DOUBLE
REMARK 200 CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS, XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37485
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.12300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.54400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: PDB ENTRY 3F7T
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM LITHIUM SULFATE, 25% PEG3350,
REMARK 280 100 MM BIS-TRIS, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 34.77000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.28000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.42500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.28000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.77000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.42500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 -11
REMARK 465 ARG A -10
REMARK 465 GLY A -9
REMARK 465 SER A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 VAL A 310
REMARK 465 ASP A 311
REMARK 465 ILE A 312
REMARK 465 ARG A 313
REMARK 465 GLU A 314
REMARK 465 VAL A 315
REMARK 465 ASP A 316
REMARK 465 MET B -11
REMARK 465 ARG B -10
REMARK 465 GLY B -9
REMARK 465 SER B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 ASP B 311
REMARK 465 ILE B 312
REMARK 465 ARG B 313
REMARK 465 GLU B 314
REMARK 465 VAL B 315
REMARK 465 ASP B 316
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 GLU A 128 CG GLU A 128 CD 0.090
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 B 230 NE - CZ - NH1 ANGL. DEV. = -3.6 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 PHE A 11 128.62 -38.63
REMARK 500 HIS A 37 158.09 68.64
REMARK 500 PRO A 64 -169.99 -57.98
REMARK 500 ARG A 87 20.55 -161.19
REMARK 500 ASP A 88 71.72 47.37
REMARK 500 LYS A 160 78.99 -105.18
REMARK 500 LYS A 193 -80.72 -132.63
REMARK 500 HIS B 37 170.51 67.39
REMARK 500 ASN B 157 98.33 -162.34
REMARK 500 LYS B 193 -73.20 -136.61
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 F3S A 997 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 12 SG
REMARK 620 2 F3S A 997 S1 118.3
REMARK 620 3 F3S A 997 S2 106.4 108.2
REMARK 620 4 F3S A 997 S3 112.1 106.2 104.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S A 997 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 96 SG
REMARK 620 2 F3S A 997 S2 113.0
REMARK 620 3 F3S A 997 S3 112.0 106.8
REMARK 620 4 F3S A 997 S4 114.2 106.6 103.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S A 997 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 197 SG
REMARK 620 2 F3S A 997 S1 102.0
REMARK 620 3 F3S A 997 S3 118.3 106.8
REMARK 620 4 F3S A 997 S4 114.9 113.9 101.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S B 997 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 12 SG
REMARK 620 2 F3S B 997 S1 116.8
REMARK 620 3 F3S B 997 S2 105.7 104.9
REMARK 620 4 F3S B 997 S3 114.7 109.5 103.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S B 997 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 96 SG
REMARK 620 2 F3S B 997 S2 114.9
REMARK 620 3 F3S B 997 S3 112.7 104.5
REMARK 620 4 F3S B 997 S4 114.0 106.3 103.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S B 997 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 197 SG
REMARK 620 2 F3S B 997 S1 107.7
REMARK 620 3 F3S B 997 S3 112.1 108.2
REMARK 620 4 F3S B 997 S4 115.2 113.6 99.9
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S A 997
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H6P A 998
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S B 997
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H6P B 998
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3F7T RELATED DB: PDB
REMARK 900 E. COLI ISPH - CLOSED CONFORMATION
REMARK 900 RELATED ID: 3DNF RELATED DB: PDB
REMARK 900 A. AEOLICUS ISPH - OPEN CONFORMATION
REMARK 900 RELATED ID: 3SZL RELATED DB: PDB
REMARK 900 ISPH:HMBPP STRUCTURE, WILD TYPE AFTER 70 SECONDS
REMARK 900 RELATED ID: 3SZO RELATED DB: PDB
REMARK 900 ISPH:HMBPP STRUCTURE AFTER 3 MINUTES X-RAY PRE-EXPOSURE
REMARK 900 RELATED ID: 3SZU RELATED DB: PDB
REMARK 900 ISPH:HMBPP STRUCTURE, E126Q MUTANT
REMARK 900 RELATED ID: 3T0F RELATED DB: PDB
REMARK 900 ISPH:HMBPP STRUCTURE, E126D MUTANT
DBREF 3T0G A 1 316 UNP P62623 ISPH_ECOLI 1 316
DBREF 3T0G B 1 316 UNP P62623 ISPH_ECOLI 1 316
SEQADV 3T0G MET A -11 UNP P62623 EXPRESSION TAG
SEQADV 3T0G ARG A -10 UNP P62623 EXPRESSION TAG
SEQADV 3T0G GLY A -9 UNP P62623 EXPRESSION TAG
SEQADV 3T0G SER A -8 UNP P62623 EXPRESSION TAG
SEQADV 3T0G HIS A -7 UNP P62623 EXPRESSION TAG
SEQADV 3T0G HIS A -6 UNP P62623 EXPRESSION TAG
SEQADV 3T0G HIS A -5 UNP P62623 EXPRESSION TAG
SEQADV 3T0G HIS A -4 UNP P62623 EXPRESSION TAG
SEQADV 3T0G HIS A -3 UNP P62623 EXPRESSION TAG
SEQADV 3T0G HIS A -2 UNP P62623 EXPRESSION TAG
SEQADV 3T0G GLY A -1 UNP P62623 EXPRESSION TAG
SEQADV 3T0G SER A 0 UNP P62623 EXPRESSION TAG
SEQADV 3T0G CYS A 167 UNP P62623 THR 167 ENGINEERED MUTATION
SEQADV 3T0G MET B -11 UNP P62623 EXPRESSION TAG
SEQADV 3T0G ARG B -10 UNP P62623 EXPRESSION TAG
SEQADV 3T0G GLY B -9 UNP P62623 EXPRESSION TAG
SEQADV 3T0G SER B -8 UNP P62623 EXPRESSION TAG
SEQADV 3T0G HIS B -7 UNP P62623 EXPRESSION TAG
SEQADV 3T0G HIS B -6 UNP P62623 EXPRESSION TAG
SEQADV 3T0G HIS B -5 UNP P62623 EXPRESSION TAG
SEQADV 3T0G HIS B -4 UNP P62623 EXPRESSION TAG
SEQADV 3T0G HIS B -3 UNP P62623 EXPRESSION TAG
SEQADV 3T0G HIS B -2 UNP P62623 EXPRESSION TAG
SEQADV 3T0G GLY B -1 UNP P62623 EXPRESSION TAG
SEQADV 3T0G SER B 0 UNP P62623 EXPRESSION TAG
SEQADV 3T0G CYS B 167 UNP P62623 THR 167 ENGINEERED MUTATION
SEQRES 1 A 328 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER MET
SEQRES 2 A 328 GLN ILE LEU LEU ALA ASN PRO ARG GLY PHE CYS ALA GLY
SEQRES 3 A 328 VAL ASP ARG ALA ILE SER ILE VAL GLU ASN ALA LEU ALA
SEQRES 4 A 328 ILE TYR GLY ALA PRO ILE TYR VAL ARG HIS GLU VAL VAL
SEQRES 5 A 328 HIS ASN ARG TYR VAL VAL ASP SER LEU ARG GLU ARG GLY
SEQRES 6 A 328 ALA ILE PHE ILE GLU GLN ILE SER GLU VAL PRO ASP GLY
SEQRES 7 A 328 ALA ILE LEU ILE PHE SER ALA HIS GLY VAL SER GLN ALA
SEQRES 8 A 328 VAL ARG ASN GLU ALA LYS SER ARG ASP LEU THR VAL PHE
SEQRES 9 A 328 ASP ALA THR CYS PRO LEU VAL THR LYS VAL HIS MET GLU
SEQRES 10 A 328 VAL ALA ARG ALA SER ARG ARG GLY GLU GLU SER ILE LEU
SEQRES 11 A 328 ILE GLY HIS ALA GLY HIS PRO GLU VAL GLU GLY THR MET
SEQRES 12 A 328 GLY GLN TYR SER ASN PRO GLU GLY GLY MET TYR LEU VAL
SEQRES 13 A 328 GLU SER PRO ASP ASP VAL TRP LYS LEU THR VAL LYS ASN
SEQRES 14 A 328 GLU GLU LYS LEU SER PHE MET THR GLN CYS THR LEU SER
SEQRES 15 A 328 VAL ASP ASP THR SER ASP VAL ILE ASP ALA LEU ARG LYS
SEQRES 16 A 328 ARG PHE PRO LYS ILE VAL GLY PRO ARG LYS ASP ASP ILE
SEQRES 17 A 328 CYS TYR ALA THR THR ASN ARG GLN GLU ALA VAL ARG ALA
SEQRES 18 A 328 LEU ALA GLU GLN ALA GLU VAL VAL LEU VAL VAL GLY SER
SEQRES 19 A 328 LYS ASN SER SER ASN SER ASN ARG LEU ALA GLU LEU ALA
SEQRES 20 A 328 GLN ARG MET GLY LYS ARG ALA PHE LEU ILE ASP ASP ALA
SEQRES 21 A 328 LYS ASP ILE GLN GLU GLU TRP VAL LYS GLU VAL LYS CYS
SEQRES 22 A 328 VAL GLY VAL THR ALA GLY ALA SER ALA PRO ASP ILE LEU
SEQRES 23 A 328 VAL GLN ASN VAL VAL ALA ARG LEU GLN GLN LEU GLY GLY
SEQRES 24 A 328 GLY GLU ALA ILE PRO LEU GLU GLY ARG GLU GLU ASN ILE
SEQRES 25 A 328 VAL PHE GLU VAL PRO LYS GLU LEU ARG VAL ASP ILE ARG
SEQRES 26 A 328 GLU VAL ASP
SEQRES 1 B 328 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER MET
SEQRES 2 B 328 GLN ILE LEU LEU ALA ASN PRO ARG GLY PHE CYS ALA GLY
SEQRES 3 B 328 VAL ASP ARG ALA ILE SER ILE VAL GLU ASN ALA LEU ALA
SEQRES 4 B 328 ILE TYR GLY ALA PRO ILE TYR VAL ARG HIS GLU VAL VAL
SEQRES 5 B 328 HIS ASN ARG TYR VAL VAL ASP SER LEU ARG GLU ARG GLY
SEQRES 6 B 328 ALA ILE PHE ILE GLU GLN ILE SER GLU VAL PRO ASP GLY
SEQRES 7 B 328 ALA ILE LEU ILE PHE SER ALA HIS GLY VAL SER GLN ALA
SEQRES 8 B 328 VAL ARG ASN GLU ALA LYS SER ARG ASP LEU THR VAL PHE
SEQRES 9 B 328 ASP ALA THR CYS PRO LEU VAL THR LYS VAL HIS MET GLU
SEQRES 10 B 328 VAL ALA ARG ALA SER ARG ARG GLY GLU GLU SER ILE LEU
SEQRES 11 B 328 ILE GLY HIS ALA GLY HIS PRO GLU VAL GLU GLY THR MET
SEQRES 12 B 328 GLY GLN TYR SER ASN PRO GLU GLY GLY MET TYR LEU VAL
SEQRES 13 B 328 GLU SER PRO ASP ASP VAL TRP LYS LEU THR VAL LYS ASN
SEQRES 14 B 328 GLU GLU LYS LEU SER PHE MET THR GLN CYS THR LEU SER
SEQRES 15 B 328 VAL ASP ASP THR SER ASP VAL ILE ASP ALA LEU ARG LYS
SEQRES 16 B 328 ARG PHE PRO LYS ILE VAL GLY PRO ARG LYS ASP ASP ILE
SEQRES 17 B 328 CYS TYR ALA THR THR ASN ARG GLN GLU ALA VAL ARG ALA
SEQRES 18 B 328 LEU ALA GLU GLN ALA GLU VAL VAL LEU VAL VAL GLY SER
SEQRES 19 B 328 LYS ASN SER SER ASN SER ASN ARG LEU ALA GLU LEU ALA
SEQRES 20 B 328 GLN ARG MET GLY LYS ARG ALA PHE LEU ILE ASP ASP ALA
SEQRES 21 B 328 LYS ASP ILE GLN GLU GLU TRP VAL LYS GLU VAL LYS CYS
SEQRES 22 B 328 VAL GLY VAL THR ALA GLY ALA SER ALA PRO ASP ILE LEU
SEQRES 23 B 328 VAL GLN ASN VAL VAL ALA ARG LEU GLN GLN LEU GLY GLY
SEQRES 24 B 328 GLY GLU ALA ILE PRO LEU GLU GLY ARG GLU GLU ASN ILE
SEQRES 25 B 328 VAL PHE GLU VAL PRO LYS GLU LEU ARG VAL ASP ILE ARG
SEQRES 26 B 328 GLU VAL ASP
HET F3S A 997 7
HET H6P A 998 15
HET F3S B 997 7
HET H6P B 998 15
HETNAM F3S FE3-S4 CLUSTER
HETNAM H6P (2E)-4-HYDROXY-3-METHYLBUT-2-EN-1-YL TRIHYDROGEN
HETNAM 2 H6P DIPHOSPHATE
FORMUL 3 F3S 2(FE3 S4)
FORMUL 4 H6P 2(C5 H12 O8 P2)
FORMUL 7 HOH *141(H2 O)
HELIX 1 1 CYS A 12 GLY A 30 1 19
HELIX 2 2 ASN A 42 GLU A 51 1 10
HELIX 3 3 SER A 77 SER A 86 1 10
HELIX 4 4 CYS A 96 ARG A 112 1 17
HELIX 5 5 HIS A 124 GLY A 132 1 9
HELIX 6 6 SER A 146 LEU A 153 1 8
HELIX 7 7 SER A 170 PHE A 185 1 16
HELIX 8 8 CYS A 197 ALA A 214 1 18
HELIX 9 9 SER A 225 MET A 238 1 14
HELIX 10 10 ASP A 247 ILE A 251 5 5
HELIX 11 11 GLN A 252 LYS A 257 1 6
HELIX 12 12 PRO A 271 LEU A 285 1 15
HELIX 13 13 PRO A 305 ARG A 309 5 5
HELIX 14 14 CYS B 12 GLY B 30 1 19
HELIX 15 15 ASN B 42 GLU B 51 1 10
HELIX 16 16 GLN B 59 VAL B 63 5 5
HELIX 17 17 SER B 77 ARG B 87 1 11
HELIX 18 18 CYS B 96 ARG B 112 1 17
HELIX 19 19 HIS B 124 GLY B 132 1 9
HELIX 20 20 SER B 146 LEU B 153 1 8
HELIX 21 21 SER B 170 PHE B 185 1 16
HELIX 22 22 CYS B 197 ALA B 214 1 18
HELIX 23 23 SER B 225 MET B 238 1 14
HELIX 24 24 ASP B 247 ILE B 251 5 5
HELIX 25 25 GLN B 252 VAL B 256 5 5
HELIX 26 26 PRO B 271 LEU B 285 1 15
HELIX 27 27 PRO B 305 ARG B 309 5 5
SHEET 1 A 5 ARG A 241 ILE A 245 0
SHEET 2 A 5 VAL A 216 VAL A 220 1 N VAL A 219 O PHE A 243
SHEET 3 A 5 CYS A 261 ALA A 266 1 O GLY A 263 N VAL A 216
SHEET 4 A 5 GLN A 2 LEU A 5 1 N LEU A 4 O VAL A 262
SHEET 5 A 5 ALA A 290 PRO A 292 1 O ILE A 291 N LEU A 5
SHEET 1 B 4 ALA A 54 ILE A 57 0
SHEET 2 B 4 ILE A 33 ARG A 36 1 N ILE A 33 O ILE A 55
SHEET 3 B 4 ILE A 68 PHE A 71 1 O ILE A 68 N TYR A 34
SHEET 4 B 4 THR A 90 ASP A 93 1 O THR A 90 N LEU A 69
SHEET 1 C 3 MET A 141 VAL A 144 0
SHEET 2 C 3 GLU A 115 ILE A 119 1 N SER A 116 O TYR A 142
SHEET 3 C 3 LEU A 161 THR A 165 1 O MET A 164 N ILE A 119
SHEET 1 D 2 ILE A 300 PHE A 302 0
SHEET 2 D 2 ILE B 300 PHE B 302 -1 O VAL B 301 N VAL A 301
SHEET 1 E 5 ARG B 241 ILE B 245 0
SHEET 2 E 5 VAL B 216 VAL B 220 1 N VAL B 219 O ILE B 245
SHEET 3 E 5 CYS B 261 ALA B 266 1 O GLY B 263 N VAL B 216
SHEET 4 E 5 GLN B 2 LEU B 5 1 N GLN B 2 O VAL B 262
SHEET 5 E 5 ALA B 290 PRO B 292 1 O ILE B 291 N LEU B 5
SHEET 1 F 4 ALA B 54 ILE B 57 0
SHEET 2 F 4 ILE B 33 ARG B 36 1 N ILE B 33 O ILE B 55
SHEET 3 F 4 ILE B 68 PHE B 71 1 O ILE B 70 N ARG B 36
SHEET 4 F 4 THR B 90 ASP B 93 1 O THR B 90 N LEU B 69
SHEET 1 G 3 MET B 141 VAL B 144 0
SHEET 2 G 3 GLU B 115 ILE B 119 1 N LEU B 118 O TYR B 142
SHEET 3 G 3 LEU B 161 THR B 165 1 O SER B 162 N ILE B 117
LINK SG CYS A 12 FE1 F3S A 997 1555 1555 2.24
LINK SG CYS A 96 FE4 F3S A 997 1555 1555 2.24
LINK SG CYS A 197 FE3 F3S A 997 1555 1555 2.36
LINK SG CYS B 12 FE1 F3S B 997 1555 1555 2.09
LINK SG CYS B 96 FE4 F3S B 997 1555 1555 2.23
LINK SG CYS B 197 FE3 F3S B 997 1555 1555 2.37
CISPEP 1 ASN A 7 PRO A 8 0 1.65
CISPEP 2 ALA A 31 PRO A 32 0 -16.21
CISPEP 3 ASN B 7 PRO B 8 0 1.10
CISPEP 4 ALA B 31 PRO B 32 0 -0.30
SITE 1 AC1 5 CYS A 12 CYS A 96 CYS A 167 CYS A 197
SITE 2 AC1 5 H6P A 998
SITE 1 AC2 13 VAL A 40 HIS A 41 ALA A 73 HIS A 74
SITE 2 AC2 13 HIS A 124 GLU A 126 THR A 168 ASN A 224
SITE 3 AC2 13 SER A 225 SER A 226 ASN A 227 SER A 269
SITE 4 AC2 13 F3S A 997
SITE 1 AC3 7 CYS B 12 CYS B 96 LEU B 98 CYS B 167
SITE 2 AC3 7 CYS B 197 ALA B 268 H6P B 998
SITE 1 AC4 14 VAL B 15 VAL B 40 HIS B 41 ALA B 73
SITE 2 AC4 14 HIS B 74 HIS B 124 GLU B 126 THR B 168
SITE 3 AC4 14 ASN B 224 SER B 225 SER B 226 ASN B 227
SITE 4 AC4 14 SER B 269 F3S B 997
CRYST1 69.540 80.850 112.560 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 0.014380 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012369 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008884 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
