HEADER OXIDOREDUCTASE 19-JUL-11 3SZO
TITLE ISPH:HMBPP COMPLEX AFTER 3 MINUTES X-RAY PRE-EXPOSURE
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
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 4FE-4S IRON-SULFUR CLUSTER, CONSERVED CYSTEINE, IPP AND DMAPP
KEYWDS 2 PRODUCTION FINAL STEP, NON-MEVALONATE PATHWAY, SUBSTRATE HMBPP,
KEYWDS 3 ALTERNATE CONFORMATIONS, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.SPAN,T.GRAEWERT,A.BACHER,W.EISENREICH,M.GROLL
REVDAT 4 13-SEP-23 3SZO 1 REMARK SEQADV LINK
REVDAT 3 15-FEB-12 3SZO 1 JRNL
REVDAT 2 11-JAN-12 3SZO 1 JRNL
REVDAT 1 30-NOV-11 3SZO 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. 1.60 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) : 1.60
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 : 73426
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) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3865
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5442
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE SET COUNT : 287
REMARK 3 BIN FREE R VALUE : 0.3080
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4773
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 46
REMARK 3 SOLVENT ATOMS : 603
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.87
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.41000
REMARK 3 B22 (A**2) : -1.68000
REMARK 3 B33 (A**2) : 2.09000
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): 0.157
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.106
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.070
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.454
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4895 ; 0.022 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6644 ; 1.650 ; 1.976
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 617 ; 3.699 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 226 ;40.695 ;24.159
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 853 ;13.877 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 44 ;21.028 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 764 ; 2.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3666 ; 0.010 ; 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): 3073 ; 1.875 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4961 ; 2.553 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1822 ; 3.943 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1659 ; 5.238 ; 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): 4895 ; 2.807 ; 3.000
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): 2383 ; 0.43 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 2383 ; 0.43 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 2383 ; 2.10 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 2383 ; 2.10 ; 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 : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 7
REMARK 3 ORIGIN FOR THE GROUP (A): -6.2473 -8.8142 -7.0609
REMARK 3 T TENSOR
REMARK 3 T11: 0.1112 T22: 0.1310
REMARK 3 T33: 0.1264 T12: 0.0210
REMARK 3 T13: -0.0217 T23: 0.0235
REMARK 3 L TENSOR
REMARK 3 L11: 11.9057 L22: 4.0476
REMARK 3 L33: 3.5448 L12: -6.6947
REMARK 3 L13: -4.0348 L23: 3.0518
REMARK 3 S TENSOR
REMARK 3 S11: -0.1397 S12: -0.0641 S13: 0.0072
REMARK 3 S21: 0.1511 S22: 0.1145 S23: 0.0030
REMARK 3 S31: 0.2067 S32: 0.1854 S33: 0.0252
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): -29.5056 -10.2147 -10.5691
REMARK 3 T TENSOR
REMARK 3 T11: 0.1330 T22: 0.1521
REMARK 3 T33: 0.0988 T12: -0.0018
REMARK 3 T13: -0.0039 T23: -0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 1.9421 L22: 0.8755
REMARK 3 L33: 0.3197 L12: 1.0639
REMARK 3 L13: 0.7342 L23: 0.5098
REMARK 3 S TENSOR
REMARK 3 S11: 0.0375 S12: -0.0947 S13: -0.1494
REMARK 3 S21: -0.0280 S22: -0.0180 S23: -0.0245
REMARK 3 S31: -0.0029 S32: -0.0161 S33: -0.0195
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): -40.3447 -12.6207 -22.3205
REMARK 3 T TENSOR
REMARK 3 T11: 0.0518 T22: 0.1003
REMARK 3 T33: 0.1118 T12: 0.0287
REMARK 3 T13: -0.0481 T23: -0.0490
REMARK 3 L TENSOR
REMARK 3 L11: 2.4244 L22: 2.2291
REMARK 3 L33: 1.7068 L12: 1.2917
REMARK 3 L13: 0.5442 L23: 1.8508
REMARK 3 S TENSOR
REMARK 3 S11: 0.0304 S12: 0.2219 S13: -0.0446
REMARK 3 S21: -0.1130 S22: -0.1089 S23: 0.0387
REMARK 3 S31: -0.1257 S32: -0.1936 S33: 0.0785
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): -26.0349 -9.9842 -22.1733
REMARK 3 T TENSOR
REMARK 3 T11: 0.1492 T22: 0.1552
REMARK 3 T33: 0.0967 T12: 0.0028
REMARK 3 T13: 0.0100 T23: -0.0164
REMARK 3 L TENSOR
REMARK 3 L11: 2.2141 L22: 0.2590
REMARK 3 L33: 0.4245 L12: 0.7439
REMARK 3 L13: 0.9590 L23: 0.3305
REMARK 3 S TENSOR
REMARK 3 S11: 0.0257 S12: 0.0139 S13: -0.1449
REMARK 3 S21: -0.0055 S22: 0.0422 S23: -0.0663
REMARK 3 S31: -0.0172 S32: 0.0310 S33: -0.0680
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): -37.4581 -9.1976 -27.8657
REMARK 3 T TENSOR
REMARK 3 T11: 0.0497 T22: 0.2432
REMARK 3 T33: 0.1874 T12: 0.0485
REMARK 3 T13: 0.0159 T23: -0.1000
REMARK 3 L TENSOR
REMARK 3 L11: 8.9997 L22: 16.4203
REMARK 3 L33: 3.5777 L12: -8.0268
REMARK 3 L13: 3.2059 L23: 1.8594
REMARK 3 S TENSOR
REMARK 3 S11: 0.5719 S12: 1.1168 S13: 0.2314
REMARK 3 S21: -0.5091 S22: -0.6946 S23: -0.3638
REMARK 3 S31: 0.1713 S32: 0.4729 S33: 0.1227
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): -41.1003 -3.7333 -20.8010
REMARK 3 T TENSOR
REMARK 3 T11: 0.1314 T22: 0.1525
REMARK 3 T33: 0.1158 T12: 0.0178
REMARK 3 T13: -0.0280 T23: -0.0228
REMARK 3 L TENSOR
REMARK 3 L11: 0.3713 L22: 4.3725
REMARK 3 L33: 1.2134 L12: 0.0815
REMARK 3 L13: 0.5487 L23: 1.4408
REMARK 3 S TENSOR
REMARK 3 S11: 0.0739 S12: 0.0135 S13: 0.0201
REMARK 3 S21: -0.2010 S22: -0.1973 S23: 0.3158
REMARK 3 S31: 0.0276 S32: -0.0307 S33: 0.1234
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): -48.1740 0.4763 -22.3487
REMARK 3 T TENSOR
REMARK 3 T11: 0.0499 T22: 0.0652
REMARK 3 T33: 0.4389 T12: 0.0052
REMARK 3 T13: -0.0161 T23: -0.0736
REMARK 3 L TENSOR
REMARK 3 L11: 1.5406 L22: 4.1591
REMARK 3 L33: 6.7894 L12: -0.4061
REMARK 3 L13: 1.8491 L23: 3.7541
REMARK 3 S TENSOR
REMARK 3 S11: -0.0518 S12: -0.0894 S13: -0.3572
REMARK 3 S21: 0.0632 S22: -0.0625 S23: 0.7645
REMARK 3 S31: -0.0206 S32: -0.1343 S33: 0.1142
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): -38.7139 0.1753 -10.9888
REMARK 3 T TENSOR
REMARK 3 T11: 0.1205 T22: 0.1670
REMARK 3 T33: 0.1096 T12: 0.0048
REMARK 3 T13: -0.0066 T23: -0.0181
REMARK 3 L TENSOR
REMARK 3 L11: 0.3014 L22: 1.0026
REMARK 3 L33: 1.0297 L12: 0.2688
REMARK 3 L13: 0.2235 L23: 1.0056
REMARK 3 S TENSOR
REMARK 3 S11: 0.0326 S12: -0.0513 S13: 0.0119
REMARK 3 S21: 0.0913 S22: -0.1042 S23: 0.0891
REMARK 3 S31: 0.0805 S32: -0.0577 S33: 0.0716
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): -43.9476 15.8277 -9.5244
REMARK 3 T TENSOR
REMARK 3 T11: 0.0396 T22: 0.0950
REMARK 3 T33: 0.2795 T12: -0.0145
REMARK 3 T13: 0.0582 T23: -0.1014
REMARK 3 L TENSOR
REMARK 3 L11: 1.4163 L22: 10.6281
REMARK 3 L33: 4.0603 L12: -2.4733
REMARK 3 L13: 1.2744 L23: 2.0143
REMARK 3 S TENSOR
REMARK 3 S11: -0.0289 S12: 0.0437 S13: -0.1248
REMARK 3 S21: 0.5427 S22: -0.1882 S23: 0.8699
REMARK 3 S31: 0.3043 S32: 0.0306 S33: 0.2171
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): -30.6025 11.8762 -17.7336
REMARK 3 T TENSOR
REMARK 3 T11: 0.1489 T22: 0.1374
REMARK 3 T33: 0.0927 T12: 0.0108
REMARK 3 T13: -0.0255 T23: 0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 0.6568 L22: 2.3795
REMARK 3 L33: 0.2792 L12: -1.0300
REMARK 3 L13: -0.4008 L23: 0.4782
REMARK 3 S TENSOR
REMARK 3 S11: 0.0136 S12: 0.0090 S13: 0.0145
REMARK 3 S21: -0.1448 S22: -0.0014 S23: 0.0910
REMARK 3 S31: 0.0172 S32: 0.0097 S33: -0.0122
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): -34.1765 21.3718 -16.5258
REMARK 3 T TENSOR
REMARK 3 T11: 0.0853 T22: 0.0921
REMARK 3 T33: 0.0847 T12: 0.0224
REMARK 3 T13: -0.0504 T23: 0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 1.0948 L22: 2.3180
REMARK 3 L33: 0.2275 L12: 0.4201
REMARK 3 L13: -0.2116 L23: 0.2914
REMARK 3 S TENSOR
REMARK 3 S11: 0.0077 S12: 0.0919 S13: 0.0389
REMARK 3 S21: -0.2692 S22: -0.0429 S23: 0.1570
REMARK 3 S31: -0.0391 S32: 0.0221 S33: 0.0353
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): -23.4250 14.4614 -9.7938
REMARK 3 T TENSOR
REMARK 3 T11: 0.1340 T22: 0.1387
REMARK 3 T33: 0.0944 T12: 0.0098
REMARK 3 T13: -0.0116 T23: -0.0099
REMARK 3 L TENSOR
REMARK 3 L11: 0.8112 L22: 1.4997
REMARK 3 L33: 0.0149 L12: -0.1444
REMARK 3 L13: -0.1069 L23: 0.0481
REMARK 3 S TENSOR
REMARK 3 S11: 0.0279 S12: 0.0081 S13: 0.0333
REMARK 3 S21: 0.0837 S22: -0.0236 S23: -0.0957
REMARK 3 S31: 0.0017 S32: -0.0049 S33: -0.0043
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): -29.3994 22.4058 -4.5924
REMARK 3 T TENSOR
REMARK 3 T11: 0.1127 T22: 0.1164
REMARK 3 T33: 0.0755 T12: 0.0058
REMARK 3 T13: 0.0225 T23: -0.0217
REMARK 3 L TENSOR
REMARK 3 L11: 0.6663 L22: 3.9095
REMARK 3 L33: 2.6116 L12: -0.2359
REMARK 3 L13: 0.3444 L23: -3.1726
REMARK 3 S TENSOR
REMARK 3 S11: 0.0559 S12: -0.1073 S13: 0.0433
REMARK 3 S21: 0.0502 S22: -0.0216 S23: 0.0654
REMARK 3 S31: -0.0190 S32: 0.0017 S33: -0.0343
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): -19.2702 2.9204 -5.4337
REMARK 3 T TENSOR
REMARK 3 T11: 0.1404 T22: 0.1582
REMARK 3 T33: 0.0901 T12: 0.0065
REMARK 3 T13: -0.0129 T23: -0.0157
REMARK 3 L TENSOR
REMARK 3 L11: 1.8522 L22: 0.5889
REMARK 3 L33: 0.1788 L12: -0.7585
REMARK 3 L13: 0.1377 L23: -0.2719
REMARK 3 S TENSOR
REMARK 3 S11: -0.0255 S12: -0.0778 S13: 0.1103
REMARK 3 S21: 0.0098 S22: 0.0038 S23: -0.0638
REMARK 3 S31: 0.0018 S32: -0.0010 S33: 0.0217
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): -11.2716 0.4859 -15.9271
REMARK 3 T TENSOR
REMARK 3 T11: 0.1135 T22: 0.1203
REMARK 3 T33: 0.1212 T12: -0.0013
REMARK 3 T13: 0.0079 T23: 0.0050
REMARK 3 L TENSOR
REMARK 3 L11: 1.4506 L22: 0.6554
REMARK 3 L33: 0.6540 L12: 0.7021
REMARK 3 L13: 0.4889 L23: 0.5724
REMARK 3 S TENSOR
REMARK 3 S11: -0.0213 S12: 0.0207 S13: 0.0094
REMARK 3 S21: -0.0498 S22: 0.0049 S23: -0.0808
REMARK 3 S31: -0.0312 S32: -0.0452 S33: 0.0164
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): -3.0391 -8.4201 -20.9227
REMARK 3 T TENSOR
REMARK 3 T11: 0.0636 T22: 0.0996
REMARK 3 T33: 0.1188 T12: 0.0192
REMARK 3 T13: 0.0413 T23: -0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 2.0652 L22: 2.0477
REMARK 3 L33: 3.2125 L12: 0.3046
REMARK 3 L13: -0.3790 L23: 0.1932
REMARK 3 S TENSOR
REMARK 3 S11: -0.0640 S12: 0.0767 S13: -0.0949
REMARK 3 S21: -0.3108 S22: 0.1067 S23: -0.2260
REMARK 3 S31: 0.1244 S32: 0.1913 S33: -0.0427
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): -14.6578 -11.9849 -13.4162
REMARK 3 T TENSOR
REMARK 3 T11: 0.1354 T22: 0.1198
REMARK 3 T33: 0.1028 T12: 0.0065
REMARK 3 T13: -0.0039 T23: 0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 1.5313 L22: 0.8813
REMARK 3 L33: 0.2075 L12: -0.4814
REMARK 3 L13: 0.3685 L23: 0.1765
REMARK 3 S TENSOR
REMARK 3 S11: -0.0085 S12: -0.0341 S13: -0.0206
REMARK 3 S21: 0.0527 S22: 0.0146 S23: 0.0118
REMARK 3 S31: 0.0314 S32: -0.0128 S33: -0.0061
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): -8.2231 -11.8523 -7.3411
REMARK 3 T TENSOR
REMARK 3 T11: 0.1203 T22: 0.0846
REMARK 3 T33: 0.1074 T12: 0.0222
REMARK 3 T13: -0.0065 T23: 0.0345
REMARK 3 L TENSOR
REMARK 3 L11: 2.5106 L22: 0.1041
REMARK 3 L33: 1.4552 L12: 0.0470
REMARK 3 L13: -0.7523 L23: 0.3401
REMARK 3 S TENSOR
REMARK 3 S11: 0.0017 S12: -0.0937 S13: -0.1223
REMARK 3 S21: 0.0403 S22: -0.0134 S23: -0.0128
REMARK 3 S31: 0.1043 S32: 0.0009 S33: 0.0118
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): -32.0870 -7.2924 -2.0389
REMARK 3 T TENSOR
REMARK 3 T11: 0.1325 T22: 0.1711
REMARK 3 T33: 0.0717 T12: -0.0033
REMARK 3 T13: 0.0055 T23: 0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 8.3069 L22: 0.3825
REMARK 3 L33: 1.9561 L12: 1.5809
REMARK 3 L13: 3.8308 L23: 0.8531
REMARK 3 S TENSOR
REMARK 3 S11: -0.0046 S12: -0.2664 S13: -0.0821
REMARK 3 S21: 0.0525 S22: -0.0350 S23: 0.0270
REMARK 3 S31: 0.0805 S32: -0.1116 S33: 0.0396
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): -44.5084 -13.5169 -8.4707
REMARK 3 T TENSOR
REMARK 3 T11: 0.3071 T22: 0.6067
REMARK 3 T33: 0.3589 T12: 0.2281
REMARK 3 T13: -0.1971 T23: -0.4648
REMARK 3 L TENSOR
REMARK 3 L11: 33.1464 L22: 45.7120
REMARK 3 L33: 40.5534 L12: -13.8280
REMARK 3 L13: -32.1667 L23: 8.2670
REMARK 3 S TENSOR
REMARK 3 S11: -0.3332 S12: 0.3914 S13: -0.3884
REMARK 3 S21: 1.0121 S22: -1.5887 S23: 1.0971
REMARK 3 S31: -1.0914 S32: -2.3230 S33: 1.9219
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 1 B 7
REMARK 3 ORIGIN FOR THE GROUP (A): -59.5145 -8.8328 7.2291
REMARK 3 T TENSOR
REMARK 3 T11: 0.0893 T22: 0.1246
REMARK 3 T33: 0.1370 T12: -0.0191
REMARK 3 T13: -0.0225 T23: -0.0214
REMARK 3 L TENSOR
REMARK 3 L11: 7.3715 L22: 4.5217
REMARK 3 L33: 3.6135 L12: 5.0998
REMARK 3 L13: -4.4961 L23: -3.3940
REMARK 3 S TENSOR
REMARK 3 S11: -0.2973 S12: 0.2454 S13: -0.1313
REMARK 3 S21: -0.3161 S22: 0.1618 S23: 0.0872
REMARK 3 S31: 0.2297 S32: -0.0747 S33: 0.1355
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): -34.6677 -11.0215 17.7479
REMARK 3 T TENSOR
REMARK 3 T11: 0.1442 T22: 0.1326
REMARK 3 T33: 0.0868 T12: 0.0025
REMARK 3 T13: -0.0020 T23: 0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 0.6567 L22: 0.6238
REMARK 3 L33: 0.1347 L12: -0.1668
REMARK 3 L13: 0.1640 L23: -0.2548
REMARK 3 S TENSOR
REMARK 3 S11: 0.0061 S12: 0.0066 S13: -0.0299
REMARK 3 S21: 0.0210 S22: -0.0149 S23: -0.0132
REMARK 3 S31: 0.0343 S32: -0.0116 S33: 0.0088
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): -33.9140 -18.1132 25.5617
REMARK 3 T TENSOR
REMARK 3 T11: 0.1710 T22: 0.2574
REMARK 3 T33: 0.0697 T12: 0.0557
REMARK 3 T13: -0.0371 T23: 0.0690
REMARK 3 L TENSOR
REMARK 3 L11: 16.8213 L22: 12.2902
REMARK 3 L33: 6.5836 L12: 2.1757
REMARK 3 L13: 6.6221 L23: 7.7622
REMARK 3 S TENSOR
REMARK 3 S11: 0.8106 S12: -0.2956 S13: -0.7041
REMARK 3 S21: -0.4453 S22: -0.2887 S23: -0.5572
REMARK 3 S31: -0.0236 S32: -0.3084 S33: -0.5219
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): -24.6686 -5.6482 24.8915
REMARK 3 T TENSOR
REMARK 3 T11: 0.1292 T22: 0.1252
REMARK 3 T33: 0.0992 T12: 0.0035
REMARK 3 T13: -0.0218 T23: -0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 0.3470 L22: 0.4614
REMARK 3 L33: 0.4014 L12: -0.1873
REMARK 3 L13: 0.1853 L23: -0.4297
REMARK 3 S TENSOR
REMARK 3 S11: 0.0210 S12: 0.0058 S13: 0.0004
REMARK 3 S21: -0.0103 S22: -0.0073 S23: 0.0136
REMARK 3 S31: 0.0190 S32: 0.0022 S33: -0.0137
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): -18.7721 2.5968 20.5458
REMARK 3 T TENSOR
REMARK 3 T11: 0.0552 T22: 0.1304
REMARK 3 T33: 0.1758 T12: -0.0105
REMARK 3 T13: -0.0259 T23: 0.0332
REMARK 3 L TENSOR
REMARK 3 L11: 0.1949 L22: 3.3314
REMARK 3 L33: 2.4130 L12: -0.4612
REMARK 3 L13: 0.0746 L23: -2.4796
REMARK 3 S TENSOR
REMARK 3 S11: -0.0380 S12: 0.0787 S13: 0.1064
REMARK 3 S21: 0.0731 S22: -0.1734 S23: -0.3657
REMARK 3 S31: 0.0418 S32: 0.0459 S33: 0.2114
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): -23.6722 -3.8373 14.9283
REMARK 3 T TENSOR
REMARK 3 T11: 0.1222 T22: 0.1342
REMARK 3 T33: 0.1043 T12: 0.0078
REMARK 3 T13: -0.0013 T23: 0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 0.6271 L22: 0.5448
REMARK 3 L33: 1.1229 L12: -0.2520
REMARK 3 L13: 0.5969 L23: -0.1710
REMARK 3 S TENSOR
REMARK 3 S11: -0.0107 S12: 0.1041 S13: 0.0170
REMARK 3 S21: -0.0982 S22: -0.0291 S23: -0.1187
REMARK 3 S31: 0.0799 S32: 0.0087 S33: 0.0398
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): -23.9719 12.3925 8.9066
REMARK 3 T TENSOR
REMARK 3 T11: 0.0940 T22: 0.1473
REMARK 3 T33: 0.1489 T12: -0.0127
REMARK 3 T13: 0.0207 T23: 0.0513
REMARK 3 L TENSOR
REMARK 3 L11: 1.0953 L22: 5.4490
REMARK 3 L33: 0.4951 L12: 0.2075
REMARK 3 L13: 0.2095 L23: 1.6062
REMARK 3 S TENSOR
REMARK 3 S11: 0.1001 S12: 0.2304 S13: 0.0591
REMARK 3 S21: -0.2952 S22: -0.0200 S23: -0.3139
REMARK 3 S31: -0.0624 S32: 0.0181 S33: -0.0801
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): -33.5058 13.3264 16.7168
REMARK 3 T TENSOR
REMARK 3 T11: 0.1427 T22: 0.1090
REMARK 3 T33: 0.1266 T12: -0.0113
REMARK 3 T13: -0.0223 T23: -0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 0.9231 L22: 1.0960
REMARK 3 L33: 0.0962 L12: 0.1119
REMARK 3 L13: -0.2900 L23: 0.0073
REMARK 3 S TENSOR
REMARK 3 S11: 0.0088 S12: -0.0495 S13: 0.1219
REMARK 3 S21: 0.1634 S22: 0.0134 S23: -0.0623
REMARK 3 S31: 0.0157 S32: 0.0072 S33: -0.0222
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): -24.1961 15.2468 18.0532
REMARK 3 T TENSOR
REMARK 3 T11: 0.2768 T22: 0.0663
REMARK 3 T33: 0.1811 T12: -0.0013
REMARK 3 T13: -0.0954 T23: 0.0005
REMARK 3 L TENSOR
REMARK 3 L11: 1.3292 L22: 3.6811
REMARK 3 L33: 0.6115 L12: 0.7708
REMARK 3 L13: 0.7674 L23: -0.0647
REMARK 3 S TENSOR
REMARK 3 S11: -0.0829 S12: -0.1714 S13: 0.2008
REMARK 3 S21: -0.0050 S22: -0.0461 S23: -0.3875
REMARK 3 S31: 0.1132 S32: -0.1186 S33: 0.1290
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): -38.5785 19.7495 13.1928
REMARK 3 T TENSOR
REMARK 3 T11: 0.1254 T22: 0.1141
REMARK 3 T33: 0.0987 T12: -0.0089
REMARK 3 T13: 0.0057 T23: 0.0169
REMARK 3 L TENSOR
REMARK 3 L11: 0.6253 L22: 1.1248
REMARK 3 L33: 0.0259 L12: 0.0398
REMARK 3 L13: 0.0033 L23: -0.1101
REMARK 3 S TENSOR
REMARK 3 S11: 0.0272 S12: 0.0319 S13: 0.0097
REMARK 3 S21: 0.0769 S22: -0.0114 S23: -0.0358
REMARK 3 S31: 0.0174 S32: -0.0300 S33: -0.0158
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): -36.6768 22.7786 5.0229
REMARK 3 T TENSOR
REMARK 3 T11: 0.1061 T22: 0.0993
REMARK 3 T33: 0.0777 T12: 0.0062
REMARK 3 T13: 0.0114 T23: 0.0297
REMARK 3 L TENSOR
REMARK 3 L11: 1.8302 L22: 2.7362
REMARK 3 L33: 2.1417 L12: -0.2168
REMARK 3 L13: 0.1786 L23: 2.3774
REMARK 3 S TENSOR
REMARK 3 S11: -0.0014 S12: 0.0623 S13: 0.1029
REMARK 3 S21: -0.0197 S22: 0.0615 S23: -0.0832
REMARK 3 S31: -0.0048 S32: 0.0691 S33: -0.0601
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): -44.3344 3.2296 5.4969
REMARK 3 T TENSOR
REMARK 3 T11: 0.1432 T22: 0.1494
REMARK 3 T33: 0.0948 T12: -0.0070
REMARK 3 T13: 0.0032 T23: 0.0207
REMARK 3 L TENSOR
REMARK 3 L11: 0.4883 L22: 1.2431
REMARK 3 L33: 0.5443 L12: 0.6606
REMARK 3 L13: 0.0514 L23: 0.5007
REMARK 3 S TENSOR
REMARK 3 S11: -0.0199 S12: 0.0621 S13: 0.0530
REMARK 3 S21: 0.0273 S22: 0.0535 S23: 0.0255
REMARK 3 S31: 0.0655 S32: -0.0096 S33: -0.0336
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): -60.8067 0.1362 7.6663
REMARK 3 T TENSOR
REMARK 3 T11: 0.0945 T22: 0.1032
REMARK 3 T33: 0.1943 T12: 0.0043
REMARK 3 T13: -0.0391 T23: -0.0181
REMARK 3 L TENSOR
REMARK 3 L11: 5.6459 L22: 1.8888
REMARK 3 L33: 2.7981 L12: -0.6776
REMARK 3 L13: -0.3181 L23: -0.8890
REMARK 3 S TENSOR
REMARK 3 S11: 0.2155 S12: 0.2406 S13: 0.0921
REMARK 3 S21: -0.2157 S22: -0.1029 S23: 0.5341
REMARK 3 S31: -0.0977 S32: 0.1026 S33: -0.1125
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): -49.4605 0.2327 17.6680
REMARK 3 T TENSOR
REMARK 3 T11: 0.1528 T22: 0.1249
REMARK 3 T33: 0.0969 T12: 0.0108
REMARK 3 T13: 0.0249 T23: 0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 2.3723 L22: 0.3339
REMARK 3 L33: 1.5311 L12: -0.6448
REMARK 3 L13: 0.9078 L23: -0.6741
REMARK 3 S TENSOR
REMARK 3 S11: -0.0536 S12: 0.0067 S13: 0.0351
REMARK 3 S21: 0.0741 S22: 0.0096 S23: -0.0053
REMARK 3 S31: -0.1346 S32: 0.0308 S33: 0.0440
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): -57.0453 -0.7541 18.4276
REMARK 3 T TENSOR
REMARK 3 T11: 0.1161 T22: 0.1141
REMARK 3 T33: 0.1294 T12: -0.0073
REMARK 3 T13: 0.0387 T23: 0.0001
REMARK 3 L TENSOR
REMARK 3 L11: 1.1464 L22: 4.0811
REMARK 3 L33: 0.5305 L12: -1.7308
REMARK 3 L13: 0.3109 L23: -1.2392
REMARK 3 S TENSOR
REMARK 3 S11: 0.0075 S12: -0.0431 S13: 0.0337
REMARK 3 S21: 0.1702 S22: 0.0056 S23: 0.1082
REMARK 3 S31: -0.0459 S32: 0.0305 S33: -0.0131
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): -64.0923 -8.4953 20.9856
REMARK 3 T TENSOR
REMARK 3 T11: 0.0707 T22: 0.1046
REMARK 3 T33: 0.1340 T12: -0.0262
REMARK 3 T13: 0.0764 T23: 0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 5.8993 L22: 1.7596
REMARK 3 L33: 7.2177 L12: -1.8650
REMARK 3 L13: 2.7600 L23: -0.2222
REMARK 3 S TENSOR
REMARK 3 S11: -0.1645 S12: -0.4382 S13: -0.1857
REMARK 3 S21: 0.2192 S22: 0.0372 S23: 0.3571
REMARK 3 S31: -0.0369 S32: -0.4316 S33: 0.1273
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): -51.2943 -11.8358 13.5617
REMARK 3 T TENSOR
REMARK 3 T11: 0.1218 T22: 0.1073
REMARK 3 T33: 0.1121 T12: -0.0137
REMARK 3 T13: 0.0010 T23: 0.0089
REMARK 3 L TENSOR
REMARK 3 L11: 2.5552 L22: 1.1348
REMARK 3 L33: 0.5088 L12: 0.4685
REMARK 3 L13: 0.2939 L23: 0.5510
REMARK 3 S TENSOR
REMARK 3 S11: 0.0664 S12: 0.0754 S13: -0.1350
REMARK 3 S21: 0.0578 S22: -0.0332 S23: -0.0257
REMARK 3 S31: 0.0712 S32: 0.0281 S33: -0.0331
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): -58.2210 -11.9225 7.6224
REMARK 3 T TENSOR
REMARK 3 T11: 0.0562 T22: 0.1045
REMARK 3 T33: 0.1108 T12: -0.0454
REMARK 3 T13: 0.0001 T23: -0.0590
REMARK 3 L TENSOR
REMARK 3 L11: 5.5443 L22: 4.3368
REMARK 3 L33: 6.4549 L12: 2.7803
REMARK 3 L13: -4.6368 L23: -4.4120
REMARK 3 S TENSOR
REMARK 3 S11: -0.1583 S12: 0.3739 S13: -0.3052
REMARK 3 S21: -0.1461 S22: 0.0762 S23: 0.1067
REMARK 3 S31: 0.2694 S32: -0.1768 S33: 0.0821
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): -33.4296 -7.9144 2.7999
REMARK 3 T TENSOR
REMARK 3 T11: 0.2028 T22: 0.2016
REMARK 3 T33: 0.0535 T12: 0.0052
REMARK 3 T13: 0.0180 T23: -0.0156
REMARK 3 L TENSOR
REMARK 3 L11: 6.8583 L22: 0.8042
REMARK 3 L33: 2.5691 L12: -2.2933
REMARK 3 L13: 4.1610 L23: -1.4316
REMARK 3 S TENSOR
REMARK 3 S11: 0.0107 S12: 0.2706 S13: 0.0411
REMARK 3 S21: -0.0821 S22: -0.0547 S23: -0.0231
REMARK 3 S31: 0.0950 S32: 0.1421 S33: 0.0439
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): -22.8733 -15.7861 7.7173
REMARK 3 T TENSOR
REMARK 3 T11: 0.1972 T22: 0.1882
REMARK 3 T33: 0.0948 T12: 0.1214
REMARK 3 T13: 0.0690 T23: 0.0748
REMARK 3 L TENSOR
REMARK 3 L11: 23.0318 L22: 52.9735
REMARK 3 L33: 33.1129 L12: 7.8465
REMARK 3 L13: 0.1484 L23: 6.7595
REMARK 3 S TENSOR
REMARK 3 S11: -0.1357 S12: 1.4114 S13: 0.3389
REMARK 3 S21: -0.6179 S22: -0.2466 S23: -1.8297
REMARK 3 S31: 1.7224 S32: 0.6096 S33: 0.3823
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 3SZO 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_1000066852.
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 : 77603
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
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 (%) : 91.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.40800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
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 (%): 43.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
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 35.44500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.54500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.29000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.54500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.44500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.29000
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 297 CG GLU A 297 CD 0.105
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 230 NE - CZ - NH1 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ARG A 230 NE - CZ - NH2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 LEU A 231 CB - CG - CD1 ANGL. DEV. = 10.6 DEGREES
REMARK 500 ARG A 281 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG B 184 NE - CZ - NH1 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG B 184 NE - CZ - NH2 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG B 230 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 LEU B 231 CB - CG - CD1 ANGL. DEV. = 11.4 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 HIS A 37 155.36 76.02
REMARK 500 ASP A 88 57.68 -92.70
REMARK 500 LYS A 193 -76.36 -129.91
REMARK 500 HIS B 37 163.22 68.01
REMARK 500 SER B 135 19.18 -144.87
REMARK 500 LYS B 193 -78.44 -131.93
REMARK 500 GLU B 258 -0.50 72.00
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 SF4 A 997 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 12 SG
REMARK 620 2 SF4 A 997 S1 116.7
REMARK 620 3 SF4 A 997 S3 112.9 106.1
REMARK 620 4 SF4 A 997 S4 104.8 108.3 107.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 997 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 96 SG
REMARK 620 2 SF4 A 997 S2 113.0
REMARK 620 3 SF4 A 997 S3 105.9 108.7
REMARK 620 4 SF4 A 997 S4 122.8 105.3 99.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 997 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 197 SG
REMARK 620 2 SF4 A 997 S1 103.7
REMARK 620 3 SF4 A 997 S2 114.8 109.8
REMARK 620 4 SF4 A 997 S4 122.7 101.5 103.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 997 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 H6P A 998 O33
REMARK 620 2 SF4 A 997 S1 132.3
REMARK 620 3 SF4 A 997 S2 92.8 105.7
REMARK 620 4 SF4 A 997 S3 118.6 100.0 102.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B 997 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 12 SG
REMARK 620 2 SF4 B 997 S1 118.7
REMARK 620 3 SF4 B 997 S3 114.1 105.3
REMARK 620 4 SF4 B 997 S4 103.4 107.9 106.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B 997 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 96 SG
REMARK 620 2 SF4 B 997 S2 113.7
REMARK 620 3 SF4 B 997 S3 105.2 107.5
REMARK 620 4 SF4 B 997 S4 123.4 105.2 100.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B 997 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 197 SG
REMARK 620 2 SF4 B 997 S1 104.7
REMARK 620 3 SF4 B 997 S2 115.3 107.8
REMARK 620 4 SF4 B 997 S4 122.1 102.3 103.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B 997 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 H6P B 998 O33
REMARK 620 2 SF4 B 997 S1 129.1
REMARK 620 3 SF4 B 997 S2 93.5 106.0
REMARK 620 4 SF4 B 997 S3 121.1 100.4 102.3
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 SF4 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 SF4 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: 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
REMARK 900 RELATED ID: 3T0G RELATED DB: PDB
REMARK 900 ISPH:HMBPP STRUCTURE, T167C MUTANT
DBREF 3SZO A 1 316 UNP P62623 ISPH_ECOLI 1 316
DBREF 3SZO B 1 316 UNP P62623 ISPH_ECOLI 1 316
SEQADV 3SZO MET A -11 UNP P62623 EXPRESSION TAG
SEQADV 3SZO ARG A -10 UNP P62623 EXPRESSION TAG
SEQADV 3SZO GLY A -9 UNP P62623 EXPRESSION TAG
SEQADV 3SZO SER A -8 UNP P62623 EXPRESSION TAG
SEQADV 3SZO HIS A -7 UNP P62623 EXPRESSION TAG
SEQADV 3SZO HIS A -6 UNP P62623 EXPRESSION TAG
SEQADV 3SZO HIS A -5 UNP P62623 EXPRESSION TAG
SEQADV 3SZO HIS A -4 UNP P62623 EXPRESSION TAG
SEQADV 3SZO HIS A -3 UNP P62623 EXPRESSION TAG
SEQADV 3SZO HIS A -2 UNP P62623 EXPRESSION TAG
SEQADV 3SZO GLY A -1 UNP P62623 EXPRESSION TAG
SEQADV 3SZO SER A 0 UNP P62623 EXPRESSION TAG
SEQADV 3SZO MET B -11 UNP P62623 EXPRESSION TAG
SEQADV 3SZO ARG B -10 UNP P62623 EXPRESSION TAG
SEQADV 3SZO GLY B -9 UNP P62623 EXPRESSION TAG
SEQADV 3SZO SER B -8 UNP P62623 EXPRESSION TAG
SEQADV 3SZO HIS B -7 UNP P62623 EXPRESSION TAG
SEQADV 3SZO HIS B -6 UNP P62623 EXPRESSION TAG
SEQADV 3SZO HIS B -5 UNP P62623 EXPRESSION TAG
SEQADV 3SZO HIS B -4 UNP P62623 EXPRESSION TAG
SEQADV 3SZO HIS B -3 UNP P62623 EXPRESSION TAG
SEQADV 3SZO HIS B -2 UNP P62623 EXPRESSION TAG
SEQADV 3SZO GLY B -1 UNP P62623 EXPRESSION TAG
SEQADV 3SZO SER B 0 UNP P62623 EXPRESSION TAG
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 THR 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 THR 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 SF4 A 997 8
HET H6P A 998 15
HET SF4 B 997 8
HET H6P B 998 15
HETNAM SF4 IRON/SULFUR CLUSTER
HETNAM H6P (2E)-4-HYDROXY-3-METHYLBUT-2-EN-1-YL TRIHYDROGEN
HETNAM 2 H6P DIPHOSPHATE
FORMUL 3 SF4 2(FE4 S4)
FORMUL 4 H6P 2(C5 H12 O8 P2)
FORMUL 7 HOH *603(H2 O)
HELIX 1 1 CYS A 12 GLY A 30 1 19
HELIX 2 2 ASN A 42 ARG A 52 1 11
HELIX 3 3 GLN A 59 VAL A 63 5 5
HELIX 4 4 SER A 77 ARG A 87 1 11
HELIX 5 5 CYS A 96 GLY A 113 1 18
HELIX 6 6 HIS A 124 GLY A 132 1 9
HELIX 7 7 SER A 146 LEU A 153 1 8
HELIX 8 8 SER A 170 PHE A 185 1 16
HELIX 9 9 CYS A 197 GLU A 212 1 16
HELIX 10 10 SER A 225 MET A 238 1 14
HELIX 11 11 ASP A 247 ILE A 251 5 5
HELIX 12 12 GLN A 252 LYS A 257 1 6
HELIX 13 13 PRO A 271 LEU A 285 1 15
HELIX 14 14 PRO A 305 ARG A 309 5 5
HELIX 15 15 CYS B 12 GLY B 30 1 19
HELIX 16 16 ASN B 42 ARG B 52 1 11
HELIX 17 17 GLN B 59 VAL B 63 5 5
HELIX 18 18 SER B 77 ARG B 87 1 11
HELIX 19 19 CYS B 96 GLY B 113 1 18
HELIX 20 20 HIS B 124 GLY B 132 1 9
HELIX 21 21 SER B 146 LEU B 153 1 8
HELIX 22 22 SER B 170 PHE B 185 1 16
HELIX 23 23 CYS B 197 ALA B 214 1 18
HELIX 24 24 SER B 225 MET B 238 1 14
HELIX 25 25 ASP B 247 ILE B 251 5 5
HELIX 26 26 GLN B 252 LYS B 257 1 6
HELIX 27 27 PRO B 271 LEU B 285 1 15
HELIX 28 28 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 GLN A 2 O VAL A 262
SHEET 5 A 5 ALA A 290 PRO A 292 1 O ILE A 291 N ILE A 3
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 70 N ARG A 36
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 LEU A 118 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 PHE B 243
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 ILE B 3
SHEET 1 F 4 ALA B 54 ILE B 57 0
SHEET 2 F 4 ILE B 33 ARG B 36 1 N VAL B 35 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 MET B 164 N ILE B 117
LINK SG CYS A 12 FE2 SF4 A 997 1555 1555 2.31
LINK SG CYS A 96 FE1 SF4 A 997 1555 1555 2.27
LINK SG CYS A 197 FE3 SF4 A 997 1555 1555 2.32
LINK FE4 SF4 A 997 O33 H6P A 998 1555 1555 2.14
LINK SG CYS B 12 FE2 SF4 B 997 1555 1555 2.31
LINK SG CYS B 96 FE1 SF4 B 997 1555 1555 2.28
LINK SG CYS B 197 FE3 SF4 B 997 1555 1555 2.34
LINK FE4 SF4 B 997 O33 H6P B 998 1555 1555 2.09
CISPEP 1 ASN A 7 PRO A 8 0 1.55
CISPEP 2 ALA A 31 PRO A 32 0 0.94
CISPEP 3 ASN B 7 PRO B 8 0 -1.26
CISPEP 4 ALA B 31 PRO B 32 0 2.53
SITE 1 AC1 6 CYS A 12 GLY A 14 CYS A 96 LEU A 98
SITE 2 AC1 6 CYS A 197 H6P A 998
SITE 1 AC2 17 VAL A 15 VAL A 40 HIS A 41 ALA A 73
SITE 2 AC2 17 HIS A 74 VAL A 99 HIS A 124 GLU A 126
SITE 3 AC2 17 THR A 167 THR A 168 ASN A 224 SER A 225
SITE 4 AC2 17 SER A 226 ASN A 227 SER A 269 HOH A 317
SITE 5 AC2 17 SF4 A 997
SITE 1 AC3 5 CYS B 12 GLY B 14 CYS B 96 CYS B 197
SITE 2 AC3 5 H6P B 998
SITE 1 AC4 17 VAL B 15 VAL B 40 HIS B 41 ALA B 73
SITE 2 AC4 17 HIS B 74 VAL B 99 HIS B 124 GLU B 126
SITE 3 AC4 17 THR B 167 THR B 168 ASN B 224 SER B 225
SITE 4 AC4 17 SER B 226 ASN B 227 SER B 269 HOH B 318
SITE 5 AC4 17 SF4 B 997
CRYST1 70.890 80.580 111.090 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 0.014106 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012410 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009002 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
