HEADER TRANSFERASE 14-FEB-10 2X64
TITLE GLUTATHIONE-S-TRANSFERASE FROM XYLELLA FASTIDIOSA
CAVEAT 2X64 GSH F 1224 HAS WRONG CHIRALITY AT ATOM CA2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTATHIONE-S-TRANSFERASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XYLELLA FASTIDIOSA;
SOURCE 3 ORGANISM_TAXID: 160492;
SOURCE 4 STRAIN: 9A5C;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-28A
KEYWDS DETOXIFICATION ENZYME, TRANSFERASE,
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.C.MUNIZ,N.C.RODRIGUES,L.BLEICHER,R.F.TRAVENSOLO,W.GARCIA
REVDAT 2 07-DEC-11 2X64 1 CAVEAT REMARK HET HETNAM
REVDAT 2 2 FORMUL HETATM VERSN
REVDAT 1 02-MAR-10 2X64 0
JRNL AUTH N.C.RODRIGUES,J.R.C.MUNIZ,L.BLEICHER,W.GARCIA,
JRNL AUTH 2 R.F.TRAVENSOLO,A.P.ULIAN-DE-ARAUJO,E.CARRILHO,
JRNL AUTH 3 R.GARRATT
JRNL TITL STRUCTURAL AND BIOPHYSICAL CHARACTERIZATION OF THE
JRNL TITL 2 RECOMBINANT GLUTATHIONE-S-TRANSFERASE FROM XYLELLA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.8.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.67
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 53795
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) : 0.1694
REMARK 3 R VALUE (WORKING SET) : 0.1667
REMARK 3 FREE R VALUE : 0.2191
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 FREE R VALUE TEST SET COUNT : 2746
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.36
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 3858
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2145
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3680
REMARK 3 BIN R VALUE (WORKING SET) : 0.2111
REMARK 3 BIN FREE R VALUE : 0.2825
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.61
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 178
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9595
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 126
REMARK 3 SOLVENT ATOMS : 725
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.9466
REMARK 3 B22 (A**2) : -0.3152
REMARK 3 B33 (A**2) : 8.2617
REMARK 3 B12 (A**2) : -0.4394
REMARK 3 B13 (A**2) : -0.7088
REMARK 3 B23 (A**2) : 2.2971
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.272
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.9414
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.9091
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 9950 ; 2.00 ; HARMONIC
REMARK 3 BOND ANGLES : 13526 ; 2.00 ; HARMONIC
REMARK 3 TORSION ANGLES : 3402 ; 2.00 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 227 ; 2.00 ; HARMONIC
REMARK 3 GENERAL PLANES : 1490 ; 5.00 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 9950 ; 20.00 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 6 ; 5.00 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1234 ; 5.00 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 12066 ; 4.00 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.06
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.81
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.93
REMARK 3
REMARK 3 TLS DETAILS.
REMARK 3 NUMBER OF TLS GROUPS : 24
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (A1 - A74)
REMARK 3 ORIGIN FOR THE GROUP (A): -6.2684 -7.7449 44.9617
REMARK 3 T TENSOR
REMARK 3 T11: 0.0649 T22: -0.2086
REMARK 3 T33: -0.1821 T12: 0.0361
REMARK 3 T13: 0.0694 T23: -0.0354
REMARK 3 L TENSOR
REMARK 3 L11: 2.6591 L22: 5.2750
REMARK 3 L33: 4.7764 L12: 0.9568
REMARK 3 L13: -2.0746 L23: 2.2300
REMARK 3 S TENSOR
REMARK 3 S11: 0.1329 S12: -0.4479 S13: 0.2478
REMARK 3 S21: 0.4482 S22: -0.2040 S23: 0.4666
REMARK 3 S31: -0.3819 S32: -0.3101 S33: 0.0711
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (A75 - A116)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.8056 -15.2373 35.5641
REMARK 3 T TENSOR
REMARK 3 T11: 0.1719 T22: -0.1602
REMARK 3 T33: -0.0861 T12: -0.0439
REMARK 3 T13: -0.0255 T23: 0.0294
REMARK 3 L TENSOR
REMARK 3 L11: 0.3114 L22: -0.0195
REMARK 3 L33: 0.7740 L12: 0.1642
REMARK 3 L13: -0.1582 L23: 0.5537
REMARK 3 S TENSOR
REMARK 3 S11: 0.0504 S12: -0.1003 S13: 0.0620
REMARK 3 S21: -0.0081 S22: -0.0443 S23: 0.0796
REMARK 3 S31: -0.4847 S32: -0.0777 S33: -0.0061
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (A117 - A148)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.4767 -16.5388 38.6450
REMARK 3 T TENSOR
REMARK 3 T11: 0.1736 T22: -0.1647
REMARK 3 T33: 0.0034 T12: -0.0615
REMARK 3 T13: -0.0483 T23: 0.0435
REMARK 3 L TENSOR
REMARK 3 L11: 2.1671 L22: 1.0758
REMARK 3 L33: 1.5061 L12: -0.4284
REMARK 3 L13: -0.3412 L23: -1.7732
REMARK 3 S TENSOR
REMARK 3 S11: 0.1298 S12: 0.1607 S13: 0.0428
REMARK 3 S21: -0.2359 S22: -0.0148 S23: -0.3384
REMARK 3 S31: -0.1248 S32: 0.2473 S33: -0.1149
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (A149 - A205)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.0803 -3.8110 34.9023
REMARK 3 T TENSOR
REMARK 3 T11: 0.1978 T22: -0.2032
REMARK 3 T33: -0.1192 T12: -0.0670
REMARK 3 T13: -0.0233 T23: 0.0724
REMARK 3 L TENSOR
REMARK 3 L11: 1.8840 L22: 3.0051
REMARK 3 L33: 1.8525 L12: 0.5916
REMARK 3 L13: 0.4798 L23: 0.2099
REMARK 3 S TENSOR
REMARK 3 S11: 0.1099 S12: 0.0368 S13: 0.3792
REMARK 3 S21: 0.1497 S22: -0.1119 S23: -0.2373
REMARK 3 S31: -0.6400 S32: 0.2815 S33: 0.0019
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (B1 - B32)
REMARK 3 ORIGIN FOR THE GROUP (A): -0.1738 -35.5213 27.0112
REMARK 3 T TENSOR
REMARK 3 T11: -0.0071 T22: -0.0367
REMARK 3 T33: -0.0888 T12: -0.0178
REMARK 3 T13: -0.0562 T23: 0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 2.8506 L22: 4.8959
REMARK 3 L33: 5.6968 L12: -1.8923
REMARK 3 L13: -2.4839 L23: 1.0132
REMARK 3 S TENSOR
REMARK 3 S11: 0.0303 S12: 0.2873 S13: 0.0260
REMARK 3 S21: 0.1172 S22: -0.1648 S23: -0.2135
REMARK 3 S31: -0.0506 S32: 0.2441 S33: 0.1344
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (B33 - B107)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.4101 -25.4749 31.1099
REMARK 3 T TENSOR
REMARK 3 T11: -0.0004 T22: -0.1201
REMARK 3 T33: -0.1129 T12: -0.0094
REMARK 3 T13: -0.0268 T23: 0.0405
REMARK 3 L TENSOR
REMARK 3 L11: 2.4213 L22: 2.5949
REMARK 3 L33: 1.9798 L12: -0.3146
REMARK 3 L13: 0.0320 L23: 0.4149
REMARK 3 S TENSOR
REMARK 3 S11: 0.1538 S12: 0.1026 S13: 0.2293
REMARK 3 S21: -0.1397 S22: -0.1706 S23: 0.0435
REMARK 3 S31: -0.2125 S32: -0.2628 S33: 0.0168
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (B108 - B148)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.2451 -30.1901 51.3167
REMARK 3 T TENSOR
REMARK 3 T11: 0.1536 T22: -0.1691
REMARK 3 T33: -0.1077 T12: -0.1003
REMARK 3 T13: 0.0126 T23: -0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 8.3278 L22: 1.4638
REMARK 3 L33: 2.9906 L12: 0.0816
REMARK 3 L13: 1.0387 L23: 0.3376
REMARK 3 S TENSOR
REMARK 3 S11: 0.0118 S12: -0.0781 S13: 0.1166
REMARK 3 S21: 0.2847 S22: -0.1517 S23: 0.0420
REMARK 3 S31: 0.0314 S32: -0.1076 S33: 0.1399
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (B149 - B205)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.8789 -37.3633 41.4291
REMARK 3 T TENSOR
REMARK 3 T11: -0.0239 T22: -0.0134
REMARK 3 T33: -0.0935 T12: -0.0364
REMARK 3 T13: 0.0154 T23: -0.0108
REMARK 3 L TENSOR
REMARK 3 L11: 0.8167 L22: 2.5257
REMARK 3 L33: 0.2349 L12: -0.0110
REMARK 3 L13: -0.3599 L23: 0.4984
REMARK 3 S TENSOR
REMARK 3 S11: 0.0589 S12: 0.0238 S13: -0.1791
REMARK 3 S21: 0.1518 S22: -0.1145 S23: 0.3767
REMARK 3 S31: 0.0723 S32: -0.0351 S33: 0.0556
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (C1 - C32)
REMARK 3 ORIGIN FOR THE GROUP (A): -15.3182 0.4374 -17.2673
REMARK 3 T TENSOR
REMARK 3 T11: 0.0431 T22: -0.0455
REMARK 3 T33: -0.1026 T12: 0.0390
REMARK 3 T13: 0.0044 T23: -0.0309
REMARK 3 L TENSOR
REMARK 3 L11: -1.3272 L22: 4.5754
REMARK 3 L33: 1.9380 L12: 2.9117
REMARK 3 L13: 1.5956 L23: 0.4588
REMARK 3 S TENSOR
REMARK 3 S11: -0.0464 S12: -0.0894 S13: 0.0196
REMARK 3 S21: -0.2010 S22: 0.1500 S23: -0.1062
REMARK 3 S31: 0.2009 S32: 0.1737 S33: -0.1036
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (C33 - C107)
REMARK 3 ORIGIN FOR THE GROUP (A): -16.4830 -7.4384 -9.8200
REMARK 3 T TENSOR
REMARK 3 T11: 0.0277 T22: -0.0746
REMARK 3 T33: -0.1358 T12: 0.0511
REMARK 3 T13: -0.0157 T23: 0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 0.7651 L22: 1.9557
REMARK 3 L33: 2.8742 L12: 0.3255
REMARK 3 L13: -0.3618 L23: 0.1311
REMARK 3 S TENSOR
REMARK 3 S11: -0.0118 S12: -0.1111 S13: -0.0168
REMARK 3 S21: -0.0769 S22: 0.0049 S23: 0.0114
REMARK 3 S31: 0.2161 S32: 0.0483 S33: 0.0069
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (C108 - C148)
REMARK 3 ORIGIN FOR THE GROUP (A): -12.3241 -24.3391 -23.1483
REMARK 3 T TENSOR
REMARK 3 T11: 0.2689 T22: -0.1231
REMARK 3 T33: -0.1785 T12: 0.0900
REMARK 3 T13: 0.0786 T23: 0.0205
REMARK 3 L TENSOR
REMARK 3 L11: 7.3596 L22: 1.3823
REMARK 3 L33: 2.0250 L12: -0.0868
REMARK 3 L13: -0.8323 L23: 0.4962
REMARK 3 S TENSOR
REMARK 3 S11: -0.1346 S12: 0.0901 S13: -0.0379
REMARK 3 S21: -0.3106 S22: 0.1158 S23: 0.0535
REMARK 3 S31: 0.5575 S32: 0.2179 S33: 0.0188
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (C149 - C205)
REMARK 3 ORIGIN FOR THE GROUP (A): -22.8433 -11.3739 -24.5190
REMARK 3 T TENSOR
REMARK 3 T11: 0.0761 T22: -0.0566
REMARK 3 T33: -0.1501 T12: -0.0233
REMARK 3 T13: -0.0096 T23: -0.0325
REMARK 3 L TENSOR
REMARK 3 L11: 0.5397 L22: 1.2907
REMARK 3 L33: 2.8894 L12: -0.1900
REMARK 3 L13: -0.4931 L23: -0.0287
REMARK 3 S TENSOR
REMARK 3 S11: -0.1046 S12: 0.1819 S13: 0.0210
REMARK 3 S21: -0.3012 S22: 0.0057 S23: -0.0433
REMARK 3 S31: 0.1640 S32: -0.1246 S33: 0.0990
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (D1 - D74)
REMARK 3 ORIGIN FOR THE GROUP (A): -22.1377 -27.1700 0.9696
REMARK 3 T TENSOR
REMARK 3 T11: -0.0479 T22: -0.1559
REMARK 3 T33: -0.1722 T12: 0.0120
REMARK 3 T13: 0.0143 T23: 0.0248
REMARK 3 L TENSOR
REMARK 3 L11: 3.8679 L22: 3.9546
REMARK 3 L33: 3.1711 L12: 0.9332
REMARK 3 L13: 1.8326 L23: -2.0854
REMARK 3 S TENSOR
REMARK 3 S11: 0.0845 S12: 0.1832 S13: -0.3947
REMARK 3 S21: -0.2355 S22: 0.0092 S23: 0.1591
REMARK 3 S31: 0.5389 S32: -0.1415 S33: -0.0937
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (D75 - D116)
REMARK 3 ORIGIN FOR THE GROUP (A): -11.3818 -16.2776 -2.8375
REMARK 3 T TENSOR
REMARK 3 T11: -0.0068 T22: -0.0325
REMARK 3 T33: -0.1080 T12: 0.0212
REMARK 3 T13: 0.0115 T23: 0.0148
REMARK 3 L TENSOR
REMARK 3 L11: 1.9102 L22: 2.6701
REMARK 3 L33: 2.9298 L12: -1.8972
REMARK 3 L13: -1.4441 L23: 0.8639
REMARK 3 S TENSOR
REMARK 3 S11: -0.1186 S12: -0.1569 S13: -0.1624
REMARK 3 S21: -0.0688 S22: -0.0988 S23: 0.0832
REMARK 3 S31: 0.2906 S32: 0.1352 S33: 0.2174
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (D117 - D148)
REMARK 3 ORIGIN FOR THE GROUP (A): 2.7431 -19.7819 -6.5043
REMARK 3 T TENSOR
REMARK 3 T11: -0.0084 T22: 0.0792
REMARK 3 T33: -0.0788 T12: 0.1744
REMARK 3 T13: 0.0938 T23: 0.0743
REMARK 3 L TENSOR
REMARK 3 L11: 0.8458 L22: 0.8398
REMARK 3 L33: 4.0759 L12: 0.9423
REMARK 3 L13: 1.4368 L23: -1.1636
REMARK 3 S TENSOR
REMARK 3 S11: 0.1184 S12: -0.0347 S13: 0.0242
REMARK 3 S21: -0.3678 S22: -0.3041 S23: -0.5149
REMARK 3 S31: 0.2621 S32: 0.5857 S33: 0.1857
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (D149 - D205)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.4761 -21.1754 7.2225
REMARK 3 T TENSOR
REMARK 3 T11: 0.0311 T22: 0.0053
REMARK 3 T33: -0.1348 T12: 0.1092
REMARK 3 T13: 0.0068 T23: 0.0273
REMARK 3 L TENSOR
REMARK 3 L11: 2.0918 L22: 0.6130
REMARK 3 L33: 1.6049 L12: -0.1393
REMARK 3 L13: -0.1529 L23: -0.6460
REMARK 3 S TENSOR
REMARK 3 S11: -0.1331 S12: -0.2408 S13: 0.0134
REMARK 3 S21: 0.1719 S22: -0.0338 S23: -0.0894
REMARK 3 S31: 0.2625 S32: 0.3388 S33: 0.1668
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (E1 - E50)
REMARK 3 ORIGIN FOR THE GROUP (A): -31.5229 23.1548 4.1911
REMARK 3 T TENSOR
REMARK 3 T11: -0.0224 T22: -0.0034
REMARK 3 T33: -0.1248 T12: 0.1037
REMARK 3 T13: -0.0842 T23: -0.0795
REMARK 3 L TENSOR
REMARK 3 L11: 2.7176 L22: 6.5049
REMARK 3 L33: 5.6335 L12: -1.0546
REMARK 3 L13: -1.1193 L23: 0.0990
REMARK 3 S TENSOR
REMARK 3 S11: 0.1812 S12: -0.0846 S13: 0.1666
REMARK 3 S21: -0.2425 S22: -0.2502 S23: 0.3732
REMARK 3 S31: -0.6585 S32: -0.2957 S33: 0.0690
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (E51 - E107)
REMARK 3 ORIGIN FOR THE GROUP (A): -28.7837 14.2904 15.9567
REMARK 3 T TENSOR
REMARK 3 T11: 0.0166 T22: -0.0340
REMARK 3 T33: -0.1072 T12: 0.0024
REMARK 3 T13: 0.0393 T23: -0.0502
REMARK 3 L TENSOR
REMARK 3 L11: 0.8649 L22: 3.6752
REMARK 3 L33: 2.4841 L12: -0.6275
REMARK 3 L13: 0.2329 L23: 1.3388
REMARK 3 S TENSOR
REMARK 3 S11: -0.1760 S12: 0.0586 S13: -0.0491
REMARK 3 S21: 0.2838 S22: -0.0907 S23: 0.5045
REMARK 3 S31: 0.3881 S32: -0.2659 S33: 0.2667
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: (E108 - E148)
REMARK 3 ORIGIN FOR THE GROUP (A): -8.0250 22.8626 13.7393
REMARK 3 T TENSOR
REMARK 3 T11: -0.1277 T22: 0.0006
REMARK 3 T33: -0.1052 T12: 0.0317
REMARK 3 T13: -0.0189 T23: -0.0872
REMARK 3 L TENSOR
REMARK 3 L11: 1.4439 L22: 7.8102
REMARK 3 L33: 1.9801 L12: 1.6915
REMARK 3 L13: -0.4842 L23: 1.1999
REMARK 3 S TENSOR
REMARK 3 S11: 0.0493 S12: 0.0336 S13: 0.0618
REMARK 3 S21: -0.1131 S22: 0.2688 S23: -0.5046
REMARK 3 S31: 0.0127 S32: 0.3320 S33: -0.3181
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: (E149 - E205)
REMARK 3 ORIGIN FOR THE GROUP (A): -17.4806 10.9428 5.8358
REMARK 3 T TENSOR
REMARK 3 T11: 0.0031 T22: -0.0294
REMARK 3 T33: -0.0688 T12: 0.0529
REMARK 3 T13: -0.0179 T23: -0.0197
REMARK 3 L TENSOR
REMARK 3 L11: 1.6312 L22: 2.4652
REMARK 3 L33: 3.1001 L12: -0.1324
REMARK 3 L13: -0.0800 L23: 1.8370
REMARK 3 S TENSOR
REMARK 3 S11: -0.0506 S12: 0.0372 S13: 0.0495
REMARK 3 S21: -0.1024 S22: 0.0347 S23: -0.0142
REMARK 3 S31: 0.0760 S32: 0.1168 S33: 0.0159
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: (F1 - F50)
REMARK 3 ORIGIN FOR THE GROUP (A): -18.9451 16.6529 37.2745
REMARK 3 T TENSOR
REMARK 3 T11: 0.1668 T22: -0.1236
REMARK 3 T33: -0.2740 T12: 0.1910
REMARK 3 T13: 0.0109 T23: -0.0469
REMARK 3 L TENSOR
REMARK 3 L11: 6.0020 L22: 5.8818
REMARK 3 L33: 5.0928 L12: -2.3787
REMARK 3 L13: 1.1012 L23: 0.8924
REMARK 3 S TENSOR
REMARK 3 S11: -0.0982 S12: -0.0044 S13: -0.3419
REMARK 3 S21: 0.3765 S22: 0.1154 S23: -0.3925
REMARK 3 S31: 0.8954 S32: 0.5648 S33: -0.0173
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: (F51 - F105)
REMARK 3 ORIGIN FOR THE GROUP (A): -30.2873 16.9195 27.3177
REMARK 3 T TENSOR
REMARK 3 T11: 0.0840 T22: -0.1269
REMARK 3 T33: -0.1529 T12: -0.0309
REMARK 3 T13: 0.1090 T23: -0.0471
REMARK 3 L TENSOR
REMARK 3 L11: 2.5282 L22: 2.8790
REMARK 3 L33: 3.5630 L12: -0.8519
REMARK 3 L13: -1.1356 L23: 1.8030
REMARK 3 S TENSOR
REMARK 3 S11: -0.2460 S12: -0.0780 S13: -0.2442
REMARK 3 S21: 0.6020 S22: -0.1895 S23: 0.3919
REMARK 3 S31: 0.8843 S32: -0.0841 S33: 0.4355
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: (F106 - F148)
REMARK 3 ORIGIN FOR THE GROUP (A): -19.0822 36.8807 22.5093
REMARK 3 T TENSOR
REMARK 3 T11: -0.0810 T22: -0.0713
REMARK 3 T33: -0.1083 T12: 0.0278
REMARK 3 T13: -0.0204 T23: -0.0242
REMARK 3 L TENSOR (
REMARK 3 L11: 7.0047 L22: 2.4545
REMARK 3 L33: 2.6079 L12: 1.6680
REMARK 3 L13: -1.8038 L23: 0.9310
REMARK 3 S TENSOR
REMARK 3 S11: -0.0540 S12: 0.3020 S13: 0.1928
REMARK 3 S21: -0.0636 S22: 0.1384 S23: -0.0895
REMARK 3 S31: -0.2210 S32: -0.0074 S33: -0.0844
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: (F149 - F205)
REMARK 3 ORIGIN FOR THE GROUP (A): -29.6075 31.3390 34.6478
REMARK 3 T TENSOR
REMARK 3 T11: 0.0531 T22: -0.0046
REMARK 3 T33: -0.0691 T12: -0.0129
REMARK 3 T13: 0.0184 T23: -0.0623
REMARK 3 L TENSOR
REMARK 3 L11: 1.2469 L22: 1.8297
REMARK 3 L33: 1.6732 L12: -1.9790
REMARK 3 L13: -0.3463 L23: 0.6570
REMARK 3 S TENSOR
REMARK 3 S11: -0.0548 S12: -0.1142 S13: 0.1267
REMARK 3 S21: 0.4983 S22: -0.1338 S23: 0.2345
REMARK 3 S31: 0.1420 S32: -0.1433 S33: 0.1886
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: IDEAL-DIST CONTACT TERM CONTACT
REMARK 3 SETUP. RESIDUE TYPES WITHOUT CCP4 ATOM TYPE IN LIBRARY=GTT CL.
REMARK 3 NUMBER OF ATOMS WITH PROPER CCP4 ATOM TYPE=10320.
REMARK 3 NUMBER WITH APPROX DEFAULT CCP4 ATOM TYPE=120.
REMARK 3 NUMBER TREATED BY BAD NON-BONDED CONTACTS=6.
REMARK 4
REMARK 4 2X64 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-FEB-10.
REMARK 100 THE PDBE ID CODE IS EBI-42900.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54179
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : MAR345DTB
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53809
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.30
REMARK 200 RESOLUTION RANGE LOW (A) : 46.35
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.9
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 200 DATA REDUNDANCY : 2.1
REMARK 200 R MERGE (I) : 0.09
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.90
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.1
REMARK 200 R MERGE FOR SHELL (I) : 0.42
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.90
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.2 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.6 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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 HIS A -1
REMARK 465 HIS D -1
REMARK 465 HIS E -1
REMARK 465 HIS E 0
REMARK 465 HIS F -1
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 2 CG CD CE NZ
REMARK 470 GLN A 28 CG CD OE1 NE2
REMARK 470 HIS A 32 CG ND1 CD2 CE1 NE2
REMARK 470 GLN A 33 CG CD OE1 NE2
REMARK 470 LYS A 36 CE NZ
REMARK 470 GLU A 39 CG CD OE1 OE2
REMARK 470 GLN A 131 CG CD OE1 NE2
REMARK 470 ASN A 148 CG OD1 ND2
REMARK 470 LYS A 170 CE NZ
REMARK 470 LYS A 171 CG CD CE NZ
REMARK 470 ILE A 205 CG1 CG2 CD1
REMARK 470 LYS B 36 CD CE NZ
REMARK 470 GLU B 39 CG CD OE1 OE2
REMARK 470 ASP B 56 CG OD1 OD2
REMARK 470 LYS B 86 CE NZ
REMARK 470 HIS B 146 CG ND1 CD2 CE1 NE2
REMARK 470 LYS C 36 CD CE NZ
REMARK 470 GLU C 39 CG CD OE1 OE2
REMARK 470 GLU C 76 CG CD OE1 OE2
REMARK 470 GLN C 117 CG CD OE1 NE2
REMARK 470 ARG C 124 CG CD NE CZ NH1 NH2
REMARK 470 HIS D 0 CG ND1 CD2 CE1 NE2
REMARK 470 GLN D 33 CG CD OE1 NE2
REMARK 470 LYS D 36 CD CE NZ
REMARK 470 GLU D 39 CG CD OE1 OE2
REMARK 470 GLU E 39 CG CD OE1 OE2
REMARK 470 LYS E 171 CG CD CE NZ
REMARK 470 HIS F 0 CG ND1 CD2 CE1 NE2
REMARK 470 LYS F 2 CE NZ
REMARK 470 SER F 24 OG
REMARK 470 GLN F 33 CG CD OE1 NE2
REMARK 470 LYS F 36 CG CD CE NZ
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 GLN A 117 -46.81 69.51
REMARK 500 ASN A 152 19.66 56.08
REMARK 500 LEU A 179 71.22 -102.17
REMARK 500 GLN B 117 -41.40 68.54
REMARK 500 ASN B 152 18.64 55.62
REMARK 500 LEU B 179 71.37 -102.47
REMARK 500 GLN C 117 -45.44 69.27
REMARK 500 LEU C 179 73.56 -103.21
REMARK 500 GLN D 117 -52.32 68.32
REMARK 500 ASN D 152 19.11 57.01
REMARK 500 LEU D 179 70.37 -102.13
REMARK 500 GLN E 117 -48.95 71.35
REMARK 500 ASN E 152 19.45 55.51
REMARK 500 LEU E 179 70.95 -100.77
REMARK 500 SER F 178 -0.71 80.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 VAL A 172 24.3 L L OUTSIDE RANGE
REMARK 500 HIS B -1 24.9 L L OUTSIDE RANGE
REMARK 500 THR C 60 24.6 L L OUTSIDE RANGE
REMARK 500 VAL C 172 24.4 L L OUTSIDE RANGE
REMARK 500 ILE C 205 21.7 L L OUTSIDE RANGE
REMARK 500 VAL D 172 23.8 L L OUTSIDE RANGE
REMARK 500 THR E 60 24.9 L L OUTSIDE RANGE
REMARK 500 VAL E 172 24.6 L L OUTSIDE RANGE
REMARK 500 THR F 60 24.6 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH A1224
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH B1224
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH C1224
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH D1224
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH E1224
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH F1224
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C1206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E1206
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B1206
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D1206
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F1206
DBREF 2X64 A -1 0 PDB 2X64 2X64 -1 0
DBREF 2X64 A 1 205 UNP Q9PE18 Q9PE18_XYLFA 1 205
DBREF 2X64 B -1 0 PDB 2X64 2X64 -1 0
DBREF 2X64 B 1 205 UNP Q9PE18 Q9PE18_XYLFA 1 205
DBREF 2X64 C -1 0 PDB 2X64 2X64 -1 0
DBREF 2X64 C 1 205 UNP Q9PE18 Q9PE18_XYLFA 1 205
DBREF 2X64 D -1 0 PDB 2X64 2X64 -1 0
DBREF 2X64 D 1 205 UNP Q9PE18 Q9PE18_XYLFA 1 205
DBREF 2X64 E -1 0 PDB 2X64 2X64 -1 0
DBREF 2X64 E 1 205 UNP Q9PE18 Q9PE18_XYLFA 1 205
DBREF 2X64 F -1 0 PDB 2X64 2X64 -1 0
DBREF 2X64 F 1 205 UNP Q9PE18 Q9PE18_XYLFA 1 205
SEQRES 1 A 207 HIS HIS MET LYS LEU TYR ILE MET PRO GLY ALA CYS SER
SEQRES 2 A 207 LEU ALA ASP HIS ILE LEU LEU ARG TRP SER GLY SER SER
SEQRES 3 A 207 PHE ASP LEU GLN PHE LEU ASP HIS GLN SER MET LYS ALA
SEQRES 4 A 207 PRO GLU TYR LEU ALA LEU ASN PRO SER GLY ALA VAL PRO
SEQRES 5 A 207 ALA LEU GLN VAL GLY ASP TRP VAL LEU THR GLN ASN ALA
SEQRES 6 A 207 ALA ILE LEU ASN TYR ILE THR ASP ILE ALA PRO ALA GLU
SEQRES 7 A 207 ARG GLY LEU SER GLY ASP GLY SER LEU LYS ALA ARG ALA
SEQRES 8 A 207 GLU ILE ASN ARG TRP ILE ALA PHE SER ASN SER ASP VAL
SEQRES 9 A 207 HIS PRO MET TYR TRP ALA LEU PHE GLY GLY THR ALA TYR
SEQRES 10 A 207 LEU GLN ASP PRO GLN MET ILE ALA ARG SER GLN ASP ASN
SEQRES 11 A 207 ALA ARG GLN LYS LEU ARG VAL LEU TYR GLN ARG ALA ASP
SEQRES 12 A 207 ALA HIS LEU LYS HIS HIS ASN TRP LEU ALA ASN GLY GLN
SEQRES 13 A 207 ARG SER GLY ALA ASP ALA TYR LEU TYR VAL THR LEU ARG
SEQRES 14 A 207 TRP ALA LYS LYS VAL GLY VAL ASP LEU SER SER LEU ASP
SEQRES 15 A 207 ALA LEU SER ALA PHE PHE GLU ARG MET GLU ALA ASP PRO
SEQRES 16 A 207 GLY VAL GLN ALA ALA LEU GLN ALA GLU GLY LEU ILE
SEQRES 1 B 207 HIS HIS MET LYS LEU TYR ILE MET PRO GLY ALA CYS SER
SEQRES 2 B 207 LEU ALA ASP HIS ILE LEU LEU ARG TRP SER GLY SER SER
SEQRES 3 B 207 PHE ASP LEU GLN PHE LEU ASP HIS GLN SER MET LYS ALA
SEQRES 4 B 207 PRO GLU TYR LEU ALA LEU ASN PRO SER GLY ALA VAL PRO
SEQRES 5 B 207 ALA LEU GLN VAL GLY ASP TRP VAL LEU THR GLN ASN ALA
SEQRES 6 B 207 ALA ILE LEU ASN TYR ILE THR ASP ILE ALA PRO ALA GLU
SEQRES 7 B 207 ARG GLY LEU SER GLY ASP GLY SER LEU LYS ALA ARG ALA
SEQRES 8 B 207 GLU ILE ASN ARG TRP ILE ALA PHE SER ASN SER ASP VAL
SEQRES 9 B 207 HIS PRO MET TYR TRP ALA LEU PHE GLY GLY THR ALA TYR
SEQRES 10 B 207 LEU GLN ASP PRO GLN MET ILE ALA ARG SER GLN ASP ASN
SEQRES 11 B 207 ALA ARG GLN LYS LEU ARG VAL LEU TYR GLN ARG ALA ASP
SEQRES 12 B 207 ALA HIS LEU LYS HIS HIS ASN TRP LEU ALA ASN GLY GLN
SEQRES 13 B 207 ARG SER GLY ALA ASP ALA TYR LEU TYR VAL THR LEU ARG
SEQRES 14 B 207 TRP ALA LYS LYS VAL GLY VAL ASP LEU SER SER LEU ASP
SEQRES 15 B 207 ALA LEU SER ALA PHE PHE GLU ARG MET GLU ALA ASP PRO
SEQRES 16 B 207 GLY VAL GLN ALA ALA LEU GLN ALA GLU GLY LEU ILE
SEQRES 1 C 207 HIS HIS MET LYS LEU TYR ILE MET PRO GLY ALA CYS SER
SEQRES 2 C 207 LEU ALA ASP HIS ILE LEU LEU ARG TRP SER GLY SER SER
SEQRES 3 C 207 PHE ASP LEU GLN PHE LEU ASP HIS GLN SER MET LYS ALA
SEQRES 4 C 207 PRO GLU TYR LEU ALA LEU ASN PRO SER GLY ALA VAL PRO
SEQRES 5 C 207 ALA LEU GLN VAL GLY ASP TRP VAL LEU THR GLN ASN ALA
SEQRES 6 C 207 ALA ILE LEU ASN TYR ILE THR ASP ILE ALA PRO ALA GLU
SEQRES 7 C 207 ARG GLY LEU SER GLY ASP GLY SER LEU LYS ALA ARG ALA
SEQRES 8 C 207 GLU ILE ASN ARG TRP ILE ALA PHE SER ASN SER ASP VAL
SEQRES 9 C 207 HIS PRO MET TYR TRP ALA LEU PHE GLY GLY THR ALA TYR
SEQRES 10 C 207 LEU GLN ASP PRO GLN MET ILE ALA ARG SER GLN ASP ASN
SEQRES 11 C 207 ALA ARG GLN LYS LEU ARG VAL LEU TYR GLN ARG ALA ASP
SEQRES 12 C 207 ALA HIS LEU LYS HIS HIS ASN TRP LEU ALA ASN GLY GLN
SEQRES 13 C 207 ARG SER GLY ALA ASP ALA TYR LEU TYR VAL THR LEU ARG
SEQRES 14 C 207 TRP ALA LYS LYS VAL GLY VAL ASP LEU SER SER LEU ASP
SEQRES 15 C 207 ALA LEU SER ALA PHE PHE GLU ARG MET GLU ALA ASP PRO
SEQRES 16 C 207 GLY VAL GLN ALA ALA LEU GLN ALA GLU GLY LEU ILE
SEQRES 1 D 207 HIS HIS MET LYS LEU TYR ILE MET PRO GLY ALA CYS SER
SEQRES 2 D 207 LEU ALA ASP HIS ILE LEU LEU ARG TRP SER GLY SER SER
SEQRES 3 D 207 PHE ASP LEU GLN PHE LEU ASP HIS GLN SER MET LYS ALA
SEQRES 4 D 207 PRO GLU TYR LEU ALA LEU ASN PRO SER GLY ALA VAL PRO
SEQRES 5 D 207 ALA LEU GLN VAL GLY ASP TRP VAL LEU THR GLN ASN ALA
SEQRES 6 D 207 ALA ILE LEU ASN TYR ILE THR ASP ILE ALA PRO ALA GLU
SEQRES 7 D 207 ARG GLY LEU SER GLY ASP GLY SER LEU LYS ALA ARG ALA
SEQRES 8 D 207 GLU ILE ASN ARG TRP ILE ALA PHE SER ASN SER ASP VAL
SEQRES 9 D 207 HIS PRO MET TYR TRP ALA LEU PHE GLY GLY THR ALA TYR
SEQRES 10 D 207 LEU GLN ASP PRO GLN MET ILE ALA ARG SER GLN ASP ASN
SEQRES 11 D 207 ALA ARG GLN LYS LEU ARG VAL LEU TYR GLN ARG ALA ASP
SEQRES 12 D 207 ALA HIS LEU LYS HIS HIS ASN TRP LEU ALA ASN GLY GLN
SEQRES 13 D 207 ARG SER GLY ALA ASP ALA TYR LEU TYR VAL THR LEU ARG
SEQRES 14 D 207 TRP ALA LYS LYS VAL GLY VAL ASP LEU SER SER LEU ASP
SEQRES 15 D 207 ALA LEU SER ALA PHE PHE GLU ARG MET GLU ALA ASP PRO
SEQRES 16 D 207 GLY VAL GLN ALA ALA LEU GLN ALA GLU GLY LEU ILE
SEQRES 1 E 207 HIS HIS MET LYS LEU TYR ILE MET PRO GLY ALA CYS SER
SEQRES 2 E 207 LEU ALA ASP HIS ILE LEU LEU ARG TRP SER GLY SER SER
SEQRES 3 E 207 PHE ASP LEU GLN PHE LEU ASP HIS GLN SER MET LYS ALA
SEQRES 4 E 207 PRO GLU TYR LEU ALA LEU ASN PRO SER GLY ALA VAL PRO
SEQRES 5 E 207 ALA LEU GLN VAL GLY ASP TRP VAL LEU THR GLN ASN ALA
SEQRES 6 E 207 ALA ILE LEU ASN TYR ILE THR ASP ILE ALA PRO ALA GLU
SEQRES 7 E 207 ARG GLY LEU SER GLY ASP GLY SER LEU LYS ALA ARG ALA
SEQRES 8 E 207 GLU ILE ASN ARG TRP ILE ALA PHE SER ASN SER ASP VAL
SEQRES 9 E 207 HIS PRO MET TYR TRP ALA LEU PHE GLY GLY THR ALA TYR
SEQRES 10 E 207 LEU GLN ASP PRO GLN MET ILE ALA ARG SER GLN ASP ASN
SEQRES 11 E 207 ALA ARG GLN LYS LEU ARG VAL LEU TYR GLN ARG ALA ASP
SEQRES 12 E 207 ALA HIS LEU LYS HIS HIS ASN TRP LEU ALA ASN GLY GLN
SEQRES 13 E 207 ARG SER GLY ALA ASP ALA TYR LEU TYR VAL THR LEU ARG
SEQRES 14 E 207 TRP ALA LYS LYS VAL GLY VAL ASP LEU SER SER LEU ASP
SEQRES 15 E 207 ALA LEU SER ALA PHE PHE GLU ARG MET GLU ALA ASP PRO
SEQRES 16 E 207 GLY VAL GLN ALA ALA LEU GLN ALA GLU GLY LEU ILE
SEQRES 1 F 207 HIS HIS MET LYS LEU TYR ILE MET PRO GLY ALA CYS SER
SEQRES 2 F 207 LEU ALA ASP HIS ILE LEU LEU ARG TRP SER GLY SER SER
SEQRES 3 F 207 PHE ASP LEU GLN PHE LEU ASP HIS GLN SER MET LYS ALA
SEQRES 4 F 207 PRO GLU TYR LEU ALA LEU ASN PRO SER GLY ALA VAL PRO
SEQRES 5 F 207 ALA LEU GLN VAL GLY ASP TRP VAL LEU THR GLN ASN ALA
SEQRES 6 F 207 ALA ILE LEU ASN TYR ILE THR ASP ILE ALA PRO ALA GLU
SEQRES 7 F 207 ARG GLY LEU SER GLY ASP GLY SER LEU LYS ALA ARG ALA
SEQRES 8 F 207 GLU ILE ASN ARG TRP ILE ALA PHE SER ASN SER ASP VAL
SEQRES 9 F 207 HIS PRO MET TYR TRP ALA LEU PHE GLY GLY THR ALA TYR
SEQRES 10 F 207 LEU GLN ASP PRO GLN MET ILE ALA ARG SER GLN ASP ASN
SEQRES 11 F 207 ALA ARG GLN LYS LEU ARG VAL LEU TYR GLN ARG ALA ASP
SEQRES 12 F 207 ALA HIS LEU LYS HIS HIS ASN TRP LEU ALA ASN GLY GLN
SEQRES 13 F 207 ARG SER GLY ALA ASP ALA TYR LEU TYR VAL THR LEU ARG
SEQRES 14 F 207 TRP ALA LYS LYS VAL GLY VAL ASP LEU SER SER LEU ASP
SEQRES 15 F 207 ALA LEU SER ALA PHE PHE GLU ARG MET GLU ALA ASP PRO
SEQRES 16 F 207 GLY VAL GLN ALA ALA LEU GLN ALA GLU GLY LEU ILE
HET GSH A1224 20
HET GSH B1224 20
HET GSH C1224 20
HET GSH D1224 20
HET GSH E1224 20
HET GSH F1224 20
HET CL A1206 1
HET CL C1206 1
HET CL E1206 1
HET CL B1206 1
HET CL D1206 1
HET CL F1206 1
HETNAM GSH GLUTATHIONE
HETNAM CL CHLORIDE ION
FORMUL 7 GSH 6(C10 H17 N3 O6 S)
FORMUL 8 CL 6(CL 1-)
FORMUL 9 HOH *725(H2 O)
HELIX 1 1 SER A 11 GLY A 22 1 12
HELIX 2 2 ALA A 37 ALA A 42 1 6
HELIX 3 3 GLN A 61 ALA A 73 1 13
HELIX 4 4 PRO A 74 GLY A 78 5 5
HELIX 5 5 SER A 84 ASP A 101 1 18
HELIX 6 6 ASP A 101 TYR A 106 1 6
HELIX 7 7 TRP A 107 GLY A 111 5 5
HELIX 8 8 THR A 113 GLN A 117 5 5
HELIX 9 9 ASP A 118 LYS A 145 1 28
HELIX 10 10 SER A 156 GLY A 173 1 18
HELIX 11 11 LEU A 179 ALA A 191 1 13
HELIX 12 12 ASP A 192 GLU A 202 1 11
HELIX 13 13 SER B 11 GLY B 22 1 12
HELIX 14 14 ALA B 37 ALA B 42 1 6
HELIX 15 15 GLN B 61 ALA B 73 1 13
HELIX 16 16 PRO B 74 GLY B 78 5 5
HELIX 17 17 SER B 84 ASP B 101 1 18
HELIX 18 18 ASP B 101 TYR B 106 1 6
HELIX 19 19 TRP B 107 GLY B 111 5 5
HELIX 20 20 THR B 113 GLN B 117 5 5
HELIX 21 21 ASP B 118 LYS B 145 1 28
HELIX 22 22 SER B 156 GLY B 173 1 18
HELIX 23 23 LEU B 179 ALA B 191 1 13
HELIX 24 24 ASP B 192 GLU B 202 1 11
HELIX 25 25 CYS C 10 GLY C 22 1 13
HELIX 26 26 ALA C 37 ASN C 44 1 8
HELIX 27 27 GLN C 61 ALA C 73 1 13
HELIX 28 28 PRO C 74 GLY C 78 5 5
HELIX 29 29 SER C 84 ASP C 101 1 18
HELIX 30 30 ASP C 101 TYR C 106 1 6
HELIX 31 31 TRP C 107 PHE C 110 5 4
HELIX 32 32 THR C 113 GLN C 117 5 5
HELIX 33 33 ASP C 118 LYS C 145 1 28
HELIX 34 34 SER C 156 GLY C 173 1 18
HELIX 35 35 LEU C 179 ASP C 192 1 14
HELIX 36 36 ASP C 192 GLU C 202 1 11
HELIX 37 37 SER D 11 GLY D 22 1 12
HELIX 38 38 ALA D 37 ALA D 42 1 6
HELIX 39 39 GLN D 61 ALA D 73 1 13
HELIX 40 40 PRO D 74 GLY D 78 5 5
HELIX 41 41 SER D 84 ASP D 101 1 18
HELIX 42 42 ASP D 101 TYR D 106 1 6
HELIX 43 43 TRP D 107 GLY D 111 5 5
HELIX 44 44 THR D 113 GLN D 117 5 5
HELIX 45 45 ASP D 118 LYS D 145 1 28
HELIX 46 46 SER D 156 GLY D 173 1 18
HELIX 47 47 LEU D 179 ALA D 191 1 13
HELIX 48 48 ASP D 192 GLU D 202 1 11
HELIX 49 49 SER E 11 GLY E 22 1 12
HELIX 50 50 ALA E 37 ALA E 42 1 6
HELIX 51 51 GLN E 61 ALA E 73 1 13
HELIX 52 52 PRO E 74 GLY E 78 5 5
HELIX 53 53 SER E 84 ASP E 101 1 18
HELIX 54 54 ASP E 101 TYR E 106 1 6
HELIX 55 55 TRP E 107 GLY E 111 5 5
HELIX 56 56 THR E 113 GLN E 117 5 5
HELIX 57 57 ASP E 118 LYS E 145 1 28
HELIX 58 58 SER E 156 GLY E 173 1 18
HELIX 59 59 LEU E 179 ALA E 191 1 13
HELIX 60 60 ASP E 192 GLU E 202 1 11
HELIX 61 61 SER F 11 GLY F 22 1 12
HELIX 62 62 ALA F 37 ALA F 42 1 6
HELIX 63 63 GLN F 61 ALA F 73 1 13
HELIX 64 64 PRO F 74 GLY F 78 5 5
HELIX 65 65 SER F 84 ASP F 101 1 18
HELIX 66 66 ASP F 101 TYR F 106 1 6
HELIX 67 67 TRP F 107 GLY F 111 5 5
HELIX 68 68 THR F 113 GLN F 117 5 5
HELIX 69 69 ASP F 118 LYS F 145 1 28
HELIX 70 70 SER F 156 GLY F 173 1 18
HELIX 71 71 LEU F 179 ALA F 191 1 13
HELIX 72 72 ASP F 192 GLU F 202 1 11
SHEET 1 AA 4 PHE A 25 PHE A 29 0
SHEET 2 AA 4 MET A 1 ILE A 5 1 O MET A 1 N ASP A 26
SHEET 3 AA 4 ALA A 51 VAL A 54 -1 O ALA A 51 N TYR A 4
SHEET 4 AA 4 TRP A 57 LEU A 59 -1 O TRP A 57 N VAL A 54
SHEET 1 BA 4 ASP B 26 PHE B 29 0
SHEET 2 BA 4 MET B 1 ILE B 5 1 O MET B 1 N ASP B 26
SHEET 3 BA 4 ALA B 51 VAL B 54 -1 O ALA B 51 N TYR B 4
SHEET 4 BA 4 TRP B 57 LEU B 59 -1 O TRP B 57 N VAL B 54
SHEET 1 CA 4 ASP C 26 PHE C 29 0
SHEET 2 CA 4 MET C 1 ILE C 5 1 O MET C 1 N ASP C 26
SHEET 3 CA 4 ALA C 51 VAL C 54 -1 O ALA C 51 N TYR C 4
SHEET 4 CA 4 TRP C 57 LEU C 59 -1 O TRP C 57 N VAL C 54
SHEET 1 DA 4 PHE D 25 PHE D 29 0
SHEET 2 DA 4 MET D 1 ILE D 5 1 O MET D 1 N ASP D 26
SHEET 3 DA 4 ALA D 51 VAL D 54 -1 O ALA D 51 N TYR D 4
SHEET 4 DA 4 TRP D 57 LEU D 59 -1 O TRP D 57 N VAL D 54
SHEET 1 EA 4 ASP E 26 PHE E 29 0
SHEET 2 EA 4 LYS E 2 ILE E 5 1 O LEU E 3 N GLN E 28
SHEET 3 EA 4 ALA E 51 VAL E 54 -1 O ALA E 51 N TYR E 4
SHEET 4 EA 4 TRP E 57 LEU E 59 -1 O TRP E 57 N VAL E 54
SHEET 1 FA 4 PHE F 25 PHE F 29 0
SHEET 2 FA 4 MET F 1 ILE F 5 1 O MET F 1 N ASP F 26
SHEET 3 FA 4 ALA F 51 VAL F 54 -1 O ALA F 51 N TYR F 4
SHEET 4 FA 4 TRP F 57 LEU F 59 -1 O TRP F 57 N VAL F 54
CISPEP 1 VAL A 49 PRO A 50 0 0.27
CISPEP 2 VAL B 49 PRO B 50 0 -1.05
CISPEP 3 VAL C 49 PRO C 50 0 -1.90
CISPEP 4 VAL D 49 PRO D 50 0 -0.15
CISPEP 5 VAL E 49 PRO E 50 0 1.28
CISPEP 6 VAL F 49 PRO F 50 0 -0.55
SITE 1 AC1 14 CYS A 10 MET A 35 ALA A 48 VAL A 49
SITE 2 AC1 14 PRO A 50 GLN A 61 ASN A 62 ASN A 99
SITE 3 AC1 14 HIS A 103 HOH A2015 HOH A2045 HOH A2093
SITE 4 AC1 14 SER B 100 ASP B 101
SITE 1 AC2 14 SER A 100 ASP A 101 CYS B 10 MET B 35
SITE 2 AC2 14 GLY B 47 ALA B 48 VAL B 49 PRO B 50
SITE 3 AC2 14 GLN B 61 ASN B 62 ASN B 99 HIS B 103
SITE 4 AC2 14 HOH B2120 HOH B2121
SITE 1 AC3 12 CYS C 10 HIS C 32 MET C 35 ALA C 48
SITE 2 AC3 12 VAL C 49 PRO C 50 GLN C 61 ASN C 62
SITE 3 AC3 12 ASN C 99 HIS C 103 SER D 100 ASP D 101
SITE 1 AC4 13 SER C 100 ASP C 101 CYS D 10 HIS D 32
SITE 2 AC4 13 MET D 35 ALA D 48 VAL D 49 PRO D 50
SITE 3 AC4 13 GLN D 61 ASN D 62 ASN D 99 HIS D 103
SITE 4 AC4 13 TYR D 161
SITE 1 AC5 15 CYS E 10 HIS E 32 MET E 35 ALA E 48
SITE 2 AC5 15 VAL E 49 PRO E 50 GLN E 61 ASN E 62
SITE 3 AC5 15 ASN E 99 HIS E 103 HOH E2028 HOH E2055
SITE 4 AC5 15 HOH E2109 SER F 100 ASP F 101
SITE 1 AC6 16 SER E 100 ASP E 101 CYS F 10 HIS F 32
SITE 2 AC6 16 MET F 35 ALA F 48 VAL F 49 PRO F 50
SITE 3 AC6 16 THR F 60 GLN F 61 ASN F 62 ASN F 99
SITE 4 AC6 16 HIS F 103 TYR F 161 HOH F2028 HOH F2134
SITE 1 AC7 1 HOH B2029
SITE 1 AC8 1 HOH D2030
SITE 1 AC9 2 ARG E 93 HOH F2018
SITE 1 BC1 1 GLN A 61
SITE 1 BC2 2 HOH C2036 ARG D 93
SITE 1 BC3 3 THR E 60 HOH E2030 ARG F 93
CRYST1 47.670 87.890 90.780 116.53 99.33 94.49 P 1 6
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 0.020978 0.001647 0.004767 0.00000
SCALE2 0.000000 0.011413 0.006027 0.00000
SCALE3 0.000000 0.000000 0.012624 0.00000
MTRIX1 1 0.181600 -0.367300 0.912200 -0.98190 1
MTRIX2 1 -0.350800 -0.890800 -0.288800 -31.18450 1
MTRIX3 1-41.298800-27.016300 42.766400 37.11640 1
(ATOM LINES ARE NOT SHOWN.)
END
