HEADER TRANSFERASE 20-AUG-14 4W66
TITLE CRYSTAL STRUCTURE OF GLUTATHIONE S-TRANSFERASE DOMAIN PROTEIN FROM
TITLE 2 HALIANGIUM OCHRACEUM DSM 14365
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTATHIONE S-TRANSFERASE DOMAIN PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HALIANGIUM OCHRACEUM;
SOURCE 3 ORGANISM_TAXID: 502025;
SOURCE 4 STRAIN: DSM 14365 / JCM 11303 / SMP-2;
SOURCE 5 GENE: HOCH_6316;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMCSG57
KEYWDS STRUCTURAL GENOMICS, PSI-BIOLOGY, MIDWEST CENTER FOR STRUCTURAL
KEYWDS 2 GENOMICS, MCSG, TRANSFERASE, GSH
EXPDTA X-RAY DIFFRACTION
AUTHOR C.CHANG,G.CHHOR,S.CLANCY,A.JOACHIMIAK,MIDWEST CENTER FOR STRUCTURAL
AUTHOR 2 GENOMICS (MCSG)
REVDAT 2 27-DEC-23 4W66 1 SOURCE REMARK
REVDAT 1 03-SEP-14 4W66 0
JRNL AUTH C.CHANG,G.CHHOR,S.CLANCY,A.JOACHIMIAK
JRNL TITL CRYSTAL STRUCTURE OF GLUTATHIONE S-TRANSFERASE DOMAIN
JRNL TITL 2 PROTEIN FROM HALIANGIUM OCHRACEUM DSM 14365
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.36 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0071
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.36
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.95
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 22422
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1205
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.36
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.42
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1229
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 72.82
REMARK 3 BIN R VALUE (WORKING SET) : 0.2410
REMARK 3 BIN FREE R VALUE SET COUNT : 60
REMARK 3 BIN FREE R VALUE : 0.2500
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3581
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 130
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.28
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.17000
REMARK 3 B22 (A**2) : 0.17000
REMARK 3 B33 (A**2) : -0.34000
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): 0.322
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.236
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.174
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.920
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.899
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3704 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3583 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5039 ; 1.257 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8166 ; 0.763 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 453 ; 5.334 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 173 ;36.142 ;21.676
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 553 ;15.095 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 46 ;19.291 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 561 ; 0.064 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4206 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 906 ; 0.001 ; 0.020
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): 1821 ; 1.175 ; 2.241
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1820 ; 1.175 ; 2.240
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2271 ; 2.065 ; 3.352
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 15
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 39
REMARK 3 ORIGIN FOR THE GROUP (A): 24.560 71.298 -6.296
REMARK 3 T TENSOR
REMARK 3 T11: 0.0517 T22: 0.0457
REMARK 3 T33: 0.0529 T12: 0.0090
REMARK 3 T13: 0.0070 T23: 0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 2.8172 L22: 2.1951
REMARK 3 L33: 4.7920 L12: 0.5453
REMARK 3 L13: -1.0642 L23: -0.1793
REMARK 3 S TENSOR
REMARK 3 S11: 0.0455 S12: 0.0859 S13: 0.1657
REMARK 3 S21: 0.1260 S22: -0.0429 S23: -0.0204
REMARK 3 S31: -0.1254 S32: 0.3357 S33: -0.0026
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 40 A 50
REMARK 3 ORIGIN FOR THE GROUP (A): 38.824 70.020 -1.726
REMARK 3 T TENSOR
REMARK 3 T11: 0.0288 T22: 0.1144
REMARK 3 T33: 0.0922 T12: -0.0310
REMARK 3 T13: -0.0339 T23: 0.0258
REMARK 3 L TENSOR
REMARK 3 L11: 8.4978 L22: 3.3863
REMARK 3 L33: 9.0908 L12: -2.8509
REMARK 3 L13: -0.8437 L23: -4.3910
REMARK 3 S TENSOR
REMARK 3 S11: -0.0408 S12: -0.0910 S13: 0.1974
REMARK 3 S21: 0.1622 S22: -0.0211 S23: -0.0978
REMARK 3 S31: -0.2935 S32: 0.1487 S33: 0.0619
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 51 A 113
REMARK 3 ORIGIN FOR THE GROUP (A): 20.579 59.683 0.032
REMARK 3 T TENSOR
REMARK 3 T11: 0.0418 T22: 0.0556
REMARK 3 T33: 0.0316 T12: 0.0384
REMARK 3 T13: 0.0043 T23: -0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 0.9383 L22: 1.9074
REMARK 3 L33: 2.0578 L12: -0.1985
REMARK 3 L13: -0.6979 L23: -0.1762
REMARK 3 S TENSOR
REMARK 3 S11: -0.0364 S12: -0.0716 S13: 0.0616
REMARK 3 S21: 0.0684 S22: -0.0310 S23: 0.0349
REMARK 3 S31: -0.0247 S32: 0.1027 S33: 0.0674
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 114 A 146
REMARK 3 ORIGIN FOR THE GROUP (A): 24.615 46.123 -15.125
REMARK 3 T TENSOR
REMARK 3 T11: 0.0991 T22: 0.0488
REMARK 3 T33: 0.0087 T12: 0.0370
REMARK 3 T13: 0.0096 T23: -0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 10.7343 L22: 0.3806
REMARK 3 L33: 2.0616 L12: -0.6784
REMARK 3 L13: -3.4245 L23: -0.0603
REMARK 3 S TENSOR
REMARK 3 S11: 0.0278 S12: -0.0625 S13: -0.1153
REMARK 3 S21: -0.0677 S22: -0.1095 S23: 0.0161
REMARK 3 S31: 0.2810 S32: 0.1265 S33: 0.0817
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 147 A 161
REMARK 3 ORIGIN FOR THE GROUP (A): 6.428 59.917 -4.766
REMARK 3 T TENSOR
REMARK 3 T11: 0.0501 T22: 0.1852
REMARK 3 T33: 0.1235 T12: -0.0011
REMARK 3 T13: 0.0103 T23: -0.0713
REMARK 3 L TENSOR
REMARK 3 L11: 7.2922 L22: 4.1084
REMARK 3 L33: 7.6674 L12: 0.5629
REMARK 3 L13: 2.0184 L23: -2.7746
REMARK 3 S TENSOR
REMARK 3 S11: 0.1653 S12: -0.5412 S13: 0.0617
REMARK 3 S21: 0.0610 S22: -0.3416 S23: 0.3770
REMARK 3 S31: -0.0932 S32: -0.6763 S33: 0.1764
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 162 A 192
REMARK 3 ORIGIN FOR THE GROUP (A): 14.221 54.119 -18.980
REMARK 3 T TENSOR
REMARK 3 T11: 0.0639 T22: 0.0526
REMARK 3 T33: 0.0311 T12: -0.0016
REMARK 3 T13: -0.0038 T23: -0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 5.0523 L22: 1.6436
REMARK 3 L33: 4.6059 L12: 0.7037
REMARK 3 L13: 0.9977 L23: 2.3369
REMARK 3 S TENSOR
REMARK 3 S11: 0.0578 S12: 0.3039 S13: -0.0817
REMARK 3 S21: -0.1936 S22: -0.0815 S23: -0.0484
REMARK 3 S31: -0.2328 S32: -0.1260 S33: 0.0237
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 193 A 215
REMARK 3 ORIGIN FOR THE GROUP (A): 15.170 66.980 -15.015
REMARK 3 T TENSOR
REMARK 3 T11: 0.0544 T22: 0.0645
REMARK 3 T33: 0.0175 T12: 0.0111
REMARK 3 T13: -0.0178 T23: 0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 6.2492 L22: 4.7952
REMARK 3 L33: 2.1120 L12: -0.4703
REMARK 3 L13: -1.2455 L23: -0.7291
REMARK 3 S TENSOR
REMARK 3 S11: 0.1380 S12: 0.6007 S13: -0.0288
REMARK 3 S21: -0.1802 S22: -0.0815 S23: 0.2446
REMARK 3 S31: -0.1894 S32: -0.1740 S33: -0.0564
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 216 A 236
REMARK 3 ORIGIN FOR THE GROUP (A): 28.086 52.338 -24.830
REMARK 3 T TENSOR
REMARK 3 T11: 0.1190 T22: 0.1480
REMARK 3 T33: 0.1279 T12: 0.1125
REMARK 3 T13: 0.0820 T23: 0.0523
REMARK 3 L TENSOR
REMARK 3 L11: 8.4074 L22: 12.4144
REMARK 3 L33: 5.5679 L12: 7.4780
REMARK 3 L13: 4.0515 L23: 3.8486
REMARK 3 S TENSOR
REMARK 3 S11: 0.3048 S12: 0.7895 S13: 0.0426
REMARK 3 S21: -0.0739 S22: 0.2738 S23: -0.2604
REMARK 3 S31: -0.0205 S32: 0.3688 S33: -0.5786
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 3 B 38
REMARK 3 ORIGIN FOR THE GROUP (A): 21.838 36.653 9.248
REMARK 3 T TENSOR
REMARK 3 T11: 0.2220 T22: 0.0561
REMARK 3 T33: 0.0387 T12: 0.0984
REMARK 3 T13: 0.0474 T23: 0.0162
REMARK 3 L TENSOR
REMARK 3 L11: 6.0241 L22: 2.9935
REMARK 3 L33: 3.8227 L12: 0.3697
REMARK 3 L13: 0.0624 L23: -0.2691
REMARK 3 S TENSOR
REMARK 3 S11: -0.0092 S12: 0.2107 S13: -0.3338
REMARK 3 S21: 0.1014 S22: 0.0778 S23: 0.0509
REMARK 3 S31: 0.4862 S32: 0.1033 S33: -0.0686
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 52 B 113
REMARK 3 ORIGIN FOR THE GROUP (A): 22.463 49.697 6.737
REMARK 3 T TENSOR
REMARK 3 T11: 0.1176 T22: 0.0668
REMARK 3 T33: 0.0165 T12: 0.0702
REMARK 3 T13: -0.0089 T23: -0.0026
REMARK 3 L TENSOR
REMARK 3 L11: 2.3290 L22: 1.7523
REMARK 3 L33: 1.3128 L12: -0.5332
REMARK 3 L13: -0.3741 L23: -0.7308
REMARK 3 S TENSOR
REMARK 3 S11: 0.0493 S12: 0.0613 S13: -0.1754
REMARK 3 S21: 0.1638 S22: -0.0614 S23: 0.0067
REMARK 3 S31: 0.1208 S32: 0.1380 S33: 0.0121
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 114 B 146
REMARK 3 ORIGIN FOR THE GROUP (A): 40.240 49.678 -3.835
REMARK 3 T TENSOR
REMARK 3 T11: 0.0433 T22: 0.2570
REMARK 3 T33: 0.0935 T12: 0.0618
REMARK 3 T13: 0.0045 T23: 0.0211
REMARK 3 L TENSOR
REMARK 3 L11: 0.6479 L22: 6.1101
REMARK 3 L33: 10.6669 L12: 0.3265
REMARK 3 L13: 0.8077 L23: 5.6521
REMARK 3 S TENSOR
REMARK 3 S11: -0.0684 S12: 0.0233 S13: 0.1050
REMARK 3 S21: -0.2760 S22: 0.0778 S23: -0.3508
REMARK 3 S31: -0.1174 S32: 1.1081 S33: -0.0094
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 147 B 161
REMARK 3 ORIGIN FOR THE GROUP (A): 30.104 52.913 19.053
REMARK 3 T TENSOR
REMARK 3 T11: 0.1971 T22: 0.2155
REMARK 3 T33: 0.0802 T12: 0.0747
REMARK 3 T13: -0.0424 T23: -0.0328
REMARK 3 L TENSOR
REMARK 3 L11: 5.4657 L22: 9.1309
REMARK 3 L33: 7.1199 L12: 1.4516
REMARK 3 L13: 1.7438 L23: 0.2182
REMARK 3 S TENSOR
REMARK 3 S11: -0.1072 S12: -0.9479 S13: 0.2724
REMARK 3 S21: 0.7521 S22: -0.1527 S23: 0.1960
REMARK 3 S31: 0.0730 S32: 0.1395 S33: 0.2599
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 162 B 192
REMARK 3 ORIGIN FOR THE GROUP (A): 42.892 46.264 9.120
REMARK 3 T TENSOR
REMARK 3 T11: 0.1384 T22: 0.3425
REMARK 3 T33: 0.2590 T12: 0.1681
REMARK 3 T13: -0.0736 T23: 0.0817
REMARK 3 L TENSOR
REMARK 3 L11: 5.8751 L22: 2.0091
REMARK 3 L33: 3.6365 L12: -1.9582
REMARK 3 L13: 0.2053 L23: 0.5729
REMARK 3 S TENSOR
REMARK 3 S11: 0.0398 S12: 0.0285 S13: -0.1020
REMARK 3 S21: 0.1149 S22: -0.1545 S23: -0.4724
REMARK 3 S31: 0.3414 S32: 0.7555 S33: 0.1147
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 193 B 215
REMARK 3 ORIGIN FOR THE GROUP (A): 33.384 38.706 15.092
REMARK 3 T TENSOR
REMARK 3 T11: 0.2750 T22: 0.2530
REMARK 3 T33: 0.1937 T12: 0.1680
REMARK 3 T13: -0.0234 T23: 0.0225
REMARK 3 L TENSOR
REMARK 3 L11: 1.1572 L22: 5.8529
REMARK 3 L33: 4.4390 L12: 0.3557
REMARK 3 L13: 0.9008 L23: -0.8978
REMARK 3 S TENSOR
REMARK 3 S11: -0.0318 S12: -0.0080 S13: -0.2132
REMARK 3 S21: 0.6341 S22: 0.0963 S23: -0.7644
REMARK 3 S31: 0.4150 S32: 0.8106 S33: -0.0644
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 216 B 235
REMARK 3 ORIGIN FOR THE GROUP (A): 44.376 37.976 -3.988
REMARK 3 T TENSOR
REMARK 3 T11: 0.2664 T22: 0.4200
REMARK 3 T33: 0.2724 T12: 0.3204
REMARK 3 T13: 0.0250 T23: 0.0149
REMARK 3 L TENSOR
REMARK 3 L11: 7.2307 L22: 8.8089
REMARK 3 L33: 4.5561 L12: 7.0953
REMARK 3 L13: 1.7950 L23: 0.5182
REMARK 3 S TENSOR
REMARK 3 S11: -0.0779 S12: 0.0993 S13: 0.2238
REMARK 3 S21: -0.1202 S22: -0.0498 S23: -0.1760
REMARK 3 S31: 0.5179 S32: 0.6121 S33: 0.1277
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : RESIDUAL ONLY
REMARK 4
REMARK 4 4W66 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-AUG-14.
REMARK 100 THE DEPOSITION ID IS D_1000203252.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JUN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97924
REMARK 200 MONOCHROMATOR : SI(111) DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000, SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24250
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.360
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : 0.13200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.36
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.30
REMARK 200 R MERGE FOR SHELL (I) : 0.98600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: HKL-3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M CALCIUM CHLORIDE, 0.1M THIS-CL
REMARK 280 20% PEG4000, PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 8555 Y+1/2,-X+1/2,Z+1/2
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 65.20000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 65.20000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 35.07350
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 65.20000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 65.20000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 35.07350
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 65.20000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 65.20000
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 35.07350
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 65.20000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 65.20000
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 35.07350
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.
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: 4990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 ALA A 237
REMARK 465 SER A 238
REMARK 465 MSE A 239
REMARK 465 GLU A 240
REMARK 465 SER B -2
REMARK 465 ASN B -1
REMARK 465 ALA B 0
REMARK 465 MSE B 1
REMARK 465 ASN B 2
REMARK 465 GLN B 39
REMARK 465 TRP B 40
REMARK 465 SER B 41
REMARK 465 GLN B 42
REMARK 465 HIS B 43
REMARK 465 LYS B 44
REMARK 465 ASP B 45
REMARK 465 SER B 46
REMARK 465 ASP B 47
REMARK 465 ALA B 48
REMARK 465 GLY B 49
REMARK 465 GLY B 50
REMARK 465 PRO B 51
REMARK 465 GLY B 236
REMARK 465 ALA B 237
REMARK 465 SER B 238
REMARK 465 MSE B 239
REMARK 465 GLU B 240
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 GLU A 67 128.21 72.61
REMARK 500 VAL A 104 -62.34 -121.79
REMARK 500 HIS A 216 131.98 -38.35
REMARK 500 GLU B 67 125.38 81.76
REMARK 500 VAL B 104 -71.43 -128.73
REMARK 500 ALA B 215 36.06 -88.45
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 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GSH B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MCSG-APC103457 RELATED DB: TARGETTRACK
DBREF 4W66 A 1 240 UNP D0LNW1 D0LNW1_HALO1 1 240
DBREF 4W66 B 1 240 UNP D0LNW1 D0LNW1_HALO1 1 240
SEQADV 4W66 SER A -2 UNP D0LNW1 EXPRESSION TAG
SEQADV 4W66 ASN A -1 UNP D0LNW1 EXPRESSION TAG
SEQADV 4W66 ALA A 0 UNP D0LNW1 EXPRESSION TAG
SEQADV 4W66 SER B -2 UNP D0LNW1 EXPRESSION TAG
SEQADV 4W66 ASN B -1 UNP D0LNW1 EXPRESSION TAG
SEQADV 4W66 ALA B 0 UNP D0LNW1 EXPRESSION TAG
SEQRES 1 A 243 SER ASN ALA MSE ASN GLU PRO ILE ILE LEU ARG TYR PHE
SEQRES 2 A 243 PRO VAL LEU GLY ARG ALA GLN ALA LEU ARG HIS ALA LEU
SEQRES 3 A 243 ALA ASP ALA GLU LEU ALA PHE ARG ASP LEU ARG ILE PRO
SEQRES 4 A 243 LEU GLU GLN TRP SER GLN HIS LYS ASP SER ASP ALA GLY
SEQRES 5 A 243 GLY PRO TYR GLY SER LEU PRO THR LEU ARG TRP HIS GLY
SEQRES 6 A 243 VAL GLU VAL ALA GLU THR ILE ALA ILE ALA SER PHE LEU
SEQRES 7 A 243 ALA ARG SER LEU GLY HIS TYR GLU GLY ARG ASP ASN GLY
SEQRES 8 A 243 GLU ILE ALA ARG LEU GLU ALA VAL VAL SER LEU CYS TYR
SEQRES 9 A 243 THR GLU VAL SER LEU GLN ILE ALA GLN LEU LEU TRP LEU
SEQRES 10 A 243 ASP LEU PHE ASN PRO GLY VAL ASP LEU ALA ALA ALA VAL
SEQRES 11 A 243 PRO LEU GLN PHE GLY ARG LEU VAL ALA ARG LEU THR ARG
SEQRES 12 A 243 LEU GLU ALA HIS THR PRO GLU ALA GLY TRP PHE GLY GLY
SEQRES 13 A 243 GLU ARG PRO VAL MSE ALA ASP TYR PHE ALA ALA GLU ALA
SEQRES 14 A 243 ILE GLU ALA LEU ARG TYR LEU LEU GLY ARG GLU HIS ASP
SEQRES 15 A 243 ASP ALA LEU ARG THR ARG LEU PRO HIS LEU CYS ALA LEU
SEQRES 16 A 243 ALA ARG ARG MSE ALA GLN ARG PRO ALA LEU ALA GLN ALA
SEQRES 17 A 243 TRP SER THR ARG PRO GLN THR PHE THR ALA HIS PRO ASP
SEQRES 18 A 243 GLU ALA ALA MSE LEU GLU ARG LEU ARG ALA LEU PRO LEU
SEQRES 19 A 243 ALA ALA THR ILE GLY ALA SER MSE GLU
SEQRES 1 B 243 SER ASN ALA MSE ASN GLU PRO ILE ILE LEU ARG TYR PHE
SEQRES 2 B 243 PRO VAL LEU GLY ARG ALA GLN ALA LEU ARG HIS ALA LEU
SEQRES 3 B 243 ALA ASP ALA GLU LEU ALA PHE ARG ASP LEU ARG ILE PRO
SEQRES 4 B 243 LEU GLU GLN TRP SER GLN HIS LYS ASP SER ASP ALA GLY
SEQRES 5 B 243 GLY PRO TYR GLY SER LEU PRO THR LEU ARG TRP HIS GLY
SEQRES 6 B 243 VAL GLU VAL ALA GLU THR ILE ALA ILE ALA SER PHE LEU
SEQRES 7 B 243 ALA ARG SER LEU GLY HIS TYR GLU GLY ARG ASP ASN GLY
SEQRES 8 B 243 GLU ILE ALA ARG LEU GLU ALA VAL VAL SER LEU CYS TYR
SEQRES 9 B 243 THR GLU VAL SER LEU GLN ILE ALA GLN LEU LEU TRP LEU
SEQRES 10 B 243 ASP LEU PHE ASN PRO GLY VAL ASP LEU ALA ALA ALA VAL
SEQRES 11 B 243 PRO LEU GLN PHE GLY ARG LEU VAL ALA ARG LEU THR ARG
SEQRES 12 B 243 LEU GLU ALA HIS THR PRO GLU ALA GLY TRP PHE GLY GLY
SEQRES 13 B 243 GLU ARG PRO VAL MSE ALA ASP TYR PHE ALA ALA GLU ALA
SEQRES 14 B 243 ILE GLU ALA LEU ARG TYR LEU LEU GLY ARG GLU HIS ASP
SEQRES 15 B 243 ASP ALA LEU ARG THR ARG LEU PRO HIS LEU CYS ALA LEU
SEQRES 16 B 243 ALA ARG ARG MSE ALA GLN ARG PRO ALA LEU ALA GLN ALA
SEQRES 17 B 243 TRP SER THR ARG PRO GLN THR PHE THR ALA HIS PRO ASP
SEQRES 18 B 243 GLU ALA ALA MSE LEU GLU ARG LEU ARG ALA LEU PRO LEU
SEQRES 19 B 243 ALA ALA THR ILE GLY ALA SER MSE GLU
MODRES 4W66 MSE A 1 MET MODIFIED RESIDUE
MODRES 4W66 MSE A 158 MET MODIFIED RESIDUE
MODRES 4W66 MSE A 196 MET MODIFIED RESIDUE
MODRES 4W66 MSE A 222 MET MODIFIED RESIDUE
MODRES 4W66 MSE B 158 MET MODIFIED RESIDUE
MODRES 4W66 MSE B 196 MET MODIFIED RESIDUE
MODRES 4W66 MSE B 222 MET MODIFIED RESIDUE
HET MSE A 1 8
HET MSE A 158 8
HET MSE A 196 8
HET MSE A 222 8
HET MSE B 158 8
HET MSE B 196 8
HET MSE B 222 8
HET GSH A 301 20
HET GSH B 301 20
HETNAM MSE SELENOMETHIONINE
HETNAM GSH GLUTATHIONE
FORMUL 1 MSE 7(C5 H11 N O2 SE)
FORMUL 3 GSH 2(C10 H17 N3 O6 S)
FORMUL 5 HOH *130(H2 O)
HELIX 1 AA1 ALA A 16 ALA A 26 1 11
HELIX 2 AA2 PRO A 36 GLU A 38 5 3
HELIX 3 AA3 GLN A 39 LYS A 44 1 6
HELIX 4 AA4 GLU A 67 GLY A 80 1 14
HELIX 5 AA5 ASP A 86 VAL A 104 1 19
HELIX 6 AA6 VAL A 104 TRP A 113 1 10
HELIX 7 AA7 TRP A 113 ASN A 118 1 6
HELIX 8 AA8 ASP A 122 HIS A 144 1 23
HELIX 9 AA9 VAL A 157 GLY A 175 1 19
HELIX 10 AB1 HIS A 178 LEU A 186 1 9
HELIX 11 AB2 LEU A 186 GLN A 198 1 13
HELIX 12 AB3 ARG A 199 ALA A 201 5 3
HELIX 13 AB4 LEU A 202 THR A 208 1 7
HELIX 14 AB5 ASP A 218 LEU A 229 1 12
HELIX 15 AB6 PRO A 230 GLY A 236 1 7
HELIX 16 AB7 ALA B 16 ALA B 26 1 11
HELIX 17 AB8 GLU B 67 LEU B 79 1 13
HELIX 18 AB9 ASP B 86 VAL B 104 1 19
HELIX 19 AC1 VAL B 104 TRP B 113 1 10
HELIX 20 AC2 TRP B 113 ASN B 118 1 6
HELIX 21 AC3 ASP B 122 ALA B 143 1 22
HELIX 22 AC4 VAL B 157 GLY B 175 1 19
HELIX 23 AC5 HIS B 178 LEU B 186 1 9
HELIX 24 AC6 LEU B 186 GLN B 198 1 13
HELIX 25 AC7 ARG B 199 ALA B 201 5 3
HELIX 26 AC8 LEU B 202 THR B 208 1 7
HELIX 27 AC9 ASP B 218 ALA B 228 1 11
HELIX 28 AD1 PRO B 230 ILE B 235 5 6
SHEET 1 AA1 4 ARG A 31 ARG A 34 0
SHEET 2 AA1 4 ILE A 5 TYR A 9 1 N LEU A 7 O ARG A 31
SHEET 3 AA1 4 THR A 57 TRP A 60 -1 O THR A 57 N ARG A 8
SHEET 4 AA1 4 VAL A 63 ALA A 66 -1 O VAL A 65 N LEU A 58
SHEET 1 AA2 4 ARG B 31 ARG B 34 0
SHEET 2 AA2 4 ILE B 5 TYR B 9 1 N ILE B 5 O ARG B 31
SHEET 3 AA2 4 THR B 57 TRP B 60 -1 O THR B 57 N ARG B 8
SHEET 4 AA2 4 VAL B 63 ALA B 66 -1 O VAL B 65 N LEU B 58
SSBOND 1 CYS A 190 GSH A 301 1555 1555 2.16
LINK C MSE A 1 N ASN A 2 1555 1555 1.34
LINK C VAL A 157 N MSE A 158 1555 1555 1.33
LINK C MSE A 158 N ALA A 159 1555 1555 1.32
LINK C ARG A 195 N MSE A 196 1555 1555 1.33
LINK C MSE A 196 N ALA A 197 1555 1555 1.34
LINK C ALA A 221 N MSE A 222 1555 1555 1.33
LINK C MSE A 222 N LEU A 223 1555 1555 1.33
LINK C VAL B 157 N MSE B 158 1555 1555 1.33
LINK C MSE B 158 N ALA B 159 1555 1555 1.33
LINK C ARG B 195 N MSE B 196 1555 1555 1.32
LINK C MSE B 196 N ALA B 197 1555 1555 1.32
LINK C ALA B 221 N MSE B 222 1555 1555 1.33
LINK C MSE B 222 N LEU B 223 1555 1555 1.33
CISPEP 1 LEU A 55 PRO A 56 0 8.11
CISPEP 2 LEU B 55 PRO B 56 0 8.88
SITE 1 AC1 7 GLU A 168 ARG A 171 ASP A 179 ARG A 183
SITE 2 AC1 7 CYS A 190 ARG A 194 ALA A 197
SITE 1 AC2 6 GLU B 168 ARG B 171 ASP B 179 ARG B 183
SITE 2 AC2 6 CYS B 190 ARG B 194
CRYST1 130.400 130.400 70.147 90.00 90.00 90.00 I 4 16
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 0.007669 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007669 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014256 0.00000
HETATM 1 N MSE A 1 24.735 85.109 -4.769 1.00 65.16 N
ANISOU 1 N MSE A 1 12236 8028 12171 -929 898 143 N
HETATM 2 CA MSE A 1 24.535 83.615 -4.832 1.00 68.36 C
ANISOU 2 CA MSE A 1 11806 8280 12008 -768 754 139 C
HETATM 3 C MSE A 1 24.594 82.965 -3.454 1.00 65.86 C
ANISOU 3 C MSE A 1 11239 7892 11420 -837 721 -59 C
HETATM 4 O MSE A 1 24.667 81.731 -3.339 1.00 57.81 O
ANISOU 4 O MSE A 1 9959 7123 10307 -763 608 -67 O
HETATM 5 CB MSE A 1 25.589 82.976 -5.756 1.00 72.55 C
ANISOU 5 CB MSE A 1 11913 8926 12247 -880 638 237 C
HETATM 6 CG MSE A 1 25.691 83.647 -7.134 1.00 77.39 C
ANISOU 6 CG MSE A 1 12706 9549 12991 -892 679 435 C
HETATM 7 SE MSE A 1 26.162 82.395 -8.597 1.00 82.01 SE
ANISOU 7 SE MSE A 1 12779 10367 13298 -792 545 590 SE
HETATM 8 CE MSE A 1 26.810 83.690 -9.939 1.00 78.74 C
ANISOU 8 CE MSE A 1 12941 10237 13262 -999 636 799 C
(ATOM LINES ARE NOT SHOWN.)
END
