HEADER OXIDOREDUCTASE 23-FEB-16 5ID2
TITLE ASYMMETRY IN THE ACTIVE SITE OF MYCOBACTERIUM TUBERCULOSIS AHPE UPON
TITLE 2 EXPOSURE TO MYCOTHIOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE PEROXIREDOXIN RV2238C;
COMPND 3 CHAIN: A, D;
COMPND 4 SYNONYM: THIOREDOXIN REDUCTASE;
COMPND 5 EC: 1.11.1.15;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PUTATIVE PEROXIREDOXIN RV2238C;
COMPND 9 CHAIN: B, C;
COMPND 10 SYNONYM: THIOREDOXIN REDUCTASE;
COMPND 11 EC: 1.11.1.15;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS H37RV;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 ATCC: ATCC 25618;
SOURCE 6 GENE: RV2238C, MTAHPE;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET9D;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS H37RV;
SOURCE 14 ORGANISM_TAXID: 83332;
SOURCE 15 STRAIN: H37RV;
SOURCE 16 ATCC: ATCC 25618;
SOURCE 17 GENE: RV2238C, MTAHPE;
SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 20 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 22 EXPRESSION_SYSTEM_PLASMID: PET9D
KEYWDS THIOREDOXIN FOLD, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.KUMAR,A.M.BALAKRISHNA,G.GRUBER
REVDAT 4 15-NOV-23 5ID2 1 REMARK
REVDAT 3 08-NOV-23 5ID2 1 JRNL REMARK
REVDAT 2 24-AUG-16 5ID2 1 JRNL
REVDAT 1 03-AUG-16 5ID2 0
JRNL AUTH A.KUMAR,A.M.BALAKRISHNA,W.NARTEY,M.S.S.MANIMEKALAI,G.GRUBER
JRNL TITL REDOX CHEMISTRY OF MYCOBACTERIUM TUBERCULOSIS
JRNL TITL 2 ALKYLHYDROPEROXIDE REDUCTASE E (AHPE): STRUCTURAL AND
JRNL TITL 3 MECHANISTIC INSIGHT INTO A MYCOREDOXIN-1 INDEPENDENT
JRNL TITL 4 REDUCTIVE PATHWAY OF AHPE VIA MYCOTHIOL
JRNL REF FREE RADIC. BIOL. MED. V. 97 588 2016
JRNL REFN ESSN 1873-4596
JRNL PMID 27417938
JRNL DOI 10.1016/J.FREERADBIOMED.2016.07.007
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.LI,N.A.PETERSON,M.Y.KIM,C.Y.KIM,L.W.HUNG,M.YU,T.LEKIN,
REMARK 1 AUTH 2 B.W.SEGELKE,J.S.LOTT,E.N.BAKER
REMARK 1 TITL CRYSTAL STRUCTURE OF AHPE FROM MYCOBACTERIUM TUBERCULOSIS, A
REMARK 1 TITL 2 1-CYS PEROXIREDOXIN
REMARK 1 REF J.MOL.BIOL. V. 346 1035 2005
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 15701515
REMARK 1 DOI 10.1016/J.JMB.2004.12.046
REMARK 2
REMARK 2 RESOLUTION. 2.43 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.43
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 26336
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1387
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) : 2.43
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.50
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1825
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.43
REMARK 3 BIN R VALUE (WORKING SET) : 0.2430
REMARK 3 BIN FREE R VALUE SET COUNT : 112
REMARK 3 BIN FREE R VALUE : 0.2610
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4848
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 16
REMARK 3 SOLVENT ATOMS : 230
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.01
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.73
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.79000
REMARK 3 B22 (A**2) : 0.79000
REMARK 3 B33 (A**2) : -1.58000
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): 0.446
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.225
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.153
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.877
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.941
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5088 ; 0.006 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4862 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6940 ; 1.145 ; 1.944
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11012 ; 1.021 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 640 ; 5.332 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 252 ;34.749 ;23.889
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 769 ;12.888 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 38 ;11.776 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 756 ; 0.063 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5967 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1267 ; 0.004 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 6
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 0 152 B 0 152 9240 0.11 0.05
REMARK 3 2 A 0 152 C 0 152 9289 0.11 0.05
REMARK 3 3 A 0 152 D 0 152 9333 0.10 0.05
REMARK 3 4 B -3 153 C -3 153 9814 0.07 0.05
REMARK 3 5 B -1 152 D -1 152 9161 0.12 0.05
REMARK 3 6 C -1 152 D -1 152 9084 0.11 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
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 0 A 153
REMARK 3 ORIGIN FOR THE GROUP (A): 17.4479 34.5531 -30.3119
REMARK 3 T TENSOR
REMARK 3 T11: 0.0252 T22: 0.0722
REMARK 3 T33: 0.0725 T12: -0.0298
REMARK 3 T13: 0.0193 T23: -0.0256
REMARK 3 L TENSOR
REMARK 3 L11: 1.1018 L22: 0.6844
REMARK 3 L33: 0.4323 L12: -0.6860
REMARK 3 L13: -0.1631 L23: 0.0745
REMARK 3 S TENSOR
REMARK 3 S11: 0.0421 S12: -0.0302 S13: -0.0530
REMARK 3 S21: -0.0483 S22: 0.0023 S23: 0.0108
REMARK 3 S31: -0.0523 S32: -0.0182 S33: -0.0444
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 : B -3 B 153
REMARK 3 ORIGIN FOR THE GROUP (A): 40.9008 12.0732 -26.5776
REMARK 3 T TENSOR
REMARK 3 T11: 0.0724 T22: 0.0548
REMARK 3 T33: 0.0653 T12: -0.0166
REMARK 3 T13: -0.0134 T23: -0.0231
REMARK 3 L TENSOR
REMARK 3 L11: 0.1506 L22: 0.7958
REMARK 3 L33: 0.2871 L12: -0.2652
REMARK 3 L13: 0.1166 L23: -0.1808
REMARK 3 S TENSOR
REMARK 3 S11: 0.0412 S12: -0.0124 S13: 0.0388
REMARK 3 S21: -0.0287 S22: -0.0112 S23: -0.0200
REMARK 3 S31: 0.0366 S32: -0.0034 S33: -0.0300
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 : C -3 C 153
REMARK 3 ORIGIN FOR THE GROUP (A): 33.3601 58.6808 -12.1871
REMARK 3 T TENSOR
REMARK 3 T11: 0.0997 T22: 0.0296
REMARK 3 T33: 0.0927 T12: -0.0184
REMARK 3 T13: 0.0037 T23: -0.0148
REMARK 3 L TENSOR
REMARK 3 L11: 0.1684 L22: 0.5555
REMARK 3 L33: 0.3913 L12: -0.2493
REMARK 3 L13: -0.1983 L23: 0.1535
REMARK 3 S TENSOR
REMARK 3 S11: 0.0062 S12: 0.0041 S13: -0.0311
REMARK 3 S21: 0.0159 S22: 0.0243 S23: 0.0668
REMARK 3 S31: -0.0419 S32: 0.0039 S33: -0.0305
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 : D -1 D 153
REMARK 3 ORIGIN FOR THE GROUP (A): 58.2566 37.7650 -15.8384
REMARK 3 T TENSOR
REMARK 3 T11: 0.0358 T22: 0.0866
REMARK 3 T33: 0.0641 T12: -0.0238
REMARK 3 T13: 0.0085 T23: 0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 0.6586 L22: 0.6922
REMARK 3 L33: 0.3839 L12: -0.2199
REMARK 3 L13: -0.0358 L23: -0.1148
REMARK 3 S TENSOR
REMARK 3 S11: 0.0128 S12: -0.0027 S13: 0.0472
REMARK 3 S21: -0.0113 S22: -0.0414 S23: 0.0203
REMARK 3 S31: -0.0045 S32: 0.0452 S33: 0.0285
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 301 A 353
REMARK 3 RESIDUE RANGE : B 301 B 369
REMARK 3 RESIDUE RANGE : C 201 C 260
REMARK 3 RESIDUE RANGE : D 201 D 248
REMARK 3 ORIGIN FOR THE GROUP (A): 37.8282 35.3766 -20.7075
REMARK 3 T TENSOR
REMARK 3 T11: 0.0936 T22: 0.0829
REMARK 3 T33: 0.1139 T12: -0.0188
REMARK 3 T13: 0.0197 T23: -0.0190
REMARK 3 L TENSOR
REMARK 3 L11: 0.0077 L22: 0.0517
REMARK 3 L33: 0.2027 L12: -0.0039
REMARK 3 L13: 0.0150 L23: -0.0621
REMARK 3 S TENSOR
REMARK 3 S11: -0.0240 S12: -0.0028 S13: -0.0140
REMARK 3 S21: -0.0186 S22: 0.0358 S23: 0.0159
REMARK 3 S31: -0.0249 S32: 0.0043 S33: -0.0118
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 : B 201 B 201
REMARK 3 ORIGIN FOR THE GROUP (A): 43.0068 14.3618 -40.7631
REMARK 3 T TENSOR
REMARK 3 T11: 0.3997 T22: 0.1485
REMARK 3 T33: 0.3661 T12: 0.0205
REMARK 3 T13: 0.1494 T23: -0.1909
REMARK 3 L TENSOR
REMARK 3 L11: 13.0777 L22: 26.3335
REMARK 3 L33: 426.5292 L12: -3.6462
REMARK 3 L13: 47.1872 L23: 67.3884
REMARK 3 S TENSOR
REMARK 3 S11: 1.3525 S12: 0.2252 S13: 0.4102
REMARK 3 S21: 0.4455 S22: 0.1850 S23: -1.0845
REMARK 3 S31: 7.5473 S32: 1.5681 S33: -1.5375
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 : B 202 B 202
REMARK 3 ORIGIN FOR THE GROUP (A): 33.5136 17.4496 -11.2610
REMARK 3 T TENSOR
REMARK 3 T11: 0.2446 T22: 0.3134
REMARK 3 T33: 0.3837 T12: 0.1131
REMARK 3 T13: -0.0784 T23: -0.2240
REMARK 3 L TENSOR
REMARK 3 L11: 5.0030 L22: 22.7872
REMARK 3 L33: 41.4912 L12: -9.1865
REMARK 3 L13: 11.6720 L23: -30.6194
REMARK 3 S TENSOR
REMARK 3 S11: -0.3530 S12: -0.5953 S13: 0.8163
REMARK 3 S21: 0.2180 S22: 0.0587 S23: -0.4592
REMARK 3 S31: -0.1509 S32: 0.2195 S33: 0.2943
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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
REMARK 4
REMARK 4 5ID2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1000218613.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-OCT-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSRRC
REMARK 200 BEAMLINE : BL13B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27862
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.430
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.43
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.52
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.27600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
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: 1XXU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8M SODIUM MALONATE PH 5.0, 0.1M
REMARK 280 SODIUM ACETATE PH 4.5, 5% GLYCEROL, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42
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+1/2
REMARK 290 4555 Y,-X,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 16.80800
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 16.80800
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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 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: 1440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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 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 -10
REMARK 465 LYS A -9
REMARK 465 HIS 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 PRO A -2
REMARK 465 MET A -1
REMARK 465 MET B -10
REMARK 465 LYS B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 MET C -10
REMARK 465 LYS C -9
REMARK 465 HIS C -8
REMARK 465 HIS C -7
REMARK 465 HIS C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 MET D -10
REMARK 465 LYS D -9
REMARK 465 HIS D -8
REMARK 465 HIS D -7
REMARK 465 HIS D -6
REMARK 465 HIS D -5
REMARK 465 HIS D -4
REMARK 465 HIS D -3
REMARK 465 PRO D -2
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 116 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG B 142 NE - CZ - NH1 ANGL. DEV. = 3.1 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 ALA A 29 -52.76 -126.26
REMARK 500 ASP A 93 58.61 -92.64
REMARK 500 THR A 152 -56.71 -124.74
REMARK 500 ALA B 29 -53.25 -127.06
REMARK 500 ASP B 93 59.72 -94.57
REMARK 500 ALA C 29 -52.99 -127.01
REMARK 500 ALA D 29 -52.83 -126.86
REMARK 500 ASP D 93 58.68 -92.90
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 GOL A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 202
DBREF 5ID2 A 1 153 UNP P9WIE3 Y2238_MYCTU 1 153
DBREF 5ID2 B 1 153 UNP P9WIE3 Y2238_MYCTU 1 153
DBREF 5ID2 C 1 153 UNP P9WIE3 Y2238_MYCTU 1 153
DBREF 5ID2 D 1 153 UNP P9WIE3 Y2238_MYCTU 1 153
SEQADV 5ID2 MET A -10 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 LYS A -9 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 HIS A -8 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 HIS A -7 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 HIS A -6 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 HIS A -5 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 HIS A -4 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 HIS A -3 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 PRO A -2 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 MET A -1 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 VAL A 0 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 MET B -10 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 LYS B -9 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 HIS B -8 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 HIS B -7 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 HIS B -6 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 HIS B -5 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 HIS B -4 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 HIS B -3 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 PRO B -2 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 MET B -1 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 VAL B 0 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 MET C -10 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 LYS C -9 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 HIS C -8 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 HIS C -7 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 HIS C -6 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 HIS C -5 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 HIS C -4 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 HIS C -3 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 PRO C -2 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 MET C -1 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 VAL C 0 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 MET D -10 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 LYS D -9 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 HIS D -8 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 HIS D -7 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 HIS D -6 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 HIS D -5 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 HIS D -4 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 HIS D -3 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 PRO D -2 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 MET D -1 UNP P9WIE3 EXPRESSION TAG
SEQADV 5ID2 VAL D 0 UNP P9WIE3 EXPRESSION TAG
SEQRES 1 A 164 MET LYS HIS HIS HIS HIS HIS HIS PRO MET VAL MET LEU
SEQRES 2 A 164 ASN VAL GLY ALA THR ALA PRO ASP PHE THR LEU ARG ASP
SEQRES 3 A 164 GLN ASN GLN GLN LEU VAL THR LEU ARG GLY TYR ARG GLY
SEQRES 4 A 164 ALA LYS ASN VAL LEU LEU VAL PHE PHE PRO LEU ALA PHE
SEQRES 5 A 164 THR GLY ILE CSO GLN GLY GLU LEU ASP GLN LEU ARG ASP
SEQRES 6 A 164 HIS LEU PRO GLU PHE GLU ASN ASP ASP SER ALA ALA LEU
SEQRES 7 A 164 ALA ILE SER VAL GLY PRO PRO PRO THR HIS LYS ILE TRP
SEQRES 8 A 164 ALA THR GLN SER GLY PHE THR PHE PRO LEU LEU SER ASP
SEQRES 9 A 164 PHE TRP PRO HIS GLY ALA VAL SER GLN ALA TYR GLY VAL
SEQRES 10 A 164 PHE ASN GLU GLN ALA GLY ILE ALA ASN ARG GLY THR PHE
SEQRES 11 A 164 VAL VAL ASP ARG SER GLY ILE ILE ARG PHE ALA GLU MET
SEQRES 12 A 164 LYS GLN PRO GLY GLU VAL ARG ASP GLN ARG LEU TRP THR
SEQRES 13 A 164 ASP ALA LEU ALA ALA LEU THR ALA
SEQRES 1 B 164 MET LYS HIS HIS HIS HIS HIS HIS PRO MET VAL MET LEU
SEQRES 2 B 164 ASN VAL GLY ALA THR ALA PRO ASP PHE THR LEU ARG ASP
SEQRES 3 B 164 GLN ASN GLN GLN LEU VAL THR LEU ARG GLY TYR ARG GLY
SEQRES 4 B 164 ALA LYS ASN VAL LEU LEU VAL PHE PHE PRO LEU ALA PHE
SEQRES 5 B 164 THR GLY ILE CYS GLN GLY GLU LEU ASP GLN LEU ARG ASP
SEQRES 6 B 164 HIS LEU PRO GLU PHE GLU ASN ASP ASP SER ALA ALA LEU
SEQRES 7 B 164 ALA ILE SER VAL GLY PRO PRO PRO THR HIS LYS ILE TRP
SEQRES 8 B 164 ALA THR GLN SER GLY PHE THR PHE PRO LEU LEU SER ASP
SEQRES 9 B 164 PHE TRP PRO HIS GLY ALA VAL SER GLN ALA TYR GLY VAL
SEQRES 10 B 164 PHE ASN GLU GLN ALA GLY ILE ALA ASN ARG GLY THR PHE
SEQRES 11 B 164 VAL VAL ASP ARG SER GLY ILE ILE ARG PHE ALA GLU MET
SEQRES 12 B 164 LYS GLN PRO GLY GLU VAL ARG ASP GLN ARG LEU TRP THR
SEQRES 13 B 164 ASP ALA LEU ALA ALA LEU THR ALA
SEQRES 1 C 164 MET LYS HIS HIS HIS HIS HIS HIS PRO MET VAL MET LEU
SEQRES 2 C 164 ASN VAL GLY ALA THR ALA PRO ASP PHE THR LEU ARG ASP
SEQRES 3 C 164 GLN ASN GLN GLN LEU VAL THR LEU ARG GLY TYR ARG GLY
SEQRES 4 C 164 ALA LYS ASN VAL LEU LEU VAL PHE PHE PRO LEU ALA PHE
SEQRES 5 C 164 THR GLY ILE CYS GLN GLY GLU LEU ASP GLN LEU ARG ASP
SEQRES 6 C 164 HIS LEU PRO GLU PHE GLU ASN ASP ASP SER ALA ALA LEU
SEQRES 7 C 164 ALA ILE SER VAL GLY PRO PRO PRO THR HIS LYS ILE TRP
SEQRES 8 C 164 ALA THR GLN SER GLY PHE THR PHE PRO LEU LEU SER ASP
SEQRES 9 C 164 PHE TRP PRO HIS GLY ALA VAL SER GLN ALA TYR GLY VAL
SEQRES 10 C 164 PHE ASN GLU GLN ALA GLY ILE ALA ASN ARG GLY THR PHE
SEQRES 11 C 164 VAL VAL ASP ARG SER GLY ILE ILE ARG PHE ALA GLU MET
SEQRES 12 C 164 LYS GLN PRO GLY GLU VAL ARG ASP GLN ARG LEU TRP THR
SEQRES 13 C 164 ASP ALA LEU ALA ALA LEU THR ALA
SEQRES 1 D 164 MET LYS HIS HIS HIS HIS HIS HIS PRO MET VAL MET LEU
SEQRES 2 D 164 ASN VAL GLY ALA THR ALA PRO ASP PHE THR LEU ARG ASP
SEQRES 3 D 164 GLN ASN GLN GLN LEU VAL THR LEU ARG GLY TYR ARG GLY
SEQRES 4 D 164 ALA LYS ASN VAL LEU LEU VAL PHE PHE PRO LEU ALA PHE
SEQRES 5 D 164 THR GLY ILE CSO GLN GLY GLU LEU ASP GLN LEU ARG ASP
SEQRES 6 D 164 HIS LEU PRO GLU PHE GLU ASN ASP ASP SER ALA ALA LEU
SEQRES 7 D 164 ALA ILE SER VAL GLY PRO PRO PRO THR HIS LYS ILE TRP
SEQRES 8 D 164 ALA THR GLN SER GLY PHE THR PHE PRO LEU LEU SER ASP
SEQRES 9 D 164 PHE TRP PRO HIS GLY ALA VAL SER GLN ALA TYR GLY VAL
SEQRES 10 D 164 PHE ASN GLU GLN ALA GLY ILE ALA ASN ARG GLY THR PHE
SEQRES 11 D 164 VAL VAL ASP ARG SER GLY ILE ILE ARG PHE ALA GLU MET
SEQRES 12 D 164 LYS GLN PRO GLY GLU VAL ARG ASP GLN ARG LEU TRP THR
SEQRES 13 D 164 ASP ALA LEU ALA ALA LEU THR ALA
MODRES 5ID2 CSO A 45 CYS MODIFIED RESIDUE
MODRES 5ID2 CSO D 45 CYS MODIFIED RESIDUE
HET CSO A 45 7
HET CSO D 45 7
HET GOL A 201 6
HET ACT B 201 4
HET GOL B 202 6
HETNAM CSO S-HYDROXYCYSTEINE
HETNAM GOL GLYCEROL
HETNAM ACT ACETATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 CSO 2(C3 H7 N O3 S)
FORMUL 5 GOL 2(C3 H8 O3)
FORMUL 6 ACT C2 H3 O2 1-
FORMUL 8 HOH *230(H2 O)
HELIX 1 AA1 ARG A 24 ARG A 27 5 4
HELIX 2 AA2 THR A 42 HIS A 55 1 14
HELIX 3 AA3 LEU A 56 PHE A 59 5 4
HELIX 4 AA4 PRO A 73 GLY A 85 1 13
HELIX 5 AA5 GLY A 98 TYR A 104 1 7
HELIX 6 AA6 ASP A 140 ALA A 150 1 11
HELIX 7 AA7 ARG B 24 ARG B 27 5 4
HELIX 8 AA8 THR B 42 HIS B 55 1 14
HELIX 9 AA9 LEU B 56 PHE B 59 5 4
HELIX 10 AB1 PRO B 73 GLY B 85 1 13
HELIX 11 AB2 GLY B 98 TYR B 104 1 7
HELIX 12 AB3 ASP B 140 ALA B 150 1 11
HELIX 13 AB4 ARG C 24 ARG C 27 5 4
HELIX 14 AB5 THR C 42 HIS C 55 1 14
HELIX 15 AB6 LEU C 56 PHE C 59 5 4
HELIX 16 AB7 PRO C 73 GLY C 85 1 13
HELIX 17 AB8 GLY C 98 TYR C 104 1 7
HELIX 18 AB9 ASP C 140 ALA C 150 1 11
HELIX 19 AC1 ARG D 24 ARG D 27 5 4
HELIX 20 AC2 THR D 42 HIS D 55 1 14
HELIX 21 AC3 LEU D 56 PHE D 59 5 4
HELIX 22 AC4 PRO D 73 GLY D 85 1 13
HELIX 23 AC5 GLY D 98 TYR D 104 1 7
HELIX 24 AC6 ASP D 140 ALA D 150 1 11
SHEET 1 AA1 2 THR A 12 ARG A 14 0
SHEET 2 AA1 2 LEU A 20 THR A 22 -1 O VAL A 21 N LEU A 13
SHEET 1 AA2 5 LEU A 90 SER A 92 0
SHEET 2 AA2 5 SER A 64 SER A 70 1 N ALA A 68 O LEU A 91
SHEET 3 AA2 5 ASN A 31 PHE A 36 1 N LEU A 33 O ALA A 65
SHEET 4 AA2 5 ARG A 116 VAL A 121 -1 O PHE A 119 N LEU A 34
SHEET 5 AA2 5 ILE A 127 LYS A 133 -1 O ARG A 128 N VAL A 120
SHEET 1 AA3 2 PHE A 107 ASN A 108 0
SHEET 2 AA3 2 ILE A 113 ALA A 114 -1 O ILE A 113 N ASN A 108
SHEET 1 AA4 2 THR B 12 ARG B 14 0
SHEET 2 AA4 2 LEU B 20 THR B 22 -1 O VAL B 21 N LEU B 13
SHEET 1 AA5 5 LEU B 90 SER B 92 0
SHEET 2 AA5 5 SER B 64 SER B 70 1 N ALA B 68 O LEU B 91
SHEET 3 AA5 5 ASN B 31 PHE B 36 1 N LEU B 33 O ALA B 65
SHEET 4 AA5 5 ARG B 116 VAL B 121 -1 O PHE B 119 N LEU B 34
SHEET 5 AA5 5 ILE B 127 LYS B 133 -1 O ARG B 128 N VAL B 120
SHEET 1 AA6 2 PHE B 107 ASN B 108 0
SHEET 2 AA6 2 ILE B 113 ALA B 114 -1 O ILE B 113 N ASN B 108
SHEET 1 AA7 2 THR C 12 ARG C 14 0
SHEET 2 AA7 2 LEU C 20 THR C 22 -1 O VAL C 21 N LEU C 13
SHEET 1 AA8 5 LEU C 90 SER C 92 0
SHEET 2 AA8 5 SER C 64 SER C 70 1 N ALA C 68 O LEU C 91
SHEET 3 AA8 5 ASN C 31 PHE C 36 1 N LEU C 33 O ALA C 65
SHEET 4 AA8 5 ARG C 116 VAL C 121 -1 O PHE C 119 N LEU C 34
SHEET 5 AA8 5 ILE C 127 LYS C 133 -1 O ARG C 128 N VAL C 120
SHEET 1 AA9 2 PHE C 107 ASN C 108 0
SHEET 2 AA9 2 ILE C 113 ALA C 114 -1 O ILE C 113 N ASN C 108
SHEET 1 AB1 2 THR D 12 ARG D 14 0
SHEET 2 AB1 2 LEU D 20 THR D 22 -1 O VAL D 21 N LEU D 13
SHEET 1 AB2 5 LEU D 90 SER D 92 0
SHEET 2 AB2 5 SER D 64 SER D 70 1 N ALA D 68 O LEU D 91
SHEET 3 AB2 5 ASN D 31 PHE D 36 1 N LEU D 33 O ALA D 65
SHEET 4 AB2 5 GLY D 117 VAL D 121 -1 O PHE D 119 N LEU D 34
SHEET 5 AB2 5 ILE D 127 MET D 132 -1 O ARG D 128 N VAL D 120
SHEET 1 AB3 2 PHE D 107 ASN D 108 0
SHEET 2 AB3 2 ILE D 113 ALA D 114 -1 O ILE D 113 N ASN D 108
LINK C ILE A 44 N CSO A 45 1555 1555 1.33
LINK C CSO A 45 N GLN A 46 1555 1555 1.33
LINK C ILE D 44 N CSO D 45 1555 1555 1.33
LINK C CSO D 45 N GLN D 46 1555 1555 1.33
CISPEP 1 TRP A 95 PRO A 96 0 1.68
CISPEP 2 TRP B 95 PRO B 96 0 2.63
CISPEP 3 TRP C 95 PRO C 96 0 5.12
CISPEP 4 TRP D 95 PRO D 96 0 3.02
SITE 1 AC1 8 LEU A 13 ARG A 14 SER A 92 PHE A 94
SITE 2 AC1 8 TRP A 95 PRO A 96 HOH A 311 HOH A 342
SITE 1 AC2 2 THR B 87 HOH B 307
SITE 1 AC3 8 ASN B 17 GLN B 19 ASN B 108 GLN B 110
SITE 2 AC3 8 ASN B 115 GLN B 134 HOH B 322 HOH B 348
CRYST1 146.906 146.906 33.616 90.00 90.00 90.00 P 42 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 0.006807 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006807 0.000000 0.00000
SCALE3 0.000000 0.000000 0.029748 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
