HEADER TRANSFERASE 11-OCT-05 2C3Q
TITLE HUMAN GLUTATHIONE-S-TRANSFERASE T1-1 W234R MUTANT, COMPLEX WITH S-
TITLE 2 HEXYLGLUTATHIONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTATHIONE S-TRANSFERASE THETA 1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: HUMAN GLUTATHIONE TRANSFERASE T1-1, GST CLASS-THETA 1;
COMPND 5 EC: 2.5.1.18;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: XL1-BLUE
KEYWDS TRANSFERASE, GLUTATHIONE, GLUTATHIONE TRANSFERASE, T1-1, POLYMORPHISM
EXPDTA X-RAY DIFFRACTION
AUTHOR K.TARS,A.-K.LARSSON,A.SHOKEER,B.OLIN,B.MANNERVIK,G.J.KLEYWEGT
REVDAT 6 13-DEC-23 2C3Q 1 REMARK
REVDAT 5 09-OCT-19 2C3Q 1 REMARK
REVDAT 4 15-MAY-19 2C3Q 1 REMARK
REVDAT 3 24-FEB-09 2C3Q 1 VERSN
REVDAT 2 14-DEC-05 2C3Q 1 JRNL
REVDAT 1 30-NOV-05 2C3Q 0
JRNL AUTH K.TARS,A.-K.LARSSON,A.SHOKEER,B.OLIN,B.MANNERVIK,
JRNL AUTH 2 G.J.KLEYWEGT
JRNL TITL STRUCTURAL BASIS OF THE SUPPRESSED CATALYTIC ACTIVITY OF
JRNL TITL 2 WILD-TYPE HUMAN GLUTATHIONE TRANSFERASE T1-1 COMPARED TO ITS
JRNL TITL 3 W234R MUTANT.
JRNL REF J.MOL.BIOL. V. 355 96 2006
JRNL REFN ISSN 0022-2836
JRNL PMID 16298388
JRNL DOI 10.1016/J.JMB.2005.10.049
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.98
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 82135
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) : 0.224
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4328
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5714
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3460
REMARK 3 BIN FREE R VALUE SET COUNT : 315
REMARK 3 BIN FREE R VALUE : 0.3830
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7676
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 135
REMARK 3 SOLVENT ATOMS : 409
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.173
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.151
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.126
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.283
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7964 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10816 ; 1.779 ; 1.994
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 952 ; 3.693 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 340 ;32.956 ;23.647
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1376 ;11.935 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 52 ;12.529 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1224 ; 0.028 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5944 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3876 ; 0.143 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5480 ; 0.285 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 733 ; 0.146 ; 0.500
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): 44 ; 0.108 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 12 ; 0.213 ; 0.500
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): 4849 ; 0.728 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7792 ; 1.278 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3397 ; 2.209 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3024 ; 3.564 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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.
REMARK 4
REMARK 4 2C3Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-OCT-05.
REMARK 100 THE DEPOSITION ID IS D_1290025958.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-SEP-04
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.94
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 82135
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.300
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.5
REMARK 200 DATA REDUNDANCY : 1.800
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.5
REMARK 200 DATA REDUNDANCY IN SHELL : 1.70
REMARK 200 R MERGE FOR SHELL (I) : 0.57000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 2C3N
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING-DROP VAPOR-DIFFUSION
REMARK 280 TECHNIQUE, 5 MICROLITRES OF RESERVOIR SOLUTION [35% (V/V) PEG
REMARK 280 3350, 200 MM MG(NO3)2, 200 MM NAI AND 2 MM DITHIOTHREITOL] WERE
REMARK 280 MIXED WITH 5 MICROLITRES OF PROTEIN SOLUTION (10 MG/ML IN 10 MM
REMARK 280 TRIS-HCL PH 7.8, 15 % GLYCEROL), 1 MICROLITRE 100 MM CACL2 AND 1
REMARK 280 MICROLITRE 20 MM S-HEXYLGLUTATHIONE, PH 8.00, VAPOR DIFFUSION,
REMARK 280 HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 27.24950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 85.52400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.84150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 85.52400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.24950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.84150
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
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: PQS
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, TRP 233 TO ARG
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, TRP 233 TO ARG
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, TRP 233 TO ARG
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, TRP 233 TO ARG
REMARK 400
REMARK 400 THE ENGINEERED RESIDUE IS NUMBERED 234 IN THE COORDINATES
REMARK 400 BELOW.
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 -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 MET B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 MET C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 HIS C -3
REMARK 465 HIS C -2
REMARK 465 HIS C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 MET D -6
REMARK 465 HIS D -5
REMARK 465 HIS D -4
REMARK 465 HIS D -3
REMARK 465 HIS D -2
REMARK 465 HIS D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 2038 O HOH C 2032 3654 2.18
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 GLU A 66 113.65 74.96
REMARK 500 THR A 105 -84.72 -128.92
REMARK 500 VAL A 118 -54.27 -130.59
REMARK 500 PHE A 151 -68.19 -105.31
REMARK 500 GLN A 153 -125.57 48.01
REMARK 500 GLU B 66 119.99 76.72
REMARK 500 TYR B 85 80.65 -155.09
REMARK 500 THR B 105 -84.45 -126.35
REMARK 500 VAL B 118 -55.15 -121.69
REMARK 500 PHE B 151 -66.18 -101.87
REMARK 500 GLN B 153 -118.62 54.64
REMARK 500 GLU C 66 115.29 76.83
REMARK 500 TYR C 85 78.56 -150.83
REMARK 500 THR C 105 -85.13 -124.34
REMARK 500 VAL C 118 -54.82 -123.57
REMARK 500 PHE C 151 -65.47 -105.96
REMARK 500 GLN C 153 -114.54 51.74
REMARK 500 GLU D 66 114.67 77.54
REMARK 500 THR D 105 -88.29 -124.17
REMARK 500 VAL D 118 -57.14 -131.60
REMARK 500 PHE D 151 -63.43 -107.27
REMARK 500 GLN D 153 -124.82 55.92
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2003 DISTANCE = 6.14 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD C 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD C 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD D 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD D 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD D 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD D 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTX A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTX B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTX C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTX D 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2C3N RELATED DB: PDB
REMARK 900 HUMAN GLUTATHIONE-S-TRANSFERASE T1-1, APO FORM
REMARK 900 RELATED ID: 2C3T RELATED DB: PDB
REMARK 900 HUMAN GLUTATHIONE-S-TRANSFERASE T1-1, W234R MUTANT, APO FORM
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 6XHIS TAG ADDED TO THE N-TERMINUS OF PROTEIN. RESIDUE TRP
REMARK 999 234 MUTATED TO ARGININE.
DBREF 2C3Q A -6 1 PDB 2C3Q 2C3Q -6 1
DBREF 2C3Q A 2 240 UNP P30711 GSTT1_HUMAN 1 239
DBREF 2C3Q B -6 1 PDB 2C3Q 2C3Q -6 1
DBREF 2C3Q B 2 240 UNP P30711 GSTT1_HUMAN 1 239
DBREF 2C3Q C -6 1 PDB 2C3Q 2C3Q -6 1
DBREF 2C3Q C 2 240 UNP P30711 GSTT1_HUMAN 1 239
DBREF 2C3Q D -6 1 PDB 2C3Q 2C3Q -6 1
DBREF 2C3Q D 2 240 UNP P30711 GSTT1_HUMAN 1 239
SEQADV 2C3Q ARG A 234 UNP P30711 TRP 233 ENGINEERED MUTATION
SEQADV 2C3Q ARG B 234 UNP P30711 TRP 233 ENGINEERED MUTATION
SEQADV 2C3Q ARG C 234 UNP P30711 TRP 233 ENGINEERED MUTATION
SEQADV 2C3Q ARG D 234 UNP P30711 TRP 233 ENGINEERED MUTATION
SEQRES 1 A 247 MET HIS HIS HIS HIS HIS HIS MET GLY LEU GLU LEU TYR
SEQRES 2 A 247 LEU ASP LEU LEU SER GLN PRO CYS ARG ALA VAL TYR ILE
SEQRES 3 A 247 PHE ALA LYS LYS ASN ASP ILE PRO PHE GLU LEU ARG ILE
SEQRES 4 A 247 VAL ASP LEU ILE LYS GLY GLN HIS LEU SER ASP ALA PHE
SEQRES 5 A 247 ALA GLN VAL ASN PRO LEU LYS LYS VAL PRO ALA LEU LYS
SEQRES 6 A 247 ASP GLY ASP PHE THR LEU THR GLU SER VAL ALA ILE LEU
SEQRES 7 A 247 LEU TYR LEU THR ARG LYS TYR LYS VAL PRO ASP TYR TRP
SEQRES 8 A 247 TYR PRO GLN ASP LEU GLN ALA ARG ALA ARG VAL ASP GLU
SEQRES 9 A 247 TYR LEU ALA TRP GLN HIS THR THR LEU ARG ARG SER CYS
SEQRES 10 A 247 LEU ARG ALA LEU TRP HIS LYS VAL MET PHE PRO VAL PHE
SEQRES 11 A 247 LEU GLY GLU PRO VAL SER PRO GLN THR LEU ALA ALA THR
SEQRES 12 A 247 LEU ALA GLU LEU ASP VAL THR LEU GLN LEU LEU GLU ASP
SEQRES 13 A 247 LYS PHE LEU GLN ASN LYS ALA PHE LEU THR GLY PRO HIS
SEQRES 14 A 247 ILE SER LEU ALA ASP LEU VAL ALA ILE THR GLU LEU MET
SEQRES 15 A 247 HIS PRO VAL GLY ALA GLY CYS GLN VAL PHE GLU GLY ARG
SEQRES 16 A 247 PRO LYS LEU ALA THR TRP ARG GLN ARG VAL GLU ALA ALA
SEQRES 17 A 247 VAL GLY GLU ASP LEU PHE GLN GLU ALA HIS GLU VAL ILE
SEQRES 18 A 247 LEU LYS ALA LYS ASP PHE PRO PRO ALA ASP PRO THR ILE
SEQRES 19 A 247 LYS GLN LYS LEU MET PRO ARG VAL LEU ALA MET ILE ARG
SEQRES 1 B 247 MET HIS HIS HIS HIS HIS HIS MET GLY LEU GLU LEU TYR
SEQRES 2 B 247 LEU ASP LEU LEU SER GLN PRO CYS ARG ALA VAL TYR ILE
SEQRES 3 B 247 PHE ALA LYS LYS ASN ASP ILE PRO PHE GLU LEU ARG ILE
SEQRES 4 B 247 VAL ASP LEU ILE LYS GLY GLN HIS LEU SER ASP ALA PHE
SEQRES 5 B 247 ALA GLN VAL ASN PRO LEU LYS LYS VAL PRO ALA LEU LYS
SEQRES 6 B 247 ASP GLY ASP PHE THR LEU THR GLU SER VAL ALA ILE LEU
SEQRES 7 B 247 LEU TYR LEU THR ARG LYS TYR LYS VAL PRO ASP TYR TRP
SEQRES 8 B 247 TYR PRO GLN ASP LEU GLN ALA ARG ALA ARG VAL ASP GLU
SEQRES 9 B 247 TYR LEU ALA TRP GLN HIS THR THR LEU ARG ARG SER CYS
SEQRES 10 B 247 LEU ARG ALA LEU TRP HIS LYS VAL MET PHE PRO VAL PHE
SEQRES 11 B 247 LEU GLY GLU PRO VAL SER PRO GLN THR LEU ALA ALA THR
SEQRES 12 B 247 LEU ALA GLU LEU ASP VAL THR LEU GLN LEU LEU GLU ASP
SEQRES 13 B 247 LYS PHE LEU GLN ASN LYS ALA PHE LEU THR GLY PRO HIS
SEQRES 14 B 247 ILE SER LEU ALA ASP LEU VAL ALA ILE THR GLU LEU MET
SEQRES 15 B 247 HIS PRO VAL GLY ALA GLY CYS GLN VAL PHE GLU GLY ARG
SEQRES 16 B 247 PRO LYS LEU ALA THR TRP ARG GLN ARG VAL GLU ALA ALA
SEQRES 17 B 247 VAL GLY GLU ASP LEU PHE GLN GLU ALA HIS GLU VAL ILE
SEQRES 18 B 247 LEU LYS ALA LYS ASP PHE PRO PRO ALA ASP PRO THR ILE
SEQRES 19 B 247 LYS GLN LYS LEU MET PRO ARG VAL LEU ALA MET ILE ARG
SEQRES 1 C 247 MET HIS HIS HIS HIS HIS HIS MET GLY LEU GLU LEU TYR
SEQRES 2 C 247 LEU ASP LEU LEU SER GLN PRO CYS ARG ALA VAL TYR ILE
SEQRES 3 C 247 PHE ALA LYS LYS ASN ASP ILE PRO PHE GLU LEU ARG ILE
SEQRES 4 C 247 VAL ASP LEU ILE LYS GLY GLN HIS LEU SER ASP ALA PHE
SEQRES 5 C 247 ALA GLN VAL ASN PRO LEU LYS LYS VAL PRO ALA LEU LYS
SEQRES 6 C 247 ASP GLY ASP PHE THR LEU THR GLU SER VAL ALA ILE LEU
SEQRES 7 C 247 LEU TYR LEU THR ARG LYS TYR LYS VAL PRO ASP TYR TRP
SEQRES 8 C 247 TYR PRO GLN ASP LEU GLN ALA ARG ALA ARG VAL ASP GLU
SEQRES 9 C 247 TYR LEU ALA TRP GLN HIS THR THR LEU ARG ARG SER CYS
SEQRES 10 C 247 LEU ARG ALA LEU TRP HIS LYS VAL MET PHE PRO VAL PHE
SEQRES 11 C 247 LEU GLY GLU PRO VAL SER PRO GLN THR LEU ALA ALA THR
SEQRES 12 C 247 LEU ALA GLU LEU ASP VAL THR LEU GLN LEU LEU GLU ASP
SEQRES 13 C 247 LYS PHE LEU GLN ASN LYS ALA PHE LEU THR GLY PRO HIS
SEQRES 14 C 247 ILE SER LEU ALA ASP LEU VAL ALA ILE THR GLU LEU MET
SEQRES 15 C 247 HIS PRO VAL GLY ALA GLY CYS GLN VAL PHE GLU GLY ARG
SEQRES 16 C 247 PRO LYS LEU ALA THR TRP ARG GLN ARG VAL GLU ALA ALA
SEQRES 17 C 247 VAL GLY GLU ASP LEU PHE GLN GLU ALA HIS GLU VAL ILE
SEQRES 18 C 247 LEU LYS ALA LYS ASP PHE PRO PRO ALA ASP PRO THR ILE
SEQRES 19 C 247 LYS GLN LYS LEU MET PRO ARG VAL LEU ALA MET ILE ARG
SEQRES 1 D 247 MET HIS HIS HIS HIS HIS HIS MET GLY LEU GLU LEU TYR
SEQRES 2 D 247 LEU ASP LEU LEU SER GLN PRO CYS ARG ALA VAL TYR ILE
SEQRES 3 D 247 PHE ALA LYS LYS ASN ASP ILE PRO PHE GLU LEU ARG ILE
SEQRES 4 D 247 VAL ASP LEU ILE LYS GLY GLN HIS LEU SER ASP ALA PHE
SEQRES 5 D 247 ALA GLN VAL ASN PRO LEU LYS LYS VAL PRO ALA LEU LYS
SEQRES 6 D 247 ASP GLY ASP PHE THR LEU THR GLU SER VAL ALA ILE LEU
SEQRES 7 D 247 LEU TYR LEU THR ARG LYS TYR LYS VAL PRO ASP TYR TRP
SEQRES 8 D 247 TYR PRO GLN ASP LEU GLN ALA ARG ALA ARG VAL ASP GLU
SEQRES 9 D 247 TYR LEU ALA TRP GLN HIS THR THR LEU ARG ARG SER CYS
SEQRES 10 D 247 LEU ARG ALA LEU TRP HIS LYS VAL MET PHE PRO VAL PHE
SEQRES 11 D 247 LEU GLY GLU PRO VAL SER PRO GLN THR LEU ALA ALA THR
SEQRES 12 D 247 LEU ALA GLU LEU ASP VAL THR LEU GLN LEU LEU GLU ASP
SEQRES 13 D 247 LYS PHE LEU GLN ASN LYS ALA PHE LEU THR GLY PRO HIS
SEQRES 14 D 247 ILE SER LEU ALA ASP LEU VAL ALA ILE THR GLU LEU MET
SEQRES 15 D 247 HIS PRO VAL GLY ALA GLY CYS GLN VAL PHE GLU GLY ARG
SEQRES 16 D 247 PRO LYS LEU ALA THR TRP ARG GLN ARG VAL GLU ALA ALA
SEQRES 17 D 247 VAL GLY GLU ASP LEU PHE GLN GLU ALA HIS GLU VAL ILE
SEQRES 18 D 247 LEU LYS ALA LYS ASP PHE PRO PRO ALA ASP PRO THR ILE
SEQRES 19 D 247 LYS GLN LYS LEU MET PRO ARG VAL LEU ALA MET ILE ARG
HET GTX A 301 26
HET IOD A 401 1
HET IOD A 402 1
HET IOD A 403 1
HET IOD A 405 1
HET IOD A 406 1
HET IOD A 407 1
HET IOD A 408 1
HET GTX B 301 26
HET IOD B 401 1
HET IOD B 402 1
HET IOD B 403 1
HET IOD B 404 1
HET IOD B 405 1
HET IOD B 406 1
HET IOD B 407 1
HET IOD B 408 1
HET IOD B 409 1
HET GTX C 301 26
HET IOD C 401 1
HET IOD C 402 1
HET IOD C 403 1
HET IOD C 404 1
HET IOD C 405 1
HET IOD C 406 1
HET IOD C 407 1
HET IOD C 408 1
HET GTX D 301 26
HET IOD D 401 1
HET IOD D 402 1
HET IOD D 403 1
HET IOD D 404 1
HET IOD D 405 1
HET IOD D 406 1
HET IOD D 407 1
HETNAM GTX S-HEXYLGLUTATHIONE
HETNAM IOD IODIDE ION
FORMUL 5 GTX 4(C16 H30 N3 O6 S 1+)
FORMUL 6 IOD 31(I 1-)
FORMUL 40 HOH *409(H2 O)
HELIX 1 1 PRO A 13 ASN A 24 1 12
HELIX 2 2 GLY A 38 LEU A 41 5 4
HELIX 3 3 SER A 42 ASN A 49 1 8
HELIX 4 4 GLU A 66 TYR A 78 1 13
HELIX 5 5 GLN A 87 THR A 104 1 18
HELIX 6 6 THR A 105 VAL A 118 1 14
HELIX 7 7 PRO A 121 LEU A 124 5 4
HELIX 8 8 SER A 129 ASP A 149 1 21
HELIX 9 9 ALA A 166 GLY A 181 1 16
HELIX 10 10 LYS A 190 ALA A 201 1 12
HELIX 11 11 GLU A 204 LEU A 215 1 12
HELIX 12 12 ASP A 224 ILE A 239 1 16
HELIX 13 13 PRO B 13 ASN B 24 1 12
HELIX 14 14 GLY B 38 LEU B 41 5 4
HELIX 15 15 SER B 42 ASN B 49 1 8
HELIX 16 16 GLU B 66 TYR B 78 1 13
HELIX 17 17 GLN B 87 THR B 104 1 18
HELIX 18 18 THR B 105 VAL B 118 1 14
HELIX 19 19 PRO B 121 LEU B 124 5 4
HELIX 20 20 SER B 129 ASP B 149 1 21
HELIX 21 21 ALA B 166 GLY B 181 1 16
HELIX 22 22 LYS B 190 ALA B 201 1 12
HELIX 23 23 GLU B 204 LEU B 215 1 12
HELIX 24 24 ASP B 224 ILE B 239 1 16
HELIX 25 25 PRO C 13 ASN C 24 1 12
HELIX 26 26 GLY C 38 LEU C 41 5 4
HELIX 27 27 SER C 42 ASN C 49 1 8
HELIX 28 28 GLU C 66 TYR C 78 1 13
HELIX 29 29 GLN C 87 THR C 104 1 18
HELIX 30 30 THR C 105 VAL C 118 1 14
HELIX 31 31 PRO C 121 LEU C 124 5 4
HELIX 32 32 SER C 129 ASP C 149 1 21
HELIX 33 33 ALA C 166 GLY C 181 1 16
HELIX 34 34 LYS C 190 ALA C 201 1 12
HELIX 35 35 GLU C 204 LEU C 215 1 12
HELIX 36 36 ASP C 224 ILE C 239 1 16
HELIX 37 37 PRO D 13 ASN D 24 1 12
HELIX 38 38 GLY D 38 LEU D 41 5 4
HELIX 39 39 SER D 42 ASN D 49 1 8
HELIX 40 40 GLU D 66 TYR D 78 1 13
HELIX 41 41 GLN D 87 THR D 104 1 18
HELIX 42 42 THR D 105 VAL D 118 1 14
HELIX 43 43 PRO D 121 LEU D 124 5 4
HELIX 44 44 SER D 129 ASP D 149 1 21
HELIX 45 45 ALA D 166 GLY D 181 1 16
HELIX 46 46 LYS D 190 ALA D 201 1 12
HELIX 47 47 GLU D 204 LEU D 215 1 12
HELIX 48 48 ASP D 224 ILE D 239 1 16
SHEET 1 AA 4 GLU A 29 ILE A 32 0
SHEET 2 AA 4 GLY A 2 LEU A 9 1 O LEU A 3 N GLU A 29
SHEET 3 AA 4 VAL A 54 ASP A 59 -1 O ALA A 56 N TYR A 6
SHEET 4 AA 4 ASP A 61 LEU A 64 -1 O PHE A 62 N ASP A 59
SHEET 1 BA 4 GLU B 29 ILE B 32 0
SHEET 2 BA 4 GLY B 2 LEU B 9 1 O LEU B 3 N GLU B 29
SHEET 3 BA 4 VAL B 54 ASP B 59 -1 O ALA B 56 N TYR B 6
SHEET 4 BA 4 ASP B 61 LEU B 64 -1 O PHE B 62 N ASP B 59
SHEET 1 CA 4 GLU C 29 ILE C 32 0
SHEET 2 CA 4 GLY C 2 LEU C 9 1 O LEU C 3 N GLU C 29
SHEET 3 CA 4 VAL C 54 ASP C 59 -1 O ALA C 56 N TYR C 6
SHEET 4 CA 4 ASP C 61 LEU C 64 -1 O PHE C 62 N ASP C 59
SHEET 1 DA 4 GLU D 29 ILE D 32 0
SHEET 2 DA 4 GLY D 2 LEU D 9 1 O LEU D 3 N GLU D 29
SHEET 3 DA 4 VAL D 54 ASP D 59 -1 O ALA D 56 N TYR D 6
SHEET 4 DA 4 ASP D 61 LEU D 64 -1 O PHE D 62 N ASP D 59
CISPEP 1 VAL A 54 PRO A 55 0 0.58
CISPEP 2 VAL B 54 PRO B 55 0 2.76
CISPEP 3 VAL C 54 PRO C 55 0 0.72
CISPEP 4 VAL D 54 PRO D 55 0 0.36
SITE 1 AC1 2 TRP A 115 HIS A 176
SITE 1 AC2 2 TRP A 101 LYS B 53
SITE 1 AC3 1 GLN B 12
SITE 1 AC4 3 TRP B 115 HIS B 176 GTX B 301
SITE 1 AC5 2 HIS A 103 HIS B 103
SITE 1 AC6 1 GLN B 183
SITE 1 AC7 2 ALA B 156 PRO B 161
SITE 1 AC8 2 HOH A2023 TRP B 101
SITE 1 AC9 1 ARG C 107
SITE 1 BC1 2 TRP C 115 HIS C 176
SITE 1 BC2 1 ALA C 156
SITE 1 BC3 1 TRP C 101
SITE 1 BC4 1 ARG D 107
SITE 1 BC5 2 TRP D 115 HIS D 176
SITE 1 BC6 1 GLN D 183
SITE 1 BC7 4 HIS C 103 HOH C2047 HIS D 103 HOH D2053
SITE 1 BC8 1 ALA D 156
SITE 1 BC9 1 TRP D 101
SITE 1 CC1 16 SER A 11 LEU A 35 HIS A 40 LYS A 53
SITE 2 CC1 16 VAL A 54 PRO A 55 GLU A 66 SER A 67
SITE 3 CC1 16 TRP A 115 ARG A 234 MET A 238 HOH A2026
SITE 4 CC1 16 HOH A2054 HOH A2109 HOH A2110 HOH B2048
SITE 1 CC2 15 LEU B 35 HIS B 40 LYS B 53 VAL B 54
SITE 2 CC2 15 PRO B 55 GLU B 66 SER B 67 ARG B 234
SITE 3 CC2 15 MET B 238 IOD B 402 HOH B2025 HOH B2092
SITE 4 CC2 15 HOH B2095 HOH B2096 HOH B2097
SITE 1 CC3 13 PRO C 13 HIS C 40 LYS C 53 VAL C 54
SITE 2 CC3 13 PRO C 55 GLU C 66 SER C 67 ARG C 234
SITE 3 CC3 13 MET C 238 HOH C2051 HOH C2090 HOH C2093
SITE 4 CC3 13 HOH C2094
SITE 1 CC4 15 HOH C2052 SER D 11 HIS D 40 LYS D 53
SITE 2 CC4 15 VAL D 54 PRO D 55 GLU D 66 SER D 67
SITE 3 CC4 15 ARG D 234 MET D 238 HOH D2027 HOH D2032
SITE 4 CC4 15 HOH D2106 HOH D2107 HOH D2108
CRYST1 54.499 109.683 171.048 90.00 90.00 90.00 P 21 21 21 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 0.018349 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009117 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005846 0.00000
MTRIX1 1 -0.995870 0.010010 0.090233 8.84402 1
MTRIX2 1 0.000128 -0.993747 0.111656 -50.31929 1
MTRIX3 1 0.090787 0.111206 0.989642 2.41165 1
MTRIX1 2 0.997826 -0.056849 -0.033324 19.93327 1
MTRIX2 2 -0.060603 -0.990263 -0.125328 -53.89019 1
MTRIX3 2 -0.025875 0.127075 -0.991556 -81.88764 1
MTRIX1 3 -0.996643 0.071320 0.040210 31.40539 1
MTRIX2 3 0.058429 0.963595 -0.260904 -5.71790 1
MTRIX3 3 -0.057353 -0.257679 -0.964527 -91.38487 1
(ATOM LINES ARE NOT SHOWN.)
END