HEADER TRANSFERASE 22-MAY-09 3HJM
TITLE CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE TRANSFERASE PI Y108V MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTATHIONE S-TRANSFERASE P;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: GST CLASS-PI, GSTP1-1;
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 GENE: GSTP1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: TOP10;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PSE420
KEYWDS TRANSFERASE, GLUTATHIONE, DETOXIFICATION, MUTANT, POLYMORPHISM
EXPDTA X-RAY DIFFRACTION
AUTHOR L.J.PARKER
REVDAT 4 01-NOV-23 3HJM 1 REMARK
REVDAT 3 10-NOV-21 3HJM 1 REMARK SEQADV LINK
REVDAT 2 05-JAN-10 3HJM 1 JRNL
REVDAT 1 22-SEP-09 3HJM 0
JRNL AUTH I.QUESADA-SORIANO,L.J.PARKER,A.PRIMAVERA,J.M.CASAS-SOLVAS,
JRNL AUTH 2 A.VARGAS-BERENGUEL,C.BARON,C.J.MORTON,A.P.MAZZETTI,
JRNL AUTH 3 M.LO BELLO,M.W.PARKER,L.GARCIA-FUENTES
JRNL TITL INFLUENCE OF THE H-SITE RESIDUE 108 ON HUMAN GLUTATHIONE
JRNL TITL 2 TRANSFERASE P1-1 LIGAND BINDING: STRUCTURE-THERMODYNAMIC
JRNL TITL 3 RELATIONSHIPS AND THERMAL STABILITY.
JRNL REF PROTEIN SCI. V. 18 2454 2009
JRNL REFN ISSN 0961-8368
JRNL PMID 19780048
JRNL DOI 10.1002/PRO.253
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 54.55
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 53417
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) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2735
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.16
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3245
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.75
REMARK 3 BIN R VALUE (WORKING SET) : 0.2400
REMARK 3 BIN FREE R VALUE SET COUNT : 186
REMARK 3 BIN FREE R VALUE : 0.3200
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6503
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 69
REMARK 3 SOLVENT ATOMS : 621
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.99
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.36
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.25000
REMARK 3 B22 (A**2) : -1.09000
REMARK 3 B33 (A**2) : 2.04000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.16000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.218
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.185
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.135
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.108
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6698 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9085 ; 1.489 ; 1.994
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 832 ; 5.780 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 296 ;32.298 ;24.865
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1134 ;13.993 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 32 ;16.094 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1017 ; 0.096 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5048 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3126 ; 0.197 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4531 ; 0.301 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 570 ; 0.156 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 6 ; 0.117 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 54 ; 0.171 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.116 ; 0.200
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): 4292 ; 0.781 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6626 ; 1.236 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2773 ; 2.033 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2457 ; 3.101 ; 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 3HJM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-MAY-09.
REMARK 100 THE DEPOSITION ID IS D_1000053213.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-AUG-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.4
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 : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : AXCO MIRRORS
REMARK 200 OPTICS : AXCO
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.2.25
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53439
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 54.550
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : 0.11000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.2600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : 0.41000
REMARK 200 R SYM FOR SHELL (I) : 0.41000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
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: PDB ENTRY 3CSI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 270MM CALCIUM ACETATE, 20% PEG8000,
REMARK 280 100MM MES, PH5.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 45.19650
REMARK 290 SMTRY3 2 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: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 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: 3590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 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 PRO A 1
REMARK 465 PRO B 1
REMARK 465 PRO C 1
REMARK 465 PRO D 1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE1 GLN D 209 O HOH D 219 2.17
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 PRO A 9 64.57 -69.83
REMARK 500 GLN A 64 108.00 79.76
REMARK 500 TYR A 79 32.94 -146.64
REMARK 500 ASN A 110 34.68 -149.74
REMARK 500 THR A 141 -104.39 -118.64
REMARK 500 GLN B 64 108.46 85.52
REMARK 500 LEU B 78 54.89 -119.49
REMARK 500 TYR B 79 32.26 -140.66
REMARK 500 ASN B 110 30.46 -154.82
REMARK 500 THR B 141 -103.10 -112.48
REMARK 500 GLN C 64 104.60 87.70
REMARK 500 TYR C 79 28.76 -147.46
REMARK 500 ASN C 110 30.25 -153.68
REMARK 500 THR C 141 -99.28 -123.40
REMARK 500 ARG D 11 -70.72 -70.20
REMARK 500 GLN D 64 113.50 85.94
REMARK 500 TYR D 79 29.00 -141.87
REMARK 500 ASN D 110 46.89 -162.48
REMARK 500 THR D 141 -93.88 -123.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 211 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 77 O
REMARK 620 2 GLN A 147 OE1 148.4
REMARK 620 3 HOH A 219 O 79.5 104.6
REMARK 620 4 HOH A 376 O 68.1 80.4 90.6
REMARK 620 5 HOH A 547 O 75.4 132.3 101.1 138.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 211 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 77 O
REMARK 620 2 GLN B 147 OE1 137.4
REMARK 620 3 HOH B 288 O 88.6 97.9
REMARK 620 4 HOH B 289 O 66.2 72.2 86.2
REMARK 620 5 HOH B 290 O 73.1 146.3 96.8 139.1
REMARK 620 6 HOH B 291 O 144.3 78.1 89.5 149.0 71.8
REMARK 620 7 HOH B 314 O 88.3 83.4 176.5 91.2 83.8 94.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 210 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY C 77 O
REMARK 620 2 GLN C 147 OE1 144.4
REMARK 620 3 HOH C 216 O 77.9 135.5
REMARK 620 4 HOH C 240 O 80.5 101.0 99.9
REMARK 620 5 HOH C 327 O 66.6 78.1 143.1 83.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 211 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 171 OD1
REMARK 620 2 ASP C 171 OD2 48.1
REMARK 620 3 HOH C 615 O 79.1 126.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 211 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY D 77 O
REMARK 620 2 GLN D 147 OE1 145.6
REMARK 620 3 HOH D 243 O 85.9 93.6
REMARK 620 4 HOH D 244 O 72.1 142.3 89.6
REMARK 620 5 HOH D 245 O 90.1 90.4 175.8 88.1
REMARK 620 6 HOH D 246 O 147.9 66.4 92.1 75.9 90.7
REMARK 620 7 HOH D 254 O 64.9 80.8 87.7 137.0 91.7 147.1
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES A 210
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 211
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 A 212
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 213
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B 210
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 211
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 B 212
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 213
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 B 214
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 210
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 211
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 C 212
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES D 210
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 211
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 212
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 D 213
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 214
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3HJO RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GLUTATHIONE TRANSFERASE PI Y108V MUTANT IN
REMARK 900 COMPLEX WITH THE GLUTATHIONE CONJUGATE OF ETHACRYNIC ACID
REMARK 900 RELATED ID: 3HKR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GLUTATHIONE TRANSFERASE PI Y108V MUTANT
DBREF 3HJM A 1 209 UNP P09211 GSTP1_HUMAN 2 210
DBREF 3HJM B 1 209 UNP P09211 GSTP1_HUMAN 2 210
DBREF 3HJM C 1 209 UNP P09211 GSTP1_HUMAN 2 210
DBREF 3HJM D 1 209 UNP P09211 GSTP1_HUMAN 2 210
SEQADV 3HJM VAL A 108 UNP P09211 TYR 109 ENGINEERED MUTATION
SEQADV 3HJM VAL B 108 UNP P09211 TYR 109 ENGINEERED MUTATION
SEQADV 3HJM VAL C 108 UNP P09211 TYR 109 ENGINEERED MUTATION
SEQADV 3HJM VAL D 108 UNP P09211 TYR 109 ENGINEERED MUTATION
SEQRES 1 A 209 PRO PRO TYR THR VAL VAL TYR PHE PRO VAL ARG GLY ARG
SEQRES 2 A 209 CYS ALA ALA LEU ARG MET LEU LEU ALA ASP GLN GLY GLN
SEQRES 3 A 209 SER TRP LYS GLU GLU VAL VAL THR VAL GLU THR TRP GLN
SEQRES 4 A 209 GLU GLY SER LEU LYS ALA SER CYS LEU TYR GLY GLN LEU
SEQRES 5 A 209 PRO LYS PHE GLN ASP GLY ASP LEU THR LEU TYR GLN SER
SEQRES 6 A 209 ASN THR ILE LEU ARG HIS LEU GLY ARG THR LEU GLY LEU
SEQRES 7 A 209 TYR GLY LYS ASP GLN GLN GLU ALA ALA LEU VAL ASP MET
SEQRES 8 A 209 VAL ASN ASP GLY VAL GLU ASP LEU ARG CYS LYS TYR ILE
SEQRES 9 A 209 SER LEU ILE VAL THR ASN TYR GLU ALA GLY LYS ASP ASP
SEQRES 10 A 209 TYR VAL LYS ALA LEU PRO GLY GLN LEU LYS PRO PHE GLU
SEQRES 11 A 209 THR LEU LEU SER GLN ASN GLN GLY GLY LYS THR PHE ILE
SEQRES 12 A 209 VAL GLY ASP GLN ILE SER PHE ALA ASP TYR ASN LEU LEU
SEQRES 13 A 209 ASP LEU LEU LEU ILE HIS GLU VAL LEU ALA PRO GLY CYS
SEQRES 14 A 209 LEU ASP ALA PHE PRO LEU LEU SER ALA TYR VAL GLY ARG
SEQRES 15 A 209 LEU SER ALA ARG PRO LYS LEU LYS ALA PHE LEU ALA SER
SEQRES 16 A 209 PRO GLU TYR VAL ASN LEU PRO ILE ASN GLY ASN GLY LYS
SEQRES 17 A 209 GLN
SEQRES 1 B 209 PRO PRO TYR THR VAL VAL TYR PHE PRO VAL ARG GLY ARG
SEQRES 2 B 209 CYS ALA ALA LEU ARG MET LEU LEU ALA ASP GLN GLY GLN
SEQRES 3 B 209 SER TRP LYS GLU GLU VAL VAL THR VAL GLU THR TRP GLN
SEQRES 4 B 209 GLU GLY SER LEU LYS ALA SER CYS LEU TYR GLY GLN LEU
SEQRES 5 B 209 PRO LYS PHE GLN ASP GLY ASP LEU THR LEU TYR GLN SER
SEQRES 6 B 209 ASN THR ILE LEU ARG HIS LEU GLY ARG THR LEU GLY LEU
SEQRES 7 B 209 TYR GLY LYS ASP GLN GLN GLU ALA ALA LEU VAL ASP MET
SEQRES 8 B 209 VAL ASN ASP GLY VAL GLU ASP LEU ARG CYS LYS TYR ILE
SEQRES 9 B 209 SER LEU ILE VAL THR ASN TYR GLU ALA GLY LYS ASP ASP
SEQRES 10 B 209 TYR VAL LYS ALA LEU PRO GLY GLN LEU LYS PRO PHE GLU
SEQRES 11 B 209 THR LEU LEU SER GLN ASN GLN GLY GLY LYS THR PHE ILE
SEQRES 12 B 209 VAL GLY ASP GLN ILE SER PHE ALA ASP TYR ASN LEU LEU
SEQRES 13 B 209 ASP LEU LEU LEU ILE HIS GLU VAL LEU ALA PRO GLY CYS
SEQRES 14 B 209 LEU ASP ALA PHE PRO LEU LEU SER ALA TYR VAL GLY ARG
SEQRES 15 B 209 LEU SER ALA ARG PRO LYS LEU LYS ALA PHE LEU ALA SER
SEQRES 16 B 209 PRO GLU TYR VAL ASN LEU PRO ILE ASN GLY ASN GLY LYS
SEQRES 17 B 209 GLN
SEQRES 1 C 209 PRO PRO TYR THR VAL VAL TYR PHE PRO VAL ARG GLY ARG
SEQRES 2 C 209 CYS ALA ALA LEU ARG MET LEU LEU ALA ASP GLN GLY GLN
SEQRES 3 C 209 SER TRP LYS GLU GLU VAL VAL THR VAL GLU THR TRP GLN
SEQRES 4 C 209 GLU GLY SER LEU LYS ALA SER CYS LEU TYR GLY GLN LEU
SEQRES 5 C 209 PRO LYS PHE GLN ASP GLY ASP LEU THR LEU TYR GLN SER
SEQRES 6 C 209 ASN THR ILE LEU ARG HIS LEU GLY ARG THR LEU GLY LEU
SEQRES 7 C 209 TYR GLY LYS ASP GLN GLN GLU ALA ALA LEU VAL ASP MET
SEQRES 8 C 209 VAL ASN ASP GLY VAL GLU ASP LEU ARG CYS LYS TYR ILE
SEQRES 9 C 209 SER LEU ILE VAL THR ASN TYR GLU ALA GLY LYS ASP ASP
SEQRES 10 C 209 TYR VAL LYS ALA LEU PRO GLY GLN LEU LYS PRO PHE GLU
SEQRES 11 C 209 THR LEU LEU SER GLN ASN GLN GLY GLY LYS THR PHE ILE
SEQRES 12 C 209 VAL GLY ASP GLN ILE SER PHE ALA ASP TYR ASN LEU LEU
SEQRES 13 C 209 ASP LEU LEU LEU ILE HIS GLU VAL LEU ALA PRO GLY CYS
SEQRES 14 C 209 LEU ASP ALA PHE PRO LEU LEU SER ALA TYR VAL GLY ARG
SEQRES 15 C 209 LEU SER ALA ARG PRO LYS LEU LYS ALA PHE LEU ALA SER
SEQRES 16 C 209 PRO GLU TYR VAL ASN LEU PRO ILE ASN GLY ASN GLY LYS
SEQRES 17 C 209 GLN
SEQRES 1 D 209 PRO PRO TYR THR VAL VAL TYR PHE PRO VAL ARG GLY ARG
SEQRES 2 D 209 CYS ALA ALA LEU ARG MET LEU LEU ALA ASP GLN GLY GLN
SEQRES 3 D 209 SER TRP LYS GLU GLU VAL VAL THR VAL GLU THR TRP GLN
SEQRES 4 D 209 GLU GLY SER LEU LYS ALA SER CYS LEU TYR GLY GLN LEU
SEQRES 5 D 209 PRO LYS PHE GLN ASP GLY ASP LEU THR LEU TYR GLN SER
SEQRES 6 D 209 ASN THR ILE LEU ARG HIS LEU GLY ARG THR LEU GLY LEU
SEQRES 7 D 209 TYR GLY LYS ASP GLN GLN GLU ALA ALA LEU VAL ASP MET
SEQRES 8 D 209 VAL ASN ASP GLY VAL GLU ASP LEU ARG CYS LYS TYR ILE
SEQRES 9 D 209 SER LEU ILE VAL THR ASN TYR GLU ALA GLY LYS ASP ASP
SEQRES 10 D 209 TYR VAL LYS ALA LEU PRO GLY GLN LEU LYS PRO PHE GLU
SEQRES 11 D 209 THR LEU LEU SER GLN ASN GLN GLY GLY LYS THR PHE ILE
SEQRES 12 D 209 VAL GLY ASP GLN ILE SER PHE ALA ASP TYR ASN LEU LEU
SEQRES 13 D 209 ASP LEU LEU LEU ILE HIS GLU VAL LEU ALA PRO GLY CYS
SEQRES 14 D 209 LEU ASP ALA PHE PRO LEU LEU SER ALA TYR VAL GLY ARG
SEQRES 15 D 209 LEU SER ALA ARG PRO LYS LEU LYS ALA PHE LEU ALA SER
SEQRES 16 D 209 PRO GLU TYR VAL ASN LEU PRO ILE ASN GLY ASN GLY LYS
SEQRES 17 D 209 GLN
HET MES A 210 12
HET CA A 211 1
HET CO3 A 212 4
HET CL A 213 1
HET MES B 210 12
HET CA B 211 1
HET CO3 B 212 4
HET CL B 213 1
HET CO3 B 214 4
HET CA C 210 1
HET CA C 211 1
HET CO3 C 212 4
HET MES D 210 12
HET CA D 211 1
HET PO4 D 212 5
HET CO3 D 213 4
HET CL D 214 1
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM CA CALCIUM ION
HETNAM CO3 CARBONATE ION
HETNAM CL CHLORIDE ION
HETNAM PO4 PHOSPHATE ION
FORMUL 5 MES 3(C6 H13 N O4 S)
FORMUL 6 CA 5(CA 2+)
FORMUL 7 CO3 5(C O3 2-)
FORMUL 8 CL 3(CL 1-)
FORMUL 19 PO4 O4 P 3-
FORMUL 22 HOH *621(H2 O)
HELIX 1 1 ARG A 11 ARG A 13 5 3
HELIX 2 2 CYS A 14 GLN A 24 1 11
HELIX 3 3 THR A 34 GLY A 41 1 8
HELIX 4 4 GLY A 41 CYS A 47 1 7
HELIX 5 5 GLN A 64 GLY A 77 1 14
HELIX 6 6 ASP A 82 ASN A 110 1 29
HELIX 7 7 ASN A 110 ASN A 136 1 27
HELIX 8 8 GLN A 137 LYS A 140 5 4
HELIX 9 9 SER A 149 ALA A 166 1 18
HELIX 10 10 PHE A 173 ALA A 185 1 13
HELIX 11 11 ARG A 186 SER A 195 1 10
HELIX 12 12 SER A 195 ASN A 200 1 6
HELIX 13 13 ARG B 11 ARG B 13 5 3
HELIX 14 14 CYS B 14 GLN B 24 1 11
HELIX 15 15 THR B 34 GLY B 41 1 8
HELIX 16 16 GLY B 41 CYS B 47 1 7
HELIX 17 17 GLN B 64 GLY B 77 1 14
HELIX 18 18 ASP B 82 ASN B 110 1 29
HELIX 19 19 ASN B 110 GLN B 135 1 26
HELIX 20 20 ASN B 136 LYS B 140 5 5
HELIX 21 21 SER B 149 ALA B 166 1 18
HELIX 22 22 PHE B 173 ALA B 185 1 13
HELIX 23 23 ARG B 186 SER B 195 1 10
HELIX 24 24 SER B 195 ASN B 200 1 6
HELIX 25 25 ARG C 11 ARG C 13 5 3
HELIX 26 26 CYS C 14 GLN C 24 1 11
HELIX 27 27 THR C 34 GLY C 41 1 8
HELIX 28 28 GLY C 41 SER C 46 1 6
HELIX 29 29 GLN C 64 GLY C 77 1 14
HELIX 30 30 ASP C 82 ASN C 110 1 29
HELIX 31 31 ASN C 110 GLN C 135 1 26
HELIX 32 32 ASN C 136 LYS C 140 5 5
HELIX 33 33 SER C 149 ALA C 166 1 18
HELIX 34 34 GLY C 168 ALA C 172 5 5
HELIX 35 35 PHE C 173 ALA C 185 1 13
HELIX 36 36 ARG C 186 SER C 195 1 10
HELIX 37 37 SER C 195 ASN C 200 1 6
HELIX 38 38 ARG D 11 ARG D 13 5 3
HELIX 39 39 CYS D 14 GLN D 24 1 11
HELIX 40 40 THR D 34 GLY D 41 1 8
HELIX 41 41 GLY D 41 CYS D 47 1 7
HELIX 42 42 GLN D 64 GLY D 77 1 14
HELIX 43 43 ASP D 82 ASN D 110 1 29
HELIX 44 44 ASN D 110 GLN D 135 1 26
HELIX 45 45 ASN D 136 LYS D 140 5 5
HELIX 46 46 SER D 149 ALA D 166 1 18
HELIX 47 47 PHE D 173 ALA D 185 1 13
HELIX 48 48 ARG D 186 SER D 195 1 10
HELIX 49 49 SER D 195 ASN D 200 1 6
SHEET 1 A 4 LYS A 29 VAL A 32 0
SHEET 2 A 4 TYR A 3 TYR A 7 1 N VAL A 5 O GLU A 31
SHEET 3 A 4 LYS A 54 ASP A 57 -1 O LYS A 54 N VAL A 6
SHEET 4 A 4 LEU A 60 TYR A 63 -1 O LEU A 62 N PHE A 55
SHEET 1 B 4 TRP B 28 VAL B 32 0
SHEET 2 B 4 TYR B 3 TYR B 7 1 N VAL B 5 O LYS B 29
SHEET 3 B 4 LYS B 54 ASP B 57 -1 O LYS B 54 N VAL B 6
SHEET 4 B 4 LEU B 60 TYR B 63 -1 O LEU B 60 N ASP B 57
SHEET 1 C 4 LYS C 29 VAL C 32 0
SHEET 2 C 4 TYR C 3 TYR C 7 1 N VAL C 5 O GLU C 31
SHEET 3 C 4 LYS C 54 ASP C 57 -1 O LYS C 54 N VAL C 6
SHEET 4 C 4 LEU C 60 TYR C 63 -1 O LEU C 62 N PHE C 55
SHEET 1 D 4 TRP D 28 VAL D 32 0
SHEET 2 D 4 TYR D 3 TYR D 7 1 N VAL D 5 O GLU D 31
SHEET 3 D 4 LYS D 54 ASP D 57 -1 O LYS D 54 N VAL D 6
SHEET 4 D 4 LEU D 60 TYR D 63 -1 O LEU D 62 N PHE D 55
LINK O GLY A 77 CA CA A 211 1555 1555 2.45
LINK OE1 GLN A 147 CA CA A 211 1555 1555 2.63
LINK CA CA A 211 O HOH A 219 1555 1555 2.25
LINK CA CA A 211 O HOH A 376 1555 1555 2.62
LINK CA CA A 211 O HOH A 547 1555 1555 2.69
LINK O GLY B 77 CA CA B 211 1555 1555 2.51
LINK OE1 GLN B 147 CA CA B 211 1555 1555 2.49
LINK CA CA B 211 O HOH B 288 1555 1555 2.23
LINK CA CA B 211 O HOH B 289 1555 1555 2.73
LINK CA CA B 211 O HOH B 290 1555 1555 2.61
LINK CA CA B 211 O HOH B 291 1555 1555 2.48
LINK CA CA B 211 O HOH B 314 1555 1555 2.57
LINK O GLY C 77 CA CA C 210 1555 1555 2.51
LINK OE1 GLN C 147 CA CA C 210 1555 1555 2.51
LINK OD1 ASP C 171 CA CA C 211 1555 1555 2.57
LINK OD2 ASP C 171 CA CA C 211 1555 1555 2.82
LINK CA CA C 210 O HOH C 216 1555 1555 2.57
LINK CA CA C 210 O HOH C 240 1555 1555 2.38
LINK CA CA C 210 O HOH C 327 1555 1555 2.67
LINK CA CA C 211 O HOH C 615 1555 1555 2.30
LINK O GLY D 77 CA CA D 211 1555 1555 2.43
LINK OE1 GLN D 147 CA CA D 211 1555 1555 2.41
LINK CA CA D 211 O HOH D 243 1555 1555 2.37
LINK CA CA D 211 O HOH D 244 1555 1555 2.64
LINK CA CA D 211 O HOH D 245 1555 1555 2.65
LINK CA CA D 211 O HOH D 246 1555 1555 2.67
LINK CA CA D 211 O HOH D 254 1555 1555 2.66
CISPEP 1 LEU A 52 PRO A 53 0 0.16
CISPEP 2 LEU B 52 PRO B 53 0 2.83
CISPEP 3 LEU C 52 PRO C 53 0 -2.63
CISPEP 4 LEU D 52 PRO D 53 0 2.47
SITE 1 AC1 4 ALA A 22 TRP A 28 GLU A 197 HOH A 247
SITE 1 AC2 5 GLY A 77 GLN A 147 HOH A 219 HOH A 376
SITE 2 AC2 5 HOH A 547
SITE 1 AC3 8 ARG A 13 GLN A 51 PRO A 53 GLN A 64
SITE 2 AC3 8 SER A 65 HOH A 276 HOH A 450 HOH A 549
SITE 1 AC4 3 ASP A 98 GLN B 64 HOH B 241
SITE 1 AC5 5 TRP B 28 GLU B 30 PHE B 192 GLU B 197
SITE 2 AC5 5 HOH B 282
SITE 1 AC6 7 GLY B 77 GLN B 147 HOH B 288 HOH B 289
SITE 2 AC6 7 HOH B 290 HOH B 291 HOH B 314
SITE 1 AC7 7 ARG B 13 PRO B 53 GLN B 64 SER B 65
SITE 2 AC7 7 HOH B 235 HOH B 241 HOH B 245
SITE 1 AC8 4 GLN A 64 HOH A 549 ASP B 98 HOH B 584
SITE 1 AC9 4 GLN B 147 ILE B 148 ARG B 186 HOH B 371
SITE 1 BC1 5 GLY C 77 GLN C 147 HOH C 216 HOH C 240
SITE 2 BC1 5 HOH C 327
SITE 1 BC2 2 ASP C 171 HOH C 615
SITE 1 BC3 7 ARG C 13 PRO C 53 GLN C 64 SER C 65
SITE 2 BC3 7 HOH C 238 HOH C 263 HOH C 574
SITE 1 BC4 4 ALA D 22 TRP D 28 GLU D 30 GLU D 197
SITE 1 BC5 7 GLY D 77 GLN D 147 HOH D 243 HOH D 244
SITE 2 BC5 7 HOH D 245 HOH D 246 HOH D 254
SITE 1 BC6 2 ASP D 171 HOH D 477
SITE 1 BC7 5 PHE D 142 GLN D 147 ILE D 148 ARG D 186
SITE 2 BC7 5 HOH D 354
SITE 1 BC8 3 GLN C 64 HOH C 574 ASP D 98
CRYST1 69.002 90.393 75.981 90.00 97.49 90.00 P 1 21 1 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 0.014492 0.000000 0.001906 0.00000
SCALE2 0.000000 0.011063 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013274 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
