HEADER TRANSFERASE 21-OCT-11 3UAP
TITLE CRYSTAL STRUCTURE OF GLUTATHIONE TRANSFERASE (TARGET EFI-501774) FROM
TITLE 2 METHYLOCOCCUS CAPSULATUS STR. BATH
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTATHIONE S-TRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.5.1.18;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHYLOCOCCUS CAPSULATUS;
SOURCE 3 ORGANISM_TAXID: 243233;
SOURCE 4 STRAIN: NCIMB 11132 / BATH;
SOURCE 5 ATCC: 33009;
SOURCE 6 GENE: GST, MCA0074;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
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: PET
KEYWDS TRANSFERASE, GSH BINDING SITE, STRUCTURAL GENOMICS
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.PATSKOVSKY,R.TORO,R.BHOSLE,W.D.ZENCHECK,B.HILLERICH,R.D.SEIDEL,
AUTHOR 2 E.WASHINGTON,A.SCOTT GLENN,S.CHOWDHURY,B.EVANS,J.HAMMONDS,H.J.IMKER,
AUTHOR 3 R.N.ARMSTRONG,J.A.GERLT,S.C.ALMO,ENZYME FUNCTION INITIATIVE (EFI)
REVDAT 4 13-SEP-23 3UAP 1 REMARK SEQADV
REVDAT 3 24-JAN-18 3UAP 1 AUTHOR
REVDAT 2 29-FEB-12 3UAP 1 AUTHOR JRNL
REVDAT 1 02-NOV-11 3UAP 0
JRNL AUTH Y.PATSKOVSKY,R.TORO,R.BHOSLE,W.D.ZENCHECK,B.HILLERICH,
JRNL AUTH 2 R.D.SEIDEL,E.WASHINGTON,A.SCOTT GLENN,S.CHOWDHURY,B.EVANS,
JRNL AUTH 3 J.HAMMONDS,H.J.IMKER,R.N.ARMSTRONG,J.A.GERLT,S.C.ALMO
JRNL TITL CRYSTAL STRUCTURE OF GLUTATHIONE S-TRANSFERASE FROM
JRNL TITL 2 METHYLOCOCCUS CAPSULATUS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.08
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 9260
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) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.900
REMARK 3 FREE R VALUE TEST SET COUNT : 281
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 670
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3540
REMARK 3 BIN FREE R VALUE SET COUNT : 19
REMARK 3 BIN FREE R VALUE : 0.4250
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1607
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 3
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 114.9
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 102.5
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.308
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.225
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.375
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1662 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2258 ; 1.050 ; 1.987
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 204 ; 4.789 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 74 ;36.623 ;23.784
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 278 ;17.629 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;16.097 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 244 ; 0.058 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1266 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 1014 ; 2.856 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1626 ; 5.401 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 648 ; 7.555 ; 4.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 631 ;11.787 ; 6.000
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 : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.00
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 3UAP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-OCT-11.
REMARK 100 THE DEPOSITION ID IS D_1000068517.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-OCT-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.075
REMARK 200 MONOCHROMATOR : NULL
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 : 10645
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -5.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 11.90
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 11.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MR
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2DSA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM CHLORIDE, 0.1M TRIS-HCL,
REMARK 280 30% PEG3000, PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 3 2
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 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
REMARK 290 13555 Y+1/4,X+3/4,-Z+3/4
REMARK 290 14555 -Y+1/4,-X+1/4,-Z+1/4
REMARK 290 15555 Y+3/4,-X+3/4,Z+1/4
REMARK 290 16555 -Y+3/4,X+1/4,Z+3/4
REMARK 290 17555 X+1/4,Z+3/4,-Y+3/4
REMARK 290 18555 -X+3/4,Z+1/4,Y+3/4
REMARK 290 19555 -X+1/4,-Z+1/4,-Y+1/4
REMARK 290 20555 X+3/4,-Z+3/4,Y+1/4
REMARK 290 21555 Z+1/4,Y+3/4,-X+3/4
REMARK 290 22555 Z+3/4,-Y+3/4,X+1/4
REMARK 290 23555 -Z+3/4,Y+1/4,X+3/4
REMARK 290 24555 -Z+1/4,-Y+1/4,-X+1/4
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 64.62300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 64.62300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 64.62300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 64.62300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 64.62300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 64.62300
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 64.62300
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 64.62300
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 64.62300
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 64.62300
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 64.62300
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 64.62300
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 64.62300
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 64.62300
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 64.62300
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 64.62300
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 64.62300
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 64.62300
REMARK 290 SMTRY1 13 0.000000 1.000000 0.000000 32.31150
REMARK 290 SMTRY2 13 1.000000 0.000000 0.000000 96.93450
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 96.93450
REMARK 290 SMTRY1 14 0.000000 -1.000000 0.000000 32.31150
REMARK 290 SMTRY2 14 -1.000000 0.000000 0.000000 32.31150
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 32.31150
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 96.93450
REMARK 290 SMTRY2 15 -1.000000 0.000000 0.000000 96.93450
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 32.31150
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 96.93450
REMARK 290 SMTRY2 16 1.000000 0.000000 0.000000 32.31150
REMARK 290 SMTRY3 16 0.000000 0.000000 1.000000 96.93450
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 32.31150
REMARK 290 SMTRY2 17 0.000000 0.000000 1.000000 96.93450
REMARK 290 SMTRY3 17 0.000000 -1.000000 0.000000 96.93450
REMARK 290 SMTRY1 18 -1.000000 0.000000 0.000000 96.93450
REMARK 290 SMTRY2 18 0.000000 0.000000 1.000000 32.31150
REMARK 290 SMTRY3 18 0.000000 1.000000 0.000000 96.93450
REMARK 290 SMTRY1 19 -1.000000 0.000000 0.000000 32.31150
REMARK 290 SMTRY2 19 0.000000 0.000000 -1.000000 32.31150
REMARK 290 SMTRY3 19 0.000000 -1.000000 0.000000 32.31150
REMARK 290 SMTRY1 20 1.000000 0.000000 0.000000 96.93450
REMARK 290 SMTRY2 20 0.000000 0.000000 -1.000000 96.93450
REMARK 290 SMTRY3 20 0.000000 1.000000 0.000000 32.31150
REMARK 290 SMTRY1 21 0.000000 0.000000 1.000000 32.31150
REMARK 290 SMTRY2 21 0.000000 1.000000 0.000000 96.93450
REMARK 290 SMTRY3 21 -1.000000 0.000000 0.000000 96.93450
REMARK 290 SMTRY1 22 0.000000 0.000000 1.000000 96.93450
REMARK 290 SMTRY2 22 0.000000 -1.000000 0.000000 96.93450
REMARK 290 SMTRY3 22 1.000000 0.000000 0.000000 32.31150
REMARK 290 SMTRY1 23 0.000000 0.000000 -1.000000 96.93450
REMARK 290 SMTRY2 23 0.000000 1.000000 0.000000 32.31150
REMARK 290 SMTRY3 23 1.000000 0.000000 0.000000 96.93450
REMARK 290 SMTRY1 24 0.000000 0.000000 -1.000000 32.31150
REMARK 290 SMTRY2 24 0.000000 -1.000000 0.000000 32.31150
REMARK 290 SMTRY3 24 -1.000000 0.000000 0.000000 32.31150
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 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: 3610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 BIOMT1 2 -1.000000 0.000000 0.000000 -32.31150
REMARK 350 BIOMT2 2 0.000000 0.000000 1.000000 32.31150
REMARK 350 BIOMT3 2 0.000000 1.000000 0.000000 -32.31150
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 -1
REMARK 465 GLN A 203
REMARK 465 ALA A 204
REMARK 465 GLU A 205
REMARK 465 ASN A 206
REMARK 465 LEU A 207
REMARK 465 TYR A 208
REMARK 465 PHE A 209
REMARK 465 GLN A 210
REMARK 465 SER A 211
REMARK 465 HIS A 212
REMARK 465 HIS A 213
REMARK 465 HIS A 214
REMARK 465 HIS A 215
REMARK 465 HIS A 216
REMARK 465 HIS A 217
REMARK 465 TRP A 218
REMARK 465 SER A 219
REMARK 465 HIS A 220
REMARK 465 PRO A 221
REMARK 465 GLN A 222
REMARK 465 PHE A 223
REMARK 465 GLU A 224
REMARK 465 LYS A 225
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 VAL A 46 -72.34 -65.07
REMARK 500 ASP A 59 4.53 -59.60
REMARK 500 GLU A 65 103.10 84.21
REMARK 500 MET A 83 135.54 -170.15
REMARK 500 PRO A 118 177.61 -44.83
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 226
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3UAR RELATED DB: PDB
REMARK 900 RELATED ID: EFI-501774 RELATED DB: TARGETTRACK
DBREF 3UAP A 1 203 UNP Q60CN1 Q60CN1_METCA 1 203
SEQADV 3UAP MET A -1 UNP Q60CN1 EXPRESSION TAG
SEQADV 3UAP VAL A 0 UNP Q60CN1 EXPRESSION TAG
SEQADV 3UAP ALA A 204 UNP Q60CN1 EXPRESSION TAG
SEQADV 3UAP GLU A 205 UNP Q60CN1 EXPRESSION TAG
SEQADV 3UAP ASN A 206 UNP Q60CN1 EXPRESSION TAG
SEQADV 3UAP LEU A 207 UNP Q60CN1 EXPRESSION TAG
SEQADV 3UAP TYR A 208 UNP Q60CN1 EXPRESSION TAG
SEQADV 3UAP PHE A 209 UNP Q60CN1 EXPRESSION TAG
SEQADV 3UAP GLN A 210 UNP Q60CN1 EXPRESSION TAG
SEQADV 3UAP SER A 211 UNP Q60CN1 EXPRESSION TAG
SEQADV 3UAP HIS A 212 UNP Q60CN1 EXPRESSION TAG
SEQADV 3UAP HIS A 213 UNP Q60CN1 EXPRESSION TAG
SEQADV 3UAP HIS A 214 UNP Q60CN1 EXPRESSION TAG
SEQADV 3UAP HIS A 215 UNP Q60CN1 EXPRESSION TAG
SEQADV 3UAP HIS A 216 UNP Q60CN1 EXPRESSION TAG
SEQADV 3UAP HIS A 217 UNP Q60CN1 EXPRESSION TAG
SEQADV 3UAP TRP A 218 UNP Q60CN1 EXPRESSION TAG
SEQADV 3UAP SER A 219 UNP Q60CN1 EXPRESSION TAG
SEQADV 3UAP HIS A 220 UNP Q60CN1 EXPRESSION TAG
SEQADV 3UAP PRO A 221 UNP Q60CN1 EXPRESSION TAG
SEQADV 3UAP GLN A 222 UNP Q60CN1 EXPRESSION TAG
SEQADV 3UAP PHE A 223 UNP Q60CN1 EXPRESSION TAG
SEQADV 3UAP GLU A 224 UNP Q60CN1 EXPRESSION TAG
SEQADV 3UAP LYS A 225 UNP Q60CN1 EXPRESSION TAG
SEQRES 1 A 227 MET VAL MET LYS LEU TYR TYR PHE PRO GLY ALA CYS SER
SEQRES 2 A 227 LEU ALA PRO HIS ILE VAL LEU ARG GLU ALA GLY LEU ASP
SEQRES 3 A 227 PHE GLU LEU GLU ASN VAL ASP LEU GLY THR LYS LYS THR
SEQRES 4 A 227 GLY SER GLY ALA ASP PHE LEU GLN VAL ASN PRO LYS GLY
SEQRES 5 A 227 TYR VAL PRO ALA LEU GLN LEU ASP ASP GLY GLN VAL LEU
SEQRES 6 A 227 THR GLU ASP GLN VAL ILE LEU GLN TYR LEU ALA ASP LEU
SEQRES 7 A 227 LYS PRO GLU SER GLY LEU MET PRO PRO SER GLY THR PHE
SEQRES 8 A 227 GLU ARG TYR ARG LEU LEU GLU TRP LEU ALA PHE ILE SER
SEQRES 9 A 227 THR GLU ILE HIS LYS THR PHE GLY PRO PHE TRP ASN PRO
SEQRES 10 A 227 GLU SER PRO GLU ALA SER LYS GLN ILE ALA LEU GLY LEU
SEQRES 11 A 227 LEU SER ARG ARG LEU ASP TYR VAL GLU ASP ARG LEU GLU
SEQRES 12 A 227 ALA GLY GLY PRO TRP LEU MET GLY ASP ARG TYR SER VAL
SEQRES 13 A 227 ALA ASP ALA TYR LEU SER THR VAL LEU GLY TRP CYS GLU
SEQRES 14 A 227 TYR LEU LYS ILE ASP LEU SER LYS TRP PRO ARG ILE LEU
SEQRES 15 A 227 ALA TYR LEU GLU ARG ASN GLN ALA ARG PRO ALA VAL GLN
SEQRES 16 A 227 ALA ALA MET LYS ALA GLU GLY LEU ILE GLN ALA GLU ASN
SEQRES 17 A 227 LEU TYR PHE GLN SER HIS HIS HIS HIS HIS HIS TRP SER
SEQRES 18 A 227 HIS PRO GLN PHE GLU LYS
HET GOL A 226 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL C3 H8 O3
FORMUL 3 HOH *3(H2 O)
HELIX 1 1 SER A 11 ALA A 21 1 11
HELIX 2 2 ASP A 42 ASN A 47 1 6
HELIX 3 3 GLU A 65 LYS A 77 1 13
HELIX 4 4 PRO A 78 GLY A 81 5 4
HELIX 5 5 PHE A 89 ILE A 105 1 17
HELIX 6 6 HIS A 106 ASN A 114 5 9
HELIX 7 7 PRO A 118 GLY A 143 1 26
HELIX 8 8 SER A 153 GLY A 164 1 12
HELIX 9 9 GLY A 164 LEU A 169 1 6
HELIX 10 10 TRP A 176 ALA A 188 1 13
HELIX 11 11 ARG A 189 GLU A 199 1 11
SHEET 1 A 5 LYS A 36 THR A 37 0
SHEET 2 A 5 PHE A 25 ASP A 31 -1 N ASP A 31 O LYS A 36
SHEET 3 A 5 MET A 1 TYR A 5 1 N LEU A 3 O GLU A 28
SHEET 4 A 5 ALA A 54 GLN A 56 -1 O GLN A 56 N LYS A 2
SHEET 5 A 5 VAL A 62 THR A 64 -1 O LEU A 63 N LEU A 55
CISPEP 1 VAL A 52 PRO A 53 0 11.34
SITE 1 AC1 4 LYS A 49 GLU A 96 TRP A 97 TYR A 135
CRYST1 129.246 129.246 129.246 90.00 90.00 90.00 P 43 3 2 24
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 0.007737 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007737 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007737 0.00000
(ATOM LINES ARE NOT SHOWN.)
END