HEADER TRANSFERASE 04-DEC-10 3PUG
TITLE HALOFERAX VOLCANII MALATE SYNTHASE NATIVE AT 3MM GLYOXYLATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MALATE SYNTHASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.3.3.9
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HALOFERAX VOLCANII;
SOURCE 3 ORGANISM_TAXID: 309800;
SOURCE 4 STRAIN: ATCC 29605, DS2;
SOURCE 5 OTHER_DETAILS: ATCC
KEYWDS TIM BARREL, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.R.HOWARD,C.D.BRACKEN,A.M.NEIGHBOR,G.C.THOMAS,K.K.LAMLENN,
AUTHOR 2 H.L.SCHUBERT,F.G.WHITBY
REVDAT 3 21-FEB-24 3PUG 1 REMARK HETSYN LINK
REVDAT 2 08-NOV-17 3PUG 1 REMARK
REVDAT 1 01-JUN-11 3PUG 0
JRNL AUTH C.D.BRACKEN,A.M.NEIGHBOR,K.K.LAMLENN,G.C.THOMAS,
JRNL AUTH 2 H.L.SCHUBERT,F.G.WHITBY,B.R.HOWARD
JRNL TITL CRYSTAL STRUCTURES OF A HALOPHILIC ARCHAEAL MALATE SYNTHASE
JRNL TITL 2 FROM HALOFERAX VOLCANII AND COMPARISONS WITH ISOFORMS A AND
JRNL TITL 3 G.
JRNL REF BMC STRUCT.BIOL. V. 11 23 2011
JRNL REFN ESSN 1472-6807
JRNL PMID 21569248
JRNL DOI 10.1186/1472-6807-11-23
REMARK 2
REMARK 2 RESOLUTION. 2.70 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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 18194
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) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 935
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1189
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.32
REMARK 3 BIN R VALUE (WORKING SET) : 0.2500
REMARK 3 BIN FREE R VALUE SET COUNT : 57
REMARK 3 BIN FREE R VALUE : 0.2930
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2747
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 71
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 58.34
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.36000
REMARK 3 B22 (A**2) : 1.36000
REMARK 3 B33 (A**2) : -2.04000
REMARK 3 B12 (A**2) : 0.68000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.294
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.192
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.058
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.931
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.868
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2824 ; 0.014 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3831 ; 2.273 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 349 ; 7.497 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 151 ;35.733 ;24.570
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 462 ;19.552 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 23 ;14.931 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 404 ; 0.135 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2230 ; 0.012 ; 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): 1739 ; 1.247 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2800 ; 2.310 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1085 ; 3.563 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1029 ; 5.516 ; 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 : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3PUG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-DEC-10.
REMARK 100 THE DEPOSITION ID IS D_1000062825.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-MAR-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.4
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) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : R-AXIS IV, CONFOCAL OPTICS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18255
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.6000
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) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : 0.38300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SIRAS
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: SOLVE 2.13, RESOLVE 2.13
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4500, GLYCEROL, 2M KCL,13 MM
REMARK 280 MGCL2, 3MM GLYOXYLATE, PH 4.4, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 78.18500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 45.14013
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 47.15167
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 78.18500
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 45.14013
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 47.15167
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 78.18500
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 45.14013
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 47.15167
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 78.18500
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 45.14013
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 47.15167
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 78.18500
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 45.14013
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 47.15167
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 78.18500
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 45.14013
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 47.15167
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 90.28026
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 94.30333
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 90.28026
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 94.30333
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 90.28026
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 94.30333
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 90.28026
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 94.30333
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 90.28026
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 94.30333
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 90.28026
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 94.30333
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -161.0 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 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 43070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 74620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -360.0 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 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 4 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 141.45500
REMARK 350 BIOMT1 5 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 0.000000 -1.000000 141.45500
REMARK 350 BIOMT1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 6 0.000000 0.000000 -1.000000 141.45500
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 CL CL A 704 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 472 LIES ON A SPECIAL POSITION.
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 GLY A 23
REMARK 465 GLU A 24
REMARK 465 ALA A 283
REMARK 465 ASP A 284
REMARK 465 GLY A 285
REMARK 465 GLU A 286
REMARK 465 GLU A 287
REMARK 465 VAL A 288
REMARK 465 GLU A 289
REMARK 465 LEU A 290
REMARK 465 ALA A 291
REMARK 465 SER A 292
REMARK 465 GLU A 293
REMARK 465 ASP A 294
REMARK 465 GLY A 295
REMARK 465 VAL A 296
REMARK 465 GLU A 297
REMARK 465 ALA A 298
REMARK 465 TYR A 299
REMARK 465 ASP A 300
REMARK 465 GLY A 301
REMARK 465 ASP A 302
REMARK 465 ARG A 303
REMARK 465 LEU A 304
REMARK 465 SER A 305
REMARK 465 LEU A 306
REMARK 465 GLU A 307
REMARK 465 ALA A 308
REMARK 465 THR A 309
REMARK 465 ASP A 310
REMARK 465 GLY A 311
REMARK 465 GLY A 312
REMARK 465 TYR A 313
REMARK 465 GLU A 314
REMARK 465 LEU A 315
REMARK 465 ARG A 316
REMARK 465 VAL A 317
REMARK 465 GLY A 318
REMARK 465 GLY A 319
REMARK 465 ASP A 320
REMARK 465 ALA A 321
REMARK 465 ARG A 322
REMARK 465 GLU A 323
REMARK 465 LEU A 324
REMARK 465 THR A 325
REMARK 465 ALA A 326
REMARK 465 ASP A 327
REMARK 465 GLU A 328
REMARK 465 LEU A 329
REMARK 465 ARG A 330
REMARK 465 ALA A 355
REMARK 465 ALA A 356
REMARK 465 LYS A 357
REMARK 465 GLU A 358
REMARK 465 ALA A 359
REMARK 465 GLY A 360
REMARK 465 ARG A 361
REMARK 465 GLY A 362
REMARK 465 ALA A 363
REMARK 465 ILE A 364
REMARK 465 ALA A 365
REMARK 465 MET A 366
REMARK 465 THR A 367
REMARK 465 GLN A 368
REMARK 465 SER A 369
REMARK 465 ALA A 370
REMARK 465 THR A 371
REMARK 465 LEU A 372
REMARK 465 ARG A 373
REMARK 465 ILE A 374
REMARK 465 GLY A 375
REMARK 465 GLY A 376
REMARK 465 THR A 377
REMARK 465 GLU A 378
REMARK 465 ILE A 379
REMARK 465 ASP A 380
REMARK 465 ILE A 381
REMARK 465 GLU A 382
REMARK 465 LYS A 383
REMARK 465 ASP A 384
REMARK 465 ARG A 385
REMARK 465 MET A 386
REMARK 465 LEU A 433
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 32 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 MET A 102 CG - SD - CE ANGL. DEV. = -11.2 DEGREES
REMARK 500 ASP A 171 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 MET A 173 CG - SD - CE ANGL. DEV. = -10.6 DEGREES
REMARK 500 ARG A 244 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 244 NE - CZ - NH2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 ARG A 409 NE - CZ - NH2 ANGL. DEV. = 3.6 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 GLU A 51 -97.41 -103.63
REMARK 500 SER A 91 88.11 -157.80
REMARK 500 GLU A 109 16.13 -64.26
REMARK 500 GLU A 123 18.60 59.34
REMARK 500 GLU A 158 28.99 -142.19
REMARK 500 LEU A 180 -3.85 -55.91
REMARK 500 PHE A 184 -68.12 -128.56
REMARK 500 ASP A 388 -154.73 -113.61
REMARK 500 VAL A 431 38.68 -98.95
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 K A 803 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 51 OE2
REMARK 620 2 ASP A 52 OD2 91.9
REMARK 620 3 ASP A 52 OD1 78.5 43.5
REMARK 620 4 GLU A 123 OE1 100.6 136.7 179.1
REMARK 620 5 ASP A 192 OD2 123.7 76.7 118.7 61.7
REMARK 620 6 HOH A 476 O 63.4 70.5 101.0 78.5 60.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 52 OD2
REMARK 620 2 GLU A 158 OE1 168.0
REMARK 620 3 ASP A 192 OD2 88.2 91.4
REMARK 620 4 HOH A 476 O 77.9 90.1 88.1
REMARK 620 5 GLV A 501 O1 112.8 68.9 158.7 99.3
REMARK 620 6 GLV A 501 O3 130.7 61.2 89.8 151.2 74.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 801 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET A 173 O
REMARK 620 2 LYS A 175 O 104.0
REMARK 620 3 ASN A 178 OD1 79.6 92.0
REMARK 620 4 ASN A 178 O 147.7 86.1 69.4
REMARK 620 5 GLU A 181 OE1 85.7 167.9 97.0 89.5
REMARK 620 6 GLU A 181 OE2 76.7 131.9 133.9 119.2 42.6
REMARK 620 7 HOH A 435 O 122.0 88.9 157.5 88.2 79.7 55.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 804 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PRO A 176 O
REMARK 620 2 ASN A 178 O 90.5
REMARK 620 3 ASN A 179 OD1 165.3 78.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 802 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 217 OG
REMARK 620 2 SER A 217 O 66.8
REMARK 620 3 SER A 221 OG 119.5 71.5
REMARK 620 4 GLY A 252 O 68.7 126.5 160.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLV A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 804
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3OYX RELATED DB: PDB
REMARK 900 HIGH-OCCUPANCY GLYOXYLATE COMPLEX
REMARK 900 RELATED ID: 3OYZ RELATED DB: PDB
REMARK 900 PYRUVATE/ACETYL-COA TERNARY COMPLEX
DBREF 3PUG A 1 433 UNP D4GTL2 D4GTL2_HALVD 1 433
SEQRES 1 A 433 MET THR GLU ARG ARG HIS ASP ARG GLU PHE VAL ARG THR
SEQRES 2 A 433 PHE PHE THR SER PRO THR ALA VAL GLU GLY GLU ASP ASP
SEQRES 3 A 433 SER ALA LYS MET LEU ARG ARG ALA ALA GLY LEU ARG GLY
SEQRES 4 A 433 MET GLN ALA PRO ASP VAL TRP VAL PRO ASP ASN GLU ASP
SEQRES 5 A 433 ALA THR ALA PRO SER MET ARG ASP GLU GLY ALA GLU ASN
SEQRES 6 A 433 ILE VAL GLU VAL ILE SER GLU GLN GLY ALA GLU PHE PRO
SEQRES 7 A 433 GLY GLU ILE HIS PRO ARG MET VAL TRP HIS ARG ASP SER
SEQRES 8 A 433 PRO GLU THR ARG TYR GLN GLY PHE GLN HIS MET LEU ASP
SEQRES 9 A 433 ILE THR ASP PRO GLU ARG GLY ALA VAL GLU HIS ILE HIS
SEQRES 10 A 433 GLY PHE VAL ILE PRO GLU VAL GLY GLY ILE ASP ASP TRP
SEQRES 11 A 433 LYS LYS ALA ASP GLU PHE PHE THR ILE VAL GLU HIS GLU
SEQRES 12 A 433 HIS GLY LEU ASP GLU GLY SER LEU ALA MET SER VAL ILE
SEQRES 13 A 433 ILE GLU SER GLY GLU ALA GLU LEU ALA MET GLY ASP LEU
SEQRES 14 A 433 ARG ASP GLU MET GLY LYS PRO THR ASN ASN LEU GLU ARG
SEQRES 15 A 433 LEU PHE LEU LEU VAL ASP GLY GLU VAL ASP TYR THR LYS
SEQRES 16 A 433 ASP MET ARG ALA MET THR PRO THR GLY GLU LEU PRO ALA
SEQRES 17 A 433 TRP PRO GLU LEU ARG HIS ASN THR SER ARG GLY ALA SER
SEQRES 18 A 433 ALA ALA GLY CYS VAL ALA VAL ASP GLY PRO TYR ASP ASP
SEQRES 19 A 433 ILE ARG ASP VAL GLU GLY TYR ARG GLU ARG MET THR ASP
SEQRES 20 A 433 ASN GLN ALA LYS GLY MET LEU GLY ILE TRP SER LEU THR
SEQRES 21 A 433 PRO GLY GLN VAL VAL GLU ALA ASN THR SER PRO LEU PRO
SEQRES 22 A 433 PRO LYS THR GLY SER TRP LEU LEU ASP ALA ASP GLY GLU
SEQRES 23 A 433 GLU VAL GLU LEU ALA SER GLU ASP GLY VAL GLU ALA TYR
SEQRES 24 A 433 ASP GLY ASP ARG LEU SER LEU GLU ALA THR ASP GLY GLY
SEQRES 25 A 433 TYR GLU LEU ARG VAL GLY GLY ASP ALA ARG GLU LEU THR
SEQRES 26 A 433 ALA ASP GLU LEU ARG GLU GLU LEU LEU GLY LEU THR SER
SEQRES 27 A 433 TYR VAL PRO SER MET ASP ASP ILE VAL ASP SER MET GLU
SEQRES 28 A 433 GLU PHE GLU ALA ALA LYS GLU ALA GLY ARG GLY ALA ILE
SEQRES 29 A 433 ALA MET THR GLN SER ALA THR LEU ARG ILE GLY GLY THR
SEQRES 30 A 433 GLU ILE ASP ILE GLU LYS ASP ARG MET TRP ASP GLU ALA
SEQRES 31 A 433 THR TYR GLN ALA ALA MET THR PRO ILE SER LEU PHE GLN
SEQRES 32 A 433 ASP VAL TYR GLU ASN ARG PRO ASP GLN HIS GLU GLU LEU
SEQRES 33 A 433 GLU GLU ARG TYR GLY ALA GLY VAL VAL GLU ARG ALA MET
SEQRES 34 A 433 GLU VAL GLY LEU
HET GLV A 501 5
HET MG A 601 1
HET CL A 701 1
HET CL A 702 1
HET CL A 703 1
HET CL A 704 1
HET K A 801 1
HET K A 802 1
HET K A 803 1
HET K A 804 1
HETNAM GLV GLYOXYLIC ACID
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
HETNAM K POTASSIUM ION
HETSYN GLV GLYOXALATE; GLYOXYLATE
FORMUL 2 GLV C2 H2 O3
FORMUL 3 MG MG 2+
FORMUL 4 CL 4(CL 1-)
FORMUL 8 K 4(K 1+)
FORMUL 12 HOH *71(H2 O)
HELIX 1 1 ALA A 28 ALA A 35 1 8
HELIX 2 2 GLY A 36 LEU A 37 5 2
HELIX 3 3 ARG A 38 ALA A 42 5 5
HELIX 4 4 ALA A 55 SER A 57 5 3
HELIX 5 5 MET A 58 GLY A 74 1 17
HELIX 6 6 ALA A 75 PHE A 77 5 3
HELIX 7 7 SER A 91 THR A 106 1 16
HELIX 8 8 ASP A 107 GLY A 111 5 5
HELIX 9 9 ALA A 112 ILE A 116 5 5
HELIX 10 10 GLY A 126 HIS A 144 1 19
HELIX 11 11 SER A 159 MET A 166 1 8
HELIX 12 12 ASP A 168 MET A 173 1 6
HELIX 13 13 ASN A 179 GLU A 181 5 3
HELIX 14 14 GLY A 189 MET A 197 1 9
HELIX 15 15 TRP A 209 GLY A 224 1 16
HELIX 16 16 ASP A 237 ALA A 250 1 14
HELIX 17 17 THR A 260 SER A 270 1 11
HELIX 18 18 GLU A 332 THR A 337 5 6
HELIX 19 19 SER A 342 GLU A 354 1 13
HELIX 20 20 ASP A 388 ARG A 409 1 22
HELIX 21 21 ARG A 409 GLY A 421 1 13
HELIX 22 22 GLY A 421 MET A 429 1 9
SHEET 1 A 8 GLU A 80 ILE A 81 0
SHEET 2 A 8 VAL A 45 ASP A 49 1 N TRP A 46 O GLU A 80
SHEET 3 A 8 THR A 13 PRO A 18 1 N PHE A 15 O VAL A 47
SHEET 4 A 8 GLY A 255 SER A 258 1 O SER A 258 N PHE A 14
SHEET 5 A 8 VAL A 226 ASP A 229 1 N ASP A 229 O GLY A 255
SHEET 6 A 8 LEU A 183 ASP A 188 1 N ASP A 188 O VAL A 228
SHEET 7 A 8 ALA A 152 ILE A 157 1 N VAL A 155 O VAL A 187
SHEET 8 A 8 GLY A 118 ILE A 121 1 N ILE A 121 O SER A 154
LINK OE2 GLU A 51 K K A 803 1555 1555 2.94
LINK OD2 ASP A 52 MG MG A 601 1555 1555 2.96
LINK OD2 ASP A 52 K K A 803 1555 1555 2.87
LINK OD1 ASP A 52 K K A 803 1555 1555 3.11
LINK OE1 GLU A 123 K K A 803 1555 1555 3.06
LINK OE1 GLU A 158 MG MG A 601 1555 1555 2.87
LINK O MET A 173 K K A 801 1555 1555 2.72
LINK O LYS A 175 K K A 801 1555 1555 2.62
LINK O PRO A 176 K K A 804 1555 1555 2.84
LINK OD1 ASN A 178 K K A 801 1555 1555 2.74
LINK O ASN A 178 K K A 801 1555 1555 2.80
LINK O ASN A 178 K K A 804 1555 1555 2.76
LINK OD1 ASN A 179 K K A 804 1555 1555 2.86
LINK OE1 GLU A 181 K K A 801 1555 1555 2.94
LINK OE2 GLU A 181 K K A 801 1555 1555 3.14
LINK OD2 ASP A 192 MG MG A 601 1555 1555 1.99
LINK OD2 ASP A 192 K K A 803 1555 1555 2.78
LINK OG SER A 217 K K A 802 1555 1555 2.68
LINK O SER A 217 K K A 802 1555 1555 3.26
LINK OG SER A 221 K K A 802 1555 1555 2.93
LINK O GLY A 252 K K A 802 1555 1555 3.01
LINK O HOH A 435 K K A 801 1555 1555 2.74
LINK O HOH A 476 MG MG A 601 1555 1555 1.95
LINK O HOH A 476 K K A 803 1555 1555 2.63
LINK O1 GLV A 501 MG MG A 601 1555 1555 2.00
LINK O3 GLV A 501 MG MG A 601 1555 1555 2.42
SITE 1 AC1 10 ARG A 84 GLU A 158 GLY A 189 GLU A 190
SITE 2 AC1 10 VAL A 191 ASP A 192 PRO A 231 HOH A 476
SITE 3 AC1 10 HOH A 485 MG A 601
SITE 1 AC2 6 ASP A 52 GLU A 158 ASP A 192 HOH A 476
SITE 2 AC2 6 GLV A 501 K A 803
SITE 1 AC3 3 ARG A 198 ALA A 227 K A 802
SITE 1 AC4 3 ARG A 89 PRO A 92 ARG A 95
SITE 1 AC5 1 ALA A 208
SITE 1 AC6 1 ARG A 218
SITE 1 AC7 5 MET A 173 LYS A 175 ASN A 178 GLU A 181
SITE 2 AC7 5 HOH A 435
SITE 1 AC8 5 MET A 197 SER A 217 SER A 221 GLY A 252
SITE 2 AC8 5 CL A 701
SITE 1 AC9 6 GLU A 51 ASP A 52 GLU A 123 ASP A 192
SITE 2 AC9 6 HOH A 476 MG A 601
SITE 1 BC1 3 PRO A 176 ASN A 178 ASN A 179
CRYST1 156.370 156.370 141.455 90.00 90.00 120.00 H 3 2 18
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 0.006395 0.003692 0.000000 0.00000
SCALE2 0.000000 0.007384 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007069 0.00000
(ATOM LINES ARE NOT SHOWN.)
END