HEADER TRANSFERASE 20-OCT-10 3PBE
TITLE CRYSTAL STRUCTURE OF THE MUTANT W207F OF HUMAN SECRETORY GLUTAMINYL
TITLE 2 CYCLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMINYL-PEPTIDE CYCLOTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: FUNCTIONAL DOMAIN;
COMPND 5 SYNONYM: GLUTAMINYL CYCLASE, QC, GLUTAMINYL-TRNA CYCLOTRANSFERASE,
COMPND 6 GLUTAMYL CYCLASE, EC;
COMPND 7 EC: 2.3.2.5;
COMPND 8 ENGINEERED: YES;
COMPND 9 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: QPCT;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET 32A
KEYWDS ALPHA/BETA PROTEIN, ALPHA/BETA-MIXED FOLD, GLUTAMINYL CYCLASE,
KEYWDS 2 SECRETORY PATHWAY, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.F.HUANG,S.S.LIAW,W.L.HUANG,C.Y.CHIA,Y.C.LO,Y.L.CHEN,A.H.J.WANG
REVDAT 3 01-NOV-23 3PBE 1 REMARK SEQADV LINK
REVDAT 2 03-AUG-11 3PBE 1 JRNL
REVDAT 1 02-FEB-11 3PBE 0
JRNL AUTH K.F.HUANG,S.S.LIAW,W.L.HUANG,C.Y.CHIA,Y.C.LO,Y.L.CHEN,
JRNL AUTH 2 A.H.J.WANG
JRNL TITL STRUCTURES OF HUMAN GOLGI-RESIDENT GLUTAMINYL CYCLASE AND
JRNL TITL 2 ITS COMPLEXES WITH INHIBITORS REVEAL A LARGE LOOP MOVEMENT
JRNL TITL 3 UPON INHIBITOR BINDING
JRNL REF J.BIOL.CHEM. V. 286 12439 2011
JRNL REFN ISSN 0021-9258
JRNL PMID 21288892
JRNL DOI 10.1074/JBC.M110.208595
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 62497
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) : 0.145
REMARK 3 R VALUE (WORKING SET) : 0.143
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3335
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4576
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.81
REMARK 3 BIN R VALUE (WORKING SET) : 0.1630
REMARK 3 BIN FREE R VALUE SET COUNT : 229
REMARK 3 BIN FREE R VALUE : 0.2440
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5214
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 507
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.18000
REMARK 3 B22 (A**2) : 0.18000
REMARK 3 B33 (A**2) : -0.26000
REMARK 3 B12 (A**2) : 0.09000
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): 0.114
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.070
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.348
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.971
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.959
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5364 ; 0.029 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7298 ; 1.903 ; 1.954
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 638 ; 6.382 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 268 ;33.940 ;23.881
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 862 ;13.677 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 32 ;17.615 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 780 ; 0.164 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4168 ; 0.010 ; 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): 3230 ; 2.095 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5212 ; 3.193 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2134 ; 5.051 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2086 ; 7.352 ; 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): 5364 ; 2.919 ; 3.000
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 : 1.40
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
REMARK 4
REMARK 4 3PBE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-NOV-10.
REMARK 100 THE DEPOSITION ID IS D_1000062186.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSRRC
REMARK 200 BEAMLINE : BL13B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65863
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : 0.04700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 40.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 5.40
REMARK 200 R MERGE FOR SHELL (I) : 0.49100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 2AFM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.7M (NH4)2SO4, 4%(V/V) DIOXANE, 100MM
REMARK 280 MES, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 59.37700
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 34.28133
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 110.69767
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 59.37700
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 34.28133
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 110.69767
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 59.37700
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 34.28133
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 110.69767
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 59.37700
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 34.28133
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 110.69767
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 59.37700
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 34.28133
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 110.69767
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 59.37700
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 34.28133
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 110.69767
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 68.56265
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 221.39533
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 68.56265
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 221.39533
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 68.56265
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 221.39533
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 68.56265
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 221.39533
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 68.56265
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 221.39533
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 68.56265
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 221.39533
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: MONOMERIC
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 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 HOH B 661 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 896 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 THR A 183
REMARK 465 VAL A 184
REMARK 465 SER A 185
REMARK 465 ASP A 186
REMARK 465 SER A 187
REMARK 465 LYS A 188
REMARK 465 THR B 183
REMARK 465 VAL B 184
REMARK 465 SER B 185
REMARK 465 ASP B 186
REMARK 465 SER B 187
REMARK 465 LYS B 188
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 ALA A 131
REMARK 475 ALA B 131
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 NZ LYS B 177 O HOH B 855 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 LYS A 40 CE LYS A 40 NZ 0.192
REMARK 500 ALA A 100 CA ALA A 100 CB 0.134
REMARK 500 VAL A 153 CB VAL A 153 CG2 0.130
REMARK 500 GLU A 337 CB GLU A 337 CG 0.141
REMARK 500 GLU A 337 CG GLU A 337 CD 0.136
REMARK 500 VAL B 153 CB VAL B 153 CG2 0.144
REMARK 500 GLU B 269 CG GLU B 269 CD 0.101
REMARK 500 GLU B 337 CB GLU B 337 CG 0.160
REMARK 500 GLU B 337 CG GLU B 337 CD 0.153
REMARK 500
REMARK 500 REMARK: NULL
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 B 292 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ARG A 77 43.60 -152.82
REMARK 500 LEU A 205 -117.08 -106.00
REMARK 500 SER A 212 162.20 167.66
REMARK 500 TYR A 297 140.21 -174.89
REMARK 500 ARG B 77 44.36 -146.49
REMARK 500 LEU B 205 -47.43 -131.23
REMARK 500 SER B 212 159.94 169.94
REMARK 500 LEU B 243 138.05 -170.48
REMARK 500 ASN B 296 51.59 -45.72
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 ZN A 391 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 159 OD2
REMARK 620 2 GLU A 202 OE2 106.2
REMARK 620 3 HIS A 330 NE2 100.7 113.4
REMARK 620 4 HOH A 861 O 111.2 105.6 119.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 392 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 159 OD2
REMARK 620 2 GLU B 202 OE2 104.4
REMARK 620 3 HIS B 330 NE2 105.6 120.1
REMARK 620 4 HOH B 867 O 106.9 98.7 119.7
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 ZN A 391
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 392
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 395
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 396
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2AFM RELATED DB: PDB
REMARK 900 THE WILD-TYPE PROTEIN AT PH 6.5
REMARK 900 RELATED ID: 3PB4 RELATED DB: PDB
REMARK 900 RELATED ID: 3PB6 RELATED DB: PDB
REMARK 900 RELATED ID: 3PB7 RELATED DB: PDB
REMARK 900 RELATED ID: 3PB8 RELATED DB: PDB
REMARK 900 RELATED ID: 3PB9 RELATED DB: PDB
REMARK 900 RELATED ID: 3PBB RELATED DB: PDB
DBREF 3PBE A 33 361 UNP Q16769 QPCT_HUMAN 33 361
DBREF 3PBE B 33 361 UNP Q16769 QPCT_HUMAN 33 361
SEQADV 3PBE PHE A 207 UNP Q16769 TRP 207 ENGINEERED MUTATION
SEQADV 3PBE PHE B 207 UNP Q16769 TRP 207 ENGINEERED MUTATION
SEQRES 1 A 329 ALA SER ALA TRP PRO GLU GLU LYS ASN TYR HIS GLN PRO
SEQRES 2 A 329 ALA ILE LEU ASN SER SER ALA LEU ARG GLN ILE ALA GLU
SEQRES 3 A 329 GLY THR SER ILE SER GLU MET TRP GLN ASN ASP LEU GLN
SEQRES 4 A 329 PRO LEU LEU ILE GLU ARG TYR PRO GLY SER PRO GLY SER
SEQRES 5 A 329 TYR ALA ALA ARG GLN HIS ILE MET GLN ARG ILE GLN ARG
SEQRES 6 A 329 LEU GLN ALA ASP TRP VAL LEU GLU ILE ASP THR PHE LEU
SEQRES 7 A 329 SER GLN THR PRO TYR GLY TYR ARG SER PHE SER ASN ILE
SEQRES 8 A 329 ILE SER THR LEU ASN PRO THR ALA LYS ARG HIS LEU VAL
SEQRES 9 A 329 LEU ALA CYS HIS TYR ASP SER LYS TYR PHE SER HIS TRP
SEQRES 10 A 329 ASN ASN ARG VAL PHE VAL GLY ALA THR ASP SER ALA VAL
SEQRES 11 A 329 PRO CYS ALA MET MET LEU GLU LEU ALA ARG ALA LEU ASP
SEQRES 12 A 329 LYS LYS LEU LEU SER LEU LYS THR VAL SER ASP SER LYS
SEQRES 13 A 329 PRO ASP LEU SER LEU GLN LEU ILE PHE PHE ASP GLY GLU
SEQRES 14 A 329 GLU ALA PHE LEU HIS PHE SER PRO GLN ASP SER LEU TYR
SEQRES 15 A 329 GLY SER ARG HIS LEU ALA ALA LYS MET ALA SER THR PRO
SEQRES 16 A 329 HIS PRO PRO GLY ALA ARG GLY THR SER GLN LEU HIS GLY
SEQRES 17 A 329 MET ASP LEU LEU VAL LEU LEU ASP LEU ILE GLY ALA PRO
SEQRES 18 A 329 ASN PRO THR PHE PRO ASN PHE PHE PRO ASN SER ALA ARG
SEQRES 19 A 329 TRP PHE GLU ARG LEU GLN ALA ILE GLU HIS GLU LEU HIS
SEQRES 20 A 329 GLU LEU GLY LEU LEU LYS ASP HIS SER LEU GLU GLY ARG
SEQRES 21 A 329 TYR PHE GLN ASN TYR SER TYR GLY GLY VAL ILE GLN ASP
SEQRES 22 A 329 ASP HIS ILE PRO PHE LEU ARG ARG GLY VAL PRO VAL LEU
SEQRES 23 A 329 HIS LEU ILE PRO SER PRO PHE PRO GLU VAL TRP HIS THR
SEQRES 24 A 329 MET ASP ASP ASN GLU GLU ASN LEU ASP GLU SER THR ILE
SEQRES 25 A 329 ASP ASN LEU ASN LYS ILE LEU GLN VAL PHE VAL LEU GLU
SEQRES 26 A 329 TYR LEU HIS LEU
SEQRES 1 B 329 ALA SER ALA TRP PRO GLU GLU LYS ASN TYR HIS GLN PRO
SEQRES 2 B 329 ALA ILE LEU ASN SER SER ALA LEU ARG GLN ILE ALA GLU
SEQRES 3 B 329 GLY THR SER ILE SER GLU MET TRP GLN ASN ASP LEU GLN
SEQRES 4 B 329 PRO LEU LEU ILE GLU ARG TYR PRO GLY SER PRO GLY SER
SEQRES 5 B 329 TYR ALA ALA ARG GLN HIS ILE MET GLN ARG ILE GLN ARG
SEQRES 6 B 329 LEU GLN ALA ASP TRP VAL LEU GLU ILE ASP THR PHE LEU
SEQRES 7 B 329 SER GLN THR PRO TYR GLY TYR ARG SER PHE SER ASN ILE
SEQRES 8 B 329 ILE SER THR LEU ASN PRO THR ALA LYS ARG HIS LEU VAL
SEQRES 9 B 329 LEU ALA CYS HIS TYR ASP SER LYS TYR PHE SER HIS TRP
SEQRES 10 B 329 ASN ASN ARG VAL PHE VAL GLY ALA THR ASP SER ALA VAL
SEQRES 11 B 329 PRO CYS ALA MET MET LEU GLU LEU ALA ARG ALA LEU ASP
SEQRES 12 B 329 LYS LYS LEU LEU SER LEU LYS THR VAL SER ASP SER LYS
SEQRES 13 B 329 PRO ASP LEU SER LEU GLN LEU ILE PHE PHE ASP GLY GLU
SEQRES 14 B 329 GLU ALA PHE LEU HIS PHE SER PRO GLN ASP SER LEU TYR
SEQRES 15 B 329 GLY SER ARG HIS LEU ALA ALA LYS MET ALA SER THR PRO
SEQRES 16 B 329 HIS PRO PRO GLY ALA ARG GLY THR SER GLN LEU HIS GLY
SEQRES 17 B 329 MET ASP LEU LEU VAL LEU LEU ASP LEU ILE GLY ALA PRO
SEQRES 18 B 329 ASN PRO THR PHE PRO ASN PHE PHE PRO ASN SER ALA ARG
SEQRES 19 B 329 TRP PHE GLU ARG LEU GLN ALA ILE GLU HIS GLU LEU HIS
SEQRES 20 B 329 GLU LEU GLY LEU LEU LYS ASP HIS SER LEU GLU GLY ARG
SEQRES 21 B 329 TYR PHE GLN ASN TYR SER TYR GLY GLY VAL ILE GLN ASP
SEQRES 22 B 329 ASP HIS ILE PRO PHE LEU ARG ARG GLY VAL PRO VAL LEU
SEQRES 23 B 329 HIS LEU ILE PRO SER PRO PHE PRO GLU VAL TRP HIS THR
SEQRES 24 B 329 MET ASP ASP ASN GLU GLU ASN LEU ASP GLU SER THR ILE
SEQRES 25 B 329 ASP ASN LEU ASN LYS ILE LEU GLN VAL PHE VAL LEU GLU
SEQRES 26 B 329 TYR LEU HIS LEU
HET ZN A 391 1
HET SO4 A 395 5
HET ZN B 392 1
HET SO4 B 396 5
HETNAM ZN ZINC ION
HETNAM SO4 SULFATE ION
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 SO4 2(O4 S 2-)
FORMUL 7 HOH *507(H2 O)
HELIX 1 1 ALA A 35 PRO A 37 5 3
HELIX 2 2 GLU A 38 HIS A 43 1 6
HELIX 3 3 ASN A 49 THR A 60 1 12
HELIX 4 4 SER A 61 ASP A 69 1 9
HELIX 5 5 LEU A 70 LEU A 74 5 5
HELIX 6 6 SER A 81 ARG A 97 1 17
HELIX 7 7 SER A 160 LEU A 174 1 15
HELIX 8 8 LEU A 174 SER A 180 1 7
HELIX 9 9 LEU A 213 SER A 225 1 13
HELIX 10 10 PHE A 261 ASN A 263 5 3
HELIX 11 11 SER A 264 LEU A 281 1 18
HELIX 12 12 HIS A 307 ARG A 312 1 6
HELIX 13 13 ASP A 340 HIS A 360 1 21
HELIX 14 14 ALA B 35 TYR B 42 5 8
HELIX 15 15 ASN B 49 THR B 60 1 12
HELIX 16 16 SER B 61 ASP B 69 1 9
HELIX 17 17 LEU B 70 LEU B 74 5 5
HELIX 18 18 SER B 81 ARG B 97 1 17
HELIX 19 19 HIS B 148 ARG B 152 5 5
HELIX 20 20 SER B 160 LEU B 174 1 15
HELIX 21 21 LEU B 174 SER B 180 1 7
HELIX 22 22 LEU B 213 SER B 225 1 13
HELIX 23 23 PHE B 261 ASN B 263 5 3
HELIX 24 24 SER B 264 LEU B 281 1 18
HELIX 25 25 SER B 288 ARG B 292 5 5
HELIX 26 26 HIS B 307 ARG B 312 1 6
HELIX 27 27 ASP B 340 HIS B 360 1 21
SHEET 1 A 6 VAL A 103 SER A 111 0
SHEET 2 A 6 ARG A 118 THR A 126 -1 O ILE A 124 N GLU A 105
SHEET 3 A 6 LEU A 191 PHE A 198 -1 O LEU A 195 N SER A 125
SHEET 4 A 6 ARG A 133 HIS A 140 1 N CYS A 139 O PHE A 198
SHEET 5 A 6 MET A 241 LEU A 247 1 O VAL A 245 N VAL A 136
SHEET 6 A 6 VAL A 317 LEU A 320 1 O LEU A 318 N LEU A 244
SHEET 1 B 6 VAL B 103 THR B 113 0
SHEET 2 B 6 GLY B 116 THR B 126 -1 O ILE B 124 N GLU B 105
SHEET 3 B 6 LEU B 191 PHE B 198 -1 O PHE B 197 N ILE B 123
SHEET 4 B 6 ARG B 133 HIS B 140 1 N CYS B 139 O PHE B 198
SHEET 5 B 6 MET B 241 LEU B 247 1 O VAL B 245 N VAL B 136
SHEET 6 B 6 VAL B 317 LEU B 320 1 O LEU B 318 N LEU B 244
SHEET 1 C 2 PHE B 257 ASN B 259 0
SHEET 2 C 2 PHE B 294 SER B 298 1 O TYR B 297 N ASN B 259
LINK OD2 ASP A 159 ZN ZN A 391 1555 1555 2.00
LINK OE2 GLU A 202 ZN ZN A 391 1555 1555 1.96
LINK NE2 HIS A 330 ZN ZN A 391 1555 1555 2.05
LINK ZN ZN A 391 O HOH A 861 1555 1555 2.20
LINK OD2 ASP B 159 ZN ZN B 392 1555 1555 1.98
LINK OE2 GLU B 202 ZN ZN B 392 1555 1555 1.92
LINK NE2 HIS B 330 ZN ZN B 392 1555 1555 1.98
LINK ZN ZN B 392 O HOH B 867 1555 1555 2.18
CISPEP 1 ASP A 159 SER A 160 0 -4.92
CISPEP 2 HIS A 228 PRO A 229 0 -3.14
CISPEP 3 SER A 323 PRO A 324 0 4.88
CISPEP 4 ASP B 159 SER B 160 0 1.86
CISPEP 5 HIS B 228 PRO B 229 0 -4.32
CISPEP 6 SER B 323 PRO B 324 0 3.57
SITE 1 AC1 4 ASP A 159 GLU A 202 HIS A 330 HOH A 861
SITE 1 AC2 4 ASP B 159 GLU B 202 HIS B 330 HOH B 867
SITE 1 AC3 10 LYS A 144 LEU A 205 HIS A 206 PHE A 207
SITE 2 AC3 10 ASN A 263 TRP A 329 HIS A 330 HOH A 574
SITE 3 AC3 10 HOH A 703 HOH A 893
SITE 1 AC4 10 LYS B 40 LYS B 144 LEU B 205 HIS B 206
SITE 2 AC4 10 PHE B 207 HOH B 603 HOH B 604 HOH B 725
SITE 3 AC4 10 HOH B 836 HOH B 846
CRYST1 118.754 118.754 332.093 90.00 90.00 120.00 H 3 2 36
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 0.008421 0.004862 0.000000 0.00000
SCALE2 0.000000 0.009723 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003011 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
