HEADER HYDROLASE 13-JAN-14 4OEC
TITLE CRYSTAL STRUCTURE OF GLYCEROPHOSPHODIESTER PHOSPHODIESTERASE FROM
TITLE 2 THERMOCOCCUS KODAKARENSIS KOD1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCEROPHOSPHORYL DIESTER PHOSPHODIESTERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.1.4.46;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOCOCCUS KODAKARENSIS;
SOURCE 3 ORGANISM_TAXID: 69014;
SOURCE 4 STRAIN: KOD1;
SOURCE 5 GENE: TK1397;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET25B
KEYWDS TIM BARREL, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ATSUTA,D.J.YOU,K.TAKANO,Y.KOGA,S.KANAYA
REVDAT 3 08-NOV-23 4OEC 1 REMARK LINK
REVDAT 2 22-NOV-17 4OEC 1 REMARK
REVDAT 1 14-JAN-15 4OEC 0
JRNL AUTH Y.ATSUTA,D.J.YOU,K.TAKANO,Y.KOGA,S.KANAYA
JRNL TITL CRYSTAL STRUCTURE OF GLYCEROPHOSPHODIESTER PHOSPHODIESTERASE
JRNL TITL 2 FROM THERMOCOCCUS KODAKARENSIS KOD1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 79606
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) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3998
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.94
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5316
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.70
REMARK 3 BIN R VALUE (WORKING SET) : 0.2130
REMARK 3 BIN FREE R VALUE SET COUNT : 277
REMARK 3 BIN FREE R VALUE : 0.2410
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8016
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 693
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.08000
REMARK 3 B22 (A**2) : 1.91000
REMARK 3 B33 (A**2) : -2.99000
REMARK 3 B12 (A**2) : 0.00000
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): 0.173
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.164
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.111
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.673
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8140 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11008 ; 0.978 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 988 ; 7.232 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 392 ;32.312 ;24.388
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1560 ;14.998 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 72 ;18.111 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1264 ; 0.089 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6036 ; 0.015 ; 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): 4940 ; 1.507 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8008 ; 2.335 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3200 ; 3.906 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3000 ; 5.973 ; 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 : 1.40
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 4OEC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-JAN-14.
REMARK 100 THE DEPOSITION ID IS D_1000084385.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUL-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : HORIZONTAL FOCUSING MIRROR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRUKER SMART 6500
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79998
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 13.60
REMARK 200 R MERGE (I) : 0.14200
REMARK 200 R SYM (I) : 0.14200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.4930
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 14.40
REMARK 200 R MERGE FOR SHELL (I) : 0.55800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP, BALBES
REMARK 200 STARTING MODEL: 2OTD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30%(W/V) PEG4000, 0.2M MAGNESIUM
REMARK 280 CHLORIDE HEXAHYDRATE, 0.1M TRIS-HCL, PH 8.5, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 21.86200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 85.81950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 66.01700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 85.81950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.86200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 66.01700
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 TYR A 215 CD1 TYR A 215 CE1 -0.091
REMARK 500 GLU D 21 CB GLU D 21 CG -0.194
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 ASP A 47 O - C - N ANGL. DEV. = -11.9 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 ASP A 47 42.85 -100.04
REMARK 500 PRO B 125 -19.65 -46.02
REMARK 500 GLU D 21 123.31 -31.75
REMARK 500 ASP D 47 46.66 -101.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ASP A 47 -23.58
REMARK 500 ASP D 47 -13.55
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 MG A 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 39 OE2
REMARK 620 2 ASP A 41 OD1 110.1
REMARK 620 3 GLU A 106 OE1 98.7 90.7
REMARK 620 4 HOH A 713 O 86.2 83.6 173.5
REMARK 620 5 HOH A 718 O 92.3 153.4 100.3 83.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 39 OE2
REMARK 620 2 ASP B 41 OD1 110.3
REMARK 620 3 GLU B 106 OE1 100.0 93.9
REMARK 620 4 HOH B 530 O 93.1 151.2 98.5
REMARK 620 5 HOH B 570 O 162.0 81.5 92.4 72.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 39 OE2
REMARK 620 2 ASP C 41 OD1 102.0
REMARK 620 3 GLU C 106 OE2 95.2 94.3
REMARK 620 4 HOH C 592 O 86.9 91.5 173.3
REMARK 620 5 HOH C 606 O 162.2 94.9 88.8 87.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 39 OE2
REMARK 620 2 ASP D 41 OD1 110.8
REMARK 620 3 GLU D 106 OE1 98.2 93.5
REMARK 620 4 HOH D 666 O 86.4 84.9 175.4
REMARK 620 5 HOH D 672 O 97.7 147.6 97.7 81.5
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 401
DBREF 4OEC A 1 248 UNP Q5JGZ3 Q5JGZ3_THEKO 1 248
DBREF 4OEC B 1 248 UNP Q5JGZ3 Q5JGZ3_THEKO 1 248
DBREF 4OEC C 1 248 UNP Q5JGZ3 Q5JGZ3_THEKO 1 248
DBREF 4OEC D 1 248 UNP Q5JGZ3 Q5JGZ3_THEKO 1 248
SEQRES 1 A 248 MET TRP GLU ARG ASP ARG VAL ILE VAL LEU GLY HIS ARG
SEQRES 2 A 248 GLY TYR MET SER ASN TYR PRO GLU ASN THR LEU LEU ALA
SEQRES 3 A 248 PHE ARG LYS ALA VAL GLU ALA GLY ALA ASP GLY ILE GLU
SEQRES 4 A 248 LEU ASP VAL TRP LEU THR LYS ASP GLY ARG VAL VAL VAL
SEQRES 5 A 248 MET HIS ASP GLU THR ILE ASP ARG THR SER ASN MET LYS
SEQRES 6 A 248 GLY ARG GLN LYS ASP MET THR LEU GLU GLU LEU LYS LYS
SEQRES 7 A 248 ALA ASP VAL GLY GLN GLY GLU ARG ILE PRO THR LEU GLU
SEQRES 8 A 248 GLU VAL PHE GLU ALA ILE PRO ARG ASN ALA LEU VAL ASN
SEQRES 9 A 248 VAL GLU LEU LYS ASP ARG ASP ALA ALA ARG GLU VAL ALA
SEQRES 10 A 248 GLU ILE VAL ALA GLU ASN ASN PRO GLU ARG VAL MET ILE
SEQRES 11 A 248 SER SER PHE ASP ILE ASP ALA LEU ARG GLU TYR ARG LYS
SEQRES 12 A 248 TYR ASP ASP GLU THR THR MET GLY LEU LEU ILE ASP ARG
SEQRES 13 A 248 GLU GLU VAL VAL PRO LEU ILE PRO LYS LEU LYS ASP GLU
SEQRES 14 A 248 LEU ASN LEU TRP SER VAL ASN VAL PRO MET GLU ALA ILE
SEQRES 15 A 248 PRO LEU ILE GLY LEU GLU LYS THR LEU GLN ALA LEU HIS
SEQRES 16 A 248 TRP VAL ARG SER LEU GLY LEU LYS VAL VAL LEU TRP THR
SEQRES 17 A 248 GLU ASN ASP VAL LEU PHE TYR LYS ASP ASP ASN LEU ALA
SEQRES 18 A 248 LYS LEU LYS GLY LEU PHE GLU VAL VAL ILE ALA ASN ASP
SEQRES 19 A 248 VAL VAL ARG MET ILE GLU TYR LEU LYS LYS LEU GLY LEU
SEQRES 20 A 248 ARG
SEQRES 1 B 248 MET TRP GLU ARG ASP ARG VAL ILE VAL LEU GLY HIS ARG
SEQRES 2 B 248 GLY TYR MET SER ASN TYR PRO GLU ASN THR LEU LEU ALA
SEQRES 3 B 248 PHE ARG LYS ALA VAL GLU ALA GLY ALA ASP GLY ILE GLU
SEQRES 4 B 248 LEU ASP VAL TRP LEU THR LYS ASP GLY ARG VAL VAL VAL
SEQRES 5 B 248 MET HIS ASP GLU THR ILE ASP ARG THR SER ASN MET LYS
SEQRES 6 B 248 GLY ARG GLN LYS ASP MET THR LEU GLU GLU LEU LYS LYS
SEQRES 7 B 248 ALA ASP VAL GLY GLN GLY GLU ARG ILE PRO THR LEU GLU
SEQRES 8 B 248 GLU VAL PHE GLU ALA ILE PRO ARG ASN ALA LEU VAL ASN
SEQRES 9 B 248 VAL GLU LEU LYS ASP ARG ASP ALA ALA ARG GLU VAL ALA
SEQRES 10 B 248 GLU ILE VAL ALA GLU ASN ASN PRO GLU ARG VAL MET ILE
SEQRES 11 B 248 SER SER PHE ASP ILE ASP ALA LEU ARG GLU TYR ARG LYS
SEQRES 12 B 248 TYR ASP ASP GLU THR THR MET GLY LEU LEU ILE ASP ARG
SEQRES 13 B 248 GLU GLU VAL VAL PRO LEU ILE PRO LYS LEU LYS ASP GLU
SEQRES 14 B 248 LEU ASN LEU TRP SER VAL ASN VAL PRO MET GLU ALA ILE
SEQRES 15 B 248 PRO LEU ILE GLY LEU GLU LYS THR LEU GLN ALA LEU HIS
SEQRES 16 B 248 TRP VAL ARG SER LEU GLY LEU LYS VAL VAL LEU TRP THR
SEQRES 17 B 248 GLU ASN ASP VAL LEU PHE TYR LYS ASP ASP ASN LEU ALA
SEQRES 18 B 248 LYS LEU LYS GLY LEU PHE GLU VAL VAL ILE ALA ASN ASP
SEQRES 19 B 248 VAL VAL ARG MET ILE GLU TYR LEU LYS LYS LEU GLY LEU
SEQRES 20 B 248 ARG
SEQRES 1 C 248 MET TRP GLU ARG ASP ARG VAL ILE VAL LEU GLY HIS ARG
SEQRES 2 C 248 GLY TYR MET SER ASN TYR PRO GLU ASN THR LEU LEU ALA
SEQRES 3 C 248 PHE ARG LYS ALA VAL GLU ALA GLY ALA ASP GLY ILE GLU
SEQRES 4 C 248 LEU ASP VAL TRP LEU THR LYS ASP GLY ARG VAL VAL VAL
SEQRES 5 C 248 MET HIS ASP GLU THR ILE ASP ARG THR SER ASN MET LYS
SEQRES 6 C 248 GLY ARG GLN LYS ASP MET THR LEU GLU GLU LEU LYS LYS
SEQRES 7 C 248 ALA ASP VAL GLY GLN GLY GLU ARG ILE PRO THR LEU GLU
SEQRES 8 C 248 GLU VAL PHE GLU ALA ILE PRO ARG ASN ALA LEU VAL ASN
SEQRES 9 C 248 VAL GLU LEU LYS ASP ARG ASP ALA ALA ARG GLU VAL ALA
SEQRES 10 C 248 GLU ILE VAL ALA GLU ASN ASN PRO GLU ARG VAL MET ILE
SEQRES 11 C 248 SER SER PHE ASP ILE ASP ALA LEU ARG GLU TYR ARG LYS
SEQRES 12 C 248 TYR ASP ASP GLU THR THR MET GLY LEU LEU ILE ASP ARG
SEQRES 13 C 248 GLU GLU VAL VAL PRO LEU ILE PRO LYS LEU LYS ASP GLU
SEQRES 14 C 248 LEU ASN LEU TRP SER VAL ASN VAL PRO MET GLU ALA ILE
SEQRES 15 C 248 PRO LEU ILE GLY LEU GLU LYS THR LEU GLN ALA LEU HIS
SEQRES 16 C 248 TRP VAL ARG SER LEU GLY LEU LYS VAL VAL LEU TRP THR
SEQRES 17 C 248 GLU ASN ASP VAL LEU PHE TYR LYS ASP ASP ASN LEU ALA
SEQRES 18 C 248 LYS LEU LYS GLY LEU PHE GLU VAL VAL ILE ALA ASN ASP
SEQRES 19 C 248 VAL VAL ARG MET ILE GLU TYR LEU LYS LYS LEU GLY LEU
SEQRES 20 C 248 ARG
SEQRES 1 D 248 MET TRP GLU ARG ASP ARG VAL ILE VAL LEU GLY HIS ARG
SEQRES 2 D 248 GLY TYR MET SER ASN TYR PRO GLU ASN THR LEU LEU ALA
SEQRES 3 D 248 PHE ARG LYS ALA VAL GLU ALA GLY ALA ASP GLY ILE GLU
SEQRES 4 D 248 LEU ASP VAL TRP LEU THR LYS ASP GLY ARG VAL VAL VAL
SEQRES 5 D 248 MET HIS ASP GLU THR ILE ASP ARG THR SER ASN MET LYS
SEQRES 6 D 248 GLY ARG GLN LYS ASP MET THR LEU GLU GLU LEU LYS LYS
SEQRES 7 D 248 ALA ASP VAL GLY GLN GLY GLU ARG ILE PRO THR LEU GLU
SEQRES 8 D 248 GLU VAL PHE GLU ALA ILE PRO ARG ASN ALA LEU VAL ASN
SEQRES 9 D 248 VAL GLU LEU LYS ASP ARG ASP ALA ALA ARG GLU VAL ALA
SEQRES 10 D 248 GLU ILE VAL ALA GLU ASN ASN PRO GLU ARG VAL MET ILE
SEQRES 11 D 248 SER SER PHE ASP ILE ASP ALA LEU ARG GLU TYR ARG LYS
SEQRES 12 D 248 TYR ASP ASP GLU THR THR MET GLY LEU LEU ILE ASP ARG
SEQRES 13 D 248 GLU GLU VAL VAL PRO LEU ILE PRO LYS LEU LYS ASP GLU
SEQRES 14 D 248 LEU ASN LEU TRP SER VAL ASN VAL PRO MET GLU ALA ILE
SEQRES 15 D 248 PRO LEU ILE GLY LEU GLU LYS THR LEU GLN ALA LEU HIS
SEQRES 16 D 248 TRP VAL ARG SER LEU GLY LEU LYS VAL VAL LEU TRP THR
SEQRES 17 D 248 GLU ASN ASP VAL LEU PHE TYR LYS ASP ASP ASN LEU ALA
SEQRES 18 D 248 LYS LEU LYS GLY LEU PHE GLU VAL VAL ILE ALA ASN ASP
SEQRES 19 D 248 VAL VAL ARG MET ILE GLU TYR LEU LYS LYS LEU GLY LEU
SEQRES 20 D 248 ARG
HET MG A 401 1
HET MG B 401 1
HET MG C 401 1
HET MG D 401 1
HETNAM MG MAGNESIUM ION
FORMUL 5 MG 4(MG 2+)
FORMUL 9 HOH *693(H2 O)
HELIX 1 1 THR A 23 ALA A 33 1 11
HELIX 2 2 ARG A 67 MET A 71 5 5
HELIX 3 3 THR A 72 LYS A 77 1 6
HELIX 4 4 THR A 89 ILE A 97 1 9
HELIX 5 5 ASP A 109 ASP A 111 5 3
HELIX 6 6 ALA A 112 GLU A 122 1 11
HELIX 7 7 ASN A 124 GLU A 126 5 3
HELIX 8 8 ASP A 134 ASP A 145 1 12
HELIX 9 9 ARG A 156 PRO A 161 5 6
HELIX 10 10 LEU A 162 ASN A 171 1 10
HELIX 11 11 GLU A 180 GLY A 186 1 7
HELIX 12 12 GLY A 186 LEU A 200 1 15
HELIX 13 13 THR A 208 ASN A 210 5 3
HELIX 14 14 ASP A 211 LYS A 216 1 6
HELIX 15 15 ASP A 218 LEU A 223 1 6
HELIX 16 16 ASP A 234 LEU A 245 1 12
HELIX 17 17 THR B 23 ALA B 33 1 11
HELIX 18 18 ARG B 67 MET B 71 5 5
HELIX 19 19 THR B 72 LYS B 77 1 6
HELIX 20 20 THR B 89 ILE B 97 1 9
HELIX 21 21 ASP B 109 ASP B 111 5 3
HELIX 22 22 ALA B 112 GLU B 122 1 11
HELIX 23 23 ASN B 123 GLU B 126 5 4
HELIX 24 24 ASP B 134 ASP B 145 1 12
HELIX 25 25 ARG B 156 PRO B 161 5 6
HELIX 26 26 LEU B 162 ASN B 171 1 10
HELIX 27 27 GLU B 180 GLY B 186 1 7
HELIX 28 28 GLY B 186 LEU B 200 1 15
HELIX 29 29 ASP B 211 LYS B 216 1 6
HELIX 30 30 ASP B 218 LEU B 223 1 6
HELIX 31 31 ASP B 234 LEU B 245 1 12
HELIX 32 32 THR C 23 ALA C 33 1 11
HELIX 33 33 ARG C 67 MET C 71 5 5
HELIX 34 34 THR C 72 LYS C 77 1 6
HELIX 35 35 THR C 89 ILE C 97 1 9
HELIX 36 36 ASP C 109 ASP C 111 5 3
HELIX 37 37 ALA C 112 GLU C 122 1 11
HELIX 38 38 ASN C 123 GLU C 126 5 4
HELIX 39 39 ASP C 134 LYS C 143 1 10
HELIX 40 40 ARG C 156 PRO C 161 5 6
HELIX 41 41 LEU C 162 ASN C 171 1 10
HELIX 42 42 GLU C 180 ILE C 185 1 6
HELIX 43 43 GLY C 186 LEU C 200 1 15
HELIX 44 44 ASP C 211 LYS C 216 1 6
HELIX 45 45 ASP C 218 LEU C 223 1 6
HELIX 46 46 ASP C 234 GLY C 246 1 13
HELIX 47 47 THR D 23 ALA D 33 1 11
HELIX 48 48 ARG D 67 MET D 71 5 5
HELIX 49 49 THR D 72 LYS D 77 1 6
HELIX 50 50 THR D 89 ILE D 97 1 9
HELIX 51 51 ASP D 109 ASP D 111 5 3
HELIX 52 52 ALA D 112 GLU D 122 1 11
HELIX 53 53 ASN D 124 GLU D 126 5 3
HELIX 54 54 ASP D 134 ASP D 145 1 12
HELIX 55 55 ARG D 156 PRO D 161 5 6
HELIX 56 56 LEU D 162 ASN D 171 1 10
HELIX 57 57 GLU D 180 GLY D 186 1 7
HELIX 58 58 GLY D 186 LEU D 200 1 15
HELIX 59 59 ASP D 211 LYS D 216 1 6
HELIX 60 60 ASP D 218 LEU D 223 1 6
HELIX 61 61 ASP D 234 LEU D 245 1 12
SHEET 1 A10 VAL A 50 VAL A 52 0
SHEET 2 A10 GLY A 37 LEU A 44 -1 N TRP A 43 O VAL A 51
SHEET 3 A10 LEU A 102 LEU A 107 1 O GLU A 106 N LEU A 40
SHEET 4 A10 VAL A 128 SER A 132 1 O MET A 129 N VAL A 103
SHEET 5 A10 THR A 149 LEU A 153 1 O THR A 149 N ILE A 130
SHEET 6 A10 SER A 174 PRO A 178 1 O ASN A 176 N LEU A 152
SHEET 7 A10 LYS A 203 TRP A 207 1 O VAL A 205 N VAL A 175
SHEET 8 A10 VAL A 229 ALA A 232 1 O VAL A 229 N LEU A 206
SHEET 9 A10 ILE A 8 HIS A 12 1 N ILE A 8 O VAL A 230
SHEET 10 A10 GLY A 37 LEU A 44 1 O GLY A 37 N GLY A 11
SHEET 1 B10 VAL B 50 VAL B 52 0
SHEET 2 B10 GLY B 37 LEU B 44 -1 N TRP B 43 O VAL B 51
SHEET 3 B10 LEU B 102 LEU B 107 1 O GLU B 106 N LEU B 40
SHEET 4 B10 VAL B 128 SER B 132 1 O MET B 129 N VAL B 103
SHEET 5 B10 THR B 149 LEU B 153 1 O THR B 149 N ILE B 130
SHEET 6 B10 SER B 174 PRO B 178 1 O ASN B 176 N LEU B 152
SHEET 7 B10 LYS B 203 TRP B 207 1 O VAL B 205 N VAL B 177
SHEET 8 B10 VAL B 229 ALA B 232 1 O VAL B 229 N LEU B 206
SHEET 9 B10 ILE B 8 HIS B 12 1 N LEU B 10 O VAL B 230
SHEET 10 B10 GLY B 37 LEU B 44 1 O GLU B 39 N GLY B 11
SHEET 1 C10 VAL C 50 VAL C 52 0
SHEET 2 C10 GLY C 37 LEU C 44 -1 N TRP C 43 O VAL C 51
SHEET 3 C10 LEU C 102 LEU C 107 1 O GLU C 106 N LEU C 40
SHEET 4 C10 VAL C 128 SER C 132 1 O SER C 131 N VAL C 105
SHEET 5 C10 THR C 149 LEU C 153 1 O GLY C 151 N ILE C 130
SHEET 6 C10 SER C 174 PRO C 178 1 O ASN C 176 N LEU C 152
SHEET 7 C10 LYS C 203 TRP C 207 1 O VAL C 205 N VAL C 177
SHEET 8 C10 VAL C 229 ALA C 232 1 O VAL C 229 N LEU C 206
SHEET 9 C10 ILE C 8 HIS C 12 1 N ILE C 8 O VAL C 230
SHEET 10 C10 GLY C 37 LEU C 44 1 O GLU C 39 N GLY C 11
SHEET 1 D10 VAL D 50 VAL D 52 0
SHEET 2 D10 GLY D 37 LEU D 44 -1 N TRP D 43 O VAL D 51
SHEET 3 D10 LEU D 102 LEU D 107 1 O GLU D 106 N LEU D 40
SHEET 4 D10 VAL D 128 SER D 132 1 O SER D 131 N LEU D 107
SHEET 5 D10 THR D 149 LEU D 153 1 O THR D 149 N ILE D 130
SHEET 6 D10 SER D 174 PRO D 178 1 O ASN D 176 N LEU D 152
SHEET 7 D10 LYS D 203 TRP D 207 1 O VAL D 205 N VAL D 177
SHEET 8 D10 VAL D 229 ALA D 232 1 O VAL D 229 N LEU D 206
SHEET 9 D10 ILE D 8 HIS D 12 1 N ILE D 8 O VAL D 230
SHEET 10 D10 GLY D 37 LEU D 44 1 O GLY D 37 N GLY D 11
LINK OE2 GLU A 39 MG MG A 401 1555 1555 2.12
LINK OD1 ASP A 41 MG MG A 401 1555 1555 2.10
LINK OE1 GLU A 106 MG MG A 401 1555 1555 1.91
LINK MG MG A 401 O HOH A 713 1555 1555 1.95
LINK MG MG A 401 O HOH A 718 1555 1555 2.16
LINK OE2 GLU B 39 MG MG B 401 1555 1555 1.99
LINK OD1 ASP B 41 MG MG B 401 1555 1555 2.01
LINK OE1 GLU B 106 MG MG B 401 1555 1555 1.91
LINK MG MG B 401 O HOH B 530 1555 1555 2.19
LINK MG MG B 401 O HOH B 570 1555 1555 2.22
LINK OE2 GLU C 39 MG MG C 401 1555 1555 2.01
LINK OD1 ASP C 41 MG MG C 401 1555 1555 1.92
LINK OE2 GLU C 106 MG MG C 401 1555 1555 1.91
LINK MG MG C 401 O HOH C 592 1555 1555 2.12
LINK MG MG C 401 O HOH C 606 1555 1555 2.15
LINK OE2 GLU D 39 MG MG D 401 1555 1555 2.00
LINK OD1 ASP D 41 MG MG D 401 1555 1555 2.16
LINK OE1 GLU D 106 MG MG D 401 1555 1555 2.00
LINK MG MG D 401 O HOH D 666 1555 1555 1.98
LINK MG MG D 401 O HOH D 672 1555 1555 2.11
SITE 1 AC1 5 GLU A 39 ASP A 41 GLU A 106 HOH A 713
SITE 2 AC1 5 HOH A 718
SITE 1 AC2 5 GLU B 39 ASP B 41 GLU B 106 HOH B 530
SITE 2 AC2 5 HOH B 570
SITE 1 AC3 5 GLU C 39 ASP C 41 GLU C 106 HOH C 592
SITE 2 AC3 5 HOH C 606
SITE 1 AC4 5 GLU D 39 ASP D 41 GLU D 106 HOH D 666
SITE 2 AC4 5 HOH D 672
CRYST1 43.724 132.034 171.639 90.00 90.00 90.00 P 21 21 21 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.022871 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007574 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005826 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
