HEADER TRANSFERASE 17-OCT-05 2C49
TITLE CRYSTAL STRUCTURE OF METHANOCALDOCOCCUS JANNASCHII NUCLEOSIDE KINASE -
TITLE 2 AN ARCHAEAL MEMBER OF THE RIBOKINASE FAMILY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUGAR KINASE MJ0406;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: NUCLEOSIDE KINASE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOCOCCUS JANNASCHII;
SOURCE 3 ORGANISM_TAXID: 2190;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET17B;
SOURCE 8 OTHER_DETAILS: METHANOCALDOCOCCUS JANNASCHII
KEYWDS TRANSFERASE, NUCLEOSIDE KINASE, HYPERTHERMOPHILE, RIBOKINASE FAMILY,
KEYWDS 2 RIBOKINASE FOLD
EXPDTA X-RAY DIFFRACTION
AUTHOR L.ARNFORS,T.HANSEN,W.MEINING,P.SCHOENHEIT,R.LADENSTEIN
REVDAT 4 24-JUL-19 2C49 1 REMARK
REVDAT 3 13-JUL-11 2C49 1 VERSN
REVDAT 2 24-FEB-09 2C49 1 VERSN
REVDAT 1 30-AUG-06 2C49 0
JRNL AUTH L.ARNFORS,T.HANSEN,P.SCHOENHEIT,R.LADENSTEIN,W.MEINING
JRNL TITL STRUCTURE OF METHANOCALDOCOCCUS JANNASCHII NUCLEOSIDE
JRNL TITL 2 KINASE: AN ARCHAEAL MEMBER OF THE RIBOKINASE FAMILY.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 62 1085 2006
JRNL REFN ISSN 0907-4449
JRNL PMID 16929110
JRNL DOI 10.1107/S0907444906024826
REMARK 2
REMARK 2 RESOLUTION. 1.92 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 1.92
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 72.55
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 55509
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) : 0.245
REMARK 3 R VALUE (WORKING SET) : 0.243
REMARK 3 FREE R VALUE : 0.281
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2955
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) : 1.92
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.97
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3739
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2960
REMARK 3 BIN FREE R VALUE SET COUNT : 193
REMARK 3 BIN FREE R VALUE : 0.3360
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4731
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 104
REMARK 3 SOLVENT ATOMS : 162
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.37
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.39000
REMARK 3 B22 (A**2) : 1.26000
REMARK 3 B33 (A**2) : -1.64000
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): 0.181
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.167
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.111
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.803
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.916
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.891
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4982 ; 0.016 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6777 ; 1.700 ; 1.988
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 596 ; 7.538 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 727 ; 0.116 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3749 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2331 ; 0.211 ; 0.200
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): 219 ; 0.159 ; 0.200
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): 35 ; 0.196 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 12 ; 0.128 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2971 ; 0.758 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4782 ; 1.264 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2011 ; 2.072 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1988 ; 2.989 ; 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 6 A 15 4
REMARK 3 1 B 6 B 15 4
REMARK 3 2 A 42 A 97 4
REMARK 3 2 B 42 B 97 4
REMARK 3 3 A 115 A 297 4
REMARK 3 3 B 115 B 297 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1924 ; 0.44 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1924 ; 1.15 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 3 A 15
REMARK 3 RESIDUE RANGE : A 41 A 98
REMARK 3 RESIDUE RANGE : A 114 A 301
REMARK 3 ORIGIN FOR THE GROUP (A): 71.3506 22.8581 60.6100
REMARK 3 T TENSOR
REMARK 3 T11: 0.0194 T22: 0.0105
REMARK 3 T33: 0.0655 T12: 0.0081
REMARK 3 T13: -0.0077 T23: 0.0178
REMARK 3 L TENSOR
REMARK 3 L11: 2.4540 L22: 1.8679
REMARK 3 L33: 2.9687 L12: -0.6070
REMARK 3 L13: 0.4665 L23: 0.2769
REMARK 3 S TENSOR
REMARK 3 S11: 0.0232 S12: 0.1163 S13: 0.0207
REMARK 3 S21: -0.0744 S22: -0.0954 S23: 0.0044
REMARK 3 S31: -0.0685 S32: 0.1282 S33: 0.0722
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 16 A 40
REMARK 3 RESIDUE RANGE : A 99 A 113
REMARK 3 ORIGIN FOR THE GROUP (A): 71.3457 30.0739 39.1974
REMARK 3 T TENSOR
REMARK 3 T11: 0.2009 T22: 0.1518
REMARK 3 T33: 0.1783 T12: -0.0200
REMARK 3 T13: -0.0427 T23: 0.0435
REMARK 3 L TENSOR
REMARK 3 L11: 0.3299 L22: 3.3372
REMARK 3 L33: 5.4807 L12: -0.0792
REMARK 3 L13: -0.2342 L23: -1.2037
REMARK 3 S TENSOR
REMARK 3 S11: -0.0367 S12: 0.2361 S13: 0.3473
REMARK 3 S21: -0.0043 S22: -0.0586 S23: -0.3196
REMARK 3 S31: -0.5942 S32: 0.4290 S33: 0.0952
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 3 B 15
REMARK 3 RESIDUE RANGE : B 41 B 98
REMARK 3 RESIDUE RANGE : B 114 B 300
REMARK 3 ORIGIN FOR THE GROUP (A): 58.8280 23.9438 12.0094
REMARK 3 T TENSOR
REMARK 3 T11: 0.0913 T22: 0.0335
REMARK 3 T33: 0.0978 T12: 0.0067
REMARK 3 T13: -0.0052 T23: -0.0352
REMARK 3 L TENSOR
REMARK 3 L11: 1.7338 L22: 1.8826
REMARK 3 L33: 2.1245 L12: -0.1658
REMARK 3 L13: 0.3188 L23: -0.8849
REMARK 3 S TENSOR
REMARK 3 S11: -0.0040 S12: -0.1607 S13: 0.1099
REMARK 3 S21: -0.0860 S22: 0.0569 S23: 0.1399
REMARK 3 S31: -0.0371 S32: -0.0957 S33: -0.0529
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 16 B 40
REMARK 3 RESIDUE RANGE : B 99 B 113
REMARK 3 ORIGIN FOR THE GROUP (A): 59.5180 30.8366 38.0425
REMARK 3 T TENSOR
REMARK 3 T11: 0.2495 T22: 0.1168
REMARK 3 T33: 0.1516 T12: 0.0793
REMARK 3 T13: -0.0234 T23: 0.0218
REMARK 3 L TENSOR
REMARK 3 L11: 1.6212 L22: 1.5116
REMARK 3 L33: 6.1729 L12: 0.6396
REMARK 3 L13: 0.6430 L23: 1.5639
REMARK 3 S TENSOR
REMARK 3 S11: -0.0963 S12: 0.1594 S13: 0.3241
REMARK 3 S21: 0.0615 S22: -0.0025 S23: 0.1671
REMARK 3 S31: -0.5116 S32: -0.4866 S33: 0.0988
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.
REMARK 4
REMARK 4 2C49 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-OCT-05.
REMARK 100 THE DEPOSITION ID IS D_1290026013.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8098
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58526
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.930
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 13.70
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG4000, 0.10 M MGCL2, 0.1 M TRIS
REMARK 280 -HCL PH 8.5
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 32.00300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 73.39200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.56550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 73.39200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.00300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.56550
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 2
REMARK 465 ILE A 302
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 ARG B 301
REMARK 465 ILE B 302
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 202 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 209 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP B 68 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP B 140 CB - CG - OD2 ANGL. DEV. = 5.5 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 LYS A 4 -11.89 -148.75
REMARK 500 ASN A 29 49.07 71.86
REMARK 500 ASP A 68 58.44 -90.80
REMARK 500 PHE A 69 -60.84 -142.66
REMARK 500 ASN A 107 29.69 45.60
REMARK 500 THR A 138 -169.98 60.63
REMARK 500 ASN A 154 -70.63 -124.98
REMARK 500 LYS A 238 102.66 54.78
REMARK 500 LYS B 4 -31.12 -141.14
REMARK 500 GLU B 6 79.76 -60.11
REMARK 500 SER B 72 -150.49 -84.85
REMARK 500 ALA B 137 -164.12 -112.06
REMARK 500 ASN B 154 -64.81 -128.31
REMARK 500 LYS B 238 124.78 -177.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PHE B 69 LYS B 70 -97.70
REMARK 500 LYS B 70 ASN B 71 147.32
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 A1302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2046 O
REMARK 620 2 HOH A2056 O 90.5
REMARK 620 3 HOH A2057 O 90.7 87.4
REMARK 620 4 HOH A2066 O 88.8 88.3 175.7
REMARK 620 5 HOH A2077 O 90.9 177.8 94.2 90.1
REMARK 620 6 HOH A2079 O 177.9 91.3 90.6 90.0 87.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1303 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2054 O
REMARK 620 2 HOH A2018 O 91.9
REMARK 620 3 HOH A2019 O 177.6 89.4
REMARK 620 4 HOH A2042 O 91.5 89.2 86.5
REMARK 620 5 HOH A2021 O 85.1 91.4 96.8 176.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B2014 O
REMARK 620 2 HOH B2082 O 90.7
REMARK 620 3 HOH B2041 O 89.7 179.2
REMARK 620 4 HOH B2081 O 179.8 89.5 90.1
REMARK 620 5 HOH B2053 O 90.5 88.0 91.3 89.5
REMARK 620 6 HOH B2040 O 90.0 90.5 90.2 90.0 178.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1303 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B2036 O
REMARK 620 2 HOH B2048 O 91.8
REMARK 620 3 HOH B2059 O 88.5 92.1
REMARK 620 4 HOH B2058 O 178.2 86.4 91.5
REMARK 620 5 HOH B2078 O 91.0 177.0 87.2 90.7
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 A1302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B1302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B1303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADN A1301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A1304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADN B1301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP B1304
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2C4E RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF METHANOCALDOCOCCUS JANNASCHII NUCLEOSIDE
REMARK 900 KINASE - AN ARCHAEAL MEMBER OF THE RIBOKINASE FAMILY
DBREF 2C49 A 1 302 UNP Q57849 Y406_METJA 1 302
DBREF 2C49 B 1 302 UNP Q57849 Y406_METJA 1 302
SEQRES 1 A 302 MET GLY GLY LYS MET GLU LYS ILE THR CYS VAL GLY HIS
SEQRES 2 A 302 THR ALA LEU ASP TYR ILE PHE ASN VAL GLU LYS PHE PRO
SEQRES 3 A 302 GLU PRO ASN THR SER ILE GLN ILE PRO SER ALA ARG LYS
SEQRES 4 A 302 TYR TYR GLY GLY ALA ALA ALA ASN THR ALA VAL GLY ILE
SEQRES 5 A 302 LYS LYS LEU GLY VAL ASN SER GLU LEU LEU SER CYS VAL
SEQRES 6 A 302 GLY TYR ASP PHE LYS ASN SER GLY TYR GLU ARG TYR LEU
SEQRES 7 A 302 LYS ASN LEU ASP ILE ASN ILE SER LYS LEU TYR TYR SER
SEQRES 8 A 302 GLU GLU GLU GLU THR PRO LYS ALA TRP ILE PHE THR ASP
SEQRES 9 A 302 LYS ASP ASN ASN GLN ILE THR PHE PHE LEU TRP GLY ALA
SEQRES 10 A 302 ALA LYS HIS TYR LYS GLU LEU ASN PRO PRO ASN PHE ASN
SEQRES 11 A 302 THR GLU ILE VAL HIS ILE ALA THR GLY ASP PRO GLU PHE
SEQRES 12 A 302 ASN LEU LYS CYS ALA LYS LYS ALA TYR GLY ASN ASN LEU
SEQRES 13 A 302 VAL SER PHE ASP PRO GLY GLN ASP LEU PRO GLN TYR SER
SEQRES 14 A 302 LYS GLU MET LEU LEU GLU ILE ILE GLU HIS THR ASN PHE
SEQRES 15 A 302 LEU PHE MET ASN LYS HIS GLU PHE GLU ARG ALA SER ASN
SEQRES 16 A 302 LEU LEU ASN PHE GLU ILE ASP ASP TYR LEU GLU ARG VAL
SEQRES 17 A 302 ASP ALA LEU ILE VAL THR LYS GLY SER LYS GLY SER VAL
SEQRES 18 A 302 ILE TYR THR LYS ASP LYS LYS ILE GLU ILE PRO CYS ILE
SEQRES 19 A 302 LYS ALA GLY LYS VAL ILE ASP PRO THR GLY ALA GLY ASP
SEQRES 20 A 302 SER TYR ARG ALA GLY PHE LEU SER ALA TYR VAL LYS GLY
SEQRES 21 A 302 TYR ASP LEU GLU LYS CYS GLY LEU ILE GLY ALA ALA THR
SEQRES 22 A 302 ALA SER PHE VAL VAL GLU ALA LYS GLY CYS GLN THR ASN
SEQRES 23 A 302 LEU PRO THR TRP ASP LYS VAL VAL GLU ARG LEU GLU LYS
SEQRES 24 A 302 HIS ARG ILE
SEQRES 1 B 302 MET GLY GLY LYS MET GLU LYS ILE THR CYS VAL GLY HIS
SEQRES 2 B 302 THR ALA LEU ASP TYR ILE PHE ASN VAL GLU LYS PHE PRO
SEQRES 3 B 302 GLU PRO ASN THR SER ILE GLN ILE PRO SER ALA ARG LYS
SEQRES 4 B 302 TYR TYR GLY GLY ALA ALA ALA ASN THR ALA VAL GLY ILE
SEQRES 5 B 302 LYS LYS LEU GLY VAL ASN SER GLU LEU LEU SER CYS VAL
SEQRES 6 B 302 GLY TYR ASP PHE LYS ASN SER GLY TYR GLU ARG TYR LEU
SEQRES 7 B 302 LYS ASN LEU ASP ILE ASN ILE SER LYS LEU TYR TYR SER
SEQRES 8 B 302 GLU GLU GLU GLU THR PRO LYS ALA TRP ILE PHE THR ASP
SEQRES 9 B 302 LYS ASP ASN ASN GLN ILE THR PHE PHE LEU TRP GLY ALA
SEQRES 10 B 302 ALA LYS HIS TYR LYS GLU LEU ASN PRO PRO ASN PHE ASN
SEQRES 11 B 302 THR GLU ILE VAL HIS ILE ALA THR GLY ASP PRO GLU PHE
SEQRES 12 B 302 ASN LEU LYS CYS ALA LYS LYS ALA TYR GLY ASN ASN LEU
SEQRES 13 B 302 VAL SER PHE ASP PRO GLY GLN ASP LEU PRO GLN TYR SER
SEQRES 14 B 302 LYS GLU MET LEU LEU GLU ILE ILE GLU HIS THR ASN PHE
SEQRES 15 B 302 LEU PHE MET ASN LYS HIS GLU PHE GLU ARG ALA SER ASN
SEQRES 16 B 302 LEU LEU ASN PHE GLU ILE ASP ASP TYR LEU GLU ARG VAL
SEQRES 17 B 302 ASP ALA LEU ILE VAL THR LYS GLY SER LYS GLY SER VAL
SEQRES 18 B 302 ILE TYR THR LYS ASP LYS LYS ILE GLU ILE PRO CYS ILE
SEQRES 19 B 302 LYS ALA GLY LYS VAL ILE ASP PRO THR GLY ALA GLY ASP
SEQRES 20 B 302 SER TYR ARG ALA GLY PHE LEU SER ALA TYR VAL LYS GLY
SEQRES 21 B 302 TYR ASP LEU GLU LYS CYS GLY LEU ILE GLY ALA ALA THR
SEQRES 22 B 302 ALA SER PHE VAL VAL GLU ALA LYS GLY CYS GLN THR ASN
SEQRES 23 B 302 LEU PRO THR TRP ASP LYS VAL VAL GLU ARG LEU GLU LYS
SEQRES 24 B 302 HIS ARG ILE
HET ADN A1301 19
HET MG A1302 1
HET MG A1303 1
HET ANP A1304 31
HET ADN B1301 19
HET MG B1302 1
HET MG B1303 1
HET ANP B1304 31
HETNAM ADN ADENOSINE
HETNAM MG MAGNESIUM ION
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
FORMUL 3 ADN 2(C10 H13 N5 O4)
FORMUL 4 MG 4(MG 2+)
FORMUL 6 ANP 2(C10 H17 N6 O12 P3)
FORMUL 11 HOH *162(H2 O)
HELIX 1 1 GLY A 43 LEU A 55 1 13
HELIX 2 2 SER A 72 LEU A 81 1 10
HELIX 3 3 GLY A 116 LEU A 124 5 9
HELIX 4 4 ASP A 140 TYR A 152 1 13
HELIX 5 5 PRO A 161 TYR A 168 5 8
HELIX 6 6 SER A 169 GLU A 178 1 10
HELIX 7 7 ASN A 186 ASN A 198 1 13
HELIX 8 8 GLU A 200 GLU A 206 1 7
HELIX 9 9 GLY A 216 LYS A 218 5 3
HELIX 10 10 GLY A 244 LYS A 259 1 16
HELIX 11 11 ASP A 262 VAL A 278 1 17
HELIX 12 12 THR A 289 HIS A 300 1 12
HELIX 13 13 GLY B 43 LEU B 55 1 13
HELIX 14 14 SER B 72 LEU B 81 1 10
HELIX 15 15 GLY B 116 LEU B 124 5 9
HELIX 16 16 ASP B 140 TYR B 152 1 13
HELIX 17 17 PRO B 161 TYR B 168 5 8
HELIX 18 18 SER B 169 HIS B 179 1 11
HELIX 19 19 LYS B 187 ASN B 198 1 12
HELIX 20 20 GLU B 200 GLU B 206 1 7
HELIX 21 21 GLY B 216 LYS B 218 5 3
HELIX 22 22 GLY B 244 LYS B 259 1 16
HELIX 23 23 ASP B 262 VAL B 278 1 17
HELIX 24 24 THR B 289 HIS B 300 1 12
SHEET 1 AA 8 ASN A 58 LEU A 62 0
SHEET 2 AA 8 MET A 5 VAL A 11 1 O GLU A 6 N ASN A 58
SHEET 3 AA 8 THR A 131 ALA A 137 1 N GLU A 132 O MET A 5
SHEET 4 AA 8 LEU A 156 ASP A 160 1 O LEU A 156 N VAL A 134
SHEET 5 AA 8 PHE A 182 MET A 185 1 O PHE A 182 N PHE A 159
SHEET 6 AA 8 ALA A 210 THR A 214 1 O ALA A 210 N LEU A 183
SHEET 7 AA 8 SER A 220 TYR A 223 -1 O VAL A 221 N VAL A 213
SHEET 8 AA 8 LYS A 228 ILE A 231 -1 O ILE A 229 N ILE A 222
SHEET 1 AB 5 LYS A 39 GLY A 42 0
SHEET 2 AB 5 ALA A 15 ASN A 21 -1 O ALA A 15 N GLY A 42
SHEET 3 AB 5 LYS A 98 THR A 103 1 O ALA A 99 N TYR A 18
SHEET 4 AB 5 GLN A 109 LEU A 114 -1 O ILE A 110 N PHE A 102
SHEET 5 AB 5 SER B 31 ILE B 34 1 O ILE B 32 N PHE A 113
SHEET 1 AC 5 THR A 30 ILE A 34 0
SHEET 2 AC 5 GLN B 109 LEU B 114 1 O THR B 111 N ILE A 32
SHEET 3 AC 5 LYS B 98 THR B 103 -1 O LYS B 98 N LEU B 114
SHEET 4 AC 5 ALA B 15 ASN B 21 1 O LEU B 16 N ALA B 99
SHEET 5 AC 5 ARG B 38 GLY B 42 -1 O ARG B 38 N ILE B 19
SHEET 1 AD 2 CYS A 64 VAL A 65 0
SHEET 2 AD 2 TYR A 89 TYR A 90 1 O TYR A 89 N VAL A 65
SHEET 1 BA 8 ASN B 58 LEU B 62 0
SHEET 2 BA 8 MET B 5 VAL B 11 1 O GLU B 6 N ASN B 58
SHEET 3 BA 8 THR B 131 ILE B 136 1 N GLU B 132 O LYS B 7
SHEET 4 BA 8 LEU B 156 PHE B 159 1 O LEU B 156 N VAL B 134
SHEET 5 BA 8 PHE B 182 ASN B 186 1 O PHE B 182 N PHE B 159
SHEET 6 BA 8 ALA B 210 THR B 214 1 O ALA B 210 N LEU B 183
SHEET 7 BA 8 SER B 220 TYR B 223 -1 O VAL B 221 N VAL B 213
SHEET 8 BA 8 LYS B 228 ILE B 231 -1 O ILE B 229 N ILE B 222
SHEET 1 BB 2 CYS B 64 VAL B 65 0
SHEET 2 BB 2 TYR B 89 TYR B 90 1 O TYR B 89 N VAL B 65
LINK MG MG A1302 O HOH A2046 1555 1555 2.16
LINK MG MG A1302 O HOH A2056 1555 1555 2.15
LINK MG MG A1302 O HOH A2057 1555 1555 2.17
LINK MG MG A1302 O HOH A2066 1555 1555 2.18
LINK MG MG A1302 O HOH A2077 1555 1555 2.18
LINK MG MG A1302 O HOH A2079 1555 1555 2.15
LINK MG MG A1303 O HOH A2054 1555 1555 2.16
LINK MG MG A1303 O HOH A2018 1555 1555 2.19
LINK MG MG A1303 O HOH A2019 1555 1555 2.18
LINK MG MG A1303 O HOH A2042 1555 1555 2.16
LINK MG MG A1303 O HOH A2021 1555 1555 2.18
LINK MG MG B1302 O HOH B2014 1555 1555 2.18
LINK MG MG B1302 O HOH B2082 1555 1555 2.17
LINK MG MG B1302 O HOH B2041 1555 1555 2.17
LINK MG MG B1302 O HOH B2081 1555 1555 2.17
LINK MG MG B1302 O HOH B2053 1555 1555 2.18
LINK MG MG B1302 O HOH B2040 1555 1555 2.18
LINK MG MG B1303 O HOH B2036 1555 1555 2.19
LINK MG MG B1303 O HOH B2048 1555 1555 2.17
LINK MG MG B1303 O HOH B2059 1555 1555 2.17
LINK MG MG B1303 O HOH B2058 1555 1555 2.17
LINK MG MG B1303 O HOH B2078 1555 4555 2.19
SITE 1 AC1 6 HOH A2046 HOH A2056 HOH A2057 HOH A2066
SITE 2 AC1 6 HOH A2077 HOH A2079
SITE 1 AC2 5 HOH A2018 HOH A2019 HOH A2021 HOH A2042
SITE 2 AC2 5 HOH A2054
SITE 1 AC3 6 HOH B2014 HOH B2040 HOH B2041 HOH B2053
SITE 2 AC3 6 HOH B2081 HOH B2082
SITE 1 AC4 5 HOH B2036 HOH B2048 HOH B2058 HOH B2059
SITE 2 AC4 5 HOH B2078
SITE 1 AC5 16 HIS A 13 ALA A 15 ASP A 17 GLY A 42
SITE 2 AC5 16 GLY A 43 ASN A 47 THR A 111 PHE A 113
SITE 3 AC5 16 GLN A 163 ASP A 164 ASP A 247 CYS A 283
SITE 4 AC5 16 HOH A2077 HOH A2078 SER B 31 GLN B 33
SITE 1 AC6 16 GLN A 109 ASN A 186 THR A 214 GLY A 216
SITE 2 AC6 16 GLY A 219 CYS A 233 ILE A 234 VAL A 239
SITE 3 AC6 16 THR A 243 ALA A 245 GLY A 246 ALA A 274
SITE 4 AC6 16 HOH A2062 HOH A2072 HOH A2079 HOH A2080
SITE 1 AC7 7 HIS B 13 ALA B 15 ASP B 17 GLY B 42
SITE 2 AC7 7 GLY B 43 ALA B 44 HOH B2080
SITE 1 AC8 19 ASN B 186 THR B 214 LYS B 215 GLY B 216
SITE 2 AC8 19 GLY B 219 CYS B 233 ILE B 234 VAL B 239
SITE 3 AC8 19 PRO B 242 THR B 243 GLY B 244 ALA B 245
SITE 4 AC8 19 GLY B 246 TYR B 249 ARG B 250 ALA B 274
SITE 5 AC8 19 HOH B2060 HOH B2081 HOH B2082
CRYST1 64.006 83.131 146.784 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.015624 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012029 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006813 0.00000
MTRIX1 1 -0.996080 0.032971 0.082070 130.16000 1
MTRIX2 1 0.023822 0.993640 -0.110060 -1.78790 1
MTRIX3 1 -0.085177 -0.107670 -0.990530 70.50800 1
(ATOM LINES ARE NOT SHOWN.)
END