HEADER PHOSPHOTRANSFERASE 29-DEC-95 4AKE
TITLE ADENYLATE KINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENYLATE KINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ATP\:AMP PHOSPHOTRANSFERASE, MYOKINASE;
COMPND 5 EC: 2.7.4.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 CELLULAR_LOCATION: CYTOSOL;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PAK601
KEYWDS NUCLEOSIDE MONOPHOSPHATE KINASE, ATP:AMP PHOSPHOTRANSFERASE,
KEYWDS 2 MYOKINASE, PHOSPHOTRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.J.SCHLAUDERER,G.E.SCHULZ
REVDAT 3 28-FEB-24 4AKE 1 REMARK
REVDAT 2 24-FEB-09 4AKE 1 VERSN
REVDAT 1 10-JUN-96 4AKE 0
JRNL AUTH C.W.MULLER,G.J.SCHLAUDERER,J.REINSTEIN,G.E.SCHULZ
JRNL TITL ADENYLATE KINASE MOTIONS DURING CATALYSIS: AN ENERGETIC
JRNL TITL 2 COUNTERWEIGHT BALANCING SUBSTRATE BINDING.
JRNL REF STRUCTURE V. 4 147 1996
JRNL REFN ISSN 0969-2126
JRNL PMID 8805521
JRNL DOI 10.1016/S0969-2126(96)00018-4
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.VONRHEIN,G.J.SCHLAUDERER,G.E.SCHULZ
REMARK 1 TITL MOVIE OF THE STRUCTURAL CHANGES DURING A CATALYTIC CYCLE OF
REMARK 1 TITL 2 NUCLEOSIDE MONOPHOSPHATE KINASES
REMARK 1 REF STRUCTURE V. 3 483 1995
REMARK 1 REFN ISSN 0969-2126
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.W.MULLER,G.E.SCHULZ
REMARK 1 TITL STRUCTURE OF THE COMPLEX BETWEEN ADENYLATE KINASE FROM
REMARK 1 TITL 2 ESCHERICHIA COLI AND THE INHIBITOR AP5A REFINED AT 1.9 A
REMARK 1 TITL 3 RESOLUTION. A MODEL FOR A CATALYTIC TRANSITION STATE
REMARK 1 REF J.MOL.BIOL. V. 224 159 1992
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 82.0
REMARK 3 NUMBER OF REFLECTIONS : 17932
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3312
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 147
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.700
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 4.400 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 6.400 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 6.600 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 9.600 ; 2.500
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4AKE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000179257.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 1991
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SIEMENS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17932
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 10.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 82.0
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 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 400
REMARK 400 COMPOUND
REMARK 400 THE SECONDARY STRUCTURAL ELEMENTS PRESENTED BELOW ARE FROM
REMARK 400 PROGRAM DSSP. FOR MANUAL ASSIGNMENTS PLEASE SEE THE
REMARK 400 PUBLICATION.
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 ILE A 72 1.30 -67.56
REMARK 500 SER A 129 -32.57 179.14
REMARK 500 VAL A 135 -34.61 -30.52
REMARK 500 LYS A 136 -60.64 -100.30
REMARK 500 PHE B 137 -101.77 -84.33
REMARK 500 VAL B 148 -80.36 -77.91
REMARK 500 GLU B 161 -37.64 -39.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 24 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4AKE A 1 214 UNP P69441 KAD_ECOLI 1 214
DBREF 4AKE B 1 214 UNP P69441 KAD_ECOLI 1 214
SEQRES 1 A 214 MET ARG ILE ILE LEU LEU GLY ALA PRO GLY ALA GLY LYS
SEQRES 2 A 214 GLY THR GLN ALA GLN PHE ILE MET GLU LYS TYR GLY ILE
SEQRES 3 A 214 PRO GLN ILE SER THR GLY ASP MET LEU ARG ALA ALA VAL
SEQRES 4 A 214 LYS SER GLY SER GLU LEU GLY LYS GLN ALA LYS ASP ILE
SEQRES 5 A 214 MET ASP ALA GLY LYS LEU VAL THR ASP GLU LEU VAL ILE
SEQRES 6 A 214 ALA LEU VAL LYS GLU ARG ILE ALA GLN GLU ASP CYS ARG
SEQRES 7 A 214 ASN GLY PHE LEU LEU ASP GLY PHE PRO ARG THR ILE PRO
SEQRES 8 A 214 GLN ALA ASP ALA MET LYS GLU ALA GLY ILE ASN VAL ASP
SEQRES 9 A 214 TYR VAL LEU GLU PHE ASP VAL PRO ASP GLU LEU ILE VAL
SEQRES 10 A 214 ASP ARG ILE VAL GLY ARG ARG VAL HIS ALA PRO SER GLY
SEQRES 11 A 214 ARG VAL TYR HIS VAL LYS PHE ASN PRO PRO LYS VAL GLU
SEQRES 12 A 214 GLY LYS ASP ASP VAL THR GLY GLU GLU LEU THR THR ARG
SEQRES 13 A 214 LYS ASP ASP GLN GLU GLU THR VAL ARG LYS ARG LEU VAL
SEQRES 14 A 214 GLU TYR HIS GLN MET THR ALA PRO LEU ILE GLY TYR TYR
SEQRES 15 A 214 SER LYS GLU ALA GLU ALA GLY ASN THR LYS TYR ALA LYS
SEQRES 16 A 214 VAL ASP GLY THR LYS PRO VAL ALA GLU VAL ARG ALA ASP
SEQRES 17 A 214 LEU GLU LYS ILE LEU GLY
SEQRES 1 B 214 MET ARG ILE ILE LEU LEU GLY ALA PRO GLY ALA GLY LYS
SEQRES 2 B 214 GLY THR GLN ALA GLN PHE ILE MET GLU LYS TYR GLY ILE
SEQRES 3 B 214 PRO GLN ILE SER THR GLY ASP MET LEU ARG ALA ALA VAL
SEQRES 4 B 214 LYS SER GLY SER GLU LEU GLY LYS GLN ALA LYS ASP ILE
SEQRES 5 B 214 MET ASP ALA GLY LYS LEU VAL THR ASP GLU LEU VAL ILE
SEQRES 6 B 214 ALA LEU VAL LYS GLU ARG ILE ALA GLN GLU ASP CYS ARG
SEQRES 7 B 214 ASN GLY PHE LEU LEU ASP GLY PHE PRO ARG THR ILE PRO
SEQRES 8 B 214 GLN ALA ASP ALA MET LYS GLU ALA GLY ILE ASN VAL ASP
SEQRES 9 B 214 TYR VAL LEU GLU PHE ASP VAL PRO ASP GLU LEU ILE VAL
SEQRES 10 B 214 ASP ARG ILE VAL GLY ARG ARG VAL HIS ALA PRO SER GLY
SEQRES 11 B 214 ARG VAL TYR HIS VAL LYS PHE ASN PRO PRO LYS VAL GLU
SEQRES 12 B 214 GLY LYS ASP ASP VAL THR GLY GLU GLU LEU THR THR ARG
SEQRES 13 B 214 LYS ASP ASP GLN GLU GLU THR VAL ARG LYS ARG LEU VAL
SEQRES 14 B 214 GLU TYR HIS GLN MET THR ALA PRO LEU ILE GLY TYR TYR
SEQRES 15 B 214 SER LYS GLU ALA GLU ALA GLY ASN THR LYS TYR ALA LYS
SEQRES 16 B 214 VAL ASP GLY THR LYS PRO VAL ALA GLU VAL ARG ALA ASP
SEQRES 17 B 214 LEU GLU LYS ILE LEU GLY
FORMUL 3 HOH *147(H2 O)
HELIX 1 1 LYS A 13 TYR A 24 5 12
HELIX 2 2 THR A 31 LYS A 40 1 10
HELIX 3 3 GLU A 44 ASP A 54 1 11
HELIX 4 4 ASP A 61 ALA A 73 1 13
HELIX 5 5 GLU A 75 CYS A 77 5 3
HELIX 6 6 ILE A 90 GLU A 98 1 9
HELIX 7 7 ASP A 113 VAL A 121 1 9
HELIX 8 8 GLU A 161 GLU A 187 1 27
HELIX 9 9 VAL A 202 LEU A 213 1 12
HELIX 10 10 LYS B 13 TYR B 24 5 12
HELIX 11 11 THR B 31 LYS B 40 1 10
HELIX 12 12 GLU B 44 ASP B 54 1 11
HELIX 13 13 ASP B 61 ALA B 73 1 13
HELIX 14 14 GLU B 75 CYS B 77 5 3
HELIX 15 15 ILE B 90 GLU B 98 1 9
HELIX 16 16 ASP B 113 VAL B 121 1 9
HELIX 17 17 LYS B 157 ASP B 159 5 3
HELIX 18 18 GLU B 161 ALA B 188 1 28
HELIX 19 19 VAL B 202 ILE B 212 1 11
SHEET 1 A 5 LYS A 192 ASP A 197 0
SHEET 2 A 5 TYR A 105 ASP A 110 1 N VAL A 106 O LYS A 192
SHEET 3 A 5 ARG A 2 GLY A 7 1 N ILE A 4 O TYR A 105
SHEET 4 A 5 PHE A 81 ASP A 84 1 N PHE A 81 O ILE A 3
SHEET 5 A 5 PRO A 27 ILE A 29 1 N PRO A 27 O LEU A 82
SHEET 1 B 2 ARG A 123 HIS A 126 0
SHEET 2 B 2 ARG A 131 HIS A 134 -1 N TYR A 133 O ARG A 124
SHEET 1 C 5 LYS B 192 ASP B 197 0
SHEET 2 C 5 TYR B 105 ASP B 110 1 N VAL B 106 O LYS B 192
SHEET 3 C 5 ARG B 2 GLY B 7 1 N ILE B 4 O TYR B 105
SHEET 4 C 5 PHE B 81 ASP B 84 1 N PHE B 81 O ILE B 3
SHEET 5 C 5 PRO B 27 ILE B 29 1 N PRO B 27 O LEU B 82
SHEET 1 D 2 ARG B 124 HIS B 126 0
SHEET 2 D 2 ARG B 131 TYR B 133 -1 N TYR B 133 O ARG B 124
CISPEP 1 PHE A 86 PRO A 87 0 0.62
CISPEP 2 PHE B 86 PRO B 87 0 0.07
CRYST1 31.800 54.500 71.300 67.70 77.90 88.40 P 1 2
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 0.031447 -0.000878 -0.006932 0.00000
SCALE2 0.000000 0.018356 -0.007593 0.00000
SCALE3 0.000000 0.000000 0.015523 0.00000
MTRIX1 1 0.999606 -0.012438 0.025179 0.88440 1
MTRIX2 1 -0.012961 -0.999702 0.020699 0.97090 1
MTRIX3 1 0.024914 -0.021017 -0.999469 1.34950 1
(ATOM LINES ARE NOT SHOWN.)
END
