HEADER SIGNALING PROTEIN 16-APR-03 1P2S
TITLE H-RAS 166 IN 50% 2,2,2 TRIFLOUROETHANOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSFORMING PROTEIN P21/H-RAS-1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: C-H-RAS;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HRAS OR HRAS1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: JM105;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PAT
KEYWDS MOLECULAR SWITCH PROTEIN, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR G.K.BUHRMAN,V.DE SERRANO,C.MATTOS
REVDAT 3 16-AUG-23 1P2S 1 REMARK LINK
REVDAT 2 24-FEB-09 1P2S 1 VERSN
REVDAT 1 05-AUG-03 1P2S 0
JRNL AUTH G.K.BUHRMAN,V.DE SERRANO,C.MATTOS
JRNL TITL ORGANIC SOLVENTS ORDER THE DYNAMIC SWITCH II IN RAS CRYSTALS
JRNL REF STRUCTURE V. 11 747 2003
JRNL REFN ISSN 0969-2126
JRNL PMID 12842038
JRNL DOI 10.1016/S0969-2126(03)00128-X
REMARK 2
REMARK 2 RESOLUTION. 2.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.56
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 478909.450
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.2
REMARK 3 NUMBER OF REFLECTIONS : 5814
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 SET) : 0.188
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 11.100
REMARK 3 FREE R VALUE TEST SET COUNT : 648
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.009
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.60
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 809
REMARK 3 BIN R VALUE (WORKING SET) : 0.2510
REMARK 3 BIN FREE R VALUE : 0.3450
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 11.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 101
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.034
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1323
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 39
REMARK 3 SOLVENT ATOMS : 35
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.65000
REMARK 3 B22 (A**2) : 0.65000
REMARK 3 B33 (A**2) : -1.31000
REMARK 3 B12 (A**2) : 2.40000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.29
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.35
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.38
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.670
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.380 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.360 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.390 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.420 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.29
REMARK 3 BSOL : 25.76
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : LIGAND.PARAM
REMARK 3 PARAMETER FILE 3 : WATER.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : ION.TOP
REMARK 3 TOPOLOGY FILE 3 : LIGAND.TOP
REMARK 3 TOPOLOGY FILE 4 : WATER.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1P2S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018939.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 273
REMARK 200 PH : 7.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : ELLIOTT GX-13
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : OSMICS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8311
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.190
REMARK 200 RESOLUTION RANGE LOW (A) : 29.290
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 121P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG, MAGNESIUM CHLORIDE,
REMARK 280 DITHIOTHREITOL, PH 7.6, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-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 107.55333
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 53.77667
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 53.77667
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 107.55333
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 300 REMARK: THE BIOLOGICAL UNIT IS A MONOMER
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 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 HIS A 27 145.32 -175.29
REMARK 500 ASP A 30 42.15 -92.57
REMARK 500 ASP A 33 72.40 -161.59
REMARK 500 GLU A 37 114.21 -170.01
REMARK 500 GLU A 63 -14.58 -31.89
REMARK 500 TYR A 64 43.91 -102.62
REMARK 500 ALA A 66 -61.06 -94.92
REMARK 500 MET A 67 7.20 -63.28
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 168 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 17 OG
REMARK 620 2 THR A 35 OG1 79.9
REMARK 620 3 GNP A 167 O2G 166.2 86.4
REMARK 620 4 GNP A 167 O2B 100.1 175.9 93.7
REMARK 620 5 HOH A 230 O 85.7 90.2 92.3 93.9
REMARK 620 6 HOH A 231 O 82.9 84.3 97.8 91.7 168.1
REMARK 620 N 1 2 3 4 5
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 168
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP A 167
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ETF A 400
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1P2T RELATED DB: PDB
REMARK 900 H-RAS 166 IN AQUEOUS MOTHER LIQOUR, RT
REMARK 900 RELATED ID: 1P2U RELATED DB: PDB
REMARK 900 H-RAS IN 50% ISOPROPANOL
REMARK 900 RELATED ID: 1P2V RELATED DB: PDB
REMARK 900 H-RAS 166 IN 60 % 1,6 HEXANEDIOL
DBREF 1P2S A 1 166 UNP P01112 RASH_HUMAN 1 166
SEQRES 1 A 166 MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA GLY GLY
SEQRES 2 A 166 VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN ASN
SEQRES 3 A 166 HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP SER
SEQRES 4 A 166 TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR CYS LEU
SEQRES 5 A 166 LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU TYR SER
SEQRES 6 A 166 ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY PHE
SEQRES 7 A 166 LEU CYS VAL PHE ALA ILE ASN ASN THR LYS SER PHE GLU
SEQRES 8 A 166 ASP ILE HIS GLN TYR ARG GLU GLN ILE LYS ARG VAL LYS
SEQRES 9 A 166 ASP SER ASP ASP VAL PRO MET VAL LEU VAL GLY ASN LYS
SEQRES 10 A 166 CYS ASP LEU ALA ALA ARG THR VAL GLU SER ARG GLN ALA
SEQRES 11 A 166 GLN ASP LEU ALA ARG SER TYR GLY ILE PRO TYR ILE GLU
SEQRES 12 A 166 THR SER ALA LYS THR ARG GLN GLY VAL GLU ASP ALA PHE
SEQRES 13 A 166 TYR THR LEU VAL ARG GLU ILE ARG GLN HIS
HET MG A 168 1
HET GNP A 167 32
HET ETF A 400 6
HETNAM MG MAGNESIUM ION
HETNAM GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER
HETNAM ETF TRIFLUOROETHANOL
FORMUL 2 MG MG 2+
FORMUL 3 GNP C10 H17 N6 O13 P3
FORMUL 4 ETF C2 H3 F3 O
FORMUL 5 HOH *35(H2 O)
HELIX 1 1 GLY A 15 ASN A 26 1 12
HELIX 2 2 ALA A 66 GLY A 75 1 10
HELIX 3 3 ASN A 86 ASP A 105 1 20
HELIX 4 4 GLU A 126 GLY A 138 1 13
HELIX 5 5 GLY A 151 HIS A 166 1 16
SHEET 1 A 6 GLU A 37 ILE A 46 0
SHEET 2 A 6 GLU A 49 THR A 58 -1 O ILE A 55 N TYR A 40
SHEET 3 A 6 THR A 2 VAL A 9 1 N TYR A 4 O ASP A 54
SHEET 4 A 6 GLY A 77 ALA A 83 1 O LEU A 79 N VAL A 7
SHEET 5 A 6 MET A 111 ASN A 116 1 O VAL A 114 N CYS A 80
SHEET 6 A 6 TYR A 141 GLU A 143 1 O ILE A 142 N LEU A 113
LINK OG SER A 17 MG MG A 168 1555 1555 2.16
LINK OG1 THR A 35 MG MG A 168 1555 1555 2.17
LINK O2G GNP A 167 MG MG A 168 1555 1555 2.30
LINK O2B GNP A 167 MG MG A 168 1555 1555 2.19
LINK MG MG A 168 O HOH A 230 1555 1555 2.18
LINK MG MG A 168 O HOH A 231 1555 1555 2.17
SITE 1 AC1 5 SER A 17 THR A 35 GNP A 167 HOH A 230
SITE 2 AC1 5 HOH A 231
SITE 1 AC2 26 GLY A 12 GLY A 13 VAL A 14 GLY A 15
SITE 2 AC2 26 LYS A 16 SER A 17 ALA A 18 PHE A 28
SITE 3 AC2 26 VAL A 29 ASP A 30 TYR A 32 PRO A 34
SITE 4 AC2 26 THR A 35 GLY A 60 ASN A 116 LYS A 117
SITE 5 AC2 26 ASP A 119 LEU A 120 SER A 145 ALA A 146
SITE 6 AC2 26 LYS A 147 MG A 168 HOH A 204 HOH A 207
SITE 7 AC2 26 HOH A 225 HOH A 231
SITE 1 AC3 3 ARG A 97 LYS A 101 ASP A 107
CRYST1 40.330 40.330 161.330 90.00 90.00 120.00 P 32 2 1 6
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 0.024795 0.014316 0.000000 0.00000
SCALE2 0.000000 0.028631 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006198 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
