HEADER SH3 DOMAIN 24-AUG-04 1W6X
TITLE SH3 DOMAIN OF P40PHOX, COMPONENT OF THE NADPH OXIDASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUTROPHIL CYTOSOL FACTOR 4;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: SH3 DOMAIN, RESIDUES 174-228;
COMPND 5 SYNONYM: NCF-4, NEUTROPHIL NADPH OXIDASE FACTOR 4, P40PHOX, P40-PHOX;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELL: NEUTROPHILE;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PIVEX2.4
KEYWDS NADPH OXIDASE, P40PHOX, PHAGOCYTE, SH3 DOMAIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.MASSENET,S.CHENAVAS,C.COHEN-ADDAD,M.-C.DAGHER,G.BRANDOLIN,E.PEBAY-
AUTHOR 2 PEYROULA,F.FIESCHI
REVDAT 6 08-MAY-19 1W6X 1 REMARK
REVDAT 5 06-MAR-19 1W6X 1 REMARK
REVDAT 4 13-JUN-18 1W6X 1 JRNL
REVDAT 3 24-FEB-09 1W6X 1 VERSN
REVDAT 2 04-APR-05 1W6X 1 JRNL
REVDAT 1 18-JAN-05 1W6X 0
JRNL AUTH C.MASSENET,S.CHENAVAS,C.COHEN-ADDAD,M.-C.DAGHER,G.BRANDOLIN,
JRNL AUTH 2 E.PEBAY-PEYROULA,F.FIESCHI
JRNL TITL EFFECTS OF P47PHOX C-TERMINUS PHOSPHORYLATION ON BINDING
JRNL TITL 2 INTERACTIONS WITH P40PHOX AND P67PHOX: STRUCTURAL AND
JRNL TITL 3 FUNCTIONAL COMPARISON OF P40PHOX P67PHOX SH3 DOMAINS
JRNL REF J.BIOL.CHEM. V. 280 13752 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15657040
JRNL DOI 10.1074/JBC.M412897200
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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 : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 6871
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) : 0.248
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 356
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 : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.07
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 607
REMARK 3 BIN R VALUE (WORKING SET) : 0.3511
REMARK 3 BIN FREE R VALUE : 0.4380
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.36
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 45
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 : 882
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 61
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.93
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.41700
REMARK 3 B22 (A**2) : 4.57900
REMARK 3 B33 (A**2) : -4.16200
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 11.02800
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.32
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) : 0.40
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.47
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.302
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.37
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.777
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) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 49.00
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 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1W6X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-AUG-04.
REMARK 100 THE DEPOSITION ID IS D_1290020869.
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) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NONIUS
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : CCP4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6876
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 3.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.27000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
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: THE STARTING MODEL CONSISTED OF A SUPERPOSITION OF 8 SH3
REMARK 200 STRUCTURES 1SEM, 1SHG, 1ABQ, 1FYN, 1I0C,1B07, 1BB9, 1BU1 USING
REMARK 200 MAIN CHAIN ATOMS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION AT 14 DEGRE C, PROTEIN
REMARK 280 AT 14 MG/ML, 20 MM HEPES PH 7.5, 150 MM NACL MIXED WITH 40%
REMARK 280 PEG2K MME, 100 MM AS 200 MM NA AC PH 4.6., TEMPERATURE 287K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 22.58000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: PQS
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: PQS
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 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 LEU A 169
REMARK 465 ILE A 170
REMARK 465 LYS A 171
REMARK 465 HIS A 172
REMARK 465 LEU B 169
REMARK 465 ILE B 170
REMARK 465 LYS B 171
REMARK 465 HIS B 172
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 205 CG CD CE NZ
REMARK 470 LYS B 205 CG CD CE NZ
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 OG SER A 185 O HOH A 2010 0.00
REMARK 500 CB SER A 185 O HOH A 2010 1.41
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 SER A 201 167.40 167.69
REMARK 500 SER B 201 168.72 168.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2008 DISTANCE = 6.92 ANGSTROMS
REMARK 525 HOH A2013 DISTANCE = 6.55 ANGSTROMS
REMARK 525 HOH B2006 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH B2008 DISTANCE = 7.04 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1H6H RELATED DB: PDB
REMARK 900 STRUCTURE OF THE PX DOMAIN FROM P40PHOX BOUND TO
REMARK 900 PHOSPHATIDYLINOSITOL 3-PHOSPHATE
REMARK 900 RELATED ID: 1OEY RELATED DB: PDB
REMARK 900 HETERODIMER OF P40PHOX AND P67PHOX PB1 DOMAINS FROM HUMAN NADPH
REMARK 900 OXIDASE
REMARK 900 RELATED ID: 1W70 RELATED DB: PDB
REMARK 900 SH3 DOMAIN OF P40PHOX COMPLEXED WITH C- TERMINAL POLYPROLINE OF
REMARK 900 P47PHOX, COMPONENTS OF THE NADPH OXIDASE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE STRUCTURE CORRESPONDS ONLY TO THE SH3 DOMAIN
DBREF 1W6X A 169 173 PDB 1W6X 1W6X 169 173
DBREF 1W6X A 174 228 UNP Q15080 NCF4_HUMAN 174 228
DBREF 1W6X B 169 173 PDB 1W6X 1W6X 169 173
DBREF 1W6X B 174 228 UNP Q15080 NCF4_HUMAN 174 228
SEQRES 1 A 60 LEU ILE LYS HIS MET ARG ALA GLU ALA LEU PHE ASP PHE
SEQRES 2 A 60 THR GLY ASN SER LYS LEU GLU LEU ASN PHE LYS ALA GLY
SEQRES 3 A 60 ASP VAL ILE PHE LEU LEU SER ARG ILE ASN LYS ASP TRP
SEQRES 4 A 60 LEU GLU GLY THR VAL ARG GLY ALA THR GLY ILE PHE PRO
SEQRES 5 A 60 LEU SER PHE VAL LYS ILE LEU LYS
SEQRES 1 B 60 LEU ILE LYS HIS MET ARG ALA GLU ALA LEU PHE ASP PHE
SEQRES 2 B 60 THR GLY ASN SER LYS LEU GLU LEU ASN PHE LYS ALA GLY
SEQRES 3 B 60 ASP VAL ILE PHE LEU LEU SER ARG ILE ASN LYS ASP TRP
SEQRES 4 B 60 LEU GLU GLY THR VAL ARG GLY ALA THR GLY ILE PHE PRO
SEQRES 5 B 60 LEU SER PHE VAL LYS ILE LEU LYS
FORMUL 3 HOH *61(H2 O)
SHEET 1 AA 5 ALA A 215 PRO A 220 0
SHEET 2 AA 5 TRP A 207 VAL A 212 -1 O LEU A 208 N PHE A 219
SHEET 3 AA 5 VAL A 196 ASN A 204 -1 O PHE A 198 N THR A 211
SHEET 4 AA 5 ARG A 174 ALA A 177 -1 O ALA A 175 N ILE A 197
SHEET 5 AA 5 VAL A 224 LEU A 227 -1 O LYS A 225 N GLU A 176
SHEET 1 BA 5 ALA B 215 PRO B 220 0
SHEET 2 BA 5 TRP B 207 VAL B 212 -1 O LEU B 208 N PHE B 219
SHEET 3 BA 5 VAL B 196 ASN B 204 -1 O PHE B 198 N THR B 211
SHEET 4 BA 5 ARG B 174 ALA B 177 -1 O ALA B 175 N ILE B 197
SHEET 5 BA 5 VAL B 224 LEU B 227 -1 O LYS B 225 N GLU B 176
CRYST1 35.160 45.160 35.060 90.00 111.43 90.00 P 1 21 1 4
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 0.028441 0.000000 0.011163 0.00000
SCALE2 0.000000 0.022143 0.000000 0.00000
SCALE3 0.000000 0.000000 0.030641 0.00000
(ATOM LINES ARE NOT SHOWN.)
END