HEADER LIGASE 24-APR-06 2GRO
TITLE CRYSTAL STRUCTURE OF HUMAN RANGAP1-UBC9-N85Q
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 I;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: UBIQUITIN-PROTEIN LIGASE I, UBIQUITIN CARRIER PROTEIN I,
COMPND 5 SUMO-1-PROTEIN LIGASE, SUMO-1-CONJUGATING ENZYME, UBIQUITIN CARRIER
COMPND 6 PROTEIN 9, P18;
COMPND 7 EC: 6.3.2.19;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: RAN GTPASE-ACTIVATING PROTEIN 1;
COMPND 12 CHAIN: B;
COMPND 13 FRAGMENT: C-TERMINAL DOMAIN (RESIDUES 419-587);
COMPND 14 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: UBE2I, UBC9, UBCE9;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21DE3 CODON PLUS RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: RANGAP1;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21DE3 CODON PLUS RIL;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PSMT3
KEYWDS UBIQUITIN, CONJUGATION, SMALL UBIQUITIN LIKE MODIFER, SMT3, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.A.YUNUS,C.D.LIMA
REVDAT 6 14-FEB-24 2GRO 1 REMARK
REVDAT 5 20-OCT-21 2GRO 1 SEQADV
REVDAT 4 18-OCT-17 2GRO 1 REMARK
REVDAT 3 24-FEB-09 2GRO 1 VERSN
REVDAT 2 20-JUN-06 2GRO 1 JRNL
REVDAT 1 30-MAY-06 2GRO 0
JRNL AUTH A.A.YUNUS,C.D.LIMA
JRNL TITL LYSINE ACTIVATION AND FUNCTIONAL ANALYSIS OF E2-MEDIATED
JRNL TITL 2 CONJUGATION IN THE SUMO PATHWAY.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 13 491 2006
JRNL REFN ISSN 1545-9993
JRNL PMID 16732283
JRNL DOI 10.1038/NSMB1104
REMARK 2
REMARK 2 RESOLUTION. 1.70 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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.98
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 687535.938
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 39163
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) : 0.185
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1929
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.76
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3446
REMARK 3 BIN R VALUE (WORKING SET) : 0.2140
REMARK 3 BIN FREE R VALUE : 0.2850
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 174
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.022
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2473
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 428
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.29000
REMARK 3 B22 (A**2) : 0.47000
REMARK 3 B33 (A**2) : -0.76000
REMARK 3 B12 (A**2) : -1.69000
REMARK 3 B13 (A**2) : -1.55000
REMARK 3 B23 (A**2) : 1.90000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.18
REMARK 3 ESD FROM SIGMAA (A) : 0.11
REMARK 3 LOW RESOLUTION CUTOFF (A) : 6.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.19
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.15
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.930
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) : 1.140 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.780 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.230 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.170 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.42
REMARK 3 BSOL : 57.74
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 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 2GRO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-APR-06.
REMARK 100 THE DEPOSITION ID IS D_1000037472.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-OCT-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 31-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9790
REMARK 200 MONOCHROMATOR : MONOCHROMATOR KOHZU HLD-4 DOUBLE
REMARK 200 CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39181
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
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 (%) : 96.2
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.05600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.14700
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1M LITHIUM SULFATE, 0.5M AMMONIUM
REMARK 280 SULFATE, 50MM SODIUM CITRATE, PH 5.5, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 291K
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 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 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 SER A 158
REMARK 465 SER B 418
REMARK 465 THR B 419
REMARK 465 GLY B 420
REMARK 465 GLU B 421
REMARK 465 PRO B 422
REMARK 465 ALA B 423
REMARK 465 PRO B 424
REMARK 465 VAL B 425
REMARK 465 LEU B 426
REMARK 465 SER B 427
REMARK 465 SER B 428
REMARK 465 PRO B 429
REMARK 465 PRO B 430
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 83 138.02 -171.70
REMARK 500 LYS A 101 -107.02 -115.22
REMARK 500 ASN A 140 86.90 -155.21
REMARK 500 ASN B 567 125.80 -172.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2GRN RELATED DB: PDB
REMARK 900 RELATED ID: 2GRP RELATED DB: PDB
REMARK 900 RELATED ID: 2GRQ RELATED DB: PDB
REMARK 900 RELATED ID: 2GRR RELATED DB: PDB
DBREF 2GRO A 1 158 UNP P63279 UBE2I_HUMAN 1 158
DBREF 2GRO B 419 587 UNP P46060 RGP1_HUMAN 419 587
SEQADV 2GRO GLY A -2 UNP P63279 CLONING ARTIFACT
SEQADV 2GRO SER A -1 UNP P63279 CLONING ARTIFACT
SEQADV 2GRO HIS A 0 UNP P63279 CLONING ARTIFACT
SEQADV 2GRO GLN A 85 UNP P63279 ASN 85 ENGINEERED MUTATION
SEQADV 2GRO SER B 418 UNP P46060 CLONING ARTIFACT
SEQRES 1 A 161 GLY SER HIS MET SER GLY ILE ALA LEU SER ARG LEU ALA
SEQRES 2 A 161 GLN GLU ARG LYS ALA TRP ARG LYS ASP HIS PRO PHE GLY
SEQRES 3 A 161 PHE VAL ALA VAL PRO THR LYS ASN PRO ASP GLY THR MET
SEQRES 4 A 161 ASN LEU MET ASN TRP GLU CYS ALA ILE PRO GLY LYS LYS
SEQRES 5 A 161 GLY THR PRO TRP GLU GLY GLY LEU PHE LYS LEU ARG MET
SEQRES 6 A 161 LEU PHE LYS ASP ASP TYR PRO SER SER PRO PRO LYS CYS
SEQRES 7 A 161 LYS PHE GLU PRO PRO LEU PHE HIS PRO GLN VAL TYR PRO
SEQRES 8 A 161 SER GLY THR VAL CYS LEU SER ILE LEU GLU GLU ASP LYS
SEQRES 9 A 161 ASP TRP ARG PRO ALA ILE THR ILE LYS GLN ILE LEU LEU
SEQRES 10 A 161 GLY ILE GLN GLU LEU LEU ASN GLU PRO ASN ILE GLN ASP
SEQRES 11 A 161 PRO ALA GLN ALA GLU ALA TYR THR ILE TYR CYS GLN ASN
SEQRES 12 A 161 ARG VAL GLU TYR GLU LYS ARG VAL ARG ALA GLN ALA LYS
SEQRES 13 A 161 LYS PHE ALA PRO SER
SEQRES 1 B 170 SER THR GLY GLU PRO ALA PRO VAL LEU SER SER PRO PRO
SEQRES 2 B 170 PRO ALA ASP VAL SER THR PHE LEU ALA PHE PRO SER PRO
SEQRES 3 B 170 GLU LYS LEU LEU ARG LEU GLY PRO LYS SER SER VAL LEU
SEQRES 4 B 170 ILE ALA GLN GLN THR ASP THR SER ASP PRO GLU LYS VAL
SEQRES 5 B 170 VAL SER ALA PHE LEU LYS VAL SER SER VAL PHE LYS ASP
SEQRES 6 B 170 GLU ALA THR VAL ARG MET ALA VAL GLN ASP ALA VAL ASP
SEQRES 7 B 170 ALA LEU MET GLN LYS ALA PHE ASN SER SER SER PHE ASN
SEQRES 8 B 170 SER ASN THR PHE LEU THR ARG LEU LEU VAL HIS MET GLY
SEQRES 9 B 170 LEU LEU LYS SER GLU ASP LYS VAL LYS ALA ILE ALA ASN
SEQRES 10 B 170 LEU TYR GLY PRO LEU MET ALA LEU ASN HIS MET VAL GLN
SEQRES 11 B 170 GLN ASP TYR PHE PRO LYS ALA LEU ALA PRO LEU LEU LEU
SEQRES 12 B 170 ALA PHE VAL THR LYS PRO ASN SER ALA LEU GLU SER CYS
SEQRES 13 B 170 SER PHE ALA ARG HIS SER LEU LEU GLN THR LEU TYR LYS
SEQRES 14 B 170 VAL
FORMUL 3 HOH *428(H2 O)
HELIX 1 1 SER A 2 ASP A 19 1 18
HELIX 2 2 LEU A 94 GLU A 98 5 5
HELIX 3 3 THR A 108 GLU A 122 1 15
HELIX 4 4 GLN A 130 ASN A 140 1 11
HELIX 5 5 ASN A 140 PHE A 155 1 16
HELIX 6 6 ASP B 433 PHE B 440 1 8
HELIX 7 7 SER B 442 ARG B 448 1 7
HELIX 8 8 LYS B 452 GLN B 460 1 9
HELIX 9 9 ASP B 465 SER B 478 1 14
HELIX 10 10 GLU B 483 ASN B 503 1 21
HELIX 11 11 ASN B 508 MET B 520 1 13
HELIX 12 12 LEU B 535 VAL B 546 1 12
HELIX 13 13 PRO B 552 ALA B 554 5 3
HELIX 14 14 LEU B 555 LYS B 565 1 11
HELIX 15 15 ASN B 567 SER B 572 1 6
HELIX 16 16 CYS B 573 VAL B 587 1 15
SHEET 1 A 4 VAL A 25 LYS A 30 0
SHEET 2 A 4 MET A 36 PRO A 46 -1 O ASN A 37 N THR A 29
SHEET 3 A 4 LEU A 57 LEU A 63 -1 O LEU A 60 N CYS A 43
SHEET 4 A 4 LYS A 74 PHE A 77 -1 O LYS A 74 N LEU A 63
CISPEP 1 TYR A 68 PRO A 69 0 0.49
CISPEP 2 GLU A 78 PRO A 79 0 0.87
CRYST1 39.295 44.785 61.027 72.58 72.06 75.45 P 1 1
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 0.025450 -0.006600 -0.006850 0.00000
SCALE2 0.000000 0.023070 -0.005730 0.00000
SCALE3 0.000000 0.000000 0.017750 0.00000
(ATOM LINES ARE NOT SHOWN.)
END