HEADER UBIQUITIN-BINDING PROTEIN 02-AUG-16 5LN1
TITLE STRUCTURE OF UBIQUITYLATED-RPN10 FROM YEAST;
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 26S PROTEASOME REGULATORY SUBUNIT RPN10;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1-191;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: POLYUBIQUITIN-B;
COMPND 8 CHAIN: U;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 3 S288C);
SOURCE 4 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 5 ORGANISM_TAXID: 559292;
SOURCE 6 STRAIN: ATCC 204508 / S288C;
SOURCE 7 GENE: RPN10, MCB1, SUN1, YHR200W;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 GENE: UBB;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS UBIQUITIN, VWA, UBIQUITYLATION, PROTEASOME, UBIQUITIN-BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR T.KEREN-KAPLAN,I.ATTALI,O.LEVIN-KRAVETS,G.PRAG
REVDAT 3 10-JAN-24 5LN1 1 REMARK
REVDAT 2 08-MAY-19 5LN1 1 REMARK LINK
REVDAT 1 19-OCT-16 5LN1 0
JRNL AUTH T.KEREN-KAPLAN,L.ZEEV PETERS,O.LEVIN-KRAVETS,I.ATTALI,
JRNL AUTH 2 O.KLEIFELD,N.SHOHAT,S.ARTZI,O.ZUCKER,I.PILZER,N.REIS,
JRNL AUTH 3 M.H.GLICKMAN,S.BEN-AROYA,G.PRAG
JRNL TITL STRUCTURE OF UBIQUITYLATED-RPN10 PROVIDES INSIGHT INTO ITS
JRNL TITL 2 AUTOREGULATION MECHANISM.
JRNL REF NAT COMMUN V. 7 12960 2016
JRNL REFN ESSN 2041-1723
JRNL PMID 27698474
JRNL DOI 10.1038/NCOMMS12960
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.KEREN-KAPLAN,G.PRAG
REMARK 1 TITL PURIFICATION AND CRYSTALLIZATION OF MONO-UBIQUITYLATED
REMARK 1 TITL 2 UBIQUITIN RECEPTOR RPN10.
REMARK 1 REF ACTA CRYSTALLOGR. SECT. F V. 68 1120 2012
REMARK 1 REF 2 STRUCT. BIOL. CRYST. COMMUN.
REMARK 1 REFN ESSN 1744-3091
REMARK 1 PMID 22949210
REMARK 1 DOI 10.1107/S1744309112034331
REMARK 2
REMARK 2 RESOLUTION. 3.14 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8_1069
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.14
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 53.64
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 5823
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.570
REMARK 3 FREE R VALUE TEST SET COUNT : 571
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 53.6486 - 3.2490 0.99 2803 140 0.1763 0.2099
REMARK 3 2 3.2490 - 3.1400 1.00 2754 126 0.2111 0.3164
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.210
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.010 2098
REMARK 3 ANGLE : 1.409 2836
REMARK 3 CHIRALITY : 0.101 337
REMARK 3 PLANARITY : 0.006 371
REMARK 3 DIHEDRAL : 17.541 796
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5LN1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-AUG-16.
REMARK 100 THE DEPOSITION ID IS D_1200000860.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-NOV-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9393
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 5824
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.140
REMARK 200 RESOLUTION RANGE LOW (A) : 61.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 9.800
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.08400
REMARK 200 R SYM (I) : 0.09800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.14
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.22500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2X5N, 1UBQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% (W/V) PEG 20000, 0.1M MES PH 6.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 292K, EVAPORATION,
REMARK 280 RECRYSTALLIZATION
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 53.64500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.85000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 53.64500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 24.85000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, U
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 BIOMT1 2 -1.000000 0.000000 0.000000 -52.87356
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 61.79770
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 -3
REMARK 465 PRO A -2
REMARK 465 PRO A -1
REMARK 465 ARG A 0
REMARK 465 ASN A 150
REMARK 465 THR A 151
REMARK 465 GLU A 152
REMARK 465 GLY U -4
REMARK 465 ALA U -3
REMARK 465 MET U -2
REMARK 465 GLY U -1
REMARK 465 SER U 0
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 NZ LYS A 84 C GLY U 76 1.33
REMARK 500 O GLN A 149 N LEU A 153 2.06
REMARK 500 OE2 GLU A 4 NZ LYS A 40 2.18
REMARK 500 OD1 ASP A 11 OG SER A 13 2.19
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 ASN A 44 131.06 -175.83
REMARK 500 ALA A 57 3.82 156.78
REMARK 500 ASN A 58 104.93 158.09
REMARK 500 ASP A 78 -3.83 100.26
REMARK 500 ASN A 103 73.86 61.73
REMARK 500 ARG U 74 -80.63 -93.02
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5LN1 A 1 191 UNP P38886 RPN10_YEAST 1 191
DBREF 5LN1 U 1 76 UNP P0CG47 UBB_HUMAN 77 152
SEQADV 5LN1 GLY A -3 UNP P38886 EXPRESSION TAG
SEQADV 5LN1 PRO A -2 UNP P38886 EXPRESSION TAG
SEQADV 5LN1 PRO A -1 UNP P38886 EXPRESSION TAG
SEQADV 5LN1 ARG A 0 UNP P38886 EXPRESSION TAG
SEQADV 5LN1 GLY U -4 UNP P0CG47 EXPRESSION TAG
SEQADV 5LN1 ALA U -3 UNP P0CG47 EXPRESSION TAG
SEQADV 5LN1 MET U -2 UNP P0CG47 EXPRESSION TAG
SEQADV 5LN1 GLY U -1 UNP P0CG47 EXPRESSION TAG
SEQADV 5LN1 SER U 0 UNP P0CG47 EXPRESSION TAG
SEQRES 1 A 195 GLY PRO PRO ARG MET VAL LEU GLU ALA THR VAL LEU VAL
SEQRES 2 A 195 ILE ASP ASN SER GLU TYR SER ARG ASN GLY ASP PHE PRO
SEQRES 3 A 195 ARG THR ARG PHE GLU ALA GLN ILE ASP SER VAL GLU PHE
SEQRES 4 A 195 ILE PHE GLN ALA LYS ARG ASN SER ASN PRO GLU ASN THR
SEQRES 5 A 195 VAL GLY LEU ILE SER GLY ALA GLY ALA ASN PRO ARG VAL
SEQRES 6 A 195 LEU SER THR PHE THR ALA GLU PHE GLY LYS ILE LEU ALA
SEQRES 7 A 195 GLY LEU HIS ASP THR GLN ILE GLU GLY LYS LEU HIS MET
SEQRES 8 A 195 ALA THR ALA LEU GLN ILE ALA GLN LEU THR LEU LYS HIS
SEQRES 9 A 195 ARG GLN ASN LYS VAL GLN HIS GLN ARG ILE VAL ALA PHE
SEQRES 10 A 195 VAL CYS SER PRO ILE SER ASP SER ARG ASP GLU LEU ILE
SEQRES 11 A 195 ARG LEU ALA LYS THR LEU LYS LYS ASN ASN VAL ALA VAL
SEQRES 12 A 195 ASP ILE ILE ASN PHE GLY GLU ILE GLU GLN ASN THR GLU
SEQRES 13 A 195 LEU LEU ASP GLU PHE ILE ALA ALA VAL ASN ASN PRO GLN
SEQRES 14 A 195 GLU GLU THR SER HIS LEU LEU THR VAL THR PRO GLY PRO
SEQRES 15 A 195 ARG LEU LEU TYR GLU ASN ILE ALA SER SER PRO ILE ILE
SEQRES 1 U 81 GLY ALA MET GLY SER MET GLN ILE PHE VAL LYS THR LEU
SEQRES 2 U 81 THR GLY LYS THR ILE THR LEU GLU VAL GLU PRO SER ASP
SEQRES 3 U 81 THR ILE GLU ASN VAL LYS ALA LYS ILE GLN ASP LYS GLU
SEQRES 4 U 81 GLY ILE PRO PRO ASP GLN GLN ARG LEU ILE PHE ALA GLY
SEQRES 5 U 81 LYS GLN LEU GLU ASP GLY ARG THR LEU SER ASP TYR ASN
SEQRES 6 U 81 ILE GLN LYS GLU SER THR LEU HIS LEU VAL LEU ARG LEU
SEQRES 7 U 81 ARG GLY GLY
HELIX 1 AA1 SER A 13 ARG A 17 5 5
HELIX 2 AA2 THR A 24 ASN A 44 1 21
HELIX 3 AA3 GLU A 68 HIS A 77 1 10
HELIX 4 AA4 HIS A 86 HIS A 100 1 15
HELIX 5 AA5 SER A 121 ASN A 135 1 15
HELIX 6 AA6 GLN A 149 GLN A 149 1 1
HELIX 7 AA7 LEU A 154 ASN A 162 1 9
HELIX 8 AA8 LEU A 180 SER A 188 1 9
HELIX 9 AA9 THR U 22 GLY U 35 1 14
HELIX 10 AB1 PRO U 37 ASP U 39 5 3
SHEET 1 AA1 6 ARG A 60 THR A 66 0
SHEET 2 AA1 6 THR A 48 SER A 53 -1 N VAL A 49 O THR A 66
SHEET 3 AA1 6 GLU A 4 ILE A 10 1 N LEU A 8 O GLY A 50
SHEET 4 AA1 6 HIS A 107 VAL A 114 1 O VAL A 111 N VAL A 7
SHEET 5 AA1 6 VAL A 137 ASN A 143 1 O ILE A 142 N ALA A 112
SHEET 6 AA1 6 LEU A 171 THR A 173 1 O LEU A 172 N ASN A 143
SHEET 1 AA2 5 THR U 12 GLU U 16 0
SHEET 2 AA2 5 GLN U 2 THR U 7 -1 N VAL U 5 O ILE U 13
SHEET 3 AA2 5 THR U 66 LEU U 71 1 O LEU U 67 N PHE U 4
SHEET 4 AA2 5 GLN U 41 PHE U 45 -1 N ILE U 44 O HIS U 68
SHEET 5 AA2 5 LYS U 48 GLN U 49 -1 O LYS U 48 N PHE U 45
CISPEP 1 PRO A 22 ARG A 23 0 -2.63
CRYST1 107.290 49.700 81.330 90.00 130.55 90.00 C 1 2 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 0.009321 0.000000 0.007975 0.00000
SCALE2 0.000000 0.020121 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016182 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
