HEADER TRANSFERASE 13-JUL-14 4USS
TITLE POPULUS TRICHOCARPA GLUTATHIONE TRANSFERASE X1-1 (GHR1), COMPLEXED
TITLE 2 WITH GLUTATHIONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTATHIONYL HYDROQUINONE REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 35-359;
COMPND 5 EC: 2.5.1.18;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: THE EXPRESSED PROTEIN IS DEVOID OF THE FIRST 34 AMINO
COMPND 8 ACIDS.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: POPULUS TRICHOCARPA;
SOURCE 3 ORGANISM_COMMON: BLACK COTTONWOOD;
SOURCE 4 ORGANISM_TAXID: 3694;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSFERASE, CLASS XI, POPLAR, PLASTIDS
EXPDTA X-RAY DIFFRACTION
AUTHOR P.A.LALLEMENT,E.MEUX,J.M.GUALBERTO,S.DUMARACAY,F.FAVIER,C.DIDIERJEAN,
AUTHOR 2 F.SAUL,A.HAOUZ,M.MOREL-ROUHIER,E.GELHAYE,N.ROUHIER,A.HECKER
REVDAT 5 10-JAN-24 4USS 1 REMARK
REVDAT 4 23-OCT-19 4USS 1 ATOM
REVDAT 3 31-DEC-14 4USS 1 JRNL
REVDAT 2 17-DEC-14 4USS 1 JRNL
REVDAT 1 03-DEC-14 4USS 0
JRNL AUTH P.LALLEMENT,E.MEUX,J.M.GUALBERTO,S.DUMARCAY,F.FAVIER,
JRNL AUTH 2 C.DIDIERJEAN,F.SAUL,A.HAOUZ,M.MOREL-ROUHIER,E.GELHAYE,
JRNL AUTH 3 N.ROUHIER,A.HECKER
JRNL TITL GLUTATHIONYL-HYDROQUINONE REDUCTASES FROM POPLAR ARE
JRNL TITL 2 PLASTIDIAL PROTEINS THAT DEGLUTATHIONYLATE BOTH REDUCED AND
JRNL TITL 3 OXIDIZED GLUTATHIONYLATED QUINONES.
JRNL REF FEBS LETT. V. 589 37 2015
JRNL REFN ISSN 0014-5793
JRNL PMID 25455804
JRNL DOI 10.1016/J.FEBSLET.2014.11.021
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.53
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 10702
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 548
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 19.5259 - 3.9604 1.00 2639 157 0.1478 0.1766
REMARK 3 2 3.9604 - 3.1478 1.00 2534 140 0.1818 0.2478
REMARK 3 3 3.1478 - 2.7511 1.00 2502 125 0.2362 0.3144
REMARK 3 4 2.7511 - 2.5001 1.00 2479 126 0.2346 0.3108
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.000
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.73
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 : 0.003 2574
REMARK 3 ANGLE : 0.668 3491
REMARK 3 CHIRALITY : 0.029 363
REMARK 3 PLANARITY : 0.002 454
REMARK 3 DIHEDRAL : 12.561 949
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 4USS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1290061226.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-OCT-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.826560
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : KIRKPATRICK-BAEZ PAIR OF BI
REMARK 200 -MORPH MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10702
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 19.530
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 10.80
REMARK 200 R MERGE (I) : 0.16000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.1
REMARK 200 DATA REDUNDANCY IN SHELL : 10.90
REMARK 200 R MERGE FOR SHELL (I) : 0.79000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 3PPU
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 18.26500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.20450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 18.26500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.20450
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.4 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 MET A 1
REMARK 465 ALA A 2
REMARK 465 ARG A 3
REMARK 465 SER A 4
REMARK 465 ALA A 5
REMARK 465 ILE A 6
REMARK 465 ASP A 7
REMARK 465 GLU A 8
REMARK 465 THR A 9
REMARK 465 SER A 10
REMARK 465 ASP A 11
REMARK 465 THR A 12
REMARK 465 GLY A 13
REMARK 465 ALA A 14
REMARK 465 PHE A 15
REMARK 465 LYS A 16
REMARK 465 ARG A 17
REMARK 465 SER A 324
REMARK 465 SER A 325
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 THR A 154 -35.68 -131.86
REMARK 500 VAL A 249 -66.64 -120.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 502
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 DISCREPANCIES IN SEQUENCE ARE DUE TO POLYMORPHISM.
REMARK 999 AUTHORS HAVE CLARIFIED THAT DISCREPANCIES IN SEQUENCE ARE DUE
REMARK 999 TO POLYMORPHISM (RESIDUES 105, 175, 181, AND 185)
DBREF 4USS A 1 325 UNP B9ICN7 B9ICN7_POPTR 35 359
SEQADV 4USS THR A 105 UNP B9ICN7 PRO 139 SEE REMARK 999
SEQADV 4USS GLN A 175 UNP B9ICN7 ARG 209 SEE REMARK 999
SEQADV 4USS GLY A 181 UNP B9ICN7 GLU 215 SEE REMARK 999
SEQADV 4USS ASP A 185 UNP B9ICN7 ASN 219 SEE REMARK 999
SEQRES 1 A 325 MET ALA ARG SER ALA ILE ASP GLU THR SER ASP THR GLY
SEQRES 2 A 325 ALA PHE LYS ARG THR ALA SER THR PHE ARG ASN PHE ILE
SEQRES 3 A 325 SER LYS GLU PRO ASN SER GLN PHE PRO PRO GLU SER GLY
SEQRES 4 A 325 ARG TYR HIS LEU TYR VAL SER TYR ALA CYS PRO TRP ALA
SEQRES 5 A 325 SER ARG CYS LEU ALA TYR LEU LYS ILE LYS GLY LEU GLU
SEQRES 6 A 325 LYS ALA ILE ALA PHE THR SER VAL LYS PRO ILE TRP GLU
SEQRES 7 A 325 ARG THR LYS GLU SER ASP GLU HIS MET GLY TRP VAL PHE
SEQRES 8 A 325 PRO ALA SER GLU THR GLU GLU ALA GLY ALA GLU PRO ASP
SEQRES 9 A 325 THR LEU ASN GLY ALA ARG SER ILE ARG GLU LEU TYR GLU
SEQRES 10 A 325 LEU ALA SER THR ASN TYR ALA GLY LYS TYR THR VAL PRO
SEQRES 11 A 325 VAL LEU TRP ASP LYS LYS LEU LYS THR ILE VAL ASN ASN
SEQRES 12 A 325 GLU SER SER GLU ILE ILE ARG MET PHE ASN THR GLU PHE
SEQRES 13 A 325 ASN ASP ILE ALA GLU ASN ALA ALA LEU ASP LEU TYR PRO
SEQRES 14 A 325 SER HIS LEU GLN ALA GLN ILE ASP GLU THR ASN GLY TRP
SEQRES 15 A 325 VAL TYR ASP GLY ILE ASN ASN GLY VAL TYR LYS CYS GLY
SEQRES 16 A 325 PHE ALA ARG LYS GLN GLY PRO TYR GLU GLU ALA ALA ILE
SEQRES 17 A 325 GLN LEU TYR GLU ALA LEU ASP LYS CYS GLU GLU ILE LEU
SEQRES 18 A 325 GLY ARG GLN ARG TYR ILE CYS GLY ASN THR LEU SER GLU
SEQRES 19 A 325 ALA ASP ILE LYS LEU PHE VAL THR LEU ILE ARG PHE ASP
SEQRES 20 A 325 GLU VAL TYR ALA VAL HIS PHE LYS CYS ASN LYS LYS LEU
SEQRES 21 A 325 LEU ARG ASP TYR PRO ASN MET PHE ASN TYR THR LYS ASP
SEQRES 22 A 325 ILE PHE GLN ILE PRO GLY MET SER SER THR VAL ASN MET
SEQRES 23 A 325 GLN HIS ILE LYS ARG HIS TYR TYR GLY SER HIS PRO THR
SEQRES 24 A 325 VAL ASN PRO PHE GLY ILE ILE PRO LEU GLY PRO ASP ILE
SEQRES 25 A 325 ASP TYR SER SER PRO HIS ASP ARG ASN ARG PHE SER SER
HET GSH A 500 31
HET PO4 A 501 5
HET PO4 A 502 5
HETNAM GSH GLUTATHIONE
HETNAM PO4 PHOSPHATE ION
FORMUL 2 GSH C10 H17 N3 O6 S
FORMUL 3 PO4 2(O4 P 3-)
FORMUL 5 HOH *70(H2 O)
HELIX 1 1 CYS A 49 LYS A 62 1 14
HELIX 2 2 SER A 111 SER A 120 1 10
HELIX 3 3 GLU A 144 GLU A 155 1 12
HELIX 4 4 PRO A 169 ILE A 187 1 19
HELIX 5 5 ASN A 189 ALA A 197 1 9
HELIX 6 6 LYS A 199 GLN A 224 1 26
HELIX 7 7 SER A 233 ILE A 244 1 12
HELIX 8 8 VAL A 249 PHE A 254 1 6
HELIX 9 9 LEU A 260 ASP A 263 5 4
HELIX 10 10 TYR A 264 GLN A 276 1 13
HELIX 11 11 MET A 280 VAL A 284 5 5
HELIX 12 12 ASN A 285 SER A 296 1 12
HELIX 13 13 ASP A 319 PHE A 323 5 5
SHEET 1 AA 4 ALA A 69 SER A 72 0
SHEET 2 AA 4 TYR A 41 VAL A 45 1 O TYR A 41 N ALA A 69
SHEET 3 AA 4 VAL A 131 ASP A 134 -1 O VAL A 131 N TYR A 44
SHEET 4 AA 4 THR A 139 ASN A 142 -1 O THR A 139 N ASP A 134
SHEET 1 AB 2 GLU A 78 ARG A 79 0
SHEET 2 AB 2 MET A 87 GLY A 88 -1 O GLY A 88 N GLU A 78
CISPEP 1 VAL A 129 PRO A 130 0 6.14
SITE 1 AC1 10 CYS A 49 TRP A 51 TRP A 89 THR A 128
SITE 2 AC1 10 VAL A 129 PRO A 130 ASN A 143 GLU A 144
SITE 3 AC1 10 SER A 145 HOH A2030
SITE 1 AC2 6 LYS A 81 GLU A 82 SER A 83 ALA A 124
SITE 2 AC2 6 GLY A 125 LYS A 126
SITE 1 AC3 3 HIS A 42 ALA A 69 LYS A 135
CRYST1 36.530 92.409 86.901 90.00 90.00 90.00 P 21 21 2 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 0.027375 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010821 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011507 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
