HEADER TRANSPORT PROTEIN 24-JUL-14 4U58
TITLE IMPORTIN-ALPHA MINOR NLS SITE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IMPORTIN SUBUNIT ALPHA-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 72-497;
COMPND 5 SYNONYM: IMPORTIN ALPHA P1,KARYOPHERIN SUBUNIT ALPHA-2,PENDULIN,PORE
COMPND 6 TARGETING COMPLEX 58 KDA SUBUNIT,PTAC58,RAG COHORT PROTEIN 1,SRP1-
COMPND 7 ALPHA;
COMPND 8 ENGINEERED: YES;
COMPND 9 OTHER_DETAILS: DELTAIBB
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: KPNA2, RCH1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TPX2 INHIBITOR, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.STEWART,E.VALKOV,R.S.HOLVEY
REVDAT 2 08-JUL-15 4U58 1 JRNL
REVDAT 1 13-MAY-15 4U58 0
JRNL AUTH R.S.HOLVEY,E.VALKOV,D.NEAL,M.STEWART,C.ABELL
JRNL TITL SELECTIVE TARGETING OF THE TPX2 SITE OF IMPORTIN-ALPHA USING
JRNL TITL 2 FRAGMENT-BASED LIGAND DESIGN.
JRNL REF CHEMMEDCHEM V. 10 1232 2015
JRNL REFN ESSN 1860-7187
JRNL PMID 25899172
JRNL DOI 10.1002/CMDC.201500014
REMARK 2
REMARK 2 RESOLUTION. 2.56 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_1702)
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) : 2.56
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 62.31
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 23355
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.214
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.130
REMARK 3 FREE R VALUE TEST SET COUNT : 1198
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
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) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.540
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.08
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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 4U58 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1000202830.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-NOV-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 : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9686
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23793
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.560
REMARK 200 RESOLUTION RANGE LOW (A) : 62.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.5000
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: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SEE PUBLICATION, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 39.58000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.51500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.31500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.51500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.58000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.31500
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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.
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: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 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 108 CG CD CE NZ
REMARK 470 LYS A 348 CG CD CE NZ
REMARK 470 LYS A 432 CG CD CE NZ
REMARK 470 LYS A 459 CG CD CE NZ
REMARK 470 ARG A 478 CG CD NE CZ NH1 NH2
REMARK 470 TYR A 485 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 486 CG CD CE NZ
REMARK 470 SER A 497 OG
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 156 O HOH A 601 1.66
REMARK 500 O HOH A 708 O HOH A 717 1.93
REMARK 500 O HOH A 698 O HOH A 703 1.99
REMARK 500 O HOH A 633 O HOH A 669 2.04
REMARK 500 O LYS A 83 O HOH A 602 2.05
REMARK 500 OD2 ASP A 270 O HOH A 641 2.07
REMARK 500 OG1 THR A 324 O HOH A 654 2.10
REMARK 500 O HOH A 688 O HOH A 715 2.12
REMARK 500 O ALA A 214 O HOH A 706 2.16
REMARK 500 OE2 GLU A 466 O HOH A 661 2.16
REMARK 500 NZ LYS A 292 O HOH A 631 2.17
REMARK 500 NZ LYS A 123 O HOH A 712 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 88 52.07 -95.18
REMARK 500 ASN A 241 70.47 42.71
REMARK 500 ARG A 478 64.85 -69.23
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 3C6 A 501
DBREF 4U58 A 72 497 UNP P52293 IMA1_MOUSE 72 497
SEQRES 1 A 426 GLY THR VAL ASN TRP SER VAL GLU ASP ILE VAL LYS GLY
SEQRES 2 A 426 ILE ASN SER ASN ASN LEU GLU SER GLN LEU GLN ALA THR
SEQRES 3 A 426 GLN ALA ALA ARG LYS LEU LEU SER ARG GLU LYS GLN PRO
SEQRES 4 A 426 PRO ILE ASP ASN ILE ILE ARG ALA GLY LEU ILE PRO LYS
SEQRES 5 A 426 PHE VAL SER PHE LEU GLY LYS THR ASP CYS SER PRO ILE
SEQRES 6 A 426 GLN PHE GLU SER ALA TRP ALA LEU THR ASN ILE ALA SER
SEQRES 7 A 426 GLY THR SER GLU GLN THR LYS ALA VAL VAL ASP GLY GLY
SEQRES 8 A 426 ALA ILE PRO ALA PHE ILE SER LEU LEU ALA SER PRO HIS
SEQRES 9 A 426 ALA HIS ILE SER GLU GLN ALA VAL TRP ALA LEU GLY ASN
SEQRES 10 A 426 ILE ALA GLY ASP GLY SER ALA PHE ARG ASP LEU VAL ILE
SEQRES 11 A 426 LYS HIS GLY ALA ILE ASP PRO LEU LEU ALA LEU LEU ALA
SEQRES 12 A 426 VAL PRO ASP LEU SER THR LEU ALA CYS GLY TYR LEU ARG
SEQRES 13 A 426 ASN LEU THR TRP THR LEU SER ASN LEU CYS ARG ASN LYS
SEQRES 14 A 426 ASN PRO ALA PRO PRO LEU ASP ALA VAL GLU GLN ILE LEU
SEQRES 15 A 426 PRO THR LEU VAL ARG LEU LEU HIS HIS ASN ASP PRO GLU
SEQRES 16 A 426 VAL LEU ALA ASP SER CYS TRP ALA ILE SER TYR LEU THR
SEQRES 17 A 426 ASP GLY PRO ASN GLU ARG ILE GLU MET VAL VAL LYS LYS
SEQRES 18 A 426 GLY VAL VAL PRO GLN LEU VAL LYS LEU LEU GLY ALA THR
SEQRES 19 A 426 GLU LEU PRO ILE VAL THR PRO ALA LEU ARG ALA ILE GLY
SEQRES 20 A 426 ASN ILE VAL THR GLY THR ASP GLU GLN THR GLN LYS VAL
SEQRES 21 A 426 ILE ASP ALA GLY ALA LEU ALA VAL PHE PRO SER LEU LEU
SEQRES 22 A 426 THR ASN PRO LYS THR ASN ILE GLN LYS GLU ALA THR TRP
SEQRES 23 A 426 THR MET SER ASN ILE THR ALA GLY ARG GLN ASP GLN ILE
SEQRES 24 A 426 GLN GLN VAL VAL ASN HIS GLY LEU VAL PRO PHE LEU VAL
SEQRES 25 A 426 GLY VAL LEU SER LYS ALA ASP PHE LYS THR GLN LYS GLU
SEQRES 26 A 426 ALA ALA TRP ALA ILE THR ASN TYR THR SER GLY GLY THR
SEQRES 27 A 426 VAL GLU GLN ILE VAL TYR LEU VAL HIS CYS GLY ILE ILE
SEQRES 28 A 426 GLU PRO LEU MET ASN LEU LEU SER ALA LYS ASP THR LYS
SEQRES 29 A 426 ILE ILE GLN VAL ILE LEU ASP ALA ILE SER ASN ILE PHE
SEQRES 30 A 426 GLN ALA ALA GLU LYS LEU GLY GLU THR GLU LYS LEU SER
SEQRES 31 A 426 ILE MET ILE GLU GLU CYS GLY GLY LEU ASP LYS ILE GLU
SEQRES 32 A 426 ALA LEU GLN ARG HIS GLU ASN GLU SER VAL TYR LYS ALA
SEQRES 33 A 426 SER LEU ASN LEU ILE GLU LYS TYR PHE SER
HET 3C6 A 501 24
HETNAM 3C6 N~2~-[4-(PYRIDIN-3-YL)BENZOYL]-L-LYSINAMIDE
FORMUL 2 3C6 C18 H22 N4 O2
FORMUL 3 HOH *118(H2 O)
HELIX 1 AA1 SER A 77 SER A 87 1 11
HELIX 2 AA2 ASN A 89 SER A 105 1 17
HELIX 3 AA3 PRO A 111 ALA A 118 1 8
HELIX 4 AA4 GLY A 119 GLY A 129 1 11
HELIX 5 AA5 CYS A 133 SER A 149 1 17
HELIX 6 AA6 THR A 151 GLY A 161 1 11
HELIX 7 AA7 GLY A 162 LEU A 170 1 9
HELIX 8 AA8 LEU A 171 SER A 173 5 3
HELIX 9 AA9 HIS A 175 ASP A 192 1 18
HELIX 10 AB1 GLY A 193 HIS A 203 1 11
HELIX 11 AB2 ALA A 205 LEU A 212 1 8
HELIX 12 AB3 ASP A 217 LEU A 221 5 5
HELIX 13 AB4 ALA A 222 CYS A 237 1 16
HELIX 14 AB5 PRO A 245 LEU A 260 1 16
HELIX 15 AB6 ASP A 264 THR A 279 1 16
HELIX 16 AB7 PRO A 282 LYS A 291 1 10
HELIX 17 AB8 VAL A 294 GLY A 303 1 10
HELIX 18 AB9 GLU A 306 VAL A 321 1 16
HELIX 19 AC1 THR A 324 ALA A 334 1 11
HELIX 20 AC2 GLY A 335 ALA A 338 5 4
HELIX 21 AC3 VAL A 339 LEU A 344 1 6
HELIX 22 AC4 LYS A 348 THR A 363 1 16
HELIX 23 AC5 ARG A 366 HIS A 376 1 11
HELIX 24 AC6 LEU A 378 LYS A 388 1 11
HELIX 25 AC7 ASP A 390 GLY A 408 1 19
HELIX 26 AC8 THR A 409 CYS A 419 1 11
HELIX 27 AC9 ILE A 421 LEU A 428 1 8
HELIX 28 AD1 LEU A 429 ALA A 431 5 3
HELIX 29 AD2 ASP A 433 LEU A 454 1 22
HELIX 30 AD3 GLU A 456 CYS A 467 1 12
HELIX 31 AD4 GLY A 468 ALA A 475 1 8
HELIX 32 AD5 ASN A 481 PHE A 496 1 16
CISPEP 1 ASN A 241 PRO A 242 0 -2.58
SITE 1 AC1 9 SER A 360 ASN A 361 ALA A 364 GLU A 396
SITE 2 AC1 9 TRP A 399 ASN A 403 SER A 406 HOH A 633
SITE 3 AC1 9 HOH A 669
CRYST1 79.160 90.630 101.030 90.00 90.00 90.00 P 21 21 21 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 0.012633 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011034 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009898 0.00000
(ATOM LINES ARE NOT SHOWN.)
END