HEADER HYDROLASE 30-JUN-10 3NR1
TITLE A METAZOAN ORTHOLOG OF SPOT HYDROLYZES PPGPP AND PLAYS A ROLE IN
TITLE 2 STARVATION RESPONSES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HD DOMAIN-CONTAINING PROTEIN 3;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: METAZOAN SPOT HOMOLOG 1, MESH1;
COMPND 5 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: HDDC3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28(A)
KEYWDS STRINGENT RESPONSE, PYROPHOSPHOHYDROLASE, HD (HISTIDINE AND ASPARTIC
KEYWDS 2 ACID) FAMILY, PPGPP HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.W.SUN,H.Y.KIM,K.J.KIM,Y.H.JEON,J.CHUNG
REVDAT 4 27-DEC-23 3NR1 1 REMARK LINK
REVDAT 3 08-NOV-17 3NR1 1 REMARK
REVDAT 2 09-OCT-13 3NR1 1 JRNL VERSN
REVDAT 1 08-SEP-10 3NR1 0
JRNL AUTH D.W.SUN,G.LEE,J.H.LEE,H.Y.KIM,H.W.RHEE,S.Y.PARK,K.J.KIM,
JRNL AUTH 2 Y.KIM,B.Y.KIM,J.I.HONG,C.PARK,H.E.CHOY,J.H.KIM,Y.H.JEON,
JRNL AUTH 3 J.CHUNG
JRNL TITL A METAZOAN ORTHOLOG OF SPOT HYDROLYZES PPGPP AND FUNCTIONS
JRNL TITL 2 IN STARVATION RESPONSES
JRNL REF NAT.STRUCT.MOL.BIOL. V. 17 1188 2010
JRNL REFN ISSN 1545-9993
JRNL PMID 20818390
JRNL DOI 10.1038/NSMB.1906
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 27178
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.700
REMARK 3 FREE R VALUE TEST SET COUNT : 1890
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 2850
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 220
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.39
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.17700
REMARK 3 B22 (A**2) : -0.36900
REMARK 3 B33 (A**2) : 0.19100
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 3.99700
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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) : 1.225 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.838 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.296 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.499 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 64.58
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 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3NR1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-JUL-10.
REMARK 100 THE DEPOSITION ID IS D_1000060172.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-SEP-07; 06-MAR-08
REMARK 200 TEMPERATURE (KELVIN) : 293; NULL
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : PAL/PLS; PAL/PLS
REMARK 200 BEAMLINE : 4A; 6C1
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97953; 0.97955
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210; ADSC QUANTUM
REMARK 200 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28330
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.35400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SAD; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE 2.13, RESOLVE 2.13
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-25% PEG 3350, 0.2M SODIUM CITRATE,
REMARK 280 PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 296K
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 31.20000
REMARK 290 SMTRY3 2 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: 2440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
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 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 199 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 35 NE2
REMARK 620 2 HIS A 61 NE2 89.3
REMARK 620 3 ASP A 62 OD2 103.1 72.1
REMARK 620 4 ASP A 122 OD1 79.9 98.4 169.8
REMARK 620 5 HOH A 304 O 112.2 157.5 95.6 92.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 199 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 35 NE2
REMARK 620 2 HIS B 61 NE2 87.4
REMARK 620 3 ASP B 62 OD2 101.0 68.5
REMARK 620 4 ASP B 122 OD1 82.0 100.1 167.9
REMARK 620 5 HOH B 275 O 102.8 165.9 99.7 91.0
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 199
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 199
DBREF 3NR1 A 2 179 UNP Q8N4P3 HDDC3_HUMAN 2 179
DBREF 3NR1 B 2 179 UNP Q8N4P3 HDDC3_HUMAN 2 179
SEQRES 1 A 178 GLY SER GLU ALA ALA GLN LEU LEU GLU ALA ALA ASP PHE
SEQRES 2 A 178 ALA ALA ARG LYS HIS ARG GLN GLN ARG ARG LYS ASP PRO
SEQRES 3 A 178 GLU GLY THR PRO TYR ILE ASN HIS PRO ILE GLY VAL ALA
SEQRES 4 A 178 ARG ILE LEU THR HIS GLU ALA GLY ILE THR ASP ILE VAL
SEQRES 5 A 178 VAL LEU GLN ALA ALA LEU LEU HIS ASP THR VAL GLU ASP
SEQRES 6 A 178 THR ASP THR THR LEU ASP GLU VAL GLU LEU HIS PHE GLY
SEQRES 7 A 178 ALA GLN VAL ARG ARG LEU VAL GLU GLU VAL THR ASP ASP
SEQRES 8 A 178 LYS THR LEU PRO LYS LEU GLU ARG LYS ARG LEU GLN VAL
SEQRES 9 A 178 GLU GLN ALA PRO HIS SER SER PRO GLY ALA LYS LEU VAL
SEQRES 10 A 178 LYS LEU ALA ASP LYS LEU TYR ASN LEU ARG ASP LEU ASN
SEQRES 11 A 178 ARG CYS THR PRO GLU GLY TRP SER GLU HIS ARG VAL GLN
SEQRES 12 A 178 GLU TYR PHE GLU TRP ALA ALA GLN VAL VAL LYS GLY LEU
SEQRES 13 A 178 GLN GLY THR ASN ARG GLN LEU GLU GLU ALA LEU LYS HIS
SEQRES 14 A 178 LEU PHE LYS GLN ARG GLY LEU THR ILE
SEQRES 1 B 178 GLY SER GLU ALA ALA GLN LEU LEU GLU ALA ALA ASP PHE
SEQRES 2 B 178 ALA ALA ARG LYS HIS ARG GLN GLN ARG ARG LYS ASP PRO
SEQRES 3 B 178 GLU GLY THR PRO TYR ILE ASN HIS PRO ILE GLY VAL ALA
SEQRES 4 B 178 ARG ILE LEU THR HIS GLU ALA GLY ILE THR ASP ILE VAL
SEQRES 5 B 178 VAL LEU GLN ALA ALA LEU LEU HIS ASP THR VAL GLU ASP
SEQRES 6 B 178 THR ASP THR THR LEU ASP GLU VAL GLU LEU HIS PHE GLY
SEQRES 7 B 178 ALA GLN VAL ARG ARG LEU VAL GLU GLU VAL THR ASP ASP
SEQRES 8 B 178 LYS THR LEU PRO LYS LEU GLU ARG LYS ARG LEU GLN VAL
SEQRES 9 B 178 GLU GLN ALA PRO HIS SER SER PRO GLY ALA LYS LEU VAL
SEQRES 10 B 178 LYS LEU ALA ASP LYS LEU TYR ASN LEU ARG ASP LEU ASN
SEQRES 11 B 178 ARG CYS THR PRO GLU GLY TRP SER GLU HIS ARG VAL GLN
SEQRES 12 B 178 GLU TYR PHE GLU TRP ALA ALA GLN VAL VAL LYS GLY LEU
SEQRES 13 B 178 GLN GLY THR ASN ARG GLN LEU GLU GLU ALA LEU LYS HIS
SEQRES 14 B 178 LEU PHE LYS GLN ARG GLY LEU THR ILE
HET MN A 199 1
HET MN B 199 1
HETNAM MN MANGANESE (II) ION
FORMUL 3 MN 2(MN 2+)
FORMUL 5 HOH *220(H2 O)
HELIX 1 1 SER A 3 HIS A 19 1 17
HELIX 2 2 ILE A 33 GLU A 46 1 14
HELIX 3 3 ASP A 51 HIS A 61 1 11
HELIX 4 4 ASP A 62 THR A 67 1 6
HELIX 5 5 THR A 70 VAL A 89 1 20
HELIX 6 6 PRO A 96 ALA A 108 1 13
HELIX 7 7 PRO A 109 SER A 111 5 3
HELIX 8 8 SER A 112 CYS A 133 1 22
HELIX 9 9 SER A 139 GLN A 158 1 20
HELIX 10 10 ASN A 161 GLN A 174 1 14
HELIX 11 11 SER B 3 HIS B 19 1 17
HELIX 12 12 ILE B 33 GLU B 46 1 14
HELIX 13 13 ASP B 51 HIS B 61 1 11
HELIX 14 14 ASP B 62 THR B 67 1 6
HELIX 15 15 THR B 70 VAL B 89 1 20
HELIX 16 16 PRO B 96 ALA B 108 1 13
HELIX 17 17 PRO B 109 SER B 111 5 3
HELIX 18 18 SER B 112 CYS B 133 1 22
HELIX 19 19 SER B 139 GLY B 156 1 18
HELIX 20 20 ASN B 161 ARG B 175 1 15
LINK NE2 HIS A 35 MN MN A 199 1555 1555 2.32
LINK NE2 HIS A 61 MN MN A 199 1555 1555 2.26
LINK OD2 ASP A 62 MN MN A 199 1555 1555 2.55
LINK OD1 ASP A 122 MN MN A 199 1555 1555 2.25
LINK MN MN A 199 O HOH A 304 1555 1555 2.31
LINK NE2 HIS B 35 MN MN B 199 1555 1555 2.35
LINK NE2 HIS B 61 MN MN B 199 1555 1555 2.28
LINK OD2 ASP B 62 MN MN B 199 1555 1555 2.56
LINK OD1 ASP B 122 MN MN B 199 1555 1555 2.22
LINK MN MN B 199 O HOH B 275 1555 1555 2.29
SITE 1 AC1 5 HIS A 35 HIS A 61 ASP A 62 ASP A 122
SITE 2 AC1 5 HOH A 304
SITE 1 AC2 5 HIS B 35 HIS B 61 ASP B 62 ASP B 122
SITE 2 AC2 5 HOH B 275
CRYST1 53.900 62.400 53.900 90.00 95.30 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 0.018553 0.000000 0.001721 0.00000
SCALE2 0.000000 0.016026 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018633 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
