HEADER HYDROLASE 23-MAY-04 1TDL
TITLE STRUCTURE OF SER130GLY SHV-1 BETA-LACTAMASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-LACTAMASE SHV-1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PIT-2;
COMPND 5 EC: 3.5.2.6;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: KLEBSIELLA PNEUMONIAE;
SOURCE 3 ORGANISM_TAXID: 573;
SOURCE 4 GENE: BLA, SHV1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI STR. K-12 SUBSTR. DH10B;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 316385;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: DH10B;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PBC SK
KEYWDS CLASS A BETA-LACTAMASE, PENICILLINASE, BETA-LACTAM HYDROLASE,
KEYWDS 2 DETERGENT BINDING, DRUG DESIGN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.SUN,C.R.BETHEL,R.A.BONOMO,J.R.KNOX
REVDAT 5 23-AUG-23 1TDL 1 REMARK
REVDAT 4 27-OCT-21 1TDL 1 REMARK SEQADV
REVDAT 3 11-OCT-17 1TDL 1 REMARK
REVDAT 2 24-FEB-09 1TDL 1 VERSN
REVDAT 1 23-NOV-04 1TDL 0
JRNL AUTH T.SUN,C.R.BETHEL,R.A.BONOMO,J.R.KNOX
JRNL TITL INHIBITOR-RESISTANT CLASS A BETA-LACTAMASES: CONSEQUENCES OF
JRNL TITL 2 THE SER130-TO-GLY MUTATION SEEN IN APO AND TAZOBACTAM
JRNL TITL 3 STRUCTURES OF THE SHV-1 VARIANT
JRNL REF BIOCHEMISTRY V. 43 14111 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15518561
JRNL DOI 10.1021/BI0487903
REMARK 2
REMARK 2 RESOLUTION. 1.80 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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
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) (%) : 93.4
REMARK 3 NUMBER OF REFLECTIONS : 20611
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) : 0.142
REMARK 3 FREE R VALUE : 0.181
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1001
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 : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1670
REMARK 3 BIN FREE R VALUE : 0.2416
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 141
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 : 2022
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 414
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.40
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.14
REMARK 3 ESD FROM SIGMAA (A) : 0.09
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.18
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.16
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.400
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) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1TDL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUL-04.
REMARK 100 THE DEPOSITION ID IS D_1000022562.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-AUG-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : DOUBLE-MIRROR FRANKS FOCUSING
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SIEMENS HI-STAR
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : X-GEN
REMARK 200 DATA SCALING SOFTWARE : X-GEN
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20676
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 37.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.6
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.03300
REMARK 200 R SYM (I) : 0.03300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 34.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.91
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.06800
REMARK 200 R SYM FOR SHELL (I) : 0.06800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 12.10
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: EPMR
REMARK 200 STARTING MODEL: PDB ENTRY 1TDG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 6000, 50 MM HEPES, 0.56 MM
REMARK 280 CYMAL-6 DETERGENT, PH 7.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
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 24.80400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.04000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.65050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.04000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.80400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 27.65050
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: MONOMERIC
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 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 MET A 69 -150.41 58.23
REMARK 500 TYR A 105 88.31 70.80
REMARK 500 VAL A 159 -53.49 -120.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 MA4 A 810
REMARK 610 EPE A 900
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MA4 A 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MA4 A 810
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 900
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1SHV RELATED DB: PDB
REMARK 900 SHV-1 BETA-LACTAMASE (WILDTYPE)
REMARK 900 RELATED ID: 1TDG RELATED DB: PDB
REMARK 900 COMPLEX OF SER130GLY SHV-1 BETA-LACTAMASE WITH TAZOBACTAM
REMARK 900 RELATED ID: 1G56 RELATED DB: PDB
REMARK 900 COMPLEX OF SHV-1 WITH TAZOBACTAM
REMARK 900 RELATED ID: 1RCJ RELATED DB: PDB
REMARK 900 COMPLEX OF GLU166ALA SHV-1 WITH TAZOBACTAM
DBREF 1TDL A 26 292 UNP P14557 BLA1_ECOLI 22 286
SEQADV 1TDL GLY A 130 UNP P14557 SER 126 ENGINEERED MUTATION
SEQRES 1 A 265 SER PRO GLN PRO LEU GLU GLN ILE LYS LEU SER GLU SER
SEQRES 2 A 265 GLN LEU SER GLY ARG VAL GLY MET ILE GLU MET ASP LEU
SEQRES 3 A 265 ALA SER GLY ARG THR LEU THR ALA TRP ARG ALA ASP GLU
SEQRES 4 A 265 ARG PHE PRO MET MET SER THR PHE LYS VAL VAL LEU CYS
SEQRES 5 A 265 GLY ALA VAL LEU ALA ARG VAL ASP ALA GLY ASP GLU GLN
SEQRES 6 A 265 LEU GLU ARG LYS ILE HIS TYR ARG GLN GLN ASP LEU VAL
SEQRES 7 A 265 ASP TYR SER PRO VAL SER GLU LYS HIS LEU ALA ASP GLY
SEQRES 8 A 265 MET THR VAL GLY GLU LEU CYS ALA ALA ALA ILE THR MET
SEQRES 9 A 265 GLY ASP ASN SER ALA ALA ASN LEU LEU LEU ALA THR VAL
SEQRES 10 A 265 GLY GLY PRO ALA GLY LEU THR ALA PHE LEU ARG GLN ILE
SEQRES 11 A 265 GLY ASP ASN VAL THR ARG LEU ASP ARG TRP GLU THR GLU
SEQRES 12 A 265 LEU ASN GLU ALA LEU PRO GLY ASP ALA ARG ASP THR THR
SEQRES 13 A 265 THR PRO ALA SER MET ALA ALA THR LEU ARG LYS LEU LEU
SEQRES 14 A 265 THR SER GLN ARG LEU SER ALA ARG SER GLN ARG GLN LEU
SEQRES 15 A 265 LEU GLN TRP MET VAL ASP ASP ARG VAL ALA GLY PRO LEU
SEQRES 16 A 265 ILE ARG SER VAL LEU PRO ALA GLY TRP PHE ILE ALA ASP
SEQRES 17 A 265 LYS THR GLY ALA GLY GLU ARG GLY ALA ARG GLY ILE VAL
SEQRES 18 A 265 ALA LEU LEU GLY PRO ASN ASN LYS ALA GLU ARG ILE VAL
SEQRES 19 A 265 VAL ILE TYR LEU ARG ASP THR PRO ALA SER MET ALA GLU
SEQRES 20 A 265 ARG ASN GLN GLN ILE ALA GLY ILE GLY ALA ALA LEU ILE
SEQRES 21 A 265 GLU HIS TRP GLN ARG
HET MA4 A 800 47
HET MA4 A 810 10
HET EPE A 900 5
HETNAM MA4 CYCLOHEXYL-HEXYL-BETA-D-MALTOSIDE
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETSYN EPE HEPES
FORMUL 2 MA4 2(C24 H44 O11)
FORMUL 4 EPE C8 H18 N2 O4 S
FORMUL 5 HOH *414(H2 O)
HELIX 1 1 GLN A 28 SER A 41 1 14
HELIX 2 2 THR A 71 ALA A 86 1 16
HELIX 3 3 ARG A 98 LEU A 102 5 5
HELIX 4 4 VAL A 108 HIS A 112 5 5
HELIX 5 5 VAL A 119 GLY A 130 1 12
HELIX 6 6 ASP A 131 VAL A 142 1 12
HELIX 7 7 GLY A 143 ILE A 155 1 13
HELIX 8 8 THR A 167 GLU A 171 5 5
HELIX 9 9 THR A 182 SER A 196 1 15
HELIX 10 10 SER A 200 ASP A 213 1 14
HELIX 11 11 ALA A 217 LEU A 225 1 9
HELIX 12 12 SER A 271 HIS A 289 1 19
SHEET 1 A 5 THR A 56 TRP A 60 0
SHEET 2 A 5 ARG A 43 ASP A 50 -1 N GLU A 48 O LEU A 57
SHEET 3 A 5 ARG A 259 ARG A 266 -1 O ILE A 260 N MET A 49
SHEET 4 A 5 ARG A 244 GLY A 251 -1 N ARG A 244 O LEU A 265
SHEET 5 A 5 PHE A 230 ALA A 237 -1 N PHE A 230 O GLY A 251
SHEET 1 B 2 PHE A 66 PRO A 67 0
SHEET 2 B 2 THR A 180 THR A 181 -1 O THR A 181 N PHE A 66
SHEET 1 C 2 LYS A 94 ILE A 95 0
SHEET 2 C 2 MET A 117 THR A 118 -1 O MET A 117 N ILE A 95
SSBOND 1 CYS A 77 CYS A 123 1555 1555 2.03
CISPEP 1 GLU A 166 THR A 167 0 0.85
SITE 1 AC1 20 ARG A 93 LYS A 94 ILE A 95 HIS A 96
SITE 2 AC1 20 ARG A 98 VAL A 224 PRO A 226 ILE A 231
SITE 3 AC1 20 ILE A 246 ALA A 248 VAL A 261 ILE A 279
SITE 4 AC1 20 ALA A 280 ALA A 284 GLU A 288 HOH A 313
SITE 5 AC1 20 HOH A 360 HOH A 444 HOH A 447 HOH A 619
SITE 1 AC2 3 LEU A 220 ARG A 244 ILE A 279
SITE 1 AC3 6 SER A 70 LYS A 73 GLY A 130 LYS A 234
SITE 2 AC3 6 HOH A 359 HOH A 545
CRYST1 49.608 55.301 84.080 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 0.020158 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018083 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011893 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
