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HEADER HYDROLASE 30-JUN-19 6KD0
TITLE CRYSTAL STRUCTURE OF VIBRALACTONE CYCLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VIBRALACTONE CYCLASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOREOSTEREUM VIBRANS;
SOURCE 3 ORGANISM_TAXID: 1826779;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS VIBRALACTONE CYCLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ZENG,K.N.FENG
REVDAT 1 24-JUN-20 6KD0 0
JRNL AUTH K.N.FENG,Y.L.YANG,Y.X.XU,Y.ZHANG,T.FENG,S.X.HUANG,J.K.LIU,
JRNL AUTH 2 Y.ZENG
JRNL TITL A HYDROLASE-CATALYZED CYCLIZATION FORMS THE FUSED BICYCLIC
JRNL TITL 2 BETA-LACTONE IN VIBRALACTONE.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 59 7209 2020
JRNL REFN ESSN 1521-3773
JRNL PMID 32050043
JRNL DOI 10.1002/ANIE.202000710
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 37766
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 2019
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.84
REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.1700
REMARK 3 BIN FREE R VALUE SET COUNT : NULL
REMARK 3 BIN FREE R VALUE : 0.2000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2728
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 268
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6KD0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-JUL-19.
REMARK 100 THE DEPOSITION ID IS D_1300012756.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-MAY-19
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 : SSRF
REMARK 200 BEAMLINE : BL18U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.988
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39851
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.1000
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) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.63100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.300
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: 5LK6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
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 40.11700
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: 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 ALA A 2 -164.12 -103.76
REMARK 500 LEU A 7 -87.19 -96.68
REMARK 500 GLU A 9 43.62 140.75
REMARK 500 VAL A 45 -57.04 -121.66
REMARK 500 TRP A 106 -9.69 73.99
REMARK 500 PRO A 143 35.83 -98.49
REMARK 500 SER A 177 -122.08 56.75
REMARK 500 TYR A 208 57.35 36.87
REMARK 500 LEU A 236 -16.97 72.52
REMARK 500 TRP A 280 73.48 -101.39
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6KD0 A 1 343 PDB 6KD0 6KD0 1 343
SEQRES 1 A 343 MET ALA ILE THR LEU PHE LEU ASP GLU GLY LEU SER THR
SEQRES 2 A 343 ALA HIS PRO GLU PHE ALA PRO VAL TRP ALA ALA PHE PRO
SEQRES 3 A 343 GLN PRO THR ASP PRO PHE PRO PRO LEU GLU ALA ARG ARG
SEQRES 4 A 343 ALA PHE TRP ASP GLU VAL VAL ILE PRO ASN LEU ASN LYS
SEQRES 5 A 343 PHE LEU GLU PRO SER LEU PRO SER GLU ASP ARG TYR ARG
SEQRES 6 A 343 LEU GLU ASP TYR TYR ILE PRO VAL GLU GLY THR ASN MET
SEQRES 7 A 343 HIS VAL ARG THR TYR ILE PRO THR SER SER PRO ASP LYS
SEQRES 8 A 343 THR LYS THR TYR PRO LEU LEU TYR TRP VAL HIS CYS GLY
SEQRES 9 A 343 GLY TRP ALA ILE GLY ASN TYR GLU MET ASP ASP TYR ASP
SEQRES 10 A 343 LEU ARG ILE ILE CYS ASP LYS LEU GLN VAL CYS ALA VAL
SEQRES 11 A 343 SER ILE ASP TYR ARG LEU THR PRO GLU SER SER SER PRO
SEQRES 12 A 343 THR GLY ALA LYS ASP VAL TYR ALA GLY LEU LYS TRP ALA
SEQRES 13 A 343 ALA ALA ASN ALA GLY SER PHE ASN ALA ASP PRO LYS LYS
SEQRES 14 A 343 GLY PHE VAL ILE ALA GLY GLN SER ALA GLY GLY ASN LEU
SEQRES 15 A 343 SER LEU ILE ALA ALA HIS TRP ALA ARG ASP ASP PRO PHE
SEQRES 16 A 343 PHE ALA ASN THR PRO LEU THR GLY GLN LEU VAL GLN TYR
SEQRES 17 A 343 PRO PRO THR CYS HIS PRO GLU ALA MET PRO GLU GLU TYR
SEQRES 18 A 343 LYS SER CYS ILE LYS SER MET GLU GLU CYS ARG ASP ALA
SEQRES 19 A 343 PRO LEU LEU SER LYS LYS GLU VAL TYR TRP PHE ASN GLU
SEQRES 20 A 343 LEU ALA ASN PRO ALA ASP PRO HIS ASP PRO SER PHE SER
SEQRES 21 A 343 PRO LEU LEU PHE PRO SER HIS ALA ASN LEU PRO PRO LEU
SEQRES 22 A 343 PHE PHE MET SER CYS GLY TRP ASP PRO LEU ARG ASP GLU
SEQRES 23 A 343 GLY LEU LEU TYR HIS ALA LEU VAL LYS GLU ALA GLY VAL
SEQRES 24 A 343 GLU THR ARG MET THR MET TYR PRO GLY VAL PRO HIS ALA
SEQRES 25 A 343 PHE HIS MET LEU PHE ARG SER MET LYS LEU ALA GLN LYS
SEQRES 26 A 343 PHE GLN GLU GLU THR ILE GLU GLY MET SER TRP LEU PHE
SEQRES 27 A 343 SER LYS THR PRO GLN
FORMUL 2 HOH *268(H2 O)
HELIX 1 AA1 GLU A 17 PHE A 25 1 9
HELIX 2 AA2 PRO A 34 VAL A 45 1 12
HELIX 3 AA3 VAL A 45 GLU A 55 1 11
HELIX 4 AA4 PRO A 56 LEU A 58 5 3
HELIX 5 AA5 SER A 60 ASP A 62 5 3
HELIX 6 AA6 ASN A 110 MET A 113 5 4
HELIX 7 AA7 ASP A 114 GLN A 126 1 13
HELIX 8 AA8 PRO A 143 ASN A 159 1 17
HELIX 9 AA9 ALA A 160 ASN A 164 5 5
HELIX 10 AB1 ASP A 166 LYS A 169 5 4
HELIX 11 AB2 SER A 177 ASP A 193 1 17
HELIX 12 AB3 PRO A 194 ALA A 197 5 4
HELIX 13 AB4 HIS A 213 MET A 217 5 5
HELIX 14 AB5 PRO A 218 ILE A 225 5 8
HELIX 15 AB6 LYS A 226 CYS A 231 1 6
HELIX 16 AB7 SER A 238 ASN A 250 1 13
HELIX 17 AB8 SER A 260 PHE A 264 5 5
HELIX 18 AB9 LEU A 283 ALA A 297 1 15
HELIX 19 AC1 ALA A 312 PHE A 317 1 6
HELIX 20 AC2 MET A 320 SER A 339 1 20
SHEET 1 AA1 8 TYR A 64 VAL A 73 0
SHEET 2 AA1 8 THR A 76 PRO A 85 -1 O THR A 76 N VAL A 73
SHEET 3 AA1 8 CYS A 128 ILE A 132 -1 O SER A 131 N ARG A 81
SHEET 4 AA1 8 LEU A 97 VAL A 101 1 N TRP A 100 O VAL A 130
SHEET 5 AA1 8 PHE A 171 GLN A 176 1 O VAL A 172 N TYR A 99
SHEET 6 AA1 8 GLY A 203 GLN A 207 1 O LEU A 205 N ILE A 173
SHEET 7 AA1 8 LEU A 273 TRP A 280 1 O PHE A 274 N GLN A 204
SHEET 8 AA1 8 THR A 301 PRO A 310 1 O TYR A 306 N GLY A 279
CISPEP 1 THR A 137 PRO A 138 0 -6.13
CISPEP 2 SER A 142 PRO A 143 0 9.01
CRYST1 47.324 80.234 59.184 90.00 102.36 90.00 P 1 21 1 2
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 0.021131 0.000000 0.004630 0.00000
SCALE2 0.000000 0.012464 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017297 0.00000
TER 2729 GLN A 343
MASTER 252 0 0 20 8 0 0 6 2996 1 0 27
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