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HEADER HYDROLASE 04-JUN-24 8ZRG
TITLE ARABIDOPSIS CARBOXYLESTERASE CXE15 C14S MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STRIGOLACTONES HYDROLASE CXE15;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CARBOXYLESTERASE 15,ATCXE15;
COMPND 5 EC: 3.1.1.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: THALE CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: CXE15, AT5G06570, F15M7.10;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 866768
KEYWDS CATABOLIC ENZYME, STRIGOLACTOONE, CARBOXYLESTERASE, CXE15, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.T.AROLD,U.F.S.HAMEED
REVDAT 1 28-MAY-25 8ZRG 0
JRNL AUTH S.T.AROLD,U.F.S.HAMEED
JRNL TITL ARABIDOPSIS CARBOXYLESTERASE CXE15 C14S MUTANT
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC V5.7
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.07
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 10510
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 + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.500
REMARK 3 FREE R VALUE TEST SET COUNT : 972
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2491
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 29
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 64.47
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.17000
REMARK 3 B22 (A**2) : -0.17000
REMARK 3 B33 (A**2) : 0.33000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 1.200
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.315
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.240
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.015
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; 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 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 8ZRG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-JUN-24.
REMARK 100 THE DEPOSITION ID IS D_1300048410.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-MAY-24
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) : 0.987
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12939
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.750
REMARK 200 RESOLUTION RANGE LOW (A) : 49.070
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 20.00
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.2600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.3
REMARK 200 DATA REDUNDANCY IN SHELL : 15.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.910
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: AF-Q9FG13-F1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.056 M SODIUM PHOSPHATE MONOBASIC
REMARK 280 MONOHYDRATE, 1.344 M POTASSIUM PHOSPHATE DIBASIC, PH 8.2, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 60.44400
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 41.90750
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 41.90750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 30.22200
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 41.90750
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 41.90750
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 90.66600
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 41.90750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 41.90750
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 30.22200
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 41.90750
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 41.90750
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 90.66600
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 60.44400
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: 5630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 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 350 BIOMT1 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 60.44400
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 SER A 169 -120.86 48.19
REMARK 500 LEU A 220 -48.36 -134.18
REMARK 500 ARG A 240 1.39 -69.95
REMARK 500 PHE A 248 71.17 -151.70
REMARK 500 LEU A 255 -4.75 64.54
REMARK 500 ASN A 299 14.00 59.37
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 92 0.16 SIDE CHAIN
REMARK 500 ARG A 162 0.08 SIDE CHAIN
REMARK 500 ARG A 193 0.12 SIDE CHAIN
REMARK 500 ARG A 291 0.29 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 429 DISTANCE = 6.42 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 8ZR6 RELATED DB: PDB
DBREF 8ZRG A 14 329 UNP Q9FG13 CXE15_ARATH 14 329
SEQADV 8ZRG SER A 14 UNP Q9FG13 CYS 14 ENGINEERED MUTATION
SEQRES 1 A 316 SER MET GLY LEU LEU GLN LEU LEU SER ASN GLY THR VAL
SEQRES 2 A 316 LEU ARG SER GLU SER ILE ASP LEU ILE THR GLN GLN ILE
SEQRES 3 A 316 PRO PHE LYS ASN ASN GLN THR VAL LEU PHE LYS ASP SER
SEQRES 4 A 316 ILE TYR HIS LYS PRO ASN ASN LEU HIS LEU ARG LEU TYR
SEQRES 5 A 316 LYS PRO ILE SER ALA SER ASN ARG THR ALA LEU PRO VAL
SEQRES 6 A 316 VAL VAL PHE PHE HIS GLY GLY GLY PHE CYS PHE GLY SER
SEQRES 7 A 316 ARG SER TRP PRO HIS PHE HIS ASN PHE CYS LEU THR LEU
SEQRES 8 A 316 ALA SER SER LEU ASN ALA LEU VAL VAL SER PRO ASP TYR
SEQRES 9 A 316 ARG LEU ALA PRO GLU HIS ARG LEU PRO ALA ALA PHE GLU
SEQRES 10 A 316 ASP ALA GLU ALA VAL LEU THR TRP LEU TRP ASP GLN ALA
SEQRES 11 A 316 VAL SER ASP GLY VAL ASN HIS TRP PHE GLU ASP GLY THR
SEQRES 12 A 316 ASP VAL ASP PHE ASP ARG VAL PHE VAL VAL GLY ASP SER
SEQRES 13 A 316 SER GLY GLY ASN ILE ALA HIS GLN LEU ALA VAL ARG PHE
SEQRES 14 A 316 GLY SER GLY SER ILE GLU LEU THR PRO VAL ARG VAL ARG
SEQRES 15 A 316 GLY TYR VAL LEU MET GLY PRO PHE PHE GLY GLY GLU GLU
SEQRES 16 A 316 ARG THR ASN SER GLU ASN GLY PRO SER GLU ALA LEU LEU
SEQRES 17 A 316 SER LEU ASP LEU LEU ASP LYS PHE TRP ARG LEU SER LEU
SEQRES 18 A 316 PRO ASN GLY ALA THR ARG ASP HIS HIS MET ALA ASN PRO
SEQRES 19 A 316 PHE GLY PRO THR SER PRO THR LEU GLU SER ILE SER LEU
SEQRES 20 A 316 GLU PRO MET LEU VAL ILE VAL GLY GLY SER GLU LEU LEU
SEQRES 21 A 316 ARG ASP ARG ALA LYS GLU TYR ALA TYR LYS LEU LYS LYS
SEQRES 22 A 316 MET GLY GLY LYS ARG VAL ASP TYR ILE GLU PHE GLU ASN
SEQRES 23 A 316 LYS GLU HIS GLY PHE TYR SER ASN TYR PRO SER SER GLU
SEQRES 24 A 316 ALA ALA GLU GLN VAL LEU ARG ILE ILE GLY ASP PHE MET
SEQRES 25 A 316 ASN ASN LEU SER
FORMUL 2 HOH *29(H2 O)
HELIX 1 AA1 GLY A 16 GLY A 24 1 9
HELIX 2 AA2 SER A 69 ASN A 72 5 4
HELIX 3 AA3 TRP A 94 ASN A 109 1 16
HELIX 4 AA4 PRO A 126 VAL A 144 1 19
HELIX 5 AA5 ASP A 146 TRP A 151 5 6
HELIX 6 AA6 SER A 169 SER A 184 1 16
HELIX 7 AA7 THR A 210 GLY A 215 1 6
HELIX 8 AA8 SER A 222 LEU A 234 1 13
HELIX 9 AA9 LEU A 273 MET A 287 1 15
HELIX 10 AB1 GLY A 303 TYR A 308 1 6
HELIX 11 AB2 SER A 311 ASN A 327 1 17
SHEET 1 AA1 8 VAL A 47 HIS A 55 0
SHEET 2 AA1 8 LEU A 60 PRO A 67 -1 O LYS A 66 N LEU A 48
SHEET 3 AA1 8 LEU A 111 PRO A 115 -1 O SER A 114 N ARG A 63
SHEET 4 AA1 8 LEU A 76 PHE A 82 1 N VAL A 79 O VAL A 113
SHEET 5 AA1 8 VAL A 158 ASP A 168 1 O ARG A 162 N VAL A 78
SHEET 6 AA1 8 VAL A 194 MET A 200 1 O MET A 200 N GLY A 167
SHEET 7 AA1 8 MET A 263 GLY A 268 1 O LEU A 264 N LEU A 199
SHEET 8 AA1 8 VAL A 292 PHE A 297 1 O ILE A 295 N VAL A 265
CISPEP 1 ALA A 120 PRO A 121 0 19.10
CISPEP 2 LEU A 125 PRO A 126 0 19.62
CISPEP 3 THR A 190 PRO A 191 0 30.00
CRYST1 83.815 83.815 120.888 90.00 90.00 90.00 P 41 21 2 8
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 0.011931 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011931 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008272 0.00000
TER 2492 SER A 329
MASTER 272 0 0 11 8 0 0 6 2520 1 0 25
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