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HEADER HYDROLASE 03-SEP-20 7CY0
TITLE CRYSTAL STRUCTURE OF A NEW PETASE TRIPLE MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(ETHYLENE TEREPHTHALATE) HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PETASE,PET-DIGESTING ENZYME;
COMPND 5 EC: 3.1.1.101;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: IDEONELLA SAKAIENSIS (STRAIN NBRC 110686 /
SOURCE 3 TISTR 2288 / 201-F6);
SOURCE 4 ORGANISM_TAXID: 1547922;
SOURCE 5 STRAIN: NBRC 110686 / TISTR 2288 / 201-F6;
SOURCE 6 GENE: ISF6_4831;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET32A
KEYWDS POLY(ETHYLENE TEREPHTHALATE) HYDROLASE, SUBSTRATE BINDING, INHIBITOR,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.HAN,W.D.LIU,Y.Y.ZHENG,C.C.CHEN,R.T.GUO
REVDAT 1 26-MAY-21 7CY0 0
JRNL AUTH X.HAN,W.D.LIU,Y.Y.ZHENG,C.C.CHEN,R.T.GUO
JRNL TITL CRYSTAL STRUCTURE OF A NEW PETASE TRIPLE MUTANT
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.32 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0266
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.32
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 48671
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) : 0.145
REMARK 3 R VALUE (WORKING SET) : 0.144
REMARK 3 FREE R VALUE : 0.166
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2481
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.32
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3409
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.09
REMARK 3 BIN R VALUE (WORKING SET) : 0.2160
REMARK 3 BIN FREE R VALUE SET COUNT : 208
REMARK 3 BIN FREE R VALUE : 0.2550
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1915
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 330
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.77
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.52000
REMARK 3 B22 (A**2) : -0.61000
REMARK 3 B33 (A**2) : 1.13000
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): 0.047
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.049
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.029
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.685
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.977
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.971
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1984 ; 0.010 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 1792 ; 0.000 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2707 ; 1.495 ; 1.641
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4129 ; 1.539 ; 1.572
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 266 ; 6.828 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 89 ;31.495 ;21.798
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 285 ;10.390 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;15.846 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 270 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2359 ; 0.016 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 473 ; 0.007 ; 0.020
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 : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 7CY0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-SEP-20.
REMARK 100 THE DEPOSITION ID IS D_1300018376.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-OCT-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSRRC
REMARK 200 BEAMLINE : BL15A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51200
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.320
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.04500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.32
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.5
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : 0.43800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 5XG0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: POLYETHYLENE GLYCOL 6000, GLYCEROL,
REMARK 280 MES, PH 6.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
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 25.46250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.14350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.90300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.14350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.46250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 25.90300
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 ASN A 44 38.37 -149.27
REMARK 500 THR A 59 -4.15 74.12
REMARK 500 ALA A 131 -118.19 65.37
REMARK 500 ALA A 180 67.20 -118.44
REMARK 500 HIS A 185 -84.07 -122.64
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 7CY0 A 1 261 UNP PETH_IDESA
DBREF2 7CY0 A A0A0K8P6T7 30 290
SEQADV 7CY0 GLY A 103 UNP A0A0K8P6T ARG 132 ENGINEERED MUTATION
SEQADV 7CY0 ALA A 131 UNP A0A0K8P6T SER 160 ENGINEERED MUTATION
SEQADV 7CY0 HIS A 185 UNP A0A0K8P6T SER 214 ENGINEERED MUTATION
SEQRES 1 A 261 ASN PRO TYR ALA ARG GLY PRO ASN PRO THR ALA ALA SER
SEQRES 2 A 261 LEU GLU ALA SER ALA GLY PRO PHE THR VAL ARG SER PHE
SEQRES 3 A 261 THR VAL SER ARG PRO SER GLY TYR GLY ALA GLY THR VAL
SEQRES 4 A 261 TYR TYR PRO THR ASN ALA GLY GLY THR VAL GLY ALA ILE
SEQRES 5 A 261 ALA ILE VAL PRO GLY TYR THR ALA ARG GLN SER SER ILE
SEQRES 6 A 261 LYS TRP TRP GLY PRO ARG LEU ALA SER HIS GLY PHE VAL
SEQRES 7 A 261 VAL ILE THR ILE ASP THR ASN SER THR LEU ASP GLN PRO
SEQRES 8 A 261 SER SER ARG SER SER GLN GLN MET ALA ALA LEU GLY GLN
SEQRES 9 A 261 VAL ALA SER LEU ASN GLY THR SER SER SER PRO ILE TYR
SEQRES 10 A 261 GLY LYS VAL ASP THR ALA ARG MET GLY VAL MET GLY TRP
SEQRES 11 A 261 ALA MET GLY GLY GLY GLY SER LEU ILE SER ALA ALA ASN
SEQRES 12 A 261 ASN PRO SER LEU LYS ALA ALA ALA PRO GLN ALA PRO TRP
SEQRES 13 A 261 ASP SER SER THR ASN PHE SER SER VAL THR VAL PRO THR
SEQRES 14 A 261 LEU ILE PHE ALA CYS GLU ASN ASP SER ILE ALA PRO VAL
SEQRES 15 A 261 ASN SER HIS ALA LEU PRO ILE TYR ASP SER MET SER ARG
SEQRES 16 A 261 ASN ALA LYS GLN PHE LEU GLU ILE ASN GLY GLY SER HIS
SEQRES 17 A 261 SER CYS ALA ASN SER GLY ASN SER ASN GLN ALA LEU ILE
SEQRES 18 A 261 GLY LYS LYS GLY VAL ALA TRP MET LYS ARG PHE MET ASP
SEQRES 19 A 261 ASN ASP THR ARG TYR SER THR PHE ALA CYS GLU ASN PRO
SEQRES 20 A 261 ASN SER THR ARG VAL SER ASP PHE ARG THR ALA ASN CYS
SEQRES 21 A 261 SER
HET ACY A 301 4
HET ACY A 302 4
HET ACY A 303 4
HETNAM ACY ACETIC ACID
FORMUL 2 ACY 3(C2 H4 O2)
FORMUL 5 HOH *330(H2 O)
HELIX 1 AA1 THR A 10 ALA A 16 1 7
HELIX 2 AA2 ARG A 61 LYS A 66 5 6
HELIX 3 AA3 TRP A 67 SER A 74 1 8
HELIX 4 AA4 GLN A 90 GLY A 110 1 21
HELIX 5 AA5 ALA A 131 ASN A 144 1 14
HELIX 6 AA6 HIS A 185 MET A 193 1 9
HELIX 7 AA7 ASN A 217 ASP A 234 1 18
HELIX 8 AA8 ASP A 236 ARG A 238 5 3
HELIX 9 AA9 TYR A 239 GLU A 245 1 7
SHEET 1 AA1 6 VAL A 23 THR A 27 0
SHEET 2 AA1 6 ALA A 36 PRO A 42 -1 O VAL A 39 N PHE A 26
SHEET 3 AA1 6 VAL A 78 ASP A 83 -1 O VAL A 79 N TYR A 40
SHEET 4 AA1 6 VAL A 49 VAL A 55 1 N ILE A 54 O ILE A 80
SHEET 5 AA1 6 VAL A 120 GLY A 129 1 O ASP A 121 N VAL A 49
SHEET 6 AA1 6 ALA A 149 ALA A 150 1 O ALA A 149 N VAL A 127
SHEET 1 AA2 3 THR A 169 CYS A 174 0
SHEET 2 AA2 3 LYS A 198 ILE A 203 1 O GLN A 199 N ILE A 171
SHEET 3 AA2 3 VAL A 252 ALA A 258 -1 O ASP A 254 N GLU A 202
SSBOND 1 CYS A 174 CYS A 210 1555 1555 2.05
SSBOND 2 CYS A 244 CYS A 260 1555 1555 2.09
CRYST1 50.925 51.806 84.287 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 0.019637 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019303 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011864 0.00000
TER 1928 SER A 261
MASTER 256 0 3 9 9 0 0 6 2257 1 16 21
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