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HEADER HYDROLASE 25-OCT-17 5YNS
TITLE CRYSTAL STRCUTURE OF PETASE R280A MUTANT FROM IDEONELLA SAKAIENSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(ETHYLENE TEREPHTHALATE) HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: A/B HYDROLASE SUPERFAMILY;
COMPND 5 SYNONYM: PETASE;
COMPND 6 EC: 3.1.1.101;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: IDEONELLA SAKAIENSIS (STRAIN 201-F6);
SOURCE 3 ORGANISM_TAXID: 1547922;
SOURCE 4 STRAIN: 201-F6;
SOURCE 5 GENE: ISF6_4831;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA GAMI-B;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.JOO,K.-J.KIM
REVDAT 1 14-FEB-18 5YNS 0
JRNL AUTH S.JOO,I.J.CHO,H.SEO,H.F.SON,H.-Y.SAGONG,T.J.SHIN,S.Y.CHOI,
JRNL AUTH 2 S.Y.LEE,K.-J.KIM
JRNL TITL STRUCTURAL INSIGHT INTO MOLECULAR MECHANISM OF POLY(ETHYLENE
JRNL TITL 2 TEREPHTHALATE) DEGRADATION.
JRNL REF NAT COMMUN V. 9 382 2018
JRNL REFN ESSN 2041-1723
JRNL PMID 29374183
JRNL DOI 10.1038/S41467-018-02881-1
REMARK 2
REMARK 2 RESOLUTION. 1.36 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.36
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.30
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 58473
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) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3116
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) : 1.36
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.40
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4047
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.61
REMARK 3 BIN R VALUE (WORKING SET) : 0.2740
REMARK 3 BIN FREE R VALUE SET COUNT : 236
REMARK 3 BIN FREE R VALUE : 0.2940
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1933
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 294
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.34
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.86000
REMARK 3 B22 (A**2) : -0.45000
REMARK 3 B33 (A**2) : -0.41000
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): 0.048
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.052
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.034
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.858
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.971
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.960
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2009 ; 0.025 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1825 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2740 ; 2.249 ; 1.932
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4198 ; 1.037 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 269 ; 6.529 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 80 ;33.275 ;23.750
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 296 ;10.323 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;17.565 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 300 ; 0.151 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2379 ; 0.013 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 476 ; 0.001 ; 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 : NULL
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 5YNS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-NOV-17.
REMARK 100 THE DEPOSITION ID IS D_1300005603.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-OCT-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 7A (6B, 6C1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62494
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.360
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 (%) : 98.7
REMARK 200 DATA REDUNDANCY : 9.300
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 40.7900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.37400
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: NULL
REMARK 200 STARTING MODEL: 5XJH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: BIS-TRIS, AMMONIUM ACETATE, PEG 10000,
REMARK 280 PH 5.5, VAPOR DIFFUSION, HANGING DROP, 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 21.80350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 64.79050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.29300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 64.79050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.80350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 25.29300
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 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 73 47.00 -141.23
REMARK 500 THR A 88 -9.70 73.79
REMARK 500 SER A 160 -118.93 63.11
REMARK 500 SER A 214 -83.18 -127.58
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 5YNS A 34 290 UNP PETH_IDESA
DBREF2 5YNS A A0A0K8P6T7 34 290
SEQADV 5YNS GLY A 30 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 5YNS SER A 31 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 5YNS HIS A 32 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 5YNS MET A 33 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 5YNS ALA A 280 UNP A0A0K8P6T ARG 280 ENGINEERED MUTATION
SEQADV 5YNS LEU A 291 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 5YNS GLU A 292 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 5YNS ASP A 293 UNP A0A0K8P6T EXPRESSION TAG
SEQRES 1 A 264 GLY SER HIS MET ARG GLY PRO ASN PRO THR ALA ALA SER
SEQRES 2 A 264 LEU GLU ALA SER ALA GLY PRO PHE THR VAL ARG SER PHE
SEQRES 3 A 264 THR VAL SER ARG PRO SER GLY TYR GLY ALA GLY THR VAL
SEQRES 4 A 264 TYR TYR PRO THR ASN ALA GLY GLY THR VAL GLY ALA ILE
SEQRES 5 A 264 ALA ILE VAL PRO GLY TYR THR ALA ARG GLN SER SER ILE
SEQRES 6 A 264 LYS TRP TRP GLY PRO ARG LEU ALA SER HIS GLY PHE VAL
SEQRES 7 A 264 VAL ILE THR ILE ASP THR ASN SER THR LEU ASP GLN PRO
SEQRES 8 A 264 SER SER ARG SER SER GLN GLN MET ALA ALA LEU ARG GLN
SEQRES 9 A 264 VAL ALA SER LEU ASN GLY THR SER SER SER PRO ILE TYR
SEQRES 10 A 264 GLY LYS VAL ASP THR ALA ARG MET GLY VAL MET GLY TRP
SEQRES 11 A 264 SER MET GLY GLY GLY GLY SER LEU ILE SER ALA ALA ASN
SEQRES 12 A 264 ASN PRO SER LEU LYS ALA ALA ALA PRO GLN ALA PRO TRP
SEQRES 13 A 264 ASP SER SER THR ASN PHE SER SER VAL THR VAL PRO THR
SEQRES 14 A 264 LEU ILE PHE ALA CYS GLU ASN ASP SER ILE ALA PRO VAL
SEQRES 15 A 264 ASN SER SER ALA LEU PRO ILE TYR ASP SER MET SER ARG
SEQRES 16 A 264 ASN ALA LYS GLN PHE LEU GLU ILE ASN GLY GLY SER HIS
SEQRES 17 A 264 SER CYS ALA ASN SER GLY ASN SER ASN GLN ALA LEU ILE
SEQRES 18 A 264 GLY LYS LYS GLY VAL ALA TRP MET LYS ARG PHE MET ASP
SEQRES 19 A 264 ASN ASP THR ARG TYR SER THR PHE ALA CYS GLU ASN PRO
SEQRES 20 A 264 ASN SER THR ALA VAL SER ASP PHE ARG THR ALA ASN CYS
SEQRES 21 A 264 SER LEU GLU ASP
FORMUL 2 HOH *294(H2 O)
HELIX 1 AA1 THR A 39 ALA A 45 1 7
HELIX 2 AA2 ARG A 90 LYS A 95 5 6
HELIX 3 AA3 TRP A 96 SER A 103 1 8
HELIX 4 AA4 GLN A 119 GLY A 139 1 21
HELIX 5 AA5 SER A 160 ASN A 173 1 14
HELIX 6 AA6 SER A 214 MET A 222 1 9
HELIX 7 AA7 ASN A 246 ASP A 263 1 18
HELIX 8 AA8 ASP A 265 ARG A 267 5 3
HELIX 9 AA9 TYR A 268 GLU A 274 1 7
SHEET 1 AA1 6 VAL A 52 THR A 56 0
SHEET 2 AA1 6 ALA A 65 PRO A 71 -1 O VAL A 68 N PHE A 55
SHEET 3 AA1 6 VAL A 107 ASP A 112 -1 O VAL A 108 N TYR A 69
SHEET 4 AA1 6 VAL A 78 VAL A 84 1 N ILE A 81 O ILE A 109
SHEET 5 AA1 6 VAL A 149 GLY A 158 1 O GLY A 155 N ALA A 80
SHEET 6 AA1 6 ALA A 178 ALA A 179 1 O ALA A 178 N VAL A 156
SHEET 1 AA2 3 THR A 198 CYS A 203 0
SHEET 2 AA2 3 LYS A 227 ILE A 232 1 O GLN A 228 N ILE A 200
SHEET 3 AA2 3 VAL A 281 ALA A 287 -1 O ARG A 285 N PHE A 229
SSBOND 1 CYS A 203 CYS A 239 1555 1555 2.11
SSBOND 2 CYS A 273 CYS A 289 1555 1555 2.01
CRYST1 43.607 50.586 129.581 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 0.022932 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019768 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007717 0.00000
TER 1961 ASP A 293
MASTER 259 0 0 9 9 0 0 6 2227 1 4 21
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