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HEADER HYDROLASE 26-JAN-21 7DZU
TITLE CYRSTAL STRUCTURE OF PETASE K169A MUTANT FROM RHIZOBACTER GUMMIPHILUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DLH DOMAIN-CONTAINING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHIZOBACTER GUMMIPHILUS;
SOURCE 3 ORGANISM_COMMON: METHYLIBIUM SP. NS21;
SOURCE 4 ORGANISM_TAXID: 946333;
SOURCE 5 STRAIN: NS21;
SOURCE 6 GENE: A4W93_05950;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: ROSETTA GAMI-B
KEYWDS PET HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.-Y.SAGONG,K.-J.KIM
REVDAT 1 07-JUL-21 7DZU 0
JRNL AUTH H.-Y.SAGONG,H.F.SON,H.SEO,H.HONG,D.LEE,K.-J.KIM
JRNL TITL IMPLICATIONS FOR THE PET DECOMPOSITION MECHANISM THROUGH
JRNL TITL 2 SIMILARITY AND DISSIMILARITY BETWEEN PETASES FROM
JRNL TITL 3 RHIZOBACTER GUMMIPHILUS AND IDEONELLA SAKAIENSIS.
JRNL REF J HAZARD MATER 2021
JRNL REFN ISSN 1873-3336
JRNL DOI 10.1016/J.JHAZMAT.2021.126075
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0258
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.07
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 11585
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) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 634
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 785
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.53
REMARK 3 BIN R VALUE (WORKING SET) : 0.2560
REMARK 3 BIN FREE R VALUE SET COUNT : 47
REMARK 3 BIN FREE R VALUE : 0.4320
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2000
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 104
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.98
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.24000
REMARK 3 B22 (A**2) : 5.25000
REMARK 3 B33 (A**2) : -2.01000
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): 0.367
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.265
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.194
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.033
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.906
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2051 ; 0.008 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 1803 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2793 ; 1.620 ; 1.642
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4198 ; 1.339 ; 1.568
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 267 ; 7.309 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 97 ;33.046 ;21.753
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 305 ;15.815 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;12.652 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 270 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2354 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 437 ; 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 : 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 7DZU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-JAN-21.
REMARK 100 THE DEPOSITION ID IS D_1300020511.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-DEC-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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 : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12259
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
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 (%) : 98.1
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.11300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.41400
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: MOLREP
REMARK 200 STARTING MODEL: 7DZT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NACL, HEPES, PH 7.5, EVAPORATION,
REMARK 280 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 25.56950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.06800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.05300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.06800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.56950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 27.05300
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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HIS A 102 NZ LYS A 256 2.14
REMARK 500
REMARK 500 REMARK: NULL
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 71 50.80 -146.84
REMARK 500 THR A 86 -6.64 75.69
REMARK 500 SER A 158 -110.90 62.54
REMARK 500 HIS A 211 -88.49 -121.57
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 7DZU A 27 292 UNP A0A1W6L588_9BURK
DBREF2 7DZU A A0A1W6L588 27 292
SEQADV 7DZU ALA A 169 UNP A0A1W6L58 LYS 169 ENGINEERED MUTATION
SEQADV 7DZU LEU A 293 UNP A0A1W6L58 EXPRESSION TAG
SEQADV 7DZU GLU A 294 UNP A0A1W6L58 EXPRESSION TAG
SEQRES 1 A 268 THR ASN PRO TYR GLN ARG GLY PRO ASP PRO THR VAL SER
SEQRES 2 A 268 SER LEU GLU ALA THR ARG GLY PRO PHE SER THR SER SER
SEQRES 3 A 268 PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA GLY THR
SEQRES 4 A 268 VAL TYR TYR PRO THR ASN ALA GLY GLY LYS VAL GLY ALA
SEQRES 5 A 268 ILE ALA VAL VAL PRO GLY TYR THR ALA ARG GLN SER SER
SEQRES 6 A 268 ILE ASN TRP TRP GLY PRO ARG LEU ALA SER HIS GLY PHE
SEQRES 7 A 268 VAL VAL ILE THR ILE ASP THR ASN SER THR LEU ASP GLN
SEQRES 8 A 268 PRO SER SER ARG SER SER GLN GLN MET ALA ALA LEU ARG
SEQRES 9 A 268 GLN VAL VAL SER LEU ALA GLY THR SER SER SER PRO ILE
SEQRES 10 A 268 TYR ASN LYS VAL ASP THR ALA ARG LEU GLY VAL MET GLY
SEQRES 11 A 268 TRP SER MET GLY GLY GLY GLY SER LEU ILE SER ALA ALA
SEQRES 12 A 268 ASN ASN PRO SER LEU ARG ALA ALA ALA PRO GLN ALA PRO
SEQRES 13 A 268 TRP ALA GLN GLU SER PHE SER SER VAL THR VAL PRO THR
SEQRES 14 A 268 LEU ILE VAL SER CYS GLU ASN ASP SER ILE ALA PRO ASN
SEQRES 15 A 268 SER SER HIS SER PHE PRO PHE TYR ASN GLN MET THR ARG
SEQRES 16 A 268 ASN LYS LYS ALA ASN LEU VAL ILE ASN GLY GLY SER HIS
SEQRES 17 A 268 SER CYS ALA ASN SER GLY ASN SER ASP ALA GLY LEU ILE
SEQRES 18 A 268 GLY LYS TYR GLY VAL ALA TRP MET LYS ARG PHE MET ASP
SEQRES 19 A 268 ASP ASP THR ARG TYR SER LYS PHE LEU CYS GLY ALA GLU
SEQRES 20 A 268 HIS GLN ALA ASP LEU SER LYS ARG ALA VAL GLU ALA TYR
SEQRES 21 A 268 LYS GLU ASN CYS PRO TYR LEU GLU
FORMUL 2 HOH *104(H2 O)
HELIX 1 AA1 THR A 37 ALA A 43 1 7
HELIX 2 AA2 ARG A 88 ASN A 93 5 6
HELIX 3 AA3 TRP A 94 SER A 101 1 8
HELIX 4 AA4 GLN A 117 ALA A 136 1 20
HELIX 5 AA5 SER A 158 ASN A 171 1 14
HELIX 6 AA6 HIS A 211 MET A 219 1 9
HELIX 7 AA7 ASP A 243 ASP A 260 1 18
HELIX 8 AA8 ASP A 262 ARG A 264 5 3
HELIX 9 AA9 TYR A 265 GLY A 271 1 7
HELIX 10 AB1 GLY A 271 LEU A 278 1 8
SHEET 1 AA1 6 THR A 50 THR A 54 0
SHEET 2 AA1 6 ALA A 63 PRO A 69 -1 O VAL A 66 N PHE A 53
SHEET 3 AA1 6 VAL A 105 ASP A 110 -1 O VAL A 106 N TYR A 67
SHEET 4 AA1 6 VAL A 76 VAL A 82 1 N ILE A 79 O ILE A 107
SHEET 5 AA1 6 VAL A 147 TRP A 157 1 O TRP A 157 N VAL A 82
SHEET 6 AA1 6 ALA A 176 GLN A 180 1 O GLN A 180 N GLY A 156
SHEET 1 AA2 3 THR A 195 CYS A 200 0
SHEET 2 AA2 3 LYS A 224 ILE A 229 1 O ALA A 225 N ILE A 197
SHEET 3 AA2 3 VAL A 283 GLU A 288 -1 O ALA A 285 N VAL A 228
SSBOND 1 CYS A 200 CYS A 236 1555 1555 2.08
SSBOND 2 CYS A 270 CYS A 290 1555 1555 2.08
CISPEP 1 CYS A 290 PRO A 291 0 1.93
CRYST1 51.139 54.106 110.136 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 0.019555 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018482 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009080 0.00000
TER 2001 GLU A 294
MASTER 265 0 0 10 9 0 0 6 2104 1 4 21
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