| content |
HEADER HYDROLASE 19-DEC-23 8VEL
TITLE ISPETASE - ACCCC MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(ETHYLENE TEREPHTHALATE) HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PET HYDROLASE,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: PISCINIBACTER SAKAIENSIS;
SOURCE 3 ORGANISM_TAXID: 1547922;
SOURCE 4 GENE: ISF6_4831;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS PETASE, PROTEIN ENGINEERING, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.JOHO,S.ROYAN,S.NEWTON,A.T.CAPUTO,A.ARDEVOL GRAU,C.JACKSON
REVDAT 1 19-JUN-24 8VEL 0
JRNL AUTH Y.JOHO,S.ROYAN,A.T.CAPUTO,S.NEWTON,T.S.PEAT,J.NEWMAN,
JRNL AUTH 2 C.JACKSON,A.ARDEVOL
JRNL TITL ENHANCING PET DEGRADING ENZYMES: A COMBINATORY APPROACH.
JRNL REF CHEMBIOCHEM V. 25 00084 2024
JRNL REFN ESSN 1439-7633
JRNL PMID 38584134
JRNL DOI 10.1002/CBIC.202400084
REMARK 2
REMARK 2 RESOLUTION. 1.62 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.3
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.62
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.74
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 82.7
REMARK 3 NUMBER OF REFLECTIONS : 29388
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) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1413
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.62
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.69
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 14.12
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : NULL
REMARK 3 BIN R VALUE (WORKING + TEST SET) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2335
REMARK 3 BIN FREE R VALUE : 0.2879
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 24
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1919
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 287
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.42690
REMARK 3 B22 (A**2) : 0.49920
REMARK 3 B33 (A**2) : -0.07230
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.210
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.115
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.102
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.133
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.096
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4083 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 7375 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1255 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : 694 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2093 ; 10.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 291 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 3711 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 0.99
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 4.52
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 14.03
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -7.5457 18.3454 -14.0631
REMARK 3 T TENSOR
REMARK 3 T11: -0.0431 T22: -0.0385
REMARK 3 T33: -0.0357 T12: -0.0076
REMARK 3 T13: 0.0001 T23: 0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 1.1845 L22: 0.6111
REMARK 3 L33: 0.7053 L12: 0.0594
REMARK 3 L13: -0.143 L23: 0.0477
REMARK 3 S TENSOR
REMARK 3 S11: -0.0235 S12: -0.0442 S13: 0.0033
REMARK 3 S21: -0.0442 S22: 0.063 S23: -0.0372
REMARK 3 S31: 0.0033 S32: -0.0372 S33: -0.0395
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 8VEL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-DEC-23.
REMARK 100 THE DEPOSITION ID IS D_1000280041.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-NOV-20
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 : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95372
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29388
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.624
REMARK 200 RESOLUTION RANGE LOW (A) : 51.738
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 200 DATA REDUNDANCY : 13.30
REMARK 200 R MERGE (I) : 0.15500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.62
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 63.9
REMARK 200 DATA REDUNDANCY IN SHELL : 10.40
REMARK 200 R MERGE FOR SHELL (I) : 1.69800
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.138 M AMMONIUM SULFATE; 30 W/V
REMARK 280 POLYETHYLENE GLYCOL 8000, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 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 25.41850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.56100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.19250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.56100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.41850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.19250
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 27
REMARK 465 GLY A 28
REMARK 465 ALA A 291
REMARK 465 SER A 292
REMARK 465 HIS A 293
REMARK 465 HIS A 294
REMARK 465 HIS A 295
REMARK 465 HIS A 296
REMARK 465 HIS A 297
REMARK 465 HIS A 298
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 OG SER A 160 O1 SO4 A 302 2.19
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 73 44.05 -141.11
REMARK 500 THR A 88 -10.06 74.91
REMARK 500 SER A 160 -119.61 62.55
REMARK 500 SER A 214 -78.97 -129.74
REMARK 500 SER A 214 -79.52 -129.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 8VE9 RELATED DB: PDB
REMARK 900 DIFFERENT POINT MUTANTS OF SAME ENZYME
REMARK 900 RELATED ID: 8VEK RELATED DB: PDB
REMARK 900 DIFFERENT POINT MUTANTS OF SAME ENZYME
DBREF1 8VEL A 30 290 UNP PETH_IDESA
DBREF2 8VEL A A0A0K8P6T7 30 290
SEQADV 8VEL MET A 27 UNP A0A0K8P6T INITIATING METHIONINE
SEQADV 8VEL GLY A 28 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8VEL SER A 29 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8VEL CYS A 179 UNP A0A0K8P6T ALA 179 ENGINEERED MUTATION
SEQADV 8VEL ALA A 186 UNP A0A0K8P6T ASP 186 ENGINEERED MUTATION
SEQADV 8VEL CYS A 198 UNP A0A0K8P6T THR 198 ENGINEERED MUTATION
SEQADV 8VEL CYS A 233 UNP A0A0K8P6T ASN 233 ENGINEERED MUTATION
SEQADV 8VEL CYS A 282 UNP A0A0K8P6T SER 282 ENGINEERED MUTATION
SEQADV 8VEL ALA A 291 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8VEL SER A 292 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8VEL HIS A 293 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8VEL HIS A 294 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8VEL HIS A 295 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8VEL HIS A 296 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8VEL HIS A 297 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8VEL HIS A 298 UNP A0A0K8P6T EXPRESSION TAG
SEQRES 1 A 272 MET GLY SER ASN PRO TYR ALA ARG GLY PRO ASN PRO THR
SEQRES 2 A 272 ALA ALA SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL
SEQRES 3 A 272 ARG SER PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA
SEQRES 4 A 272 GLY THR VAL TYR TYR PRO THR ASN ALA GLY GLY THR VAL
SEQRES 5 A 272 GLY ALA ILE ALA ILE VAL PRO GLY TYR THR ALA ARG GLN
SEQRES 6 A 272 SER SER ILE LYS TRP TRP GLY PRO ARG LEU ALA SER HIS
SEQRES 7 A 272 GLY PHE VAL VAL ILE THR ILE ASP THR ASN SER THR LEU
SEQRES 8 A 272 ASP GLN PRO SER SER ARG SER SER GLN GLN MET ALA ALA
SEQRES 9 A 272 LEU ARG GLN VAL ALA SER LEU ASN GLY THR SER SER SER
SEQRES 10 A 272 PRO ILE TYR GLY LYS VAL ASP THR ALA ARG MET GLY VAL
SEQRES 11 A 272 MET GLY TRP SER MET GLY GLY GLY GLY SER LEU ILE SER
SEQRES 12 A 272 ALA ALA ASN ASN PRO SER LEU LYS ALA CYS ALA PRO GLN
SEQRES 13 A 272 ALA PRO TRP ALA SER SER THR ASN PHE SER SER VAL THR
SEQRES 14 A 272 VAL PRO CYS LEU ILE PHE ALA CYS GLU ASN ASP SER ILE
SEQRES 15 A 272 ALA PRO VAL ASN SER SER ALA LEU PRO ILE TYR ASP SER
SEQRES 16 A 272 MET SER ARG ASN ALA LYS GLN PHE LEU GLU ILE CYS GLY
SEQRES 17 A 272 GLY SER HIS SER CYS ALA ASN SER GLY ASN SER ASN GLN
SEQRES 18 A 272 ALA LEU ILE GLY LYS LYS GLY VAL ALA TRP MET LYS ARG
SEQRES 19 A 272 PHE MET ASP ASN ASP THR ARG TYR SER THR PHE ALA CYS
SEQRES 20 A 272 GLU ASN PRO ASN SER THR ARG VAL CYS ASP PHE ARG THR
SEQRES 21 A 272 ALA ASN CYS SER ALA SER HIS HIS HIS HIS HIS HIS
HET SO4 A 301 5
HET SO4 A 302 5
HETNAM SO4 SULFATE ION
FORMUL 2 SO4 2(O4 S 2-)
FORMUL 4 HOH *287(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 PHE A 106 1 11
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 83 O ILE A 109
SHEET 5 AA1 6 VAL A 149 TRP A 159 1 O ASP A 150 N VAL A 78
SHEET 6 AA1 6 ALA A 178 GLN A 182 1 O GLN A 182 N GLY A 158
SHEET 1 AA2 3 CYS 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 2.04
SSBOND 2 CYS A 233 CYS A 282 1555 1555 2.04
SSBOND 3 CYS A 273 CYS A 289 1555 1555 2.04
CRYST1 50.837 68.385 79.122 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 0.019671 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014623 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012639 0.00000
TER 4008 SER A 290
MASTER 283 0 2 9 9 0 0 6 2216 1 16 21
END |