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HEADER HYDROLASE 13-OCT-22 8H5K
TITLE CRYSTAL STRUCTURE OF PETASE
TITLE 2 N37D/S121E/R132E/A171C/A180V/P181V/D186H/S193C/R224E/N233C/S242T/N246
TITLE 3 D/S282C MUTANT FROM IDEONELLA SAKAIENSIS
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
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: IDEONELLA SAKAIENSIS;
SOURCE 3 ORGANISM_TAXID: 1547922;
SOURCE 4 GENE: ISF6_4831;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PET HYDROLASE ; IDEONELLA SAKAIENSIS; MUTANT, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.H.LEE,H.SEO,K.-J.KIM
REVDAT 1 25-OCT-23 8H5K 0
JRNL AUTH S.H.LEE,H.SEO,K.J.KIM
JRNL TITL A CASE OF BALANCE ENGINEERING EXHIBITS KINETIC RELATIONSHIP
JRNL TITL 2 BETWEEN MESOPHILIC AND THERMOPHILIC POLY(ETHYLENE
JRNL TITL 3 TEREPHTHALATE) DEPOLYMERASES.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0350
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) : 1.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.05
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 59685
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) : 0.160
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.187
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.23
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4191
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.01
REMARK 3 BIN R VALUE (WORKING SET) : 0.3030
REMARK 3 BIN FREE R VALUE SET COUNT : 207
REMARK 3 BIN FREE R VALUE : 0.3110
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1913
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 329
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.98
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.48000
REMARK 3 B22 (A**2) : -0.85000
REMARK 3 B33 (A**2) : 2.34000
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): 0.042
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.045
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.045
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.120
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.981
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): 2062 ; 0.010 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): 1766 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2826 ; 1.641 ; 1.632
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4150 ; 0.587 ; 1.546
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 284 ; 6.831 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 11 ;10.914 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 310 ;14.296 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 310 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2463 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 413 ; 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 8H5K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-OCT-22.
REMARK 100 THE DEPOSITION ID IS D_1300031251.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-FEB-22
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 : 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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63001
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.200
REMARK 200 RESOLUTION RANGE LOW (A) : 25.050
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 37.5530
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.22
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: REFMAC
REMARK 200 STARTING MODEL: 5XJH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 32.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15 % PEG3350, 0.1 M SODIUM HEPES
REMARK 280 PH7.0, 0.01 M MAGNESIUM CHLORIDE HEXAHYDRATE, AND 0.005 M NICKEL
REMARK 280 (II) CHLORIDE HEXAHYDRATE, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 295K
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 25.50950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 32.78400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.86200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 32.78400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.50950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.86200
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 NH1 ARG A 90 O HOH A 301 1.54
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O GLY A 48 NH1 ARG A 59 3545 1.99
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 36.86 -143.41
REMARK 500 THR A 88 -3.41 73.59
REMARK 500 SER A 160 -133.82 66.95
REMARK 500 SER A 160 -127.76 59.19
REMARK 500 SER A 214 -78.59 -127.35
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 123 0.12 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 8H5K A 34 290 UNP PETH_IDESA
DBREF2 8H5K A A0A0K8P6T7 34 290
SEQADV 8H5K SER A 31 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5K HIS A 32 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5K MET A 33 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H5K ASP A 37 UNP A0A0K8P6T ASN 37 ENGINEERED MUTATION
SEQADV 8H5K GLU A 121 UNP A0A0K8P6T SER 121 ENGINEERED MUTATION
SEQADV 8H5K GLU A 132 UNP A0A0K8P6T ARG 132 ENGINEERED MUTATION
SEQADV 8H5K CYS A 171 UNP A0A0K8P6T ALA 171 ENGINEERED MUTATION
SEQADV 8H5K VAL A 180 UNP A0A0K8P6T ALA 180 ENGINEERED MUTATION
SEQADV 8H5K VAL A 181 UNP A0A0K8P6T PRO 181 ENGINEERED MUTATION
SEQADV 8H5K HIS A 186 UNP A0A0K8P6T ASP 186 ENGINEERED MUTATION
SEQADV 8H5K CYS A 193 UNP A0A0K8P6T SER 193 ENGINEERED MUTATION
SEQADV 8H5K GLU A 224 UNP A0A0K8P6T ARG 224 ENGINEERED MUTATION
SEQADV 8H5K CYS A 233 UNP A0A0K8P6T ASN 233 ENGINEERED MUTATION
SEQADV 8H5K THR A 242 UNP A0A0K8P6T SER 242 ENGINEERED MUTATION
SEQADV 8H5K ASP A 246 UNP A0A0K8P6T ASN 246 ENGINEERED MUTATION
SEQADV 8H5K CYS A 282 UNP A0A0K8P6T SER 282 ENGINEERED MUTATION
SEQRES 1 A 260 SER HIS MET ARG GLY PRO ASP PRO THR ALA ALA SER LEU
SEQRES 2 A 260 GLU ALA SER ALA GLY PRO PHE THR VAL ARG SER PHE THR
SEQRES 3 A 260 VAL SER ARG PRO SER GLY TYR GLY ALA GLY THR VAL TYR
SEQRES 4 A 260 TYR PRO THR ASN ALA GLY GLY THR VAL GLY ALA ILE ALA
SEQRES 5 A 260 ILE VAL PRO GLY TYR THR ALA ARG GLN SER SER ILE LYS
SEQRES 6 A 260 TRP TRP GLY PRO ARG LEU ALA SER HIS GLY PHE VAL VAL
SEQRES 7 A 260 ILE THR ILE ASP THR ASN SER THR LEU ASP GLN PRO GLU
SEQRES 8 A 260 SER ARG SER SER GLN GLN MET ALA ALA LEU GLU GLN VAL
SEQRES 9 A 260 ALA SER LEU ASN GLY THR SER SER SER PRO ILE TYR GLY
SEQRES 10 A 260 LYS VAL ASP THR ALA ARG MET GLY VAL MET GLY TRP SER
SEQRES 11 A 260 MET GLY GLY GLY GLY SER LEU ILE SER ALA CYS ASN ASN
SEQRES 12 A 260 PRO SER LEU LYS ALA ALA VAL VAL GLN ALA PRO TRP HIS
SEQRES 13 A 260 SER SER THR ASN PHE SER CYS VAL THR VAL PRO THR LEU
SEQRES 14 A 260 ILE PHE ALA CYS GLU ASN ASP SER ILE ALA PRO VAL ASN
SEQRES 15 A 260 SER SER ALA LEU PRO ILE TYR ASP SER MET SER GLU ASN
SEQRES 16 A 260 ALA LYS GLN PHE LEU GLU ILE CYS GLY GLY SER HIS SER
SEQRES 17 A 260 CYS ALA ASN THR GLY ASN SER ASP GLN ALA LEU ILE GLY
SEQRES 18 A 260 LYS LYS GLY VAL ALA TRP MET LYS ARG PHE MET ASP ASN
SEQRES 19 A 260 ASP THR ARG TYR SER THR PHE ALA CYS GLU ASN PRO ASN
SEQRES 20 A 260 SER THR ARG VAL CYS ASP PHE ARG THR ALA ASN CYS SER
FORMUL 2 HOH *329(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 ASP 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 9 VAL A 52 THR A 56 0
SHEET 2 AA1 9 ALA A 65 PRO A 71 -1 O VAL A 68 N PHE A 55
SHEET 3 AA1 9 VAL A 107 ASP A 112 -1 O VAL A 108 N TYR A 69
SHEET 4 AA1 9 VAL A 78 VAL A 84 1 N ILE A 83 O ILE A 109
SHEET 5 AA1 9 VAL A 149 TRP A 159 1 O ASP A 150 N VAL A 78
SHEET 6 AA1 9 ALA A 178 GLN A 182 1 O GLN A 182 N GLY A 158
SHEET 7 AA1 9 THR A 198 CYS A 203 1 O PHE A 201 N VAL A 181
SHEET 8 AA1 9 LYS A 227 ILE A 232 1 O ILE A 232 N ALA A 202
SHEET 9 AA1 9 VAL A 281 ALA A 287 -1 O CYS A 282 N GLU A 231
SSBOND 1 CYS A 171 CYS A 193 1555 1555 2.01
SSBOND 2 CYS A 203 CYS A 239 1555 1555 2.06
SSBOND 3 CYS A 233 CYS A 282 1555 1555 1.99
SSBOND 4 CYS A 273 CYS A 289 1555 1555 2.09
CRYST1 51.019 59.724 65.568 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 0.019601 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016744 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015251 0.00000
TER 2011 SER A 290
MASTER 303 0 0 9 9 0 0 6 2242 1 8 20
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