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HEADER HYDROLASE 23-APR-23 8J5N
TITLE CRYSTAL STRUCTURE OF A PETASE VARIANT V20 FROM IDEONELLA SAKAIENSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(ETHYLENE TEREPHTHALATE) HYDROLASE;
COMPND 3 CHAIN: A, D;
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: IDEONELLA SAKAIENSIS;
SOURCE 3 ORGANISM_TAXID: 1547922;
SOURCE 4 GENE: ISF6_4831;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 866768
KEYWDS PLASTIC DEGRADATION, PET, MUTANT, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.L.WEI,S.F.GAO,Q.LI,W.D.LIU,L.L.ZHU
REVDAT 1 24-APR-24 8J5N 0
JRNL AUTH H.L.WEI,S.F.GAO,Q.LI,W.D.LIU,L.L.ZHU
JRNL TITL CRYSTAL STRUCTURE OF A PETASE VARIANT V20 FROM IDEONELLA
JRNL TITL 2 SAKAIENSIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0267
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.81
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 31578
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) : 0.228
REMARK 3 R VALUE (WORKING SET) : 0.226
REMARK 3 FREE R VALUE : 0.278
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1585
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2173
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.40
REMARK 3 BIN R VALUE (WORKING SET) : 0.3050
REMARK 3 BIN FREE R VALUE SET COUNT : 114
REMARK 3 BIN FREE R VALUE : 0.3450
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3834
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 209
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.04000
REMARK 3 B33 (A**2) : -0.04000
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): 0.237
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.204
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.158
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.755
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.892
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3928 ; 0.008 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 3572 ; 0.001 ; 0.018
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5354 ; 1.552 ; 1.643
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8230 ; 1.337 ; 1.571
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 520 ; 7.552 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 174 ;35.131 ;21.724
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 578 ;15.680 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;15.864 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 538 ; 0.071 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4592 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 928 ; 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): 2086 ; 1.443 ; 1.996
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2085 ; 1.438 ; 1.995
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2604 ; 2.216 ; 2.984
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2605 ; 2.217 ; 2.985
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1842 ; 1.783 ; 2.191
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1842 ; 1.781 ; 2.191
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2751 ; 2.806 ; 3.220
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4438 ; 4.581 ;24.471
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4438 ; 4.582 ;24.467
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
REMARK 4
REMARK 4 8J5N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-APR-23.
REMARK 100 THE DEPOSITION ID IS D_1300037234.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-APR-23
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL18U1
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32014
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 48.810
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 10.00
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1
REMARK 200 DATA REDUNDANCY IN SHELL : 8.10
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: PHASER
REMARK 200 STARTING MODEL: 5XH3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% TACSIMATE PH 5.0, 20% POLYETHYLENE
REMARK 280 GLYCOL 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 297K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 X,-Y,-Z
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 -X,-Y+1/2,Z+1/2
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.96250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 62.52000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.96250
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 62.52000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH D 365 LIES ON A SPECIAL POSITION.
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 1
REMARK 465 ASN A 2
REMARK 465 PHE A 3
REMARK 465 PRO A 4
REMARK 465 ARG A 5
REMARK 465 ALA A 6
REMARK 465 SER A 7
REMARK 465 ARG A 8
REMARK 465 LEU A 9
REMARK 465 MET A 10
REMARK 465 GLN A 11
REMARK 465 ALA A 12
REMARK 465 ALA A 13
REMARK 465 GLU A 14
REMARK 465 LEU A 15
REMARK 465 GLY A 16
REMARK 465 GLY A 17
REMARK 465 PRO A 18
REMARK 465 MET A 19
REMARK 465 ALA A 20
REMARK 465 VAL A 21
REMARK 465 SER A 22
REMARK 465 ALA A 23
REMARK 465 ALA A 24
REMARK 465 ALA A 25
REMARK 465 THR A 26
REMARK 465 ALA A 27
REMARK 465 GLN A 28
REMARK 465 SER A 290
REMARK 465 LEU A 291
REMARK 465 GLU 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 465 MET D 1
REMARK 465 ASN D 2
REMARK 465 PHE D 3
REMARK 465 PRO D 4
REMARK 465 ARG D 5
REMARK 465 ALA D 6
REMARK 465 SER D 7
REMARK 465 ARG D 8
REMARK 465 LEU D 9
REMARK 465 MET D 10
REMARK 465 GLN D 11
REMARK 465 ALA D 12
REMARK 465 ALA D 13
REMARK 465 GLU D 14
REMARK 465 LEU D 15
REMARK 465 GLY D 16
REMARK 465 GLY D 17
REMARK 465 PRO D 18
REMARK 465 MET D 19
REMARK 465 ALA D 20
REMARK 465 VAL D 21
REMARK 465 SER D 22
REMARK 465 ALA D 23
REMARK 465 ALA D 24
REMARK 465 ALA D 25
REMARK 465 THR D 26
REMARK 465 ALA D 27
REMARK 465 GLN D 28
REMARK 465 SER D 290
REMARK 465 LEU D 291
REMARK 465 GLU D 292
REMARK 465 HIS D 293
REMARK 465 HIS D 294
REMARK 465 HIS D 295
REMARK 465 HIS D 296
REMARK 465 HIS D 297
REMARK 465 HIS D 298
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ILE A 208 CG1 CG2 CD1
REMARK 470 ILE D 208 CG1 CG2 CD1
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 46.01 -143.06
REMARK 500 THR A 88 -17.06 79.68
REMARK 500 SER A 160 -116.38 67.14
REMARK 500 SER A 214 -84.46 -123.03
REMARK 500 THR D 88 -5.96 75.00
REMARK 500 SER D 160 -118.16 72.98
REMARK 500 ALA D 178 149.79 -170.10
REMARK 500 ALA D 183 55.48 36.69
REMARK 500 SER D 214 -84.64 -129.42
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 8J5N A 1 290 UNP PETH_IDESA
DBREF2 8J5N A A0A0K8P6T7 1 290
DBREF1 8J5N D 1 290 UNP PETH_IDESA
DBREF2 8J5N D A0A0K8P6T7 1 290
SEQADV 8J5N GLU A 14 UNP A0A0K8P6T VAL 14 ENGINEERED MUTATION
SEQADV 8J5N PRO A 18 UNP A0A0K8P6T LEU 18 ENGINEERED MUTATION
SEQADV 8J5N GLN A 53 UNP A0A0K8P6T ARG 53 ENGINEERED MUTATION
SEQADV 8J5N LEU A 84 UNP A0A0K8P6T VAL 84 ENGINEERED MUTATION
SEQADV 8J5N HIS A 186 UNP A0A0K8P6T ASP 186 ENGINEERED MUTATION
SEQADV 8J5N ILE A 201 UNP A0A0K8P6T PHE 201 ENGINEERED MUTATION
SEQADV 8J5N TYR A 229 UNP A0A0K8P6T PHE 229 ENGINEERED MUTATION
SEQADV 8J5N LYS A 233 UNP A0A0K8P6T ASN 233 ENGINEERED MUTATION
SEQADV 8J5N GLU A 280 UNP A0A0K8P6T ARG 280 ENGINEERED MUTATION
SEQADV 8J5N ARG A 283 UNP A0A0K8P6T ASP 283 ENGINEERED MUTATION
SEQADV 8J5N LEU A 291 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J5N GLU A 292 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J5N HIS A 293 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J5N HIS A 294 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J5N HIS A 295 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J5N HIS A 296 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J5N HIS A 297 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J5N HIS A 298 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J5N GLU D 14 UNP A0A0K8P6T VAL 14 ENGINEERED MUTATION
SEQADV 8J5N PRO D 18 UNP A0A0K8P6T LEU 18 ENGINEERED MUTATION
SEQADV 8J5N GLN D 53 UNP A0A0K8P6T ARG 53 ENGINEERED MUTATION
SEQADV 8J5N LEU D 84 UNP A0A0K8P6T VAL 84 ENGINEERED MUTATION
SEQADV 8J5N HIS D 186 UNP A0A0K8P6T ASP 186 ENGINEERED MUTATION
SEQADV 8J5N ILE D 201 UNP A0A0K8P6T PHE 201 ENGINEERED MUTATION
SEQADV 8J5N TYR D 229 UNP A0A0K8P6T PHE 229 ENGINEERED MUTATION
SEQADV 8J5N LYS D 233 UNP A0A0K8P6T ASN 233 ENGINEERED MUTATION
SEQADV 8J5N GLU D 280 UNP A0A0K8P6T ARG 280 ENGINEERED MUTATION
SEQADV 8J5N ARG D 283 UNP A0A0K8P6T ASP 283 ENGINEERED MUTATION
SEQADV 8J5N LEU D 291 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J5N GLU D 292 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J5N HIS D 293 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J5N HIS D 294 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J5N HIS D 295 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J5N HIS D 296 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J5N HIS D 297 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8J5N HIS D 298 UNP A0A0K8P6T EXPRESSION TAG
SEQRES 1 A 298 MET ASN PHE PRO ARG ALA SER ARG LEU MET GLN ALA ALA
SEQRES 2 A 298 GLU LEU GLY GLY PRO MET ALA VAL SER ALA ALA ALA THR
SEQRES 3 A 298 ALA GLN THR ASN PRO TYR ALA ARG GLY PRO ASN PRO THR
SEQRES 4 A 298 ALA ALA SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL
SEQRES 5 A 298 GLN SER PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA
SEQRES 6 A 298 GLY THR VAL TYR TYR PRO THR ASN ALA GLY GLY THR VAL
SEQRES 7 A 298 GLY ALA ILE ALA ILE LEU PRO GLY TYR THR ALA ARG GLN
SEQRES 8 A 298 SER SER ILE LYS TRP TRP GLY PRO ARG LEU ALA SER HIS
SEQRES 9 A 298 GLY PHE VAL VAL ILE THR ILE ASP THR ASN SER THR LEU
SEQRES 10 A 298 ASP GLN PRO SER SER ARG SER SER GLN GLN MET ALA ALA
SEQRES 11 A 298 LEU ARG GLN VAL ALA SER LEU ASN GLY THR SER SER SER
SEQRES 12 A 298 PRO ILE TYR GLY LYS VAL ASP THR ALA ARG MET GLY VAL
SEQRES 13 A 298 MET GLY TRP SER MET GLY GLY GLY GLY SER LEU ILE SER
SEQRES 14 A 298 ALA ALA ASN ASN PRO SER LEU LYS ALA ALA ALA PRO GLN
SEQRES 15 A 298 ALA PRO TRP HIS SER SER THR ASN PHE SER SER VAL THR
SEQRES 16 A 298 VAL PRO THR LEU ILE ILE ALA CYS GLU ASN ASP SER ILE
SEQRES 17 A 298 ALA PRO VAL ASN SER SER ALA LEU PRO ILE TYR ASP SER
SEQRES 18 A 298 MET SER ARG ASN ALA LYS GLN TYR LEU GLU ILE LYS GLY
SEQRES 19 A 298 GLY SER HIS SER CYS ALA ASN SER GLY ASN SER ASN GLN
SEQRES 20 A 298 ALA LEU ILE GLY LYS LYS GLY VAL ALA TRP MET LYS ARG
SEQRES 21 A 298 PHE MET ASP ASN ASP THR ARG TYR SER THR PHE ALA CYS
SEQRES 22 A 298 GLU ASN PRO ASN SER THR GLU VAL SER ARG PHE ARG THR
SEQRES 23 A 298 ALA ASN CYS SER LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 D 298 MET ASN PHE PRO ARG ALA SER ARG LEU MET GLN ALA ALA
SEQRES 2 D 298 GLU LEU GLY GLY PRO MET ALA VAL SER ALA ALA ALA THR
SEQRES 3 D 298 ALA GLN THR ASN PRO TYR ALA ARG GLY PRO ASN PRO THR
SEQRES 4 D 298 ALA ALA SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL
SEQRES 5 D 298 GLN SER PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA
SEQRES 6 D 298 GLY THR VAL TYR TYR PRO THR ASN ALA GLY GLY THR VAL
SEQRES 7 D 298 GLY ALA ILE ALA ILE LEU PRO GLY TYR THR ALA ARG GLN
SEQRES 8 D 298 SER SER ILE LYS TRP TRP GLY PRO ARG LEU ALA SER HIS
SEQRES 9 D 298 GLY PHE VAL VAL ILE THR ILE ASP THR ASN SER THR LEU
SEQRES 10 D 298 ASP GLN PRO SER SER ARG SER SER GLN GLN MET ALA ALA
SEQRES 11 D 298 LEU ARG GLN VAL ALA SER LEU ASN GLY THR SER SER SER
SEQRES 12 D 298 PRO ILE TYR GLY LYS VAL ASP THR ALA ARG MET GLY VAL
SEQRES 13 D 298 MET GLY TRP SER MET GLY GLY GLY GLY SER LEU ILE SER
SEQRES 14 D 298 ALA ALA ASN ASN PRO SER LEU LYS ALA ALA ALA PRO GLN
SEQRES 15 D 298 ALA PRO TRP HIS SER SER THR ASN PHE SER SER VAL THR
SEQRES 16 D 298 VAL PRO THR LEU ILE ILE ALA CYS GLU ASN ASP SER ILE
SEQRES 17 D 298 ALA PRO VAL ASN SER SER ALA LEU PRO ILE TYR ASP SER
SEQRES 18 D 298 MET SER ARG ASN ALA LYS GLN TYR LEU GLU ILE LYS GLY
SEQRES 19 D 298 GLY SER HIS SER CYS ALA ASN SER GLY ASN SER ASN GLN
SEQRES 20 D 298 ALA LEU ILE GLY LYS LYS GLY VAL ALA TRP MET LYS ARG
SEQRES 21 D 298 PHE MET ASP ASN ASP THR ARG TYR SER THR PHE ALA CYS
SEQRES 22 D 298 GLU ASN PRO ASN SER THR GLU VAL SER ARG PHE ARG THR
SEQRES 23 D 298 ALA ASN CYS SER LEU GLU HIS HIS HIS HIS HIS HIS
FORMUL 3 HOH *209(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 ASN A 138 1 20
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
HELIX 10 AB1 THR D 39 ALA D 45 1 7
HELIX 11 AB2 ARG D 90 LYS D 95 5 6
HELIX 12 AB3 TRP D 96 SER D 103 1 8
HELIX 13 AB4 GLN D 119 THR D 140 1 22
HELIX 14 AB5 SER D 160 ASN D 173 1 14
HELIX 15 AB6 SER D 214 MET D 222 1 9
HELIX 16 AB7 ASN D 246 ASP D 263 1 18
HELIX 17 AB8 ASP D 265 ARG D 267 5 3
HELIX 18 AB9 TYR D 268 GLU D 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 TYR A 70 N GLN A 53
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 LEU A 84 1 N ILE A 81 O VAL A 107
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 LEU A 230 N ALA A 202
SHEET 3 AA2 3 VAL A 281 ALA A 287 -1 O ARG A 285 N TYR A 229
SHEET 1 AA3 6 VAL D 52 THR D 56 0
SHEET 2 AA3 6 ALA D 65 PRO D 71 -1 O VAL D 68 N PHE D 55
SHEET 3 AA3 6 VAL D 107 ASP D 112 -1 O VAL D 108 N TYR D 69
SHEET 4 AA3 6 VAL D 78 LEU D 84 1 N ILE D 83 O ILE D 109
SHEET 5 AA3 6 VAL D 149 TRP D 159 1 O ASP D 150 N VAL D 78
SHEET 6 AA3 6 ALA D 178 GLN D 182 1 O GLN D 182 N GLY D 158
SHEET 1 AA4 3 THR D 198 CYS D 203 0
SHEET 2 AA4 3 LYS D 227 ILE D 232 1 O GLN D 228 N ILE D 200
SHEET 3 AA4 3 VAL D 281 ALA D 287 -1 O ARG D 285 N TYR D 229
SSBOND 1 CYS A 203 CYS A 239 1555 1555 2.04
SSBOND 2 CYS A 273 CYS A 289 1555 1555 2.03
SSBOND 3 CYS D 203 CYS D 239 1555 1555 2.06
SSBOND 4 CYS D 273 CYS D 289 1555 1555 2.06
CRYST1 50.279 77.925 125.040 90.00 90.00 90.00 P 2 21 21 8
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 0.019889 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012833 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007997 0.00000
TER 1918 CYS A 289
TER 3836 CYS D 289
MASTER 364 0 0 18 18 0 0 6 4043 2 8 46
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