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HEADER HYDROLASE 18-DEC-23 8VE9
TITLE ISPETASE - ACCCETN MUTANT - COMBIPETASE
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 8VE9 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. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0419
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.59
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 36462
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.145
REMARK 3 FREE R VALUE : 0.172
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1823
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2510
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.14
REMARK 3 BIN R VALUE (WORKING SET) : 0.2430
REMARK 3 BIN FREE R VALUE SET COUNT : 142
REMARK 3 BIN FREE R VALUE : 0.2940
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1928
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 13
REMARK 3 SOLVENT ATOMS : 197
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.26
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.07100
REMARK 3 B22 (A**2) : 0.11000
REMARK 3 B33 (A**2) : 0.96200
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): 0.068
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.070
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.050
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.507
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.978
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.968
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2030 ; 0.011 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): 1853 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2779 ; 1.846 ; 1.769
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4283 ; 0.648 ; 1.715
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 282 ; 6.576 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 12 ;10.624 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 300 ;11.285 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 313 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2486 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 480 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 421 ; 0.220 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 36 ; 0.195 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1034 ; 0.181 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 123 ; 0.250 ; 0.200
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): 1071 ; 1.849 ; 2.176
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1071 ; 1.853 ; 2.177
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1342 ; 2.419 ; 3.898
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1343 ; 2.418 ; 3.901
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 959 ; 2.751 ; 2.399
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 960 ; 2.749 ; 2.402
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1427 ; 3.999 ; 4.299
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1428 ; 3.998 ; 4.300
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 BULK SOLVENT
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 THEIR
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 8VE9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-DEC-23.
REMARK 100 THE DEPOSITION ID IS D_1000279667.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-NOV-23
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 3.71
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95373
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC 1.0.5
REMARK 200 DATA SCALING SOFTWARE : AUTOPROC 1.0.5
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36462
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 51.588
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 13.50
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.60
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: PHASER 2.8.3
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22.4% (W/V) PEG 3350, 0.23 M TMAO, 0.1
REMARK 280 M TRISODIUM CITRATE-CITRIC ACID PH 3.71, VAPOR DIFFUSION,
REMARK 280 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 25.23750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.29600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.12950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.29600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.23750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.12950
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 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 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG A 59 CD NE CZ NH1 NH2
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 H PHE A 191 HG SER A 221 1.28
REMARK 500 O PRO A 210 HG1 THR A 214 1.59
REMARK 500 OG SER A 223 O HOH A 401 2.07
REMARK 500 O HOH A 543 O HOH A 574 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 132 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 MET A 161 CG - SD - CE ANGL. DEV. = -9.7 DEGREES
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 42.38 -144.78
REMARK 500 THR A 88 -11.45 80.26
REMARK 500 SER A 160 -119.21 62.00
REMARK 500 THR A 214 -78.14 -129.15
REMARK 500 THR A 214 -76.20 -130.47
REMARK 500 THR A 214 -76.49 -130.23
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 59 0.23 SIDE CHAIN
REMARK 500 ARG A 123 0.12 SIDE CHAIN
REMARK 500 ARG A 132 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 8VEK RELATED DB: PDB
REMARK 900 RELATED ID: 8VEL RELATED DB: PDB
REMARK 900 RELATED ID: 8VEM RELATED DB: PDB
DBREF1 8VE9 A 30 290 UNP PETH_IDESA
DBREF2 8VE9 A A0A0K8P6T7 30 290
SEQADV 8VE9 MET A 27 UNP A0A0K8P6T INITIATING METHIONINE
SEQADV 8VE9 GLY A 28 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8VE9 SER A 29 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8VE9 ASN A 95 UNP A0A0K8P6T LYS 95 ENGINEERED MUTATION
SEQADV 8VE9 GLU A 136 UNP A0A0K8P6T SER 136 ENGINEERED MUTATION
SEQADV 8VE9 CYS A 179 UNP A0A0K8P6T ALA 179 ENGINEERED MUTATION
SEQADV 8VE9 ALA A 186 UNP A0A0K8P6T ASP 186 ENGINEERED MUTATION
SEQADV 8VE9 THR A 214 UNP A0A0K8P6T SER 214 ENGINEERED MUTATION
SEQADV 8VE9 CYS A 233 UNP A0A0K8P6T ASN 233 ENGINEERED MUTATION
SEQADV 8VE9 CYS A 282 UNP A0A0K8P6T SER 282 ENGINEERED MUTATION
SEQADV 8VE9 ALA A 291 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8VE9 SER A 292 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8VE9 HIS A 293 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8VE9 HIS A 294 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8VE9 HIS A 295 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8VE9 HIS A 296 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8VE9 HIS A 297 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8VE9 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 ASN 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 GLU 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 THR LEU ILE PHE ALA CYS GLU ASN ASP SER ILE
SEQRES 15 A 272 ALA PRO VAL ASN SER THR 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 GOL A 301 14
HET CL A 302 1
HET GOL A 303 14
HETNAM GOL GLYCEROL
HETNAM CL CHLORIDE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL 2(C3 H8 O3)
FORMUL 3 CL CL 1-
FORMUL 5 HOH *197(H2 O)
HELIX 1 AA1 THR A 39 ALA A 45 1 7
HELIX 2 AA2 ARG A 90 ASN 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 THR 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 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 2.05
SSBOND 2 CYS A 233 CYS A 282 1555 1555 2.15
SSBOND 3 CYS A 273 CYS A 289 1555 1555 2.15
CRYST1 50.475 68.259 78.592 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 0.019812 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014650 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012724 0.00000
TER 3897 ALA A 291
MASTER 338 0 3 9 9 0 0 6 2138 1 34 21
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