| content |
HEADER HYDROLASE 21-OCT-22 8H83
TITLE CRYSTAL STRUCTURE OF A ISPETASE VARIANT V22 FROM IDEONELLA SAKAIENSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(ETHYLENE TEREPHTHALATE) HYDROLASE;
COMPND 3 CHAIN: A, B;
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 STRAIN: NBRC 110686 / TISTR 2288 / 201-F6;
SOURCE 5 GENE: ISF6_4831;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-28A
KEYWDS PET DEGRADATION, MUTANT, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.L.WEI,S.F.GAO,Q.LI,X.HAN,J.GAO,W.D.LIU
REVDAT 1 24-APR-24 8H83 0
JRNL AUTH H.L.WEI,S.F.GAO,Q.LI,X.HAN,J.GAO,W.D.LIU
JRNL TITL CRYSTAL STRUCTURE OF A ISPETASE VARIANT V22 FROM IDEONELLA
JRNL TITL 2 SAKAIENSIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.92 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.92
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.89
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 41956
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2098
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 47.8900 - 4.1400 1.00 4351 229 0.1864 0.1829
REMARK 3 2 4.1400 - 3.2900 1.00 4183 220 0.1669 0.1812
REMARK 3 3 3.2900 - 2.8700 1.00 4125 217 0.1762 0.1781
REMARK 3 4 2.8700 - 2.6100 1.00 4104 217 0.1782 0.2126
REMARK 3 5 2.6100 - 2.4200 1.00 4114 216 0.1867 0.2015
REMARK 3 6 2.4200 - 2.2800 1.00 4080 214 0.1993 0.2418
REMARK 3 7 2.2800 - 2.1600 1.00 4058 213 0.2102 0.2390
REMARK 3 8 2.1600 - 2.0700 1.00 4032 213 0.2275 0.2712
REMARK 3 9 2.0700 - 1.9900 0.97 3936 208 0.2551 0.2773
REMARK 3 10 1.9900 - 1.9200 0.71 2875 151 0.3228 0.3608
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.640
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.79
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.43
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN A AND RESID 62 THROUGH 321)
REMARK 3 SELECTION : CHAIN B
REMARK 3 ATOM PAIRS NUMBER : 1579
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 8H83 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-OCT-22.
REMARK 100 THE DEPOSITION ID IS D_1300032472.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-SEP-22
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL19U1
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 : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43072
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.920
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 13.00
REMARK 200 R MERGE (I) : 0.21800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 3.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.93
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 8.70
REMARK 200 R MERGE FOR SHELL (I) : 1.51600
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 (%): 38.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0 M SODIUM CITRATE, 0.1 M IMIDAZOLE
REMARK 280 PH 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K
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 40.32800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 67.38200
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.32800
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 67.38200
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: B
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 A 513 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 520 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 527 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 -31
REMARK 465 LYS A -30
REMARK 465 TYR A -29
REMARK 465 LEU A -28
REMARK 465 LEU A -27
REMARK 465 PRO A -26
REMARK 465 THR A -25
REMARK 465 ALA A -24
REMARK 465 ALA A -23
REMARK 465 ALA A -22
REMARK 465 GLY A -21
REMARK 465 LEU A -20
REMARK 465 LEU A -19
REMARK 465 LEU A -18
REMARK 465 LEU A -17
REMARK 465 ALA A -16
REMARK 465 ALA A -15
REMARK 465 GLN A -14
REMARK 465 PRO A -13
REMARK 465 THR A -12
REMARK 465 MET A -11
REMARK 465 ALA A -10
REMARK 465 MET A -9
REMARK 465 ASP A -8
REMARK 465 ILE A -7
REMARK 465 GLY A -6
REMARK 465 ILE A -5
REMARK 465 ASN A -4
REMARK 465 SER A -3
REMARK 465 ASP A -2
REMARK 465 PRO A -1
REMARK 465 ASN A 0
REMARK 465 SER 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 THR A 29
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 B -31
REMARK 465 LYS B -30
REMARK 465 TYR B -29
REMARK 465 LEU B -28
REMARK 465 LEU B -27
REMARK 465 PRO B -26
REMARK 465 THR B -25
REMARK 465 ALA B -24
REMARK 465 ALA B -23
REMARK 465 ALA B -22
REMARK 465 GLY B -21
REMARK 465 LEU B -20
REMARK 465 LEU B -19
REMARK 465 LEU B -18
REMARK 465 LEU B -17
REMARK 465 ALA B -16
REMARK 465 ALA B -15
REMARK 465 GLN B -14
REMARK 465 PRO B -13
REMARK 465 THR B -12
REMARK 465 MET B -11
REMARK 465 ALA B -10
REMARK 465 MET B -9
REMARK 465 ASP B -8
REMARK 465 ILE B -7
REMARK 465 GLY B -6
REMARK 465 ILE B -5
REMARK 465 ASN B -4
REMARK 465 SER B -3
REMARK 465 ASP B -2
REMARK 465 PRO B -1
REMARK 465 ASN B 0
REMARK 465 SER B 1
REMARK 465 ASN B 2
REMARK 465 PHE B 3
REMARK 465 PRO B 4
REMARK 465 ARG B 5
REMARK 465 ALA B 6
REMARK 465 SER B 7
REMARK 465 ARG B 8
REMARK 465 LEU B 9
REMARK 465 MET B 10
REMARK 465 GLN B 11
REMARK 465 ALA B 12
REMARK 465 ALA B 13
REMARK 465 GLU B 14
REMARK 465 LEU B 15
REMARK 465 GLY B 16
REMARK 465 GLY B 17
REMARK 465 PRO B 18
REMARK 465 MET B 19
REMARK 465 ALA B 20
REMARK 465 VAL B 21
REMARK 465 SER B 22
REMARK 465 ALA B 23
REMARK 465 ALA B 24
REMARK 465 ALA B 25
REMARK 465 THR B 26
REMARK 465 ALA B 27
REMARK 465 GLN B 28
REMARK 465 THR B 29
REMARK 465 SER B 290
REMARK 465 LEU B 291
REMARK 465 GLU B 292
REMARK 465 HIS B 293
REMARK 465 HIS B 294
REMARK 465 HIS B 295
REMARK 465 HIS B 296
REMARK 465 HIS B 297
REMARK 465 HIS B 298
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 THR A 88 -5.15 69.73
REMARK 500 SER A 160 -111.03 60.75
REMARK 500 SER A 214 -81.45 -126.99
REMARK 500 THR B 88 -4.58 69.37
REMARK 500 SER B 160 -111.26 59.57
REMARK 500 SER B 214 -74.04 -122.64
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 8H83 A 2 290 UNP PETH_IDESA
DBREF2 8H83 A A0A0K8P6T7 2 290
DBREF1 8H83 B 2 290 UNP PETH_IDESA
DBREF2 8H83 B A0A0K8P6T7 2 290
SEQADV 8H83 MET A -31 UNP A0A0K8P6T INITIATING METHIONINE
SEQADV 8H83 LYS A -30 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 TYR A -29 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 LEU A -28 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 LEU A -27 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 PRO A -26 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 THR A -25 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 ALA A -24 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 ALA A -23 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 ALA A -22 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 GLY A -21 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 LEU A -20 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 LEU A -19 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 LEU A -18 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 LEU A -17 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 ALA A -16 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 ALA A -15 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 GLN A -14 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 PRO A -13 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 THR A -12 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 MET A -11 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 ALA A -10 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 MET A -9 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 ASP A -8 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 ILE A -7 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 GLY A -6 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 ILE A -5 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 ASN A -4 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 SER A -3 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 ASP A -2 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 PRO A -1 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 ASN A 0 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 SER A 1 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 GLU A 14 UNP A0A0K8P6T VAL 14 VARIANT
SEQADV 8H83 PRO A 18 UNP A0A0K8P6T LEU 18 VARIANT
SEQADV 8H83 LEU A 84 UNP A0A0K8P6T VAL 84 VARIANT
SEQADV 8H83 ILE A 201 UNP A0A0K8P6T PHE 201 VARIANT
SEQADV 8H83 GLN A 204 UNP A0A0K8P6T GLU 204 VARIANT
SEQADV 8H83 TYR A 229 UNP A0A0K8P6T PHE 229 VARIANT
SEQADV 8H83 LYS A 233 UNP A0A0K8P6T ASN 233 VARIANT
SEQADV 8H83 GLU A 280 UNP A0A0K8P6T ARG 280 VARIANT
SEQADV 8H83 ARG A 283 UNP A0A0K8P6T ASP 283 VARIANT
SEQADV 8H83 LEU A 291 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 GLU A 292 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 HIS A 293 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 HIS A 294 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 HIS A 295 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 HIS A 296 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 HIS A 297 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 HIS A 298 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 MET B -31 UNP A0A0K8P6T INITIATING METHIONINE
SEQADV 8H83 LYS B -30 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 TYR B -29 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 LEU B -28 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 LEU B -27 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 PRO B -26 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 THR B -25 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 ALA B -24 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 ALA B -23 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 ALA B -22 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 GLY B -21 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 LEU B -20 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 LEU B -19 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 LEU B -18 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 LEU B -17 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 ALA B -16 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 ALA B -15 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 GLN B -14 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 PRO B -13 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 THR B -12 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 MET B -11 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 ALA B -10 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 MET B -9 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 ASP B -8 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 ILE B -7 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 GLY B -6 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 ILE B -5 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 ASN B -4 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 SER B -3 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 ASP B -2 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 PRO B -1 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 ASN B 0 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 SER B 1 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 GLU B 14 UNP A0A0K8P6T VAL 14 VARIANT
SEQADV 8H83 PRO B 18 UNP A0A0K8P6T LEU 18 VARIANT
SEQADV 8H83 LEU B 84 UNP A0A0K8P6T VAL 84 VARIANT
SEQADV 8H83 ILE B 201 UNP A0A0K8P6T PHE 201 VARIANT
SEQADV 8H83 GLN B 204 UNP A0A0K8P6T GLU 204 VARIANT
SEQADV 8H83 TYR B 229 UNP A0A0K8P6T PHE 229 VARIANT
SEQADV 8H83 LYS B 233 UNP A0A0K8P6T ASN 233 VARIANT
SEQADV 8H83 GLU B 280 UNP A0A0K8P6T ARG 280 VARIANT
SEQADV 8H83 ARG B 283 UNP A0A0K8P6T ASP 283 VARIANT
SEQADV 8H83 LEU B 291 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 GLU B 292 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 HIS B 293 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 HIS B 294 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 HIS B 295 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 HIS B 296 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 HIS B 297 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8H83 HIS B 298 UNP A0A0K8P6T EXPRESSION TAG
SEQRES 1 A 330 MET LYS TYR LEU LEU PRO THR ALA ALA ALA GLY LEU LEU
SEQRES 2 A 330 LEU LEU ALA ALA GLN PRO THR MET ALA MET ASP ILE GLY
SEQRES 3 A 330 ILE ASN SER ASP PRO ASN SER ASN PHE PRO ARG ALA SER
SEQRES 4 A 330 ARG LEU MET GLN ALA ALA GLU LEU GLY GLY PRO MET ALA
SEQRES 5 A 330 VAL SER ALA ALA ALA THR ALA GLN THR ASN PRO TYR ALA
SEQRES 6 A 330 ARG GLY PRO ASN PRO THR ALA ALA SER LEU GLU ALA SER
SEQRES 7 A 330 ALA GLY PRO PHE THR VAL ARG SER PHE THR VAL SER ARG
SEQRES 8 A 330 PRO SER GLY TYR GLY ALA GLY THR VAL TYR TYR PRO THR
SEQRES 9 A 330 ASN ALA GLY GLY THR VAL GLY ALA ILE ALA ILE LEU PRO
SEQRES 10 A 330 GLY TYR THR ALA ARG GLN SER SER ILE LYS TRP TRP GLY
SEQRES 11 A 330 PRO ARG LEU ALA SER HIS GLY PHE VAL VAL ILE THR ILE
SEQRES 12 A 330 ASP THR ASN SER THR LEU ASP GLN PRO SER SER ARG SER
SEQRES 13 A 330 SER GLN GLN MET ALA ALA LEU ARG GLN VAL ALA SER LEU
SEQRES 14 A 330 ASN GLY THR SER SER SER PRO ILE TYR GLY LYS VAL ASP
SEQRES 15 A 330 THR ALA ARG MET GLY VAL MET GLY TRP SER MET GLY GLY
SEQRES 16 A 330 GLY GLY SER LEU ILE SER ALA ALA ASN ASN PRO SER LEU
SEQRES 17 A 330 LYS ALA ALA ALA PRO GLN ALA PRO TRP ASP SER SER THR
SEQRES 18 A 330 ASN PHE SER SER VAL THR VAL PRO THR LEU ILE ILE ALA
SEQRES 19 A 330 CYS GLN ASN ASP SER ILE ALA PRO VAL ASN SER SER ALA
SEQRES 20 A 330 LEU PRO ILE TYR ASP SER MET SER ARG ASN ALA LYS GLN
SEQRES 21 A 330 TYR LEU GLU ILE LYS GLY GLY SER HIS SER CYS ALA ASN
SEQRES 22 A 330 SER GLY ASN SER ASN GLN ALA LEU ILE GLY LYS LYS GLY
SEQRES 23 A 330 VAL ALA TRP MET LYS ARG PHE MET ASP ASN ASP THR ARG
SEQRES 24 A 330 TYR SER THR PHE ALA CYS GLU ASN PRO ASN SER THR GLU
SEQRES 25 A 330 VAL SER ARG PHE ARG THR ALA ASN CYS SER LEU GLU HIS
SEQRES 26 A 330 HIS HIS HIS HIS HIS
SEQRES 1 B 330 MET LYS TYR LEU LEU PRO THR ALA ALA ALA GLY LEU LEU
SEQRES 2 B 330 LEU LEU ALA ALA GLN PRO THR MET ALA MET ASP ILE GLY
SEQRES 3 B 330 ILE ASN SER ASP PRO ASN SER ASN PHE PRO ARG ALA SER
SEQRES 4 B 330 ARG LEU MET GLN ALA ALA GLU LEU GLY GLY PRO MET ALA
SEQRES 5 B 330 VAL SER ALA ALA ALA THR ALA GLN THR ASN PRO TYR ALA
SEQRES 6 B 330 ARG GLY PRO ASN PRO THR ALA ALA SER LEU GLU ALA SER
SEQRES 7 B 330 ALA GLY PRO PHE THR VAL ARG SER PHE THR VAL SER ARG
SEQRES 8 B 330 PRO SER GLY TYR GLY ALA GLY THR VAL TYR TYR PRO THR
SEQRES 9 B 330 ASN ALA GLY GLY THR VAL GLY ALA ILE ALA ILE LEU PRO
SEQRES 10 B 330 GLY TYR THR ALA ARG GLN SER SER ILE LYS TRP TRP GLY
SEQRES 11 B 330 PRO ARG LEU ALA SER HIS GLY PHE VAL VAL ILE THR ILE
SEQRES 12 B 330 ASP THR ASN SER THR LEU ASP GLN PRO SER SER ARG SER
SEQRES 13 B 330 SER GLN GLN MET ALA ALA LEU ARG GLN VAL ALA SER LEU
SEQRES 14 B 330 ASN GLY THR SER SER SER PRO ILE TYR GLY LYS VAL ASP
SEQRES 15 B 330 THR ALA ARG MET GLY VAL MET GLY TRP SER MET GLY GLY
SEQRES 16 B 330 GLY GLY SER LEU ILE SER ALA ALA ASN ASN PRO SER LEU
SEQRES 17 B 330 LYS ALA ALA ALA PRO GLN ALA PRO TRP ASP SER SER THR
SEQRES 18 B 330 ASN PHE SER SER VAL THR VAL PRO THR LEU ILE ILE ALA
SEQRES 19 B 330 CYS GLN ASN ASP SER ILE ALA PRO VAL ASN SER SER ALA
SEQRES 20 B 330 LEU PRO ILE TYR ASP SER MET SER ARG ASN ALA LYS GLN
SEQRES 21 B 330 TYR LEU GLU ILE LYS GLY GLY SER HIS SER CYS ALA ASN
SEQRES 22 B 330 SER GLY ASN SER ASN GLN ALA LEU ILE GLY LYS LYS GLY
SEQRES 23 B 330 VAL ALA TRP MET LYS ARG PHE MET ASP ASN ASP THR ARG
SEQRES 24 B 330 TYR SER THR PHE ALA CYS GLU ASN PRO ASN SER THR GLU
SEQRES 25 B 330 VAL SER ARG PHE ARG THR ALA ASN CYS SER LEU GLU HIS
SEQRES 26 B 330 HIS HIS HIS HIS HIS
FORMUL 3 HOH *453(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 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 B 39 ALA B 45 1 7
HELIX 11 AB2 ARG B 90 LYS B 95 1 6
HELIX 12 AB3 TRP B 96 SER B 103 1 8
HELIX 13 AB4 GLN B 119 GLY B 139 1 21
HELIX 14 AB5 SER B 160 ASN B 173 1 14
HELIX 15 AB6 SER B 214 MET B 222 1 9
HELIX 16 AB7 ASN B 246 ASP B 263 1 18
HELIX 17 AB8 ASP B 265 ARG B 267 5 3
HELIX 18 AB9 TYR B 268 GLU B 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 ARG 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 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 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 B 52 THR B 56 0
SHEET 2 AA3 6 ALA B 65 PRO B 71 -1 O VAL B 68 N PHE B 55
SHEET 3 AA3 6 VAL B 107 ASP B 112 -1 O VAL B 108 N TYR B 69
SHEET 4 AA3 6 VAL B 78 LEU B 84 1 N ILE B 81 O VAL B 107
SHEET 5 AA3 6 VAL B 149 TRP B 159 1 O ASP B 150 N VAL B 78
SHEET 6 AA3 6 ALA B 178 GLN B 182 1 O GLN B 182 N GLY B 158
SHEET 1 AA4 3 THR B 198 CYS B 203 0
SHEET 2 AA4 3 LYS B 227 ILE B 232 1 O LEU B 230 N ALA B 202
SHEET 3 AA4 3 VAL B 281 ALA B 287 -1 O ARG B 285 N TYR B 229
SSBOND 1 CYS A 203 CYS A 239 1555 1555 2.06
SSBOND 2 CYS A 273 CYS A 289 1555 1555 2.05
SSBOND 3 CYS B 203 CYS B 239 1555 1555 2.05
SSBOND 4 CYS B 273 CYS B 289 1555 1555 2.05
CRYST1 51.234 80.656 134.764 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 0.019518 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012398 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007420 0.00000
TER 1920 SER A 290
TER 3834 CYS B 289
MASTER 388 0 0 18 18 0 0 6 4285 2 8 52
END |