| 7qvh-pdb | HEADER HYDROLASE 21-JAN-22 7QVH
TITLE THE CRYSTAL STRUCTURE OF HOTPETASE, AN EVOLVED THERMOSTABLE VARIANT OF
TITLE 2 ISPETASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(ETHYLENE TEREPHTHALATE) HYDROLASE;
COMPND 3 CHAIN: A, B, C;
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;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PET-DEPOLYMERASE, PETASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.J.HARDY,C.LEVY,A.P.GREEN
REVDAT 1 03-AUG-22 7QVH 0
JRNL AUTH E.L.BELL,R.SMITHSON,S.KILLBRIDE,J.FOSTER,F.H.HARDY,
JRNL AUTH 2 S.RAMACHANDRAN,A.TEDSTONE,S.J.HAIGH,A.GARFORTH,P.DAY,C.LEVY,
JRNL AUTH 3 M.SHAVER,A.P.GREEN
JRNL TITL DIRECTED EVOLUTION OF AN EFFICIENT AND THERMOSTABLE PET
JRNL TITL 2 DEPOLYMERASE
JRNL REF TO BE PUBLISHED
JRNL REFN
JRNL DOI 10.1038/S41929-022-00821-3
REMARK 2
REMARK 2 RESOLUTION. 2.24 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.18.2_3874
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.24
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 72.63
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 42230
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.560
REMARK 3 FREE R VALUE TEST SET COUNT : 1926
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 72.6300 - 5.4000 0.99 3000 105 0.1810 0.2220
REMARK 3 2 5.4000 - 4.2800 1.00 2926 119 0.1554 0.1834
REMARK 3 3 4.2800 - 3.7400 1.00 2925 108 0.1509 0.1998
REMARK 3 4 3.7400 - 3.4000 1.00 2888 133 0.1746 0.2219
REMARK 3 5 3.4000 - 3.1600 1.00 2900 134 0.1937 0.2663
REMARK 3 6 3.1600 - 2.9700 1.00 2891 136 0.1940 0.2636
REMARK 3 7 2.9700 - 2.8200 1.00 2847 147 0.2172 0.2527
REMARK 3 8 2.8200 - 2.7000 1.00 2853 159 0.2233 0.2752
REMARK 3 9 2.7000 - 2.6000 1.00 2864 140 0.2334 0.2599
REMARK 3 10 2.6000 - 2.5100 1.00 2897 114 0.2533 0.3175
REMARK 3 11 2.5100 - 2.4300 1.00 2861 133 0.2648 0.3308
REMARK 3 12 2.4300 - 2.3600 1.00 2846 166 0.2808 0.3398
REMARK 3 13 2.3600 - 2.3000 1.00 2810 184 0.3127 0.3577
REMARK 3 14 2.3000 - 2.2400 0.98 2804 148 0.3472 0.3880
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
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) : 0.398
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.140
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.46
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.11
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 : 0.003 6108
REMARK 3 ANGLE : 0.539 8318
REMARK 3 CHIRALITY : 0.044 917
REMARK 3 PLANARITY : 0.004 1091
REMARK 3 DIHEDRAL : 8.556 876
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 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7QVH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-JAN-22.
REMARK 100 THE DEPOSITION ID IS D_1292120403.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-OCT-21
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 : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42290
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.240
REMARK 200 RESOLUTION RANGE LOW (A) : 72.630
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.22330
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 5.1300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.24
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.680
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: 5XJH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.85 M SODIUM CITRATE TRIBASIC
REMARK 280 DEHYDRATE, 0.1 M TRIS PH 8.0 AND 0.1 M SODIUM CHLORIDE (LMB
REMARK 280 SCREEN HT96 H7 MOLECULAR DIMENSIONS)., VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 37.42750
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 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 HIS C 294
REMARK 465 HIS C 295
REMARK 465 HIS C 296
REMARK 465 HIS C 297
REMARK 465 HIS C 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 ASN A 37 124.03 -37.82
REMARK 500 PRO A 85 -169.76 -75.81
REMARK 500 TYR A 87 123.96 -39.51
REMARK 500 THR A 88 -13.30 75.18
REMARK 500 TYR A 146 108.41 -57.70
REMARK 500 SER A 160 -114.11 61.68
REMARK 500 ALA A 183 59.69 38.54
REMARK 500 TYR A 214 -70.41 -126.10
REMARK 500 SER A 223 -30.72 -131.74
REMARK 500 THR B 88 -2.27 69.72
REMARK 500 SER B 160 -123.90 61.02
REMARK 500 TYR B 214 -69.71 -132.12
REMARK 500 ASN B 277 70.24 45.69
REMARK 500 ASN C 73 51.63 -143.24
REMARK 500 THR C 88 -13.59 77.58
REMARK 500 THR C 90 -169.48 -126.44
REMARK 500 SER C 160 -119.80 60.52
REMARK 500 PRO C 174 -9.98 -59.55
REMARK 500 TYR C 214 -73.24 -134.89
REMARK 500 ASP C 283 116.56 -176.55
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 7QVH A 28 290 UNP PETH_IDESA
DBREF2 7QVH A A0A0K8P6T7 28 290
DBREF1 7QVH B 28 290 UNP PETH_IDESA
DBREF2 7QVH B A0A0K8P6T7 28 290
DBREF1 7QVH C 28 290 UNP PETH_IDESA
DBREF2 7QVH C A0A0K8P6T7 28 290
SEQADV 7QVH MET A 27 UNP A0A0K8P6T INITIATING METHIONINE
SEQADV 7QVH ALA A 58 UNP A0A0K8P6T SER 58 ENGINEERED MUTATION
SEQADV 7QVH VAL A 61 UNP A0A0K8P6T SER 61 ENGINEERED MUTATION
SEQADV 7QVH THR A 90 UNP A0A0K8P6T ARG 90 ENGINEERED MUTATION
SEQADV 7QVH ASN A 95 UNP A0A0K8P6T LYS 95 ENGINEERED MUTATION
SEQADV 7QVH LYS A 119 UNP A0A0K8P6T GLN 119 ENGINEERED MUTATION
SEQADV 7QVH GLU A 121 UNP A0A0K8P6T SER 121 ENGINEERED MUTATION
SEQADV 7QVH GLY A 154 UNP A0A0K8P6T MET 154 ENGINEERED MUTATION
SEQADV 7QVH VAL A 181 UNP A0A0K8P6T PRO 181 ENGINEERED MUTATION
SEQADV 7QVH MET A 182 UNP A0A0K8P6T GLN 182 ENGINEERED MUTATION
SEQADV 7QVH HIS A 186 UNP A0A0K8P6T ASP 186 ENGINEERED MUTATION
SEQADV 7QVH ARG A 207 UNP A0A0K8P6T SER 207 ENGINEERED MUTATION
SEQADV 7QVH LYS A 212 UNP A0A0K8P6T ASN 212 ENGINEERED MUTATION
SEQADV 7QVH GLU A 213 UNP A0A0K8P6T SER 213 ENGINEERED MUTATION
SEQADV 7QVH TYR A 214 UNP A0A0K8P6T SER 214 ENGINEERED MUTATION
SEQADV 7QVH LEU A 224 UNP A0A0K8P6T ARG 224 ENGINEERED MUTATION
SEQADV 7QVH CYS A 233 UNP A0A0K8P6T ASN 233 ENGINEERED MUTATION
SEQADV 7QVH CYS A 241 UNP A0A0K8P6T ASN 241 ENGINEERED MUTATION
SEQADV 7QVH MET A 252 UNP A0A0K8P6T LYS 252 ENGINEERED MUTATION
SEQADV 7QVH GLN A 270 UNP A0A0K8P6T THR 270 ENGINEERED MUTATION
SEQADV 7QVH ALA A 280 UNP A0A0K8P6T ARG 280 ENGINEERED MUTATION
SEQADV 7QVH CYS A 282 UNP A0A0K8P6T SER 282 ENGINEERED MUTATION
SEQADV 7QVH LEU A 291 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7QVH GLU A 292 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7QVH HIS A 293 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7QVH HIS A 294 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7QVH HIS A 295 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7QVH HIS A 296 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7QVH HIS A 297 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7QVH HIS A 298 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7QVH MET B 27 UNP A0A0K8P6T INITIATING METHIONINE
SEQADV 7QVH ALA B 58 UNP A0A0K8P6T SER 58 ENGINEERED MUTATION
SEQADV 7QVH VAL B 61 UNP A0A0K8P6T SER 61 ENGINEERED MUTATION
SEQADV 7QVH THR B 90 UNP A0A0K8P6T ARG 90 ENGINEERED MUTATION
SEQADV 7QVH ASN B 95 UNP A0A0K8P6T LYS 95 ENGINEERED MUTATION
SEQADV 7QVH LYS B 119 UNP A0A0K8P6T GLN 119 ENGINEERED MUTATION
SEQADV 7QVH GLU B 121 UNP A0A0K8P6T SER 121 ENGINEERED MUTATION
SEQADV 7QVH GLY B 154 UNP A0A0K8P6T MET 154 ENGINEERED MUTATION
SEQADV 7QVH VAL B 181 UNP A0A0K8P6T PRO 181 ENGINEERED MUTATION
SEQADV 7QVH MET B 182 UNP A0A0K8P6T GLN 182 ENGINEERED MUTATION
SEQADV 7QVH HIS B 186 UNP A0A0K8P6T ASP 186 ENGINEERED MUTATION
SEQADV 7QVH ARG B 207 UNP A0A0K8P6T SER 207 ENGINEERED MUTATION
SEQADV 7QVH LYS B 212 UNP A0A0K8P6T ASN 212 ENGINEERED MUTATION
SEQADV 7QVH GLU B 213 UNP A0A0K8P6T SER 213 ENGINEERED MUTATION
SEQADV 7QVH TYR B 214 UNP A0A0K8P6T SER 214 ENGINEERED MUTATION
SEQADV 7QVH LEU B 224 UNP A0A0K8P6T ARG 224 ENGINEERED MUTATION
SEQADV 7QVH CYS B 233 UNP A0A0K8P6T ASN 233 ENGINEERED MUTATION
SEQADV 7QVH CYS B 241 UNP A0A0K8P6T ASN 241 ENGINEERED MUTATION
SEQADV 7QVH MET B 252 UNP A0A0K8P6T LYS 252 ENGINEERED MUTATION
SEQADV 7QVH GLN B 270 UNP A0A0K8P6T THR 270 ENGINEERED MUTATION
SEQADV 7QVH ALA B 280 UNP A0A0K8P6T ARG 280 ENGINEERED MUTATION
SEQADV 7QVH CYS B 282 UNP A0A0K8P6T SER 282 ENGINEERED MUTATION
SEQADV 7QVH LEU B 291 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7QVH GLU B 292 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7QVH HIS B 293 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7QVH HIS B 294 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7QVH HIS B 295 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7QVH HIS B 296 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7QVH HIS B 297 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7QVH HIS B 298 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7QVH MET C 27 UNP A0A0K8P6T INITIATING METHIONINE
SEQADV 7QVH ALA C 58 UNP A0A0K8P6T SER 58 ENGINEERED MUTATION
SEQADV 7QVH VAL C 61 UNP A0A0K8P6T SER 61 ENGINEERED MUTATION
SEQADV 7QVH THR C 90 UNP A0A0K8P6T ARG 90 ENGINEERED MUTATION
SEQADV 7QVH ASN C 95 UNP A0A0K8P6T LYS 95 ENGINEERED MUTATION
SEQADV 7QVH LYS C 119 UNP A0A0K8P6T GLN 119 ENGINEERED MUTATION
SEQADV 7QVH GLU C 121 UNP A0A0K8P6T SER 121 ENGINEERED MUTATION
SEQADV 7QVH GLY C 154 UNP A0A0K8P6T MET 154 ENGINEERED MUTATION
SEQADV 7QVH VAL C 181 UNP A0A0K8P6T PRO 181 ENGINEERED MUTATION
SEQADV 7QVH MET C 182 UNP A0A0K8P6T GLN 182 ENGINEERED MUTATION
SEQADV 7QVH HIS C 186 UNP A0A0K8P6T ASP 186 ENGINEERED MUTATION
SEQADV 7QVH ARG C 207 UNP A0A0K8P6T SER 207 ENGINEERED MUTATION
SEQADV 7QVH LYS C 212 UNP A0A0K8P6T ASN 212 ENGINEERED MUTATION
SEQADV 7QVH GLU C 213 UNP A0A0K8P6T SER 213 ENGINEERED MUTATION
SEQADV 7QVH TYR C 214 UNP A0A0K8P6T SER 214 ENGINEERED MUTATION
SEQADV 7QVH LEU C 224 UNP A0A0K8P6T ARG 224 ENGINEERED MUTATION
SEQADV 7QVH CYS C 233 UNP A0A0K8P6T ASN 233 ENGINEERED MUTATION
SEQADV 7QVH CYS C 241 UNP A0A0K8P6T ASN 241 ENGINEERED MUTATION
SEQADV 7QVH MET C 252 UNP A0A0K8P6T LYS 252 ENGINEERED MUTATION
SEQADV 7QVH GLN C 270 UNP A0A0K8P6T THR 270 ENGINEERED MUTATION
SEQADV 7QVH ALA C 280 UNP A0A0K8P6T ARG 280 ENGINEERED MUTATION
SEQADV 7QVH CYS C 282 UNP A0A0K8P6T SER 282 ENGINEERED MUTATION
SEQADV 7QVH LEU C 291 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7QVH GLU C 292 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7QVH HIS C 293 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7QVH HIS C 294 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7QVH HIS C 295 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7QVH HIS C 296 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7QVH HIS C 297 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7QVH HIS C 298 UNP A0A0K8P6T EXPRESSION TAG
SEQRES 1 A 272 MET GLN THR 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 ALA ARG PRO VAL 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 THR 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 LYS PRO GLU 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 GLY 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 ALA ALA VAL MET
SEQRES 13 A 272 ALA PRO TRP HIS SER SER THR ASN PHE SER SER VAL THR
SEQRES 14 A 272 VAL PRO THR LEU ILE PHE ALA CYS GLU ASN ASP ARG ILE
SEQRES 15 A 272 ALA PRO VAL LYS GLU TYR ALA LEU PRO ILE TYR ASP SER
SEQRES 16 A 272 MET SER LEU ASN ALA LYS GLN PHE LEU GLU ILE CYS GLY
SEQRES 17 A 272 GLY SER HIS SER CYS ALA CYS SER GLY ASN SER ASN GLN
SEQRES 18 A 272 ALA LEU ILE GLY MET LYS GLY VAL ALA TRP MET LYS ARG
SEQRES 19 A 272 PHE MET ASP ASN ASP THR ARG TYR SER GLN PHE ALA CYS
SEQRES 20 A 272 GLU ASN PRO ASN SER THR ALA VAL CYS ASP PHE ARG THR
SEQRES 21 A 272 ALA ASN CYS SER LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 272 MET GLN THR ASN PRO TYR ALA ARG GLY PRO ASN PRO THR
SEQRES 2 B 272 ALA ALA SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL
SEQRES 3 B 272 ARG SER PHE THR VAL ALA ARG PRO VAL GLY TYR GLY ALA
SEQRES 4 B 272 GLY THR VAL TYR TYR PRO THR ASN ALA GLY GLY THR VAL
SEQRES 5 B 272 GLY ALA ILE ALA ILE VAL PRO GLY TYR THR ALA THR GLN
SEQRES 6 B 272 SER SER ILE ASN TRP TRP GLY PRO ARG LEU ALA SER HIS
SEQRES 7 B 272 GLY PHE VAL VAL ILE THR ILE ASP THR ASN SER THR LEU
SEQRES 8 B 272 ASP LYS PRO GLU SER ARG SER SER GLN GLN MET ALA ALA
SEQRES 9 B 272 LEU ARG GLN VAL ALA SER LEU ASN GLY THR SER SER SER
SEQRES 10 B 272 PRO ILE TYR GLY LYS VAL ASP THR ALA ARG GLY GLY VAL
SEQRES 11 B 272 MET GLY TRP SER MET GLY GLY GLY GLY SER LEU ILE SER
SEQRES 12 B 272 ALA ALA ASN ASN PRO SER LEU LYS ALA ALA ALA VAL MET
SEQRES 13 B 272 ALA PRO TRP HIS SER SER THR ASN PHE SER SER VAL THR
SEQRES 14 B 272 VAL PRO THR LEU ILE PHE ALA CYS GLU ASN ASP ARG ILE
SEQRES 15 B 272 ALA PRO VAL LYS GLU TYR ALA LEU PRO ILE TYR ASP SER
SEQRES 16 B 272 MET SER LEU ASN ALA LYS GLN PHE LEU GLU ILE CYS GLY
SEQRES 17 B 272 GLY SER HIS SER CYS ALA CYS SER GLY ASN SER ASN GLN
SEQRES 18 B 272 ALA LEU ILE GLY MET LYS GLY VAL ALA TRP MET LYS ARG
SEQRES 19 B 272 PHE MET ASP ASN ASP THR ARG TYR SER GLN PHE ALA CYS
SEQRES 20 B 272 GLU ASN PRO ASN SER THR ALA VAL CYS ASP PHE ARG THR
SEQRES 21 B 272 ALA ASN CYS SER LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 272 MET GLN THR ASN PRO TYR ALA ARG GLY PRO ASN PRO THR
SEQRES 2 C 272 ALA ALA SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL
SEQRES 3 C 272 ARG SER PHE THR VAL ALA ARG PRO VAL GLY TYR GLY ALA
SEQRES 4 C 272 GLY THR VAL TYR TYR PRO THR ASN ALA GLY GLY THR VAL
SEQRES 5 C 272 GLY ALA ILE ALA ILE VAL PRO GLY TYR THR ALA THR GLN
SEQRES 6 C 272 SER SER ILE ASN TRP TRP GLY PRO ARG LEU ALA SER HIS
SEQRES 7 C 272 GLY PHE VAL VAL ILE THR ILE ASP THR ASN SER THR LEU
SEQRES 8 C 272 ASP LYS PRO GLU SER ARG SER SER GLN GLN MET ALA ALA
SEQRES 9 C 272 LEU ARG GLN VAL ALA SER LEU ASN GLY THR SER SER SER
SEQRES 10 C 272 PRO ILE TYR GLY LYS VAL ASP THR ALA ARG GLY GLY VAL
SEQRES 11 C 272 MET GLY TRP SER MET GLY GLY GLY GLY SER LEU ILE SER
SEQRES 12 C 272 ALA ALA ASN ASN PRO SER LEU LYS ALA ALA ALA VAL MET
SEQRES 13 C 272 ALA PRO TRP HIS SER SER THR ASN PHE SER SER VAL THR
SEQRES 14 C 272 VAL PRO THR LEU ILE PHE ALA CYS GLU ASN ASP ARG ILE
SEQRES 15 C 272 ALA PRO VAL LYS GLU TYR ALA LEU PRO ILE TYR ASP SER
SEQRES 16 C 272 MET SER LEU ASN ALA LYS GLN PHE LEU GLU ILE CYS GLY
SEQRES 17 C 272 GLY SER HIS SER CYS ALA CYS SER GLY ASN SER ASN GLN
SEQRES 18 C 272 ALA LEU ILE GLY MET LYS GLY VAL ALA TRP MET LYS ARG
SEQRES 19 C 272 PHE MET ASP ASN ASP THR ARG TYR SER GLN PHE ALA CYS
SEQRES 20 C 272 GLU ASN PRO ASN SER THR ALA VAL CYS ASP PHE ARG THR
SEQRES 21 C 272 ALA ASN CYS SER LEU GLU HIS HIS HIS HIS HIS HIS
HET PGE A 401 24
HET PGE C 401 24
HETNAM PGE TRIETHYLENE GLYCOL
FORMUL 4 PGE 2(C6 H14 O4)
FORMUL 6 HOH *212(H2 O)
HELIX 1 AA1 THR A 39 ALA A 45 1 7
HELIX 2 AA2 THR A 90 ASN A 95 5 6
HELIX 3 AA3 TRP A 96 SER A 103 1 8
HELIX 4 AA4 LYS A 119 GLY A 139 1 21
HELIX 5 AA5 SER A 160 ASN A 173 1 14
HELIX 6 AA6 TYR 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 THR B 90 ASN B 95 5 6
HELIX 12 AB3 TRP B 96 SER B 103 1 8
HELIX 13 AB4 LYS B 119 GLY B 139 1 21
HELIX 14 AB5 SER B 160 ASN B 173 1 14
HELIX 15 AB6 TYR B 214 SER B 221 1 8
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
HELIX 19 AC1 THR C 39 ALA C 45 1 7
HELIX 20 AC2 THR C 90 ASN C 95 5 6
HELIX 21 AC3 TRP C 96 SER C 103 1 8
HELIX 22 AC4 LYS C 119 GLY C 139 1 21
HELIX 23 AC5 SER C 160 ASN C 173 1 14
HELIX 24 AC6 TYR C 214 MET C 222 1 9
HELIX 25 AC7 ASN C 246 ASP C 263 1 18
HELIX 26 AC8 ASP C 265 ARG C 267 5 3
HELIX 27 AC9 TYR C 268 GLU C 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 81 O VAL A 107
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 MET A 182 1 O MET 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 ARG A 285 N PHE A 229
SHEET 1 AA2 9 VAL B 52 THR B 56 0
SHEET 2 AA2 9 ALA B 65 PRO B 71 -1 O VAL B 68 N PHE B 55
SHEET 3 AA2 9 VAL B 107 ASP B 112 -1 O VAL B 108 N TYR B 69
SHEET 4 AA2 9 VAL B 78 VAL B 84 1 N ILE B 81 O ILE B 109
SHEET 5 AA2 9 VAL B 149 TRP B 159 1 O ASP B 150 N VAL B 78
SHEET 6 AA2 9 ALA B 178 MET B 182 1 O MET B 182 N GLY B 158
SHEET 7 AA2 9 THR B 198 CYS B 203 1 O PHE B 201 N VAL B 181
SHEET 8 AA2 9 LYS B 227 ILE B 232 1 O ILE B 232 N ALA B 202
SHEET 9 AA2 9 VAL B 281 ALA B 287 -1 O ARG B 285 N PHE B 229
SHEET 1 AA3 9 VAL C 52 THR C 56 0
SHEET 2 AA3 9 ALA C 65 PRO C 71 -1 O VAL C 68 N PHE C 55
SHEET 3 AA3 9 VAL C 107 ASP C 112 -1 O VAL C 108 N TYR C 69
SHEET 4 AA3 9 VAL C 78 VAL C 84 1 N ILE C 81 O ILE C 109
SHEET 5 AA3 9 VAL C 149 TRP C 159 1 O ASP C 150 N VAL C 78
SHEET 6 AA3 9 ALA C 178 MET C 182 1 O MET C 182 N GLY C 158
SHEET 7 AA3 9 THR C 198 CYS C 203 1 O PHE C 201 N VAL C 181
SHEET 8 AA3 9 LYS C 227 ILE C 232 1 O ILE C 232 N ALA C 202
SHEET 9 AA3 9 VAL C 281 ALA C 287 -1 O ARG C 285 N PHE C 229
SSBOND 1 CYS A 203 CYS A 239 1555 1555 2.03
SSBOND 2 CYS A 233 CYS A 282 1555 1555 2.03
SSBOND 3 CYS A 273 CYS A 289 1555 1555 2.03
SSBOND 4 CYS B 203 CYS B 239 1555 1555 2.03
SSBOND 5 CYS B 233 CYS B 282 1555 1555 2.03
SSBOND 6 CYS B 273 CYS B 289 1555 1555 2.03
SSBOND 7 CYS C 203 CYS C 239 1555 1555 2.03
SSBOND 8 CYS C 233 CYS C 282 1555 1555 2.03
SSBOND 9 CYS C 273 CYS C 289 1555 1555 2.03
CRYST1 81.700 74.855 82.701 90.00 118.57 90.00 P 1 21 1 6
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 0.012240 0.000000 0.006666 0.00000
SCALE2 0.000000 0.013359 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013769 0.00000
TER 3842 LEU A 291
TER 7801 HIS B 298
TER 11665 HIS C 293
MASTER 264 0 2 27 27 0 0 6 6165 3 66 63
END
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