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HEADER HYDROLASE 11-APR-25 9QVA
TITLE POLYESTER HYDROLASE LEIPZIG 7 (PHL7) VARIANT R2M2-P155G-A186S
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYESTER HYDROLASE LEIPZIG 7 (PHL-7), CATALYSIS-DEFICIENT
COMPND 3 S131A MUTANT;
COMPND 4 CHAIN: A, B;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: COMPOST METAGENOME;
SOURCE 3 ORGANISM_TAXID: 702656;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PET HYDROLASE, ENZYMATIC PLASTIC DEGRADATION, ENZYME ENGINEERING,
KEYWDS 2 POLYESTER HYDROLASE LEIPZIG 7, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.USEINI,N.STRATER,G.KUENZE,C.SONNENDECKER
REVDAT 1 27-MAY-26 9QVA 0
JRNL AUTH P.BLAZQUEZ-SANCHEZ,J.GUNKEL,A.USEINI,A.ZLOBIN,J.D.ZAKARY,
JRNL AUTH 2 A.SCHOLER,N.GRAEFE,F.ENGELBERGER,F.CANTANHEDE,R.FRANK,
JRNL AUTH 3 Z.ZHAO,A.ZAREI,E.BUTENSCHON,J.MATYSIK,W.ZIMMERMANN,
JRNL AUTH 4 N.STRATER,C.SONNENDECKER,G.KUNZE
JRNL TITL COMPUTATIONAL ENGINEERING OF THE POLYESTER HYDROLASE PHL7
JRNL TITL 2 FOR EFFICIENT POLY(ETHYLENE TEREPHTHALATE) DEGRADATION IN
JRNL TITL 3 BIOCATALYTIC RECYCLING PROCESSES.
JRNL REF NAT COMMUN V. 17 2026
JRNL REFN ESSN 2041-1723
JRNL PMID 42140896
JRNL DOI 10.1038/S41467-026-70868-4
REMARK 2
REMARK 2 RESOLUTION. 1.59 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.59
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 62.95
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 56.4
REMARK 3 NUMBER OF REFLECTIONS : 72371
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.530
REMARK 3 FREE R VALUE TEST SET COUNT : 4002
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 62.9500 - 4.8800 0.97 4062 232 0.2156 0.2469
REMARK 3 2 4.8700 - 3.8700 0.99 4193 224 0.1501 0.2030
REMARK 3 3 3.8700 - 3.3800 1.00 4206 212 0.1544 0.1913
REMARK 3 4 3.3800 - 3.0700 0.99 4109 275 0.1717 0.2188
REMARK 3 5 3.0700 - 2.8500 0.96 4072 222 0.1877 0.2569
REMARK 3 6 2.8500 - 2.6800 0.96 3993 240 0.2026 0.2582
REMARK 3 7 2.6800 - 2.5500 0.98 4102 249 0.2104 0.2141
REMARK 3 8 2.5500 - 2.4400 0.98 4033 298 0.2168 0.2458
REMARK 3 9 2.4400 - 2.3400 0.94 3944 218 0.2130 0.2715
REMARK 3 10 2.3400 - 2.2600 0.87 3598 218 0.2110 0.2660
REMARK 3 11 2.2600 - 2.1900 0.81 3391 172 0.2132 0.2918
REMARK 3 12 2.1900 - 2.1300 0.75 3159 179 0.2203 0.2546
REMARK 3 13 2.1300 - 2.0700 0.69 2884 157 0.2326 0.3098
REMARK 3 14 2.0700 - 2.0200 0.62 2573 137 0.2403 0.3049
REMARK 3 15 2.0200 - 1.9800 0.54 2279 122 0.2420 0.2804
REMARK 3 16 1.9800 - 1.9400 0.49 2088 108 0.2432 0.2216
REMARK 3 17 1.9400 - 1.9000 0.44 1790 118 0.2577 0.2982
REMARK 3 18 1.9000 - 1.8600 0.39 1663 92 0.2682 0.3011
REMARK 3 19 1.8600 - 1.8300 0.36 1495 102 0.2706 0.2480
REMARK 3 20 1.8300 - 1.8000 0.32 1348 78 0.2875 0.3452
REMARK 3 21 1.8000 - 1.7700 0.28 1175 83 0.2781 0.3523
REMARK 3 22 1.7700 - 1.7400 0.25 1032 72 0.2861 0.3371
REMARK 3 23 1.7400 - 1.7200 0.21 853 55 0.2844 0.3226
REMARK 3 24 1.7100 - 1.6900 0.00 758 43 0.2946 0.3348
REMARK 3 25 1.6900 - 1.6700 0.00 578 47 0.2582 0.3097
REMARK 3 26 1.6700 - 1.6500 0.00 467 23 0.2462 0.3517
REMARK 3 27 1.6500 - 1.6300 0.00 271 13 0.0000 0.1956
REMARK 3 28 1.6300 - 1.6100 0.00 171 13 0.3135 0.4048
REMARK 3 29 1.6100 - 1.5900 0.00 82 0 0.3170 0.0000
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) : 0.216
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.311
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.93
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.19
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 : 0.002 4240
REMARK 3 ANGLE : 0.483 5840
REMARK 3 CHIRALITY : 0.042 653
REMARK 3 PLANARITY : 0.005 781
REMARK 3 DIHEDRAL : 10.500 1572
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 : ens_1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "A" and (resid 2 through 13 or
REMARK 3 resid 15 through 19 or resid 21 through
REMARK 3 24 or resid 26 through 30 or resid 32
REMARK 3 through 103 or resid 105 through 116 or
REMARK 3 resid 119 through 138 or resid 140
REMARK 3 through 143 or resid 145 or resid 147
REMARK 3 through 165 or resid 167 through 178 or
REMARK 3 resid 180 through 186 or resid 188
REMARK 3 through 191 or resid 193 through 194 or
REMARK 3 resid 196 through 211 or resid 213 or
REMARK 3 resid 215 through 251 or resid 253
REMARK 3 through 261 or resid 301))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "B" and (resid 2 through 13 or
REMARK 3 resid 15 through 19 or resid 21 through
REMARK 3 24 or resid 26 through 30 or resid 32
REMARK 3 through 103 or resid 105 through 116 or
REMARK 3 resid 119 through 138 or resid 140
REMARK 3 through 143 or resid 145 or resid 147
REMARK 3 through 165 or resid 167 through 178 or
REMARK 3 resid 180 through 186 or resid 188
REMARK 3 through 191 or resid 193 through 194 or
REMARK 3 resid 196 through 211 or resid 213 or
REMARK 3 resid 215 through 251 or resid 253
REMARK 3 through 261 or resid 301))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 9QVA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-APR-25.
REMARK 100 THE DEPOSITION ID IS D_1292146341.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-23
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 : PETRA III, EMBL C/O DESY
REMARK 200 BEAMLINE : P14 (MX2)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97625
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : STARANISO
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72371
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.590
REMARK 200 RESOLUTION RANGE LOW (A) : 62.950
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.6
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.59
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.75
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CITRATE PH 4.0, 10% (W/V)
REMARK 280 PEG 6000, 3% (V/V) 1,6-HEXANEDIOL, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 292K
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 37.02800
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
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 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 HIS A 264
REMARK 465 HIS A 265
REMARK 465 HIS A 266
REMARK 465 HIS A 267
REMARK 465 MET B 1
REMARK 465 HIS B 262
REMARK 465 HIS B 263
REMARK 465 HIS B 264
REMARK 465 HIS B 265
REMARK 465 HIS B 266
REMARK 465 HIS B 267
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 SER A 131 -122.95 61.10
REMARK 500 HIS A 185 -88.75 -119.51
REMARK 500 THR A 256 35.61 -98.51
REMARK 500 SER B 131 -123.99 61.10
REMARK 500 HIS B 185 -89.34 -119.22
REMARK 500 THR B 256 34.05 -97.64
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 9QVA A 1 262 UNP A0AA82WPD4_9ZZZZ
DBREF2 9QVA A A0AA82WPD4 1 262
DBREF1 9QVA B 1 262 UNP A0AA82WPD4_9ZZZZ
DBREF2 9QVA B A0AA82WPD4 1 262
SEQADV 9QVA GLN A 6 UNP A0AA82WPD GLU 6 ENGINEERED MUTATION
SEQADV 9QVA ASP A 34 UNP A0AA82WPD GLN 34 ENGINEERED MUTATION
SEQADV 9QVA SER A 36 UNP A0AA82WPD ASP 36 ENGINEERED MUTATION
SEQADV 9QVA SER A 68 UNP A0AA82WPD GLU 68 ENGINEERED MUTATION
SEQADV 9QVA SER A 91 UNP A0AA82WPD THR 91 ENGINEERED MUTATION
SEQADV 9QVA LEU A 104 UNP A0AA82WPD GLN 104 ENGINEERED MUTATION
SEQADV 9QVA TYR A 109 UNP A0AA82WPD HIS 109 ENGINEERED MUTATION
SEQADV 9QVA THR A 111 UNP A0AA82WPD ARG 111 ENGINEERED MUTATION
SEQADV 9QVA ASP A 113 UNP A0AA82WPD ASN 113 ENGINEERED MUTATION
SEQADV 9QVA THR A 115 UNP A0AA82WPD VAL 115 ENGINEERED MUTATION
SEQADV 9QVA ASP A 118 UNP A0AA82WPD ASN 118 ENGINEERED MUTATION
SEQADV 9QVA SER A 131 UNP A0AA82WPD ALA 131 ENGINEERED MUTATION
SEQADV 9QVA PRO A 145 UNP A0AA82WPD THR 145 ENGINEERED MUTATION
SEQADV 9QVA LYS A 148 UNP A0AA82WPD GLU 148 ENGINEERED MUTATION
SEQADV 9QVA ASP A 161 UNP A0AA82WPD ASN 161 ENGINEERED MUTATION
SEQADV 9QVA VAL A 167 UNP A0AA82WPD THR 167 ENGINEERED MUTATION
SEQADV 9QVA ILE A 171 UNP A0AA82WPD VAL 171 ENGINEERED MUTATION
SEQADV 9QVA SER A 196 UNP A0AA82WPD ASP 196 ENGINEERED MUTATION
SEQADV 9QVA PRO A 198 UNP A0AA82WPD ASP 198 ENGINEERED MUTATION
SEQADV 9QVA ASP A 208 UNP A0AA82WPD SER 208 ENGINEERED MUTATION
SEQADV 9QVA ASN A 216 UNP A0AA82WPD ASP 216 ENGINEERED MUTATION
SEQADV 9QVA THR A 235 UNP A0AA82WPD LEU 235 ENGINEERED MUTATION
SEQADV 9QVA PRO A 248 UNP A0AA82WPD PHE 248 ENGINEERED MUTATION
SEQADV 9QVA HIS A 263 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QVA HIS A 264 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QVA HIS A 265 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QVA HIS A 266 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QVA HIS A 267 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QVA GLN B 6 UNP A0AA82WPD GLU 6 ENGINEERED MUTATION
SEQADV 9QVA ASP B 34 UNP A0AA82WPD GLN 34 ENGINEERED MUTATION
SEQADV 9QVA SER B 36 UNP A0AA82WPD ASP 36 ENGINEERED MUTATION
SEQADV 9QVA SER B 68 UNP A0AA82WPD GLU 68 ENGINEERED MUTATION
SEQADV 9QVA SER B 91 UNP A0AA82WPD THR 91 ENGINEERED MUTATION
SEQADV 9QVA LEU B 104 UNP A0AA82WPD GLN 104 ENGINEERED MUTATION
SEQADV 9QVA TYR B 109 UNP A0AA82WPD HIS 109 ENGINEERED MUTATION
SEQADV 9QVA THR B 111 UNP A0AA82WPD ARG 111 ENGINEERED MUTATION
SEQADV 9QVA ASP B 113 UNP A0AA82WPD ASN 113 ENGINEERED MUTATION
SEQADV 9QVA THR B 115 UNP A0AA82WPD VAL 115 ENGINEERED MUTATION
SEQADV 9QVA ASP B 118 UNP A0AA82WPD ASN 118 ENGINEERED MUTATION
SEQADV 9QVA SER B 131 UNP A0AA82WPD ALA 131 ENGINEERED MUTATION
SEQADV 9QVA PRO B 145 UNP A0AA82WPD THR 145 ENGINEERED MUTATION
SEQADV 9QVA LYS B 148 UNP A0AA82WPD GLU 148 ENGINEERED MUTATION
SEQADV 9QVA ASP B 161 UNP A0AA82WPD ASN 161 ENGINEERED MUTATION
SEQADV 9QVA VAL B 167 UNP A0AA82WPD THR 167 ENGINEERED MUTATION
SEQADV 9QVA ILE B 171 UNP A0AA82WPD VAL 171 ENGINEERED MUTATION
SEQADV 9QVA SER B 196 UNP A0AA82WPD ASP 196 ENGINEERED MUTATION
SEQADV 9QVA PRO B 198 UNP A0AA82WPD ASP 198 ENGINEERED MUTATION
SEQADV 9QVA ASP B 208 UNP A0AA82WPD SER 208 ENGINEERED MUTATION
SEQADV 9QVA ASN B 216 UNP A0AA82WPD ASP 216 ENGINEERED MUTATION
SEQADV 9QVA THR B 235 UNP A0AA82WPD LEU 235 ENGINEERED MUTATION
SEQADV 9QVA PRO B 248 UNP A0AA82WPD PHE 248 ENGINEERED MUTATION
SEQADV 9QVA HIS B 263 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QVA HIS B 264 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QVA HIS B 265 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QVA HIS B 266 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QVA HIS B 267 UNP A0AA82WPD EXPRESSION TAG
SEQRES 1 A 267 MET ALA ASN PRO TYR GLN ARG GLY PRO ASP PRO THR GLU
SEQRES 2 A 267 SER SER ILE GLU ALA VAL ARG GLY PRO PHE ALA VAL ALA
SEQRES 3 A 267 GLN THR THR VAL SER ARG LEU ASP ALA SER GLY PHE GLY
SEQRES 4 A 267 GLY GLY THR ILE TYR TYR PRO THR ASP THR SER GLN GLY
SEQRES 5 A 267 THR PHE GLY ALA VAL ALA ILE SER PRO GLY PHE THR ALA
SEQRES 6 A 267 GLY GLN SER SER ILE ALA TRP LEU GLY PRO ARG ILE ALA
SEQRES 7 A 267 SER GLN GLY PHE VAL VAL ILE THR ILE ASP THR ILE SER
SEQRES 8 A 267 ARG LEU ASP GLN PRO ASP SER ARG GLY ARG GLN LEU LEU
SEQRES 9 A 267 ALA ALA LEU ASP TYR LEU THR THR ASP SER THR VAL ARG
SEQRES 10 A 267 ASP ARG ILE ASP PRO ASN ARG MET ALA VAL MET GLY HIS
SEQRES 11 A 267 SER MET GLY GLY GLY GLY ALA LEU SER ALA ALA ALA ASN
SEQRES 12 A 267 ASN PRO SER LEU LYS ALA ALA ILE PRO LEU GLN GLY TRP
SEQRES 13 A 267 HIS THR ARG LYS ASP TRP SER SER VAL ARG VAL PRO THR
SEQRES 14 A 267 LEU ILE VAL GLY ALA GLN LEU ASP THR ILE ALA PRO VAL
SEQRES 15 A 267 SER SER HIS SER GLU ALA PHE TYR ASN SER LEU PRO SER
SEQRES 16 A 267 SER LEU PRO LYS ALA TYR MET GLU LEU ARG GLY ALA ASP
SEQRES 17 A 267 HIS LEU VAL SER ASN THR PRO ASN THR THR THR ALA LYS
SEQRES 18 A 267 TYR SER ILE ALA TRP LEU LYS ARG PHE VAL ASP ASP ASP
SEQRES 19 A 267 THR ARG TYR GLU GLN PHE LEU CYS PRO ALA PRO ASP ASP
SEQRES 20 A 267 PRO ALA ILE SER GLU TYR ARG SER THR CYS PRO PHE LEU
SEQRES 21 A 267 GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 267 MET ALA ASN PRO TYR GLN ARG GLY PRO ASP PRO THR GLU
SEQRES 2 B 267 SER SER ILE GLU ALA VAL ARG GLY PRO PHE ALA VAL ALA
SEQRES 3 B 267 GLN THR THR VAL SER ARG LEU ASP ALA SER GLY PHE GLY
SEQRES 4 B 267 GLY GLY THR ILE TYR TYR PRO THR ASP THR SER GLN GLY
SEQRES 5 B 267 THR PHE GLY ALA VAL ALA ILE SER PRO GLY PHE THR ALA
SEQRES 6 B 267 GLY GLN SER SER ILE ALA TRP LEU GLY PRO ARG ILE ALA
SEQRES 7 B 267 SER GLN GLY PHE VAL VAL ILE THR ILE ASP THR ILE SER
SEQRES 8 B 267 ARG LEU ASP GLN PRO ASP SER ARG GLY ARG GLN LEU LEU
SEQRES 9 B 267 ALA ALA LEU ASP TYR LEU THR THR ASP SER THR VAL ARG
SEQRES 10 B 267 ASP ARG ILE ASP PRO ASN ARG MET ALA VAL MET GLY HIS
SEQRES 11 B 267 SER MET GLY GLY GLY GLY ALA LEU SER ALA ALA ALA ASN
SEQRES 12 B 267 ASN PRO SER LEU LYS ALA ALA ILE PRO LEU GLN GLY TRP
SEQRES 13 B 267 HIS THR ARG LYS ASP TRP SER SER VAL ARG VAL PRO THR
SEQRES 14 B 267 LEU ILE VAL GLY ALA GLN LEU ASP THR ILE ALA PRO VAL
SEQRES 15 B 267 SER SER HIS SER GLU ALA PHE TYR ASN SER LEU PRO SER
SEQRES 16 B 267 SER LEU PRO LYS ALA TYR MET GLU LEU ARG GLY ALA ASP
SEQRES 17 B 267 HIS LEU VAL SER ASN THR PRO ASN THR THR THR ALA LYS
SEQRES 18 B 267 TYR SER ILE ALA TRP LEU LYS ARG PHE VAL ASP ASP ASP
SEQRES 19 B 267 THR ARG TYR GLU GLN PHE LEU CYS PRO ALA PRO ASP ASP
SEQRES 20 B 267 PRO ALA ILE SER GLU TYR ARG SER THR CYS PRO PHE LEU
SEQRES 21 B 267 GLU HIS HIS HIS HIS HIS HIS
HET CIT A 301 18
HET CIT B 301 18
HETNAM CIT CITRIC ACID
FORMUL 3 CIT 2(C6 H8 O7)
FORMUL 5 HOH *698(H2 O)
HELIX 1 AA1 THR A 12 ALA A 18 1 7
HELIX 2 AA2 GLY A 66 ALA A 71 5 6
HELIX 3 AA3 TRP A 72 SER A 79 1 8
HELIX 4 AA4 GLN A 95 ASP A 113 1 19
HELIX 5 AA5 VAL A 116 ASP A 118 5 3
HELIX 6 AA6 SER A 131 ASN A 144 1 14
HELIX 7 AA7 HIS A 185 LEU A 193 1 9
HELIX 8 AA8 LEU A 210 THR A 214 5 5
HELIX 9 AA9 ASN A 216 ASP A 232 1 17
HELIX 10 AB1 ASP A 234 ARG A 236 5 3
HELIX 11 AB2 TYR A 237 CYS A 242 1 6
HELIX 12 AB3 THR B 12 ALA B 18 1 7
HELIX 13 AB4 GLY B 66 ALA B 71 5 6
HELIX 14 AB5 TRP B 72 SER B 79 1 8
HELIX 15 AB6 GLN B 95 ASP B 113 1 19
HELIX 16 AB7 VAL B 116 ASP B 118 5 3
HELIX 17 AB8 SER B 131 ASN B 144 1 14
HELIX 18 AB9 HIS B 185 LEU B 193 1 9
HELIX 19 AC1 LEU B 210 THR B 214 5 5
HELIX 20 AC2 ASN B 216 ASP B 232 1 17
HELIX 21 AC3 ASP B 234 ARG B 236 5 3
HELIX 22 AC4 TYR B 237 CYS B 242 1 6
SHEET 1 AA1 6 VAL A 25 VAL A 30 0
SHEET 2 AA1 6 GLY A 41 PRO A 46 -1 O ILE A 43 N THR A 28
SHEET 3 AA1 6 PHE A 82 ILE A 87 -1 O VAL A 84 N TYR A 44
SHEET 4 AA1 6 PHE A 54 SER A 60 1 N VAL A 57 O VAL A 83
SHEET 5 AA1 6 ILE A 120 HIS A 130 1 O ASP A 121 N PHE A 54
SHEET 6 AA1 6 ALA A 149 LEU A 153 1 O LEU A 153 N GLY A 129
SHEET 1 AA2 3 THR A 169 ALA A 174 0
SHEET 2 AA2 3 LYS A 199 LEU A 204 1 O ALA A 200 N ILE A 171
SHEET 3 AA2 3 ILE A 250 SER A 255 -1 O ARG A 254 N TYR A 201
SHEET 1 AA3 6 VAL B 25 VAL B 30 0
SHEET 2 AA3 6 GLY B 41 PRO B 46 -1 O ILE B 43 N THR B 28
SHEET 3 AA3 6 PHE B 82 ILE B 87 -1 O VAL B 84 N TYR B 44
SHEET 4 AA3 6 PHE B 54 SER B 60 1 N VAL B 57 O VAL B 83
SHEET 5 AA3 6 ILE B 120 HIS B 130 1 O ASP B 121 N PHE B 54
SHEET 6 AA3 6 ALA B 149 LEU B 153 1 O LEU B 153 N GLY B 129
SHEET 1 AA4 3 THR B 169 ALA B 174 0
SHEET 2 AA4 3 LYS B 199 LEU B 204 1 O LEU B 204 N GLY B 173
SHEET 3 AA4 3 ILE B 250 SER B 255 -1 O ARG B 254 N TYR B 201
SSBOND 1 CYS A 242 CYS A 257 1555 1555 2.03
SSBOND 2 CYS B 242 CYS B 257 1555 1555 2.03
CISPEP 1 CYS A 242 PRO A 243 0 -1.96
CISPEP 2 CYS A 257 PRO A 258 0 -3.71
CISPEP 3 CYS B 242 PRO B 243 0 -2.55
CISPEP 4 CYS B 257 PRO B 258 0 -3.17
CRYST1 52.610 74.056 63.503 90.00 97.57 90.00 P 1 21 1 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 0.019008 0.000000 0.002526 0.00000
SCALE2 0.000000 0.013503 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015886 0.00000
MTRIX1 1 0.964990 -0.000920 0.262285 -3.11122 1
MTRIX2 1 -0.001727 -0.999994 0.002848 17.59721 1
MTRIX3 1 0.262281 -0.003202 -0.964986 24.73915 1
TER 4076 HIS A 263
TER 8108 GLU B 261
MASTER 290 0 2 22 18 0 0 9 4670 2 40 42
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