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HEADER HYDROLASE 25-MAR-25 9QNM
TITLE POLYESTER HYDROLASE LEIPZIG 7 (PHL7) VARIANT R2M2
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
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 9QNM 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. 1.12 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) : 1.12
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 63.10
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 53.6
REMARK 3 NUMBER OF REFLECTIONS : 99522
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.570
REMARK 3 FREE R VALUE TEST SET COUNT : 5041
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 63.1000 - 3.4700 1.00 11850 301 0.1596 0.1976
REMARK 3 2 3.4700 - 2.7600 0.99 11713 335 0.1566 0.1887
REMARK 3 3 2.7600 - 2.4100 1.00 11853 342 0.1590 0.1837
REMARK 3 4 2.4100 - 2.1900 0.81 9649 256 0.1446 0.1770
REMARK 3 5 2.1900 - 2.0300 0.91 10883 286 0.1467 0.1820
REMARK 3 6 2.0300 - 1.9100 0.89 10534 251 0.1467 0.1766
REMARK 3 7 1.9100 - 1.8200 0.99 11675 330 0.1674 0.2038
REMARK 3 8 1.8200 - 1.7400 0.98 11687 301 0.1843 0.2276
REMARK 3 9 1.7400 - 1.6700 0.94 11147 257 0.1936 0.2035
REMARK 3 10 1.6700 - 1.6100 0.88 10434 271 0.1907 0.2035
REMARK 3 11 1.6100 - 1.5600 0.81 9593 258 0.2023 0.2307
REMARK 3 12 1.5600 - 1.5200 0.73 8666 224 0.2060 0.2388
REMARK 3 13 1.5200 - 1.4800 0.66 7868 215 0.2120 0.2488
REMARK 3 14 1.4800 - 1.4400 0.60 7123 215 0.2202 0.2387
REMARK 3 15 1.4400 - 1.4100 0.54 6397 163 0.2211 0.2448
REMARK 3 16 1.4100 - 1.3800 0.48 5715 175 0.2272 0.2386
REMARK 3 17 1.3800 - 1.3500 0.43 5163 145 0.2394 0.2325
REMARK 3 18 1.3500 - 1.3300 0.39 4637 134 0.2448 0.2440
REMARK 3 19 1.3300 - 1.3000 0.36 4289 111 0.2388 0.2423
REMARK 3 20 1.3000 - 1.2800 0.33 3907 106 0.2541 0.2677
REMARK 3 21 1.2800 - 1.2600 0.29 3436 90 0.2538 0.2791
REMARK 3 22 1.2600 - 1.2400 0.25 2980 70 0.2494 0.3421
REMARK 3 23 1.2400 - 1.2200 0.21 2534 50 0.2500 0.3703
REMARK 3 24 1.2200 - 1.2000 0.17 2053 50 0.2596 0.2532
REMARK 3 25 1.2000 - 1.1900 0.14 1643 31 0.2660 0.2997
REMARK 3 26 1.1900 - 1.1700 0.11 1319 30 0.2529 0.2167
REMARK 3 27 1.1700 - 1.1600 0.09 1016 24 0.2555 0.2620
REMARK 3 28 1.1600 - 1.1400 0.06 674 12 0.2708 0.3456
REMARK 3 29 1.1400 - 1.1300 0.03 400 0 0.3187 0.0000
REMARK 3 30 1.1300 - 1.1200 0.00 203 8 0.2901 0.5621
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) : 0.120
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.010
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.010 NULL
REMARK 3 ANGLE : 1.025 NULL
REMARK 3 CHIRALITY : 0.083 651
REMARK 3 PLANARITY : 0.013 775
REMARK 3 DIHEDRAL : 11.445 1561
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 9QNM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-MAR-25.
REMARK 100 THE DEPOSITION ID IS D_1292146151.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JUL-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 : P13 (MX1)
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 : 99522
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.120
REMARK 200 RESOLUTION RANGE LOW (A) : 63.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.8
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.12
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.24
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
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
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 37.04800
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 THR A 64 -2.80 69.25
REMARK 500 SER A 131 -119.60 58.78
REMARK 500 HIS A 185 -100.82 -116.18
REMARK 500 THR B 64 -3.85 71.49
REMARK 500 SER B 131 -121.05 58.19
REMARK 500 HIS B 185 -99.45 -116.72
REMARK 500 THR B 256 31.27 -98.42
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 99 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 9QNM A 1 262 UNP A0AA82WPD4_9ZZZZ
DBREF2 9QNM A A0AA82WPD4 1 262
DBREF1 9QNM B 1 262 UNP A0AA82WPD4_9ZZZZ
DBREF2 9QNM B A0AA82WPD4 1 262
SEQADV 9QNM GLN A 6 UNP A0AA82WPD GLU 6 ENGINEERED MUTATION
SEQADV 9QNM ASP A 34 UNP A0AA82WPD GLN 34 ENGINEERED MUTATION
SEQADV 9QNM SER A 36 UNP A0AA82WPD ASP 36 ENGINEERED MUTATION
SEQADV 9QNM SER A 68 UNP A0AA82WPD GLU 68 ENGINEERED MUTATION
SEQADV 9QNM SER A 91 UNP A0AA82WPD THR 91 ENGINEERED MUTATION
SEQADV 9QNM LEU A 104 UNP A0AA82WPD GLN 104 ENGINEERED MUTATION
SEQADV 9QNM TYR A 109 UNP A0AA82WPD HIS 109 ENGINEERED MUTATION
SEQADV 9QNM THR A 111 UNP A0AA82WPD ARG 111 ENGINEERED MUTATION
SEQADV 9QNM ASP A 113 UNP A0AA82WPD ASN 113 ENGINEERED MUTATION
SEQADV 9QNM THR A 115 UNP A0AA82WPD VAL 115 ENGINEERED MUTATION
SEQADV 9QNM ASP A 118 UNP A0AA82WPD ASN 118 ENGINEERED MUTATION
SEQADV 9QNM SER A 131 UNP A0AA82WPD ALA 131 ENGINEERED MUTATION
SEQADV 9QNM PRO A 145 UNP A0AA82WPD THR 145 ENGINEERED MUTATION
SEQADV 9QNM LYS A 148 UNP A0AA82WPD GLU 148 ENGINEERED MUTATION
SEQADV 9QNM PRO A 155 UNP A0AA82WPD GLY 155 ENGINEERED MUTATION
SEQADV 9QNM ASP A 161 UNP A0AA82WPD ASN 161 ENGINEERED MUTATION
SEQADV 9QNM VAL A 167 UNP A0AA82WPD THR 167 ENGINEERED MUTATION
SEQADV 9QNM ILE A 171 UNP A0AA82WPD VAL 171 ENGINEERED MUTATION
SEQADV 9QNM ALA A 186 UNP A0AA82WPD SER 186 ENGINEERED MUTATION
SEQADV 9QNM SER A 196 UNP A0AA82WPD ASP 196 ENGINEERED MUTATION
SEQADV 9QNM PRO A 198 UNP A0AA82WPD ASP 198 ENGINEERED MUTATION
SEQADV 9QNM ASP A 208 UNP A0AA82WPD SER 208 ENGINEERED MUTATION
SEQADV 9QNM ASN A 216 UNP A0AA82WPD ASP 216 ENGINEERED MUTATION
SEQADV 9QNM THR A 235 UNP A0AA82WPD LEU 235 ENGINEERED MUTATION
SEQADV 9QNM PRO A 248 UNP A0AA82WPD PHE 248 ENGINEERED MUTATION
SEQADV 9QNM HIS A 263 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QNM HIS A 264 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QNM HIS A 265 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QNM HIS A 266 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QNM HIS A 267 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QNM GLN B 6 UNP A0AA82WPD GLU 6 ENGINEERED MUTATION
SEQADV 9QNM ASP B 34 UNP A0AA82WPD GLN 34 ENGINEERED MUTATION
SEQADV 9QNM SER B 36 UNP A0AA82WPD ASP 36 ENGINEERED MUTATION
SEQADV 9QNM SER B 68 UNP A0AA82WPD GLU 68 ENGINEERED MUTATION
SEQADV 9QNM SER B 91 UNP A0AA82WPD THR 91 ENGINEERED MUTATION
SEQADV 9QNM LEU B 104 UNP A0AA82WPD GLN 104 ENGINEERED MUTATION
SEQADV 9QNM TYR B 109 UNP A0AA82WPD HIS 109 ENGINEERED MUTATION
SEQADV 9QNM THR B 111 UNP A0AA82WPD ARG 111 ENGINEERED MUTATION
SEQADV 9QNM ASP B 113 UNP A0AA82WPD ASN 113 ENGINEERED MUTATION
SEQADV 9QNM THR B 115 UNP A0AA82WPD VAL 115 ENGINEERED MUTATION
SEQADV 9QNM ASP B 118 UNP A0AA82WPD ASN 118 ENGINEERED MUTATION
SEQADV 9QNM SER B 131 UNP A0AA82WPD ALA 131 ENGINEERED MUTATION
SEQADV 9QNM PRO B 145 UNP A0AA82WPD THR 145 ENGINEERED MUTATION
SEQADV 9QNM LYS B 148 UNP A0AA82WPD GLU 148 ENGINEERED MUTATION
SEQADV 9QNM PRO B 155 UNP A0AA82WPD GLY 155 ENGINEERED MUTATION
SEQADV 9QNM ASP B 161 UNP A0AA82WPD ASN 161 ENGINEERED MUTATION
SEQADV 9QNM VAL B 167 UNP A0AA82WPD THR 167 ENGINEERED MUTATION
SEQADV 9QNM ILE B 171 UNP A0AA82WPD VAL 171 ENGINEERED MUTATION
SEQADV 9QNM ALA B 186 UNP A0AA82WPD SER 186 ENGINEERED MUTATION
SEQADV 9QNM SER B 196 UNP A0AA82WPD ASP 196 ENGINEERED MUTATION
SEQADV 9QNM PRO B 198 UNP A0AA82WPD ASP 198 ENGINEERED MUTATION
SEQADV 9QNM ASP B 208 UNP A0AA82WPD SER 208 ENGINEERED MUTATION
SEQADV 9QNM ASN B 216 UNP A0AA82WPD ASP 216 ENGINEERED MUTATION
SEQADV 9QNM THR B 235 UNP A0AA82WPD LEU 235 ENGINEERED MUTATION
SEQADV 9QNM PRO B 248 UNP A0AA82WPD PHE 248 ENGINEERED MUTATION
SEQADV 9QNM HIS B 263 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QNM HIS B 264 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QNM HIS B 265 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QNM HIS B 266 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QNM 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 PRO 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 ALA 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 PRO 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 ALA 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 *757(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 SER B 31 ALA B 35 5 5
HELIX 14 AB5 GLY B 66 ALA B 71 5 6
HELIX 15 AB6 TRP B 72 SER B 79 1 8
HELIX 16 AB7 GLN B 95 ASP B 113 1 19
HELIX 17 AB8 VAL B 116 ASP B 118 5 3
HELIX 18 AB9 SER B 131 ASN B 144 1 14
HELIX 19 AC1 HIS B 185 LEU B 193 1 9
HELIX 20 AC2 LEU B 210 THR B 214 5 5
HELIX 21 AC3 ASN B 216 ASP B 232 1 17
HELIX 22 AC4 ASP B 234 ARG B 236 5 3
HELIX 23 AC5 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 VAL A 83 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 ILE A 85
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 LEU A 204 N GLY A 173
SHEET 3 AA2 3 ILE A 250 SER A 255 -1 O GLU A 252 N GLU A 203
SHEET 1 AA3 6 VAL B 25 VAL B 30 0
SHEET 2 AA3 6 GLY B 41 PRO B 46 -1 O TYR B 45 N ALA B 26
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 ILE B 85
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 2.05
SSBOND 2 CYS B 242 CYS B 257 1555 1555 2.05
CISPEP 1 CYS A 242 PRO A 243 0 -3.27
CISPEP 2 CYS A 257 PRO A 258 0 -0.89
CISPEP 3 CYS B 242 PRO B 243 0 -4.42
CISPEP 4 CYS B 257 PRO B 258 0 -2.16
CRYST1 52.260 74.096 63.596 90.00 97.14 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 0.019135 0.000000 0.002397 0.00000
SCALE2 0.000000 0.013496 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015847 0.00000
TER 4034 HIS A 263
TER 8067 GLU B 261
MASTER 275 0 2 23 18 0 0 6 4733 2 40 42
END |