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HEADER HYDROLASE 17-APR-25 9QYB
TITLE POLYESTER HYDROLASE LEIPZIG 7 (PHL7) VARIANT R4M10
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYESTER HYDROLASE LEIPZIG 7 (PHL7) VARIANT R4M10;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 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 9QYB 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. 1.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.21.2_5419: ???)
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) : 1.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.74
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 107657
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.153
REMARK 3 R VALUE (WORKING SET) : 0.153
REMARK 3 FREE R VALUE : 0.170
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.010
REMARK 3 FREE R VALUE TEST SET COUNT : 2162
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 38.7400 - 2.7100 1.00 7562 144 0.1491 0.1758
REMARK 3 2 2.7100 - 2.1500 1.00 7196 142 0.1385 0.1342
REMARK 3 3 2.1500 - 1.8800 1.00 7114 132 0.1303 0.1599
REMARK 3 4 1.8800 - 1.7100 1.00 7056 157 0.1354 0.1614
REMARK 3 5 1.7100 - 1.5900 1.00 7040 127 0.1346 0.1441
REMARK 3 6 1.5900 - 1.4900 1.00 7006 152 0.1342 0.1450
REMARK 3 7 1.4900 - 1.4200 1.00 6999 144 0.1471 0.1635
REMARK 3 8 1.4200 - 1.3600 1.00 6974 154 0.1636 0.1880
REMARK 3 9 1.3600 - 1.3000 1.00 6929 154 0.1704 0.1833
REMARK 3 10 1.3000 - 1.2600 1.00 6946 138 0.1768 0.1898
REMARK 3 11 1.2600 - 1.2200 1.00 6946 147 0.1982 0.2213
REMARK 3 12 1.2200 - 1.1800 1.00 6920 165 0.2079 0.2088
REMARK 3 13 1.1800 - 1.1500 1.00 6923 145 0.2191 0.2427
REMARK 3 14 1.1500 - 1.1300 1.00 6955 126 0.2386 0.2449
REMARK 3 15 1.1300 - 1.1000 1.00 6929 135 0.2606 0.2553
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) : 0.100
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.090
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.89
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 : 0.013 NULL
REMARK 3 ANGLE : 1.187 NULL
REMARK 3 CHIRALITY : 0.096 319
REMARK 3 PLANARITY : 0.016 392
REMARK 3 DIHEDRAL : 12.306 778
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -5.4234 26.7721 -5.1447
REMARK 3 T TENSOR
REMARK 3 T11: 0.0910 T22: 0.0647
REMARK 3 T33: 0.0721 T12: -0.0110
REMARK 3 T13: 0.0269 T23: -0.0101
REMARK 3 L TENSOR
REMARK 3 L11: 0.7144 L22: 0.7153
REMARK 3 L33: 1.2366 L12: 0.1049
REMARK 3 L13: 0.1265 L23: -0.1307
REMARK 3 S TENSOR
REMARK 3 S11: 0.0458 S12: -0.0081 S13: 0.0559
REMARK 3 S21: 0.0714 S22: 0.0075 S23: -0.0039
REMARK 3 S31: -0.1329 S32: 0.0618 S33: -0.0365
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 9QYB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-APR-25.
REMARK 100 THE DEPOSITION ID IS D_1292147200.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-DEC-24
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) : 0.72930
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 : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 107770
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.100
REMARK 200 RESOLUTION RANGE LOW (A) : 69.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 40.00
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.12
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 (%): 45.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.1 M SODIUM MALONATE, 0.1 M HEPES PH
REMARK 280 7.0, 0.5% (V/V) JEFFAMINE ED-2003, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 46.01400
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 92.02800
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 69.02100
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 115.03500
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 23.00700
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 46.01400
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 92.02800
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 115.03500
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 69.02100
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 23.00700
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 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 CL CL A 302 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 HIS A 260
REMARK 465 HIS A 261
REMARK 465 HIS A 262
REMARK 465 HIS A 263
REMARK 465 HIS A 264
REMARK 465 HIS A 265
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 -11.22 74.40
REMARK 500 SER A 131 -126.28 64.71
REMARK 500 HIS A 185 -101.45 -125.66
REMARK 500 PRO A 243 -176.20 -66.09
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 0.11 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 9QYB A 2 265 PDB 9QYB 9QYB 2 265
SEQRES 1 A 264 ALA ASN PRO TYR GLN ARG GLY PRO ASP PRO THR GLU SER
SEQRES 2 A 264 SER ILE GLU ALA VAL ARG GLY PRO PHE ALA VAL ALA GLN
SEQRES 3 A 264 THR THR VAL SER ARG LEU ASP ALA SER GLY PHE GLY GLY
SEQRES 4 A 264 GLY THR ILE TYR TYR PRO THR ASP THR SER GLN GLY THR
SEQRES 5 A 264 PHE GLY ALA VAL ALA ILE SER PRO GLY PHE THR ALA GLY
SEQRES 6 A 264 GLN SER SER ILE ALA TRP LEU GLY PRO ARG ILE ALA SER
SEQRES 7 A 264 GLN GLY PHE VAL VAL ILE THR ILE ASP THR ILE SER ARG
SEQRES 8 A 264 PHE ASP TYR PRO ASP SER ARG GLY ARG GLN LEU GLN ALA
SEQRES 9 A 264 ALA LEU ASP TYR LEU THR THR ASP SER THR VAL ARG ASP
SEQRES 10 A 264 ARG ILE ASP PRO ASN ARG MET ALA VAL MET GLY HIS SER
SEQRES 11 A 264 MET GLY GLY GLY GLY ALA LEU SER ALA ALA ALA ASN ASN
SEQRES 12 A 264 PRO SER LEU LYS ALA ALA ILE PRO LEU GLN GLY TRP HIS
SEQRES 13 A 264 THR ARG LYS ASP TRP SER SER VAL ARG VAL PRO THR LEU
SEQRES 14 A 264 ILE VAL GLY ALA GLU LEU ASP THR ILE ALA PRO VAL SER
SEQRES 15 A 264 SER HIS SER GLU ALA PHE TYR ASN SER LEU PRO SER SER
SEQRES 16 A 264 LEU PRO LYS ALA TYR MET GLU LEU ARG GLY ALA SER HIS
SEQRES 17 A 264 THR VAL SER ASN THR PRO ASN THR THR THR ALA LYS TYR
SEQRES 18 A 264 SER ILE ALA TRP LEU LYS ARG PHE VAL ASP ASP ASP THR
SEQRES 19 A 264 ARG TYR GLU GLN PHE LEU CYS PRO ALA PRO ASP ASP PRO
SEQRES 20 A 264 ALA ILE SER GLU TYR ARG SER THR CYS PRO PHE HIS HIS
SEQRES 21 A 264 HIS HIS HIS HIS
HET CL A 301 1
HET CL A 302 1
HETNAM CL CHLORIDE ION
FORMUL 2 CL 2(CL 1-)
FORMUL 4 HOH *294(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 TYR 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 SER A 208 THR A 214 5 7
HELIX 9 AA9 ASN A 216 ASP A 232 1 17
HELIX 10 AB1 ASP A 234 LEU A 241 5 8
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 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
SSBOND 1 CYS A 242 CYS A 257 1555 1555 2.04
CISPEP 1 CYS A 242 PRO A 243 0 -9.65
CISPEP 2 CYS A 257 PRO A 258 0 4.04
CRYST1 80.717 80.717 138.042 90.00 90.00 120.00 P 61 2 2 12
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 0.012389 0.007153 0.000000 0.00000
SCALE2 0.000000 0.014306 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007244 0.00000
TER 4044 PHE A 259
MASTER 307 0 2 10 9 0 0 6 2246 1 2 21
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