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HEADER HYDROLASE 17-APR-25 9QYA
TITLE POLYESTER HYDROLASE LEIPZIG 7 (PHL7) VARIANT R4M6
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYESTER HYDROLASE LEIPZIG 7 (PHL7) VARIANT R4M6;
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 9QYA 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. 1.53 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.20.1)
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) : 1.53
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 62.13
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 67.7
REMARK 3 NUMBER OF REFLECTIONS : 27313
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.160
REMARK 3 R VALUE (WORKING SET) : 0.157
REMARK 3 FREE R VALUE : 0.195
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.870
REMARK 3 FREE R VALUE TEST SET COUNT : 1876
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 62.1300 - 3.6000 1.00 3158 236 0.1554 0.1927
REMARK 3 2 3.6000 - 2.8600 1.00 2977 206 0.1471 0.1803
REMARK 3 3 2.8600 - 2.5000 1.00 2940 198 0.1494 0.1815
REMARK 3 4 2.5000 - 2.2700 1.00 2898 222 0.1329 0.1956
REMARK 3 5 2.2700 - 2.1100 1.00 2865 211 0.1428 0.1671
REMARK 3 6 2.1100 - 1.9800 1.00 2870 215 0.1636 0.2059
REMARK 3 7 1.9800 - 1.8800 0.99 2822 208 0.1939 0.2209
REMARK 3 8 1.8800 - 1.8000 0.76 2186 166 0.2074 0.2466
REMARK 3 9 1.8000 - 1.7300 0.41 1146 101 0.2326 0.2790
REMARK 3 10 1.7300 - 1.6700 0.28 790 55 0.2483 0.2824
REMARK 3 11 1.6700 - 1.6200 0.18 496 46 0.2437 0.2486
REMARK 3 12 1.6200 - 1.5700 0.08 235 11 0.2722 0.3475
REMARK 3 13 1.5700 - 1.5300 0.02 54 1 0.2409 0.3135
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) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.970
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 : 0.004 NULL
REMARK 3 ANGLE : 0.726 NULL
REMARK 3 CHIRALITY : 0.047 313
REMARK 3 PLANARITY : 0.010 373
REMARK 3 DIHEDRAL : 12.103 743
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): -5.4514 26.8088 -4.7353
REMARK 3 T TENSOR
REMARK 3 T11: 0.1224 T22: 0.1055
REMARK 3 T33: 0.1144 T12: -0.0051
REMARK 3 T13: 0.0183 T23: -0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 0.5044 L22: 0.5518
REMARK 3 L33: 0.9497 L12: 0.1234
REMARK 3 L13: 0.0641 L23: -0.1018
REMARK 3 S TENSOR
REMARK 3 S11: 0.0313 S12: -0.0050 S13: 0.0366
REMARK 3 S21: 0.0571 S22: -0.0010 S23: -0.0061
REMARK 3 S31: -0.1235 S32: 0.0299 S33: 0.0002
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 9QYA 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_1292147188.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-MAY-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 : P14 (MX2)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97626
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 : 27315
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.530
REMARK 200 RESOLUTION RANGE LOW (A) : 62.130
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : 38.40
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.53
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.71
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 (%): 46.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
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 45.93933
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 91.87867
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 68.90900
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 114.84833
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 22.96967
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 45.93933
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 91.87867
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 114.84833
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 68.90900
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 22.96967
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 MET A 1
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 -0.48 68.69
REMARK 500 SER A 131 -128.65 62.33
REMARK 500 HIS A 185 -96.90 -125.85
REMARK 500 THR A 256 32.77 -99.14
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
DBREF 9QYA A 1 259 PDB 9QYA 9QYA 1 259
SEQRES 1 A 259 MET ALA ASN PRO TYR GLN ARG GLY PRO ASP PRO THR GLU
SEQRES 2 A 259 SER SER ILE GLU ALA VAL ARG GLY PRO PHE ALA VAL ALA
SEQRES 3 A 259 GLN THR THR VAL SER ARG LEU ASP ALA SER GLY PHE GLY
SEQRES 4 A 259 GLY GLY THR ILE TYR TYR PRO THR ASP THR SER GLN GLY
SEQRES 5 A 259 THR PHE GLY ALA VAL ALA ILE SER PRO GLY PHE THR ALA
SEQRES 6 A 259 GLY GLN SER SER ILE ALA TRP LEU GLY PRO ARG ILE ALA
SEQRES 7 A 259 SER GLN GLY PHE VAL VAL ILE THR ILE ASP THR ILE SER
SEQRES 8 A 259 ARG LEU ASP GLN PRO ASP SER ARG GLY ARG GLN LEU GLN
SEQRES 9 A 259 ALA ALA LEU ASP TYR LEU THR THR ASP SER THR VAL ARG
SEQRES 10 A 259 ASP ARG ILE ASP PRO ASN ARG MET ALA VAL MET GLY HIS
SEQRES 11 A 259 SER MET GLY GLY GLY GLY ALA LEU SER ALA ALA ALA ASN
SEQRES 12 A 259 ASN PRO SER LEU LYS ALA ALA ILE PRO LEU GLN GLY TRP
SEQRES 13 A 259 HIS THR ARG LYS ASP TRP SER SER VAL ARG VAL PRO THR
SEQRES 14 A 259 LEU ILE VAL GLY ALA GLU LEU ASP THR ILE ALA PRO VAL
SEQRES 15 A 259 SER SER HIS SER GLU ALA PHE TYR ASN SER LEU PRO SER
SEQRES 16 A 259 SER LEU PRO LYS ALA TYR MET GLU LEU ARG GLY ALA SER
SEQRES 17 A 259 HIS THR VAL SER ASN THR PRO ASN THR THR THR ALA LYS
SEQRES 18 A 259 TYR SER ILE ALA TRP LEU LYS ARG PHE VAL ASP ASP ASP
SEQRES 19 A 259 THR ARG TYR GLU GLN PHE LEU CYS PRO ALA PRO ASP ASP
SEQRES 20 A 259 PRO ALA ILE SER GLU TYR ARG SER THR CYS PRO PHE
HET CL A 301 1
HET CL A 302 1
HETNAM CL CHLORIDE ION
FORMUL 2 CL 2(CL 1-)
FORMUL 4 HOH *273(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 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 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 GLU A 252 N GLU A 203
SSBOND 1 CYS A 242 CYS A 257 1555 1555 2.03
CISPEP 1 CYS A 242 PRO A 243 0 -4.67
CISPEP 2 CYS A 257 PRO A 258 0 0.20
CRYST1 80.375 80.375 137.818 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 0.012442 0.007183 0.000000 0.00000
SCALE2 0.000000 0.014366 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007256 0.00000
TER 3913 PHE A 259
MASTER 300 0 2 10 9 0 0 6 2219 1 2 20
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