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HEADER HYDROLASE 16-JUL-25 9PM1
TITLE CRYSTAL STRUCTURE OF AN ENGINEERED PETASE, EV2, DERIVED FROM
TITLE 2 THERMOBIFIDA FUSCA CUTINASE (TFCUT2)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(ETHYLENE TEREPHTHALATE) HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.101;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOBIFIDA FUSCA;
SOURCE 3 ORGANISM_TAXID: 2021;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_VARIANT: C41
KEYWDS PETASE, EVOLUTION-INFORMED DESIGN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.I.MATHEWS,B.NORTON-BAKER,O.O.STORMENT,J.E.MCGEEHAN,G.T.BECKHAM,
AUTHOR 2 N.P.GAUTHIER
REVDAT 1 22-JUL-26 9PM1 0
JRNL AUTH B.NORTON-BAKER
JRNL TITL ITERATIVE COMPUTATIONAL AND RATIONAL DESIGN GENERATES
JRNL TITL 2 HUNDREDS OF DIVERSE AND ACTIVE PLASTIC-DEPOLYMERIZING
JRNL TITL 3 ENZYMES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.08 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) : 1.08
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.71
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.1
REMARK 3 NUMBER OF REFLECTIONS : 178115
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.137
REMARK 3 R VALUE (WORKING SET) : 0.136
REMARK 3 FREE R VALUE : 0.159
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 8907
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 37.7100 - 3.3500 0.99 6297 332 0.1312 0.1475
REMARK 3 2 3.3500 - 2.6600 0.98 6185 326 0.1469 0.1649
REMARK 3 3 2.6600 - 2.3300 0.98 6195 326 0.1475 0.1723
REMARK 3 4 2.3300 - 2.1100 0.97 6140 323 0.1379 0.1469
REMARK 3 5 2.1100 - 1.9600 0.97 6174 325 0.1371 0.1595
REMARK 3 6 1.9600 - 1.8500 0.97 6077 319 0.1405 0.1605
REMARK 3 7 1.8500 - 1.7500 0.96 6099 321 0.1416 0.1699
REMARK 3 8 1.7500 - 1.6800 0.96 6043 319 0.1373 0.1625
REMARK 3 9 1.6800 - 1.6100 0.95 6041 317 0.1268 0.1564
REMARK 3 10 1.6100 - 1.5600 0.95 6011 317 0.1204 0.1407
REMARK 3 11 1.5600 - 1.5100 0.95 5940 313 0.1172 0.1346
REMARK 3 12 1.5100 - 1.4700 0.94 5956 313 0.1168 0.1440
REMARK 3 13 1.4700 - 1.4300 0.94 6003 316 0.1159 0.1686
REMARK 3 14 1.4300 - 1.3900 0.93 5903 311 0.1233 0.1409
REMARK 3 15 1.3900 - 1.3600 0.93 5864 308 0.1242 0.1426
REMARK 3 16 1.3600 - 1.3300 0.93 5859 309 0.1205 0.1546
REMARK 3 17 1.3300 - 1.3100 0.93 5923 312 0.1199 0.1528
REMARK 3 18 1.3100 - 1.2800 0.92 5809 305 0.1220 0.1415
REMARK 3 19 1.2800 - 1.2600 0.92 5836 308 0.1211 0.1710
REMARK 3 20 1.2600 - 1.2400 0.91 5758 303 0.1220 0.1655
REMARK 3 21 1.2400 - 1.2200 0.87 5463 287 0.1274 0.1689
REMARK 3 22 1.2200 - 1.2000 0.85 5449 287 0.1275 0.1737
REMARK 3 23 1.2000 - 1.1800 0.83 5171 272 0.1317 0.1607
REMARK 3 24 1.1800 - 1.1600 0.81 5138 271 0.1448 0.1499
REMARK 3 25 1.1600 - 1.1500 0.78 4943 260 0.1485 0.1805
REMARK 3 26 1.1500 - 1.1300 0.77 4873 256 0.1552 0.1814
REMARK 3 27 1.1300 - 1.1200 0.75 4678 247 0.1612 0.2074
REMARK 3 28 1.1200 - 1.1100 0.72 4649 244 0.1743 0.2055
REMARK 3 29 1.1100 - 1.0900 0.71 4459 235 0.1892 0.2061
REMARK 3 30 1.0900 - 1.0800 0.68 4272 225 0.1918 0.2041
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) : 0.080
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.440
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 : 0.012 4308
REMARK 3 ANGLE : 1.266 5930
REMARK 3 CHIRALITY : 0.108 664
REMARK 3 PLANARITY : 0.016 787
REMARK 3 DIHEDRAL : 16.325 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 9PM1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUL-25.
REMARK 100 THE DEPOSITION ID IS D_1000294703.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAY-24
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97946
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : RH COATED COLLIMATING MIRRORS, K
REMARK 200 -B FOCUSING MIRRORS
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 : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 178134
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.080
REMARK 200 RESOLUTION RANGE LOW (A) : 37.710
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.2
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.9400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.08
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.11
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.69200
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM ACETATE, 0.1 M MES (4.6),
REMARK 280 20% PEG 8K, PH 4.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 CYS B 253 CA - CB - SG ANGL. DEV. = 8.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 61 -9.72 78.01
REMARK 500 THR A 61 -9.72 79.21
REMARK 500 SER A 130 -118.42 66.11
REMARK 500 THR A 153 54.83 35.99
REMARK 500 HIS A 184 -87.35 -124.16
REMARK 500 THR A 258 31.19 -98.78
REMARK 500 THR B 61 -7.65 75.58
REMARK 500 THR B 61 -7.65 77.74
REMARK 500 SER B 130 -117.95 64.79
REMARK 500 THR B 153 57.64 35.63
REMARK 500 HIS B 184 -87.05 -123.37
REMARK 500 PHE B 249 10.02 59.98
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 96 0.09 SIDE CHAIN
REMARK 500 ARG B 96 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 743 DISTANCE = 7.08 ANGSTROMS
DBREF 9PM1 A 1 261 PDB 9PM1 9PM1 1 261
DBREF 9PM1 B 1 261 PDB 9PM1 9PM1 1 261
SEQRES 1 A 261 ALA ASN PRO TYR GLU ARG GLY PRO ASN PRO THR ASP ALA
SEQRES 2 A 261 LEU LEU GLU ALA THR ARG GLY PRO PHE SER VAL SER THR
SEQRES 3 A 261 THR SER VAL SER ARG LEU SER VAL SER GLY PHE GLY GLY
SEQRES 4 A 261 GLY THR ILE TYR TYR PRO THR THR THR GLY THR PHE GLY
SEQRES 5 A 261 ALA VAL ALA ILE SER PRO GLY TYR THR ALA THR GLN SER
SEQRES 6 A 261 SER ILE ALA TRP LEU GLY PRO ARG LEU ALA SER HIS GLY
SEQRES 7 A 261 PHE VAL VAL ILE THR ILE ASP THR ASN THR THR LEU ASP
SEQRES 8 A 261 GLY PRO ASP SER ARG GLY ARG GLN LEU LEU ALA ALA LEU
SEQRES 9 A 261 ASP TYR LEU VAL ASN ARG ALA SER SER SER VAL ARG SER
SEQRES 10 A 261 ARG ILE ASP ALA SER ARG LEU ALA VAL MET GLY HIS SER
SEQRES 11 A 261 MET GLY GLY GLY GLY THR LEU ARG ALA ALA SER ASP ARG
SEQRES 12 A 261 PRO GLU LEU LYS ALA ALA ILE PRO LEU THR PRO TRP HIS
SEQRES 13 A 261 LEU ASP LYS THR TRP SER SER VAL ARG VAL PRO THR LEU
SEQRES 14 A 261 ILE ILE GLY ALA GLU ASN ASP THR ILE ALA PRO VAL ALA
SEQRES 15 A 261 THR HIS ALA GLU PRO PHE TYR ASN SER LEU PRO SER SER
SEQRES 16 A 261 LEU GLU LYS ALA TYR LEU GLU LEU CYS GLY ALA THR HIS
SEQRES 17 A 261 ILE ALA PRO ASN LEU PRO ASN THR THR ILE GLY LYS TYR
SEQRES 18 A 261 SER VAL SER TRP LEU LYS ARG PHE VAL ASP ASN ASP THR
SEQRES 19 A 261 ARG TYR THR GLN PHE LEU CYS PRO GLY PRO ARG ASP GLY
SEQRES 20 A 261 LEU PHE GLY GLU VAL CYS GLU TYR ARG SER THR CYS PRO
SEQRES 21 A 261 PHE
SEQRES 1 B 261 ALA ASN PRO TYR GLU ARG GLY PRO ASN PRO THR ASP ALA
SEQRES 2 B 261 LEU LEU GLU ALA THR ARG GLY PRO PHE SER VAL SER THR
SEQRES 3 B 261 THR SER VAL SER ARG LEU SER VAL SER GLY PHE GLY GLY
SEQRES 4 B 261 GLY THR ILE TYR TYR PRO THR THR THR GLY THR PHE GLY
SEQRES 5 B 261 ALA VAL ALA ILE SER PRO GLY TYR THR ALA THR GLN SER
SEQRES 6 B 261 SER ILE ALA TRP LEU GLY PRO ARG LEU ALA SER HIS GLY
SEQRES 7 B 261 PHE VAL VAL ILE THR ILE ASP THR ASN THR THR LEU ASP
SEQRES 8 B 261 GLY PRO ASP SER ARG GLY ARG GLN LEU LEU ALA ALA LEU
SEQRES 9 B 261 ASP TYR LEU VAL ASN ARG ALA SER SER SER VAL ARG SER
SEQRES 10 B 261 ARG ILE ASP ALA SER ARG LEU ALA VAL MET GLY HIS SER
SEQRES 11 B 261 MET GLY GLY GLY GLY THR LEU ARG ALA ALA SER ASP ARG
SEQRES 12 B 261 PRO GLU LEU LYS ALA ALA ILE PRO LEU THR PRO TRP HIS
SEQRES 13 B 261 LEU ASP LYS THR TRP SER SER VAL ARG VAL PRO THR LEU
SEQRES 14 B 261 ILE ILE GLY ALA GLU ASN ASP THR ILE ALA PRO VAL ALA
SEQRES 15 B 261 THR HIS ALA GLU PRO PHE TYR ASN SER LEU PRO SER SER
SEQRES 16 B 261 LEU GLU LYS ALA TYR LEU GLU LEU CYS GLY ALA THR HIS
SEQRES 17 B 261 ILE ALA PRO ASN LEU PRO ASN THR THR ILE GLY LYS TYR
SEQRES 18 B 261 SER VAL SER TRP LEU LYS ARG PHE VAL ASP ASN ASP THR
SEQRES 19 B 261 ARG TYR THR GLN PHE LEU CYS PRO GLY PRO ARG ASP GLY
SEQRES 20 B 261 LEU PHE GLY GLU VAL CYS GLU TYR ARG SER THR CYS PRO
SEQRES 21 B 261 PHE
HET ACT A 301 4
HET EDO A 302 4
HET ACT B 301 4
HET CL B 302 1
HETNAM ACT ACETATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CL CHLORIDE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 ACT 2(C2 H3 O2 1-)
FORMUL 4 EDO C2 H6 O2
FORMUL 6 CL CL 1-
FORMUL 7 HOH *675(H2 O)
HELIX 1 AA1 THR A 11 ALA A 17 1 7
HELIX 2 AA2 SER A 30 VAL A 34 5 5
HELIX 3 AA3 THR A 63 ALA A 68 5 6
HELIX 4 AA4 TRP A 69 SER A 76 1 8
HELIX 5 AA5 GLY A 92 ARG A 110 1 19
HELIX 6 AA6 SER A 112 SER A 117 1 6
HELIX 7 AA7 SER A 130 ARG A 143 1 14
HELIX 8 AA8 HIS A 184 LEU A 192 1 9
HELIX 9 AA9 ILE A 209 LEU A 213 5 5
HELIX 10 AB1 ASN A 215 ASP A 231 1 17
HELIX 11 AB2 ASP A 233 ARG A 235 5 3
HELIX 12 AB3 TYR A 236 CYS A 241 1 6
HELIX 13 AB4 GLY A 247 GLY A 250 5 4
HELIX 14 AB5 THR B 11 ALA B 17 1 7
HELIX 15 AB6 SER B 30 VAL B 34 5 5
HELIX 16 AB7 THR B 63 ALA B 68 5 6
HELIX 17 AB8 TRP B 69 SER B 76 1 8
HELIX 18 AB9 GLY B 92 ARG B 110 1 19
HELIX 19 AC1 SER B 112 SER B 117 1 6
HELIX 20 AC2 SER B 130 ARG B 143 1 14
HELIX 21 AC3 HIS B 184 LEU B 192 1 9
HELIX 22 AC4 ILE B 209 LEU B 213 5 5
HELIX 23 AC5 ASN B 215 ASP B 231 1 17
HELIX 24 AC6 ASP B 233 ARG B 235 5 3
HELIX 25 AC7 TYR B 236 CYS B 241 1 6
HELIX 26 AC8 GLY B 247 GLY B 250 5 4
SHEET 1 AA1 6 VAL A 24 VAL A 29 0
SHEET 2 AA1 6 GLY A 40 PRO A 45 -1 O GLY A 40 N VAL A 29
SHEET 3 AA1 6 VAL A 80 ILE A 84 -1 O VAL A 81 N TYR A 43
SHEET 4 AA1 6 PHE A 51 SER A 57 1 N VAL A 54 O ILE A 82
SHEET 5 AA1 6 ILE A 119 HIS A 129 1 O ASP A 120 N PHE A 51
SHEET 6 AA1 6 ALA A 148 LEU A 152 1 O LEU A 152 N GLY A 128
SHEET 1 AA2 3 THR A 168 ALA A 173 0
SHEET 2 AA2 3 LYS A 198 LEU A 203 1 O LEU A 203 N GLY A 172
SHEET 3 AA2 3 VAL A 252 SER A 257 -1 O CYS A 253 N GLU A 202
SHEET 1 AA3 6 VAL B 24 VAL B 29 0
SHEET 2 AA3 6 GLY B 40 PRO B 45 -1 O ILE B 42 N THR B 27
SHEET 3 AA3 6 PHE B 79 ILE B 84 -1 O VAL B 81 N TYR B 43
SHEET 4 AA3 6 PHE B 51 SER B 57 1 N VAL B 54 O VAL B 80
SHEET 5 AA3 6 ILE B 119 HIS B 129 1 O ASP B 120 N PHE B 51
SHEET 6 AA3 6 ALA B 148 LEU B 152 1 O LEU B 152 N GLY B 128
SHEET 1 AA4 3 THR B 168 ALA B 173 0
SHEET 2 AA4 3 LYS B 198 LEU B 203 1 O LEU B 203 N GLY B 172
SHEET 3 AA4 3 VAL B 252 SER B 257 -1 O CYS B 253 N GLU B 202
SSBOND 1 CYS A 241 CYS A 259 1555 1555 2.10
SSBOND 2 CYS B 241 CYS B 259 1555 1555 2.09
CISPEP 1 CYS A 241 PRO A 242 0 5.83
CISPEP 2 CYS A 259 PRO A 260 0 5.23
CISPEP 3 CYS B 241 PRO B 242 0 6.04
CISPEP 4 CYS B 259 PRO B 260 0 5.60
CRYST1 42.370 42.380 69.180 97.96 91.60 101.94 P 1 2
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 0.023602 0.004993 0.001413 0.00000
SCALE2 0.000000 0.024118 0.003598 0.00000
SCALE3 0.000000 0.000000 0.014621 0.00000
TER 2078 PHE A 261
TER 4165 PHE B 261
MASTER 291 0 4 26 18 0 0 6 4623 2 16 42
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