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HEADER HYDROLASE 10-FEB-23 8IBM
TITLE SULFATE BOUND FORM OF PET-DEGRADING CUTINASE CUT190 WITH
TITLE 2 THERMOSTABILITY-IMPROVING MUTATIONS OF S226P/R228S/Q138A/D250C-
TITLE 3 E296C/Q123H/N202H AND S176A INACTIVATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE FAMILY PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CUTINASE;
COMPND 5 EC: 3.1.1.74;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMONOSPORA VIRIDIS;
SOURCE 3 ORGANISM_TAXID: 1852;
SOURCE 4 GENE: CUT190, SAMN02982918_2340;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ROSETTA-GAMI B(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PQE80L
KEYWDS PROTEIN ENGINEERING, POLYESTERASE, DISULFIDE BOND, METAL BINDING,
KEYWDS 2 LIGAND COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.EMORI,N.NUMOTO,N.KAMIYA,M.ODA
REVDAT 1 15-MAR-23 8IBM 0
JRNL AUTH N.NUMOTO,N.KAMIYA,M.ODA
JRNL TITL IMPROVEMENT OF THERMOSTABILITY AND ACTIVITY OF PET-DEGRADING
JRNL TITL 2 ENZYME CUT190 TOWARDS A DETAILED UNDERSTANDING AND
JRNL TITL 3 APPLICATION OF THE ENZYMATIC REACTION MECHANISM.
JRNL REF BIORXIV 2023
JRNL REFN ISSN 2692-8205
JRNL DOI 10.1101/2023.02.26.529345
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19.2_4158
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.27
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 25592
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.235
REMARK 3 R VALUE (WORKING SET) : 0.234
REMARK 3 FREE R VALUE : 0.267
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960
REMARK 3 FREE R VALUE TEST SET COUNT : 1270
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 36.2700 - 4.5800 1.00 2701 158 0.1919 0.2133
REMARK 3 2 4.5700 - 3.6300 0.99 2701 136 0.1924 0.2371
REMARK 3 3 3.6300 - 3.1700 1.00 2724 146 0.2349 0.2887
REMARK 3 4 3.1700 - 2.8800 1.00 2701 134 0.2559 0.2660
REMARK 3 5 2.8800 - 2.6800 1.00 2753 142 0.2731 0.3377
REMARK 3 6 2.6800 - 2.5200 0.99 2667 142 0.2930 0.3083
REMARK 3 7 2.5200 - 2.3900 0.99 2692 149 0.2735 0.3251
REMARK 3 8 2.3900 - 2.2900 0.99 2706 136 0.3195 0.3564
REMARK 3 9 2.2900 - 2.2000 0.98 2677 127 0.3689 0.3642
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
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) : 0.338
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 38.290
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.44
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.01
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 4184
REMARK 3 ANGLE : 0.478 5702
REMARK 3 CHIRALITY : 0.042 614
REMARK 3 PLANARITY : 0.005 748
REMARK 3 DIHEDRAL : 11.760 1530
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 8IBM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-FEB-23.
REMARK 100 THE DEPOSITION ID IS D_1300035369.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-MAR-21
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-17A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
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 : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25685
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 37.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.12500
REMARK 200 FOR THE DATA SET : 10.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 1.46000
REMARK 200 FOR SHELL : 1.400
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 (%): 45.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES MONOHYDRATE PH 6.5, 0.2 M
REMARK 280 AMMONIUM SULFATE, AND 30% (W/V) PEG MME 5,000, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,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 -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 0.00000
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL
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 GLY A 45
REMARK 465 GLY B 45
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 ALA A 176 -116.47 60.89
REMARK 500 THR A 199 57.14 38.81
REMARK 500 HIS A 230 -78.27 -125.15
REMARK 500 ALA B 176 -116.33 60.30
REMARK 500 THR B 199 56.25 39.52
REMARK 500 HIS B 230 -79.06 -129.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 76 O
REMARK 620 2 ALA A 78 O 102.6
REMARK 620 3 PHE A 81 O 95.9 75.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 76 O
REMARK 620 2 ALA B 78 O 100.6
REMARK 620 3 PHE B 81 O 90.6 73.1
REMARK 620 N 1 2
DBREF 8IBM A 47 304 UNP W0TJ64 W0TJ64_9PSEU 47 304
DBREF 8IBM B 47 304 UNP W0TJ64 W0TJ64_9PSEU 47 304
SEQADV 8IBM GLY A 45 UNP W0TJ64 EXPRESSION TAG
SEQADV 8IBM PRO A 46 UNP W0TJ64 EXPRESSION TAG
SEQADV 8IBM HIS A 123 UNP W0TJ64 GLN 123 ENGINEERED MUTATION
SEQADV 8IBM ALA A 138 UNP W0TJ64 GLN 138 ENGINEERED MUTATION
SEQADV 8IBM ALA A 176 UNP W0TJ64 SER 176 ENGINEERED MUTATION
SEQADV 8IBM HIS A 202 UNP W0TJ64 ASN 202 ENGINEERED MUTATION
SEQADV 8IBM PRO A 226 UNP W0TJ64 SER 226 ENGINEERED MUTATION
SEQADV 8IBM SER A 228 UNP W0TJ64 ARG 228 ENGINEERED MUTATION
SEQADV 8IBM CYS A 250 UNP W0TJ64 ASP 250 ENGINEERED MUTATION
SEQADV 8IBM CYS A 296 UNP W0TJ64 GLU 296 ENGINEERED MUTATION
SEQADV 8IBM LYS A 305 UNP W0TJ64 EXPRESSION TAG
SEQADV 8IBM LEU A 306 UNP W0TJ64 EXPRESSION TAG
SEQADV 8IBM ASN A 307 UNP W0TJ64 EXPRESSION TAG
SEQADV 8IBM GLY B 45 UNP W0TJ64 EXPRESSION TAG
SEQADV 8IBM PRO B 46 UNP W0TJ64 EXPRESSION TAG
SEQADV 8IBM HIS B 123 UNP W0TJ64 GLN 123 ENGINEERED MUTATION
SEQADV 8IBM ALA B 138 UNP W0TJ64 GLN 138 ENGINEERED MUTATION
SEQADV 8IBM ALA B 176 UNP W0TJ64 SER 176 ENGINEERED MUTATION
SEQADV 8IBM HIS B 202 UNP W0TJ64 ASN 202 ENGINEERED MUTATION
SEQADV 8IBM PRO B 226 UNP W0TJ64 SER 226 ENGINEERED MUTATION
SEQADV 8IBM SER B 228 UNP W0TJ64 ARG 228 ENGINEERED MUTATION
SEQADV 8IBM CYS B 250 UNP W0TJ64 ASP 250 ENGINEERED MUTATION
SEQADV 8IBM CYS B 296 UNP W0TJ64 GLU 296 ENGINEERED MUTATION
SEQADV 8IBM LYS B 305 UNP W0TJ64 EXPRESSION TAG
SEQADV 8IBM LEU B 306 UNP W0TJ64 EXPRESSION TAG
SEQADV 8IBM ASN B 307 UNP W0TJ64 EXPRESSION TAG
SEQRES 1 A 263 GLY PRO ASN PRO TYR GLU ARG GLY PRO ASP PRO THR GLU
SEQRES 2 A 263 ASP SER ILE GLU ALA ILE ARG GLY PRO PHE SER VAL ALA
SEQRES 3 A 263 THR GLU ARG VAL SER SER PHE ALA SER GLY PHE GLY GLY
SEQRES 4 A 263 GLY THR ILE TYR TYR PRO ARG GLU THR ASP GLU GLY THR
SEQRES 5 A 263 PHE GLY ALA VAL ALA VAL ALA PRO GLY PHE THR ALA SER
SEQRES 6 A 263 GLN GLY SER MET SER TRP TYR GLY GLU ARG VAL ALA SER
SEQRES 7 A 263 HIS GLY PHE ILE VAL PHE THR ILE ASP THR ASN THR ARG
SEQRES 8 A 263 LEU ASP ALA PRO GLY GLN ARG GLY ARG GLN LEU LEU ALA
SEQRES 9 A 263 ALA LEU ASP TYR LEU VAL GLU ARG SER ASP ARG LYS VAL
SEQRES 10 A 263 ARG GLU ARG LEU ASP PRO ASN ARG LEU ALA VAL MET GLY
SEQRES 11 A 263 HIS ALA MET GLY GLY GLY GLY SER LEU GLU ALA THR VAL
SEQRES 12 A 263 MET ARG PRO SER LEU LYS ALA SER ILE PRO LEU THR PRO
SEQRES 13 A 263 TRP HIS LEU ASP LYS THR TRP GLY GLN VAL GLN VAL PRO
SEQRES 14 A 263 THR PHE ILE ILE GLY ALA GLU LEU ASP THR ILE ALA PRO
SEQRES 15 A 263 VAL SER THR HIS ALA LYS PRO PHE TYR GLU SER LEU PRO
SEQRES 16 A 263 SER SER LEU PRO LYS ALA TYR MET GLU LEU CYS GLY ALA
SEQRES 17 A 263 THR HIS PHE ALA PRO ASN ILE PRO ASN THR THR ILE ALA
SEQRES 18 A 263 LYS TYR VAL ILE SER TRP LEU LYS ARG PHE VAL ASP GLU
SEQRES 19 A 263 ASP THR ARG TYR SER GLN PHE LEU CYS PRO ASN PRO THR
SEQRES 20 A 263 ASP ARG ALA ILE CYS GLU TYR ARG SER THR CYS PRO TYR
SEQRES 21 A 263 LYS LEU ASN
SEQRES 1 B 263 GLY PRO ASN PRO TYR GLU ARG GLY PRO ASP PRO THR GLU
SEQRES 2 B 263 ASP SER ILE GLU ALA ILE ARG GLY PRO PHE SER VAL ALA
SEQRES 3 B 263 THR GLU ARG VAL SER SER PHE ALA SER GLY PHE GLY GLY
SEQRES 4 B 263 GLY THR ILE TYR TYR PRO ARG GLU THR ASP GLU GLY THR
SEQRES 5 B 263 PHE GLY ALA VAL ALA VAL ALA PRO GLY PHE THR ALA SER
SEQRES 6 B 263 GLN GLY SER MET SER TRP TYR GLY GLU ARG VAL ALA SER
SEQRES 7 B 263 HIS GLY PHE ILE VAL PHE THR ILE ASP THR ASN THR ARG
SEQRES 8 B 263 LEU ASP ALA PRO GLY GLN ARG GLY ARG GLN LEU LEU ALA
SEQRES 9 B 263 ALA LEU ASP TYR LEU VAL GLU ARG SER ASP ARG LYS VAL
SEQRES 10 B 263 ARG GLU ARG LEU ASP PRO ASN ARG LEU ALA VAL MET GLY
SEQRES 11 B 263 HIS ALA MET GLY GLY GLY GLY SER LEU GLU ALA THR VAL
SEQRES 12 B 263 MET ARG PRO SER LEU LYS ALA SER ILE PRO LEU THR PRO
SEQRES 13 B 263 TRP HIS LEU ASP LYS THR TRP GLY GLN VAL GLN VAL PRO
SEQRES 14 B 263 THR PHE ILE ILE GLY ALA GLU LEU ASP THR ILE ALA PRO
SEQRES 15 B 263 VAL SER THR HIS ALA LYS PRO PHE TYR GLU SER LEU PRO
SEQRES 16 B 263 SER SER LEU PRO LYS ALA TYR MET GLU LEU CYS GLY ALA
SEQRES 17 B 263 THR HIS PHE ALA PRO ASN ILE PRO ASN THR THR ILE ALA
SEQRES 18 B 263 LYS TYR VAL ILE SER TRP LEU LYS ARG PHE VAL ASP GLU
SEQRES 19 B 263 ASP THR ARG TYR SER GLN PHE LEU CYS PRO ASN PRO THR
SEQRES 20 B 263 ASP ARG ALA ILE CYS GLU TYR ARG SER THR CYS PRO TYR
SEQRES 21 B 263 LYS LEU ASN
HET CA A 401 1
HET SO4 A 402 5
HET CA B 401 1
HET SO4 B 402 5
HETNAM CA CALCIUM ION
HETNAM SO4 SULFATE ION
FORMUL 3 CA 2(CA 2+)
FORMUL 4 SO4 2(O4 S 2-)
FORMUL 7 HOH *61(H2 O)
HELIX 1 AA1 THR A 56 ALA A 62 1 7
HELIX 2 AA2 SER A 109 MET A 113 5 5
HELIX 3 AA3 SER A 114 SER A 122 1 9
HELIX 4 AA4 ALA A 138 ARG A 156 1 19
HELIX 5 AA5 ASP A 158 GLU A 163 1 6
HELIX 6 AA6 ALA A 176 ARG A 189 1 14
HELIX 7 AA7 HIS A 230 LEU A 238 1 9
HELIX 8 AA8 PHE A 255 ILE A 259 5 5
HELIX 9 AA9 ASN A 261 ASP A 277 1 17
HELIX 10 AB1 ASP A 279 ARG A 281 5 3
HELIX 11 AB2 TYR A 282 CYS A 287 1 6
HELIX 12 AB3 THR B 56 ALA B 62 1 7
HELIX 13 AB4 SER B 109 SER B 114 5 6
HELIX 14 AB5 TRP B 115 SER B 122 1 8
HELIX 15 AB6 ALA B 138 ARG B 156 1 19
HELIX 16 AB7 ASP B 158 GLU B 163 1 6
HELIX 17 AB8 ALA B 176 ARG B 189 1 14
HELIX 18 AB9 HIS B 230 LEU B 238 1 9
HELIX 19 AC1 PHE B 255 ILE B 259 5 5
HELIX 20 AC2 ASN B 261 ASP B 277 1 17
HELIX 21 AC3 ASP B 279 ARG B 281 5 3
HELIX 22 AC4 TYR B 282 CYS B 287 1 6
SHEET 1 AA1 6 VAL A 69 VAL A 74 0
SHEET 2 AA1 6 GLY A 84 PRO A 89 -1 O ILE A 86 N GLU A 72
SHEET 3 AA1 6 ILE A 126 ILE A 130 -1 O VAL A 127 N TYR A 87
SHEET 4 AA1 6 PHE A 97 ALA A 103 1 N VAL A 102 O PHE A 128
SHEET 5 AA1 6 LEU A 165 HIS A 175 1 O MET A 173 N ALA A 103
SHEET 6 AA1 6 ALA A 194 LEU A 198 1 O LEU A 198 N GLY A 174
SHEET 1 AA2 3 THR A 214 ALA A 219 0
SHEET 2 AA2 3 LYS A 244 LEU A 249 1 O MET A 247 N GLY A 218
SHEET 3 AA2 3 ILE A 295 SER A 300 -1 O CYS A 296 N GLU A 248
SHEET 1 AA3 6 VAL B 69 VAL B 74 0
SHEET 2 AA3 6 GLY B 84 PRO B 89 -1 O GLY B 84 N VAL B 74
SHEET 3 AA3 6 ILE B 126 ILE B 130 -1 O VAL B 127 N TYR B 87
SHEET 4 AA3 6 PHE B 97 ALA B 103 1 N VAL B 100 O ILE B 126
SHEET 5 AA3 6 LEU B 165 HIS B 175 1 O ASP B 166 N PHE B 97
SHEET 6 AA3 6 ALA B 194 LEU B 198 1 O LEU B 198 N GLY B 174
SHEET 1 AA4 3 THR B 214 ALA B 219 0
SHEET 2 AA4 3 LYS B 244 LEU B 249 1 O LEU B 249 N GLY B 218
SHEET 3 AA4 3 ILE B 295 SER B 300 -1 O CYS B 296 N GLU B 248
SSBOND 1 CYS A 250 CYS A 296 1555 1555 2.03
SSBOND 2 CYS A 287 CYS A 302 1555 1555 2.03
SSBOND 3 CYS B 250 CYS B 296 1555 1555 2.03
SSBOND 4 CYS B 287 CYS B 302 1555 1555 2.03
LINK O SER A 76 CA CA A 401 1555 1555 2.37
LINK O ALA A 78 CA CA A 401 1555 1555 2.33
LINK O PHE A 81 CA CA A 401 1555 1555 2.36
LINK O SER B 76 CA CA B 401 1555 1555 2.40
LINK O ALA B 78 CA CA B 401 1555 1555 2.31
LINK O PHE B 81 CA CA B 401 1555 1555 2.46
CISPEP 1 CYS A 287 PRO A 288 0 -0.55
CISPEP 2 CYS A 302 PRO A 303 0 0.16
CISPEP 3 CYS B 287 PRO B 288 0 -0.83
CISPEP 4 CYS B 302 PRO B 303 0 0.43
CRYST1 83.755 83.755 64.752 90.00 90.00 120.00 P 3 6
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 0.011940 0.006893 0.000000 0.00000
SCALE2 0.000000 0.013787 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015444 0.00000
TER 2032 ASN A 307
TER 4064 ASN B 307
MASTER 261 0 4 22 18 0 0 6 4135 2 26 42
END |