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HEADER HYDROLASE 10-FEB-23 8IBL
TITLE MES BOUND FORM OF PET-DEGRADING CUTINASE CUT190 WITH THERMOSTABILITY-
TITLE 2 IMPROVING MUTATIONS OF S226P/R228S/Q138A/D250C-E296C/Q123H/N202H AND
TITLE 3 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
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 8IBL 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. 2.60 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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.36
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.980
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 15664
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950
REMARK 3 FREE R VALUE TEST SET COUNT : 775
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 32.3600 - 4.7200 1.00 2464 145 0.1916 0.2211
REMARK 3 2 4.7200 - 3.7500 1.00 2508 122 0.1776 0.2323
REMARK 3 3 3.7500 - 3.2700 1.00 2478 138 0.2199 0.2820
REMARK 3 4 3.2700 - 2.9800 1.00 2478 126 0.2181 0.3081
REMARK 3 5 2.9700 - 2.7600 1.00 2489 122 0.2514 0.3398
REMARK 3 6 2.7600 - 2.6000 1.00 2472 122 0.2891 0.2979
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) : 0.391
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.296
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.34
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.35
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 : 0.003 4200
REMARK 3 ANGLE : 0.556 5722
REMARK 3 CHIRALITY : 0.043 614
REMARK 3 PLANARITY : 0.006 748
REMARK 3 DIHEDRAL : 14.513 1548
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 8IBL 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_1300035367.
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 : 15681
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 33.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.27600
REMARK 200 FOR THE DATA SET : 5.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.61
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.76
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) : 1.22000
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 (%): 45.92
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: 90 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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: 90 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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 -118.73 60.34
REMARK 500 THR A 199 54.50 39.17
REMARK 500 LEU A 221 32.68 -99.40
REMARK 500 HIS A 230 -77.38 -119.70
REMARK 500 THR A 301 38.93 -96.55
REMARK 500 ALA B 176 -116.24 59.06
REMARK 500 HIS B 230 -79.37 -124.66
REMARK 500 THR B 301 34.75 -89.40
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 88.1
REMARK 620 3 PHE A 81 O 86.6 77.0
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 115.6
REMARK 620 3 PHE B 81 O 102.5 73.4
REMARK 620 N 1 2
DBREF 8IBL A 47 304 UNP W0TJ64 W0TJ64_9PSEU 47 304
DBREF 8IBL B 47 304 UNP W0TJ64 W0TJ64_9PSEU 47 304
SEQADV 8IBL GLY A 45 UNP W0TJ64 EXPRESSION TAG
SEQADV 8IBL PRO A 46 UNP W0TJ64 EXPRESSION TAG
SEQADV 8IBL HIS A 123 UNP W0TJ64 GLN 123 ENGINEERED MUTATION
SEQADV 8IBL ALA A 138 UNP W0TJ64 GLN 138 ENGINEERED MUTATION
SEQADV 8IBL ALA A 176 UNP W0TJ64 SER 176 ENGINEERED MUTATION
SEQADV 8IBL HIS A 202 UNP W0TJ64 ASN 202 ENGINEERED MUTATION
SEQADV 8IBL PRO A 226 UNP W0TJ64 SER 226 ENGINEERED MUTATION
SEQADV 8IBL SER A 228 UNP W0TJ64 ARG 228 ENGINEERED MUTATION
SEQADV 8IBL CYS A 250 UNP W0TJ64 ASP 250 ENGINEERED MUTATION
SEQADV 8IBL CYS A 296 UNP W0TJ64 GLU 296 ENGINEERED MUTATION
SEQADV 8IBL LYS A 305 UNP W0TJ64 EXPRESSION TAG
SEQADV 8IBL LEU A 306 UNP W0TJ64 EXPRESSION TAG
SEQADV 8IBL ASN A 307 UNP W0TJ64 EXPRESSION TAG
SEQADV 8IBL GLY B 45 UNP W0TJ64 EXPRESSION TAG
SEQADV 8IBL PRO B 46 UNP W0TJ64 EXPRESSION TAG
SEQADV 8IBL HIS B 123 UNP W0TJ64 GLN 123 ENGINEERED MUTATION
SEQADV 8IBL ALA B 138 UNP W0TJ64 GLN 138 ENGINEERED MUTATION
SEQADV 8IBL ALA B 176 UNP W0TJ64 SER 176 ENGINEERED MUTATION
SEQADV 8IBL HIS B 202 UNP W0TJ64 ASN 202 ENGINEERED MUTATION
SEQADV 8IBL PRO B 226 UNP W0TJ64 SER 226 ENGINEERED MUTATION
SEQADV 8IBL SER B 228 UNP W0TJ64 ARG 228 ENGINEERED MUTATION
SEQADV 8IBL CYS B 250 UNP W0TJ64 ASP 250 ENGINEERED MUTATION
SEQADV 8IBL CYS B 296 UNP W0TJ64 GLU 296 ENGINEERED MUTATION
SEQADV 8IBL LYS B 305 UNP W0TJ64 EXPRESSION TAG
SEQADV 8IBL LEU B 306 UNP W0TJ64 EXPRESSION TAG
SEQADV 8IBL 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 MES A 402 12
HET CL A 403 1
HET CA B 401 1
HET MES B 402 12
HET CL B 403 1
HETNAM CA CALCIUM ION
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM CL CHLORIDE ION
FORMUL 3 CA 2(CA 2+)
FORMUL 4 MES 2(C6 H13 N O4 S)
FORMUL 5 CL 2(CL 1-)
FORMUL 9 HOH *61(H2 O)
HELIX 1 AA1 SER A 109 MET A 113 5 5
HELIX 2 AA2 SER A 114 SER A 122 1 9
HELIX 3 AA3 ALA A 138 ARG A 156 1 19
HELIX 4 AA4 ASP A 158 GLU A 163 1 6
HELIX 5 AA5 ALA A 176 ARG A 189 1 14
HELIX 6 AA6 HIS A 230 LEU A 238 1 9
HELIX 7 AA7 PHE A 255 ILE A 259 5 5
HELIX 8 AA8 ASN A 261 ASP A 277 1 17
HELIX 9 AA9 ASP A 279 ARG A 281 5 3
HELIX 10 AB1 TYR A 282 CYS A 287 1 6
HELIX 11 AB2 THR B 56 ALA B 62 1 7
HELIX 12 AB3 SER B 109 SER B 112 5 4
HELIX 13 AB4 MET B 113 SER B 122 1 10
HELIX 14 AB5 ALA B 138 ARG B 156 1 19
HELIX 15 AB6 ASP B 158 GLU B 163 1 6
HELIX 16 AB7 ALA B 176 ARG B 189 1 14
HELIX 17 AB8 HIS B 230 LEU B 238 1 9
HELIX 18 AB9 PHE B 255 ILE B 259 5 5
HELIX 19 AC1 ASN B 261 ASP B 277 1 17
HELIX 20 AC2 ASP B 279 ARG B 281 5 3
HELIX 21 AC3 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 GLY A 84 N VAL A 74
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 MET B 247 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 2.04
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 2.38
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 2.39
LINK O PHE B 81 CA CA B 401 1555 1555 2.47
CISPEP 1 CYS A 287 PRO A 288 0 -2.11
CISPEP 2 CYS A 302 PRO A 303 0 -3.59
CISPEP 3 CYS B 287 PRO B 288 0 -0.58
CISPEP 4 CYS B 302 PRO B 303 0 -1.50
CRYST1 83.869 83.869 64.723 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 0.011923 0.006884 0.000000 0.00000
SCALE2 0.000000 0.013768 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015450 0.00000
TER 2032 ASN A 307
TER 4064 ASN B 307
MASTER 260 0 6 21 18 0 0 6 4151 2 40 42
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