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HEADER HYDROLASE 06-JUL-01 1JJI
TITLE THE CRYSTAL STRUCTURE OF A HYPER-THERMOPHILIC
TITLE 2 CARBOXYLESTERASE FROM THE ARCHAEON ARCHAEOGLOBUS FULGIDUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLESTERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS;
SOURCE 3 ORGANISM_COMMON: ARCHAEA;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PT7-7SCII
KEYWDS ALPHA-BETA HYDROLASE FOLD
EXPDTA X-RAY DIFFRACTION
AUTHOR G.DE SIMONE,V.MENCHISE,G.MANCO,L.MANDRICH,N.SORRENTINO,
AUTHOR 2 D.LANG,M.ROSSI,C.PEDONE
REVDAT 1 05-DEC-01 1JJI 0
JRNL AUTH G.DE SIMONE,V.MENCHISE,G.MANCO,L.MANDRICH,
JRNL AUTH 2 N.SORRENTINO,D.LANG,M.ROSSI,C.PEDONE
JRNL TITL THE CRYSTAL STRUCTURE OF A HYPER-THERMOPHILIC
JRNL TITL 2 CARBOXYLESTERASE FROM THE ARCHAEON ARCHAEOGLOBUS
JRNL TITL 3 FULGIDUS.
JRNL REF J.MOL.BIOL. V. 314 507 2001
JRNL REFN ASTM JMOBAK UK ISSN 0022-2836
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.MANCO,E.GIOSUE,S.D'AURIA,P.HERMAN,G.CARREA,
REMARK 1 AUTH 2 M.ROSSI
REMARK 1 TITL CLONING, OVEREXPRESSION AND PROPERTIES OF A NEW
REMARK 1 TITL 2 THERMOPHILIC AND TERMOSTABLE ESTERASE WITH
REMARK 1 TITL 3 SEQUENCE SIMILARITY TO HORMONE-SENSITIVE LIPASE
REMARK 1 TITL 4 SUBFAMILY FROM THE ARCHAEON ARCHAEOGLOBUS FULGIDUS
REMARK 1 REF ARCH.BIOCHEM.BIOPHYS. V. 373 182 2000
REMARK 1 REFN ASTM ABBIA4 US ISSN 0003-9861
REMARK 1 REFERENCE 2
REMARK 1 AUTH G.DE SIMONE,S.GALDIERO,G.MANCO,D.LANG,M.ROSSI,
REMARK 1 AUTH 2 C.PEDONE
REMARK 1 TITL A SNAPSHOT OF THE TRANSITION STATE OF A NOVEL
REMARK 1 TITL 2 THERMOPHILIC ESTERASE BELONGING TO THE SUBFAMILY
REMARK 1 TITL 3 OF MAMMALIAN HORMONE-SENSITIVE LIPASE
REMARK 1 REF J.MOL.BIOL. V. 303 761 2000
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 83680
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4177
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10032
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 56
REMARK 3 SOLVENT ATOMS : 561
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.45
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JJI COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUL-2001.
REMARK 100 THE RCSB ID CODE IS RCSB013845.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-OCT-2000
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ELETTRA
REMARK 200 BEAMLINE : X-RD
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 84834
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 21.7000
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) : 2.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.36000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.940
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1EVQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.5
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, MAGNESIUM ACETATE, HEPES
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,2/3+Z
REMARK 290 3555 -X+Y,-X,1/3+Z
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,2/3+Z
REMARK 290 6555 X-Y,X,1/3+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 69.69600
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 34.84800
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 0.00000
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 69.69600
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 34.84800
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 4 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMOLECULE: 3
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMOLECULE: 4
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI
REMARK 500 O PHE C 223 O HOH 438 2.19
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 MET A 4 CE MET A 4 SD -0.104
REMARK 500 MET A 172 CE MET A 172 SD -0.080
REMARK 500 GLU A 260 CG GLU A 260 CB -0.098
REMARK 500 MET A 267 CE MET A 267 SD 0.116
REMARK 500 MET B 1 CE MET B 1 SD -0.094
REMARK 500 PRO C 245 CG PRO C 245 CB 0.078
REMARK 500 PRO D 77 CG PRO D 77 CB 0.087
REMARK 500 MET D 215 CE MET D 215 SD -0.098
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 2 N - CA - C ANGL. DEV. = -9.7 DEGREES
REMARK 500 ASP A 3 N - CA - C ANGL. DEV. =-11.8 DEGREES
REMARK 500 MET A 4 N - CA - C ANGL. DEV. = 10.3 DEGREES
REMARK 500 MET A 4 C - N - CA ANGL. DEV. =-11.8 DEGREES
REMARK 500 VAL A 81 CB - CA - C ANGL. DEV. =-10.5 DEGREES
REMARK 500 PRO A 189 CB - CG - CD ANGL. DEV. = -8.9 DEGREES
REMARK 500 VAL A 190 N - CA - C ANGL. DEV. =-10.4 DEGREES
REMARK 500 LEU A 284 CA - CB - CG ANGL. DEV. = 8.6 DEGREES
REMARK 500 LEU B 2 CA - CB - CG ANGL. DEV. =-12.8 DEGREES
REMARK 500 VAL B 81 CB - CA - C ANGL. DEV. =-11.3 DEGREES
REMARK 500 PRO B 127 C - N - CA ANGL. DEV. = 9.4 DEGREES
REMARK 500 SER B 160 CA - CB - OG ANGL. DEV. = 9.8 DEGREES
REMARK 500 VAL B 190 N - CA - C ANGL. DEV. = -9.9 DEGREES
REMARK 500 PRO B 232 C - N - CA ANGL. DEV. = -8.7 DEGREES
REMARK 500 LEU B 248 N - CA - C ANGL. DEV. = -9.1 DEGREES
REMARK 500 ASP B 311 C - N - CA ANGL. DEV. = 9.5 DEGREES
REMARK 500 PRO C 127 C - N - CA ANGL. DEV. = 12.1 DEGREES
REMARK 500 GLN C 184 CB - CA - C ANGL. DEV. = -8.6 DEGREES
REMARK 500 VAL C 190 N - CA - C ANGL. DEV. =-10.1 DEGREES
REMARK 500 LEU C 248 N - CA - C ANGL. DEV. = -8.7 DEGREES
REMARK 500 VAL D 81 CB - CA - C ANGL. DEV. = -8.6 DEGREES
REMARK 500 PRO D 127 C - N - CA ANGL. DEV. = 12.3 DEGREES
REMARK 500 LEU D 284 CA - CB - CG ANGL. DEV. = 8.7 DEGREES
REMARK 500 PRO D 292 C - N - CA ANGL. DEV. = -9.6 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 SER A 160 -117.96 63.78
REMARK 500 ILE A 209 -57.25 69.88
REMARK 500 SER B 160 -118.95 61.98
REMARK 500 ILE B 209 -105.77 54.08
REMARK 500 SER C 160 -119.35 60.21
REMARK 500 ILE C 209 -85.75 91.02
REMARK 500 ILE D 209 -83.18 73.83
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 SER160 IN EACH MONOMER IS COVALENTLY BOUND TO A
REMARK 600 HEPES MOLECULE.
DBREF 1JJI A 1 311 PIR 7448882 C69464 1 311
DBREF 1JJI B 1 311 PIR 7448882 C69464 1 311
DBREF 1JJI C 1 311 PIR 7448882 C69464 1 311
DBREF 1JJI D 1 311 PIR 7448882 C69464 1 311
SEQRES 1 A 311 MET LEU ASP MET PRO ILE ASP PRO VAL TYR TYR GLN LEU
SEQRES 2 A 311 ALA GLU TYR PHE ASP SER LEU PRO LYS PHE ASP GLN PHE
SEQRES 3 A 311 SER SER ALA ARG GLU TYR ARG GLU ALA ILE ASN ARG ILE
SEQRES 4 A 311 TYR GLU GLU ARG ASN ARG GLN LEU SER GLN HIS GLU ARG
SEQRES 5 A 311 VAL GLU ARG VAL GLU ASP ARG THR ILE LYS GLY ARG ASN
SEQRES 6 A 311 GLY ASP ILE ARG VAL ARG VAL TYR GLN GLN LYS PRO ASP
SEQRES 7 A 311 SER PRO VAL LEU VAL TYR TYR HIS GLY GLY GLY PHE VAL
SEQRES 8 A 311 ILE CYS SER ILE GLU SER HIS ASP ALA LEU CYS ARG ARG
SEQRES 9 A 311 ILE ALA ARG LEU SER ASN SER THR VAL VAL SER VAL ASP
SEQRES 10 A 311 TYR ARG LEU ALA PRO GLU HIS LYS PHE PRO ALA ALA VAL
SEQRES 11 A 311 TYR ASP CYS TYR ASP ALA THR LYS TRP VAL ALA GLU ASN
SEQRES 12 A 311 ALA GLU GLU LEU ARG ILE ASP PRO SER LYS ILE PHE VAL
SEQRES 13 A 311 GLY GLY ASP SER ALA GLY GLY ASN LEU ALA ALA ALA VAL
SEQRES 14 A 311 SER ILE MET ALA ARG ASP SER GLY GLU ASP PHE ILE LYS
SEQRES 15 A 311 HIS GLN ILE LEU ILE TYR PRO VAL VAL ASN PHE VAL ALA
SEQRES 16 A 311 PRO THR PRO SER LEU LEU GLU PHE GLY GLU GLY LEU TRP
SEQRES 17 A 311 ILE LEU ASP GLN LYS ILE MET SER TRP PHE SER GLU GLN
SEQRES 18 A 311 TYR PHE SER ARG GLU GLU ASP LYS PHE ASN PRO LEU ALA
SEQRES 19 A 311 SER VAL ILE PHE ALA ASP LEU GLU ASN LEU PRO PRO ALA
SEQRES 20 A 311 LEU ILE ILE THR ALA GLU TYR ASP PRO LEU ARG ASP GLU
SEQRES 21 A 311 GLY GLU VAL PHE GLY GLN MET LEU ARG ARG ALA GLY VAL
SEQRES 22 A 311 GLU ALA SER ILE VAL ARG TYR ARG GLY VAL LEU HIS GLY
SEQRES 23 A 311 PHE ILE ASN TYR TYR PRO VAL LEU LYS ALA ALA ARG ASP
SEQRES 24 A 311 ALA ILE ASN GLN ILE ALA ALA LEU LEU VAL PHE ASP
SEQRES 1 B 311 MET LEU ASP MET PRO ILE ASP PRO VAL TYR TYR GLN LEU
SEQRES 2 B 311 ALA GLU TYR PHE ASP SER LEU PRO LYS PHE ASP GLN PHE
SEQRES 3 B 311 SER SER ALA ARG GLU TYR ARG GLU ALA ILE ASN ARG ILE
SEQRES 4 B 311 TYR GLU GLU ARG ASN ARG GLN LEU SER GLN HIS GLU ARG
SEQRES 5 B 311 VAL GLU ARG VAL GLU ASP ARG THR ILE LYS GLY ARG ASN
SEQRES 6 B 311 GLY ASP ILE ARG VAL ARG VAL TYR GLN GLN LYS PRO ASP
SEQRES 7 B 311 SER PRO VAL LEU VAL TYR TYR HIS GLY GLY GLY PHE VAL
SEQRES 8 B 311 ILE CYS SER ILE GLU SER HIS ASP ALA LEU CYS ARG ARG
SEQRES 9 B 311 ILE ALA ARG LEU SER ASN SER THR VAL VAL SER VAL ASP
SEQRES 10 B 311 TYR ARG LEU ALA PRO GLU HIS LYS PHE PRO ALA ALA VAL
SEQRES 11 B 311 TYR ASP CYS TYR ASP ALA THR LYS TRP VAL ALA GLU ASN
SEQRES 12 B 311 ALA GLU GLU LEU ARG ILE ASP PRO SER LYS ILE PHE VAL
SEQRES 13 B 311 GLY GLY ASP SER ALA GLY GLY ASN LEU ALA ALA ALA VAL
SEQRES 14 B 311 SER ILE MET ALA ARG ASP SER GLY GLU ASP PHE ILE LYS
SEQRES 15 B 311 HIS GLN ILE LEU ILE TYR PRO VAL VAL ASN PHE VAL ALA
SEQRES 16 B 311 PRO THR PRO SER LEU LEU GLU PHE GLY GLU GLY LEU TRP
SEQRES 17 B 311 ILE LEU ASP GLN LYS ILE MET SER TRP PHE SER GLU GLN
SEQRES 18 B 311 TYR PHE SER ARG GLU GLU ASP LYS PHE ASN PRO LEU ALA
SEQRES 19 B 311 SER VAL ILE PHE ALA ASP LEU GLU ASN LEU PRO PRO ALA
SEQRES 20 B 311 LEU ILE ILE THR ALA GLU TYR ASP PRO LEU ARG ASP GLU
SEQRES 21 B 311 GLY GLU VAL PHE GLY GLN MET LEU ARG ARG ALA GLY VAL
SEQRES 22 B 311 GLU ALA SER ILE VAL ARG TYR ARG GLY VAL LEU HIS GLY
SEQRES 23 B 311 PHE ILE ASN TYR TYR PRO VAL LEU LYS ALA ALA ARG ASP
SEQRES 24 B 311 ALA ILE ASN GLN ILE ALA ALA LEU LEU VAL PHE ASP
SEQRES 1 C 311 MET LEU ASP MET PRO ILE ASP PRO VAL TYR TYR GLN LEU
SEQRES 2 C 311 ALA GLU TYR PHE ASP SER LEU PRO LYS PHE ASP GLN PHE
SEQRES 3 C 311 SER SER ALA ARG GLU TYR ARG GLU ALA ILE ASN ARG ILE
SEQRES 4 C 311 TYR GLU GLU ARG ASN ARG GLN LEU SER GLN HIS GLU ARG
SEQRES 5 C 311 VAL GLU ARG VAL GLU ASP ARG THR ILE LYS GLY ARG ASN
SEQRES 6 C 311 GLY ASP ILE ARG VAL ARG VAL TYR GLN GLN LYS PRO ASP
SEQRES 7 C 311 SER PRO VAL LEU VAL TYR TYR HIS GLY GLY GLY PHE VAL
SEQRES 8 C 311 ILE CYS SER ILE GLU SER HIS ASP ALA LEU CYS ARG ARG
SEQRES 9 C 311 ILE ALA ARG LEU SER ASN SER THR VAL VAL SER VAL ASP
SEQRES 10 C 311 TYR ARG LEU ALA PRO GLU HIS LYS PHE PRO ALA ALA VAL
SEQRES 11 C 311 TYR ASP CYS TYR ASP ALA THR LYS TRP VAL ALA GLU ASN
SEQRES 12 C 311 ALA GLU GLU LEU ARG ILE ASP PRO SER LYS ILE PHE VAL
SEQRES 13 C 311 GLY GLY ASP SER ALA GLY GLY ASN LEU ALA ALA ALA VAL
SEQRES 14 C 311 SER ILE MET ALA ARG ASP SER GLY GLU ASP PHE ILE LYS
SEQRES 15 C 311 HIS GLN ILE LEU ILE TYR PRO VAL VAL ASN PHE VAL ALA
SEQRES 16 C 311 PRO THR PRO SER LEU LEU GLU PHE GLY GLU GLY LEU TRP
SEQRES 17 C 311 ILE LEU ASP GLN LYS ILE MET SER TRP PHE SER GLU GLN
SEQRES 18 C 311 TYR PHE SER ARG GLU GLU ASP LYS PHE ASN PRO LEU ALA
SEQRES 19 C 311 SER VAL ILE PHE ALA ASP LEU GLU ASN LEU PRO PRO ALA
SEQRES 20 C 311 LEU ILE ILE THR ALA GLU TYR ASP PRO LEU ARG ASP GLU
SEQRES 21 C 311 GLY GLU VAL PHE GLY GLN MET LEU ARG ARG ALA GLY VAL
SEQRES 22 C 311 GLU ALA SER ILE VAL ARG TYR ARG GLY VAL LEU HIS GLY
SEQRES 23 C 311 PHE ILE ASN TYR TYR PRO VAL LEU LYS ALA ALA ARG ASP
SEQRES 24 C 311 ALA ILE ASN GLN ILE ALA ALA LEU LEU VAL PHE ASP
SEQRES 1 D 311 MET LEU ASP MET PRO ILE ASP PRO VAL TYR TYR GLN LEU
SEQRES 2 D 311 ALA GLU TYR PHE ASP SER LEU PRO LYS PHE ASP GLN PHE
SEQRES 3 D 311 SER SER ALA ARG GLU TYR ARG GLU ALA ILE ASN ARG ILE
SEQRES 4 D 311 TYR GLU GLU ARG ASN ARG GLN LEU SER GLN HIS GLU ARG
SEQRES 5 D 311 VAL GLU ARG VAL GLU ASP ARG THR ILE LYS GLY ARG ASN
SEQRES 6 D 311 GLY ASP ILE ARG VAL ARG VAL TYR GLN GLN LYS PRO ASP
SEQRES 7 D 311 SER PRO VAL LEU VAL TYR TYR HIS GLY GLY GLY PHE VAL
SEQRES 8 D 311 ILE CYS SER ILE GLU SER HIS ASP ALA LEU CYS ARG ARG
SEQRES 9 D 311 ILE ALA ARG LEU SER ASN SER THR VAL VAL SER VAL ASP
SEQRES 10 D 311 TYR ARG LEU ALA PRO GLU HIS LYS PHE PRO ALA ALA VAL
SEQRES 11 D 311 TYR ASP CYS TYR ASP ALA THR LYS TRP VAL ALA GLU ASN
SEQRES 12 D 311 ALA GLU GLU LEU ARG ILE ASP PRO SER LYS ILE PHE VAL
SEQRES 13 D 311 GLY GLY ASP SER ALA GLY GLY ASN LEU ALA ALA ALA VAL
SEQRES 14 D 311 SER ILE MET ALA ARG ASP SER GLY GLU ASP PHE ILE LYS
SEQRES 15 D 311 HIS GLN ILE LEU ILE TYR PRO VAL VAL ASN PHE VAL ALA
SEQRES 16 D 311 PRO THR PRO SER LEU LEU GLU PHE GLY GLU GLY LEU TRP
SEQRES 17 D 311 ILE LEU ASP GLN LYS ILE MET SER TRP PHE SER GLU GLN
SEQRES 18 D 311 TYR PHE SER ARG GLU GLU ASP LYS PHE ASN PRO LEU ALA
SEQRES 19 D 311 SER VAL ILE PHE ALA ASP LEU GLU ASN LEU PRO PRO ALA
SEQRES 20 D 311 LEU ILE ILE THR ALA GLU TYR ASP PRO LEU ARG ASP GLU
SEQRES 21 D 311 GLY GLU VAL PHE GLY GLN MET LEU ARG ARG ALA GLY VAL
SEQRES 22 D 311 GLU ALA SER ILE VAL ARG TYR ARG GLY VAL LEU HIS GLY
SEQRES 23 D 311 PHE ILE ASN TYR TYR PRO VAL LEU LYS ALA ALA ARG ASP
SEQRES 24 D 311 ALA ILE ASN GLN ILE ALA ALA LEU LEU VAL PHE ASP
HET EPE A 455 14
HET EPE B 455 14
HET EPE C 455 14
HET EPE D 455 14
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETSYN EPE HEPES
FORMUL 5 EPE 4(C8 H18 N2 O4 S1)
FORMUL 9 HOH *561(H2 O1)
HELIX 1 1 ASP A 7 LEU A 13 1 7
HELIX 2 2 LEU A 13 LEU A 20 1 8
HELIX 3 3 LYS A 22 PHE A 26 5 5
HELIX 4 4 SER A 28 GLN A 49 1 22
HELIX 5 5 ILE A 95 SER A 97 5 3
HELIX 6 6 HIS A 98 ASN A 110 1 13
HELIX 7 7 PRO A 127 ASN A 143 1 17
HELIX 8 8 ASN A 143 ARG A 148 1 6
HELIX 9 9 SER A 160 SER A 176 1 17
HELIX 10 10 THR A 197 PHE A 203 1 7
HELIX 11 11 ASP A 211 PHE A 223 1 13
HELIX 12 12 ARG A 225 ASN A 231 5 7
HELIX 13 13 SER A 235 ALA A 239 5 5
HELIX 14 14 LEU A 257 ALA A 271 1 15
HELIX 15 15 GLY A 286 TYR A 291 5 6
HELIX 16 16 LEU A 294 PHE A 310 1 17
HELIX 17 17 PRO B 8 LEU B 20 1 13
HELIX 18 18 LYS B 22 PHE B 26 5 5
HELIX 19 19 SER B 28 GLN B 49 1 22
HELIX 20 20 ILE B 95 SER B 97 5 3
HELIX 21 21 HIS B 98 ASN B 110 1 13
HELIX 22 22 PRO B 127 ASN B 143 1 17
HELIX 23 23 ASN B 143 ARG B 148 1 6
HELIX 24 24 SER B 160 SER B 176 1 17
HELIX 25 25 THR B 197 PHE B 203 1 7
HELIX 26 26 ASP B 211 PHE B 223 1 13
HELIX 27 27 ARG B 225 ASN B 231 5 7
HELIX 28 28 SER B 235 ALA B 239 5 5
HELIX 29 29 LEU B 257 ALA B 271 1 15
HELIX 30 30 GLY B 286 TYR B 291 5 6
HELIX 31 31 LEU B 294 PHE B 310 1 17
HELIX 32 32 PRO C 8 LEU C 13 1 6
HELIX 33 33 LEU C 13 LEU C 20 1 8
HELIX 34 34 LYS C 22 PHE C 26 5 5
HELIX 35 35 SER C 28 GLN C 49 1 22
HELIX 36 36 ILE C 95 SER C 97 5 3
HELIX 37 37 HIS C 98 ASN C 110 1 13
HELIX 38 38 PRO C 127 ASN C 143 1 17
HELIX 39 39 ASN C 143 ARG C 148 1 6
HELIX 40 40 SER C 160 ASP C 175 1 16
HELIX 41 41 THR C 197 PHE C 203 1 7
HELIX 42 42 ASP C 211 PHE C 223 1 13
HELIX 43 43 ARG C 225 ASN C 231 5 7
HELIX 44 44 SER C 235 ALA C 239 5 5
HELIX 45 45 LEU C 257 ALA C 271 1 15
HELIX 46 46 GLY C 286 TYR C 291 5 6
HELIX 47 47 LEU C 294 PHE C 310 1 17
HELIX 48 48 PRO D 8 LEU D 20 1 13
HELIX 49 49 LYS D 22 PHE D 26 5 5
HELIX 50 50 SER D 28 GLN D 49 1 22
HELIX 51 51 HIS D 98 ASN D 110 1 13
HELIX 52 52 PRO D 127 ASN D 143 1 17
HELIX 53 53 ASN D 143 ARG D 148 1 6
HELIX 54 54 SER D 160 SER D 176 1 17
HELIX 55 55 THR D 197 PHE D 203 1 7
HELIX 56 56 ASP D 211 PHE D 223 1 13
HELIX 57 57 ARG D 225 ASN D 231 5 7
HELIX 58 58 SER D 235 ALA D 239 5 5
HELIX 59 59 LEU D 257 ALA D 271 1 15
HELIX 60 60 GLY D 286 TYR D 291 5 6
HELIX 61 61 LEU D 294 PHE D 310 1 17
SHEET 1 A16 ARG A 55 GLY A 63 0
SHEET 2 A16 GLY A 66 GLN A 74 -1 O GLY A 66 N GLY A 63
SHEET 3 A16 THR A 112 ASP A 117 -1 O VAL A 113 N TYR A 73
SHEET 4 A16 SER A 79 TYR A 85 1 O PRO A 80 N THR A 112
SHEET 5 A16 ILE A 149 ASP A 159 1 N ASP A 150 O SER A 79
SHEET 6 A16 ILE A 181 ILE A 187 1 N LYS A 182 O ILE A 154
SHEET 7 A16 ALA A 247 TYR A 254 1 O LEU A 248 N LEU A 186
SHEET 8 A16 ALA A 275 LEU A 284 1 O SER A 276 N ILE A 249
SHEET 9 A16 ALA B 275 LEU B 284 -1 O ILE B 277 N ARG A 281
SHEET 10 A16 ALA B 247 TYR B 254 1 O ALA B 247 N SER B 276
SHEET 11 A16 ILE B 181 ILE B 187 1 O GLN B 184 N LEU B 248
SHEET 12 A16 ILE B 149 ASP B 159 1 O ILE B 154 N LYS B 182
SHEET 13 A16 SER B 79 TYR B 85 1 O SER B 79 N ASP B 150
SHEET 14 A16 THR B 112 ASP B 117 1 N THR B 112 O PRO B 80
SHEET 15 A16 GLY B 66 GLN B 74 -1 O ARG B 69 N ASP B 117
SHEET 16 A16 ARG B 55 GLY B 63 -1 O ARG B 55 N GLN B 74
SHEET 1 B16 ARG C 55 GLY C 63 0
SHEET 2 B16 GLY C 66 GLN C 74 -1 O GLY C 66 N GLY C 63
SHEET 3 B16 THR C 112 ASP C 117 -1 O VAL C 113 N TYR C 73
SHEET 4 B16 SER C 79 TYR C 85 1 O PRO C 80 N THR C 112
SHEET 5 B16 ILE C 149 ASP C 159 1 N ASP C 150 O SER C 79
SHEET 6 B16 ILE C 181 ILE C 187 1 N LYS C 182 O ILE C 154
SHEET 7 B16 ALA C 247 TYR C 254 1 O LEU C 248 N LEU C 186
SHEET 8 B16 ALA C 275 LEU C 284 1 O SER C 276 N ILE C 249
SHEET 9 B16 ALA D 275 LEU D 284 -1 O ILE D 277 N ARG C 281
SHEET 10 B16 ALA D 247 TYR D 254 1 O ALA D 247 N SER D 276
SHEET 11 B16 ILE D 181 ILE D 187 1 O GLN D 184 N LEU D 248
SHEET 12 B16 ILE D 149 ASP D 159 1 O ILE D 154 N LYS D 182
SHEET 13 B16 SER D 79 TYR D 85 1 O SER D 79 N ASP D 150
SHEET 14 B16 THR D 112 ASP D 117 1 O THR D 112 N LEU D 82
SHEET 15 B16 GLY D 66 GLN D 74 -1 O ARG D 69 N ASP D 117
SHEET 16 B16 ARG D 55 GLY D 63 -1 O ARG D 55 N GLN D 74
LINK OG SER A 160 S EPE A 455
LINK OG SER B 160 S EPE B 455
LINK OG SER C 160 S EPE C 455
LINK OG SER D 160 S EPE D 455
CISPEP 1 ALA A 121 PRO A 122 0 0.53
CISPEP 2 PHE A 126 PRO A 127 0 0.97
CISPEP 3 ALA B 121 PRO B 122 0 0.18
CISPEP 4 PHE B 126 PRO B 127 0 -0.85
CISPEP 5 ALA C 121 PRO C 122 0 1.23
CISPEP 6 PHE C 126 PRO C 127 0 0.09
CISPEP 7 ALA D 121 PRO D 122 0 0.40
CISPEP 8 PHE D 126 PRO D 127 0 4.42
CRYST1 169.050 169.050 104.544 90.00 90.00 120.00 P 62 24
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 0.005920 0.003420 0.000000 0.00000
SCALE2 0.000000 0.006830 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009570 0.00000
END |