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HEADER HYDROLASE 20-APR-00 1EVQ
TITLE THE CRYSTAL STRUCTURE OF THE THERMOPHILIC CARBOXYLESTERASE
TITLE 2 EST2 FROM ALICYCLOBACILLUS ACIDOCALDARIUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ALICYCLOBACILLUS ACIDOCALDARIUS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PT7-7SCII
KEYWDS ALPHA/BETA HYDROLASE FOLD
EXPDTA X-RAY DIFFRACTION
AUTHOR G.DE SIMONE,S.GALDIERO,G.MANCO,D.LANG,M.ROSSI,C.PEDONE
REVDAT 1 22-NOV-00 1EVQ 0
JRNL AUTH G.DE SIMONE,S.GALDIERO,G.MANCO,D.LANG,M.ROSSI,
JRNL AUTH 2 C.PEDONE
JRNL TITL A SNAPSHOT OF THE TRANSITION STATE ANALOGUE OF A
JRNL TITL 2 NOVEL THERMOPHILIC ESTERASE BELONGING TO THE
JRNL TITL 3 SUBFAMILY OF MAMMALIAN HORMONE-SENSITIVE LIPASE
JRNL REF J.MOL.BIOL. V. 303 761 2000
JRNL REFN ASTM JMOBAK UK ISSN 0022-2836
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.DE SIMONE,G.MANCO,S.GALDIERO,A.LOMBARDI,M.ROSSI,
REMARK 1 AUTH 2 V.PAVONE
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION
REMARK 1 TITL 2 STUDIES OF THE CARBOXYLESTERASE EST2 FROM
REMARK 1 TITL 3 ALICYCLOBACILLUS ACIDOCALDARIUS
REMARK 1 REF ACTA CRYSTALLOGR., SECT.D V. 55 1348 1999
REMARK 1 REFN ASTM ABCRE6 DK ISSN 0907-4449
REMARK 1 REFERENCE 2
REMARK 1 AUTH Y.WEI,J.A.CONTRERAS,P.SHEFFIELD,T.OSTERLUND,
REMARK 1 AUTH 2 U.DEREWENDA,R.E.KNEUSEL,U.MATERN,C.HOLM,
REMARK 1 AUTH 3 Z.S.DEREWENDA
REMARK 1 TITL CRYSTAL STRUCTURE OF BREFELDIN A ESTERASE, A
REMARK 1 TITL 2 BACTERIAL HOMOLOG OF THE MAMMALIAN
REMARK 1 TITL 3 HORMONE-SENSITIVE LIPASE
REMARK 1 REF NAT.STRUCT.BIOL. V. 6 340 1999
REMARK 1 REFN ASTM NSBIEW US ISSN 1072-8368
REMARK 2
REMARK 2 RESOLUTION. 2.60 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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 10753
REMARK 3
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 515
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 : 2423
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 78
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) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.60
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
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 1EVQ COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 6
REMARK 6 RESIDUE ARG215 HAS BEEN MODELED AS TWO CONFORMERS.
REMARK 6 THE TWO N-TERMINAL RESIDUES ARE NOT VISIBLE IN THE
REMARK 6 ELECTRON DENSITY.
REMARK 6 THE ELECTRON DENSITY FOR THE LOOP REGION GLN33-LEU36
REMARK 6 WAS VERY POORLY DEFINED.
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-APR-2000.
REMARK 100 THE RCSB ID CODE IS RCSB010935.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAR-1999
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.80
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X31
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9785, 0.9786, 0.9810
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
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 : 10886
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 18.000
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 31.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.23600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: WAVELENGTH 0.9785 IS THE PEAK WAVELENGTH, 0.9786
REMARK 200 IS THE INFLECTION, AND 0.9810 IS REMOTE.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.8
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2% PEG 400, 100MM HEPES PH
REMARK 280 7.8, 2M AMMONIUM SULPHATE, 1MM DTT
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,1/2+Z
REMARK 290 3555 1/2-Y,1/2+X,1/4+Z
REMARK 290 4555 1/2+Y,1/2-X,3/4+Z
REMARK 290 5555 1/2-X,1/2+Y,1/4-Z
REMARK 290 6555 1/2+X,1/2-Y,3/4-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,1/2-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 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.64500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.55250
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.55250
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 26.82250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.55250
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.55250
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 80.46750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.55250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.55250
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 26.82250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.55250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.55250
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 80.46750
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 53.64500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 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 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 465 PRO A 2
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 LEU A 36 CD2 LEU A 36 CG 0.094
REMARK 500 LEU A 36 O LEU A 36 C -0.080
REMARK 500 SER A 155 OG SER A 155 CB 0.222
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 36 N - CA - C ANGL. DEV. = 16.0 DEGREES
REMARK 500 TYR A 74 N - CA - C ANGL. DEV. = 9.4 DEGREES
REMARK 500 PRO A 75 N - CA - C ANGL. DEV. =-10.9 DEGREES
REMARK 500 PHE A 121 N - CA - C ANGL. DEV. =-11.0 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 155 59.21 -118.41
REMARK 500 LEU A 205 70.27 -72.56
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 SER155 IS COVALENTLY BOUND TO A SULPHONYL DERIVATIVE.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THERE ARE NO SUITABLE PROTEIN SEQUENCE DATABASE MATCHES.
REMARK 999 THE DNA SEQUENCE HAS BEEN DEPOSITED TO EMBL,
REMARK 999 ACCESSION X62835.
SEQRES 1 A 310 MET PRO LEU ASP PRO VAL ILE GLN GLN VAL LEU ASP GLN
SEQRES 2 A 310 LEU ASN ARG MET PRO ALA PRO ASP TYR LYS HIS LEU SER
SEQRES 3 A 310 ALA GLN GLN PHE ARG SER GLN GLN SER LEU PHE PRO PRO
SEQRES 4 A 310 VAL LYS LYS GLU PRO VAL ALA GLU VAL ARG GLU PHE ASP
SEQRES 5 A 310 MSE ASP LEU PRO GLY ARG THR LEU LYS VAL ARG MSE TYR
SEQRES 6 A 310 ARG PRO GLU GLY VAL GLU PRO PRO TYR PRO ALA LEU VAL
SEQRES 7 A 310 TYR TYR HIS GLY GLY GLY TRP VAL VAL GLY ASP LEU GLU
SEQRES 8 A 310 THR HIS ASP PRO VAL CYS ARG VAL LEU ALA LYS ASP GLY
SEQRES 9 A 310 ARG ALA VAL VAL PHE SER VAL ASP TYR ARG LEU ALA PRO
SEQRES 10 A 310 GLU HIS LYS PHE PRO ALA ALA VAL GLU ASP ALA TYR ASP
SEQRES 11 A 310 ALA LEU GLN TRP ILE ALA GLU ARG ALA ALA ASP PHE HIS
SEQRES 12 A 310 LEU ASP PRO ALA ARG ILE ALA VAL GLY GLY ASP SER ALA
SEQRES 13 A 310 GLY GLY ASN LEU ALA ALA VAL THR SER ILE LEU ALA LYS
SEQRES 14 A 310 GLU ARG GLY GLY PRO ALA LEU ALA PHE GLN LEU LEU ILE
SEQRES 15 A 310 TYR PRO SER THR GLY TYR ASP PRO ALA HIS PRO PRO ALA
SEQRES 16 A 310 SER ILE GLU GLU ASN ALA GLU GLY TYR LEU LEU THR GLY
SEQRES 17 A 310 GLY MSE MSE LEU TRP PHE ARG ASP GLN TYR LEU ASN SER
SEQRES 18 A 310 LEU GLU GLU LEU THR HIS PRO TRP PHE SER PRO VAL LEU
SEQRES 19 A 310 TYR PRO ASP LEU SER GLY LEU PRO PRO ALA TYR ILE ALA
SEQRES 20 A 310 THR ALA GLN TYR ASP PRO LEU ARG ASP VAL GLY LYS LEU
SEQRES 21 A 310 TYR ALA GLU ALA LEU ASN LYS ALA GLY VAL LYS VAL GLU
SEQRES 22 A 310 ILE GLU ASN PHE GLU ASP LEU ILE HIS GLY PHE ALA GLN
SEQRES 23 A 310 PHE TYR SER LEU SER PRO GLY ALA THR LYS ALA LEU VAL
SEQRES 24 A 310 ARG ILE ALA GLU LYS LEU ARG ASP ALA LEU ALA
MODRES 1EVQ MSE A 53 MET SELENOMETHIONINE
MODRES 1EVQ MSE A 64 MET SELENOMETHIONINE
MODRES 1EVQ MSE A 210 MET SELENOMETHIONINE
MODRES 1EVQ MSE A 211 MET SELENOMETHIONINE
HET MSE A 53 8
HET MSE A 64 8
HET MSE A 210 8
HET MSE A 211 8
HET EPE A 455 14
HET TRS 401 8
HETNAM MSE SELENOMETHIONINE
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETSYN EPE HEPES
HETSYN TRS TRIS BUFFER
FORMUL 1 MSE 4(C5 H11 N1 O2 SE1)
FORMUL 2 EPE C8 H18 N2 O4 S1
FORMUL 3 TRS C4 H12 N1 O3 1+
FORMUL 4 HOH *78(H2 O1)
HELIX 1 1 ASP A 4 ASN A 15 1 12
HELIX 2 2 SER A 26 GLN A 33 1 8
HELIX 3 3 HIS A 93 ARG A 105 1 13
HELIX 4 4 PRO A 122 GLU A 137 1 16
HELIX 5 5 ARG A 138 PHE A 142 5 5
HELIX 6 6 SER A 155 ARG A 171 1 17
HELIX 7 7 PRO A 194 ASN A 200 1 7
HELIX 8 8 THR A 207 LEU A 219 1 13
HELIX 9 9 SER A 221 HIS A 227 5 7
HELIX 10 10 SER A 231 TYR A 235 5 5
HELIX 11 11 LEU A 254 ALA A 268 1 15
HELIX 12 12 GLY A 283 TYR A 288 5 6
HELIX 13 13 SER A 291 ALA A 310 1 20
SHEET 1 A 8 GLU A 47 LEU A 55 0
SHEET 2 A 8 ARG A 58 ARG A 66 -1 O ARG A 58 N LEU A 55
SHEET 3 A 8 VAL A 107 VAL A 111 -1 O VAL A 108 N TYR A 65
SHEET 4 A 8 TYR A 74 TYR A 80 1 O PRO A 75 N VAL A 107
SHEET 5 A 8 LEU A 144 ASP A 154 1 N ASP A 145 O TYR A 74
SHEET 6 A 8 GLN A 179 ILE A 182 1 N LEU A 180 O VAL A 151
SHEET 7 A 8 ALA A 244 ALA A 249 1 O TYR A 245 N LEU A 181
SHEET 8 A 8 VAL A 272 PHE A 277 1 O GLU A 273 N ILE A 246
LINK OG SER A 155 S EPE A 455
CISPEP 1 PRO A 72 PRO A 73 0 -1.79
CISPEP 2 ALA A 116 PRO A 117 0 0.30
CISPEP 3 PHE A 121 PRO A 122 0 1.16
CISPEP 4 GLY A 173 PRO A 174 0 0.80
CRYST1 79.105 79.105 107.290 90.00 90.00 90.00 P 41 21 2 8
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 0.012640 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012640 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009320 0.00000
END |