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HEADER HYDROLASE 30-JUL-13 4BZZ
TITLE COMPLETE CRYSTAL STRUCTURE OF CARBOXYLESTERASE CEST-2923
TITLE 2 FROM LACTOBACILLUS PLANTARUM WCFS1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE/ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CEST-2923;
COMPND 5 EC: 3.1.1.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOBACILLUS PLANTARUM;
SOURCE 3 ORGANISM_TAXID: 220668;
SOURCE 4 STRAIN: WCFS1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS HYDROLASE, CARBOXYLESTERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.BENAVENTE,M.ESTEBAN-TORRES,I.ACEBRON,B.DE LAS RIVAS,R.MUNOZ,
AUTHOR 2 Y.ALVAREZ,J.M.MANCHENO
REVDAT 1 30-OCT-13 4BZZ 0
JRNL AUTH R.BENAVENTE,M.ESTEBAN-TORRES,I.ACEBRON,B.DE LAS RIVAS,
JRNL AUTH 2 R.MUNOZ,Y.ALVAREZ,J.M.MANCHENO
JRNL TITL STRUCTURE, BIOCHEMICAL CHARACTERIZATION AND ANALYSIS OF THE
JRNL TITL 2 PLEOMORPHISM OF CARBOXYLESTERASE CEST-2923 FROM
JRNL TITL 3 LACTOBACILLUS PLANTARUM WCFS1
JRNL REF FEBS J. 2013
JRNL REFN ESSN 1742-4658
JRNL PMID 24127688
JRNL DOI 10.1111/FEBS.12569
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT 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) : 3.000
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.062
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.34
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.03
REMARK 3 NUMBER OF REFLECTIONS : 9984
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1547
REMARK 3 R VALUE (WORKING SET) : 0.1520
REMARK 3 FREE R VALUE : 0.2078
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.8
REMARK 3 FREE R VALUE TEST SET COUNT : 480
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 46.0672 - 4.3260 0.98 3291 160 0.1438 0.1857
REMARK 3 2 4.3260 - 3.4340 0.99 3124 160 0.1438 0.2216
REMARK 3 3 3.4340 - 3.0000 0.99 3089 160 0.1862 0.2419
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) : 0.26
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.67
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 52.06
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 : 0.007 2231
REMARK 3 ANGLE : 1.042 3053
REMARK 3 CHIRALITY : 0.075 338
REMARK 3 PLANARITY : 0.004 394
REMARK 3 DIHEDRAL : 15.475 767
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESID 1 THROUGH 21 )
REMARK 3 ORIGIN FOR THE GROUP (A): 62.3491 -41.9692 12.6666
REMARK 3 T TENSOR
REMARK 3 T11: 0.3870 T22: 0.4657
REMARK 3 T33: 0.3861 T12: -0.0829
REMARK 3 T13: 0.0962 T23: -0.0861
REMARK 3 L TENSOR
REMARK 3 L11: 6.6243 L22: 2.0874
REMARK 3 L33: 4.1627 L12: 0.7025
REMARK 3 L13: 5.2464 L23: 0.6574
REMARK 3 S TENSOR
REMARK 3 S11: -0.0913 S12: 0.2110 S13: 0.0152
REMARK 3 S21: -0.1774 S22: -0.3288 S23: -0.0403
REMARK 3 S31: -0.0729 S32: 0.4939 S33: 0.3411
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESID 22 THROUGH 183 )
REMARK 3 ORIGIN FOR THE GROUP (A): 52.7438 -46.6043 19.6151
REMARK 3 T TENSOR
REMARK 3 T11: 0.2635 T22: 0.5290
REMARK 3 T33: 0.3553 T12: -0.0717
REMARK 3 T13: 0.0438 T23: -0.0992
REMARK 3 L TENSOR
REMARK 3 L11: 1.1628 L22: 2.1270
REMARK 3 L33: 3.9309 L12: 0.6494
REMARK 3 L13: -0.0553 L23: -0.7854
REMARK 3 S TENSOR
REMARK 3 S11: 0.1591 S12: -0.3906 S13: 0.1461
REMARK 3 S21: 0.1812 S22: -0.1817 S23: -0.0204
REMARK 3 S31: -0.3413 S32: 0.2418 S33: 0.0303
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESID 184 THROUGH 239 )
REMARK 3 ORIGIN FOR THE GROUP (A): 41.3754 -57.6990 22.1543
REMARK 3 T TENSOR
REMARK 3 T11: 0.2600 T22: 0.5438
REMARK 3 T33: 0.3215 T12: -0.1047
REMARK 3 T13: 0.0507 T23: -0.0368
REMARK 3 L TENSOR
REMARK 3 L11: 2.0958 L22: 5.4239
REMARK 3 L33: 3.5126 L12: -0.2784
REMARK 3 L13: -0.6111 L23: 0.5829
REMARK 3 S TENSOR
REMARK 3 S11: 0.2605 S12: -0.5749 S13: -0.1257
REMARK 3 S21: 0.4021 S22: -0.2301 S23: 0.3223
REMARK 3 S31: 0.1023 S32: -0.2751 S33: -0.0170
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESID 240 THROUGH 275 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.1688 -58.4674 7.6933
REMARK 3 T TENSOR
REMARK 3 T11: 0.3288 T22: 0.4996
REMARK 3 T33: 0.2735 T12: -0.0638
REMARK 3 T13: -0.0270 T23: -0.0344
REMARK 3 L TENSOR
REMARK 3 L11: 7.2040 L22: 4.3940
REMARK 3 L33: 6.0796 L12: -3.3148
REMARK 3 L13: -1.8669 L23: 2.0759
REMARK 3 S TENSOR
REMARK 3 S11: 0.2628 S12: 0.0164 S13: -0.6844
REMARK 3 S21: -0.6108 S22: -0.2357 S23: 0.7540
REMARK 3 S31: 0.4342 S32: -0.1174 S33: 0.1109
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 4BZZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-JUL-13.
REMARK 100 THE PDBE ID CODE IS EBI-57863.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
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 : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9687
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9994
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.99
REMARK 200 RESOLUTION RANGE LOW (A) : 49.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 7.5
REMARK 200 R MERGE (I) : 0.12
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.70
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.99
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : 7.3
REMARK 200 R MERGE FOR SHELL (I) : 0.47
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.10
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: PDB EBTRY 3D3N
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.8
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.7 M AMMONIUM SULPHATE, 0.15 M
REMARK 280 SODIUM ACETATE, PH 4.6
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 6 2 2
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 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z
REMARK 290 6555 X-Y,X,Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z
REMARK 290 10555 -Y,-X,-Z
REMARK 290 11555 -X+Y,Y,-Z
REMARK 290 12555 X,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 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 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 0.00000
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 0.00000
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 26170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 52600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -415.7 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 BIOMT1 2 -0.500000 -0.866025 0.000000 70.36050
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 -121.86796
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 140.72100
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 4 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 5 -1.000000 0.000000 0.000000 140.72100
REMARK 350 BIOMT2 5 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 6 0.500000 0.866025 0.000000 70.36050
REMARK 350 BIOMT2 6 0.866025 -0.500000 0.000000 -121.86796
REMARK 350 BIOMT3 6 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 HIS A 277
REMARK 465 HIS A 278
REMARK 465 HIS A 279
REMARK 465 HIS A 280
REMARK 465 HIS A 281
REMARK 465 HIS A 282
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 TYR A 276 CA C O CB CG CD1 CD2 CE1 CE2 CZ OH
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 10 49.76 -81.26
REMARK 500 ASP A 27 36.32 -90.90
REMARK 500 GLU A 53 -96.86 -108.35
REMARK 500 HIS A 104 74.98 53.18
REMARK 500 SER A 116 -114.75 45.78
REMARK 500 TYR A 154 58.00 32.31
REMARK 500 ALA A 236 -114.17 56.57
REMARK 500 ASN A 239 -168.23 -124.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1276
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1277
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1278
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1279
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1280
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1281
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1282
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CCN A1283
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4BZW RELATED DB: PDB
REMARK 900 COMPLETE CRYSTAL STRUCTURE OF THE CARBOXYLESTERASE CEST-
REMARK 900 2923 (LP_2923) FROM LACTOBACILLUS PLANTARUM WCFS1
REMARK 900 RELATED ID: 4C01 RELATED DB: PDB
REMARK 900 COMPLETE CRYSTAL STRUCTURE OF CARBOXYLESTERASE CEST-2923
REMARK 900 (LP_2923) FROM LACTOBACILLUS PLANTARUM WCFS1
DBREF 4BZZ A 1 276 UNP F9US10 F9US10_LACPL 1 276
SEQADV 4BZZ HIS A 277 UNP F9US10 EXPRESSION TAG
SEQADV 4BZZ HIS A 278 UNP F9US10 EXPRESSION TAG
SEQADV 4BZZ HIS A 279 UNP F9US10 EXPRESSION TAG
SEQADV 4BZZ HIS A 280 UNP F9US10 EXPRESSION TAG
SEQADV 4BZZ HIS A 281 UNP F9US10 EXPRESSION TAG
SEQADV 4BZZ HIS A 282 UNP F9US10 EXPRESSION TAG
SEQRES 1 A 282 MET GLN VAL GLU GLN ARG THR LEU ASN THR ALA ALA HIS
SEQRES 2 A 282 PRO PHE GLN ILE THR ALA TYR TRP LEU ASP GLN ILE SER
SEQRES 3 A 282 ASP PHE GLU THR ALA VAL ASP TYR PRO ILE MET ILE ILE
SEQRES 4 A 282 CYS PRO GLY GLY GLY PHE THR TYR HIS SER GLY ARG GLU
SEQRES 5 A 282 GLU ALA PRO ILE ALA THR ARG MET MET ALA ALA GLY MET
SEQRES 6 A 282 HIS THR VAL VAL LEU ASN TYR GLN LEU ILE VAL GLY ASP
SEQRES 7 A 282 GLN SER VAL TYR PRO TRP ALA LEU GLN GLN LEU GLY ALA
SEQRES 8 A 282 THR ILE ASP TRP ILE THR THR GLN ALA SER ALA HIS HIS
SEQRES 9 A 282 VAL ASP CYS GLN ARG ILE ILE LEU ALA GLY PHE SER ALA
SEQRES 10 A 282 GLY GLY HIS VAL VAL ALA THR TYR ASN GLY VAL ALA THR
SEQRES 11 A 282 GLN PRO GLU LEU ARG THR ARG TYR HIS LEU ASP HIS TYR
SEQRES 12 A 282 GLN GLY GLN HIS ALA ALA ILE ILE LEU GLY TYR PRO VAL
SEQRES 13 A 282 ILE ASP LEU THR ALA GLY PHE PRO THR THR SER ALA ALA
SEQRES 14 A 282 ARG ASN GLN ILE THR THR ASP ALA ARG LEU TRP ALA ALA
SEQRES 15 A 282 GLN ARG LEU VAL THR PRO ALA SER LYS PRO ALA PHE VAL
SEQRES 16 A 282 TRP GLN THR ALA THR ASP GLU SER VAL PRO PRO ILE ASN
SEQRES 17 A 282 SER LEU LYS TYR VAL GLN ALA MET LEU GLN HIS GLN VAL
SEQRES 18 A 282 ALA THR ALA TYR HIS LEU PHE GLY SER GLY ILE HIS GLY
SEQRES 19 A 282 LEU ALA LEU ALA ASN HIS VAL THR GLN LYS PRO GLY LYS
SEQRES 20 A 282 ASP LYS TYR LEU ASN ASP GLN ALA ALA ILE TRP PRO GLN
SEQRES 21 A 282 LEU ALA LEU ARG TRP LEU GLN GLU GLN GLY LEU LEU ALA
SEQRES 22 A 282 GLY ASN TYR HIS HIS HIS HIS HIS HIS
HET ACT A1276 4
HET ACT A1277 4
HET ACT A1278 4
HET SO4 A1279 5
HET SO4 A1280 5
HET SO4 A1281 5
HET SO4 A1282 5
HET CCN A1283 3
HETNAM SO4 SULFATE ION
HETNAM CCN ACETONITRILE
HETNAM ACT ACETATE ION
FORMUL 2 SO4 4(O4 S 2-)
FORMUL 3 CCN C2 H3 N
FORMUL 4 ACT 3(C2 H3 O2 1-)
FORMUL 5 HOH *4(H2 O)
HELIX 1 1 SER A 49 GLU A 52 5 4
HELIX 2 2 GLU A 53 ALA A 62 1 10
HELIX 3 3 PRO A 83 THR A 98 1 16
HELIX 4 4 GLN A 99 HIS A 104 1 6
HELIX 5 5 ALA A 117 ALA A 129 1 13
HELIX 6 6 GLN A 131 TYR A 138 1 8
HELIX 7 7 THR A 166 THR A 174 1 9
HELIX 8 8 ALA A 182 VAL A 186 5 5
HELIX 9 9 PRO A 206 HIS A 219 1 14
HELIX 10 10 LYS A 247 LEU A 251 5 5
HELIX 11 11 GLN A 254 ALA A 256 5 3
HELIX 12 12 ILE A 257 GLN A 269 1 13
SHEET 1 AA 8 GLN A 2 LEU A 8 0
SHEET 2 AA 8 PHE A 15 TRP A 21 -1 O PHE A 15 N LEU A 8
SHEET 3 AA 8 HIS A 66 LEU A 70 -1 O THR A 67 N TYR A 20
SHEET 4 AA 8 TYR A 34 CYS A 40 1 O PRO A 35 N HIS A 66
SHEET 5 AA 8 VAL A 105 PHE A 115 1 N ASP A 106 O TYR A 34
SHEET 6 AA 8 ALA A 149 GLY A 153 1 O ALA A 149 N LEU A 112
SHEET 7 AA 8 ALA A 193 THR A 198 1 O PHE A 194 N LEU A 152
SHEET 8 AA 8 THR A 223 PHE A 228 1 O ALA A 224 N VAL A 195
CISPEP 1 TYR A 82 PRO A 83 0 -1.58
CISPEP 2 PHE A 163 PRO A 164 0 -1.15
SITE 1 AC1 3 GLY A 43 GLY A 44 SER A 116
SITE 1 AC2 1 ARG A 109
SITE 1 AC3 4 ARG A 59 ALA A 63 ASN A 239 LEU A 263
SITE 1 AC4 5 ASP A 201 GLU A 202 SER A 203 ILE A 232
SITE 2 AC4 5 HIS A 233
SITE 1 AC5 3 GLN A 5 ARG A 6 GLN A 99
SITE 1 AC6 4 LYS A 244 LYS A 247 LYS A 249 TYR A 250
SITE 1 AC7 6 GLU A 133 ARG A 137 SER A 167 ARG A 170
SITE 2 AC7 6 ASN A 171 TRP A 180
SITE 1 AC8 2 ASP A 248 LYS A 249
CRYST1 140.721 140.721 82.290 90.00 90.00 120.00 P 6 2 2 12
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 0.007106 0.004103 0.000000 0.00000
SCALE2 0.000000 0.008206 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012152 0.00000
TER 2145 TYR A 276
MASTER 387 0 8 12 8 0 10 6 2183 1 35 22
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