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HEADER HYDROLASE 08-NOV-22 8HEA
TITLE ESTERASE2 (EAEST2) FROM EXIGUOBACTERIUM ANTARCTICUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THERMOSTABLE CARBOXYLESTERASE EST30;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: EXIGUOBACTERIUM ANTARCTICUM B7;
SOURCE 3 ORGANISM_TAXID: 1087448;
SOURCE 4 GENE: EAB7_2224;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.HWANG,J.H.LEE
REVDAT 1 20-SEP-23 8HEA 0
JRNL AUTH J.HWANG,W.YOO,S.C.SHIN,K.K.KIM,H.W.KIM,H.DO,J.H.LEE
JRNL TITL STRUCTURAL AND BIOCHEMICAL INSIGHTS INTO BIS(2-HYDROXYETHYL)
JRNL TITL 2 TEREPHTHALATE DEGRADING CARBOXYLESTERASE ISOLATED FROM
JRNL TITL 3 PSYCHROTROPHIC BACTERIUM EXIGUOBACTERIUM ANTARCTICUM.
JRNL REF INT J MOL SCI V. 24 2023
JRNL REFN ESSN 1422-0067
JRNL PMID 37569396
JRNL DOI 10.3390/IJMS241512022
REMARK 2
REMARK 2 RESOLUTION. 1.74 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.14_3260
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 : CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.74
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.70
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 32192
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 1619
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 31.7000 - 3.9800 1.00 2697 155 0.1747 0.1806
REMARK 3 2 3.9800 - 3.1600 1.00 2625 124 0.1844 0.1947
REMARK 3 3 3.1600 - 2.7600 1.00 2582 128 0.2075 0.2189
REMARK 3 4 2.7600 - 2.5100 1.00 2547 115 0.2034 0.2506
REMARK 3 5 2.5100 - 2.3300 1.00 2521 155 0.2051 0.2236
REMARK 3 6 2.3300 - 2.1900 1.00 2523 135 0.2083 0.2083
REMARK 3 7 2.1900 - 2.0800 1.00 2540 131 0.2072 0.2323
REMARK 3 8 2.0800 - 1.9900 1.00 2505 147 0.2060 0.2490
REMARK 3 9 1.9900 - 1.9100 1.00 2529 117 0.2113 0.2459
REMARK 3 10 1.9100 - 1.8500 1.00 2504 143 0.2016 0.2331
REMARK 3 11 1.8500 - 1.7900 1.00 2478 149 0.2263 0.2777
REMARK 3 12 1.7900 - 1.7400 1.00 2522 120 0.2307 0.2624
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) : 0.176
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.735
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.30
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 : 0.016 1977
REMARK 3 ANGLE : 1.781 2679
REMARK 3 CHIRALITY : 0.106 291
REMARK 3 PLANARITY : 0.011 347
REMARK 3 DIHEDRAL : 22.074 733
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 8HEA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-NOV-22.
REMARK 100 THE DEPOSITION ID IS D_1300033473.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-MAY-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 5C (4A)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9796
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32327
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.740
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 13.00
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 53.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.74
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.79
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) : NULL
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: MOLREP
REMARK 200 STARTING MODEL: 1TQH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES:NAOH (PH 7.5), 20% (W/V)
REMARK 280 PEG 8000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 296K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+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 25.18100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 44.80850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.89450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 44.80850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.18100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.89450
REMARK 290 SMTRY3 4 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: MONOMERIC
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 LYS 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),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 LYS A 7 C PRO A 8 N 0.143
REMARK 500
REMARK 500 REMARK: NULL
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 25 -4.50 72.18
REMARK 500 SER A 93 -122.28 55.77
REMARK 500 ASN A 189 49.23 -95.53
REMARK 500
REMARK 500 REMARK: NULL
DBREF 8HEA A 1 246 UNP K0AFS0 K0AFS0_EXIAB 1 246
SEQRES 1 A 246 MET LYS ILE THR LEU PRO LYS PRO PHE PHE PHE GLU GLY
SEQRES 2 A 246 GLY ASN ARG ALA VAL LEU LEU LEU HIS GLY PHE THR GLY
SEQRES 3 A 246 SER SER ALA ASP VAL ARG MET LEU GLY ARG TYR LEU GLN
SEQRES 4 A 246 LYS HIS GLY TYR THR SER LEU ALA PRO GLN TYR LYS GLY
SEQRES 5 A 246 HIS ALA ALA PRO PRO GLU GLU LEU THR LYS THR GLY PRO
SEQRES 6 A 246 ALA ASP TRP TRP GLN ASP VAL LEU ASP GLY TYR GLU GLU
SEQRES 7 A 246 LEU LYS ALA LYS GLY TYR ASP GLU ILE ALA VAL CYS GLY
SEQRES 8 A 246 LEU SER LEU GLY GLY VAL MET SER LEU ARG LEU SER MET
SEQRES 9 A 246 HIS ARG PRO VAL LYS ALA VAL ILE PRO MET CYS ALA PRO
SEQRES 10 A 246 ALA TYR ILE LYS SER GLU ASP VAL MET TYR ALA GLY VAL
SEQRES 11 A 246 THR GLU TYR ALA ARG GLU PHE LYS LYS ARG GLU GLY LYS
SEQRES 12 A 246 SER VAL ASP GLU ILE GLU GLN GLU MET ALA VAL PHE GLU
SEQRES 13 A 246 PRO MET PRO THR LEU LYS ASP LEU GLN ALA LEU LEU LYS
SEQRES 14 A 246 GLU THR ARG ASP SER LEU GLU ASP VAL TYR ALA PRO THR
SEQRES 15 A 246 LEU VAL VAL GLN ALA ARG ASN ASP HIS MET ILE ASN THR
SEQRES 16 A 246 ASP SER ALA ASN ILE ILE HIS ASP GLY VAL SER ALA LEU
SEQRES 17 A 246 GLN LYS GLU LEU ILE TRP TYR GLU ASN SER GLY HIS VAL
SEQRES 18 A 246 ILE THR LEU ASP LYS GLU LYS GLU THR LEU HIS GLN ASP
SEQRES 19 A 246 ILE HIS GLU PHE LEU ASP GLY LEU ASN TRP SER HIS
FORMUL 2 HOH *169(H2 O)
HELIX 1 AA1 SER A 27 ASP A 30 5 4
HELIX 2 AA2 VAL A 31 HIS A 41 1 11
HELIX 3 AA3 PRO A 56 THR A 61 1 6
HELIX 4 AA4 GLY A 64 LYS A 82 1 19
HELIX 5 AA5 SER A 93 ARG A 106 1 14
HELIX 6 AA6 SER A 122 GLU A 141 1 20
HELIX 7 AA7 SER A 144 VAL A 154 1 11
HELIX 8 AA8 THR A 160 SER A 174 1 15
HELIX 9 AA9 LEU A 175 VAL A 178 5 4
HELIX 10 AB1 ASP A 196 VAL A 205 1 10
HELIX 11 AB2 VAL A 221 ASP A 225 5 5
HELIX 12 AB3 GLU A 227 GLY A 241 1 15
SHEET 1 AA1 5 PHE A 9 PHE A 11 0
SHEET 2 AA1 5 THR A 44 ALA A 47 -1 O SER A 45 N PHE A 11
SHEET 3 AA1 5 ALA A 17 LEU A 21 1 N LEU A 20 O LEU A 46
SHEET 4 AA1 5 ILE A 87 LEU A 92 1 O ALA A 88 N LEU A 19
SHEET 5 AA1 5 VAL A 111 MET A 114 1 O MET A 114 N GLY A 91
SHEET 1 AA2 2 THR A 182 ALA A 187 0
SHEET 2 AA2 2 LYS A 210 TYR A 215 1 O GLU A 211 N VAL A 184
CRYST1 50.362 67.789 89.617 90.00 90.00 90.00 P 21 21 21 4
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 0.019856 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014752 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011159 0.00000
TER 1931 HIS A 246
MASTER 246 0 0 12 7 0 0 6 2099 1 0 19
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