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HEADER HYDROLASE 10-SEP-15 5AOA
TITLE THE STRUCTURE OF A NOVEL THERMOPHILIC ESTERASE FROM THE
TITLE 2 PLANCTOMYCETES SPECIES, THERMOGUTTA TERRIFONTIS, EST2-
TITLE 3 PROPIONATE BOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOGUTTA TERRIFONTIS;
SOURCE 3 ORGANISM_TAXID: 1331910;
SOURCE 4 STRAIN: R1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PLATE31
KEYWDS HYDROLASE, CARBOXYL ESTERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.SAYER,Z.SZABO,M.N.ISUPOV,C.INGHAM,J.A.LITTLECHILD
REVDAT 1 09-DEC-15 5AOA 0
JRNL AUTH C.SAYER,Z.SZABO,M.N.ISUPOV,C.INGHAM,J.A.LITTLECHILD
JRNL TITL THE STRUCTURE OF A NOVEL THERMOPHILIC ESTERASE FROM THE
JRNL TITL 2 PLANCTOMYCETES SPECIES, THERMOGUTTA TERRIFONTIS REVEALS AN
JRNL TITL 3 OPEN ACTIVE SITE DUE TO A MINIMAL 'CAP' DOMAIN
JRNL REF FRONT.MICROBIOL. 2015
JRNL REFN ESSN 1664-302X
JRNL DOI 10.3389/FMICB.2015.01294
REMARK 2
REMARK 2 RESOLUTION. 1.71 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0131
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,
REMARK 3 STEINER,NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.71
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.69
REMARK 3 NUMBER OF REFLECTIONS : 34986
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.16976
REMARK 3 R VALUE (WORKING SET) : 0.16810
REMARK 3 FREE R VALUE : 0.20221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.7
REMARK 3 FREE R VALUE TEST SET COUNT : 1718
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.710
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.754
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2533
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.73
REMARK 3 BIN R VALUE (WORKING SET) : 0.349
REMARK 3 BIN FREE R VALUE SET COUNT : 113
REMARK 3 BIN FREE R VALUE : 0.385
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2268
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 84
REMARK 3 SOLVENT ATOMS : 228
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.569
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.01
REMARK 3 B22 (A**2) : -1.43
REMARK 3 B33 (A**2) : 0.41
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.095
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.096
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.078
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.589
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2418 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2359 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3265 ; 1.353 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5454 ; 0.939 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 316 ; 5.526 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 119 ;31.779 ;23.025
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 401 ;14.378 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;16.809 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 332 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2738 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 570 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1139 ; 3.374 ; 6.545
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1138 ; 3.376 ; 6.530
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1432 ; 4.351 ;10.954
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1279 ; 5.089 ; 8.392
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 5AOA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-SEP-15.
REMARK 100 THE PDBE ID CODE IS EBI-64896.
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 : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91731
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AIMLESS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36869
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.71
REMARK 200 RESOLUTION RANGE LOW (A) : 51.80
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.5
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.2
REMARK 200 R MERGE (I) : 0.07
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.90
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.71
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.8
REMARK 200 R MERGE FOR SHELL (I) : 1.13
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.50
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: PDB ENTRY 1EVQ
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 30.97850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.93050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.45450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 37.93050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.97850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.45450
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 ALA A 1
REMARK 465 GLU A 2
REMARK 465 VAL A 3
REMARK 465 GLY A 4
REMARK 465 ARG A 5
REMARK 465 LYS A 172
REMARK 465 ASP A 173
REMARK 465 HIS A 174
REMARK 465 VAL A 175
REMARK 465 PRO A 176
REMARK 465 GLU A 283
REMARK 465 SER A 284
REMARK 465 GLN A 285
REMARK 465 PRO A 286
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 DISTANCE
REMARK 500 O B PRO A 40 O HOH A 2054 1.50
REMARK 500 NE A ARG A 43 O HOH A 2061 1.84
REMARK 500 CZ A ARG A 43 O HOH A 2061 1.20
REMARK 500 NH1A ARG A 43 O HOH A 2062 1.95
REMARK 500 NH1A ARG A 43 O HOH A 2061 1.84
REMARK 500 NH2A ARG A 43 O HOH A 2061 1.68
REMARK 500 NH1A ARG A 104 OE2A GLU A 146 1.56
REMARK 500 OE2B GLU A 112 O HOH A 2132 1.74
REMARK 500 CD A GLU A 186 O HOH A 2158 1.90
REMARK 500 OE2A GLU A 186 O HOH A 2158 1.79
REMARK 500 OE2B GLU A 186 O HOH A 2113 1.86
REMARK 500 CD A GLU A 191 O HOH A 2159 1.52
REMARK 500 OE1A GLU A 191 O HOH A 2159 1.33
REMARK 500 OE2A GLU A 191 O HOH A 2154 1.87
REMARK 500 OE2A GLU A 191 O HOH A 2159 1.80
REMARK 500 OE1A GLU A 244 O HOH A 2173 1.32
REMARK 500 OE2A GLU A 244 O HOH A 2194 1.74
REMARK 500 CD A ARG A 255 C2 EDO A 1294 2.09
REMARK 500 NE A ARG A 255 C2 EDO A 1294 1.83
REMARK 500 NE A ARG A 255 O2 EDO A 1294 2.06
REMARK 500 CZ A ARG A 255 C2 EDO A 1294 1.33
REMARK 500 CZ A ARG A 255 O2 EDO A 1294 0.78
REMARK 500 NH1A ARG A 255 C1 EDO A 1294 1.42
REMARK 500 NH1A ARG A 255 C2 EDO A 1294 0.78
REMARK 500 NH1A ARG A 255 O2 EDO A 1294 0.98
REMARK 500 NH2A ARG A 255 O2 EDO A 1294 1.38
REMARK 500 C3 A PPI A 1285 O HOH A 2072 0.98
REMARK 500 O1 EDO A 1294 O HOH A 2208 2.10
REMARK 500 O HOH A 2077 O HOH A 2111 1.76
REMARK 500 O HOH A 2112 O HOH A 2205 1.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NE2B GLN A 108 OE1B GLU A 266 3555 2.07
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 ALA A 41 -0.74 83.91
REMARK 500 SER A 126 -114.83 54.51
REMARK 500 ASN A 161 65.27 21.13
REMARK 500 ASN A 258 19.46 56.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ASN A 161 24.2 L L OUTSIDE RANGE
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 PG4 A1283
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A1284
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PPI A1285
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1286
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1287
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1288
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1289
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1290
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1291
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1292
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1293
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1294
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1295
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5AO9 RELATED DB: PDB
REMARK 900 THE STRUCTURE OF A NOVEL THERMOPHILIC ESTERASE FROM
REMARK 900 THE PLANCTOMYCETES SPECIES, THERMOGUTTA TERRIFONTIS, EST2-
REMARK 900 NATIVE
REMARK 900 RELATED ID: 5AOB RELATED DB: PDB
REMARK 900 THE STRUCTURE OF A NOVEL THERMOPHILIC ESTERASE FROM
REMARK 900 THE PLANCTOMYCETES SPECIES, THERMOGUTTA TERRIFONTIS, EST2-
REMARK 900 BUTYRATE BOUND
REMARK 900 RELATED ID: 5AOC RELATED DB: PDB
REMARK 900 THE STRUCTURE OF A NOVEL THERMOPHILIC ESTERASE FROM
REMARK 900 THE PLANCTOMYCETES SPECIES, THERMOGUTTA TERRIFONTIS, EST2-
REMARK 900 VALERATE BOUND
DBREF 5AOA A 1 286 PDB 5AOA 5AOA 1 286
SEQRES 1 A 286 ALA GLU VAL GLY ARG LEU ARG TYR PRO PRO GLU MET PRO
SEQRES 2 A 286 GLY ALA GLU VAL LYS VAL TYR LYS LYS VAL ASP ASN VAL
SEQRES 3 A 286 ASP LEU LYS LEU TYR ILE TYR LYS PRO ALA ASP TRP LYS
SEQRES 4 A 286 PRO ALA ASP ARG ARG SER ALA ILE VAL PHE PHE PHE GLY
SEQRES 5 A 286 GLY GLY TRP GLN SER GLY SER PRO ALA GLN PHE ARG PRO
SEQRES 6 A 286 GLN CYS GLU TYR PHE ALA GLY ARG GLY MET VAL ALA MET
SEQRES 7 A 286 ALA ALA ASP TYR ARG VAL GLY SER ARG HIS ASN VAL LYS
SEQRES 8 A 286 VAL ALA ASP CYS VAL ALA ASP ALA LYS SER ALA ILE ARG
SEQRES 9 A 286 TRP VAL ARG GLN HIS ALA ALA GLU LEU GLY VAL ASP PRO
SEQRES 10 A 286 GLN LYS ILE VAL ALA SER GLY GLY SER ALA GLY GLY HIS
SEQRES 11 A 286 LEU ALA ALA CYS THR VAL MET VAL PRO ASP LEU GLU ALA
SEQRES 12 A 286 PRO GLU GLU ASP HIS THR ILE SER SER GLN ALA ASN ALA
SEQRES 13 A 286 ALA ILE LEU PHE ASN PRO VAL LEU ILE LEU SER ARG GLU
SEQRES 14 A 286 GLY LEU LYS ASP HIS VAL PRO ARG GLN ASP TRP GLU GLU
SEQRES 15 A 286 ARG LEU ARG GLU ARG LEU GLY THR GLU PRO LYS ALA VAL
SEQRES 16 A 286 SER PRO TYR HIS HIS ILE ARG ALA GLY LEU PRO PRO MET
SEQRES 17 A 286 ILE ILE PHE HIS GLY THR ALA ASP ASN THR VAL PRO PHE
SEQRES 18 A 286 GLU THR ILE ARG LEU PHE ALA GLU ALA MET LYS LYS ALA
SEQRES 19 A 286 GLY ASN ARG CYS GLU LEU VAL PRO PHE GLU GLY ALA ALA
SEQRES 20 A 286 HIS GLY PHE PHE ASN PHE GLY ARG GLY ASP ASN LEU ALA
SEQRES 21 A 286 TYR GLN LYS THR LEU GLU LEU ALA ASP GLU PHE LEU VAL
SEQRES 22 A 286 GLU ILE GLY PHE LEU ALA PRO LYS GLY GLU SER GLN PRO
HET PG4 A1283 13
HET PG4 A1284 13
HET PPI A1285 9
HET PEG A1286 7
HET PEG A1287 7
HET PEG A1288 7
HET PEG A1289 7
HET EDO A1290 4
HET EDO A1291 4
HET EDO A1292 4
HET EDO A1293 4
HET EDO A1294 4
HET CL A1295 1
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CL CHLORIDE ION
HETNAM PPI PROPANOIC ACID
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 PG4 2(C8 H18 O5)
FORMUL 3 EDO 5(C2 H6 O2)
FORMUL 4 CL CL 1-
FORMUL 5 PPI C3 H6 O2
FORMUL 6 PEG 4(C4 H10 O3)
FORMUL 7 HOH *228(H2 O)
HELIX 1 1 SER A 59 GLN A 62 5 4
HELIX 2 2 PHE A 63 ARG A 73 1 11
HELIX 3 3 VAL A 84 ASN A 89 1 6
HELIX 4 4 LYS A 91 HIS A 109 1 19
HELIX 5 5 HIS A 109 GLY A 114 1 6
HELIX 6 6 SER A 126 VAL A 138 1 13
HELIX 7 7 ARG A 177 GLY A 189 1 13
HELIX 8 8 GLU A 191 SER A 196 5 6
HELIX 9 9 SER A 196 ILE A 201 5 6
HELIX 10 10 PRO A 220 ALA A 234 1 15
HELIX 11 11 ARG A 255 ASP A 257 5 3
HELIX 12 12 ASN A 258 ILE A 275 1 18
SHEET 1 AA 8 GLU A 16 VAL A 23 0
SHEET 2 AA 8 VAL A 26 TYR A 33 -1 O VAL A 26 N VAL A 23
SHEET 3 AA 8 VAL A 76 ALA A 80 -1 O ALA A 77 N TYR A 33
SHEET 4 AA 8 ARG A 44 PHE A 50 1 O SER A 45 N VAL A 76
SHEET 5 AA 8 VAL A 115 GLY A 125 1 N ASP A 116 O ARG A 44
SHEET 6 AA 8 ALA A 156 PHE A 160 1 O ALA A 156 N ALA A 122
SHEET 7 AA 8 MET A 208 GLY A 213 1 O ILE A 209 N LEU A 159
SHEET 8 AA 8 CYS A 238 PHE A 243 1 O GLU A 239 N ILE A 210
CISPEP 1 TYR A 8 PRO A 9 0 -3.27
SITE 1 AC1 5 VAL A 138 ASP A 140 GLN A 153 HOH A2146
SITE 2 AC1 5 HOH A2224
SITE 1 AC2 9 GLN A 118 THR A 149 SER A 151 GLN A 153
SITE 2 AC2 9 ASN A 155 HOH A2133 HOH A2134 HOH A2147
SITE 3 AC2 9 HOH A2226
SITE 1 AC3 7 GLY A 53 GLY A 54 SER A 126 ALA A 127
SITE 2 AC3 7 HIS A 248 PEG A1286 HOH A2072
SITE 1 AC4 1 PPI A1285
SITE 1 AC5 5 GLY A 54 GLN A 56 ARG A 187 HOH A2076
SITE 2 AC5 5 HOH A2114
SITE 1 AC6 9 VAL A 19 TYR A 20 LYS A 22 TRP A 105
SITE 2 AC6 9 GLU A 270 GLU A 274 HOH A2029 HOH A2033
SITE 3 AC6 9 HOH A2141
SITE 1 AC7 5 ASP A 42 ARG A 44 EDO A1293 HOH A2059
SITE 2 AC7 5 HOH A2227
SITE 1 AC8 1 ARG A 168
SITE 1 AC9 3 SER A 86 ARG A 87 ASN A 89
SITE 1 BC1 2 ALA A 61 PHE A 253
SITE 1 BC2 3 LYS A 119 PHE A 277 PEG A1289
SITE 1 BC3 6 HIS A 248 GLY A 249 PHE A 250 ARG A 255
SITE 2 BC3 6 HOH A2200 HOH A2208
SITE 1 BC4 4 ASN A 217 HIS A 248 HOH A2179 HOH A2180
CRYST1 61.957 70.909 75.861 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 0.016140 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014103 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013182 0.00000
TER 2269 GLY A 282
MASTER 415 0 13 12 8 0 22 6 2580 1 83 22
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