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HEADER HYDROLASE 24-MAR-15 4UHD
TITLE STRUCTURAL STUDIES OF A THERMOPHILIC ESTERASE FROM
TITLE 2 THERMOGUTTA TERRIFONTIS (ACETATE 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: PLANCTOMYCETES BACTERIUM R1;
SOURCE 3 ORGANISM_TAXID: 1331910;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: ARCTICEXPRESS (DE3)RIL;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PLATE31
KEYWDS HYDROLASE, ALPHA BETA HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.SAYER,M.N.ISUPOV,E.BONCH-OSMOLOVSKAYA,J.A.LITTLECHILD
REVDAT 1 10-JUN-15 4UHD 0
JRNL AUTH C.SAYER,M.N.ISUPOV,E.BONCH-OSMOLOVSKAYA,J.A.LITTLECHILD
JRNL TITL STRUCTURAL STUDIES OF A THERMOPHILIC ESTERASE FROM A NEW
JRNL TITL 2 PLANCTOMYCETES SPECIES, THERMOGUTTA TERRIFONTIS.
JRNL REF FEBS J. 2015
JRNL REFN ESSN 1742-4658
JRNL PMID 26011036
JRNL DOI 10.1111/FEBS.13326
REMARK 2
REMARK 2 RESOLUTION. 1.07 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0103
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) : 1.07
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.48
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.15
REMARK 3 NUMBER OF REFLECTIONS : 95076
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) : 0.09443
REMARK 3 R VALUE (WORKING SET) : 0.09351
REMARK 3 FREE R VALUE : 0.11203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.9
REMARK 3 FREE R VALUE TEST SET COUNT : 4856
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) : 1.070
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.098
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3847
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 50.67
REMARK 3 BIN R VALUE (WORKING SET) : 0.132
REMARK 3 BIN FREE R VALUE SET COUNT : 232
REMARK 3 BIN FREE R VALUE : 0.156
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2625
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 364
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.802
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.02
REMARK 3 B22 (A**2) : 0.02
REMARK 3 B33 (A**2) : -0.06
REMARK 3 B12 (A**2) : 0.01
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): 0.022
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.022
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.012
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.521
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.985
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.982
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2775 ; 0.014 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2810 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3866 ; 1.836 ; 2.000
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6575 ; 1.062 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 410 ; 5.809 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 146 ;28.688 ;22.397
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 552 ;13.925 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 45 ;16.862 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 425 ; 0.105 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3271 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 646 ; 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): 1276 ; 6.857 ; 2.697
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1273 ; 6.867 ; 2.686
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1635 ; 7.314 ; 4.605
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1499 ; 5.706 ; 3.783
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): 5584 ; 2.896 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 41 ;32.712 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 5784 ;12.171 ; 5.000
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 4UHD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-MAR-15.
REMARK 100 THE PDBE ID CODE IS EBI-63374.
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
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 99937
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.07
REMARK 200 RESOLUTION RANGE LOW (A) : 37.48
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.5
REMARK 200 DATA REDUNDANCY : 9.1
REMARK 200 R MERGE (I) : 0.03
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 33.30
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.07
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 51.1
REMARK 200 DATA REDUNDANCY IN SHELL : 5.5
REMARK 200 R MERGE FOR SHELL (I) : 0.28
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.60
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 2XUA
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.3
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 151.52667
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 75.76333
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 75.76333
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 151.52667
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2085 LIES ON A SPECIAL POSITION.
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 GLY A 276
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 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 OE1B GLU A 21 O HOH A 2045 2.16
REMARK 500 OE2B GLU A 21 O HOH A 2044 1.91
REMARK 500 NH1B ARG A 46 O HOH A 2080 2.00
REMARK 500 CD B GLU A 48 O HOH A 2095 1.78
REMARK 500 OE1B GLU A 48 O HOH A 2095 0.86
REMARK 500 OE2B GLU A 48 O HOH A 2097 1.63
REMARK 500 NE A ARG A 112 O HOH A 2158 1.78
REMARK 500 CZ A ARG A 112 O HOH A 2158 1.63
REMARK 500 NH1A ARG A 112 O HOH A 2160 1.48
REMARK 500 NH2A ARG A 112 O HOH A 2158 1.18
REMARK 500 NH1B ARG A 112 O HOH A 2137 1.87
REMARK 500 OD1B ASP A 116 O HOH A 2163 1.74
REMARK 500 OD1B ASP A 116 O HOH A 2169 1.88
REMARK 500 CZ B ARG A 117 O HOH A 2170 1.09
REMARK 500 NH1B ARG A 117 O HOH A 2169 1.48
REMARK 500 NH1B ARG A 117 O HOH A 2170 1.90
REMARK 500 NH2B ARG A 117 O HOH A 2170 0.44
REMARK 500 CZ B ARG A 127 O HOH A 2154 1.32
REMARK 500 NH1B ARG A 127 O HOH A 2154 1.70
REMARK 500 NH2B ARG A 127 O HOH A 2154 1.00
REMARK 500 NH1A ARG A 129 CG A GLU A 229 2.19
REMARK 500 NH1A ARG A 129 CD A GLU A 229 2.17
REMARK 500 NH1A ARG A 129 OE2A GLU A 229 1.67
REMARK 500 NH2C ARG A 129 O HOH A 2181 2.04
REMARK 500 CD A GLU A 134 O HOH A 2191 1.17
REMARK 500 OE1A GLU A 134 O HOH A 2191 0.69
REMARK 500 OE2A GLU A 134 O HOH A 2191 1.77
REMARK 500 CD B GLU A 134 O HOH A 2188 1.20
REMARK 500 OE1B GLU A 134 O HOH A 2188 0.76
REMARK 500 OE2B GLU A 134 O HOH A 2188 1.62
REMARK 500 OD1B ASN A 138 O HOH A 2190 1.95
REMARK 500 CD A ARG A 141 O HOH A 2201 1.89
REMARK 500 CG B ARG A 141 O HOH A 2209 2.09
REMARK 500 CD B ARG A 141 O HOH A 2209 2.13
REMARK 500 NH1B ARG A 141 O HOH A 2209 1.95
REMARK 500 OE1A GLU A 144 O HOH A 2212 1.77
REMARK 500 NH1A ARG A 145 O HOH A 2210 1.94
REMARK 500 CD B ARG A 148 O HOH A 2221 1.32
REMARK 500 NE B ARG A 148 O HOH A 2221 1.62
REMARK 500 CZ B ARG A 148 O HOH A 2221 2.03
REMARK 500 NH1B ARG A 148 O HOH A 2221 2.15
REMARK 500 NH1B ARG A 148 O HOH A 2222 1.57
REMARK 500 NH2B ARG A 148 O B HOH A 2213 1.74
REMARK 500 CZ C ARG A 148 O HOH A 2223 1.92
REMARK 500 NH1C ARG A 148 O HOH A 2223 1.11
REMARK 500 CD A GLU A 149 O HOH A 2215 1.64
REMARK 500 OE2A GLU A 149 O HOH A 2215 0.67
REMARK 500 CD B GLU A 165 O HOH A 2238 1.64
REMARK 500 OE2B GLU A 165 O HOH A 2238 0.52
REMARK 500 CD B GLU A 176 O HOH A 2250 2.00
REMARK 500
REMARK 500 THIS ENTRY HAS 121 CLOSE CONTACTS
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 CG2B THR A 12 NZ A LYS A 270 1655 2.00
REMARK 500 CG B PRO A 70 OE1B GLN A 262 1655 2.03
REMARK 500 ND1B HIS A 88 ND1B HIS A 88 4555 1.42
REMARK 500 ND1B HIS A 88 CE1B HIS A 88 4555 1.83
REMARK 500 CE1B HIS A 88 CE1B HIS A 88 4555 2.02
REMARK 500 CD B GLU A 134 OE1B GLU A 165 6444 1.87
REMARK 500 OE2B GLU A 134 OE1B GLU A 165 6444 1.28
REMARK 500 CZ B ARG A 140 CZ B ARG A 140 6554 1.47
REMARK 500 CZ B ARG A 140 NH2B ARG A 140 6554 1.49
REMARK 500 CZ B ARG A 140 NH1B ARG A 140 6554 1.35
REMARK 500 NH1B ARG A 140 NH2B ARG A 140 6554 0.48
REMARK 500 NH2A ARG A 141 CD B GLU A 144 6554 2.17
REMARK 500 NH1B ARG A 147 OD2A ASP A 247 1655 1.72
REMARK 500 CD A GLU A 188 NH2A ARG A 259 1655 1.49
REMARK 500 CD A GLU A 188 NH2C ARG A 259 1655 1.89
REMARK 500 OE1A GLU A 188 NH2C ARG A 259 1655 2.17
REMARK 500 OE2A GLU A 188 CZ A ARG A 259 1655 1.53
REMARK 500 OE2A GLU A 188 NH2A ARG A 259 1655 0.39
REMARK 500 OE2A GLU A 188 CZ C ARG A 259 1655 2.18
REMARK 500 OE2A GLU A 188 NH2C ARG A 259 1655 1.18
REMARK 500 OD1A ASP A 247 O B HOH A 2213 1455 2.12
REMARK 500 O HOH A 2014 O HOH A 2014 4555 1.59
REMARK 500 O HOH A 2015 O HOH A 2015 4555 1.72
REMARK 500 O HOH A 2085 O HOH A 2086 6554 1.65
REMARK 500 O HOH A 2086 O HOH A 2086 6554 0.58
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 LEU A 37 -155.13 -107.80
REMARK 500 SER A 101 -110.17 56.80
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1277 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2316 O
REMARK 620 2 HOH A2326 O 94.4
REMARK 620 3 SER A 240 OG 91.4 79.7
REMARK 620 4 ILE A 237 O 178.0 84.1 89.8
REMARK 620 5 HOH A2317 O 89.4 95.8 175.5 89.4
REMARK 620 6 ALA A 234 O 91.7 163.1 84.5 90.1 100.0
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1276
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 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 ACT A1279
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1280
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1281
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4UHC RELATED DB: PDB
REMARK 900 STRUCTURAL STUDIES OF A THERMOPHILIC ESTERASE FROM
REMARK 900 THERMOGUTTA TERRIFONTIS (NATIVE)
REMARK 900 RELATED ID: 4UHE RELATED DB: PDB
REMARK 900 STRUCTURAL STUDIES OF A THERMOPHILIC ESTERASE FROM
REMARK 900 THERMOGUTTA TERRIFONTIS (MALATE BOUND)
REMARK 900 RELATED ID: 4UHF RELATED DB: PDB
REMARK 900 STRUCTURAL STUDIES OF A THERMOPHILIC ESTERASE FROM
REMARK 900 THERMOGUTTA TERRIFONTIS (L37A MUTANT WITH BUTYRATE BOUND)
REMARK 900 RELATED ID: 4UHH RELATED DB: PDB
REMARK 900 STRUCTURAL STUDIES OF A THERMOPHILIC ESTERASE FROM
REMARK 900 THERMOGUTTA TERRIFONTIS (CACODYLATE COMPLEX)
DBREF 4UHD A 1 282 PDB 4UHD 4UHD 1 282
SEQRES 1 A 282 MET ALA GLN ARG VAL LYS ILE THR THR THR ALA THR PRO
SEQRES 2 A 282 GLY GLU ILE GLU LEU ALA PHE GLU ASP THR GLY THR GLY
SEQRES 3 A 282 LEU PRO VAL LEU LEU VAL HIS GLY PHE PRO LEU ASP ARG
SEQRES 4 A 282 THR MET TRP LYS ALA GLN ARG GLU GLU LEU CYS ASP GLU
SEQRES 5 A 282 PHE ARG VAL ILE VAL PRO ASP LEU ARG GLY PHE GLY GLU
SEQRES 6 A 282 SER GLN VAL ILE PRO GLY VAL ALA THR MET GLU ALA MET
SEQRES 7 A 282 ALA ASP ASP LEU ALA GLY LEU CYS ASN HIS LEU GLY LEU
SEQRES 8 A 282 THR GLY LYS ILE VAL LEU GLY GLY LEU SER MET GLY GLY
SEQRES 9 A 282 TYR VAL ALA PHE ALA PHE ALA ARG LYS TYR ARG ASP ARG
SEQRES 10 A 282 LEU ALA GLY LEU ILE LEU CYS ASP THR ARG ALA ARG PRO
SEQRES 11 A 282 ASP SER PRO GLU ALA LYS GLU ASN ARG ARG ARG VAL ALA
SEQRES 12 A 282 GLU ARG VAL ARG ARG GLU GLY PRO GLY PHE ILE ALA GLU
SEQRES 13 A 282 GLU MET ILE PRO ARG LEU CYS CYS GLU SER THR PHE ARG
SEQRES 14 A 282 ASN HIS PRO GLU VAL ILE GLU LYS ILE ARG GLN MET ILE
SEQRES 15 A 282 LEU SER ALA PRO PRO GLU GLY VAL ALA ALA ALA ALA LEU
SEQRES 16 A 282 GLY MET ALA GLU ARG PRO ASP SER THR ASP LEU LEU PRO
SEQRES 17 A 282 ALA LEU SER CYS PRO THR LEU VAL LEU VAL GLY GLN PHE
SEQRES 18 A 282 ASP ALA ILE SER PRO PRO GLU GLU MET GLU ALA MET ALA
SEQRES 19 A 282 ARG THR ILE PRO GLN SER GLN PHE VAL VAL ILE PRO ASP
SEQRES 20 A 282 ALA GLY HIS LEU PRO PRO MET GLU GLN PRO GLU ARG VAL
SEQRES 21 A 282 THR GLN ALA ILE ARG GLU TRP LEU ARG LYS VAL HIS THR
SEQRES 22 A 282 GLU ALA GLY HIS HIS HIS HIS HIS HIS
HET CL A1276 1
HET MG A1277 1
HET ACT A1278 4
HET ACT A1279 4
HET PEG A1280 7
HET PEG A1281 7
HETNAM CL CHLORIDE ION
HETNAM ACT ACETATE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM MG MAGNESIUM ION
FORMUL 2 CL CL 1-
FORMUL 3 ACT 2(C2 H3 O2 1-)
FORMUL 4 PEG 2(C4 H10 O3)
FORMUL 5 MG MG 2+
FORMUL 6 HOH *364(H2 O)
HELIX 1 1 ASP A 38 MET A 41 5 4
HELIX 2 2 TRP A 42 CYS A 50 1 9
HELIX 3 3 THR A 74 GLY A 90 1 17
HELIX 4 4 SER A 101 TYR A 114 1 14
HELIX 5 5 SER A 132 GLY A 150 1 19
HELIX 6 6 PRO A 151 CYS A 163 1 13
HELIX 7 7 CYS A 164 HIS A 171 1 8
HELIX 8 8 HIS A 171 SER A 184 1 14
HELIX 9 9 PRO A 186 ARG A 200 1 15
HELIX 10 10 SER A 203 LEU A 210 5 8
HELIX 11 11 PRO A 226 ARG A 235 1 10
HELIX 12 12 LEU A 251 GLN A 256 1 6
HELIX 13 13 GLN A 256 ALA A 275 1 20
SHEET 1 AA 8 GLN A 3 THR A 8 0
SHEET 2 AA 8 GLU A 15 THR A 23 -1 O ILE A 16 N ILE A 7
SHEET 3 AA 8 ARG A 54 PRO A 58 -1 O VAL A 55 N THR A 23
SHEET 4 AA 8 PRO A 28 VAL A 32 1 O VAL A 29 N ILE A 56
SHEET 5 AA 8 ILE A 95 LEU A 100 1 O VAL A 96 N LEU A 30
SHEET 6 AA 8 LEU A 118 CYS A 124 1 N ALA A 119 O ILE A 95
SHEET 7 AA 8 THR A 214 GLY A 219 1 O LEU A 215 N LEU A 123
SHEET 8 AA 8 SER A 240 ILE A 245 1 O GLN A 241 N VAL A 216
LINK MG MG A1277 O HOH A2316 1555 1555 2.40
LINK MG MG A1277 O HOH A2326 1555 1555 2.57
LINK MG MG A1277 OG SER A 240 1555 1555 2.34
LINK MG MG A1277 O ILE A 237 1555 1555 2.32
LINK MG MG A1277 O HOH A2317 1555 1555 2.35
LINK MG MG A1277 O ALA A 234 1555 1555 2.43
CISPEP 1 THR A 12 PRO A 13 0 6.19
CISPEP 2 PHE A 35 PRO A 36 0 -16.19
SITE 1 AC1 5 LYS A 43 ARG A 46 HOH A2044 HOH A2045
SITE 2 AC1 5 HOH A2075
SITE 1 AC2 6 ALA A 234 ILE A 237 SER A 240 HOH A2316
SITE 2 AC2 6 HOH A2317 HOH A2326
SITE 1 AC3 8 GLY A 34 PHE A 35 SER A 101 MET A 102
SITE 2 AC3 8 HIS A 250 ACT A1279 HOH A2362 HOH A2363
SITE 1 AC4 6 SER A 101 TYR A 105 ARG A 139 ACT A1278
SITE 2 AC4 6 HOH A2178 HOH A2362
SITE 1 AC5 12 SER A 132 PRO A 133 PRO A 160 ARG A 161
SITE 2 AC5 12 CYS A 163 CYS A 164 PHE A 221 ALA A 223
SITE 3 AC5 12 HOH A2188 HOH A2193 HOH A2233 HOH A2364
SITE 1 AC6 6 GLN A 3 GLU A 21 ASP A 22 HOH A2050
SITE 2 AC6 6 HOH A2051 HOH A2052
CRYST1 43.280 43.280 227.290 90.00 90.00 120.00 P 32 2 1 6
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 0.023105 0.013340 0.000000 0.00000
SCALE2 0.000000 0.026680 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004400 0.00000
TER 2626 ALA A 275
MASTER 438 0 6 13 8 0 13 6 3015 1 30 22
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