longtext: 4UHD-pdb

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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
END