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PDBsum entry 2zth

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Transferase PDB id
2zth
Jmol
Contents
Protein chain
206 a.a.
Ligands
SAM
Metals
_MG
Waters ×42
HEADER    TRANSFERASE                             01-OCT-08   2ZTH
TITLE     CRYSTAL STRUCTURE OF HOLO FORM OF RAT CATECHOL-O-
TITLE    2 METHYLTRANSFERASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CATECHOL O-METHYLTRANSFERASE;
COMPND   3 CHAIN: A;
COMPND   4 EC: 2.1.1.6;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE   3 ORGANISM_COMMON: BROWN RAT,RAT,RATS;
SOURCE   4 ORGANISM_TAXID: 10116;
SOURCE   5 GENE: LIVER;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS    S-ADENOSYLMETHIONINE DEPENDENT METHYLTRANSFERASE,
KEYWDS   2 ALTERNATIVE INITIATION, CATECHOLAMINE METABOLISM, CELL
KEYWDS   3 MEMBRANE, CYTOPLASM, MAGNESIUM, MEMBRANE, METAL-BINDING,
KEYWDS   4 METHYLTRANSFERASE, NEUROTRANSMITTER DEGRADATION,
KEYWDS   5 PHOSPHOPROTEIN, S-ADENOSYL-L-METHIONINE, SIGNAL-ANCHOR,
KEYWDS   6 TRANSFERASE, TRANSMEMBRANE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    E.TSUJI
REVDAT   2   24-MAR-09 2ZTH    1       JRNL   REMARK
REVDAT   1   13-JAN-09 2ZTH    0
JRNL        AUTH   E.TSUJI,K.OKAZAKI,M.ISAJI,K.TAKEDA
JRNL        TITL   CRYSTAL STRUCTURES OF THE APO AND HOLO FORM OF RAT
JRNL        TITL 2 CATECHOL-O-METHYLTRANSFERASE
JRNL        REF    J.STRUCT.BIOL.                V. 165   133 2009
JRNL        REFN                   ISSN 1047-8477
JRNL        PMID   19111934
JRNL        DOI    10.1016/J.JSB.2008.11.012
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0005
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.90
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4
REMARK   3   NUMBER OF REFLECTIONS             : 6225
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) : 0.196
REMARK   3   R VALUE            (WORKING SET) : 0.187
REMARK   3   FREE R VALUE                     : 0.281
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 688
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) : 2.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 421
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.09
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2480
REMARK   3   BIN FREE R VALUE SET COUNT          : 45
REMARK   3   BIN FREE R VALUE                    : 0.4030
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1615
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 42
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 45.10
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.26
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 2.88000
REMARK   3    B22 (A**2) : -2.29000
REMARK   3    B33 (A**2) : -0.59000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.395
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.262
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.401
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.883
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1674 ; 0.016 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2272 ; 2.002 ; 2.011
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   204 ; 7.673 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    73 ;39.161 ;24.795
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   290 ;21.487 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ;26.961 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   260 ; 0.177 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1250 ; 0.006 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   801 ; 0.244 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1089 ; 0.315 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    68 ; 0.180 ; 0.200
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):    62 ; 0.262 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     2 ; 0.206 ; 0.200
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):  1065 ; 0.720 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1657 ; 1.279 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   707 ; 1.733 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   615 ; 2.676 ; 4.500
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 : BABINET MODEL WITH 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 2ZTH COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-OCT-08.
REMARK 100 THE RCSB ID CODE IS RCSB028404.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 26-MAY-03
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SPRING-8
REMARK 200  BEAMLINE                       : BL32B2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU JUPITER 210
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6906
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 52.850
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : 6.800
REMARK 200  R MERGE                    (I) : 0.10100
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 14.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.37400
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 5.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1VID
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 42.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M (NH4)2SO4, 26% PEG 8000, 0.2%
REMARK 280  SUCROSE, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280  298K
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       16.45150
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       52.68450
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       30.54450
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       52.68450
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       16.45150
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       30.54450
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     GLY A    -1
REMARK 465     SER A     0
REMARK 465     MET A     1
REMARK 465     GLY A     2
REMARK 465     LYS A    36
REMARK 465     GLU A    37
REMARK 465     TRP A    38
REMARK 465     ALA A    39
REMARK 465     MET A    40
REMARK 465     ASN A    41
REMARK 465     PRO A   215
REMARK 465     SER A   216
REMARK 465     SER A   217
REMARK 465     PRO A   218
REMARK 465     ASP A   219
REMARK 465     LYS A   220
REMARK 465     SER A   221
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     LYS A  46    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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   ATM2   ATM3
REMARK 500    ILE A 172   CG1 -  CB  -  CG2 ANGL. DEV. = -16.9 DEGREES
REMARK 500    ILE A 172   C   -  N   -  CA  ANGL. DEV. =  17.9 DEGREES
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    LYS A  46      -12.80    -48.24
REMARK 500    TYR A  68      -93.82    -88.45
REMARK 500    ASP A 133      -84.76    -81.61
REMARK 500    ASP A 141       25.69   -147.18
REMARK 500    HIS A 142     -138.42   -100.52
REMARK 500    ASN A 170       65.50     64.87
REMARK 500    ILE A 172     -103.32    117.23
REMARK 500    THR A 176       34.75     75.47
REMARK 500    ASP A 205     -166.94   -126.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 VAL A  171     ILE A  172                  -33.48
REMARK 500 PRO A  174     GLY A  175                 -145.03
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 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: (11X,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     VAL A 171        21.9      L          L   OUTSIDE RANGE
REMARK 500     ILE A 172         6.5      L          D   EXPECTING SP3
REMARK 500     THR A 176        21.8      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 352        DISTANCE =  5.50 ANGSTROMS
REMARK 525    HOH A 358        DISTANCE =  5.74 ANGSTROMS
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 A 300  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 141   OD1
REMARK 620 2 ASN A 170   OD1  94.5
REMARK 620 N                    1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 300
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAM A 305
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1VID   RELATED DB: PDB
REMARK 900 J.VIDGREN,L.A.SVENSSON,A.LILJAS. CRYSTAL STRUCTURE OF
REMARK 900 CATECHOL O-METHYLTRANSFERASE. NATURE V. 368 354 1994
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE OF THIS ENTITY WAS BASED ON ISOFORM 2 OF UNIPROTKB/
REMARK 999 SWISS-PROT P22734 (COMT_RAT). UNP-RESIDUES 1-43 WERE MISSING IN
REMARK 999 ISOFORM-2.
DBREF  2ZTH A    1   221  UNP    P22734   COMT_RAT        44    264
SEQADV 2ZTH GLY A   -1  UNP  P22734              EXPRESSION TAG
SEQADV 2ZTH SER A    0  UNP  P22734              EXPRESSION TAG
SEQRES   1 A  223  GLY SER MET GLY ASP THR LYS GLU GLN ARG ILE LEU ARG
SEQRES   2 A  223  TYR VAL GLN GLN ASN ALA LYS PRO GLY ASP PRO GLN SER
SEQRES   3 A  223  VAL LEU GLU ALA ILE ASP THR TYR CYS THR GLN LYS GLU
SEQRES   4 A  223  TRP ALA MET ASN VAL GLY ASP ALA LYS GLY GLN ILE MET
SEQRES   5 A  223  ASP ALA VAL ILE ARG GLU TYR SER PRO SER LEU VAL LEU
SEQRES   6 A  223  GLU LEU GLY ALA TYR CYS GLY TYR SER ALA VAL ARG MET
SEQRES   7 A  223  ALA ARG LEU LEU GLN PRO GLY ALA ARG LEU LEU THR MET
SEQRES   8 A  223  GLU MET ASN PRO ASP TYR ALA ALA ILE THR GLN GLN MET
SEQRES   9 A  223  LEU ASN PHE ALA GLY LEU GLN ASP LYS VAL THR ILE LEU
SEQRES  10 A  223  ASN GLY ALA SER GLN ASP LEU ILE PRO GLN LEU LYS LYS
SEQRES  11 A  223  LYS TYR ASP VAL ASP THR LEU ASP MET VAL PHE LEU ASP
SEQRES  12 A  223  HIS TRP LYS ASP ARG TYR LEU PRO ASP THR LEU LEU LEU
SEQRES  13 A  223  GLU LYS CYS GLY LEU LEU ARG LYS GLY THR VAL LEU LEU
SEQRES  14 A  223  ALA ASP ASN VAL ILE VAL PRO GLY THR PRO ASP PHE LEU
SEQRES  15 A  223  ALA TYR VAL ARG GLY SER SER SER PHE GLU CYS THR HIS
SEQRES  16 A  223  TYR SER SER TYR LEU GLU TYR MET LYS VAL VAL ASP GLY
SEQRES  17 A  223  LEU GLU LYS ALA ILE TYR GLN GLY PRO SER SER PRO ASP
SEQRES  18 A  223  LYS SER
HET     MG  A 300       1
HET    SAM  A 305      27
HETNAM      MG MAGNESIUM ION
HETNAM     SAM S-ADENOSYLMETHIONINE
FORMUL   2   MG    MG 2+
FORMUL   3  SAM    C15 H22 N6 O5 S
FORMUL   4  HOH   *42(H2 O)
HELIX    1   1 GLU A    6  ALA A   17  1                                  12
HELIX    2   2 ASP A   21  CYS A   33  1                                  13
HELIX    3   3 ASP A   44  SER A   58  1                                  15
HELIX    4   4 GLY A   70  ARG A   78  1                                   9
HELIX    5   5 ASN A   92  GLY A  107  1                                  16
HELIX    6   6 ALA A  118  ILE A  123  1                                   6
HELIX    7   7 PRO A  124  LEU A  126  5                                   3
HELIX    8   8 TRP A  143  ASP A  145  5                                   3
HELIX    9   9 ARG A  146  CYS A  157  1                                  12
HELIX   10  10 THR A  176  SER A  186  1                                  11
SHEET    1   A 7 VAL A 112  ASN A 116  0
SHEET    2   A 7 ARG A  85  GLU A  90  1  N  THR A  88   O  LEU A 115
SHEET    3   A 7 LEU A  61  LEU A  65  1  N  GLU A  64   O  MET A  89
SHEET    4   A 7 LEU A 135  LEU A 140  1  O  PHE A 139   N  LEU A  65
SHEET    5   A 7 LEU A 160  ALA A 168  1  O  LEU A 167   N  LEU A 140
SHEET    6   A 7 VAL A 203  TYR A 212 -1  O  TYR A 212   N  GLY A 163
SHEET    7   A 7 PHE A 189  LEU A 198 -1  N  SER A 196   O  ASP A 205
LINK         OD1 ASP A 141                MG    MG A 300     1555   1555  2.41
LINK         OD1 ASN A 170                MG    MG A 300     1555   1555  2.23
CISPEP   1 VAL A  173    PRO A  174          0        -7.27
SITE     1 AC1  3 ASP A 141  ASP A 169  ASN A 170
SITE     1 AC2 18 VAL A  42  GLY A  66  ALA A  67  TYR A  68
SITE     2 AC2 18 TYR A  71  SER A  72  GLU A  90  MET A  91
SITE     3 AC2 18 TYR A  95  GLY A 117  ALA A 118  SER A 119
SITE     4 AC2 18 GLN A 120  ASP A 141  HIS A 142  TRP A 143
SITE     5 AC2 18 ARG A 146  HOH A 358
CRYST1   32.903   61.089  105.369  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      0.030392  0.000000  0.000000        0.00000
SCALE2      0.000000  0.016370  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009490        0.00000
      
PROCHECK
Go to PROCHECK summary
 References