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PDBsum entry 3ozs

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Transferase/transferase inhibitor PDB id
3ozs
Jmol
Contents
Protein chain
213 a.a.
Ligands
OZS
Metals
_MG
Waters ×104
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       27-SEP-10   3OZS
TITLE     RAT CATECHOL O-METHYLTRANSFERASE IN COMPLEX WITH A CATECHOL-TYPE,
TITLE    2 TRIFLUOROMETHYL-IMIDAZOLYL-CONTAINING INHIBITOR - HUMANIZED FORM
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CATECHOL O-METHYLTRANSFERASE;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: SOLUBLE FORM, UNP RESIDUES 44-264;
COMPND   5 EC: 2.1.1.6;
COMPND   6 ENGINEERED: YES;
COMPND   7 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE   3 ORGANISM_COMMON: RAT;
SOURCE   4 ORGANISM_TAXID: 10116;
SOURCE   5 TISSUE: LIVER;
SOURCE   6 GENE: COMT;
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PDS56/RBSII
KEYWDS    METHYLTRANSFERASE, NEUROTRANSMITTER DEGRADATION, ALTERNATIVE
KEYWDS   2 INITIATION, CATECHOLAMINE METABOLISM, CELL MEMBRANE, MAGNESIUM,
KEYWDS   3 METAL-BINDING, S-ADENOSYL-L-METHIONINE, SIGNAL-ANCHOR, TRANSFERASE,
KEYWDS   4 TRANSMEMBRANE METHYLTRANSFERASE, TRANSFERASE-TRANSFERASE INHIBITOR
KEYWDS   5 COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.EHLER,D.SCHLATTER,M.STIHLE,J.BENZ,M.G.RUDOLPH
REVDAT   4   15-AUG-12 3OZS    1       TITLE
REVDAT   3   23-MAY-12 3OZS    1       AUTHOR VERSN
REVDAT   2   01-JUN-11 3OZS    1       JRNL
REVDAT   1   16-MAR-11 3OZS    0
JRNL        AUTH   M.ELLERMANN,R.PAULINI,R.JAKOB-ROETNE,C.LERNER,E.BORRONI,
JRNL        AUTH 2 D.ROTH,A.EHLER,W.B.SCHWEIZER,D.SCHLATTER,M.G.RUDOLPH,
JRNL        AUTH 3 F.DIEDERICH
JRNL        TITL   MOLECULAR RECOGNITION AT THE ACTIVE SITE OF
JRNL        TITL 2 CATECHOL-O-METHYLTRANSFERASE (COMT): ADENINE REPLACEMENTS IN
JRNL        TITL 3 BISUBSTRATE INHIBITORS
JRNL        REF    CHEMISTRY                     V.  17  6369 2011
JRNL        REFN                   ISSN 0947-6539
JRNL        PMID   21538606
JRNL        DOI    10.1002/CHEM.201003648
REMARK   2
REMARK   2 RESOLUTION.    1.44 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.6.0081
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) : 1.44
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.91
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.4
REMARK   3   NUMBER OF REFLECTIONS             : 42052
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) : 0.181
REMARK   3   R VALUE            (WORKING SET) : 0.180
REMARK   3   FREE R VALUE                     : 0.209
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 2201
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) : 1.44
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.48
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2726
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 85.61
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3630
REMARK   3   BIN FREE R VALUE SET COUNT          : 141
REMARK   3   BIN FREE R VALUE                    : 0.3350
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1673
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 34
REMARK   3   SOLVENT ATOMS            : 103
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.63
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.44000
REMARK   3    B22 (A**2) : 0.44000
REMARK   3    B33 (A**2) : -0.67000
REMARK   3    B12 (A**2) : 0.22000
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): 0.066
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.054
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.451
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.977
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.971
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1804 ; 0.022 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  1197 ; 0.004 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2466 ; 1.923 ; 2.009
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2954 ; 1.040 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   232 ; 5.773 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    76 ;37.467 ;24.868
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   325 ;12.899 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ;17.987 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   281 ; 0.123 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1991 ; 0.010 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):   335 ; 0.001 ; 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):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL
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 : 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 USED IF PRESENT IN
REMARK   3  THE INPUT U VALUES: REFINED INDIVIDUALLY
REMARK   4
REMARK   4 3OZS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-OCT-10.
REMARK 100 THE RCSB ID CODE IS RCSB061777.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-AUG-10
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 9
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SLS
REMARK 200  BEAMLINE                       : X10SA
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : PIXEL
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS (VERSION DECEMBER 28, 2009)
REMARK 200  DATA SCALING SOFTWARE          : SADABS
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46330
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.440
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.510
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7
REMARK 200  DATA REDUNDANCY                : 9.690
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 14.3900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.44
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.54
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.80
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: INHOUSE MODEL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 51.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, CHES, PH 9, VAPOR
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 300K
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      111.63800
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       55.81900
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       55.81900
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      111.63800
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL
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 350   BIOMT1   2 -0.500000  0.866025  0.000000      -76.11750
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000       43.94646
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A     1
REMARK 465     GLY A     2
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 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   OE2  GLU A    64     OG   SER A    72              2.16
REMARK 500
REMARK 500 REMARK: NULL
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    ARG A  75   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 DEGREES
REMARK 500    ARG A  78   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    TYR A 147   CB  -  CG  -  CD1 ANGL. DEV. =   3.6 DEGREES
REMARK 500    MET A 201   CG  -  SD  -  CE  ANGL. DEV. = -10.6 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    MET A  40       42.59    -77.31
REMARK 500    TYR A  68     -111.04     61.44
REMARK 500    ASP A 133      -83.43    -98.90
REMARK 500    ASP A 141       31.90   -154.03
REMARK 500    HIS A 142     -151.29   -100.74
REMARK 500    SER A 196     -143.61   -154.87
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 309        DISTANCE =  5.26 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 222  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 141   OD1
REMARK 620 2 HOH A 236   O    93.0
REMARK 620 3 ASP A 169   OD2  93.2  92.1
REMARK 620 4 ASN A 170   OD1  92.5 173.2  83.6
REMARK 620 5 OZS A 223   O26  89.1 100.8 166.8  83.2
REMARK 620 6 OZS A 223   O27 167.6  88.0  99.1  87.5  78.6
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 MG A 222
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OZS A 223
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3NW9   RELATED DB: PDB
REMARK 900 RELATED ID: 3NWB   RELATED DB: PDB
REMARK 900 RELATED ID: 3NWE   RELATED DB: PDB
REMARK 900 RELATED ID: 3OZR   RELATED DB: PDB
REMARK 900 RELATED ID: 3OZT   RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE RAT COMT WAS HUMANIZED, AND RESIDUE 91 ILE AND 95 CYS ARE HUMAN
REMARK 999 SEQUENCE REFERING TO ISOFORM 2 OF P21964 (COMT_HUMAN).
DBREF  3OZS A    1   221  UNP    P22734   COMT_RAT        44    264
SEQADV 3OZS ILE A   91  UNP  P22734    MET   134 ENGINEERED MUTATION
SEQADV 3OZS CYS A   95  UNP  P22734    TYR   138 ENGINEERED MUTATION
SEQRES   1 A  221  MET GLY ASP THR LYS GLU GLN ARG ILE LEU ARG TYR VAL
SEQRES   2 A  221  GLN GLN ASN ALA LYS PRO GLY ASP PRO GLN SER VAL LEU
SEQRES   3 A  221  GLU ALA ILE ASP THR TYR CYS THR GLN LYS GLU TRP ALA
SEQRES   4 A  221  MET ASN VAL GLY ASP ALA LYS GLY GLN ILE MET ASP ALA
SEQRES   5 A  221  VAL ILE ARG GLU TYR SER PRO SER LEU VAL LEU GLU LEU
SEQRES   6 A  221  GLY ALA TYR CYS GLY TYR SER ALA VAL ARG MET ALA ARG
SEQRES   7 A  221  LEU LEU GLN PRO GLY ALA ARG LEU LEU THR MET GLU ILE
SEQRES   8 A  221  ASN PRO ASP CYS ALA ALA ILE THR GLN GLN MET LEU ASN
SEQRES   9 A  221  PHE ALA GLY LEU GLN ASP LYS VAL THR ILE LEU ASN GLY
SEQRES  10 A  221  ALA SER GLN ASP LEU ILE PRO GLN LEU LYS LYS LYS TYR
SEQRES  11 A  221  ASP VAL ASP THR LEU ASP MET VAL PHE LEU ASP HIS TRP
SEQRES  12 A  221  LYS ASP ARG TYR LEU PRO ASP THR LEU LEU LEU GLU LYS
SEQRES  13 A  221  CYS GLY LEU LEU ARG LYS GLY THR VAL LEU LEU ALA ASP
SEQRES  14 A  221  ASN VAL ILE VAL PRO GLY THR PRO ASP PHE LEU ALA TYR
SEQRES  15 A  221  VAL ARG GLY SER SER SER PHE GLU CYS THR HIS TYR SER
SEQRES  16 A  221  SER TYR LEU GLU TYR MET LYS VAL VAL ASP GLY LEU GLU
SEQRES  17 A  221  LYS ALA ILE TYR GLN GLY PRO SER SER PRO ASP LYS SER
HET     MG  A 222       1
HET    OZS  A 223      33
HETNAM      MG MAGNESIUM ION
HETNAM     OZS N-[(E)-3-[(2R,3S,4R,5R)-3,4-DIHYDROXY-5-[4-
HETNAM   2 OZS  (TRIFLUOROMETHYL)IMIDAZOL-1-YL]OXOLAN-2-YL]PROP-2-
HETNAM   3 OZS  ENYL]-2,3-DIHYDROXY-5-NITRO-BENZAMIDE
FORMUL   2   MG    MG 2+
FORMUL   3  OZS    C18 H17 F3 N4 O8
FORMUL   4  HOH   *103(H2 O)
HELIX    1   1 THR A    4  ALA A   17  1                                  14
HELIX    2   2 ASP A   21  LYS A   36  1                                  16
HELIX    3   3 VAL A   42  SER A   58  1                                  17
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 LEU A  108  ASP A  110  5                                   3
HELIX    7   7 ALA A  118  ILE A  123  1                                   6
HELIX    8   8 GLN A  125  ASP A  131  1                                   7
HELIX    9   9 TRP A  143  ASP A  145  5                                   3
HELIX   10  10 ARG A  146  CYS A  157  1                                  12
HELIX   11  11 THR A  176  SER A  186  1                                  11
SHEET    1   A 5 VAL A 112  ASN A 116  0
SHEET    2   A 5 ARG A  85  GLU A  90  1  N  THR A  88   O  LEU A 115
SHEET    3   A 5 LEU A  61  LEU A  65  1  N  GLU A  64   O  MET A  89
SHEET    4   A 5 MET A 137  LEU A 140  1  O  PHE A 139   N  LEU A  65
SHEET    5   A 5 VAL A 165  ALA A 168  1  O  LEU A 167   N  VAL A 138
LINK         OD1 ASP A 141                MG    MG A 222     1555   1555  2.02
LINK        MG    MG A 222                 O   HOH A 236     1555   1555  2.08
LINK         OD2 ASP A 169                MG    MG A 222     1555   1555  2.09
LINK         OD1 ASN A 170                MG    MG A 222     1555   1555  2.10
LINK        MG    MG A 222                 O26 OZS A 223     1555   1555  2.15
LINK        MG    MG A 222                 O27 OZS A 223     1555   1555  2.16
CISPEP   1 VAL A  173    PRO A  174          0        -0.29
SITE     1 AC1  5 ASP A 141  ASP A 169  ASN A 170  OZS A 223
SITE     2 AC1  5 HOH A 236
SITE     1 AC2 21 TRP A  38  MET A  40  GLY A  66  TYR A  68
SITE     2 AC2 21 MET A  89  GLU A  90  ILE A  91  ASN A  92
SITE     3 AC2 21 GLY A 117  SER A 119  ASP A 141  HIS A 142
SITE     4 AC2 21 TRP A 143  LYS A 144  ASP A 169  ASN A 170
SITE     5 AC2 21 PRO A 174  GLU A 199   MG A 222  HOH A 236
SITE     6 AC2 21 HOH A 320
CRYST1   50.745   50.745  167.457  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      0.019706  0.011377  0.000000        0.00000
SCALE2      0.000000  0.022755  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005972        0.00000
      
PROCHECK
Go to PROCHECK summary
 References