HEADER TRANSFERASE 26-SEP-09 3A7E
TITLE CRYSTAL STRUCTURE OF HUMAN COMT COMPLEXED WITH SAM AND 3,5-
TITLE 2 DINITROCATECHOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATECHOL O-METHYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 51-264;
COMPND 5 EC: 2.1.1.6;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: COMT;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 CODON PLUS (DE3) RP;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS COMT, ALTERNATIVE INITIATION, CATECHOLAMINE METABOLISM, MAGNESIUM,
KEYWDS 2 METHYLTRANSFERASE, NEUROTRANSMITTER DEGRADATION, S-ADENOSYL-L-
KEYWDS 3 METHIONINE, TRANSFERASE, CELL MEMBRANE, MEMBRANE, METAL-BINDING,
KEYWDS 4 PHOSPHOPROTEIN, SIGNAL-ANCHOR, TRANSMEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.TSUJI
REVDAT 2 01-NOV-23 3A7E 1 REMARK SEQADV LINK
REVDAT 1 15-SEP-10 3A7E 0
JRNL AUTH Y.NONAKA,T.MOMOSE,T.OZAWA,M.OZAWA,M.NAKATSU,E.TSUJI,
JRNL AUTH 2 K.OKAZAKI,Y.TAKASE,T.KIYOTANI
JRNL TITL HIT TO LEAD: COMPREHENSIVE STRATEGY OF DE NOVO SCAFFOLD
JRNL TITL 2 GENERATION BY FBDD. PART 1: IN SILICO FRAGMENTS LINKING AND
JRNL TITL 3 VERIFICATION OF SPATIAL PROXIMITY USING INTER LIGAND NOE
JRNL TITL 4 APPROACHS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : 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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 5888
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) : 0.226
REMARK 3 R VALUE (WORKING SET) : 0.218
REMARK 3 FREE R VALUE : 0.298
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 654
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 394
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.1990
REMARK 3 BIN FREE R VALUE SET COUNT : 46
REMARK 3 BIN FREE R VALUE : 0.3430
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1660
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 42
REMARK 3 SOLVENT ATOMS : 46
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.19000
REMARK 3 B22 (A**2) : 0.19000
REMARK 3 B33 (A**2) : -0.29000
REMARK 3 B12 (A**2) : 0.10000
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): 0.471
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.353
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.410
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.899
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.821
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1733 ; 0.005 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2352 ; 0.912 ; 2.001
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 211 ; 4.475 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 76 ;34.618 ;24.868
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 301 ;18.171 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;16.248 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 267 ; 0.067 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1297 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 1059 ; 0.604 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1707 ; 1.195 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 674 ; 1.910 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 645 ; 3.184 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER 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 : 1.40
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3A7E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-SEP-09.
REMARK 100 THE DEPOSITION ID IS D_1000028904.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAR-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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) : 1.54180
REMARK 200 MONOCHROMATOR : SI 111
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 : 6727
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 28.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.16300
REMARK 200 R SYM (I) : 0.13700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.33400
REMARK 200 R SYM FOR SHELL (I) : 0.35200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 12.70
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 (%): 53.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH7.5, 2% (V/V) PEG 400,
REMARK 280 2.0M (NH4)2SO4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 112.12400
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 56.06200
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 56.06200
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 112.12400
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 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 CD1 ILE A 89 O HOH A 263 2.03
REMARK 500 NE2 HIS A 12 O HOH A 260 2.09
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 36 -59.47 -125.45
REMARK 500 MET A 40 39.14 -75.40
REMARK 500 GLN A 58 67.55 38.90
REMARK 500 TYR A 68 -106.52 65.08
REMARK 500 ASP A 131 77.26 51.51
REMARK 500 ASP A 133 -85.91 -93.34
REMARK 500 ASP A 141 23.60 -158.52
REMARK 500 HIS A 142 -152.44 -85.62
REMARK 500 SER A 196 -146.62 -139.32
REMARK 500 ASP A 205 -168.67 -118.13
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 A 215 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 141 OD2
REMARK 620 2 ASP A 141 OD1 50.1
REMARK 620 3 ASP A 169 OD2 85.3 82.5
REMARK 620 4 ASN A 170 OD1 87.9 137.1 85.7
REMARK 620 5 DNC A 217 O2 90.7 106.8 163.8 78.5
REMARK 620 6 DNC A 217 O1 160.9 146.4 104.2 76.5 75.5
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 215
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAM A 216
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DNC A 217
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3A7D RELATED DB: PDB
REMARK 900 RAT CATECHOL-O-METHYLTRANSFERASE COMPLEXED WITH BI-SUBSTRATE TYPE
REMARK 900 INHIBITOR
REMARK 900 RELATED ID: 3BWM RELATED DB: PDB
REMARK 900 HUMAN CATECHOL-O-METHYLTRANSFERASE COMPLEXED WITH SAM AND 3,5-
REMARK 900 DINITROCATECHOL
REMARK 900 RELATED ID: 3BWY RELATED DB: PDB
REMARK 900 HUMAN CATECHOL-O-METHYLTRANSFERASE COMPLEXED WITH SAM AND 3,5-
REMARK 900 DINITROCATECHOL
REMARK 900 RELATED ID: 1VID RELATED DB: PDB
REMARK 900 RAT CATECHOL-O-METHYLTRANSFERASE COMPLEXED WITH SAM AND 3,5-
REMARK 900 DINITROCATECHOL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE IS BASED ON ISOFORM SOLUBLE OF P21964(COMT_HUMAN).
DBREF 3A7E A 1 214 UNP P21964 COMT_HUMAN 51 264
SEQADV 3A7E GLY A -1 UNP P21964 EXPRESSION TAG
SEQADV 3A7E SER A 0 UNP P21964 EXPRESSION TAG
SEQRES 1 A 216 GLY SER MET GLY ASP THR LYS GLU GLN ARG ILE LEU ASN
SEQRES 2 A 216 HIS VAL LEU GLN HIS ALA GLU PRO GLY ASN ALA GLN SER
SEQRES 3 A 216 VAL LEU GLU ALA ILE ASP THR TYR CYS GLU GLN LYS GLU
SEQRES 4 A 216 TRP ALA MET ASN VAL GLY ASP LYS LYS GLY LYS ILE VAL
SEQRES 5 A 216 ASP ALA VAL ILE GLN GLU HIS GLN PRO SER VAL LEU LEU
SEQRES 6 A 216 GLU LEU GLY ALA TYR CYS GLY TYR SER ALA VAL ARG MET
SEQRES 7 A 216 ALA ARG LEU LEU SER PRO GLY ALA ARG LEU ILE THR ILE
SEQRES 8 A 216 GLU ILE ASN PRO ASP CYS ALA ALA ILE THR GLN ARG MET
SEQRES 9 A 216 VAL ASP PHE ALA GLY VAL LYS ASP LYS VAL THR LEU VAL
SEQRES 10 A 216 VAL GLY ALA SER GLN ASP ILE ILE PRO GLN LEU LYS LYS
SEQRES 11 A 216 LYS TYR ASP VAL ASP THR LEU ASP MET VAL PHE LEU ASP
SEQRES 12 A 216 HIS TRP LYS ASP ARG TYR LEU PRO ASP THR LEU LEU LEU
SEQRES 13 A 216 GLU GLU CYS GLY LEU LEU ARG LYS GLY THR VAL LEU LEU
SEQRES 14 A 216 ALA ASP ASN VAL ILE CYS PRO GLY ALA PRO ASP PHE LEU
SEQRES 15 A 216 ALA HIS VAL ARG GLY SER SER CYS PHE GLU CYS THR HIS
SEQRES 16 A 216 TYR GLN SER PHE LEU GLU TYR ARG GLU VAL VAL ASP GLY
SEQRES 17 A 216 LEU GLU LYS ALA ILE TYR LYS GLY
HET MG A 215 1
HET SAM A 216 27
HET DNC A 217 14
HETNAM MG MAGNESIUM ION
HETNAM SAM S-ADENOSYLMETHIONINE
HETNAM DNC 3,5-DINITROCATECHOL
FORMUL 2 MG MG 2+
FORMUL 3 SAM C15 H22 N6 O5 S
FORMUL 4 DNC C6 H4 N2 O6
FORMUL 5 HOH *46(H2 O)
HELIX 1 1 THR A 4 ALA A 17 1 14
HELIX 2 2 ASN A 21 LYS A 36 1 16
HELIX 3 3 GLY A 43 GLN A 58 1 16
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 GLN A 125 TYR A 130 1 6
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 ALA A 176 SER A 186 1 11
SHEET 1 A 7 VAL A 112 VAL A 116 0
SHEET 2 A 7 ARG A 85 GLU A 90 1 N LEU A 86 O THR A 113
SHEET 3 A 7 VAL A 61 LEU A 65 1 N GLU A 64 O ILE A 87
SHEET 4 A 7 LEU A 135 LEU A 140 1 O PHE A 139 N LEU A 63
SHEET 5 A 7 LEU A 160 ALA A 168 1 O LEU A 167 N VAL A 138
SHEET 6 A 7 VAL A 204 TYR A 212 -1 O ALA A 210 N LEU A 166
SHEET 7 A 7 PHE A 189 PHE A 197 -1 N THR A 192 O LYS A 209
LINK OD2 ASP A 141 MG MG A 215 1555 1555 2.09
LINK OD1 ASP A 141 MG MG A 215 1555 1555 2.82
LINK OD2 ASP A 169 MG MG A 215 1555 1555 1.99
LINK OD1 ASN A 170 MG MG A 215 1555 1555 2.08
LINK MG MG A 215 O2 DNC A 217 1555 1555 1.99
LINK MG MG A 215 O1 DNC A 217 1555 1555 2.58
CISPEP 1 CYS A 173 PRO A 174 0 -6.73
SITE 1 AC1 5 ASP A 141 ASP A 169 ASN A 170 SAM A 216
SITE 2 AC1 5 DNC A 217
SITE 1 AC2 21 MET A 40 VAL A 42 GLU A 64 GLY A 66
SITE 2 AC2 21 ALA A 67 TYR A 68 TYR A 71 SER A 72
SITE 3 AC2 21 ILE A 89 GLU A 90 ILE A 91 GLY A 117
SITE 4 AC2 21 SER A 119 GLN A 120 ASP A 141 HIS A 142
SITE 5 AC2 21 TRP A 143 ARG A 146 MG A 215 DNC A 217
SITE 6 AC2 21 HOH A 251
SITE 1 AC3 11 TRP A 38 ASP A 141 HIS A 142 TRP A 143
SITE 2 AC3 11 LYS A 144 ASP A 169 ASN A 170 PRO A 174
SITE 3 AC3 11 GLU A 199 MG A 215 SAM A 216
CRYST1 50.909 50.909 168.186 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 0.019643 0.011341 0.000000 0.00000
SCALE2 0.000000 0.022682 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005946 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
