HEADER TRANSFERASE 26-SEP-09 3A7D
TITLE CRYSTAL STRUCTURES OF RAT CATECHOL-O-METHYLTRANSFERASE COMPLEXED WITH
TITLE 2 NEW BI-SUBSTRATE TYPE INHIBITOR
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: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: COMT;
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 METHYLTRANSFERASE, NEUROTRANSMITTER DEGRADATION, ALTERNATIVE
KEYWDS 2 INITIATION, CATECHOLAMINE METABOLISM, S-ADENOSYL-L-METHIONINE, CELL
KEYWDS 3 MEMBRANE, MAGNESIUM, MEMBRANE, METAL-BINDING, PHOSPHOPROTEIN,
KEYWDS 4 SIGNAL-ANCHOR, TRANSFERASE, TRANSMEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.TSUJI
REVDAT 2 01-NOV-23 3A7D 1 REMARK SEQADV HETSYN
REVDAT 1 15-SEP-10 3A7D 0
JRNL AUTH H.MURANAKA,M.NAKATSU,E.TSUJI,K.OKAZAKI
JRNL TITL HIT TO LEAD: COMPREHENSIVE STRATEGY OF DE NOVO SCAFFOLD
JRNL TITL 2 GENERATION BY FBDD. PART 2: LIGAND FISHING USING MASS
JRNL TITL 3 SPECTROMETRY BY DETECTION OF LIGAND-PROTEIN NON-COVALENT
JRNL TITL 4 COMPLEX AFTER MATRIX CLICK CHEMISTRY
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.40 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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 3 NUMBER OF REFLECTIONS : 8064
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) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 891
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 533
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.75
REMARK 3 BIN R VALUE (WORKING SET) : 0.2150
REMARK 3 BIN FREE R VALUE SET COUNT : 62
REMARK 3 BIN FREE R VALUE : 0.3100
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1676
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 49
REMARK 3 SOLVENT ATOMS : 93
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.68
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.49000
REMARK 3 B22 (A**2) : 1.23000
REMARK 3 B33 (A**2) : -0.74000
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): 0.606
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.269
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.174
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.573
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.914
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1757 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2387 ; 1.181 ; 2.018
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 213 ; 4.870 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 75 ;35.440 ;24.800
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 301 ;14.910 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;11.646 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 264 ; 0.069 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1313 ; 0.004 ; 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): 1062 ; 0.954 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1708 ; 1.828 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 695 ; 3.297 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 679 ; 5.191 ; 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 : 1.20
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3A7D 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_1000028903.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-APR-09
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) : 1.0
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
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 : 9468
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 46.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.07200
REMARK 200 R SYM (I) : 0.07800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.1
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : 0.21800
REMARK 200 R SYM FOR SHELL (I) : 0.23600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 9.100
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 (%): 46.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M (NH4)2SO4, 0.1M TRIS PH 7.5, 30%
REMARK 280 (W/V) PEG 400, 0.35% (V/V) GLYCEROL, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
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 25.03750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.59900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.04100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.59900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.03750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.04100
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 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 128 CD CE NZ
REMARK 470 ASP A 131 CB CG OD1 OD2
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 CE3 TRP A 143 O HOH A 272 1.69
REMARK 500 O4 SO4 A 303 O HOH A 311 1.94
REMARK 500 O HOH A 273 O HOH A 318 2.01
REMARK 500 N SER A 72 O3 SO4 A 303 2.10
REMARK 500 O SER A 186 O HOH A 264 2.13
REMARK 500 O HOH A 277 O HOH A 307 2.17
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 ASP A 3 93.01 112.46
REMARK 500 MET A 40 40.86 -85.70
REMARK 500 TYR A 68 -114.02 62.90
REMARK 500 ASP A 133 -97.80 -71.91
REMARK 500 ASP A 141 25.64 -148.46
REMARK 500 HIS A 142 -151.56 -99.40
REMARK 500 SER A 196 -151.40 -158.58
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 300 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 141 OD1
REMARK 620 2 ASP A 169 OD2 101.3
REMARK 620 3 ASN A 170 OD1 97.9 80.4
REMARK 620 4 FBN A 304 O53 158.7 99.6 81.2
REMARK 620 5 FBN A 304 O52 83.4 166.7 86.7 75.2
REMARK 620 6 HOH A 312 O 96.6 89.5 163.7 87.9 102.3
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 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FBN A 304
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1VID RELATED DB: PDB
REMARK 900 RAT CATECHOL-O-METHYLTRANSFERASE COMPLEXED WITH SAM AND 3,5-
REMARK 900 DINITROCATECHOL
REMARK 900 RELATED ID: 1JR4 RELATED DB: PDB
REMARK 900 RAT CATECHOL-O-METHYLTRANSFERASE COMPLEXED WITH BI-SUBSTRATE TYPE
REMARK 900 INHIBITOR
REMARK 900 RELATED ID: 3A7E RELATED DB: PDB
REMARK 900 HUMAN COMT 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 2 OF P22734(COMT_RAT).
DBREF 3A7D A 1 221 UNP P22734 COMT_RAT 44 264
SEQADV 3A7D GLY A -1 UNP P22734 EXPRESSION TAG
SEQADV 3A7D 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 SO4 A 303 5
HET SO4 A 301 5
HET FBN A 304 38
HETNAM MG MAGNESIUM ION
HETNAM SO4 SULFATE ION
HETNAM FBN 5'-DEOXY-5'-[4-({[(2,3-DIHYDROXY-5-NITROPHENYL)
HETNAM 2 FBN CARBONYL]AMINO}METHYL)-1H-1,2,3-TRIAZOL-1-YL]ADENOSINE
HETSYN FBN N-[(1-{[(2R,3S,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-3,4-
HETSYN 2 FBN DIHYDROXYOXOLAN-2-YL]METHYL}-1H-1,2,3-TRIAZOL-4-YL)
HETSYN 3 FBN METHYL]-2,3-DIHY DROXY-5-NITROBENZAMIDE
FORMUL 2 MG MG 2+
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 FBN C20 H20 N10 O8
FORMUL 6 HOH *93(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 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 VAL A 62 O LEU A 87
SHEET 4 A 7 MET A 137 LEU A 140 1 O PHE A 139 N LEU A 65
SHEET 5 A 7 VAL A 165 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 TYR A 197 -1 N THR A 192 O LYS A 209
LINK OD1 ASP A 141 MG MG A 300 1555 1555 1.99
LINK OD2 ASP A 169 MG MG A 300 1555 1555 2.11
LINK OD1 ASN A 170 MG MG A 300 1555 1555 2.18
LINK MG MG A 300 O53 FBN A 304 1555 1555 2.19
LINK MG MG A 300 O52 FBN A 304 1555 1555 2.38
LINK MG MG A 300 O HOH A 312 1555 1555 1.98
CISPEP 1 VAL A 173 PRO A 174 0 1.05
SITE 1 AC1 5 ASP A 141 ASP A 169 ASN A 170 FBN A 304
SITE 2 AC1 5 HOH A 312
SITE 1 AC2 9 MET A 40 ASN A 41 VAL A 42 ALA A 67
SITE 2 AC2 9 TYR A 68 TYR A 71 SER A 72 ASP A 141
SITE 3 AC2 9 HOH A 311
SITE 1 AC3 7 GLY A 43 ASP A 44 ALA A 45 GLU A 199
SITE 2 AC3 7 TYR A 200 HOH A 223 HOH A 240
SITE 1 AC4 23 TRP A 38 MET A 40 TYR A 68 MET A 89
SITE 2 AC4 23 GLU A 90 MET A 91 ASN A 92 TYR A 95
SITE 3 AC4 23 ALA A 118 SER A 119 GLN A 120 ASP A 141
SITE 4 AC4 23 HIS A 142 TRP A 143 LYS A 144 ASP A 169
SITE 5 AC4 23 ASN A 170 PRO A 174 GLU A 199 HOH A 224
SITE 6 AC4 23 HOH A 229 MG A 300 HOH A 312
CRYST1 50.075 58.082 79.198 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 0.019970 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017217 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012627 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
