HEADER TRANSFERASE 19-OCT-16 5P9U
TITLE HUMANIZED RAT CATECHOL O-METHYLTRANSFERASE IN COMPLEX WITH SAH AND 6-
TITLE 2 BROMO-8-HYDROXY-3H-QUINAZOLIN-4-ONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATECHOL O-METHYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SOLUBLE FORM, RESIDUES 44-264;
COMPND 5 SYNONYM: HUMANIZED RAT COMT;
COMPND 6 EC: 2.1.1.6;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: 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: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS METHYLTRANSFERASE, NEUROTRANSMITTER DEGRADATION, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.EHLER,B.BUETTELMANN,M.G.RUDOLPH
REVDAT 4 03-APR-24 5P9U 1 REMARK
REVDAT 3 17-NOV-21 5P9U 1 LINK
REVDAT 2 21-FEB-18 5P9U 1 REMARK
REVDAT 1 22-NOV-17 5P9U 0
JRNL AUTH C.LERNER,R.JAKOB-ROETNE,K.GROEBKE-ZBINDEN,B.BUETTELMANN,
JRNL AUTH 2 M.G.RUDOLPH
JRNL TITL CRYSTAL STRUCTURE OF A COMT COMPLEX
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.42 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0077
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) : 1.42
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.67
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 44241
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) : 0.211
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2346
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) : 1.42
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2934
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.3660
REMARK 3 BIN FREE R VALUE SET COUNT : 167
REMARK 3 BIN FREE R VALUE : 0.3720
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1679
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 106
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.02
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.96
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.90000
REMARK 3 B22 (A**2) : 0.90000
REMARK 3 B33 (A**2) : -1.35000
REMARK 3 B12 (A**2) : 0.45000
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): 0.068
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.072
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.056
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.454
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1777 ; 0.021 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1191 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2417 ; 1.961 ; 2.014
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2927 ; 1.047 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 221 ; 5.677 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 76 ;39.685 ;24.737
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 314 ;14.072 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;17.354 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 273 ; 0.115 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1952 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 332 ; 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 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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: BROMINE ATOM PARTIALLY RADIOLYZED, HAS
REMARK 3 NEGATIVE DENSITY. LAST BETA-STRAND PARTIALLY DOMAIN SWAPPED,
REMARK 3 MODELED AS SUCH. HYDROGENS HAVE BEEN USED IF PRESENT IN THE
REMARK 3 INPUT U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5P9U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-NOV-16.
REMARK 100 THE DEPOSITION ID IS D_1001400399.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-JUL-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
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47849
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.420
REMARK 200 RESOLUTION RANGE LOW (A) : 43.660
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 18.88
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.8400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.42
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.79300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.450
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 (%): 50.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, CHES, PH 9, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 295K
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 112.17467
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 56.08733
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 56.08733
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 112.17467
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: 4780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 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 75.63000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 -43.66500
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 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: 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 ASP A 141 CB - CG - OD1 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ARG A 146 NE - CZ - NH1 ANGL. DEV. = -3.8 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 36 -62.06 -106.92
REMARK 500 MET A 40 33.46 -84.63
REMARK 500 TYR A 68 -109.55 66.20
REMARK 500 ASP A 133 -78.44 -96.68
REMARK 500 ASP A 141 41.61 -161.12
REMARK 500 HIS A 142 -78.35 -103.35
REMARK 500 SER A 196 -146.91 -152.25
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 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 141 OD1
REMARK 620 2 ASP A 169 OD2 92.2
REMARK 620 3 ASN A 170 OD1 90.5 84.9
REMARK 620 4 7JL A 303 O6 163.9 103.1 86.0
REMARK 620 5 HOH A 440 O 96.6 91.2 172.1 88.2
REMARK 620 N 1 2 3 4
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 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7JL A 303
DBREF 5P9U A 1 221 UNP P22734 COMT_RAT 44 264
SEQADV 5P9U ILE A 91 UNP P22734 MET 134 ENGINEERED MUTATION
SEQADV 5P9U 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 301 1
HET SAH A 302 26
HET 7JL A 303 13
HETNAM MG MAGNESIUM ION
HETNAM SAH S-ADENOSYL-L-HOMOCYSTEINE
HETNAM 7JL 6-BROMANYL-8-OXIDANYL-3~{H}-QUINAZOLIN-4-ONE
HETSYN 7JL 6-BROMO-8-HYDROXY-3H-QUINAZOLIN-4-ONE
FORMUL 2 MG MG 2+
FORMUL 3 SAH C14 H20 N6 O5 S
FORMUL 4 7JL C8 H5 BR N2 O2
FORMUL 5 HOH *106(H2 O)
HELIX 1 AA1 THR A 4 ALA A 17 1 14
HELIX 2 AA2 ASP A 21 LYS A 36 1 16
HELIX 3 AA3 GLY A 43 SER A 58 1 16
HELIX 4 AA4 GLY A 70 ARG A 78 1 9
HELIX 5 AA5 ASN A 92 GLY A 107 1 16
HELIX 6 AA6 ALA A 118 ILE A 123 1 6
HELIX 7 AA7 GLN A 125 ASP A 131 1 7
HELIX 8 AA8 TRP A 143 ASP A 145 5 3
HELIX 9 AA9 ARG A 146 CYS A 157 1 12
HELIX 10 AB1 THR A 176 SER A 186 1 11
SHEET 1 AA1 5 VAL A 112 ASN A 116 0
SHEET 2 AA1 5 ARG A 85 GLU A 90 1 N THR A 88 O LEU A 115
SHEET 3 AA1 5 LEU A 61 LEU A 65 1 N VAL A 62 O LEU A 87
SHEET 4 AA1 5 MET A 137 LEU A 140 1 O PHE A 139 N LEU A 65
SHEET 5 AA1 5 VAL A 165 ALA A 168 1 O LEU A 167 N VAL A 138
LINK OD1 ASP A 141 MG MG A 301 1555 1555 2.00
LINK OD2 ASP A 169 MG MG A 301 1555 1555 2.05
LINK OD1 ASN A 170 MG MG A 301 1555 1555 2.18
LINK MG MG A 301 O6 7JL A 303 1555 1555 2.17
LINK MG MG A 301 O HOH A 440 1555 1555 2.02
CISPEP 1 VAL A 173 PRO A 174 0 1.02
SITE 1 AC1 5 ASP A 141 ASP A 169 ASN A 170 7JL A 303
SITE 2 AC1 5 HOH A 440
SITE 1 AC2 19 MET A 40 ASN A 41 VAL A 42 GLY A 66
SITE 2 AC2 19 ALA A 67 TYR A 68 TYR A 71 SER A 72
SITE 3 AC2 19 GLU A 90 ILE A 91 GLY A 117 ALA A 118
SITE 4 AC2 19 SER A 119 GLN A 120 ASP A 141 HIS A 142
SITE 5 AC2 19 7JL A 303 HOH A 416 HOH A 451
SITE 1 AC3 10 MET A 40 ASP A 141 HIS A 142 TRP A 143
SITE 2 AC3 10 ASP A 169 ASN A 170 GLU A 199 MG A 301
SITE 3 AC3 10 SAH A 302 HOH A 440
CRYST1 50.420 50.420 168.262 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 0.019833 0.011451 0.000000 0.00000
SCALE2 0.000000 0.022902 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005943 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
