HEADER TRANSFERASE 19-OCT-16 5PA5
TITLE HUMANIZED RAT COMT IN COMPLEX WITH 6-(2,4-DIMETHYL-1,3-THIAZOL-5-YL)-
TITLE 2 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,C.LERNER,M.G.RUDOLPH
REVDAT 4 03-APR-24 5PA5 1 REMARK
REVDAT 3 17-NOV-21 5PA5 1 LINK
REVDAT 2 21-FEB-18 5PA5 1 REMARK
REVDAT 1 22-NOV-17 5PA5 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. 1.63 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0081
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) : 1.63
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.19
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 3 NUMBER OF REFLECTIONS : 25476
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) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1322
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) : 1.63
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1654
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.16
REMARK 3 BIN R VALUE (WORKING SET) : 0.3240
REMARK 3 BIN FREE R VALUE SET COUNT : 102
REMARK 3 BIN FREE R VALUE : 0.3590
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 : 69
REMARK 3 SOLVENT ATOMS : 182
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.42
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.28
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.56000
REMARK 3 B22 (A**2) : 1.74000
REMARK 3 B33 (A**2) : -1.18000
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): 0.096
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.102
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.070
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.099
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.944
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1793 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1189 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2440 ; 1.563 ; 2.027
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2924 ; 0.954 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 220 ; 5.223 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 75 ;39.471 ;24.933
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 312 ;12.055 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;20.860 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 276 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1953 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 331 ; 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: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5PA5 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_1001400410.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-OCT-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) : 1.000000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28116
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.630
REMARK 200 RESOLUTION RANGE LOW (A) : 45.190
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 6.430
REMARK 200 R MERGE (I) : 0.13500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.6600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.63
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.67
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.24000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.260
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 (%): 44.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
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 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 24.86600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.62100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.19350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.62100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.86600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 27.19350
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 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: 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 37.57 -76.44
REMARK 500 SER A 58 59.81 38.97
REMARK 500 SER A 58 60.27 38.58
REMARK 500 TYR A 68 -110.00 60.19
REMARK 500 ASP A 133 -80.49 -89.18
REMARK 500 ASP A 141 41.89 -157.78
REMARK 500 HIS A 142 -79.56 -105.57
REMARK 500 SER A 196 -145.58 -151.62
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 92.4
REMARK 620 3 ASN A 170 OD1 93.0 82.6
REMARK 620 4 7JH A 306 O19 163.0 103.8 83.9
REMARK 620 5 HOH A 445 O 96.0 93.2 170.2 88.5
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 CL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7JH A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue D1D A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 308
DBREF 5PA5 A 1 221 UNP P22734 COMT_RAT 44 264
SEQADV 5PA5 ILE A 91 UNP P22734 MET 134 ENGINEERED MUTATION
SEQADV 5PA5 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 CL A 302 1
HET SO4 A 303 5
HET SO4 A 304 5
HET SAH A 305 26
HET 7JH A 306 19
HET D1D A 307 8
HET ACT A 308 4
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
HETNAM SO4 SULFATE ION
HETNAM SAH S-ADENOSYL-L-HOMOCYSTEINE
HETNAM 7JH 6-(2,4-DIMETHYL-1,3-THIAZOL-5-YL)-8-OXIDANYL-3~{H}-
HETNAM 2 7JH QUINAZOLIN-4-ONE
HETNAM D1D (4S,5S)-1,2-DITHIANE-4,5-DIOL
HETNAM ACT ACETATE ION
HETSYN 7JH 6-(2,4-DIMETHYL-1,3-THIAZOL-5-YL)-8-HYDROXY-3H-
HETSYN 2 7JH QUINAZOLIN-4-ONE
FORMUL 2 MG MG 2+
FORMUL 3 CL CL 1-
FORMUL 4 SO4 2(O4 S 2-)
FORMUL 6 SAH C14 H20 N6 O5 S
FORMUL 7 7JH C13 H11 N3 O2 S
FORMUL 8 D1D C4 H8 O2 S2
FORMUL 9 ACT C2 H3 O2 1-
FORMUL 10 HOH *182(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 VAL A 42 SER A 58 1 17
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 PRO A 124 LEU A 126 5 3
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 7 VAL A 112 ASN A 116 0
SHEET 2 AA1 7 ARG A 85 GLU A 90 1 N THR A 88 O LEU A 115
SHEET 3 AA1 7 LEU A 61 LEU A 65 1 N GLU A 64 O LEU A 87
SHEET 4 AA1 7 MET A 137 LEU A 140 1 O PHE A 139 N LEU A 65
SHEET 5 AA1 7 VAL A 165 ALA A 168 1 O LEU A 167 N VAL A 138
SHEET 6 AA1 7 VAL A 204 TYR A 212 -1 O ALA A 210 N LEU A 166
SHEET 7 AA1 7 PHE A 189 TYR A 197 -1 N THR A 192 O LYS A 209
LINK OD1 ASP A 141 MG MG A 301 1555 1555 2.11
LINK OD2 ASP A 169 MG MG A 301 1555 1555 2.00
LINK OD1 ASN A 170 MG MG A 301 1555 1555 2.16
LINK MG MG A 301 O19 7JH A 306 1555 1555 2.13
LINK MG MG A 301 O HOH A 445 1555 1555 2.13
CISPEP 1 VAL A 173 PRO A 174 0 0.51
SITE 1 AC1 5 ASP A 141 ASP A 169 ASN A 170 7JH A 306
SITE 2 AC1 5 HOH A 445
SITE 1 AC2 4 ASP A 44 ALA A 45 TYR A 200 HOH A 546
SITE 1 AC3 5 PRO A 82 GLY A 83 ARG A 85 LYS A 111
SITE 2 AC3 5 LYS A 128
SITE 1 AC4 4 ASP A 3 THR A 4 LYS A 5 ARG A 8
SITE 1 AC5 21 MET A 40 ASN A 41 VAL A 42 GLY A 66
SITE 2 AC5 21 ALA A 67 TYR A 68 TYR A 71 SER A 72
SITE 3 AC5 21 GLU A 90 ILE A 91 GLY A 117 ALA A 118
SITE 4 AC5 21 SER A 119 GLN A 120 ASP A 141 HIS A 142
SITE 5 AC5 21 ARG A 146 7JH A 306 ACT A 308 HOH A 455
SITE 6 AC5 21 HOH A 485
SITE 1 AC6 15 MET A 40 ALA A 97 GLN A 100 ASN A 104
SITE 2 AC6 15 ASP A 141 HIS A 142 TRP A 143 ASP A 169
SITE 3 AC6 15 ASN A 170 GLU A 199 MG A 301 SAH A 305
SITE 4 AC6 15 D1D A 307 HOH A 430 HOH A 445
SITE 1 AC7 8 TRP A 38 ALA A 97 GLN A 100 ASN A 116
SITE 2 AC7 8 MET A 201 7JH A 306 HOH A 404 HOH A 423
SITE 1 AC8 3 GLN A 120 ARG A 146 SAH A 305
CRYST1 49.732 54.387 81.242 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 0.020108 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018387 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012309 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
