HEADER TRANSFERASE 16-MAY-04 1T9B
TITLE CRYSTAL STRUCTURE OF YEAST ACETOHYDROXYACID SYNTHASE IN COMPLEX WITH A
TITLE 2 SULFONYLUREA HERBICIDE, CHLORSULFURON
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETOLACTATE SYNTHASE, MITOCHONDRIAL;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATALYTIC SUBUNIT;
COMPND 5 SYNONYM: ACETOHYDROXY-ACID SYNTHASE, ALS, AHAS;
COMPND 6 EC: 2.2.1.6;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: ILV2, SMR1, YMR108W, YM9718.07;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET30(C)
KEYWDS ACETOHYDROXYACID SYNTHASE, ACETOLACTATE SYNTHASE, HERBICIDE,
KEYWDS 2 SULFONYLUREA, THIAMIN DIPHOSPHATE, FAD, INHIBITOR, CHLORSULFURON,
KEYWDS 3 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.A.MCCOURT,S.S.PANG,L.W.GUDDAT,R.G.DUGGLEBY
REVDAT 5 23-AUG-23 1T9B 1 REMARK SEQADV LINK
REVDAT 4 11-OCT-17 1T9B 1 REMARK
REVDAT 3 24-FEB-09 1T9B 1 VERSN
REVDAT 2 01-MAR-05 1T9B 1 JRNL
REVDAT 1 21-DEC-04 1T9B 0
JRNL AUTH J.A.MCCOURT,S.S.PANG,L.W.GUDDAT,R.G.DUGGLEBY
JRNL TITL ELUCIDATING THE SPECIFICITY OF BINDING OF SULFONYLUREA
JRNL TITL 2 HERBICIDES TO ACETOHYDROXYACID SYNTHASE.
JRNL REF BIOCHEMISTRY V. 44 2330 2005
JRNL REFN ISSN 0006-2960
JRNL PMID 15709745
JRNL DOI 10.1021/BI047980A
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.5
REMARK 3 NUMBER OF REFLECTIONS : 99442
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 SET) : 0.162
REMARK 3 FREE R VALUE : 0.195
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 9986
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.28
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 53.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2180
REMARK 3 BIN FREE R VALUE : 0.2430
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 530
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8929
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 205
REMARK 3 SOLVENT ATOMS : 1360
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20
REMARK 3 ESD FROM SIGMAA (A) : 0.18
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.22
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1T9B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUL-04.
REMARK 100 THE DEPOSITION ID IS D_1000022473.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-DEC-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 14-BM-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.90
REMARK 200 MONOCHROMATOR : GE (III)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : ADX
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 102885
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.190
REMARK 200 RESOLUTION RANGE LOW (A) : 99.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.9
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.19
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 53.4
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.21900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.110
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 1N0H
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: POTASSIUM PHOSPHATE, THIAMIN
REMARK 280 DIPHOSPHATE, FAD, MAGNESIUM CHLORIDE, DTT, CHLORSULFURON, TRIS-
REMARK 280 HCL, LITHIUM SULFATE, SODIUM POTASSIUM TARTRATE, PH 7.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 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 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 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 300 REMARK: THE ASYMMETRIC UNIT CONTAINS THE MINIMUM BIOLOGICAL UNIT
REMARK 300 REQUIRED FOR ACTIVITY, A DIMER.
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -81.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 11
REMARK 465 HIS A 12
REMARK 465 HIS A 13
REMARK 465 HIS A 14
REMARK 465 HIS A 15
REMARK 465 HIS A 16
REMARK 465 HIS A 17
REMARK 465 SER A 18
REMARK 465 SER A 19
REMARK 465 GLY A 20
REMARK 465 LEU A 21
REMARK 465 VAL A 22
REMARK 465 PRO A 23
REMARK 465 ARG A 24
REMARK 465 GLY A 25
REMARK 465 SER A 26
REMARK 465 GLY A 27
REMARK 465 MET A 28
REMARK 465 LYS A 29
REMARK 465 GLU A 30
REMARK 465 THR A 31
REMARK 465 ALA A 32
REMARK 465 ALA A 33
REMARK 465 ALA A 34
REMARK 465 LYS A 35
REMARK 465 PHE A 36
REMARK 465 GLU A 37
REMARK 465 ARG A 38
REMARK 465 GLN A 39
REMARK 465 HIS A 40
REMARK 465 MET A 41
REMARK 465 ASP A 42
REMARK 465 SER A 43
REMARK 465 PRO A 44
REMARK 465 ASP A 45
REMARK 465 LEU A 46
REMARK 465 GLY A 47
REMARK 465 THR A 48
REMARK 465 ASP A 49
REMARK 465 ASP A 50
REMARK 465 ASP A 51
REMARK 465 ASP A 52
REMARK 465 LYS A 53
REMARK 465 ALA A 54
REMARK 465 MET A 55
REMARK 465 GLY A 56
REMARK 465 SER A 57
REMARK 465 ALA A 58
REMARK 465 PRO A 59
REMARK 465 SER A 60
REMARK 465 PHE A 61
REMARK 465 ASN A 62
REMARK 465 VAL A 63
REMARK 465 ASP A 64
REMARK 465 PRO A 65
REMARK 465 LEU A 66
REMARK 465 GLU A 67
REMARK 465 GLN A 68
REMARK 465 PRO A 69
REMARK 465 ALA A 70
REMARK 465 GLU A 71
REMARK 465 PRO A 72
REMARK 465 SER A 73
REMARK 465 LYS A 74
REMARK 465 LEU A 75
REMARK 465 ALA A 76
REMARK 465 LYS A 77
REMARK 465 LYS A 78
REMARK 465 LEU A 79
REMARK 465 ARG A 80
REMARK 465 ALA A 81
REMARK 465 GLU A 82
REMARK 465 PRO A 83
REMARK 465 ASP A 84
REMARK 465 THR A 264
REMARK 465 LYS A 265
REMARK 465 THR A 266
REMARK 465 THR A 267
REMARK 465 LEU A 268
REMARK 465 PRO A 269
REMARK 465 SER A 270
REMARK 465 ASN A 271
REMARK 465 ALA A 272
REMARK 465 LEU A 273
REMARK 465 ASN A 274
REMARK 465 GLN A 275
REMARK 465 LEU A 276
REMARK 465 THR A 277
REMARK 465 SER A 278
REMARK 465 ARG A 279
REMARK 465 ALA A 280
REMARK 465 GLN A 281
REMARK 465 ASP A 282
REMARK 465 GLU A 283
REMARK 465 MET B 11
REMARK 465 HIS B 12
REMARK 465 HIS B 13
REMARK 465 HIS B 14
REMARK 465 HIS B 15
REMARK 465 HIS B 16
REMARK 465 HIS B 17
REMARK 465 SER B 18
REMARK 465 SER B 19
REMARK 465 GLY B 20
REMARK 465 LEU B 21
REMARK 465 VAL B 22
REMARK 465 PRO B 23
REMARK 465 ARG B 24
REMARK 465 GLY B 25
REMARK 465 SER B 26
REMARK 465 GLY B 27
REMARK 465 MET B 28
REMARK 465 LYS B 29
REMARK 465 GLU B 30
REMARK 465 THR B 31
REMARK 465 ALA B 32
REMARK 465 ALA B 33
REMARK 465 ALA B 34
REMARK 465 LYS B 35
REMARK 465 PHE B 36
REMARK 465 GLU B 37
REMARK 465 ARG B 38
REMARK 465 GLN B 39
REMARK 465 HIS B 40
REMARK 465 MET B 41
REMARK 465 ASP B 42
REMARK 465 SER B 43
REMARK 465 PRO B 44
REMARK 465 ASP B 45
REMARK 465 LEU B 46
REMARK 465 GLY B 47
REMARK 465 THR B 48
REMARK 465 ASP B 49
REMARK 465 ASP B 50
REMARK 465 ASP B 51
REMARK 465 ASP B 52
REMARK 465 LYS B 53
REMARK 465 ALA B 54
REMARK 465 MET B 55
REMARK 465 GLY B 56
REMARK 465 SER B 57
REMARK 465 ALA B 58
REMARK 465 PRO B 59
REMARK 465 SER B 60
REMARK 465 PHE B 61
REMARK 465 ASN B 62
REMARK 465 VAL B 63
REMARK 465 ASP B 64
REMARK 465 PRO B 65
REMARK 465 LEU B 66
REMARK 465 GLU B 67
REMARK 465 GLN B 68
REMARK 465 PRO B 69
REMARK 465 ALA B 70
REMARK 465 GLU B 71
REMARK 465 PRO B 72
REMARK 465 SER B 73
REMARK 465 LYS B 74
REMARK 465 LEU B 75
REMARK 465 ALA B 76
REMARK 465 LYS B 77
REMARK 465 LYS B 78
REMARK 465 LEU B 79
REMARK 465 ARG B 80
REMARK 465 ALA B 81
REMARK 465 GLU B 82
REMARK 465 PRO B 83
REMARK 465 ASP B 84
REMARK 465 SER B 270
REMARK 465 ASN B 271
REMARK 465 ALA B 272
REMARK 465 LEU B 273
REMARK 465 ASN B 274
REMARK 465 GLN B 275
REMARK 465 LEU B 276
REMARK 465 THR B 277
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 221 CG CD CE NZ
REMARK 470 LYS A 300 CG CD CE NZ
REMARK 470 LYS A 411 CG CD CE NZ
REMARK 470 GLN A 418 CG CD OE1 NE2
REMARK 470 PHE A 439 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 453 CG CD CE NZ
REMARK 470 LYS A 456 CG CD CE NZ
REMARK 470 GLU A 457 CG CD OE1 OE2
REMARK 470 LYS A 636 CG CD CE NZ
REMARK 470 LYS A 681 CG CD CE NZ
REMARK 470 LYS A 686 CG CD CE NZ
REMARK 470 LYS B 265 CG CD CE NZ
REMARK 470 LYS B 453 CG CD CE NZ
REMARK 470 LYS B 456 CG CD CE NZ
REMARK 470 LYS B 630 CG CD CE NZ
REMARK 470 GLU B 677 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH2 ARG B 511 NH2 ARG B 511 5556 2.19
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 TRP A 216 149.66 -170.71
REMARK 500 ASP A 350 -159.24 75.99
REMARK 500 ASN A 384 106.25 -58.49
REMARK 500 TYR A 460 75.73 -65.41
REMARK 500 ARG A 511 -21.61 -143.98
REMARK 500 GLU A 663 39.57 -98.63
REMARK 500 ASP B 350 -164.67 72.26
REMARK 500 ARG B 511 -25.39 -140.20
REMARK 500 GLU B 592 50.70 39.03
REMARK 500 GLU B 663 49.79 -106.80
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 K A1696 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 343 OE1
REMARK 620 2 ASP A 350 OD2 88.9
REMARK 620 3 GLN A 506 O 158.9 102.0
REMARK 620 4 TRP A 508 O 74.5 163.0 92.5
REMARK 620 5 HOH A4034 O 79.1 66.5 88.8 105.5
REMARK 620 6 HOH A4147 O 61.0 77.7 138.7 97.3 126.2
REMARK 620 7 HOH A4492 O 131.1 91.7 67.2 102.1 144.0 71.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1699 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 550 OD1
REMARK 620 2 ASN A 577 OD1 80.7
REMARK 620 3 GLU A 579 O 105.1 84.4
REMARK 620 4 P22 A1702 O3B 162.0 93.4 91.1
REMARK 620 5 P22 A1702 O1A 88.0 168.3 95.4 98.4
REMARK 620 6 HOH A4051 O 82.7 86.5 166.9 80.0 95.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 696 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN B 343 OE1
REMARK 620 2 ASP B 350 OD2 87.5
REMARK 620 3 GLN B 506 O 162.3 99.2
REMARK 620 4 TRP B 508 O 79.3 166.2 92.5
REMARK 620 5 HOH B4232 O 83.2 68.7 84.1 105.6
REMARK 620 6 HOH B4657 O 129.2 93.9 67.0 97.4 143.8
REMARK 620 7 HOH B4676 O 75.0 46.1 121.3 131.7 110.9 70.3
REMARK 620 8 HOH B5202 O 67.9 90.6 128.0 87.9 145.3 61.3 44.6
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 699 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 550 OD1
REMARK 620 2 ASN B 577 OD1 81.3
REMARK 620 3 GLU B 579 O 105.8 86.4
REMARK 620 4 P25 B 698 O3B 160.5 93.1 92.4
REMARK 620 5 P25 B 698 O1A 93.3 174.6 95.6 91.8
REMARK 620 6 HOH B4246 O 81.4 86.1 168.7 79.6 92.7
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 K B 696
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 699
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 1696
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1699
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1CS A 695
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P25 B 698
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NSP A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1CS B 1695
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 1701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P22 A 1702
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YF3 A 1705
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1N0H RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF YEAST ACETOHYDROXYACID SYNTHASE IN COMPLEX
REMARK 900 WITH A SULFONYLUREA HERBICIDE, CHLORIMURON ETHYL
REMARK 900 RELATED ID: 1T9C RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF YEAST ACETOHYDROXYACID SYNTHASE IN COMPLEX
REMARK 900 WITH A SULFONYLUREA HERBICIDE, SULFOMETURON METHYL
REMARK 900 RELATED ID: 1T9D RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF YEAST ACETOHYDROXYACID SYNTHASE IN COMPLEX
REMARK 900 WITH A SULFONYLUREA HERBICIDE, METSULFURON METHYL
REMARK 900 RELATED ID: 1T9A RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF YEAST ACETOHYDROXYACID SYNTHASE IN COMPLEX
REMARK 900 WITH A SULFONYLUREA HERBICIDE, TRIBENURON METHYL
DBREF 1T9B A 58 687 UNP P07342 ILVB_YEAST 58 687
DBREF 1T9B B 58 687 UNP P07342 ILVB_YEAST 58 687
SEQADV 1T9B MET A 11 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B HIS A 12 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B HIS A 13 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B HIS A 14 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B HIS A 15 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B HIS A 16 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B HIS A 17 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B SER A 18 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B SER A 19 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B GLY A 20 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B LEU A 21 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B VAL A 22 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B PRO A 23 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B ARG A 24 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B GLY A 25 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B SER A 26 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B GLY A 27 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B MET A 28 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B LYS A 29 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B GLU A 30 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B THR A 31 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B ALA A 32 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B ALA A 33 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B ALA A 34 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B LYS A 35 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B PHE A 36 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B GLU A 37 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B ARG A 38 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B GLN A 39 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B HIS A 40 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B MET A 41 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B ASP A 42 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B SER A 43 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B PRO A 44 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B ASP A 45 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B LEU A 46 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B GLY A 47 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B THR A 48 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B ASP A 49 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B ASP A 50 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B ASP A 51 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B ASP A 52 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B LYS A 53 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B ALA A 54 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B MET A 55 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B GLY A 56 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B SER A 57 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B MET B 11 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B HIS B 12 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B HIS B 13 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B HIS B 14 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B HIS B 15 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B HIS B 16 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B HIS B 17 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B SER B 18 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B SER B 19 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B GLY B 20 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B LEU B 21 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B VAL B 22 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B PRO B 23 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B ARG B 24 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B GLY B 25 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B SER B 26 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B GLY B 27 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B MET B 28 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B LYS B 29 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B GLU B 30 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B THR B 31 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B ALA B 32 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B ALA B 33 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B ALA B 34 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B LYS B 35 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B PHE B 36 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B GLU B 37 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B ARG B 38 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B GLN B 39 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B HIS B 40 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B MET B 41 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B ASP B 42 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B SER B 43 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B PRO B 44 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B ASP B 45 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B LEU B 46 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B GLY B 47 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B THR B 48 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B ASP B 49 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B ASP B 50 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B ASP B 51 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B ASP B 52 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B LYS B 53 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B ALA B 54 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B MET B 55 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B GLY B 56 UNP P07342 CLONING ARTIFACT
SEQADV 1T9B SER B 57 UNP P07342 CLONING ARTIFACT
SEQRES 1 A 677 MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO
SEQRES 2 A 677 ARG GLY SER GLY MET LYS GLU THR ALA ALA ALA LYS PHE
SEQRES 3 A 677 GLU ARG GLN HIS MET ASP SER PRO ASP LEU GLY THR ASP
SEQRES 4 A 677 ASP ASP ASP LYS ALA MET GLY SER ALA PRO SER PHE ASN
SEQRES 5 A 677 VAL ASP PRO LEU GLU GLN PRO ALA GLU PRO SER LYS LEU
SEQRES 6 A 677 ALA LYS LYS LEU ARG ALA GLU PRO ASP MET ASP THR SER
SEQRES 7 A 677 PHE VAL GLY LEU THR GLY GLY GLN ILE PHE ASN GLU MET
SEQRES 8 A 677 MET SER ARG GLN ASN VAL ASP THR VAL PHE GLY TYR PRO
SEQRES 9 A 677 GLY GLY ALA ILE LEU PRO VAL TYR ASP ALA ILE HIS ASN
SEQRES 10 A 677 SER ASP LYS PHE ASN PHE VAL LEU PRO LYS HIS GLU GLN
SEQRES 11 A 677 GLY ALA GLY HIS MET ALA GLU GLY TYR ALA ARG ALA SER
SEQRES 12 A 677 GLY LYS PRO GLY VAL VAL LEU VAL THR SER GLY PRO GLY
SEQRES 13 A 677 ALA THR ASN VAL VAL THR PRO MET ALA ASP ALA PHE ALA
SEQRES 14 A 677 ASP GLY ILE PRO MET VAL VAL PHE THR GLY GLN VAL PRO
SEQRES 15 A 677 THR SER ALA ILE GLY THR ASP ALA PHE GLN GLU ALA ASP
SEQRES 16 A 677 VAL VAL GLY ILE SER ARG SER CYS THR LYS TRP ASN VAL
SEQRES 17 A 677 MET VAL LYS SER VAL GLU GLU LEU PRO LEU ARG ILE ASN
SEQRES 18 A 677 GLU ALA PHE GLU ILE ALA THR SER GLY ARG PRO GLY PRO
SEQRES 19 A 677 VAL LEU VAL ASP LEU PRO LYS ASP VAL THR ALA ALA ILE
SEQRES 20 A 677 LEU ARG ASN PRO ILE PRO THR LYS THR THR LEU PRO SER
SEQRES 21 A 677 ASN ALA LEU ASN GLN LEU THR SER ARG ALA GLN ASP GLU
SEQRES 22 A 677 PHE VAL MET GLN SER ILE ASN LYS ALA ALA ASP LEU ILE
SEQRES 23 A 677 ASN LEU ALA LYS LYS PRO VAL LEU TYR VAL GLY ALA GLY
SEQRES 24 A 677 ILE LEU ASN HIS ALA ASP GLY PRO ARG LEU LEU LYS GLU
SEQRES 25 A 677 LEU SER ASP ARG ALA GLN ILE PRO VAL THR THR THR LEU
SEQRES 26 A 677 GLN GLY LEU GLY SER PHE ASP GLN GLU ASP PRO LYS SER
SEQRES 27 A 677 LEU ASP MET LEU GLY MET HIS GLY CYS ALA THR ALA ASN
SEQRES 28 A 677 LEU ALA VAL GLN ASN ALA ASP LEU ILE ILE ALA VAL GLY
SEQRES 29 A 677 ALA ARG PHE ASP ASP ARG VAL THR GLY ASN ILE SER LYS
SEQRES 30 A 677 PHE ALA PRO GLU ALA ARG ARG ALA ALA ALA GLU GLY ARG
SEQRES 31 A 677 GLY GLY ILE ILE HIS PHE GLU VAL SER PRO LYS ASN ILE
SEQRES 32 A 677 ASN LYS VAL VAL GLN THR GLN ILE ALA VAL GLU GLY ASP
SEQRES 33 A 677 ALA THR THR ASN LEU GLY LYS MET MET SER LYS ILE PHE
SEQRES 34 A 677 PRO VAL LYS GLU ARG SER GLU TRP PHE ALA GLN ILE ASN
SEQRES 35 A 677 LYS TRP LYS LYS GLU TYR PRO TYR ALA TYR MET GLU GLU
SEQRES 36 A 677 THR PRO GLY SER LYS ILE LYS PRO GLN THR VAL ILE LYS
SEQRES 37 A 677 LYS LEU SER LYS VAL ALA ASN ASP THR GLY ARG HIS VAL
SEQRES 38 A 677 ILE VAL THR THR GLY VAL GLY GLN HIS GLN MET TRP ALA
SEQRES 39 A 677 ALA GLN HIS TRP THR TRP ARG ASN PRO HIS THR PHE ILE
SEQRES 40 A 677 THR SER GLY GLY LEU GLY THR MET GLY TYR GLY LEU PRO
SEQRES 41 A 677 ALA ALA ILE GLY ALA GLN VAL ALA LYS PRO GLU SER LEU
SEQRES 42 A 677 VAL ILE ASP ILE ASP GLY ASP ALA SER PHE ASN MET THR
SEQRES 43 A 677 LEU THR GLU LEU SER SER ALA VAL GLN ALA GLY THR PRO
SEQRES 44 A 677 VAL LYS ILE LEU ILE LEU ASN ASN GLU GLU GLN GLY MET
SEQRES 45 A 677 VAL THR GLN TRP GLN SER LEU PHE TYR GLU HIS ARG TYR
SEQRES 46 A 677 SER HIS THR HIS GLN LEU ASN PRO ASP PHE ILE LYS LEU
SEQRES 47 A 677 ALA GLU ALA MET GLY LEU LYS GLY LEU ARG VAL LYS LYS
SEQRES 48 A 677 GLN GLU GLU LEU ASP ALA LYS LEU LYS GLU PHE VAL SER
SEQRES 49 A 677 THR LYS GLY PRO VAL LEU LEU GLU VAL GLU VAL ASP LYS
SEQRES 50 A 677 LYS VAL PRO VAL LEU PRO MET VAL ALA GLY GLY SER GLY
SEQRES 51 A 677 LEU ASP GLU PHE ILE ASN PHE ASP PRO GLU VAL GLU ARG
SEQRES 52 A 677 GLN GLN THR GLU LEU ARG HIS LYS ARG THR GLY GLY LYS
SEQRES 53 A 677 HIS
SEQRES 1 B 677 MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO
SEQRES 2 B 677 ARG GLY SER GLY MET LYS GLU THR ALA ALA ALA LYS PHE
SEQRES 3 B 677 GLU ARG GLN HIS MET ASP SER PRO ASP LEU GLY THR ASP
SEQRES 4 B 677 ASP ASP ASP LYS ALA MET GLY SER ALA PRO SER PHE ASN
SEQRES 5 B 677 VAL ASP PRO LEU GLU GLN PRO ALA GLU PRO SER LYS LEU
SEQRES 6 B 677 ALA LYS LYS LEU ARG ALA GLU PRO ASP MET ASP THR SER
SEQRES 7 B 677 PHE VAL GLY LEU THR GLY GLY GLN ILE PHE ASN GLU MET
SEQRES 8 B 677 MET SER ARG GLN ASN VAL ASP THR VAL PHE GLY TYR PRO
SEQRES 9 B 677 GLY GLY ALA ILE LEU PRO VAL TYR ASP ALA ILE HIS ASN
SEQRES 10 B 677 SER ASP LYS PHE ASN PHE VAL LEU PRO LYS HIS GLU GLN
SEQRES 11 B 677 GLY ALA GLY HIS MET ALA GLU GLY TYR ALA ARG ALA SER
SEQRES 12 B 677 GLY LYS PRO GLY VAL VAL LEU VAL THR SER GLY PRO GLY
SEQRES 13 B 677 ALA THR ASN VAL VAL THR PRO MET ALA ASP ALA PHE ALA
SEQRES 14 B 677 ASP GLY ILE PRO MET VAL VAL PHE THR GLY GLN VAL PRO
SEQRES 15 B 677 THR SER ALA ILE GLY THR ASP ALA PHE GLN GLU ALA ASP
SEQRES 16 B 677 VAL VAL GLY ILE SER ARG SER CYS THR LYS TRP ASN VAL
SEQRES 17 B 677 MET VAL LYS SER VAL GLU GLU LEU PRO LEU ARG ILE ASN
SEQRES 18 B 677 GLU ALA PHE GLU ILE ALA THR SER GLY ARG PRO GLY PRO
SEQRES 19 B 677 VAL LEU VAL ASP LEU PRO LYS ASP VAL THR ALA ALA ILE
SEQRES 20 B 677 LEU ARG ASN PRO ILE PRO THR LYS THR THR LEU PRO SER
SEQRES 21 B 677 ASN ALA LEU ASN GLN LEU THR SER ARG ALA GLN ASP GLU
SEQRES 22 B 677 PHE VAL MET GLN SER ILE ASN LYS ALA ALA ASP LEU ILE
SEQRES 23 B 677 ASN LEU ALA LYS LYS PRO VAL LEU TYR VAL GLY ALA GLY
SEQRES 24 B 677 ILE LEU ASN HIS ALA ASP GLY PRO ARG LEU LEU LYS GLU
SEQRES 25 B 677 LEU SER ASP ARG ALA GLN ILE PRO VAL THR THR THR LEU
SEQRES 26 B 677 GLN GLY LEU GLY SER PHE ASP GLN GLU ASP PRO LYS SER
SEQRES 27 B 677 LEU ASP MET LEU GLY MET HIS GLY CYS ALA THR ALA ASN
SEQRES 28 B 677 LEU ALA VAL GLN ASN ALA ASP LEU ILE ILE ALA VAL GLY
SEQRES 29 B 677 ALA ARG PHE ASP ASP ARG VAL THR GLY ASN ILE SER LYS
SEQRES 30 B 677 PHE ALA PRO GLU ALA ARG ARG ALA ALA ALA GLU GLY ARG
SEQRES 31 B 677 GLY GLY ILE ILE HIS PHE GLU VAL SER PRO LYS ASN ILE
SEQRES 32 B 677 ASN LYS VAL VAL GLN THR GLN ILE ALA VAL GLU GLY ASP
SEQRES 33 B 677 ALA THR THR ASN LEU GLY LYS MET MET SER LYS ILE PHE
SEQRES 34 B 677 PRO VAL LYS GLU ARG SER GLU TRP PHE ALA GLN ILE ASN
SEQRES 35 B 677 LYS TRP LYS LYS GLU TYR PRO TYR ALA TYR MET GLU GLU
SEQRES 36 B 677 THR PRO GLY SER LYS ILE LYS PRO GLN THR VAL ILE LYS
SEQRES 37 B 677 LYS LEU SER LYS VAL ALA ASN ASP THR GLY ARG HIS VAL
SEQRES 38 B 677 ILE VAL THR THR GLY VAL GLY GLN HIS GLN MET TRP ALA
SEQRES 39 B 677 ALA GLN HIS TRP THR TRP ARG ASN PRO HIS THR PHE ILE
SEQRES 40 B 677 THR SER GLY GLY LEU GLY THR MET GLY TYR GLY LEU PRO
SEQRES 41 B 677 ALA ALA ILE GLY ALA GLN VAL ALA LYS PRO GLU SER LEU
SEQRES 42 B 677 VAL ILE ASP ILE ASP GLY ASP ALA SER PHE ASN MET THR
SEQRES 43 B 677 LEU THR GLU LEU SER SER ALA VAL GLN ALA GLY THR PRO
SEQRES 44 B 677 VAL LYS ILE LEU ILE LEU ASN ASN GLU GLU GLN GLY MET
SEQRES 45 B 677 VAL THR GLN TRP GLN SER LEU PHE TYR GLU HIS ARG TYR
SEQRES 46 B 677 SER HIS THR HIS GLN LEU ASN PRO ASP PHE ILE LYS LEU
SEQRES 47 B 677 ALA GLU ALA MET GLY LEU LYS GLY LEU ARG VAL LYS LYS
SEQRES 48 B 677 GLN GLU GLU LEU ASP ALA LYS LEU LYS GLU PHE VAL SER
SEQRES 49 B 677 THR LYS GLY PRO VAL LEU LEU GLU VAL GLU VAL ASP LYS
SEQRES 50 B 677 LYS VAL PRO VAL LEU PRO MET VAL ALA GLY GLY SER GLY
SEQRES 51 B 677 LEU ASP GLU PHE ILE ASN PHE ASP PRO GLU VAL GLU ARG
SEQRES 52 B 677 GLN GLN THR GLU LEU ARG HIS LYS ARG THR GLY GLY LYS
SEQRES 53 B 677 HIS
HET K A1696 1
HET MG A1699 1
HET 1CS A 695 23
HET FAD A 701 53
HET NSP A 704 10
HET P22 A1702 11
HET YF3 A1705 14
HET K B 696 1
HET MG B 699 1
HET P25 B 698 14
HET 1CS B1695 23
HET FAD B1701 53
HETNAM K POTASSIUM ION
HETNAM MG MAGNESIUM ION
HETNAM 1CS 1-(2-CHLOROPHENYLSULFONYL)-3-(4-METHOXY-6-METHYL-L,3,5-
HETNAM 2 1CS TRIAZIN-2-YL)UREA
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM NSP 5-(AMINOMETHYL)-2-METHYLPYRIMIDIN-4-AMINE
HETNAM P22 ETHYL DIHYDROGEN DIPHOSPHATE
HETNAM YF3 2-{[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)
HETNAM 2 YF3 METHYL]AMINO}PROPANE-1-THIOL
HETNAM P25 PENTYL TRIHYDROGEN DIPHOSPHATE
FORMUL 3 K 2(K 1+)
FORMUL 4 MG 2(MG 2+)
FORMUL 5 1CS 2(C12 H12 CL N5 O4 S)
FORMUL 6 FAD 2(C27 H33 N9 O15 P2)
FORMUL 7 NSP C6 H10 N4
FORMUL 8 P22 C2 H8 O7 P2
FORMUL 9 YF3 C9 H16 N4 S
FORMUL 12 P25 C5 H14 O7 P2
FORMUL 15 HOH *1360(H2 O)
HELIX 1 1 THR A 93 GLN A 105 1 13
HELIX 2 2 GLY A 115 ALA A 117 5 3
HELIX 3 3 ILE A 118 ILE A 125 1 8
HELIX 4 4 HIS A 138 GLY A 154 1 17
HELIX 5 5 GLY A 164 ASN A 169 1 6
HELIX 6 6 VAL A 170 GLY A 181 1 12
HELIX 7 7 ASP A 205 SER A 210 1 6
HELIX 8 8 ARG A 211 THR A 214 5 4
HELIX 9 9 SER A 222 GLU A 224 5 3
HELIX 10 10 GLU A 225 SER A 239 1 15
HELIX 11 11 LYS A 251 ALA A 256 1 6
HELIX 12 12 PHE A 284 LEU A 298 1 15
HELIX 13 13 ALA A 308 HIS A 313 5 6
HELIX 14 14 ASP A 315 ALA A 327 1 13
HELIX 15 15 LEU A 335 LEU A 338 5 4
HELIX 16 16 CYS A 357 ALA A 367 1 11
HELIX 17 17 ASN A 384 PHE A 388 5 5
HELIX 18 18 ALA A 389 GLU A 398 1 10
HELIX 19 19 SER A 409 ILE A 413 5 5
HELIX 20 20 ASP A 426 SER A 436 1 11
HELIX 21 21 ARG A 444 TYR A 458 1 15
HELIX 22 22 LYS A 472 ASP A 486 1 15
HELIX 23 23 GLY A 498 TRP A 508 1 11
HELIX 24 24 TYR A 527 LYS A 539 1 13
HELIX 25 25 ASP A 550 LEU A 557 1 8
HELIX 26 26 GLU A 559 GLY A 567 1 9
HELIX 27 27 GLN A 580 TYR A 591 1 12
HELIX 28 28 ASP A 604 MET A 612 1 9
HELIX 29 29 LYS A 621 GLU A 623 5 3
HELIX 30 30 GLU A 624 THR A 635 1 12
HELIX 31 31 ASP A 668 THR A 683 1 16
HELIX 32 32 THR B 93 GLN B 105 1 13
HELIX 33 33 ILE B 118 ILE B 125 1 8
HELIX 34 34 HIS B 138 GLY B 154 1 17
HELIX 35 35 GLY B 164 ASN B 169 1 6
HELIX 36 36 VAL B 170 GLY B 181 1 12
HELIX 37 37 ASP B 205 SER B 210 1 6
HELIX 38 38 ARG B 211 THR B 214 5 4
HELIX 39 39 SER B 222 GLU B 224 5 3
HELIX 40 40 GLU B 225 SER B 239 1 15
HELIX 41 41 LYS B 251 ALA B 256 1 6
HELIX 42 42 PRO B 263 LEU B 268 5 6
HELIX 43 43 SER B 278 ALA B 299 1 22
HELIX 44 44 ALA B 308 HIS B 313 5 6
HELIX 45 45 ASP B 315 GLN B 328 1 14
HELIX 46 46 LEU B 335 LEU B 338 5 4
HELIX 47 47 CYS B 357 ALA B 367 1 11
HELIX 48 48 ASN B 384 PHE B 388 5 5
HELIX 49 49 ALA B 389 GLU B 398 1 10
HELIX 50 50 SER B 409 ILE B 413 5 5
HELIX 51 51 ASP B 426 MET B 435 1 10
HELIX 52 52 SER B 436 ILE B 438 5 3
HELIX 53 53 ARG B 444 TYR B 458 1 15
HELIX 54 54 LYS B 472 THR B 487 1 16
HELIX 55 55 GLY B 498 TRP B 508 1 11
HELIX 56 56 TYR B 527 LYS B 539 1 13
HELIX 57 57 ASP B 550 LEU B 557 1 8
HELIX 58 58 GLU B 559 GLY B 567 1 9
HELIX 59 59 GLN B 580 TYR B 591 1 12
HELIX 60 60 ASP B 604 MET B 612 1 9
HELIX 61 61 LYS B 621 GLU B 623 5 3
HELIX 62 62 GLU B 624 THR B 635 1 12
HELIX 63 63 ASP B 668 THR B 683 1 16
SHEET 1 A 6 ASN A 132 VAL A 134 0
SHEET 2 A 6 THR A 109 GLY A 112 1 N VAL A 110 O VAL A 134
SHEET 3 A 6 GLY A 157 VAL A 161 1 O VAL A 158 N PHE A 111
SHEET 4 A 6 MET A 184 GLN A 190 1 O PHE A 187 N VAL A 159
SHEET 5 A 6 PRO A 244 PRO A 250 1 O LEU A 249 N THR A 188
SHEET 6 A 6 TRP A 216 MET A 219 1 N VAL A 218 O ASP A 248
SHEET 1 B 6 SER A 348 MET A 351 0
SHEET 2 B 6 VAL A 331 THR A 333 1 N VAL A 331 O LEU A 349
SHEET 3 B 6 PRO A 302 VAL A 306 1 N LEU A 304 O THR A 332
SHEET 4 B 6 LEU A 369 VAL A 373 1 O ILE A 371 N VAL A 303
SHEET 5 B 6 GLY A 402 GLU A 407 1 O PHE A 406 N ALA A 372
SHEET 6 B 6 ILE A 421 GLU A 424 1 O ILE A 421 N HIS A 405
SHEET 1 C 6 PHE A 516 ILE A 517 0
SHEET 2 C 6 VAL A 491 THR A 495 1 N VAL A 493 O ILE A 517
SHEET 3 C 6 LEU A 543 GLY A 549 1 O ILE A 545 N ILE A 492
SHEET 4 C 6 LYS A 571 ASN A 576 1 O LEU A 573 N ASP A 548
SHEET 5 C 6 VAL A 639 GLU A 644 1 O LEU A 641 N ILE A 572
SHEET 6 C 6 LYS A 615 VAL A 619 1 N LEU A 617 O LEU A 640
SHEET 1 D 6 ASN B 132 VAL B 134 0
SHEET 2 D 6 THR B 109 GLY B 112 1 N VAL B 110 O VAL B 134
SHEET 3 D 6 GLY B 157 VAL B 161 1 O VAL B 158 N PHE B 111
SHEET 4 D 6 MET B 184 GLN B 190 1 O PHE B 187 N VAL B 159
SHEET 5 D 6 PRO B 244 PRO B 250 1 O LEU B 249 N THR B 188
SHEET 6 D 6 TRP B 216 MET B 219 1 N VAL B 218 O ASP B 248
SHEET 1 E 6 SER B 348 MET B 351 0
SHEET 2 E 6 VAL B 331 THR B 333 1 N VAL B 331 O LEU B 349
SHEET 3 E 6 PRO B 302 VAL B 306 1 N VAL B 306 O THR B 332
SHEET 4 E 6 LEU B 369 VAL B 373 1 O VAL B 373 N TYR B 305
SHEET 5 E 6 GLY B 402 GLU B 407 1 O PHE B 406 N ALA B 372
SHEET 6 E 6 ILE B 421 GLU B 424 1 O VAL B 423 N HIS B 405
SHEET 1 F 6 PHE B 516 ILE B 517 0
SHEET 2 F 6 VAL B 491 THR B 495 1 N VAL B 493 O ILE B 517
SHEET 3 F 6 LEU B 543 GLY B 549 1 O ILE B 545 N ILE B 492
SHEET 4 F 6 LYS B 571 ASN B 576 1 O LEU B 573 N ASP B 548
SHEET 5 F 6 VAL B 639 GLU B 644 1 O LEU B 641 N ILE B 572
SHEET 6 F 6 LYS B 615 VAL B 619 1 N LEU B 617 O GLU B 642
LINK OE1 GLN A 343 K K A1696 1555 1555 2.79
LINK OD2 ASP A 350 K K A1696 1555 1555 2.89
LINK O GLN A 506 K K A1696 1555 1555 2.58
LINK O TRP A 508 K K A1696 1555 1555 2.66
LINK OD1 ASP A 550 MG MG A1699 1555 1555 2.19
LINK OD1 ASN A 577 MG MG A1699 1555 1555 2.16
LINK O GLU A 579 MG MG A1699 1555 1555 2.23
LINK K K A1696 O HOH A4034 1555 1555 2.69
LINK K K A1696 O HOH A4147 1555 1555 3.48
LINK K K A1696 O HOH A4492 1555 1555 2.93
LINK MG MG A1699 O3B P22 A1702 1555 1555 2.13
LINK MG MG A1699 O1A P22 A1702 1555 1555 2.08
LINK MG MG A1699 O HOH A4051 1555 1555 2.13
LINK OE1 GLN B 343 K K B 696 1555 1555 2.75
LINK OD2 ASP B 350 K K B 696 1555 1555 2.84
LINK O GLN B 506 K K B 696 1555 1555 2.72
LINK O TRP B 508 K K B 696 1555 1555 2.67
LINK OD1 ASP B 550 MG MG B 699 1555 1555 2.08
LINK OD1 ASN B 577 MG MG B 699 1555 1555 2.22
LINK O GLU B 579 MG MG B 699 1555 1555 2.17
LINK K K B 696 O HOH B4232 1555 1555 2.74
LINK K K B 696 O HOH B4657 1555 1555 3.67
LINK K K B 696 O HOH B4676 1555 1555 3.71
LINK K K B 696 O HOH B5202 1555 1555 3.02
LINK O3B P25 B 698 MG MG B 699 1555 1555 2.03
LINK O1A P25 B 698 MG MG B 699 1555 1555 2.12
LINK MG MG B 699 O HOH B4246 1555 1555 2.18
CISPEP 1 LEU A 652 PRO A 653 0 -0.10
CISPEP 2 LEU B 652 PRO B 653 0 0.09
SITE 1 AC1 6 GLN B 343 ASP B 350 GLN B 506 TRP B 508
SITE 2 AC1 6 HOH B4232 HOH B5202
SITE 1 AC2 5 ASP B 550 ASN B 577 GLU B 579 P25 B 698
SITE 2 AC2 5 HOH B4246
SITE 1 AC3 6 GLN A 343 ASP A 350 GLN A 506 TRP A 508
SITE 2 AC3 6 HOH A4034 HOH A4492
SITE 1 AC4 5 ASP A 550 ASN A 577 GLU A 579 P22 A1702
SITE 2 AC4 5 HOH A4051
SITE 1 AC5 11 ASP A 379 ARG A 380 MET A 582 TRP A 586
SITE 2 AC5 11 FAD A 701 HOH A4808 HOH A5138 GLY B 116
SITE 3 AC5 11 VAL B 191 ALA B 200 PHE B 201
SITE 1 AC6 17 NSP A 704 VAL B 497 GLY B 498 GLN B 499
SITE 2 AC6 17 HIS B 500 MET B 525 GLY B 549 ASP B 550
SITE 3 AC6 17 ALA B 551 SER B 552 ASN B 577 GLU B 579
SITE 4 AC6 17 GLN B 580 GLY B 581 MET B 582 MG B 699
SITE 5 AC6 17 HOH B4246
SITE 1 AC7 37 ASP A 180 ARG A 241 GLY A 307 ALA A 308
SITE 2 AC7 37 GLY A 309 ASN A 312 THR A 334 LEU A 335
SITE 3 AC7 37 LEU A 352 MET A 354 HIS A 355 GLY A 374
SITE 4 AC7 37 ALA A 375 ARG A 376 ASP A 378 ARG A 380
SITE 5 AC7 37 VAL A 381 GLU A 407 VAL A 408 SER A 409
SITE 6 AC7 37 ASN A 412 GLY A 425 ASP A 426 ALA A 427
SITE 7 AC7 37 GLN A 501 MET A 502 SER A 519 GLY A 520
SITE 8 AC7 37 GLY A 521 1CS A 695 HOH A4014 HOH A4015
SITE 9 AC7 37 HOH A4031 HOH A4144 HOH A4325 HOH A4534
SITE 10 AC7 37 PHE B 201
SITE 1 AC8 10 GLU A 139 PRO A 165 ASN A 169 GLN A 202
SITE 2 AC8 10 GLY B 523 MET B 525 MET B 555 VAL B 583
SITE 3 AC8 10 P25 B 698 HOH B4820
SITE 1 AC9 15 GLY A 116 VAL A 191 PRO A 192 ALA A 200
SITE 2 AC9 15 PHE A 201 LYS A 251 HOH A4076 MET B 354
SITE 3 AC9 15 ASP B 379 ARG B 380 MET B 582 TRP B 586
SITE 4 AC9 15 FAD B1701 HOH B4593 HOH B4816
SITE 1 BC1 40 PHE A 201 ASP B 180 ARG B 241 GLY B 307
SITE 2 BC1 40 ALA B 308 GLY B 309 ASN B 312 THR B 334
SITE 3 BC1 40 LEU B 335 GLN B 336 MET B 351 LEU B 352
SITE 4 BC1 40 GLY B 353 MET B 354 HIS B 355 GLY B 374
SITE 5 BC1 40 ALA B 375 ARG B 376 ASP B 378 ARG B 380
SITE 6 BC1 40 VAL B 381 PHE B 406 GLU B 407 VAL B 408
SITE 7 BC1 40 ASN B 412 GLY B 425 ASP B 426 ALA B 427
SITE 8 BC1 40 GLN B 501 MET B 502 SER B 519 GLY B 520
SITE 9 BC1 40 GLY B 521 1CS B1695 HOH B4204 HOH B4212
SITE 10 BC1 40 HOH B4229 HOH B4259 HOH B4539 HOH B5172
SITE 1 BC2 16 VAL A 497 GLY A 498 GLN A 499 HIS A 500
SITE 2 BC2 16 GLY A 549 ASP A 550 ALA A 551 SER A 552
SITE 3 BC2 16 ASN A 577 GLU A 579 GLN A 580 GLY A 581
SITE 4 BC2 16 MET A 582 MG A1699 YF3 A1705 HOH A4051
SITE 1 BC3 12 GLY A 523 MET A 525 MET A 555 GLN A 580
SITE 2 BC3 12 VAL A 583 P22 A1702 TYR B 113 PRO B 114
SITE 3 BC3 12 GLU B 139 PRO B 165 ASN B 169 GLN B 202
CRYST1 154.579 154.579 178.759 90.00 90.00 90.00 P 4 2 2 16
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 0.006469 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006469 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005594 0.00000
(ATOM LINES ARE NOT SHOWN.)
END