HEADER LYASE 14-OCT-02 1N0H
TITLE CRYSTAL STRUCTURE OF YEAST ACETOHYDROXYACID SYNTHASE IN COMPLEX WITH A
TITLE 2 SULFONYLUREA HERBICIDE, CHLORIMURON ETHYL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETOLACTATE SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: MATURE CATALYTIC SUBUNIT;
COMPND 5 SYNONYM: ACETOHYDROXY-ACID SYNTHASE, ALS, AHAS;
COMPND 6 EC: 4.1.3.18;
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;
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: PET30C
KEYWDS ACETOHYDROXYACID SYNTHASE, SULFONYLUREA, HERBICIDE INHIBITION,
KEYWDS 2 THIAMINE DIPHOSPHATE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.S.PANG,L.W.GUDDAT,R.G.DUGGLEBY
REVDAT 4 11-OCT-17 1N0H 1 REMARK
REVDAT 3 24-FEB-09 1N0H 1 VERSN
REVDAT 2 15-APR-03 1N0H 1 JRNL
REVDAT 1 07-JAN-03 1N0H 0
JRNL AUTH S.S.PANG,L.W.GUDDAT,R.G.DUGGLEBY
JRNL TITL MOLECULAR BASIS OF SULFONYLUREA HERBICIDE INHIBITION OF
JRNL TITL 2 ACETOHYDROXYACID SYNTHASE
JRNL REF J.BIOL.CHEM. V. 278 7639 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 14557277
JRNL DOI 10.1074/JBC.M211648200
REMARK 2
REMARK 2 RESOLUTION. 2.80 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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.70
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) (%) : 95.3
REMARK 3 NUMBER OF REFLECTIONS : 50877
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) : 0.163
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 5203
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.90
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 73.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2460
REMARK 3 BIN FREE R VALUE : 0.2780
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 386
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 : 9106
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 230
REMARK 3 SOLVENT ATOMS : 832
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.17900
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : -3.17900
REMARK 3 B13 (A**2) : 6.35800
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.31
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) : 0.31
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.37
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.210
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.830
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ANISOTROPIC
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 1N0H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-OCT-02.
REMARK 100 THE DEPOSITION ID IS D_1000017365.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JUL-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-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
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 : 52457
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 48.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 10.90
REMARK 200 R MERGE (I) : 0.09100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.91
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.26900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
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 1JSC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: POTASSIUM PHOSPHATE, THIAMINE
REMARK 280 DIPHOSPHATE, FAD, MAGNESIUM CHLORIDE, DTT, CHLORIMURON ETHYL,
REMARK 280 TRIS-HCL, LITHIUM SULFATE, SODIUM POTASSIUM TARTRATE, PH 7.0,
REMARK 280 VAPOR 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 BIOLOGICAL UNIT IS A DIMER, WHICH IS THE SAME ASSEMBLY
REMARK 300 FOUND IN THE ASYMMETRIC UNIT OF THE CRYSTAL STRUCTURE
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: 14100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -99.0 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 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 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 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 265 CG CD CE NZ
REMARK 470 THR A 277 OG1 CG2
REMARK 470 LYS A 453 CG CD CE NZ
REMARK 470 LYS A 456 CG CD CE NZ
REMARK 470 SER B 278 OG
REMARK 470 ARG B 279 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 456 CG CD CE NZ
REMARK 470 LYS B 636 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 MET A 582 CA MET A 582 CB 0.140
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 ASN A 127 16.37 55.80
REMARK 500 THR A 266 -6.35 -52.88
REMARK 500 PRO A 269 170.38 -47.26
REMARK 500 ASP A 350 -168.51 76.93
REMARK 500 ALA A 389 59.40 35.48
REMARK 500 ARG A 444 58.90 -140.17
REMARK 500 TYR A 460 68.74 -68.45
REMARK 500 ARG A 511 -31.57 -141.60
REMARK 500 PRO A 569 49.65 -69.06
REMARK 500 GLU A 663 61.79 -112.70
REMARK 500 ASN B 127 18.14 54.79
REMARK 500 PRO B 269 99.35 -50.72
REMARK 500 ARG B 279 -163.12 54.15
REMARK 500 ASP B 350 -147.89 86.67
REMARK 500 SER B 445 -35.68 -35.49
REMARK 500 TYR B 458 72.74 -113.75
REMARK 500 ARG B 511 -30.43 -141.64
REMARK 500 GLU B 592 50.15 36.42
REMARK 500 GLU B 663 45.75 -99.61
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 A 696 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 753 O
REMARK 620 2 GLN A 343 NE2 51.4
REMARK 620 3 GLN A 343 OE1 78.7 38.0
REMARK 620 4 GLN A 506 O 91.1 139.4 163.8
REMARK 620 5 TRP A 508 O 101.4 107.0 76.0 93.9
REMARK 620 6 HOH A1382 O 172.5 121.4 96.1 95.1 82.5
REMARK 620 7 ASP A 350 OD2 75.2 55.6 84.5 105.2 160.6 99.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 699 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 550 OD1
REMARK 620 2 ASN A 577 OD1 86.4
REMARK 620 3 HOH A 771 O 76.2 88.6
REMARK 620 4 AYD A 700 O3B 159.5 97.7 83.8
REMARK 620 5 AYD A 700 O1A 89.4 175.7 90.8 86.5
REMARK 620 6 GLU A 579 O 104.8 86.4 174.8 95.5 94.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B1696 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 350 OD2
REMARK 620 2 GLN B 506 O 98.6
REMARK 620 3 HOH B1017 O 67.9 93.5
REMARK 620 4 GLN B 343 NE2 63.0 143.4 51.0
REMARK 620 5 TRP B 508 O 170.4 90.9 113.3 109.7
REMARK 620 6 GLN B 343 OE1 95.5 163.0 83.1 39.9 75.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1699 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B1032 O
REMARK 620 2 ASP B 550 OD1 78.6
REMARK 620 3 TPP B1702 O3B 79.6 158.1
REMARK 620 4 GLU B 579 O 172.1 108.6 93.0
REMARK 620 5 TPP B1702 O3A 59.9 118.5 50.0 117.3
REMARK 620 6 TPP B1702 O1A 97.6 99.1 86.0 84.7 50.5
REMARK 620 7 ASN B 577 OD1 88.6 83.4 93.9 89.0 133.2 173.7
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 696
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 699
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 1696
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1699
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIE A 695
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTT A 698
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AYD A 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIE B 1695
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTT B 1698
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TPP B 1702
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 1701
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JSC RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN THE ABSENCE OF THE HERBICIDAL INHIBITOR
DBREF 1N0H A 58 687 UNP P07342 ILVB_YEAST 58 687
DBREF 1N0H B 58 687 UNP P07342 ILVB_YEAST 58 687
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 A 696 1
HET MG A 699 1
HET CIE A 695 27
HET DTT A 698 8
HET AYD A 700 24
HET FAD A 701 53
HET K B1696 1
HET MG B1699 1
HET CIE B1695 27
HET DTT B1698 8
HET TPP B1702 26
HET FAD B1701 53
HETNAM K POTASSIUM ION
HETNAM MG MAGNESIUM ION
HETNAM CIE 2-[[[[(4-CHLORO-6-METHOXY-2-PYRIMIDINYL)
HETNAM 2 CIE AMINO]CARBONYL]AMINO]SULFONYL]BENZOIC ACID ETHYL ESTER
HETNAM DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE
HETNAM AYD 4-{[(4'-AMINO-2'-METHYLPYRIMIDIN-5'-YL)
HETNAM 2 AYD METHYL]AMINO}PENT-3-ENYL DIPHOSPHATE
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM TPP THIAMINE DIPHOSPHATE
HETSYN CIE CHLORIMURON ETHYL
HETSYN DTT 1,4-DITHIOTHREITOL
FORMUL 3 K 2(K 1+)
FORMUL 4 MG 2(MG 2+)
FORMUL 5 CIE 2(C15 H15 CL N4 O6 S)
FORMUL 6 DTT 2(C4 H10 O2 S2)
FORMUL 7 AYD C11 H20 N4 O7 P2
FORMUL 8 FAD 2(C27 H33 N9 O15 P2)
FORMUL 13 TPP C12 H19 N4 O7 P2 S 1+
FORMUL 15 HOH *832(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 ASP A 180 1 11
HELIX 7 7 PRO A 192 ILE A 196 5 5
HELIX 8 8 ASP A 205 SER A 210 1 6
HELIX 9 9 ARG A 211 THR A 214 5 4
HELIX 10 10 SER A 222 GLU A 224 5 3
HELIX 11 11 GLU A 225 SER A 239 1 15
HELIX 12 12 LYS A 251 ALA A 256 1 6
HELIX 13 14 SER A 278 ASN A 297 1 20
HELIX 14 15 ALA A 308 HIS A 313 5 6
HELIX 15 16 ASP A 315 GLN A 328 1 14
HELIX 16 17 LEU A 335 LEU A 338 5 4
HELIX 17 18 CYS A 357 ALA A 367 1 11
HELIX 18 19 ASN A 384 PHE A 388 5 5
HELIX 19 20 ALA A 389 GLU A 398 1 10
HELIX 20 21 SER A 409 ILE A 413 5 5
HELIX 21 22 ASP A 426 MET A 435 1 10
HELIX 22 23 SER A 436 ILE A 438 5 3
HELIX 23 24 ARG A 444 TYR A 458 1 15
HELIX 24 25 LYS A 472 ASP A 486 1 15
HELIX 25 26 GLY A 498 TRP A 508 1 11
HELIX 26 27 TYR A 527 LYS A 539 1 13
HELIX 27 28 ASP A 550 LEU A 557 1 8
HELIX 28 29 GLU A 559 GLY A 567 1 9
HELIX 29 30 GLN A 580 TYR A 591 1 12
HELIX 30 31 ASP A 604 GLY A 613 1 10
HELIX 31 32 LYS A 621 GLU A 623 5 3
HELIX 32 33 GLU A 624 THR A 635 1 12
HELIX 33 34 ASP A 668 THR A 683 1 16
HELIX 34 35 THR B 93 GLN B 105 1 13
HELIX 35 36 GLY B 115 ALA B 117 5 3
HELIX 36 37 ILE B 118 ILE B 125 1 8
HELIX 37 38 HIS B 138 GLY B 154 1 17
HELIX 38 39 GLY B 164 ASN B 169 1 6
HELIX 39 40 VAL B 170 ASP B 180 1 11
HELIX 40 41 ASP B 205 SER B 210 1 6
HELIX 41 42 ARG B 211 THR B 214 5 4
HELIX 42 43 SER B 222 GLU B 224 5 3
HELIX 43 44 GLU B 225 SER B 239 1 15
HELIX 44 45 LYS B 251 ALA B 256 1 6
HELIX 45 46 THR B 264 LEU B 268 1 5
HELIX 46 47 GLN B 281 ALA B 299 1 19
HELIX 47 48 ALA B 308 HIS B 313 5 6
HELIX 48 49 ASP B 315 ALA B 327 1 13
HELIX 49 50 LEU B 335 LEU B 338 5 4
HELIX 50 51 CYS B 357 ALA B 367 1 11
HELIX 51 52 ASP B 378 GLY B 383 1 6
HELIX 52 53 ASN B 384 PHE B 388 5 5
HELIX 53 54 ALA B 389 GLU B 398 1 10
HELIX 54 55 SER B 409 ILE B 413 5 5
HELIX 55 56 ASP B 426 SER B 436 1 11
HELIX 56 57 ARG B 444 TYR B 458 1 15
HELIX 57 58 LYS B 472 ASP B 486 1 15
HELIX 58 59 GLY B 498 TRP B 508 1 11
HELIX 59 60 TYR B 527 LYS B 539 1 13
HELIX 60 61 ASP B 550 LEU B 557 1 8
HELIX 61 62 GLU B 559 GLY B 567 1 9
HELIX 62 63 GLN B 580 PHE B 590 1 11
HELIX 63 64 ASP B 604 GLY B 613 1 10
HELIX 64 65 LYS B 621 GLU B 623 5 3
HELIX 65 66 GLU B 624 THR B 635 1 12
HELIX 66 67 ASP B 668 THR B 683 1 16
SHEET 1 A 2 MET A 85 ASP A 86 0
SHEET 2 A 2 ILE A 262 PRO A 263 -1 O ILE A 262 N ASP A 86
SHEET 1 B 6 ASN A 132 VAL A 134 0
SHEET 2 B 6 THR A 109 TYR A 113 1 N VAL A 110 O VAL A 134
SHEET 3 B 6 GLY A 157 VAL A 161 1 O VAL A 158 N PHE A 111
SHEET 4 B 6 MET A 184 GLN A 190 1 O PHE A 187 N VAL A 159
SHEET 5 B 6 PRO A 244 PRO A 250 1 O VAL A 245 N VAL A 186
SHEET 6 B 6 TRP A 216 MET A 219 1 N VAL A 218 O ASP A 248
SHEET 1 C 6 SER A 348 MET A 351 0
SHEET 2 C 6 VAL A 331 THR A 333 1 N VAL A 331 O LEU A 349
SHEET 3 C 6 PRO A 302 VAL A 306 1 N VAL A 306 O THR A 332
SHEET 4 C 6 LEU A 369 VAL A 373 1 O ILE A 371 N VAL A 303
SHEET 5 C 6 GLY A 402 GLU A 407 1 O PHE A 406 N ALA A 372
SHEET 6 C 6 ILE A 421 GLU A 424 1 O ILE A 421 N HIS A 405
SHEET 1 D 6 PHE A 516 ILE A 517 0
SHEET 2 D 6 VAL A 491 THR A 495 1 N VAL A 493 O ILE A 517
SHEET 3 D 6 LEU A 543 GLY A 549 1 O ILE A 545 N ILE A 492
SHEET 4 D 6 LYS A 571 ASN A 576 1 O LEU A 573 N ASP A 548
SHEET 5 D 6 VAL A 639 GLU A 644 1 O LEU A 641 N ILE A 572
SHEET 6 D 6 LYS A 615 VAL A 619 1 N LEU A 617 O GLU A 642
SHEET 1 E 2 MET B 85 ASP B 86 0
SHEET 2 E 2 ILE B 262 PRO B 263 -1 O ILE B 262 N ASP B 86
SHEET 1 F 6 ASN B 132 VAL B 134 0
SHEET 2 F 6 THR B 109 TYR B 113 1 N VAL B 110 O VAL B 134
SHEET 3 F 6 GLY B 157 VAL B 161 1 O VAL B 158 N PHE B 111
SHEET 4 F 6 MET B 184 GLN B 190 1 O PHE B 187 N VAL B 159
SHEET 5 F 6 PRO B 244 PRO B 250 1 O VAL B 245 N VAL B 186
SHEET 6 F 6 TRP B 216 MET B 219 1 N VAL B 218 O ASP B 248
SHEET 1 G 6 SER B 348 MET B 351 0
SHEET 2 G 6 VAL B 331 THR B 333 1 N VAL B 331 O LEU B 349
SHEET 3 G 6 PRO B 302 VAL B 306 1 N LEU B 304 O THR B 332
SHEET 4 G 6 LEU B 369 VAL B 373 1 O ILE B 371 N VAL B 303
SHEET 5 G 6 GLY B 402 GLU B 407 1 O PHE B 406 N ALA B 372
SHEET 6 G 6 ILE B 421 GLU B 424 1 O ILE B 421 N HIS B 405
SHEET 1 H 6 PHE B 516 ILE B 517 0
SHEET 2 H 6 VAL B 491 THR B 495 1 N VAL B 493 O ILE B 517
SHEET 3 H 6 LEU B 543 GLY B 549 1 O ILE B 545 N ILE B 492
SHEET 4 H 6 LYS B 571 ASN B 576 1 O LEU B 573 N ASP B 548
SHEET 5 H 6 VAL B 639 GLU B 644 1 O VAL B 639 N ILE B 572
SHEET 6 H 6 LYS B 615 VAL B 619 1 N LEU B 617 O LEU B 640
LINK SG CYS A 357 S1 DTT A 698 1555 1555 2.04
LINK SG CYS B 357 S1 DTT B1698 1555 1555 2.04
LINK K K A 696 O HOH A 753 1555 1555 2.74
LINK K K A 696 NE2 GLN A 343 1555 1555 3.66
LINK K K A 696 OE1 GLN A 343 1555 1555 2.80
LINK K K A 696 O GLN A 506 1555 1555 2.66
LINK K K A 696 O TRP A 508 1555 1555 2.61
LINK K K A 696 O HOH A1382 1555 1555 3.06
LINK K K A 696 OD2 ASP A 350 1555 1555 2.94
LINK MG MG A 699 OD1 ASP A 550 1555 1555 2.12
LINK MG MG A 699 OD1 ASN A 577 1555 1555 2.07
LINK MG MG A 699 O HOH A 771 1555 1555 2.19
LINK MG MG A 699 O3B AYD A 700 1555 1555 2.12
LINK MG MG A 699 O1A AYD A 700 1555 1555 2.20
LINK MG MG A 699 O GLU A 579 1555 1555 2.17
LINK K K B1696 OD2 ASP B 350 1555 1555 3.04
LINK K K B1696 O GLN B 506 1555 1555 2.72
LINK K K B1696 O HOH B1017 1555 1555 2.85
LINK K K B1696 NE2 GLN B 343 1555 1555 3.49
LINK K K B1696 O TRP B 508 1555 1555 2.66
LINK K K B1696 OE1 GLN B 343 1555 1555 2.82
LINK MG MG B1699 O HOH B1032 1555 1555 2.34
LINK MG MG B1699 OD1 ASP B 550 1555 1555 2.17
LINK MG MG B1699 O3B TPP B1702 1555 1555 2.40
LINK MG MG B1699 O GLU B 579 1555 1555 2.13
LINK MG MG B1699 O3A TPP B1702 1555 1555 3.09
LINK MG MG B1699 O1A TPP B1702 1555 1555 2.09
LINK MG MG B1699 OD1 ASN B 577 1555 1555 2.14
CISPEP 1 LEU A 652 PRO A 653 0 0.91
CISPEP 2 LEU B 652 PRO B 653 0 -0.13
SITE 1 AC1 6 GLN A 343 ASP A 350 GLN A 506 TRP A 508
SITE 2 AC1 6 HOH A 753 HOH A1382
SITE 1 AC2 5 ASP A 550 ASN A 577 GLU A 579 AYD A 700
SITE 2 AC2 5 HOH A 771
SITE 1 AC3 5 GLN B 343 ASP B 350 GLN B 506 TRP B 508
SITE 2 AC3 5 HOH B1017
SITE 1 AC4 5 ASP B 550 ASN B 577 GLU B 579 HOH B1032
SITE 2 AC4 5 TPP B1702
SITE 1 AC5 13 MET A 354 ASP A 379 ARG A 380 VAL A 583
SITE 2 AC5 13 TRP A 586 FAD A 701 GLY B 116 ALA B 117
SITE 3 AC5 13 VAL B 191 PRO B 192 PHE B 201 GLN B 202
SITE 4 AC5 13 LYS B 251
SITE 1 AC6 5 CYS A 357 THR A 359 LYS A 455 TYR A 458
SITE 2 AC6 5 TYR A 460
SITE 1 AC7 26 VAL A 497 GLY A 498 GLN A 499 HIS A 500
SITE 2 AC7 26 GLY A 523 MET A 525 GLY A 549 ASP A 550
SITE 3 AC7 26 ALA A 551 SER A 552 MET A 555 ASN A 577
SITE 4 AC7 26 GLU A 579 GLN A 580 GLY A 581 MET A 582
SITE 5 AC7 26 VAL A 583 MG A 699 HOH A 724 HOH A 771
SITE 6 AC7 26 HOH A1108 PRO B 114 GLU B 139 PRO B 165
SITE 7 AC7 26 ASN B 169 GLN B 202
SITE 1 AC8 36 ASP A 180 ARG A 241 GLY A 307 ALA A 308
SITE 2 AC8 36 GLY A 309 ASN A 312 THR A 334 LEU A 335
SITE 3 AC8 36 LEU A 352 GLY A 353 MET A 354 HIS A 355
SITE 4 AC8 36 GLY A 374 ALA A 375 ARG A 376 ASP A 378
SITE 5 AC8 36 ARG A 380 VAL A 381 PHE A 406 GLU A 407
SITE 6 AC8 36 VAL A 408 ASN A 412 GLY A 425 ASP A 426
SITE 7 AC8 36 ALA A 427 GLN A 501 MET A 502 GLY A 520
SITE 8 AC8 36 GLY A 521 MET A 582 CIE A 695 HOH A 725
SITE 9 AC8 36 HOH A 726 HOH A 747 HOH A 892 PHE B 201
SITE 1 AC9 14 GLY A 116 ALA A 117 VAL A 191 PRO A 192
SITE 2 AC9 14 PHE A 201 GLN A 202 LYS A 251 MET B 354
SITE 3 AC9 14 ASP B 379 ARG B 380 MET B 582 TRP B 586
SITE 4 AC9 14 HOH B1520 FAD B1701
SITE 1 BC1 7 ASP B 350 CYS B 357 THR B 359 LYS B 455
SITE 2 BC1 7 TYR B 458 PRO B 459 HOH B1018
SITE 1 BC2 25 TYR A 113 PRO A 114 GLU A 139 PRO A 165
SITE 2 BC2 25 ASN A 169 GLN A 202 VAL B 497 GLY B 498
SITE 3 BC2 25 GLN B 499 HIS B 500 GLY B 523 MET B 525
SITE 4 BC2 25 GLY B 549 ASP B 550 ALA B 551 SER B 552
SITE 5 BC2 25 MET B 555 ASN B 577 GLU B 579 GLN B 580
SITE 6 BC2 25 GLY B 581 MET B 582 VAL B 583 HOH B1032
SITE 7 BC2 25 MG B1699
SITE 1 BC3 36 PHE A 201 ASP B 180 ARG B 241 GLY B 307
SITE 2 BC3 36 ALA B 308 GLY B 309 ASN B 312 THR B 334
SITE 3 BC3 36 LEU B 335 LEU B 352 GLY B 353 MET B 354
SITE 4 BC3 36 HIS B 355 GLY B 374 ALA B 375 ARG B 376
SITE 5 BC3 36 ASP B 378 ARG B 380 VAL B 381 GLU B 407
SITE 6 BC3 36 VAL B 408 ASN B 412 GLY B 425 ASP B 426
SITE 7 BC3 36 ALA B 427 GLN B 501 MET B 502 GLY B 520
SITE 8 BC3 36 GLY B 521 MET B 582 HOH B 982 HOH B 991
SITE 9 BC3 36 HOH B1008 HOH B1013 HOH B1051 CIE B1695
CRYST1 153.976 153.976 178.298 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 0.006495 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006495 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005609 0.00000
(ATOM LINES ARE NOT SHOWN.)
END