HEADER OXIDOREDUCTASE 14-SEP-05 2B0M
TITLE HUMAN DIHYDROOROTATE DEHYDROGENASE BOUND TO A NOVEL INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROOROTATE DEHYDROGENASE, MITOCHONDRIAL;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DIHYDROOROTATE OXIDASE; DHODEHASE;
COMPND 5 EC: 1.3.3.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: DHODH;
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: PET-19B
KEYWDS TIM BARREL; ALPHA/BETA BARREL, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.E.HURT,A.E.SUTTON,J.CLARDY
REVDAT 4 23-AUG-23 2B0M 1 REMARK SEQADV
REVDAT 3 24-MAR-09 2B0M 1 JRNL
REVDAT 2 24-FEB-09 2B0M 1 VERSN
REVDAT 1 27-SEP-05 2B0M 0
JRNL AUTH D.E.HURT,A.E.SUTTON,J.CLARDY
JRNL TITL BREQUINAR DERIVATIVES AND SPECIES-SPECIFIC DRUG DESIGN FOR
JRNL TITL 2 DIHYDROOROTATE DEHYDROGENASE.
JRNL REF BIOORG.MED.CHEM.LETT. V. 16 1610 2006
JRNL REFN ISSN 0960-894X
JRNL PMID 16406782
JRNL DOI 10.1016/J.BMCL.2005.12.029
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.E.HURT,J.WIDOM,J.CLARDY
REMARK 1 TITL STRUCTURE OF PLASMODIUM FALCIPARUM DIHYROOROTATE
REMARK 1 TITL 2 DEHYDROGENASE WITH A BOUND INHIBITOR
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.500
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 35765
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.218
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1866
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.07
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2500
REMARK 3 BIN FREE R VALUE : 0.2900
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 156
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 : 2757
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 66
REMARK 3 SOLVENT ATOMS : 141
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.32
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.75300
REMARK 3 B22 (A**2) : -1.75300
REMARK 3 B33 (A**2) : 3.50500
REMARK 3 B12 (A**2) : -2.41100
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.16
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) : 0.28
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.16
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.220
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.810
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) : 1.223 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.815 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.056 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.034 ; 2.500
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 2B0M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1000034526.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-FEB-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : PAIR OF VERTICALLY DIFFRACTING
REMARK 200 SI(111) CRYSTALS WITH THE SECOND
REMARK 200 CRYSTAL PROVIDING SAGITTAL
REMARK 200 FOCUSING, PLUS A RHODIUM COATED
REMARK 200 SILICON MIRROR FOR VERTICAL
REMARK 200 FOCUSING
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37871
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.37000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 8.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1D3G
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 34.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, SODIUM ACETATE,
REMARK 280 C11DAO, C10DAO, PH 4.6, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.22133
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 41.11067
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 41.11067
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 82.22133
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 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 4
REMARK 465 GLY A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 HIS A 9
REMARK 465 HIS A 10
REMARK 465 HIS A 11
REMARK 465 HIS A 12
REMARK 465 HIS A 13
REMARK 465 HIS A 14
REMARK 465 HIS A 15
REMARK 465 SER A 16
REMARK 465 SER A 17
REMARK 465 GLY A 18
REMARK 465 HIS A 19
REMARK 465 ILE A 20
REMARK 465 ASP A 21
REMARK 465 ASP A 22
REMARK 465 ASP A 23
REMARK 465 ASP A 24
REMARK 465 LYS A 25
REMARK 465 HIS A 26
REMARK 465 MET A 27
REMARK 465 LEU A 28
REMARK 465 GLU A 29
REMARK 465 MET A 30
REMARK 465 ALA A 31
REMARK 465 THR A 32
REMARK 465 ARG A 70
REMARK 465 ALA A 71
REMARK 465 ARG A 72
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 34 99.48 58.26
REMARK 500 HIS A 41 -65.69 -127.86
REMARK 500 ASP A 99 77.23 -116.96
REMARK 500 ARG A 146 48.80 -141.11
REMARK 500 THR A 283 123.41 55.38
REMARK 500 ASN A 284 -156.61 -92.90
REMARK 500 SER A 337 -0.49 -140.94
REMARK 500 TYR A 356 -64.31 -149.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 201 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORO A 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1D3G RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH BREQUINAR
REMARK 900 RELATED ID: 1D3H RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH A77 1726
REMARK 900 RELATED ID: 1TV5 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN FROM PLASMODIUM FALCIPARUM COMPLEXED WITH A77 1726
REMARK 900 RELATED ID: 1F76 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN FROM E. COLI (NO INHIBITOR BOUND)
REMARK 900 RELATED ID: 1UUM RELATED DB: PDB
REMARK 900 THE SAME PROTEIN FROM RAT COMPLEXED WITH ATOVAQUONE
REMARK 900 RELATED ID: 1UUO RELATED DB: PDB
REMARK 900 THE SAME PROTEIN FROM RAT COMPLEXED WITH BREQUINAR
DBREF 2B0M A 30 396 UNP Q02127 PYRD_HUMAN 29 395
SEQADV 2B0M MET A 4 UNP Q02127 EXPRESSION TAG
SEQADV 2B0M GLY A 5 UNP Q02127 EXPRESSION TAG
SEQADV 2B0M HIS A 6 UNP Q02127 EXPRESSION TAG
SEQADV 2B0M HIS A 7 UNP Q02127 EXPRESSION TAG
SEQADV 2B0M HIS A 8 UNP Q02127 EXPRESSION TAG
SEQADV 2B0M HIS A 9 UNP Q02127 EXPRESSION TAG
SEQADV 2B0M HIS A 10 UNP Q02127 EXPRESSION TAG
SEQADV 2B0M HIS A 11 UNP Q02127 EXPRESSION TAG
SEQADV 2B0M HIS A 12 UNP Q02127 EXPRESSION TAG
SEQADV 2B0M HIS A 13 UNP Q02127 EXPRESSION TAG
SEQADV 2B0M HIS A 14 UNP Q02127 EXPRESSION TAG
SEQADV 2B0M HIS A 15 UNP Q02127 EXPRESSION TAG
SEQADV 2B0M SER A 16 UNP Q02127 EXPRESSION TAG
SEQADV 2B0M SER A 17 UNP Q02127 EXPRESSION TAG
SEQADV 2B0M GLY A 18 UNP Q02127 EXPRESSION TAG
SEQADV 2B0M HIS A 19 UNP Q02127 EXPRESSION TAG
SEQADV 2B0M ILE A 20 UNP Q02127 EXPRESSION TAG
SEQADV 2B0M ASP A 21 UNP Q02127 EXPRESSION TAG
SEQADV 2B0M ASP A 22 UNP Q02127 EXPRESSION TAG
SEQADV 2B0M ASP A 23 UNP Q02127 EXPRESSION TAG
SEQADV 2B0M ASP A 24 UNP Q02127 EXPRESSION TAG
SEQADV 2B0M LYS A 25 UNP Q02127 EXPRESSION TAG
SEQADV 2B0M HIS A 26 UNP Q02127 EXPRESSION TAG
SEQADV 2B0M MET A 27 UNP Q02127 EXPRESSION TAG
SEQADV 2B0M LEU A 28 UNP Q02127 EXPRESSION TAG
SEQADV 2B0M GLU A 29 UNP Q02127 EXPRESSION TAG
SEQRES 1 A 393 MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER
SEQRES 2 A 393 SER GLY HIS ILE ASP ASP ASP ASP LYS HIS MET LEU GLU
SEQRES 3 A 393 MET ALA THR GLY ASP GLU ARG PHE TYR ALA GLU HIS LEU
SEQRES 4 A 393 MET PRO THR LEU GLN GLY LEU LEU ASP PRO GLU SER ALA
SEQRES 5 A 393 HIS ARG LEU ALA VAL ARG PHE THR SER LEU GLY LEU LEU
SEQRES 6 A 393 PRO ARG ALA ARG PHE GLN ASP SER ASP MET LEU GLU VAL
SEQRES 7 A 393 ARG VAL LEU GLY HIS LYS PHE ARG ASN PRO VAL GLY ILE
SEQRES 8 A 393 ALA ALA GLY PHE ASP LYS HIS GLY GLU ALA VAL ASP GLY
SEQRES 9 A 393 LEU TYR LYS MET GLY PHE GLY PHE VAL GLU ILE GLY SER
SEQRES 10 A 393 VAL THR PRO LYS PRO GLN GLU GLY ASN PRO ARG PRO ARG
SEQRES 11 A 393 VAL PHE ARG LEU PRO GLU ASP GLN ALA VAL ILE ASN ARG
SEQRES 12 A 393 TYR GLY PHE ASN SER HIS GLY LEU SER VAL VAL GLU HIS
SEQRES 13 A 393 ARG LEU ARG ALA ARG GLN GLN LYS GLN ALA LYS LEU THR
SEQRES 14 A 393 GLU ASP GLY LEU PRO LEU GLY VAL ASN LEU GLY LYS ASN
SEQRES 15 A 393 LYS THR SER VAL ASP ALA ALA GLU ASP TYR ALA GLU GLY
SEQRES 16 A 393 VAL ARG VAL LEU GLY PRO LEU ALA ASP TYR LEU VAL VAL
SEQRES 17 A 393 ASN VAL SER SER PRO ASN THR ALA GLY LEU ARG SER LEU
SEQRES 18 A 393 GLN GLY LYS ALA GLU LEU ARG ARG LEU LEU THR LYS VAL
SEQRES 19 A 393 LEU GLN GLU ARG ASP GLY LEU ARG ARG VAL HIS ARG PRO
SEQRES 20 A 393 ALA VAL LEU VAL LYS ILE ALA PRO ASP LEU THR SER GLN
SEQRES 21 A 393 ASP LYS GLU ASP ILE ALA SER VAL VAL LYS GLU LEU GLY
SEQRES 22 A 393 ILE ASP GLY LEU ILE VAL THR ASN THR THR VAL SER ARG
SEQRES 23 A 393 PRO ALA GLY LEU GLN GLY ALA LEU ARG SER GLU THR GLY
SEQRES 24 A 393 GLY LEU SER GLY LYS PRO LEU ARG ASP LEU SER THR GLN
SEQRES 25 A 393 THR ILE ARG GLU MET TYR ALA LEU THR GLN GLY ARG VAL
SEQRES 26 A 393 PRO ILE ILE GLY VAL GLY GLY VAL SER SER GLY GLN ASP
SEQRES 27 A 393 ALA LEU GLU LYS ILE ARG ALA GLY ALA SER LEU VAL GLN
SEQRES 28 A 393 LEU TYR THR ALA LEU THR PHE TRP GLY PRO PRO VAL VAL
SEQRES 29 A 393 GLY LYS VAL LYS ARG GLU LEU GLU ALA LEU LEU LYS GLU
SEQRES 30 A 393 GLN GLY PHE GLY GLY VAL THR ASP ALA ILE GLY ALA ASP
SEQRES 31 A 393 HIS ARG ARG
HET 201 A 401 24
HET FMN A 402 31
HET ORO A 403 11
HETNAM 201 3-AMIDO-5-BIPHENYL-BENZOIC ACID
HETNAM FMN FLAVIN MONONUCLEOTIDE
HETNAM ORO OROTIC ACID
HETSYN 201 5-(AMINOCARBONYL)-1,1':4',1''-TERPHENYL-3-CARBOXYLIC
HETSYN 2 201 ACID
HETSYN FMN RIBOFLAVIN MONOPHOSPHATE
FORMUL 2 201 C20 H15 N O3
FORMUL 3 FMN C17 H21 N4 O9 P
FORMUL 4 ORO C5 H4 N2 O4
FORMUL 5 HOH *141(H2 O)
HELIX 1 1 ASP A 34 HIS A 41 1 8
HELIX 2 2 HIS A 41 GLY A 48 1 8
HELIX 3 3 ASP A 51 LEU A 65 1 15
HELIX 4 4 SER A 76 GLU A 80 5 5
HELIX 5 5 ALA A 104 MET A 111 1 8
HELIX 6 6 PRO A 138 ASP A 140 5 3
HELIX 7 7 GLY A 153 ALA A 163 1 11
HELIX 8 8 ARG A 164 ASP A 174 1 11
HELIX 9 9 ASP A 190 GLY A 203 1 14
HELIX 10 10 PRO A 204 ALA A 206 5 3
HELIX 11 11 LEU A 221 GLN A 225 5 5
HELIX 12 12 GLY A 226 GLY A 243 1 18
HELIX 13 13 ARG A 245 ARG A 249 5 5
HELIX 14 14 THR A 261 GLY A 276 1 16
HELIX 15 15 LEU A 309 THR A 324 1 16
HELIX 16 16 SER A 338 GLY A 349 1 12
HELIX 17 17 TYR A 356 GLY A 363 1 8
HELIX 18 18 PRO A 364 GLN A 381 1 18
HELIX 19 19 GLY A 385 ILE A 390 1 6
HELIX 20 20 GLY A 391 ARG A 396 1 6
SHEET 1 A 2 VAL A 81 VAL A 83 0
SHEET 2 A 2 HIS A 86 PHE A 88 -1 O PHE A 88 N VAL A 81
SHEET 1 B 9 VAL A 92 ILE A 94 0
SHEET 2 B 9 PHE A 115 VAL A 121 1 O PHE A 115 N ILE A 94
SHEET 3 B 9 LEU A 178 LEU A 182 1 O GLY A 179 N VAL A 116
SHEET 4 B 9 TYR A 208 ASN A 212 1 O VAL A 210 N LEU A 182
SHEET 5 B 9 ALA A 251 LYS A 255 1 O ALA A 251 N LEU A 209
SHEET 6 B 9 GLY A 279 VAL A 282 1 O ILE A 281 N VAL A 254
SHEET 7 B 9 ILE A 330 VAL A 333 1 O ILE A 331 N LEU A 280
SHEET 8 B 9 LEU A 352 LEU A 355 1 O LEU A 352 N GLY A 332
SHEET 9 B 9 VAL A 92 ILE A 94 1 N GLY A 93 O VAL A 353
SHEET 1 C 3 VAL A 134 LEU A 137 0
SHEET 2 C 3 ALA A 142 ASN A 145 -1 O ILE A 144 N PHE A 135
SHEET 3 C 3 GLY A 303 GLY A 306 -1 O GLY A 303 N ASN A 145
CISPEP 1 ARG A 131 PRO A 132 0 0.01
SITE 1 AC1 13 TYR A 38 LEU A 46 GLN A 47 ALA A 55
SITE 2 AC1 13 HIS A 56 ALA A 59 LEU A 67 LEU A 68
SITE 3 AC1 13 ARG A 136 TYR A 356 THR A 360 HOH A 496
SITE 4 AC1 13 HOH A 524
SITE 1 AC2 24 ALA A 95 ALA A 96 GLY A 97 LYS A 100
SITE 2 AC2 24 SER A 120 ASN A 145 TYR A 147 ASN A 181
SITE 3 AC2 24 ASN A 212 LYS A 255 THR A 283 ASN A 284
SITE 4 AC2 24 THR A 285 SER A 305 GLY A 306 VAL A 333
SITE 5 AC2 24 GLY A 334 GLY A 335 LEU A 355 TYR A 356
SITE 6 AC2 24 THR A 357 ORO A 403 HOH A 407 HOH A 419
SITE 1 AC3 11 LYS A 100 ASN A 145 TYR A 147 GLY A 148
SITE 2 AC3 11 PHE A 149 ASN A 212 SER A 215 ASN A 217
SITE 3 AC3 11 ASN A 284 THR A 285 FMN A 402
CRYST1 90.398 90.398 123.332 90.00 90.00 120.00 P 32 2 1 6
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.011062 0.006387 0.000000 0.00000
SCALE2 0.000000 0.012774 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008108 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
