HEADER OXIDOREDUCTASE 30-NOV-09 3KVL
TITLE CRYSTAL STRUCTURE OF HUMAN DIHYDROOROTATE DEHYDROGENASE (DHODH) WITH
TITLE 2 AMINO-BENZOIC ACID INHIBITOR 715 AT 1.85A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROOROTATE DEHYDROGENASE, MITOCHONDRIAL;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DHODEHASE, DIHYDROOROTATE OXIDASE;
COMPND 5 EC: 1.3.5.2;
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;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PYRD;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET19B
KEYWDS PROTEIN-ANTIPROLIFERATIVE AGENT COMPLEX, OXIDOREDUCTASE,
KEYWDS 2 FLAVOPROTEIN, FMN, MEMBRANE, MITOCHONDRION, MITOCHONDRION INNER
KEYWDS 3 MEMBRANE, POLYMORPHISM, PYRIMIDINE BIOSYNTHESIS, TRANSIT PEPTIDE,
KEYWDS 4 TRANSMEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.MCLEAN,Y.ZHANG
REVDAT 4 06-SEP-23 3KVL 1 REMARK SEQADV
REVDAT 3 01-NOV-17 3KVL 1 REMARK
REVDAT 2 09-MAR-10 3KVL 1 JRNL
REVDAT 1 02-MAR-10 3KVL 0
JRNL AUTH L.R.MCLEAN,Y.ZHANG,W.DEGNEN,J.PEPPARD,D.CABEL,C.ZOU,
JRNL AUTH 2 J.T.TSAY,A.SUBRAMANIAM,R.J.VAZ,Y.LI
JRNL TITL DISCOVERY OF NOVEL INHIBITORS FOR DHODH VIA VIRTUAL
JRNL TITL 2 SCREENING AND X-RAY CRYSTALLOGRAPHIC STRUCTURES.
JRNL REF BIOORG.MED.CHEM.LETT. V. 20 1981 2010
JRNL REFN ISSN 0960-894X
JRNL PMID 20153645
JRNL DOI 10.1016/J.BMCL.2010.01.115
REMARK 2
REMARK 2 RESOLUTION. 1.85 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 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.74
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 225676.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 48450
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.191
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2418
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.1770
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.1760
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.194
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 2506
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : 0.0040
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 50123
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.97
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7207
REMARK 3 BIN R VALUE (WORKING SET) : 0.1920
REMARK 3 BIN FREE R VALUE : 0.2180
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 375
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.011
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2741
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 89
REMARK 3 SOLVENT ATOMS : 302
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.26
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.13000
REMARK 3 B22 (A**2) : 1.13000
REMARK 3 B33 (A**2) : -2.26000
REMARK 3 B12 (A**2) : 1.12000
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) : 0.17
REMARK 3 ESD FROM SIGMAA (A) : 0.09
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) : 0.19
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.09
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.004
REMARK 3 BOND ANGLES (DEGREES) : 0.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 19.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.710
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.160 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.720 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.080 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.220 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.39
REMARK 3 BSOL : 49.88
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : 715.PAR
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : 715.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3KVL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-DEC-09.
REMARK 100 THE DEPOSITION ID IS D_1000056502.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-NOV-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50141
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.08500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.41000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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 (%): 64.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4 M AMMONIUM SULFATE, 15% GLYCEROL,
REMARK 280 0.1 M NA-ACETATE, PH 5.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
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 82.14533
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 41.07267
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 41.07267
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 82.14533
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 7
REMARK 465 GLY 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 HIS A 16
REMARK 465 HIS A 17
REMARK 465 HIS A 18
REMARK 465 SER A 19
REMARK 465 SER A 20
REMARK 465 GLY A 21
REMARK 465 HIS A 22
REMARK 465 ILE A 23
REMARK 465 ASP A 24
REMARK 465 ASP A 25
REMARK 465 ASP A 26
REMARK 465 ASP A 27
REMARK 465 LYS A 28
REMARK 465 HIS A 29
REMARK 465 MET A 30
REMARK 465 ALA A 31
REMARK 465 THR A 32
REMARK 465 GLY A 33
REMARK 465 ASP A 34
REMARK 465 GLU A 35
REMARK 465 ARG A 36
REMARK 465 ARG A 396
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 HIS A 41 -56.73 -130.17
REMARK 500 ASP A 99 79.45 -109.22
REMARK 500 ARG A 133 10.49 -142.86
REMARK 500 LEU A 137 77.23 -119.48
REMARK 500 TYR A 356 -62.39 -140.23
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 SO4 A 397
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN A 398
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DOR A 399
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DET A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 7Z5 A 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3KVJ RELATED DB: PDB
REMARK 900 RELATED ID: 3KVK RELATED DB: PDB
REMARK 900 RELATED ID: 3KVM RELATED DB: PDB
DBREF 3KVL A 30 396 UNP Q02127 PYRD_HUMAN 29 395
SEQADV 3KVL MET A 7 UNP Q02127 EXPRESSION TAG
SEQADV 3KVL GLY A 8 UNP Q02127 EXPRESSION TAG
SEQADV 3KVL HIS A 9 UNP Q02127 EXPRESSION TAG
SEQADV 3KVL HIS A 10 UNP Q02127 EXPRESSION TAG
SEQADV 3KVL HIS A 11 UNP Q02127 EXPRESSION TAG
SEQADV 3KVL HIS A 12 UNP Q02127 EXPRESSION TAG
SEQADV 3KVL HIS A 13 UNP Q02127 EXPRESSION TAG
SEQADV 3KVL HIS A 14 UNP Q02127 EXPRESSION TAG
SEQADV 3KVL HIS A 15 UNP Q02127 EXPRESSION TAG
SEQADV 3KVL HIS A 16 UNP Q02127 EXPRESSION TAG
SEQADV 3KVL HIS A 17 UNP Q02127 EXPRESSION TAG
SEQADV 3KVL HIS A 18 UNP Q02127 EXPRESSION TAG
SEQADV 3KVL SER A 19 UNP Q02127 EXPRESSION TAG
SEQADV 3KVL SER A 20 UNP Q02127 EXPRESSION TAG
SEQADV 3KVL GLY A 21 UNP Q02127 EXPRESSION TAG
SEQADV 3KVL HIS A 22 UNP Q02127 EXPRESSION TAG
SEQADV 3KVL ILE A 23 UNP Q02127 EXPRESSION TAG
SEQADV 3KVL ASP A 24 UNP Q02127 EXPRESSION TAG
SEQADV 3KVL ASP A 25 UNP Q02127 EXPRESSION TAG
SEQADV 3KVL ASP A 26 UNP Q02127 EXPRESSION TAG
SEQADV 3KVL ASP A 27 UNP Q02127 EXPRESSION TAG
SEQADV 3KVL LYS A 28 UNP Q02127 EXPRESSION TAG
SEQADV 3KVL HIS A 29 UNP Q02127 EXPRESSION TAG
SEQRES 1 A 390 MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER
SEQRES 2 A 390 SER GLY HIS ILE ASP ASP ASP ASP LYS HIS MET ALA THR
SEQRES 3 A 390 GLY ASP GLU ARG PHE TYR ALA GLU HIS LEU MET PRO THR
SEQRES 4 A 390 LEU GLN GLY LEU LEU ASP PRO GLU SER ALA HIS ARG LEU
SEQRES 5 A 390 ALA VAL ARG PHE THR SER LEU GLY LEU LEU PRO ARG ALA
SEQRES 6 A 390 ARG PHE GLN ASP SER ASP MET LEU GLU VAL ARG VAL LEU
SEQRES 7 A 390 GLY HIS LYS PHE ARG ASN PRO VAL GLY ILE ALA ALA GLY
SEQRES 8 A 390 PHE ASP LYS HIS GLY GLU ALA VAL ASP GLY LEU TYR LYS
SEQRES 9 A 390 MET GLY PHE GLY PHE VAL GLU ILE GLY SER VAL THR PRO
SEQRES 10 A 390 LYS PRO GLN GLU GLY ASN PRO ARG PRO ARG VAL PHE ARG
SEQRES 11 A 390 LEU PRO GLU ASP GLN ALA VAL ILE ASN ARG TYR GLY PHE
SEQRES 12 A 390 ASN SER HIS GLY LEU SER VAL VAL GLU HIS ARG LEU ARG
SEQRES 13 A 390 ALA ARG GLN GLN LYS GLN ALA LYS LEU THR GLU ASP GLY
SEQRES 14 A 390 LEU PRO LEU GLY VAL ASN LEU GLY LYS ASN LYS THR SER
SEQRES 15 A 390 VAL ASP ALA ALA GLU ASP TYR ALA GLU GLY VAL ARG VAL
SEQRES 16 A 390 LEU GLY PRO LEU ALA ASP TYR LEU VAL VAL ASN VAL SER
SEQRES 17 A 390 SER PRO ASN THR ALA GLY LEU ARG SER LEU GLN GLY LYS
SEQRES 18 A 390 ALA GLU LEU ARG ARG LEU LEU THR LYS VAL LEU GLN GLU
SEQRES 19 A 390 ARG ASP GLY LEU ARG ARG VAL HIS ARG PRO ALA VAL LEU
SEQRES 20 A 390 VAL LYS ILE ALA PRO ASP LEU THR SER GLN ASP LYS GLU
SEQRES 21 A 390 ASP ILE ALA SER VAL VAL LYS GLU LEU GLY ILE ASP GLY
SEQRES 22 A 390 LEU ILE VAL THR ASN THR THR VAL SER ARG PRO ALA GLY
SEQRES 23 A 390 LEU GLN GLY ALA LEU ARG SER GLU THR GLY GLY LEU SER
SEQRES 24 A 390 GLY LYS PRO LEU ARG ASP LEU SER THR GLN THR ILE ARG
SEQRES 25 A 390 GLU MET TYR ALA LEU THR GLN GLY ARG VAL PRO ILE ILE
SEQRES 26 A 390 GLY VAL GLY GLY VAL SER SER GLY GLN ASP ALA LEU GLU
SEQRES 27 A 390 LYS ILE ARG ALA GLY ALA SER LEU VAL GLN LEU TYR THR
SEQRES 28 A 390 ALA LEU THR PHE TRP GLY PRO PRO VAL VAL GLY LYS VAL
SEQRES 29 A 390 LYS ARG GLU LEU GLU ALA LEU LEU LYS GLU GLN GLY PHE
SEQRES 30 A 390 GLY GLY VAL THR ASP ALA ILE GLY ALA ASP HIS ARG ARG
HET SO4 A 397 5
HET FMN A 398 31
HET DOR A 399 11
HET DET A 400 15
HET ACT A 401 4
HET 7Z5 A 402 23
HETNAM SO4 SULFATE ION
HETNAM FMN FLAVIN MONONUCLEOTIDE
HETNAM DOR (4S)-2,6-DIOXOHEXAHYDROPYRIMIDINE-4-CARBOXYLIC ACID
HETNAM DET UNDECYLAMINE-N,N-DIMETHYL-N-OXIDE
HETNAM ACT ACETATE ION
HETNAM 7Z5 5-[METHYL(PYRIDIN-3-YLMETHYL)AMINO]-2-(PROPANOYLAMINO)
HETNAM 2 7Z5 BENZOIC ACID
HETSYN FMN RIBOFLAVIN MONOPHOSPHATE
HETSYN DOR DIHYDROOROTIC ACID
FORMUL 2 SO4 O4 S 2-
FORMUL 3 FMN C17 H21 N4 O9 P
FORMUL 4 DOR C5 H6 N2 O4
FORMUL 5 DET C13 H29 N O
FORMUL 6 ACT C2 H3 O2 1-
FORMUL 7 7Z5 C17 H19 N3 O3
FORMUL 8 HOH *302(H2 O)
HELIX 1 1 HIS A 41 GLY A 48 1 8
HELIX 2 2 ASP A 51 LEU A 65 1 15
HELIX 3 3 SER A 76 GLU A 80 5 5
HELIX 4 4 ALA A 104 MET A 111 1 8
HELIX 5 5 PRO A 138 ASP A 140 5 3
HELIX 6 6 GLY A 153 ALA A 163 1 11
HELIX 7 7 ARG A 164 ASP A 174 1 11
HELIX 8 8 ASP A 190 GLY A 203 1 14
HELIX 9 9 PRO A 204 ALA A 206 5 3
HELIX 10 10 GLY A 220 GLN A 225 5 6
HELIX 11 11 GLY A 226 GLY A 243 1 18
HELIX 12 12 ARG A 245 ARG A 249 5 5
HELIX 13 13 THR A 261 GLY A 276 1 16
HELIX 14 14 LEU A 309 THR A 324 1 16
HELIX 15 15 SER A 338 GLY A 349 1 12
HELIX 16 16 TYR A 356 GLY A 363 1 8
HELIX 17 17 PRO A 364 GLN A 381 1 18
HELIX 18 18 GLY A 385 ILE A 390 1 6
HELIX 19 19 GLY A 391 ARG A 395 5 5
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 ILE A 256 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 ALA A 142 N LEU A 137
SHEET 3 C 3 GLY A 303 GLY A 306 -1 O SER A 305 N VAL A 143
CISPEP 1 GLY A 119 SER A 120 0 4.73
CISPEP 2 ARG A 131 PRO A 132 0 -1.97
CISPEP 3 VAL A 282 THR A 283 0 10.38
SITE 1 AC1 5 ARG A 245 VAL A 247 HIS A 248 HOH A 606
SITE 2 AC1 5 HOH A 695
SITE 1 AC2 26 ALA A 95 ALA A 96 GLY A 97 LYS A 100
SITE 2 AC2 26 GLY A 119 SER A 120 ASN A 145 TYR A 147
SITE 3 AC2 26 ASN A 181 ASN A 212 LYS A 255 THR A 283
SITE 4 AC2 26 ASN A 284 THR A 285 SER A 305 GLY A 306
SITE 5 AC2 26 LEU A 309 VAL A 333 GLY A 334 GLY A 335
SITE 6 AC2 26 LEU A 355 TYR A 356 THR A 357 DOR A 399
SITE 7 AC2 26 HOH A 405 HOH A 409
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 398
SITE 1 AC4 9 GLU A 53 HIS A 56 ARG A 57 HIS A 101
SITE 2 AC4 9 GLN A 126 TYR A 147 ASN A 150 SER A 151
SITE 3 AC4 9 HOH A 568
SITE 1 AC5 7 LYS A 307 PRO A 308 ASP A 311 THR A 314
SITE 2 AC5 7 GLN A 315 ARG A 318 HOH A 429
SITE 1 AC6 12 MET A 43 LEU A 46 GLN A 47 ALA A 55
SITE 2 AC6 12 HIS A 56 ALA A 59 THR A 63 LEU A 68
SITE 3 AC6 12 ARG A 136 TYR A 356 THR A 360 HOH A 688
CRYST1 90.695 90.695 123.218 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 0.011026 0.006366 0.000000 0.00000
SCALE2 0.000000 0.012732 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008116 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
