HEADER OXIDOREDUCTASE 31-JUL-09 3II4
TITLE STRUCTURE OF MYCOBACTERIAL LIPOAMIDE DEHYDROGENASE BOUND TO A
TITLE 2 TRIAZASPIRODIMETHOXYBENZOYL INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROLIPOYL DEHYDROGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DIHYDROLIPOAMIDE DEHYDROGENASE, E3 COMPONENT OF ALPHA KETO
COMPND 5 ACID DEHYDROGENASE COMPLEXES;
COMPND 6 EC: 1.8.1.4;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: LPD, LPD RV0462, MT0478, MTV038.06, RV0462;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) CODON PLUS RIL;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PSMT3
KEYWDS DIHYDROLIPOYL DEHYDROGENASE, DHLDH, E3, PROTEIN-N6-(DIHYDROLIPOYL)
KEYWDS 2 LYSINE, NAD+ OXIDOREDUCTASE, NAD+, NADH, CYTOPLASM, DISULFIDE BOND,
KEYWDS 3 FAD, FLAVOPROTEIN, GLYCOLYSIS, NAD, OXIDOREDUCTASE, REDOX-ACTIVE
KEYWDS 4 CENTER
EXPDTA X-RAY DIFFRACTION
AUTHOR C.D.LIMA
REVDAT 5 06-SEP-23 3II4 1 REMARK SEQADV
REVDAT 4 24-JUL-19 3II4 1 REMARK
REVDAT 3 01-NOV-17 3II4 1 REMARK
REVDAT 2 09-MAR-10 3II4 1 JRNL
REVDAT 1 26-JAN-10 3II4 0
JRNL AUTH R.BRYK,N.ARANGO,A.VENUGOPAL,J.D.WARREN,Y.H.PARK,M.S.PATEL,
JRNL AUTH 2 C.D.LIMA,C.NATHAN
JRNL TITL TRIAZASPIRODIMETHOXYBENZOYLS AS SELECTIVE INHIBITORS OF
JRNL TITL 2 MYCOBACTERIAL LIPOAMIDE DEHYDROGENASE .
JRNL REF BIOCHEMISTRY V. 49 1616 2010
JRNL REFN ISSN 0006-2960
JRNL PMID 20078138
JRNL DOI 10.1021/BI9016186
REMARK 2
REMARK 2 RESOLUTION. 2.42 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
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) : 2.42
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.66
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2137803.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 39110
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) : 0.185
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1942
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.42
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.51
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3418
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE : 0.3110
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 162
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.024
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6930
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 192
REMARK 3 SOLVENT ATOMS : 751
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.04000
REMARK 3 B22 (A**2) : 5.74000
REMARK 3 B33 (A**2) : -3.70000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.27
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) : 0.35
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.36
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 : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.140 ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.830 ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.830 ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.650 ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 50.57
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 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : IN5D.PAR
REMARK 3 PARAMETER FILE 5 : FAD_XPLOR.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : IN5D.TOP
REMARK 3 TOPOLOGY FILE 5 : FAD_XPLOR.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3II4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-AUG-09.
REMARK 100 THE DEPOSITION ID IS D_1000054439.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-AUG-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC MULTILAYER
REMARK 200 OPTICS : OSMIC MULTILAYER
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39154
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.420
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.42
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.51
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.35600
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 2A8X
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MICROM LPD, 300 MICROM 3II, 600
REMARK 280 MICROM NADH, 100 MM TRIS PH 8.5, 10 MM NACL, 11% PEG 10000, 15%
REMARK 280 ETHYLENE GLYCOL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 41.95000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.90000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.20000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.90000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 41.95000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.20000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 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 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 570 O HOH A 756 2.16
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 LYS A 35 -61.17 -135.96
REMARK 500 CYS A 46 -75.15 -26.61
REMARK 500 ASN A 119 13.35 -141.25
REMARK 500 ALA A 179 38.56 -97.12
REMARK 500 ALA A 266 57.96 -147.98
REMARK 500 ASP A 295 5.13 -62.18
REMARK 500 GLN A 315 78.32 -68.87
REMARK 500 PHE A 350 36.91 -95.19
REMARK 500 ASN A 463 44.10 -94.76
REMARK 500 LYS B 35 -58.75 -135.66
REMARK 500 PHE B 62 19.83 -63.12
REMARK 500 THR B 63 -39.51 -133.28
REMARK 500 LYS B 251 114.73 -160.54
REMARK 500 ALA B 266 49.41 -151.90
REMARK 500 GLN B 315 71.20 -69.29
REMARK 500 PHE B 350 31.79 -95.69
REMARK 500 TRP B 429 46.09 -106.01
REMARK 500 ASP B 430 50.32 36.61
REMARK 500 ASN B 463 45.45 -85.07
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 FAD A 480
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3II A 465
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 580
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3II B 465
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2A8X RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF LIPOAMIDE DEHYDROGENASE FROM MYCOBACTERIUM
REMARK 900 TUBERCULOSIS
DBREF 3II4 A 1 464 UNP P66004 DLDH_MYCTU 1 464
DBREF 3II4 B 1 464 UNP P66004 DLDH_MYCTU 1 464
SEQADV 3II4 GLY A -1 UNP P66004 EXPRESSION TAG
SEQADV 3II4 SER A 0 UNP P66004 EXPRESSION TAG
SEQADV 3II4 GLY B -1 UNP P66004 EXPRESSION TAG
SEQADV 3II4 SER B 0 UNP P66004 EXPRESSION TAG
SEQRES 1 A 466 GLY SER MET THR HIS TYR ASP VAL VAL VAL LEU GLY ALA
SEQRES 2 A 466 GLY PRO GLY GLY TYR VAL ALA ALA ILE ARG ALA ALA GLN
SEQRES 3 A 466 LEU GLY LEU SER THR ALA ILE VAL GLU PRO LYS TYR TRP
SEQRES 4 A 466 GLY GLY VAL CYS LEU ASN VAL GLY CYS ILE PRO SER LYS
SEQRES 5 A 466 ALA LEU LEU ARG ASN ALA GLU LEU VAL HIS ILE PHE THR
SEQRES 6 A 466 LYS ASP ALA LYS ALA PHE GLY ILE SER GLY GLU VAL THR
SEQRES 7 A 466 PHE ASP TYR GLY ILE ALA TYR ASP ARG SER ARG LYS VAL
SEQRES 8 A 466 ALA GLU GLY ARG VAL ALA GLY VAL HIS PHE LEU MET LYS
SEQRES 9 A 466 LYS ASN LYS ILE THR GLU ILE HIS GLY TYR GLY THR PHE
SEQRES 10 A 466 ALA ASP ALA ASN THR LEU LEU VAL ASP LEU ASN ASP GLY
SEQRES 11 A 466 GLY THR GLU SER VAL THR PHE ASP ASN ALA ILE ILE ALA
SEQRES 12 A 466 THR GLY SER SER THR ARG LEU VAL PRO GLY THR SER LEU
SEQRES 13 A 466 SER ALA ASN VAL VAL THR TYR GLU GLU GLN ILE LEU SER
SEQRES 14 A 466 ARG GLU LEU PRO LYS SER ILE ILE ILE ALA GLY ALA GLY
SEQRES 15 A 466 ALA ILE GLY MET GLU PHE GLY TYR VAL LEU LYS ASN TYR
SEQRES 16 A 466 GLY VAL ASP VAL THR ILE VAL GLU PHE LEU PRO ARG ALA
SEQRES 17 A 466 LEU PRO ASN GLU ASP ALA ASP VAL SER LYS GLU ILE GLU
SEQRES 18 A 466 LYS GLN PHE LYS LYS LEU GLY VAL THR ILE LEU THR ALA
SEQRES 19 A 466 THR LYS VAL GLU SER ILE ALA ASP GLY GLY SER GLN VAL
SEQRES 20 A 466 THR VAL THR VAL THR LYS ASP GLY VAL ALA GLN GLU LEU
SEQRES 21 A 466 LYS ALA GLU LYS VAL LEU GLN ALA ILE GLY PHE ALA PRO
SEQRES 22 A 466 ASN VAL GLU GLY TYR GLY LEU ASP LYS ALA GLY VAL ALA
SEQRES 23 A 466 LEU THR ASP ARG LYS ALA ILE GLY VAL ASP ASP TYR MET
SEQRES 24 A 466 ARG THR ASN VAL GLY HIS ILE TYR ALA ILE GLY ASP VAL
SEQRES 25 A 466 ASN GLY LEU LEU GLN LEU ALA HIS VAL ALA GLU ALA GLN
SEQRES 26 A 466 GLY VAL VAL ALA ALA GLU THR ILE ALA GLY ALA GLU THR
SEQRES 27 A 466 LEU THR LEU GLY ASP HIS ARG MET LEU PRO ARG ALA THR
SEQRES 28 A 466 PHE CYS GLN PRO ASN VAL ALA SER PHE GLY LEU THR GLU
SEQRES 29 A 466 GLN GLN ALA ARG ASN GLU GLY TYR ASP VAL VAL VAL ALA
SEQRES 30 A 466 LYS PHE PRO PHE THR ALA ASN ALA LYS ALA HIS GLY VAL
SEQRES 31 A 466 GLY ASP PRO SER GLY PHE VAL LYS LEU VAL ALA ASP ALA
SEQRES 32 A 466 LYS HIS GLY GLU LEU LEU GLY GLY HIS LEU VAL GLY HIS
SEQRES 33 A 466 ASP VAL ALA GLU LEU LEU PRO GLU LEU THR LEU ALA GLN
SEQRES 34 A 466 ARG TRP ASP LEU THR ALA SER GLU LEU ALA ARG ASN VAL
SEQRES 35 A 466 HIS THR HIS PRO THR MET SER GLU ALA LEU GLN GLU CYS
SEQRES 36 A 466 PHE HIS GLY LEU VAL GLY HIS MET ILE ASN PHE
SEQRES 1 B 466 GLY SER MET THR HIS TYR ASP VAL VAL VAL LEU GLY ALA
SEQRES 2 B 466 GLY PRO GLY GLY TYR VAL ALA ALA ILE ARG ALA ALA GLN
SEQRES 3 B 466 LEU GLY LEU SER THR ALA ILE VAL GLU PRO LYS TYR TRP
SEQRES 4 B 466 GLY GLY VAL CYS LEU ASN VAL GLY CYS ILE PRO SER LYS
SEQRES 5 B 466 ALA LEU LEU ARG ASN ALA GLU LEU VAL HIS ILE PHE THR
SEQRES 6 B 466 LYS ASP ALA LYS ALA PHE GLY ILE SER GLY GLU VAL THR
SEQRES 7 B 466 PHE ASP TYR GLY ILE ALA TYR ASP ARG SER ARG LYS VAL
SEQRES 8 B 466 ALA GLU GLY ARG VAL ALA GLY VAL HIS PHE LEU MET LYS
SEQRES 9 B 466 LYS ASN LYS ILE THR GLU ILE HIS GLY TYR GLY THR PHE
SEQRES 10 B 466 ALA ASP ALA ASN THR LEU LEU VAL ASP LEU ASN ASP GLY
SEQRES 11 B 466 GLY THR GLU SER VAL THR PHE ASP ASN ALA ILE ILE ALA
SEQRES 12 B 466 THR GLY SER SER THR ARG LEU VAL PRO GLY THR SER LEU
SEQRES 13 B 466 SER ALA ASN VAL VAL THR TYR GLU GLU GLN ILE LEU SER
SEQRES 14 B 466 ARG GLU LEU PRO LYS SER ILE ILE ILE ALA GLY ALA GLY
SEQRES 15 B 466 ALA ILE GLY MET GLU PHE GLY TYR VAL LEU LYS ASN TYR
SEQRES 16 B 466 GLY VAL ASP VAL THR ILE VAL GLU PHE LEU PRO ARG ALA
SEQRES 17 B 466 LEU PRO ASN GLU ASP ALA ASP VAL SER LYS GLU ILE GLU
SEQRES 18 B 466 LYS GLN PHE LYS LYS LEU GLY VAL THR ILE LEU THR ALA
SEQRES 19 B 466 THR LYS VAL GLU SER ILE ALA ASP GLY GLY SER GLN VAL
SEQRES 20 B 466 THR VAL THR VAL THR LYS ASP GLY VAL ALA GLN GLU LEU
SEQRES 21 B 466 LYS ALA GLU LYS VAL LEU GLN ALA ILE GLY PHE ALA PRO
SEQRES 22 B 466 ASN VAL GLU GLY TYR GLY LEU ASP LYS ALA GLY VAL ALA
SEQRES 23 B 466 LEU THR ASP ARG LYS ALA ILE GLY VAL ASP ASP TYR MET
SEQRES 24 B 466 ARG THR ASN VAL GLY HIS ILE TYR ALA ILE GLY ASP VAL
SEQRES 25 B 466 ASN GLY LEU LEU GLN LEU ALA HIS VAL ALA GLU ALA GLN
SEQRES 26 B 466 GLY VAL VAL ALA ALA GLU THR ILE ALA GLY ALA GLU THR
SEQRES 27 B 466 LEU THR LEU GLY ASP HIS ARG MET LEU PRO ARG ALA THR
SEQRES 28 B 466 PHE CYS GLN PRO ASN VAL ALA SER PHE GLY LEU THR GLU
SEQRES 29 B 466 GLN GLN ALA ARG ASN GLU GLY TYR ASP VAL VAL VAL ALA
SEQRES 30 B 466 LYS PHE PRO PHE THR ALA ASN ALA LYS ALA HIS GLY VAL
SEQRES 31 B 466 GLY ASP PRO SER GLY PHE VAL LYS LEU VAL ALA ASP ALA
SEQRES 32 B 466 LYS HIS GLY GLU LEU LEU GLY GLY HIS LEU VAL GLY HIS
SEQRES 33 B 466 ASP VAL ALA GLU LEU LEU PRO GLU LEU THR LEU ALA GLN
SEQRES 34 B 466 ARG TRP ASP LEU THR ALA SER GLU LEU ALA ARG ASN VAL
SEQRES 35 B 466 HIS THR HIS PRO THR MET SER GLU ALA LEU GLN GLU CYS
SEQRES 36 B 466 PHE HIS GLY LEU VAL GLY HIS MET ILE ASN PHE
HET FAD A 480 53
HET 3II A 465 43
HET FAD B 580 53
HET 3II B 465 43
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM 3II N-[2-(2,4-DICHLOROPHENYL)ETHYL]-2-{8-[(2,4-
HETNAM 2 3II DIMETHOXYPHENYL)CARBONYL]-4-OXO-1-PHENYL-1,3,8-
HETNAM 3 3II TRIAZASPIRO[4.5]DEC-3-YL}ACETAMIDE
FORMUL 3 FAD 2(C27 H33 N9 O15 P2)
FORMUL 4 3II 2(C32 H34 CL2 N4 O5)
FORMUL 7 HOH *751(H2 O)
HELIX 1 1 GLY A 12 LEU A 25 1 14
HELIX 2 2 GLY A 38 GLY A 45 1 8
HELIX 3 3 GLY A 45 ALA A 66 1 22
HELIX 4 4 LYS A 67 PHE A 69 5 3
HELIX 5 5 ASP A 78 ASN A 104 1 27
HELIX 6 6 THR A 160 LEU A 166 1 7
HELIX 7 7 GLY A 180 TYR A 193 1 14
HELIX 8 8 ASP A 211 GLY A 226 1 16
HELIX 9 9 GLY A 277 GLY A 282 1 6
HELIX 10 10 GLY A 308 GLY A 312 5 5
HELIX 11 11 LEU A 316 GLY A 333 1 18
HELIX 12 12 ASP A 341 LEU A 345 5 5
HELIX 13 13 THR A 361 GLY A 369 1 9
HELIX 14 14 ASN A 382 GLY A 389 1 8
HELIX 15 15 ASP A 415 LEU A 419 5 5
HELIX 16 16 LEU A 420 TRP A 429 1 10
HELIX 17 17 THR A 432 ALA A 437 1 6
HELIX 18 18 SER A 447 GLY A 459 1 13
HELIX 19 19 GLY B 12 LEU B 25 1 14
HELIX 20 20 GLY B 38 GLY B 45 1 8
HELIX 21 21 GLY B 45 ASP B 65 1 21
HELIX 22 22 ASP B 78 ASN B 104 1 27
HELIX 23 23 THR B 160 LEU B 166 1 7
HELIX 24 24 GLY B 180 TYR B 193 1 14
HELIX 25 25 ASP B 211 GLY B 226 1 16
HELIX 26 26 GLY B 277 GLY B 282 1 6
HELIX 27 27 GLY B 308 GLY B 312 5 5
HELIX 28 28 LEU B 316 GLY B 333 1 18
HELIX 29 29 ASP B 341 LEU B 345 5 5
HELIX 30 30 THR B 361 GLU B 368 1 8
HELIX 31 31 ASN B 382 GLY B 389 1 8
HELIX 32 32 ASP B 415 GLU B 418 5 4
HELIX 33 33 LEU B 419 TRP B 429 1 11
HELIX 34 34 THR B 432 ALA B 437 1 6
HELIX 35 35 SER B 447 GLY B 459 1 13
SHEET 1 A 6 THR A 107 ILE A 109 0
SHEET 2 A 6 THR A 29 VAL A 32 1 N ILE A 31 O THR A 107
SHEET 3 A 6 HIS A 3 LEU A 9 1 N VAL A 8 O ALA A 30
SHEET 4 A 6 THR A 130 ILE A 140 1 O ILE A 139 N LEU A 9
SHEET 5 A 6 THR A 120 LEU A 125 -1 N LEU A 121 O VAL A 133
SHEET 6 A 6 GLY A 111 PHE A 115 -1 N THR A 114 O LEU A 122
SHEET 1 B 5 THR A 107 ILE A 109 0
SHEET 2 B 5 THR A 29 VAL A 32 1 N ILE A 31 O THR A 107
SHEET 3 B 5 HIS A 3 LEU A 9 1 N VAL A 8 O ALA A 30
SHEET 4 B 5 THR A 130 ILE A 140 1 O ILE A 139 N LEU A 9
SHEET 5 B 5 ILE A 304 ALA A 306 1 O TYR A 305 N ALA A 138
SHEET 1 C 2 ILE A 71 SER A 72 0
SHEET 2 C 2 THR B 76 PHE B 77 -1 O THR B 76 N SER A 72
SHEET 1 D 2 THR A 76 PHE A 77 0
SHEET 2 D 2 ILE B 71 SER B 72 -1 O SER B 72 N THR A 76
SHEET 1 E 2 SER A 144 THR A 146 0
SHEET 2 E 2 PHE A 269 PRO A 271 -1 O ALA A 270 N SER A 145
SHEET 1 F 5 VAL A 158 VAL A 159 0
SHEET 2 F 5 LYS A 262 GLN A 265 1 O GLN A 265 N VAL A 159
SHEET 3 F 5 SER A 173 ALA A 177 1 N ALA A 177 O LEU A 264
SHEET 4 F 5 ASP A 196 VAL A 200 1 O VAL A 200 N ILE A 176
SHEET 5 F 5 THR A 228 LEU A 230 1 O LEU A 230 N ILE A 199
SHEET 1 G 3 THR A 233 ASP A 240 0
SHEET 2 G 3 VAL A 245 LYS A 251 -1 O THR A 246 N ALA A 239
SHEET 3 G 3 VAL A 254 ALA A 260 -1 O ALA A 260 N VAL A 245
SHEET 1 H 5 ARG A 347 THR A 349 0
SHEET 2 H 5 ASN A 354 GLY A 359 -1 O SER A 357 N ARG A 347
SHEET 3 H 5 GLU A 405 GLY A 413 -1 O LEU A 411 N ALA A 356
SHEET 4 H 5 PHE A 394 ASP A 400 -1 N VAL A 398 O LEU A 407
SHEET 5 H 5 VAL A 372 PRO A 378 -1 N VAL A 373 O ALA A 399
SHEET 1 I 6 THR B 107 ILE B 109 0
SHEET 2 I 6 THR B 29 VAL B 32 1 N ILE B 31 O ILE B 109
SHEET 3 I 6 THR B 2 LEU B 9 1 N VAL B 8 O VAL B 32
SHEET 4 I 6 GLU B 131 ILE B 140 1 O ILE B 139 N LEU B 9
SHEET 5 I 6 THR B 120 LEU B 125 -1 N LEU B 121 O VAL B 133
SHEET 6 I 6 GLY B 111 PHE B 115 -1 N THR B 114 O LEU B 122
SHEET 1 J 5 THR B 107 ILE B 109 0
SHEET 2 J 5 THR B 29 VAL B 32 1 N ILE B 31 O ILE B 109
SHEET 3 J 5 THR B 2 LEU B 9 1 N VAL B 8 O VAL B 32
SHEET 4 J 5 GLU B 131 ILE B 140 1 O ILE B 139 N LEU B 9
SHEET 5 J 5 ILE B 304 ALA B 306 1 O TYR B 305 N ILE B 140
SHEET 1 K 2 SER B 144 THR B 146 0
SHEET 2 K 2 PHE B 269 PRO B 271 -1 O ALA B 270 N SER B 145
SHEET 1 L 5 VAL B 158 VAL B 159 0
SHEET 2 L 5 LYS B 262 GLN B 265 1 O GLN B 265 N VAL B 159
SHEET 3 L 5 SER B 173 ALA B 177 1 N ALA B 177 O LEU B 264
SHEET 4 L 5 ASP B 196 GLU B 201 1 O THR B 198 N ILE B 176
SHEET 5 L 5 THR B 228 THR B 231 1 O THR B 228 N ILE B 199
SHEET 1 M 3 LYS B 234 ASP B 240 0
SHEET 2 M 3 VAL B 245 LYS B 251 -1 O THR B 246 N ALA B 239
SHEET 3 M 3 VAL B 254 ALA B 260 -1 O LEU B 258 N VAL B 247
SHEET 1 N 5 ARG B 347 THR B 349 0
SHEET 2 N 5 ASN B 354 GLY B 359 -1 O VAL B 355 N THR B 349
SHEET 3 N 5 GLU B 405 GLY B 413 -1 O LEU B 411 N ALA B 356
SHEET 4 N 5 PHE B 394 ASP B 400 -1 N VAL B 398 O GLY B 408
SHEET 5 N 5 VAL B 372 PRO B 378 -1 N VAL B 373 O ALA B 399
SSBOND 1 CYS A 41 CYS A 46 1555 1555 2.04
SSBOND 2 CYS B 41 CYS B 46 1555 1555 2.04
CISPEP 1 GLN A 352 PRO A 353 0 0.06
CISPEP 2 HIS A 443 PRO A 444 0 -0.28
CISPEP 3 GLN B 352 PRO B 353 0 0.01
CISPEP 4 HIS B 443 PRO B 444 0 -0.50
SITE 1 AC1 37 LEU A 9 GLY A 10 GLY A 12 PRO A 13
SITE 2 AC1 37 GLY A 14 VAL A 32 GLU A 33 PRO A 34
SITE 3 AC1 37 TYR A 36 GLY A 39 VAL A 40 CYS A 41
SITE 4 AC1 37 CYS A 46 LYS A 50 TYR A 112 GLY A 113
SITE 5 AC1 37 ALA A 141 THR A 142 GLY A 143 TYR A 161
SITE 6 AC1 37 TYR A 276 GLY A 308 ASP A 309 GLN A 315
SITE 7 AC1 37 LEU A 316 ALA A 317 HIS A 318 ALA A 320
SITE 8 AC1 37 3II A 465 HOH A 467 HOH A 468 HOH A 488
SITE 9 AC1 37 HOH A 496 HOH A 563 HOH A 838 HIS B 443
SITE 10 AC1 37 PRO B 444
SITE 1 AC2 20 LYS A 50 ARG A 147 ALA A 181 ILE A 182
SITE 2 AC2 20 GLU A 185 ASN A 209 GLU A 210 PHE A 269
SITE 3 AC2 20 ARG A 288 ALA A 290 GLY A 312 LEU A 313
SITE 4 AC2 20 LEU A 314 GLN A 315 LEU A 316 ARG A 347
SITE 5 AC2 20 ALA A 348 PHE A 350 FAD A 480 HOH A 573
SITE 1 AC3 37 HIS A 443 PRO A 444 LEU B 9 GLY B 10
SITE 2 AC3 37 GLY B 12 PRO B 13 GLY B 14 VAL B 32
SITE 3 AC3 37 GLU B 33 PRO B 34 TYR B 36 GLY B 39
SITE 4 AC3 37 VAL B 40 CYS B 41 CYS B 46 LYS B 50
SITE 5 AC3 37 TYR B 112 GLY B 113 ALA B 141 THR B 142
SITE 6 AC3 37 GLY B 143 TYR B 161 ILE B 182 TYR B 276
SITE 7 AC3 37 GLY B 308 ASP B 309 GLN B 315 LEU B 316
SITE 8 AC3 37 ALA B 317 HIS B 318 3II B 465 HOH B 470
SITE 9 AC3 37 HOH B 480 HOH B 481 HOH B 484 HOH B 575
SITE 10 AC3 37 HOH B 822
SITE 1 AC4 18 LYS B 50 ALA B 181 ILE B 182 GLU B 185
SITE 2 AC4 18 ASN B 209 GLU B 210 PRO B 271 ARG B 288
SITE 3 AC4 18 GLY B 312 LEU B 313 LEU B 314 GLN B 315
SITE 4 AC4 18 LEU B 316 ARG B 347 ALA B 348 PHE B 350
SITE 5 AC4 18 FAD B 580 HOH B 820
CRYST1 83.900 98.400 123.800 90.00 90.00 90.00 P 21 21 21 8
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 0.011919 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010163 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008078 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
