HEADER OXIDOREDUCTASE 01-MAR-04 1SIR
TITLE THE CRYSTAL STRUCTURE AND MECHANISM OF HUMAN GLUTARYL-COA
TITLE 2 DEHYDROGENASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTARYL-COA DEHYDROGENASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GCD;
COMPND 5 EC: 1.3.99.7
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 STRAIN: BACTERIAL:BL21
KEYWDS ACYL-COA DEHYDROGENASE, DECOBOXYLATION FLAVIN PROTEIN, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.WANG,Z.FU,R.PASCHKE,S.L.GOODMAN,F.E.FRERMAN,J.J.KIM
REVDAT 3 13-JUL-11 1SIR 1 VERSN
REVDAT 2 24-FEB-09 1SIR 1 VERSN
REVDAT 1 07-SEP-04 1SIR 0
JRNL AUTH Z.FU,M.WANG,R.PASCHKE,K.S.RAO,F.E.FRERMAN,J.J.KIM
JRNL TITL CRYSTAL STRUCTURES OF HUMAN GLUTARYL-COA DEHYDROGENASE WITH
JRNL TITL 2 AND WITHOUT AN ALTERNATE SUBSTRATE: STRUCTURAL BASES OF
JRNL TITL 3 DEHYDROGENATION AND DECARBOXYLATION REACTIONS
JRNL REF BIOCHEMISTRY V. 43 9674 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15274622
JRNL DOI 10.1021/BI049290C
REMARK 2
REMARK 2 RESOLUTION. 2.60 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.82
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 300083.740
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 83.8
REMARK 3 NUMBER OF REFLECTIONS : 13764
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) : 0.187
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1105
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.69
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 62.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 918
REMARK 3 BIN R VALUE (WORKING SET) : 0.3240
REMARK 3 BIN FREE R VALUE : 0.3680
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 7.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 79
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.041
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3011
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 109
REMARK 3 SOLVENT ATOMS : 77
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.55000
REMARK 3 B22 (A**2) : 0.55000
REMARK 3 B33 (A**2) : -1.10000
REMARK 3 B12 (A**2) : 16.78000
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) : 0.28
REMARK 3 ESD FROM SIGMAA (A) : 0.47
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) : 0.36
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.47
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.79
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) : 2.380 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.660 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 4.020 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 6.030 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.31
REMARK 3 BSOL : 40.22
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.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : FAD.PARAM
REMARK 3 PARAMETER FILE 5 : NBC.PARAM
REMARK 3 PARAMETER FILE 6 : 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 : FAD.TOP
REMARK 3 TOPOLOGY FILE 5 : NBC.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 1SIR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAR-04.
REMARK 100 THE RCSB ID CODE IS RCSB021739.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-JUL-00
REMARK 200 TEMPERATURE (KELVIN) : 277
REMARK 200 PH : 6.5
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 : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13764
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 29.820
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 83.9
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 61.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.32000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS 1.1
REMARK 200 STARTING MODEL: PDB ENTRY 1SIQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MES BUFFER, PEG5KMME, AMMONIUM
REMARK 280 SULFATE, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+1/3
REMARK 290 6555 X-Y,X,Z+2/3
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+1/3
REMARK 290 11555 -X+Y,Y,-Z
REMARK 290 12555 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 42.67800
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 85.35600
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 42.67800
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 85.35600
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 42.67800
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 85.35600
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 42.67800
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 85.35600
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 30650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44950 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -146.0 KCAL/MOL
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 -58.36100
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 101.08422
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 -42.67800
REMARK 350 BIOMT1 4 0.500000 0.866025 0.000000 -58.36100
REMARK 350 BIOMT2 4 0.866025 -0.500000 0.000000 101.08422
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 -42.67800
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 ARG A 1
REMARK 465 PRO A 2
REMARK 465 SER A 393
REMARK 465 LYS A 394
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 8 66.36 -161.41
REMARK 500 GLU A 14 13.59 -66.76
REMARK 500 ASN A 171 -11.97 77.31
REMARK 500 HIS A 355 -37.26 63.30
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 399
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NBC A 400
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1SIQ RELATED DB: PDB
REMARK 900 NATIVE CRYSTAL
DBREF 1SIR A 1 394 UNP Q92947 GCDH_HUMAN 45 440
SEQRES 1 A 394 ARG PRO GLU PHE ASP TRP GLN ASP PRO LEU VAL LEU GLU
SEQRES 2 A 394 GLU GLN LEU THR THR ASP GLU ILE LEU ILE ARG ASP THR
SEQRES 3 A 394 PHE ARG THR TYR CYS GLN GLU ARG LEU MET PRO ARG ILE
SEQRES 4 A 394 LEU LEU ALA ASN ARG ASN GLU VAL PHE HIS ARG GLU ILE
SEQRES 5 A 394 ILE SER GLU MET GLY GLU LEU GLY VAL LEU GLY PRO THR
SEQRES 6 A 394 ILE LYS GLY TYR GLY CYS ALA GLY VAL SER SER VAL ALA
SEQRES 7 A 394 TYR GLY LEU LEU ALA ARG GLU LEU GLU ARG VAL ASP SER
SEQRES 8 A 394 GLY TYR ARG SER ALA MET SER VAL GLN SER SER LEU VAL
SEQRES 9 A 394 MET HIS PRO ILE TYR ALA TYR GLY SER GLU GLU GLN ARG
SEQRES 10 A 394 GLN LYS TYR LEU PRO GLN LEU ALA LYS GLY GLU LEU LEU
SEQRES 11 A 394 GLY CYS PHE GLY LEU THR GLU PRO ASN SER GLY SER ASP
SEQRES 12 A 394 PRO SER SER MET GLU THR ARG ALA HIS TYR ASN SER SER
SEQRES 13 A 394 ASN LYS SER TYR THR LEU ASN GLY THR LYS THR TRP ILE
SEQRES 14 A 394 THR ASN SER PRO MET ALA ASP LEU PHE VAL VAL TRP ALA
SEQRES 15 A 394 ARG CYS GLU ASP GLY CYS ILE ARG GLY PHE LEU LEU GLU
SEQRES 16 A 394 LYS GLY MET ARG GLY LEU SER ALA PRO ARG ILE GLN GLY
SEQRES 17 A 394 LYS PHE SER LEU ARG ALA SER ALA THR GLY MET ILE ILE
SEQRES 18 A 394 MET ASP GLY VAL GLU VAL PRO GLU GLU ASN VAL LEU PRO
SEQRES 19 A 394 GLY ALA SER SER LEU GLY GLY PRO PHE GLY CYS LEU ASN
SEQRES 20 A 394 ASN ALA ARG TYR GLY ILE ALA TRP GLY VAL LEU GLY ALA
SEQRES 21 A 394 SER GLU PHE CYS LEU HIS THR ALA ARG GLN TYR ALA LEU
SEQRES 22 A 394 ASP ARG MET GLN PHE GLY VAL PRO LEU ALA ARG ASN GLN
SEQRES 23 A 394 LEU ILE GLN LYS LYS LEU ALA ASP MET LEU THR GLU ILE
SEQRES 24 A 394 THR LEU GLY LEU HIS ALA CYS LEU GLN LEU GLY ARG LEU
SEQRES 25 A 394 LYS ASP GLN ASP LYS ALA ALA PRO GLU MET VAL SER LEU
SEQRES 26 A 394 LEU LYS ARG ASN ASN CYS GLY LYS ALA LEU ASP ILE ALA
SEQRES 27 A 394 ARG GLN ALA ARG ASP MET LEU GLY GLY ASN GLY ILE SER
SEQRES 28 A 394 ASP GLU TYR HIS VAL ILE ARG HIS ALA MET ASN LEU GLU
SEQRES 29 A 394 ALA VAL ASN THR TYR GLU GLY THR HIS ASP ILE HIS ALA
SEQRES 30 A 394 LEU ILE LEU GLY ARG ALA ILE THR GLY ILE GLN ALA PHE
SEQRES 31 A 394 THR ALA SER LYS
HET FAD A 399 53
HET NBC A 400 56
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM NBC S-4-NITROBUTYRYL-COA
FORMUL 2 FAD C27 H33 N9 O15 P2
FORMUL 3 NBC C25 H41 N8 O19 P3 S
FORMUL 4 HOH *77(H2 O)
HELIX 1 1 LEU A 12 LEU A 16 5 5
HELIX 2 2 THR A 17 ARG A 34 1 18
HELIX 3 3 LEU A 35 ASN A 45 1 11
HELIX 4 4 ARG A 50 GLY A 60 1 11
HELIX 5 5 SER A 75 ARG A 88 1 14
HELIX 6 6 ASP A 90 LEU A 103 1 14
HELIX 7 7 VAL A 104 GLY A 112 1 9
HELIX 8 8 SER A 113 LYS A 126 1 14
HELIX 9 9 ASP A 143 MET A 147 5 5
HELIX 10 10 SER A 172 ALA A 175 5 4
HELIX 11 11 LEU A 239 ARG A 275 1 37
HELIX 12 12 ASN A 285 GLN A 315 1 31
HELIX 13 13 ALA A 319 LEU A 345 1 27
HELIX 14 14 GLY A 346 TYR A 354 5 9
HELIX 15 15 HIS A 355 ASN A 367 1 13
HELIX 16 16 ASP A 374 GLY A 386 1 13
SHEET 1 A 2 LYS A 67 GLY A 68 0
SHEET 2 A 2 CYS A 71 ALA A 72 -1 O CYS A 71 N GLY A 68
SHEET 1 B 6 GLY A 131 GLY A 134 0
SHEET 2 B 6 LEU A 177 CYS A 184 1 O VAL A 179 N GLY A 134
SHEET 3 B 6 ARG A 150 ASN A 154 1 N ALA A 151 O ARG A 183
SHEET 4 B 6 SER A 159 THR A 170 -1 O SER A 159 N ASN A 154
SHEET 5 B 6 THR A 217 PRO A 228 -1 O GLY A 218 N ILE A 169
SHEET 6 B 6 LEU A 201 SER A 202 -1 N SER A 202 O ILE A 221
SHEET 1 C 4 GLY A 131 GLY A 134 0
SHEET 2 C 4 LEU A 177 CYS A 184 1 O VAL A 179 N GLY A 134
SHEET 3 C 4 ILE A 189 GLU A 195 -1 O PHE A 192 N VAL A 180
SHEET 4 C 4 VAL A 232 LEU A 233 -1 O LEU A 233 N GLY A 191
SHEET 1 D 2 MET A 276 GLN A 277 0
SHEET 2 D 2 VAL A 280 PRO A 281 -1 O VAL A 280 N GLN A 277
SITE 1 AC1 24 PHE A 133 LEU A 135 THR A 136 GLY A 141
SITE 2 AC1 24 SER A 142 TRP A 168 ILE A 169 THR A 170
SITE 3 AC1 24 LEU A 212 ARG A 275 PHE A 278 LEU A 282
SITE 4 AC1 24 ASN A 285 GLN A 286 ASP A 343 MET A 344
SITE 5 AC1 24 GLY A 347 ILE A 350 THR A 372 PHE A 390
SITE 6 AC1 24 NBC A 400 HOH A 501 HOH A 502 HOH A 506
SITE 1 AC2 16 ARG A 94 SER A 95 LEU A 103 SER A 142
SITE 2 AC2 16 PRO A 144 THR A 170 PHE A 243 GLY A 244
SITE 3 AC2 16 LEU A 246 ASN A 247 ARG A 250 PRO A 320
SITE 4 AC2 16 TYR A 369 GLU A 370 ARG A 382 FAD A 399
CRYST1 116.722 116.722 128.034 90.00 90.00 120.00 P 64 2 2 12
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 0.008567 0.004946 0.000000 0.00000
SCALE2 0.000000 0.009893 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007810 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
