HEADER OXIDOREDUCTASE 20-AUG-07 2R0M
TITLE THE EFFECT OF A GLU370ASP MUTATION IN GLUTARYL-COA
TITLE 2 DEHYDROGENASE ON PROTON TRANSFER TO THE DIENOLATE
TITLE 3 INTERMEDIATE
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;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS GLUTARYL-COA DEHYDROGENASE, FLAVOPROTEIN, ISOMERASE,
KEYWDS 2 ALTERNATIVE SPLICING, DISEASE MUTATION, FAD, MITOCHONDRION,
KEYWDS 3 OXIDOREDUCTASE, POLYMORPHISM, TRANSIT PEPTIDE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.S.RAO,Z.FU,M.ALBRO,B.NARAYANAN,S.BADDAM,H.J.LEE,J.J.KIM,
AUTHOR 2 F.E.FRERMAN
REVDAT 2 24-FEB-09 2R0M 1 VERSN
REVDAT 1 22-APR-08 2R0M 0
JRNL AUTH K.S.RAO,Z.FU,M.ALBRO,B.NARAYANAN,S.BADDAM,H.J.LEE,
JRNL AUTH 2 J.J.KIM,F.E.FRERMAN
JRNL TITL THE EFFECT OF A GLU370ASP MUTATION IN GLUTARYL-COA
JRNL TITL 2 DEHYDROGENASE ON PROTON TRANSFER TO THE DIENOLATE
JRNL TITL 3 INTERMEDIATE.
JRNL REF BIOCHEMISTRY V. 46 14468 2007
JRNL REFN ISSN 0006-2960
JRNL PMID 18020372
JRNL DOI 10.1021/BI7009597
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.70 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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.07
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 251131.020
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 81.4
REMARK 3 NUMBER OF REFLECTIONS : 12000
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) : 0.191
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.300
REMARK 3 FREE R VALUE TEST SET COUNT : 1240
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.80
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 75.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 962
REMARK 3 BIN R VALUE (WORKING SET) : 0.3120
REMARK 3 BIN FREE R VALUE : 0.3450
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 11.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 119
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.032
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3010
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 62
REMARK 3 SOLVENT ATOMS : 48
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.07000
REMARK 3 B22 (A**2) : 3.07000
REMARK 3 B33 (A**2) : -6.14000
REMARK 3 B12 (A**2) : 1.89000
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) : 0.29
REMARK 3 ESD FROM SIGMAA (A) : 0.45
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) : 0.53
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.78
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) : 1.480 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.370 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.250 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.310 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.33
REMARK 3 BSOL : 47.36
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.PAR
REMARK 3 PARAMETER FILE 5 : 4NB.PAR
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 : 4NB.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2R0M COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-SEP-07.
REMARK 100 THE RCSB ID CODE IS RCSB044277.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-03
REMARK 200 TEMPERATURE (KELVIN) : 277
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 3
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 : GRAPHITE
REMARK 200 OPTICS : MIRRORS
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 : 12017
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 28.070
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 81.4
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.15300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 75.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.33700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MERLOT
REMARK 200 STARTING MODEL: PDB ENTRY 1SIQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES BUFFER PH 6.5, 30%
REMARK 280 PEGMME5000, 200 MM AMMONIUM SULFATE, VAPOR DIFFUSION, HANGING
REMARK 280 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 42.70333
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 85.40667
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 42.70333
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 85.40667
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 42.70333
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 85.40667
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 42.70333
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 85.40667
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
REMARK 350 TOTAL BURIED SURFACE AREA: 25030 ANGSTROM**2
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 116.88000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 128.11000
REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 116.88000
REMARK 350 BIOMT2 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 128.11000
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 GLU A 14 23.41 -75.17
REMARK 500 TYR A 69 19.94 55.75
REMARK 500 VAL A 89 -64.48 -94.55
REMARK 500 LEU A 135 -53.87 -120.65
REMARK 500 SER A 145 16.63 -69.10
REMARK 500 ASN A 171 -24.73 74.67
REMARK 500 SER A 211 134.73 -172.74
REMARK 500 ASP A 223 73.48 -102.08
REMARK 500 LEU A 239 -14.86 -41.72
REMARK 500 ALA A 283 -7.28 -56.77
REMARK 500 HIS A 355 -35.19 56.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 525 DISTANCE = 6.35 ANGSTROMS
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 401
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4NI A 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2R0N RELATED DB: PDB
DBREF 2R0M A 1 394 UNP Q92947 GCDH_HUMAN 45 438
SEQADV 2R0M ASP A 370 UNP Q92947 GLU 414 ENGINEERED
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 ASP 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 401 53
HET 4NI A 402 9
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM 4NI 4-NITROBUTANOIC ACID
FORMUL 2 FAD C27 H33 N9 O15 P2
FORMUL 3 4NI C4 H7 N O4
FORMUL 4 HOH *48(H2 O)
HELIX 1 1 LEU A 12 LEU A 16 5 5
HELIX 2 2 THR A 17 LEU A 35 1 19
HELIX 3 3 ARG A 38 ASN A 45 1 8
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 GLU A 230 VAL A 232 5 3
HELIX 12 12 LEU A 239 ARG A 275 1 37
HELIX 13 13 ASN A 285 GLN A 315 1 31
HELIX 14 14 ALA A 319 LEU A 345 1 27
HELIX 15 15 GLY A 346 TYR A 354 5 9
HELIX 16 16 HIS A 355 ASN A 367 1 13
HELIX 17 17 THR A 372 GLY A 386 1 15
SHEET 1 A 3 GLY A 131 GLY A 134 0
SHEET 2 A 3 LEU A 177 CYS A 184 1 O VAL A 179 N CYS A 132
SHEET 3 A 3 ILE A 189 GLU A 195 -1 O PHE A 192 N VAL A 180
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 CYS A 132
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 VAL A 227 N TYR A 160
SHEET 6 B 6 LEU A 201 SER A 202 -1 N SER A 202 O ILE A 221
SHEET 1 C 2 MET A 276 GLN A 277 0
SHEET 2 C 2 VAL A 280 PRO A 281 -1 O VAL A 280 N GLN A 277
SITE 1 AC1 23 PHE A 133 LEU A 135 THR A 136 GLY A 141
SITE 2 AC1 23 SER A 142 TRP A 168 ILE A 169 THR A 170
SITE 3 AC1 23 LEU A 212 ARG A 275 PHE A 278 LEU A 282
SITE 4 AC1 23 ASN A 285 GLN A 286 ASP A 343 MET A 344
SITE 5 AC1 23 GLY A 347 ILE A 350 THR A 372 PHE A 390
SITE 6 AC1 23 HOH A 500 HOH A 516 HOH A 534
SITE 1 AC2 7 ARG A 94 SER A 98 LEU A 103 PHE A 133
SITE 2 AC2 7 LEU A 246 TYR A 369 ASP A 370
CRYST1 116.880 116.880 128.110 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 0.008556 0.004940 0.000000 0.00000
SCALE2 0.000000 0.009879 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007806 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
