HEADER OXIDOREDUCTASE 10-AUG-11 3TD7
TITLE CRYSAL STRUCTURE OF THE MIMIVIRUS SULFHYDRYL OXIDASE R596
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FAD-LINKED SULFHYDRYL OXIDASE R596;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.8.3.2;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ACANTHAMOEBA POLYPHAGA MIMIVIRUS;
SOURCE 3 ORGANISM_COMMON: APMV;
SOURCE 4 ORGANISM_TAXID: 212035;
SOURCE 5 GENE: MIMI_R596, R596;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS FOUR HELIX-BUNDLE, ORFAN DOMAIN, OXIDASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.HAKIM,D.FASS
REVDAT 3 23-AUG-17 3TD7 1 REMARK
REVDAT 2 14-DEC-16 3TD7 1 JRNL
REVDAT 1 05-SEP-12 3TD7 0
JRNL AUTH M.HAKIM,D.EZERINA,A.ALON,O.VONSHAK,D.FASS
JRNL TITL EXPLORING ORFAN DOMAINS IN GIANT VIRUSES: STRUCTURE OF
JRNL TITL 2 MIMIVIRUS SULFHYDRYL OXIDASE R596.
JRNL REF PLOS ONE V. 7 50649 2012
JRNL REFN ESSN 1932-6203
JRNL PMID 23209798
JRNL DOI 10.1371/JOURNAL.PONE.0050649
REMARK 2
REMARK 2 RESOLUTION. 2.21 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) : 2.21
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 23329
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) : 0.227
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1718
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 2085
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 53
REMARK 3 SOLVENT ATOMS : 122
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.079
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
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 3TD7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-AUG-11.
REMARK 100 THE DEPOSITION ID IS D_1000067337.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-MAY-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9766
REMARK 200 MONOCHROMATOR : SI(311)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25063
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.210
REMARK 200 RESOLUTION RANGE LOW (A) : 45.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 19.30
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.21
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.6
REMARK 200 DATA REDUNDANCY IN SHELL : 19.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.74300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, 200 MM MAGNESIUM
REMARK 280 CHLORIDE, 200 MM LITHIUM SULFATE, 5% (V/V) 2-METHYL-2,4-
REMARK 280 PENTANEDIOL (MPD), AND 15-20% (W/V) PEG 1500, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K, PH 7.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 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+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 66.93000
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 133.86000
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 100.39500
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 167.32500
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 33.46500
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 66.93000
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 133.86000
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 167.32500
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 100.39500
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 33.46500
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: 7730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 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 0.500000 0.866025 0.000000 45.65300
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 -79.07332
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 33.46500
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 -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 LEU A 3
REMARK 465 SER A 4
REMARK 465 LYS A 5
REMARK 465 GLN A 6
REMARK 465 VAL A 7
REMARK 465 VAL A 8
REMARK 465 PRO A 9
REMARK 465 THR A 10
REMARK 465 HIS A 11
REMARK 465 ARG A 12
REMARK 465 VAL A 13
REMARK 465 GLU A 14
REMARK 465 ILE A 15
REMARK 465 ALA A 16
REMARK 465 PRO A 17
REMARK 465 ASN A 18
REMARK 465 SER A 19
REMARK 465 GLU A 20
REMARK 465 SER A 21
REMARK 465 THR A 22
REMARK 465 ALA A 23
REMARK 465 LYS A 24
REMARK 465 MET A 25
REMARK 465 ASP A 26
REMARK 465 HIS A 27
REMARK 465 SER A 28
REMARK 465 ASN A 29
REMARK 465 TYR A 30
REMARK 465 GLN A 31
REMARK 465 PRO A 149
REMARK 465 VAL A 150
REMARK 465 PRO A 151
REMARK 465 THR A 152
REMARK 465 VAL A 153
REMARK 465 LYS A 154
REMARK 465 GLY A 155
REMARK 465 CYS A 156
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 HIS A 32 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 148 CG CD CE NZ
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 CYS A 80 114.84 -170.92
REMARK 500 CYS A 146 58.98 -66.52
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 334
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3GWN RELATED DB: PDB
REMARK 900 TRUNCATED VERSION OF THIS PROTEIN, INCLUDES ONLY THE ERV SULFHYDRYL
REMARK 900 OXIDASE DOMAIN
REMARK 900 RELATED ID: 3P0K RELATED DB: PDB
REMARK 900 HOMOLOG FROM BACULOVIRUS
REMARK 900 RELATED ID: 3GWL RELATED DB: PDB
REMARK 900 HOMOLOG FROM AFRICAN SWINE FEVER VIRUS
DBREF 3TD7 A 1 292 UNP Q5UP54 YR596_MIMIV 1 292
SEQADV 3TD7 GLY A -2 UNP Q5UP54 EXPRESSION TAG
SEQADV 3TD7 SER A -1 UNP Q5UP54 EXPRESSION TAG
SEQADV 3TD7 HIS A 0 UNP Q5UP54 EXPRESSION TAG
SEQADV 3TD7 ALA A 23 UNP Q5UP54 CYS 23 ENGINEERED MUTATION
SEQADV 3TD7 ALA A 201 UNP Q5UP54 CYS 201 ENGINEERED MUTATION
SEQADV 3TD7 ALA A 229 UNP Q5UP54 CYS 229 ENGINEERED MUTATION
SEQADV 3TD7 ALA A 266 UNP Q5UP54 CYS 266 ENGINEERED MUTATION
SEQRES 1 A 295 GLY SER HIS MET SER LEU SER LYS GLN VAL VAL PRO THR
SEQRES 2 A 295 HIS ARG VAL GLU ILE ALA PRO ASN SER GLU SER THR ALA
SEQRES 3 A 295 LYS MET ASP HIS SER ASN TYR GLN HIS ASN GLY LEU ILE
SEQRES 4 A 295 THR LYS ILE TRP GLY THR ALA GLY TRP THR PHE ASN HIS
SEQRES 5 A 295 ALA VAL THR PHE GLY TYR PRO LEU ASN PRO THR SER ASP
SEQRES 6 A 295 ASP LYS ARG ARG TYR LYS ASN TYR PHE ILE SER LEU GLY
SEQRES 7 A 295 ASP VAL LEU PRO CYS ARG LEU CYS ARG GLU SER TYR LYS
SEQRES 8 A 295 LYS PHE ILE THR THR GLY LYS THR ALA LEU THR ASN GLU
SEQRES 9 A 295 VAL LEU ARG ASN ARG HIS THR LEU THR LYS TRP PHE TYR
SEQRES 10 A 295 ASP VAL HIS ASN ALA VAL ASN ASN LYS LEU GLU VAL ASP
SEQRES 11 A 295 TYR GLY LEU SER TYR GLU ASP VAL VAL ASN LYS TYR GLU
SEQRES 12 A 295 SER PHE ARG ALA LYS CYS GLY LYS PRO VAL PRO THR VAL
SEQRES 13 A 295 LYS GLY CYS VAL THR PRO LEU ASP HIS LYS ALA PHE SER
SEQRES 14 A 295 PHE LYS LYS LEU TYR TYR MET ASP ALA PRO ILE VAL SER
SEQRES 15 A 295 LEU ASP LYS VAL GLU ASN PHE VAL ARG ILE ALA ARG MET
SEQRES 16 A 295 ARG GLY ILE SER ASP LYS TYR PHE ALA PHE LEU GLU LEU
SEQRES 17 A 295 ALA THR VAL LEU ASN GLY ASP PHE ASN GLU LEU LYS LYS
SEQRES 18 A 295 GLN SER SER TRP GLU TYR ARG ASN LYS TYR ALA GLN LYS
SEQRES 19 A 295 LYS ILE ARG HIS MET ARG GLU ASN ALA ILE PRO SER ILE
SEQRES 20 A 295 GLU GLU GLN GLY TYR TRP LYS GLY THR PRO THR ILE ASP
SEQRES 21 A 295 GLU LEU LYS LEU LEU LEU PHE LEU ALA SER ASN LEU ASN
SEQRES 22 A 295 ARG THR GLU VAL ASN ASP ALA ILE ASN ASN VAL GLU ARG
SEQRES 23 A 295 LEU GLU SER THR HIS TYR ILE GLU ASN
HET FAD A 334 53
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
FORMUL 2 FAD C27 H33 N9 O15 P2
FORMUL 3 HOH *122(H2 O)
HELIX 1 1 ILE A 36 GLY A 54 1 19
HELIX 2 2 THR A 60 LEU A 78 1 19
HELIX 3 3 CYS A 80 ILE A 91 1 12
HELIX 4 4 THR A 92 ALA A 97 5 6
HELIX 5 5 GLU A 101 ARG A 104 5 4
HELIX 6 6 ASN A 105 GLU A 125 1 21
HELIX 7 7 SER A 131 SER A 141 1 11
HELIX 8 8 PRO A 159 TYR A 172 1 14
HELIX 9 9 SER A 179 GLU A 184 1 6
HELIX 10 10 PHE A 186 ARG A 193 1 8
HELIX 11 11 SER A 196 TYR A 199 5 4
HELIX 12 12 PHE A 200 LEU A 209 1 10
HELIX 13 13 ASP A 212 LYS A 217 1 6
HELIX 14 14 SER A 220 ASN A 239 1 20
HELIX 15 15 THR A 255 LEU A 263 1 9
HELIX 16 16 ASN A 270 GLU A 291 1 22
SSBOND 1 CYS A 80 CYS A 83 1555 1555 2.36
SITE 1 AC1 29 THR A 37 TRP A 40 GLY A 41 THR A 42
SITE 2 AC1 29 GLY A 44 TRP A 45 HIS A 49 CYS A 83
SITE 3 AC1 29 TYR A 114 HIS A 117 ASN A 118 VAL A 120
SITE 4 AC1 29 ASN A 121 LYS A 123 LEU A 124 TYR A 128
SITE 5 AC1 29 LEU A 130 VAL A 135 LYS A 138 ASP A 174
SITE 6 AC1 29 ARG A 237 HOH A 296 HOH A 299 HOH A 300
SITE 7 AC1 29 HOH A 332 HOH A 336 HOH A 337 HOH A 344
SITE 8 AC1 29 HOH A 369
CRYST1 91.306 91.306 200.790 90.00 90.00 120.00 P 61 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 0.010952 0.006323 0.000000 0.00000
SCALE2 0.000000 0.012646 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004980 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
