HEADER OXIDOREDUCTASE 17-JUN-00 1F5V
TITLE STRUCTURE AND SITE-DIRECTED MUTAGENESIS OF A FLAVOPROTEIN
TITLE 2 FROM ESCHERICHIA COLI THAT REDUCES NITROCOMPOUNDS.
TITLE 3 ALTERATION OF PYRIDINE NUCLEOTIDE BINDING BY A SINGLE
TITLE 4 AMINO ACID SUBSTITUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OXYGEN-INSENSITIVE NADPH NITROREDUCTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.6.99.6;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PAJ102
KEYWDS NITROREDUCTASE, FLAVOPROTEIN, ESCHERICHIA COLI,
KEYWDS 2 OXIDOREDUCTION, NITROCOMPOUND, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.KOBORI,H.SASAKI,W.C.LEE,S.ZENNO,K.SAIGO,M.E.P.MURPHY,
AUTHOR 2 M.TANOKURA
REVDAT 3 24-FEB-09 1F5V 1 VERSN
REVDAT 2 01-APR-03 1F5V 1 JRNL
REVDAT 1 14-FEB-01 1F5V 0
JRNL AUTH T.KOBORI,H.SASAKI,W.C.LEE,S.ZENNO,K.SAIGO,
JRNL AUTH 2 M.E.MURPHY,M.TANOKURA
JRNL TITL STRUCTURE AND SITE-DIRECTED MUTAGENESIS OF A
JRNL TITL 2 FLAVOPROTEIN FROM ESCHERICHIA COLI THAT REDUCES
JRNL TITL 3 NITROCOMPOUNDS: ALTERATION OF PYRIDINE NUCLEOTIDE
JRNL TITL 4 BINDING BY A SINGLE AMINO ACID SUBSTITUTION.
JRNL REF J.BIOL.CHEM. V. 276 2816 2001
JRNL REFN ISSN 0021-9258
JRNL PMID 11034992
JRNL DOI 10.1074/JBC.M002617200
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1, 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 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
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 : 42534
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) : 0.189
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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 : 3774
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 62
REMARK 3 SOLVENT ATOMS : 349
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) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.69
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 1F5V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUN-00.
REMARK 100 THE RCSB ID CODE IS RCSB011280.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL; 20-NOV-98
REMARK 200 TEMPERATURE (KELVIN) : 100.0; 100.0
REMARK 200 PH : 6.5; 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N; Y
REMARK 200 RADIATION SOURCE : ROTATING ANODE; PHOTON FACTORY
REMARK 200 BEAMLINE : NULL; BL-6A
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418; 1.00
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE; IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC; FUJI
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, MES, SODIUM HYDROXIDE,
REMARK 280 PEG 400, DIOXANE, PH 6.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 281.0K. PEG 6000, MES, SODIUM HYDROXIDE, PEG 400,
REMARK 280 DIOXANE, PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 281.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER CONSTRUCTED FROM
REMARK 300 CHAIN A A SYMMETRY PARTNER GENERATED BY THE TWO-FOLD.
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: 11560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -84.0 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 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 GLN A 44 67.31 38.49
REMARK 500 CYS A 45 45.34 -105.11
REMARK 500 ASN A 179 -41.11 65.24
REMARK 500 ASN A 207 97.83 -47.98
REMARK 500 GLU A 223 64.71 -114.79
REMARK 500 GLN B 44 65.77 39.28
REMARK 500 CYS B 45 44.71 -104.38
REMARK 500 ASN B 179 -40.16 66.73
REMARK 500 SER B 205 -64.63 -108.29
REMARK 500 GLU B 223 68.64 -112.64
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 B 380 DISTANCE = 6.60 ANGSTROMS
REMARK 525 HOH A 393 DISTANCE = 7.97 ANGSTROMS
REMARK 525 HOH B 459 DISTANCE = 5.55 ANGSTROMS
REMARK 525 HOH A 463 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH A 464 DISTANCE = 8.85 ANGSTROMS
REMARK 525 HOH A 499 DISTANCE = 5.77 ANGSTROMS
REMARK 525 HOH B 520 DISTANCE = 5.79 ANGSTROMS
REMARK 525 HOH B 521 DISTANCE = 5.71 ANGSTROMS
REMARK 525 HOH B 527 DISTANCE = 5.32 ANGSTROMS
REMARK 525 HOH A 528 DISTANCE = 8.80 ANGSTROMS
REMARK 525 HOH A 529 DISTANCE = 10.40 ANGSTROMS
REMARK 525 HOH B 530 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH A 530 DISTANCE = 12.16 ANGSTROMS
REMARK 525 HOH A 531 DISTANCE = 6.23 ANGSTROMS
REMARK 525 HOH B 532 DISTANCE = 8.84 ANGSTROMS
REMARK 525 HOH A 532 DISTANCE = 8.28 ANGSTROMS
REMARK 525 HOH B 533 DISTANCE = 12.02 ANGSTROMS
REMARK 525 HOH A 533 DISTANCE = 11.24 ANGSTROMS
REMARK 525 HOH B 534 DISTANCE = 9.64 ANGSTROMS
REMARK 525 HOH A 534 DISTANCE = 17.85 ANGSTROMS
REMARK 525 HOH B 535 DISTANCE = 9.78 ANGSTROMS
REMARK 525 HOH A 535 DISTANCE = 16.24 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN A 360
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN B 361
DBREF 1F5V A 1 240 UNP P17117 NFSA_ECOLI 1 240
DBREF 1F5V B 1 240 UNP P17117 NFSA_ECOLI 1 240
SEQRES 1 A 240 MET THR PRO THR ILE GLU LEU ILE CYS GLY HIS ARG SER
SEQRES 2 A 240 ILE ARG HIS PHE THR ASP GLU PRO ILE SER GLU ALA GLN
SEQRES 3 A 240 ARG GLU ALA ILE ILE ASN SER ALA ARG ALA THR SER SER
SEQRES 4 A 240 SER SER PHE LEU GLN CYS SER SER ILE ILE ARG ILE THR
SEQRES 5 A 240 ASP LYS ALA LEU ARG GLU GLU LEU VAL THR LEU THR GLY
SEQRES 6 A 240 GLY GLN LYS HIS VAL ALA GLN ALA ALA GLU PHE TRP VAL
SEQRES 7 A 240 PHE CYS ALA ASP PHE ASN ARG HIS LEU GLN ILE CYS PRO
SEQRES 8 A 240 ASP ALA GLN LEU GLY LEU ALA GLU GLN LEU LEU LEU GLY
SEQRES 9 A 240 VAL VAL ASP THR ALA MET MET ALA GLN ASN ALA LEU ILE
SEQRES 10 A 240 ALA ALA GLU SER LEU GLY LEU GLY GLY VAL TYR ILE GLY
SEQRES 11 A 240 GLY LEU ARG ASN ASN ILE GLU ALA VAL THR LYS LEU LEU
SEQRES 12 A 240 LYS LEU PRO GLN HIS VAL LEU PRO LEU PHE GLY LEU CYS
SEQRES 13 A 240 LEU GLY TRP PRO ALA ASP ASN PRO ASP LEU LYS PRO ARG
SEQRES 14 A 240 LEU PRO ALA SER ILE LEU VAL HIS GLU ASN SER TYR GLN
SEQRES 15 A 240 PRO LEU ASP LYS GLY ALA LEU ALA GLN TYR ASP GLU GLN
SEQRES 16 A 240 LEU ALA GLU TYR TYR LEU THR ARG GLY SER ASN ASN ARG
SEQRES 17 A 240 ARG ASP THR TRP SER ASP HIS ILE ARG ARG THR ILE ILE
SEQRES 18 A 240 LYS GLU SER ARG PRO PHE ILE LEU ASP TYR LEU HIS LYS
SEQRES 19 A 240 GLN GLY TRP ALA THR ARG
SEQRES 1 B 240 MET THR PRO THR ILE GLU LEU ILE CYS GLY HIS ARG SER
SEQRES 2 B 240 ILE ARG HIS PHE THR ASP GLU PRO ILE SER GLU ALA GLN
SEQRES 3 B 240 ARG GLU ALA ILE ILE ASN SER ALA ARG ALA THR SER SER
SEQRES 4 B 240 SER SER PHE LEU GLN CYS SER SER ILE ILE ARG ILE THR
SEQRES 5 B 240 ASP LYS ALA LEU ARG GLU GLU LEU VAL THR LEU THR GLY
SEQRES 6 B 240 GLY GLN LYS HIS VAL ALA GLN ALA ALA GLU PHE TRP VAL
SEQRES 7 B 240 PHE CYS ALA ASP PHE ASN ARG HIS LEU GLN ILE CYS PRO
SEQRES 8 B 240 ASP ALA GLN LEU GLY LEU ALA GLU GLN LEU LEU LEU GLY
SEQRES 9 B 240 VAL VAL ASP THR ALA MET MET ALA GLN ASN ALA LEU ILE
SEQRES 10 B 240 ALA ALA GLU SER LEU GLY LEU GLY GLY VAL TYR ILE GLY
SEQRES 11 B 240 GLY LEU ARG ASN ASN ILE GLU ALA VAL THR LYS LEU LEU
SEQRES 12 B 240 LYS LEU PRO GLN HIS VAL LEU PRO LEU PHE GLY LEU CYS
SEQRES 13 B 240 LEU GLY TRP PRO ALA ASP ASN PRO ASP LEU LYS PRO ARG
SEQRES 14 B 240 LEU PRO ALA SER ILE LEU VAL HIS GLU ASN SER TYR GLN
SEQRES 15 B 240 PRO LEU ASP LYS GLY ALA LEU ALA GLN TYR ASP GLU GLN
SEQRES 16 B 240 LEU ALA GLU TYR TYR LEU THR ARG GLY SER ASN ASN ARG
SEQRES 17 B 240 ARG ASP THR TRP SER ASP HIS ILE ARG ARG THR ILE ILE
SEQRES 18 B 240 LYS GLU SER ARG PRO PHE ILE LEU ASP TYR LEU HIS LYS
SEQRES 19 B 240 GLN GLY TRP ALA THR ARG
HET FMN A 360 31
HET FMN B 361 31
HETNAM FMN FLAVIN MONONUCLEOTIDE
HETSYN FMN RIBOFLAVIN MONOPHOSPHATE
FORMUL 3 FMN 2(C17 H21 N4 O9 P)
FORMUL 5 HOH *349(H2 O)
HELIX 1 1 THR A 2 GLY A 10 1 9
HELIX 2 2 SER A 23 ALA A 36 1 14
HELIX 3 3 SER A 39 LEU A 43 5 5
HELIX 4 4 ASP A 53 THR A 64 1 12
HELIX 5 5 LYS A 68 ALA A 73 1 6
HELIX 6 6 PHE A 83 CYS A 90 1 8
HELIX 7 7 LEU A 97 LEU A 122 1 26
HELIX 8 8 GLY A 130 ASN A 134 5 5
HELIX 9 9 ASN A 135 LEU A 143 1 9
HELIX 10 10 PRO A 171 LEU A 175 1 5
HELIX 11 11 ASP A 185 THR A 202 1 18
HELIX 12 12 THR A 211 ILE A 221 1 11
HELIX 13 13 PHE A 227 GLN A 235 1 9
HELIX 14 14 THR B 2 GLY B 10 1 9
HELIX 15 15 SER B 23 ALA B 36 1 14
HELIX 16 16 SER B 39 LEU B 43 5 5
HELIX 17 17 ASP B 53 THR B 64 1 12
HELIX 18 18 LYS B 68 ALA B 73 1 6
HELIX 19 19 PHE B 83 CYS B 90 1 8
HELIX 20 20 LEU B 97 LEU B 122 1 26
HELIX 21 21 GLY B 130 ASN B 134 5 5
HELIX 22 22 ASN B 135 LEU B 143 1 9
HELIX 23 23 PRO B 171 LEU B 175 1 5
HELIX 24 24 ASP B 185 THR B 202 1 18
HELIX 25 25 THR B 211 ILE B 221 1 11
HELIX 26 26 PHE B 227 GLN B 235 1 9
SHEET 1 A 5 GLY A 125 ILE A 129 0
SHEET 2 A 5 VAL A 149 GLY A 158 -1 O GLY A 154 N ILE A 129
SHEET 3 A 5 GLU A 75 ASP A 82 -1 N GLU A 75 O LEU A 157
SHEET 4 A 5 SER A 46 ARG A 50 -1 O SER A 47 N CYS A 80
SHEET 5 A 5 VAL B 176 GLU B 178 1 O HIS B 177 N ARG A 50
SHEET 1 B 5 VAL A 176 GLU A 178 0
SHEET 2 B 5 SER B 46 ARG B 50 1 O ILE B 48 N HIS A 177
SHEET 3 B 5 GLU B 75 ASP B 82 -1 O VAL B 78 N ILE B 49
SHEET 4 B 5 VAL B 149 GLY B 158 -1 N LEU B 150 O ALA B 81
SHEET 5 B 5 GLY B 125 ILE B 129 -1 N GLY B 125 O GLY B 158
SITE 1 AC1 22 HIS A 11 SER A 13 ARG A 15 GLN A 67
SITE 2 AC1 22 VAL A 127 TYR A 128 ILE A 129 GLY A 130
SITE 3 AC1 22 GLY A 131 LYS A 167 ARG A 169 HOH A 367
SITE 4 AC1 22 HOH A 380 HOH A 403 HOH A 475 SER B 38
SITE 5 AC1 22 SER B 39 SER B 40 PHE B 42 VAL B 106
SITE 6 AC1 22 ASP B 107 HOH B 504
SITE 1 AC2 23 SER A 38 SER A 39 SER A 40 PHE A 42
SITE 2 AC2 23 VAL A 106 ASP A 107 HIS B 11 ARG B 12
SITE 3 AC2 23 SER B 13 ARG B 15 GLN B 67 VAL B 127
SITE 4 AC2 23 TYR B 128 ILE B 129 GLY B 130 GLY B 131
SITE 5 AC2 23 LYS B 167 ARG B 169 HOH B 381 HOH B 416
SITE 6 AC2 23 HOH B 425 HOH B 427 HOH B 498
CRYST1 51.560 52.860 52.830 75.79 60.71 61.17 P 1 2
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 0.019395 -0.010676 -0.010747 0.00000
SCALE2 0.000000 0.021594 -0.000270 0.00000
SCALE3 0.000000 0.000000 0.021705 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
