HEADER ELECTRON TRANSPORT 06-MAR-09 2WC1
TITLE THREE-DIMENSIONAL STRUCTURE OF THE NITROGEN FIXATION FLAVODOXIN (NIFF)
TITLE 2 FROM RHODOBACTER CAPSULATUS AT 2.2 A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLAVODOXIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOBACTER CAPSULATUS;
SOURCE 3 ORGANISM_TAXID: 1061;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET32-FLD
KEYWDS ELECTRON TRANSPORT, FLAVOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR I.PEREZ-DORADO,C.BITTEL,J.A.HERMOSO,N.CORTEZ,N.CARRILLO
REVDAT 3 13-DEC-23 2WC1 1 REMARK
REVDAT 2 30-JUL-14 2WC1 1 JRNL REMARK
REVDAT 1 21-APR-10 2WC1 0
JRNL AUTH I.PEREZ-DORADO,A.BORTOLOTTI,N.CORTEZ,J.A.HERMOSO
JRNL TITL STRUCTURAL AND PHYLOGENETIC ANALYSIS OF RHODOBACTER
JRNL TITL 2 CAPSULATUS NIFF: UNCOVERING GENERAL FEATURES OF
JRNL TITL 3 NITROGEN-FIXATION (NIF)-FLAVODOXINS.
JRNL REF INT.J.MOL.SCI. V. 14 1152 2013
JRNL REFN ESSN 1422-0067
JRNL PMID 23303276
JRNL DOI 10.3390/IJMS14011152
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH I.PEREZ-DORADO,A.BORTOLOTTI,N.CORTEZ,J.A.HERMOSO
REMARK 1 TITL CRYSTALLIZATION OF A FLAVODOXIN INVOLVED IN NITROGEN
REMARK 1 TITL 2 FIXATION IN RHODOBACTER CAPSULATUS.
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.F V. 64 375 2008
REMARK 1 REFN ESSN 1744-3091
REMARK 1 PMID 18453705
REMARK 1 DOI 10.1107/S1744309108008038
REMARK 1 REFERENCE 2
REMARK 1 AUTH I.NOGUES,I.PEREZ-DORADO,S.FRAGO,C.BITTEL,S.G.MAYHEW,
REMARK 1 AUTH 2 C.GOMEZ-MORENO,J.A.HERMOSO,M.MEDINA,N.CORTEZ,N.CARRILLO
REMARK 1 TITL THE FERREDOXIN-NADP(H) REDUCTASE FROM RHODOBACTER
REMARK 1 TITL 2 CAPSULATUS: MOLECULAR STRUCTURE AND CATALYTIC MECHANISM.
REMARK 1 REF BIOCHEMISTRY V. 44 11730 2005
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 16128574
REMARK 1 DOI 10.1021/BI0508183
REMARK 1 REFERENCE 3
REMARK 1 AUTH C.BITTEL,L.C.TABARES,M.ARMESTO,N.CARRILLO,N.CORTEZ
REMARK 1 TITL THE OXIDANT-RESPONSIVE DIAPHORASE OF RHODOBACTER CAPSULATUS
REMARK 1 TITL 2 IS A FERREDOXIN (FLAVODOXIN)-NADP(H) REDUCTASE.
REMARK 1 REF FEBS LETT. V. 553 408 2003
REMARK 1 REFN ISSN 0014-5793
REMARK 1 PMID 14572660
REMARK 1 REFERENCE 4
REMARK 1 AUTH P.C.HALLENBECK,G.GENNARO
REMARK 1 TITL STOPPED-FLOW KINETIC STUDIES OF LOW POTENTIAL ELECTRON
REMARK 1 TITL 2 CARRIERS OF THE PHOTOSYNTHETIC BACTERIUM, RHODOBACTER
REMARK 1 TITL 3 CAPSULATUS: FERREDOXIN I AND NIFF.
REMARK 1 REF BIOCHIM.BIOPHYS.ACTA V.1365 435 1998
REMARK 1 REFN ISSN 0006-3002
REMARK 1 PMID 9711296
REMARK 1 REFERENCE 5
REMARK 1 AUTH G.GENNARO,P.HUBNER,U.SANDMEIER,A.F.YAKUNIN,P.C.HALLENBECK
REMARK 1 TITL CLONING, CHARACTERIZATION, AND REGULATION OF NIFF FROM
REMARK 1 TITL 2 RHODOBACTER CAPSULATUS.
REMARK 1 REF J.BACTERIOL. V. 178 3949 1996
REMARK 1 REFN ISSN 0021-9193
REMARK 1 PMID 8682802
REMARK 1 REFERENCE 6
REMARK 1 AUTH A.F.YAKUNIN,G.GENNARO,P.C.HALLENBECK
REMARK 1 TITL PURIFICATION AND PROPERTIES OF A NIF-SPECIFIC FLAVODOXIN
REMARK 1 TITL 2 FROM THE PHOTOSYNTHETIC BACTERIUM RHODOBACTER CAPSULATUS.
REMARK 1 REF J.BACTERIOL. V. 175 6775 1993
REMARK 1 REFN ISSN 0021-9193
REMARK 1 PMID 8226618
REMARK 2
REMARK 2 RESOLUTION. 2.17 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 2.17
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.66
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1425280.340
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 14974
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) : 0.246
REMARK 3 FREE R VALUE : 0.267
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1051
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.17
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.31
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2253
REMARK 3 BIN R VALUE (WORKING SET) : 0.3020
REMARK 3 BIN FREE R VALUE : 0.3820
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 7.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 185
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.028
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1402
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 31
REMARK 3 SOLVENT ATOMS : 74
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.41000
REMARK 3 B22 (A**2) : 5.41000
REMARK 3 B33 (A**2) : -10.82000
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) : 0.31
REMARK 3 ESD FROM SIGMAA (A) : 0.20
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) : 0.38
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.29
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.900
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) : 1.270 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.930 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.870 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.630 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.41
REMARK 3 BSOL : 67.19
REMARK 3
REMARK 3 NCS MODEL : NONE
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 5 : FMN.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 5 : FMN.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2WC1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-MAR-09.
REMARK 100 THE DEPOSITION ID IS D_1290038979.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-FEB-04
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : NULL
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 : ENRAF-NONIUS FR571
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 : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24830
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 25.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 22.40
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 22.90
REMARK 200 R MERGE FOR SHELL (I) : 0.49000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 8.200
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 1FLV
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.66000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 33.20000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 33.20000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 30.33000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 33.20000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 33.20000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 90.99000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 33.20000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 33.20000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 30.33000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 33.20000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 33.20000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 90.99000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 60.66000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 SER A 10 143.13 -170.71
REMARK 500 ASN A 69 30.40 73.96
REMARK 500 SER A 74 -136.55 -154.06
REMARK 500 GLU A 106 31.07 -140.83
REMARK 500 SER A 139 136.95 -171.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
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 183
DBREF 2WC1 A 1 182 UNP P52967 FLAV_RHOCA 1 182
SEQRES 1 A 182 MET ALA LYS ILE GLY LEU PHE PHE GLY SER ASP THR GLY
SEQRES 2 A 182 THR THR ARG LYS ILE ALA LYS GLN ILE LYS ASP MET PHE
SEQRES 3 A 182 ASP ASP GLU VAL MET ALA LYS PRO LEU ASN VAL ASN ARG
SEQRES 4 A 182 ALA ASP VAL ALA ASP PHE MET ALA TYR ASP PHE LEU ILE
SEQRES 5 A 182 LEU GLY THR PRO THR LEU GLY ASP GLY GLN LEU PRO GLY
SEQRES 6 A 182 LEU SER ALA ASN ALA ALA SER GLU SER TRP GLU GLU PHE
SEQRES 7 A 182 LEU PRO ARG ILE ALA ASP GLN ASP PHE SER GLY LYS THR
SEQRES 8 A 182 ILE ALA LEU PHE GLY LEU GLY ASP GLN VAL THR TYR PRO
SEQRES 9 A 182 LEU GLU PHE VAL ASN ALA LEU PHE PHE LEU HIS GLU PHE
SEQRES 10 A 182 PHE SER ASP ARG GLY ALA ASN VAL VAL GLY ARG TRP PRO
SEQRES 11 A 182 ALA LYS GLY TYR GLY PHE GLU ASP SER LEU ALA VAL VAL
SEQRES 12 A 182 GLU GLY GLU PHE LEU GLY LEU ALA LEU ASP GLN ASP ASN
SEQRES 13 A 182 GLN ALA ALA LEU THR PRO GLU ARG LEU LYS GLY TRP LEU
SEQRES 14 A 182 SER LEU ILE ALA ALA ASP PHE GLY LEU VAL LEU PRO ALA
HET FMN A 183 31
HETNAM FMN FLAVIN MONONUCLEOTIDE
HETSYN FMN RIBOFLAVIN MONOPHOSPHATE
FORMUL 2 FMN C17 H21 N4 O9 P
FORMUL 3 HOH *74(H2 O)
HELIX 1 1 GLY A 13 ASP A 24 1 12
HELIX 2 2 ASN A 38 ALA A 40 5 3
HELIX 3 3 ASP A 41 TYR A 48 1 8
HELIX 4 4 GLY A 65 ASN A 69 5 5
HELIX 5 5 SER A 74 LEU A 79 1 6
HELIX 6 6 PRO A 80 ALA A 83 5 4
HELIX 7 7 ASN A 109 ASP A 120 1 12
HELIX 8 8 GLN A 157 ALA A 159 5 3
HELIX 9 9 LEU A 160 ILE A 172 1 13
HELIX 10 10 ILE A 172 GLY A 177 1 6
SHEET 1 AA 5 LEU A 35 ASN A 36 0
SHEET 2 AA 5 ILE A 4 PHE A 8 1 O LEU A 6 N LEU A 35
SHEET 3 AA 5 PHE A 50 PRO A 56 1 O PHE A 50 N GLY A 5
SHEET 4 AA 5 THR A 91 LEU A 97 1 O THR A 91 N LEU A 51
SHEET 5 AA 5 ASN A 124 VAL A 126 1 O ASN A 124 N ILE A 92
SHEET 1 AB 5 LEU A 35 ASN A 36 0
SHEET 2 AB 5 ILE A 4 PHE A 8 1 O LEU A 6 N LEU A 35
SHEET 3 AB 5 PHE A 50 PRO A 56 1 O PHE A 50 N GLY A 5
SHEET 4 AB 5 THR A 91 LEU A 97 1 O THR A 91 N LEU A 51
SHEET 5 AB 5 LEU A 150 LEU A 152 1 O LEU A 150 N GLY A 96
SHEET 1 AC 3 TRP A 129 PRO A 130 0
SHEET 2 AC 3 GLU A 146 PHE A 147 -1 O PHE A 147 N TRP A 129
SHEET 3 AC 3 VAL A 142 VAL A 143 -1 O VAL A 143 N GLU A 146
SITE 1 AC1 22 SER A 10 ASP A 11 THR A 12 GLY A 13
SITE 2 AC1 22 THR A 14 THR A 15 PRO A 56 THR A 57
SITE 3 AC1 22 GLY A 59 GLY A 61 LEU A 97 GLY A 98
SITE 4 AC1 22 ASP A 99 TYR A 103 GLU A 106 PHE A 107
SITE 5 AC1 22 VAL A 108 ASP A 155 HOH A2007 HOH A2009
SITE 6 AC1 22 HOH A2073 HOH A2074
CRYST1 66.400 66.400 121.320 90.00 90.00 90.00 P 41 21 2 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 0.015060 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015060 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008243 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
