LinkDB: 2ISJ 2ISK 2ISL
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HEADER FLAVOPROTEIN 17-OCT-06 2ISJ TITLE BLUB BOUND TO OXIDIZED FMN COMPND MOL_ID: 1; COMPND 2 MOLECULE: BLUB; COMPND 3 CHAIN: A, B, C, D, E, F, G, H; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SINORHIZOBIUM MELILOTI; SOURCE 3 ORGANISM_TAXID: 382; SOURCE 4 GENE: BLUB; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-28B KEYWDS OXIDOREDUCTASE, FLAVIN, MONOOXYGENASE, FLAVIN DESTRUCTASE, VITAMIN KEYWDS 2 B12, FLAVOPROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR N.A.LARSEN,M.E.TAGA,A.R.HOWARD-JONES,C.T.WALSH,G.C.WALKER REVDAT 3 21-FEB-24 2ISJ 1 REMARK SEQADV REVDAT 2 24-FEB-09 2ISJ 1 VERSN REVDAT 1 27-MAR-07 2ISJ 0 JRNL AUTH M.E.TAGA,N.A.LARSEN,A.R.HOWARD-JONES,C.T.WALSH,G.C.WALKER JRNL TITL BLUB CANNIBALIZES FLAVIN TO FORM THE LOWER LIGAND OF VITAMIN JRNL TITL 2 B12. JRNL REF NATURE V. 446 449 2007 JRNL REFN ISSN 0028-0836 JRNL PMID 17377583 JRNL DOI 10.1038/NATURE05611 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 TITL SINORHIZOBIUM MELILOTI BLUB IS NECESSARY FOR PRODUCTION OF REMARK 1 TITL 2 5,6-DIMETHLYBENZIMIDAZOLE, THE LOWER LIGAND OF B12. REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 103 4634 2006 REMARK 1 REFN ISSN 0027-8424 REMARK 1 PMID 16537439 REMARK 1 DOI 10.1073/PNAS.0509384103 REMARK 2 REMARK 2 RESOLUTION. 2.30 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 : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00 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) (%) : 80.0 REMARK 3 NUMBER OF REFLECTIONS : 71996 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) : 0.207 REMARK 3 FREE R VALUE : 0.252 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 3618 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 : 13928 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 248 REMARK 3 SOLVENT ATOMS : 519 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.00 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.06500 REMARK 3 B22 (A**2) : -0.96400 REMARK 3 B33 (A**2) : 1.02900 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) : 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) : NULL REMARK 3 BOND ANGLES (DEGREES) : NULL REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 1.192 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.868 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 1.829 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.605 ; 2.500 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 : PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 3 : FMN2.PAR REMARK 3 PARAMETER FILE 4 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 TOPOLOGY FILE 2 : NULL REMARK 3 TOPOLOGY FILE 3 : NULL REMARK 3 TOPOLOGY FILE 4 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2ISJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-OCT-06. REMARK 100 THE DEPOSITION ID IS D_1000039961. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 02-JUN-06 REMARK 200 TEMPERATURE (KELVIN) : 120 REMARK 200 PH : 5.6 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 8.2.2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9919 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 81156 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.300 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 90.2 REMARK 200 DATA REDUNDANCY : 2.800 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.06900 REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38 REMARK 200 COMPLETENESS FOR SHELL (%) : 91.8 REMARK 200 DATA REDUNDANCY IN SHELL : 2.70 REMARK 200 R MERGE FOR SHELL (I) : 0.19400 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 50.93 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8 M AMMONIUM SULFATE, 100 MM REMARK 280 CITRATE, PH 5.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-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 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 86.36200 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4 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 UNIT IS A HOMODIMER. THERE ARE 4 HOMODIMERS REMARK 300 IN THE ASSYMETRIC UNIT. DIMER 1: CHAIN A AND B, DIMER 2: CHAIN C REMARK 300 AND D, DIMER 3: CHAIN E AND F, DIMER 4: CHAIN G AND H 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: 11640 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 15910 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -70.0 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 350 REMARK 350 BIOMOLECULE: 2 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: 11660 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 15840 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D 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 REMARK 350 BIOMOLECULE: 3 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: 11690 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 15940 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -68.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F 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 REMARK 350 BIOMOLECULE: 4 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: 11730 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 15930 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H 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 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 LEU A 2 REMARK 465 PRO A 3 REMARK 465 ASP A 4 REMARK 465 PRO A 5 REMARK 465 ASN A 6 REMARK 465 GLY A 7 REMARK 465 CYS A 8 REMARK 465 GLY B -2 REMARK 465 SER B -1 REMARK 465 HIS B 0 REMARK 465 MET B 1 REMARK 465 LEU B 2 REMARK 465 PRO B 3 REMARK 465 ASP B 4 REMARK 465 PRO B 5 REMARK 465 ASN B 6 REMARK 465 GLY B 7 REMARK 465 CYS B 8 REMARK 465 GLY C -2 REMARK 465 SER C -1 REMARK 465 HIS C 0 REMARK 465 MET C 1 REMARK 465 LEU C 2 REMARK 465 PRO C 3 REMARK 465 ASP C 4 REMARK 465 PRO C 5 REMARK 465 ASN C 6 REMARK 465 GLY C 7 REMARK 465 CYS C 8 REMARK 465 GLY D -2 REMARK 465 SER D -1 REMARK 465 HIS D 0 REMARK 465 MET D 1 REMARK 465 LEU D 2 REMARK 465 PRO D 3 REMARK 465 ASP D 4 REMARK 465 PRO D 5 REMARK 465 ASN D 6 REMARK 465 GLY D 7 REMARK 465 CYS D 8 REMARK 465 GLY E -2 REMARK 465 SER E -1 REMARK 465 HIS E 0 REMARK 465 MET E 1 REMARK 465 LEU E 2 REMARK 465 PRO E 3 REMARK 465 ASP E 4 REMARK 465 PRO E 5 REMARK 465 ASN E 6 REMARK 465 GLY E 7 REMARK 465 CYS E 8 REMARK 465 GLY F -2 REMARK 465 SER F -1 REMARK 465 HIS F 0 REMARK 465 MET F 1 REMARK 465 LEU F 2 REMARK 465 PRO F 3 REMARK 465 ASP F 4 REMARK 465 PRO F 5 REMARK 465 ASN F 6 REMARK 465 GLY F 7 REMARK 465 CYS F 8 REMARK 465 GLY G -2 REMARK 465 SER G -1 REMARK 465 HIS G 0 REMARK 465 MET G 1 REMARK 465 LEU G 2 REMARK 465 PRO G 3 REMARK 465 ASP G 4 REMARK 465 PRO G 5 REMARK 465 ASN G 6 REMARK 465 GLY G 7 REMARK 465 CYS G 8 REMARK 465 GLY H -2 REMARK 465 SER H -1 REMARK 465 HIS H 0 REMARK 465 MET H 1 REMARK 465 LEU H 2 REMARK 465 PRO H 3 REMARK 465 ASP H 4 REMARK 465 PRO H 5 REMARK 465 ASN H 6 REMARK 465 GLY H 7 REMARK 465 CYS H 8 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O ASP C 89 O HOH C 568 2.15 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ARG B 197 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES REMARK 500 PRO D 181 C - N - CA ANGL. DEV. = 9.7 DEGREES REMARK 500 REMARK 500 REMARK: NULL 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 ARG A 34 -52.83 -123.23 REMARK 500 PHE A 169 168.36 178.67 REMARK 500 GLU A 222 -52.05 72.09 REMARK 500 PRO B 65 1.03 -68.32 REMARK 500 GLU B 109 150.14 167.77 REMARK 500 LEU B 132 151.82 -47.45 REMARK 500 GLU B 222 -40.24 70.16 REMARK 500 ARG C 124 -9.69 -56.77 REMARK 500 GLU C 222 -41.40 64.72 REMARK 500 ARG D 210 138.09 -173.01 REMARK 500 GLU D 222 -52.88 68.05 REMARK 500 ARG E 34 -40.57 -130.06 REMARK 500 GLU E 109 168.56 175.06 REMARK 500 ARG E 134 33.13 -94.47 REMARK 500 PHE E 169 163.89 175.31 REMARK 500 PRO E 181 171.56 -58.22 REMARK 500 GLU E 222 -46.43 60.83 REMARK 500 ARG F 34 -47.35 -130.46 REMARK 500 PHE F 194 158.83 -49.94 REMARK 500 GLU F 222 -36.41 64.82 REMARK 500 ARG G 34 -42.25 -131.33 REMARK 500 GLU G 109 155.14 176.16 REMARK 500 PHE G 169 165.44 174.65 REMARK 500 GLU G 222 -39.03 62.99 REMARK 500 ALA H 12 -141.62 -141.70 REMARK 500 ARG H 72 -5.67 -143.11 REMARK 500 GLU H 90 -5.51 -59.53 REMARK 500 GLU H 93 30.38 -78.47 REMARK 500 GLN H 139 -9.97 -50.61 REMARK 500 PRO H 181 177.25 -54.05 REMARK 500 LYS H 207 10.88 -61.95 REMARK 500 GLU H 222 -37.89 69.65 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 FMN B 501 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN A 502 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN D 503 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN C 504 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN F 505 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN E 506 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN H 507 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN G 508 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2ISK RELATED DB: PDB REMARK 900 PURPLE OXIDATION STATE. BLUB IS IN A REDUCED CHARGE TRANSFER REMARK 900 COMPLEX. REMARK 900 RELATED ID: 2ISL RELATED DB: PDB REMARK 900 CLEAR OXIDATION STATE. BLUB BOUND TO REDUCED FMNH2 AND MOLECULAR REMARK 900 OXYGEN. DBREF 2ISJ A 1 227 UNP Q92PC8 Q92PC8_RHIME 1 227 DBREF 2ISJ B 1 227 UNP Q92PC8 Q92PC8_RHIME 1 227 DBREF 2ISJ C 1 227 UNP Q92PC8 Q92PC8_RHIME 1 227 DBREF 2ISJ D 1 227 UNP Q92PC8 Q92PC8_RHIME 1 227 DBREF 2ISJ E 1 227 UNP Q92PC8 Q92PC8_RHIME 1 227 DBREF 2ISJ F 1 227 UNP Q92PC8 Q92PC8_RHIME 1 227 DBREF 2ISJ G 1 227 UNP Q92PC8 Q92PC8_RHIME 1 227 DBREF 2ISJ H 1 227 UNP Q92PC8 Q92PC8_RHIME 1 227 SEQADV 2ISJ GLY A -2 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISJ SER A -1 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISJ HIS A 0 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISJ GLY B -2 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISJ SER B -1 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISJ HIS B 0 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISJ GLY C -2 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISJ SER C -1 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISJ HIS C 0 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISJ GLY D -2 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISJ SER D -1 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISJ HIS D 0 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISJ GLY E -2 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISJ SER E -1 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISJ HIS E 0 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISJ GLY F -2 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISJ SER F -1 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISJ HIS F 0 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISJ GLY G -2 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISJ SER G -1 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISJ HIS G 0 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISJ GLY H -2 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISJ SER H -1 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISJ HIS H 0 UNP Q92PC8 CLONING ARTIFACT SEQRES 1 A 230 GLY SER HIS MET LEU PRO ASP PRO ASN GLY CYS LEU THR SEQRES 2 A 230 ALA ALA GLY ALA PHE SER SER ASP GLU ARG ALA ALA VAL SEQRES 3 A 230 TYR ARG ALA ILE GLU THR ARG ARG ASP VAL ARG ASP GLU SEQRES 4 A 230 PHE LEU PRO GLU PRO LEU SER GLU GLU LEU ILE ALA ARG SEQRES 5 A 230 LEU LEU GLY ALA ALA HIS GLN ALA PRO SER VAL GLY PHE SEQRES 6 A 230 MET GLN PRO TRP ASN PHE VAL LEU VAL ARG GLN ASP GLU SEQRES 7 A 230 THR ARG GLU LYS VAL TRP GLN ALA PHE GLN ARG ALA ASN SEQRES 8 A 230 ASP GLU ALA ALA GLU MET PHE SER GLY GLU ARG GLN ALA SEQRES 9 A 230 LYS TYR ARG SER LEU LYS LEU GLU GLY ILE ARG LYS ALA SEQRES 10 A 230 PRO LEU SER ILE CYS VAL THR CYS ASP ARG THR ARG GLY SEQRES 11 A 230 GLY ALA VAL VAL LEU GLY ARG THR HIS ASN PRO GLN MET SEQRES 12 A 230 ASP LEU TYR SER THR VAL CYS ALA VAL GLN ASN LEU TRP SEQRES 13 A 230 LEU ALA ALA ARG ALA GLU GLY VAL GLY VAL GLY TRP VAL SEQRES 14 A 230 SER ILE PHE HIS GLU SER GLU ILE LYS ALA ILE LEU GLY SEQRES 15 A 230 ILE PRO ASP HIS VAL GLU ILE VAL ALA TRP LEU CYS LEU SEQRES 16 A 230 GLY PHE VAL ASP ARG LEU TYR GLN GLU PRO GLU LEU ALA SEQRES 17 A 230 ALA LYS GLY TRP ARG GLN ARG LEU PRO LEU GLU ASP LEU SEQRES 18 A 230 VAL PHE GLU GLU GLY TRP GLY VAL ARG SEQRES 1 B 230 GLY SER HIS MET LEU PRO ASP PRO ASN GLY CYS LEU THR SEQRES 2 B 230 ALA ALA GLY ALA PHE SER SER ASP GLU ARG ALA ALA VAL SEQRES 3 B 230 TYR ARG ALA ILE GLU THR ARG ARG ASP VAL ARG ASP GLU SEQRES 4 B 230 PHE LEU PRO GLU PRO LEU SER GLU GLU LEU ILE ALA ARG SEQRES 5 B 230 LEU LEU GLY ALA ALA HIS GLN ALA PRO SER VAL GLY PHE SEQRES 6 B 230 MET GLN PRO TRP ASN PHE VAL LEU VAL ARG GLN ASP GLU SEQRES 7 B 230 THR ARG GLU LYS VAL TRP GLN ALA PHE GLN ARG ALA ASN SEQRES 8 B 230 ASP GLU ALA ALA GLU MET PHE SER GLY GLU ARG GLN ALA SEQRES 9 B 230 LYS TYR ARG SER LEU LYS LEU GLU GLY ILE ARG LYS ALA SEQRES 10 B 230 PRO LEU SER ILE CYS VAL THR CYS ASP ARG THR ARG GLY SEQRES 11 B 230 GLY ALA VAL VAL LEU GLY ARG THR HIS ASN PRO GLN MET SEQRES 12 B 230 ASP LEU TYR SER THR VAL CYS ALA VAL GLN ASN LEU TRP SEQRES 13 B 230 LEU ALA ALA ARG ALA GLU GLY VAL GLY VAL GLY TRP VAL SEQRES 14 B 230 SER ILE PHE HIS GLU SER GLU ILE LYS ALA ILE LEU GLY SEQRES 15 B 230 ILE PRO ASP HIS VAL GLU ILE VAL ALA TRP LEU CYS LEU SEQRES 16 B 230 GLY PHE VAL ASP ARG LEU TYR GLN GLU PRO GLU LEU ALA SEQRES 17 B 230 ALA LYS GLY TRP ARG GLN ARG LEU PRO LEU GLU ASP LEU SEQRES 18 B 230 VAL PHE GLU GLU GLY TRP GLY VAL ARG SEQRES 1 C 230 GLY SER HIS MET LEU PRO ASP PRO ASN GLY CYS LEU THR SEQRES 2 C 230 ALA ALA GLY ALA PHE SER SER ASP GLU ARG ALA ALA VAL SEQRES 3 C 230 TYR ARG ALA ILE GLU THR ARG ARG ASP VAL ARG ASP GLU SEQRES 4 C 230 PHE LEU PRO GLU PRO LEU SER GLU GLU LEU ILE ALA ARG SEQRES 5 C 230 LEU LEU GLY ALA ALA HIS GLN ALA PRO SER VAL GLY PHE SEQRES 6 C 230 MET GLN PRO TRP ASN PHE VAL LEU VAL ARG GLN ASP GLU SEQRES 7 C 230 THR ARG GLU LYS VAL TRP GLN ALA PHE GLN ARG ALA ASN SEQRES 8 C 230 ASP GLU ALA ALA GLU MET PHE SER GLY GLU ARG GLN ALA SEQRES 9 C 230 LYS TYR ARG SER LEU LYS LEU GLU GLY ILE ARG LYS ALA SEQRES 10 C 230 PRO LEU SER ILE CYS VAL THR CYS ASP ARG THR ARG GLY SEQRES 11 C 230 GLY ALA VAL VAL LEU GLY ARG THR HIS ASN PRO GLN MET SEQRES 12 C 230 ASP LEU TYR SER THR VAL CYS ALA VAL GLN ASN LEU TRP SEQRES 13 C 230 LEU ALA ALA ARG ALA GLU GLY VAL GLY VAL GLY TRP VAL SEQRES 14 C 230 SER ILE PHE HIS GLU SER GLU ILE LYS ALA ILE LEU GLY SEQRES 15 C 230 ILE PRO ASP HIS VAL GLU ILE VAL ALA TRP LEU CYS LEU SEQRES 16 C 230 GLY PHE VAL ASP ARG LEU TYR GLN GLU PRO GLU LEU ALA SEQRES 17 C 230 ALA LYS GLY TRP ARG GLN ARG LEU PRO LEU GLU ASP LEU SEQRES 18 C 230 VAL PHE GLU GLU GLY TRP GLY VAL ARG SEQRES 1 D 230 GLY SER HIS MET LEU PRO ASP PRO ASN GLY CYS LEU THR SEQRES 2 D 230 ALA ALA GLY ALA PHE SER SER ASP GLU ARG ALA ALA VAL SEQRES 3 D 230 TYR ARG ALA ILE GLU THR ARG ARG ASP VAL ARG ASP GLU SEQRES 4 D 230 PHE LEU PRO GLU PRO LEU SER GLU GLU LEU ILE ALA ARG SEQRES 5 D 230 LEU LEU GLY ALA ALA HIS GLN ALA PRO SER VAL GLY PHE SEQRES 6 D 230 MET GLN PRO TRP ASN PHE VAL LEU VAL ARG GLN ASP GLU SEQRES 7 D 230 THR ARG GLU LYS VAL TRP GLN ALA PHE GLN ARG ALA ASN SEQRES 8 D 230 ASP GLU ALA ALA GLU MET PHE SER GLY GLU ARG GLN ALA SEQRES 9 D 230 LYS TYR ARG SER LEU LYS LEU GLU GLY ILE ARG LYS ALA SEQRES 10 D 230 PRO LEU SER ILE CYS VAL THR CYS ASP ARG THR ARG GLY SEQRES 11 D 230 GLY ALA VAL VAL LEU GLY ARG THR HIS ASN PRO GLN MET SEQRES 12 D 230 ASP LEU TYR SER THR VAL CYS ALA VAL GLN ASN LEU TRP SEQRES 13 D 230 LEU ALA ALA ARG ALA GLU GLY VAL GLY VAL GLY TRP VAL SEQRES 14 D 230 SER ILE PHE HIS GLU SER GLU ILE LYS ALA ILE LEU GLY SEQRES 15 D 230 ILE PRO ASP HIS VAL GLU ILE VAL ALA TRP LEU CYS LEU SEQRES 16 D 230 GLY PHE VAL ASP ARG LEU TYR GLN GLU PRO GLU LEU ALA SEQRES 17 D 230 ALA LYS GLY TRP ARG GLN ARG LEU PRO LEU GLU ASP LEU SEQRES 18 D 230 VAL PHE GLU GLU GLY TRP GLY VAL ARG SEQRES 1 E 230 GLY SER HIS MET LEU PRO ASP PRO ASN GLY CYS LEU THR SEQRES 2 E 230 ALA ALA GLY ALA PHE SER SER ASP GLU ARG ALA ALA VAL SEQRES 3 E 230 TYR ARG ALA ILE GLU THR ARG ARG ASP VAL ARG ASP GLU SEQRES 4 E 230 PHE LEU PRO GLU PRO LEU SER GLU GLU LEU ILE ALA ARG SEQRES 5 E 230 LEU LEU GLY ALA ALA HIS GLN ALA PRO SER VAL GLY PHE SEQRES 6 E 230 MET GLN PRO TRP ASN PHE VAL LEU VAL ARG GLN ASP GLU SEQRES 7 E 230 THR ARG GLU LYS VAL TRP GLN ALA PHE GLN ARG ALA ASN SEQRES 8 E 230 ASP GLU ALA ALA GLU MET PHE SER GLY GLU ARG GLN ALA SEQRES 9 E 230 LYS TYR ARG SER LEU LYS LEU GLU GLY ILE ARG LYS ALA SEQRES 10 E 230 PRO LEU SER ILE CYS VAL THR CYS ASP ARG THR ARG GLY SEQRES 11 E 230 GLY ALA VAL VAL LEU GLY ARG THR HIS ASN PRO GLN MET SEQRES 12 E 230 ASP LEU TYR SER THR VAL CYS ALA VAL GLN ASN LEU TRP SEQRES 13 E 230 LEU ALA ALA ARG ALA GLU GLY VAL GLY VAL GLY TRP VAL SEQRES 14 E 230 SER ILE PHE HIS GLU SER GLU ILE LYS ALA ILE LEU GLY SEQRES 15 E 230 ILE PRO ASP HIS VAL GLU ILE VAL ALA TRP LEU CYS LEU SEQRES 16 E 230 GLY PHE VAL ASP ARG LEU TYR GLN GLU PRO GLU LEU ALA SEQRES 17 E 230 ALA LYS GLY TRP ARG GLN ARG LEU PRO LEU GLU ASP LEU SEQRES 18 E 230 VAL PHE GLU GLU GLY TRP GLY VAL ARG SEQRES 1 F 230 GLY SER HIS MET LEU PRO ASP PRO ASN GLY CYS LEU THR SEQRES 2 F 230 ALA ALA GLY ALA PHE SER SER ASP GLU ARG ALA ALA VAL SEQRES 3 F 230 TYR ARG ALA ILE GLU THR ARG ARG ASP VAL ARG ASP GLU SEQRES 4 F 230 PHE LEU PRO GLU PRO LEU SER GLU GLU LEU ILE ALA ARG SEQRES 5 F 230 LEU LEU GLY ALA ALA HIS GLN ALA PRO SER VAL GLY PHE SEQRES 6 F 230 MET GLN PRO TRP ASN PHE VAL LEU VAL ARG GLN ASP GLU SEQRES 7 F 230 THR ARG GLU LYS VAL TRP GLN ALA PHE GLN ARG ALA ASN SEQRES 8 F 230 ASP GLU ALA ALA GLU MET PHE SER GLY GLU ARG GLN ALA SEQRES 9 F 230 LYS TYR ARG SER LEU LYS LEU GLU GLY ILE ARG LYS ALA SEQRES 10 F 230 PRO LEU SER ILE CYS VAL THR CYS ASP ARG THR ARG GLY SEQRES 11 F 230 GLY ALA VAL VAL LEU GLY ARG THR HIS ASN PRO GLN MET SEQRES 12 F 230 ASP LEU TYR SER THR VAL CYS ALA VAL GLN ASN LEU TRP SEQRES 13 F 230 LEU ALA ALA ARG ALA GLU GLY VAL GLY VAL GLY TRP VAL SEQRES 14 F 230 SER ILE PHE HIS GLU SER GLU ILE LYS ALA ILE LEU GLY SEQRES 15 F 230 ILE PRO ASP HIS VAL GLU ILE VAL ALA TRP LEU CYS LEU SEQRES 16 F 230 GLY PHE VAL ASP ARG LEU TYR GLN GLU PRO GLU LEU ALA SEQRES 17 F 230 ALA LYS GLY TRP ARG GLN ARG LEU PRO LEU GLU ASP LEU SEQRES 18 F 230 VAL PHE GLU GLU GLY TRP GLY VAL ARG SEQRES 1 G 230 GLY SER HIS MET LEU PRO ASP PRO ASN GLY CYS LEU THR SEQRES 2 G 230 ALA ALA GLY ALA PHE SER SER ASP GLU ARG ALA ALA VAL SEQRES 3 G 230 TYR ARG ALA ILE GLU THR ARG ARG ASP VAL ARG ASP GLU SEQRES 4 G 230 PHE LEU PRO GLU PRO LEU SER GLU GLU LEU ILE ALA ARG SEQRES 5 G 230 LEU LEU GLY ALA ALA HIS GLN ALA PRO SER VAL GLY PHE SEQRES 6 G 230 MET GLN PRO TRP ASN PHE VAL LEU VAL ARG GLN ASP GLU SEQRES 7 G 230 THR ARG GLU LYS VAL TRP GLN ALA PHE GLN ARG ALA ASN SEQRES 8 G 230 ASP GLU ALA ALA GLU MET PHE SER GLY GLU ARG GLN ALA SEQRES 9 G 230 LYS TYR ARG SER LEU LYS LEU GLU GLY ILE ARG LYS ALA SEQRES 10 G 230 PRO LEU SER ILE CYS VAL THR CYS ASP ARG THR ARG GLY SEQRES 11 G 230 GLY ALA VAL VAL LEU GLY ARG THR HIS ASN PRO GLN MET SEQRES 12 G 230 ASP LEU TYR SER THR VAL CYS ALA VAL GLN ASN LEU TRP SEQRES 13 G 230 LEU ALA ALA ARG ALA GLU GLY VAL GLY VAL GLY TRP VAL SEQRES 14 G 230 SER ILE PHE HIS GLU SER GLU ILE LYS ALA ILE LEU GLY SEQRES 15 G 230 ILE PRO ASP HIS VAL GLU ILE VAL ALA TRP LEU CYS LEU SEQRES 16 G 230 GLY PHE VAL ASP ARG LEU TYR GLN GLU PRO GLU LEU ALA SEQRES 17 G 230 ALA LYS GLY TRP ARG GLN ARG LEU PRO LEU GLU ASP LEU SEQRES 18 G 230 VAL PHE GLU GLU GLY TRP GLY VAL ARG SEQRES 1 H 230 GLY SER HIS MET LEU PRO ASP PRO ASN GLY CYS LEU THR SEQRES 2 H 230 ALA ALA GLY ALA PHE SER SER ASP GLU ARG ALA ALA VAL SEQRES 3 H 230 TYR ARG ALA ILE GLU THR ARG ARG ASP VAL ARG ASP GLU SEQRES 4 H 230 PHE LEU PRO GLU PRO LEU SER GLU GLU LEU ILE ALA ARG SEQRES 5 H 230 LEU LEU GLY ALA ALA HIS GLN ALA PRO SER VAL GLY PHE SEQRES 6 H 230 MET GLN PRO TRP ASN PHE VAL LEU VAL ARG GLN ASP GLU SEQRES 7 H 230 THR ARG GLU LYS VAL TRP GLN ALA PHE GLN ARG ALA ASN SEQRES 8 H 230 ASP GLU ALA ALA GLU MET PHE SER GLY GLU ARG GLN ALA SEQRES 9 H 230 LYS TYR ARG SER LEU LYS LEU GLU GLY ILE ARG LYS ALA SEQRES 10 H 230 PRO LEU SER ILE CYS VAL THR CYS ASP ARG THR ARG GLY SEQRES 11 H 230 GLY ALA VAL VAL LEU GLY ARG THR HIS ASN PRO GLN MET SEQRES 12 H 230 ASP LEU TYR SER THR VAL CYS ALA VAL GLN ASN LEU TRP SEQRES 13 H 230 LEU ALA ALA ARG ALA GLU GLY VAL GLY VAL GLY TRP VAL SEQRES 14 H 230 SER ILE PHE HIS GLU SER GLU ILE LYS ALA ILE LEU GLY SEQRES 15 H 230 ILE PRO ASP HIS VAL GLU ILE VAL ALA TRP LEU CYS LEU SEQRES 16 H 230 GLY PHE VAL ASP ARG LEU TYR GLN GLU PRO GLU LEU ALA SEQRES 17 H 230 ALA LYS GLY TRP ARG GLN ARG LEU PRO LEU GLU ASP LEU SEQRES 18 H 230 VAL PHE GLU GLU GLY TRP GLY VAL ARG HET FMN A 502 31 HET FMN B 501 31 HET FMN C 504 31 HET FMN D 503 31 HET FMN E 506 31 HET FMN F 505 31 HET FMN G 508 31 HET FMN H 507 31 HETNAM FMN FLAVIN MONONUCLEOTIDE HETSYN FMN RIBOFLAVIN MONOPHOSPHATE FORMUL 9 FMN 8(C17 H21 N4 O9 P) FORMUL 17 HOH *519(H2 O) HELIX 1 1 SER A 16 ARG A 30 1 15 HELIX 2 2 SER A 43 GLN A 56 1 14 HELIX 3 3 SER A 59 MET A 63 5 5 HELIX 4 4 GLN A 73 GLU A 93 1 21 HELIX 5 5 SER A 96 ARG A 104 1 9 HELIX 6 6 GLN A 139 GLU A 159 1 21 HELIX 7 7 HIS A 170 GLY A 179 1 10 HELIX 8 8 PRO A 202 LYS A 207 1 6 HELIX 9 9 PRO A 214 ASP A 217 5 4 HELIX 10 10 SER B 16 ARG B 30 1 15 HELIX 11 11 SER B 43 HIS B 55 1 13 HELIX 12 12 SER B 59 MET B 63 5 5 HELIX 13 13 GLN B 73 GLU B 93 1 21 HELIX 14 14 SER B 96 SER B 105 1 10 HELIX 15 15 GLN B 139 GLU B 159 1 21 HELIX 16 16 HIS B 170 GLY B 179 1 10 HELIX 17 17 PRO B 202 LYS B 207 1 6 HELIX 18 18 PRO B 214 ASP B 217 5 4 HELIX 19 19 SER C 16 ARG C 30 1 15 HELIX 20 20 SER C 43 GLN C 56 1 14 HELIX 21 21 SER C 59 MET C 63 5 5 HELIX 22 22 GLN C 73 MET C 94 1 22 HELIX 23 23 SER C 96 LEU C 106 1 11 HELIX 24 24 GLN C 139 GLU C 159 1 21 HELIX 25 25 HIS C 170 GLY C 179 1 10 HELIX 26 26 PRO C 202 LYS C 207 1 6 HELIX 27 27 PRO C 214 LEU C 218 1 5 HELIX 28 28 SER D 16 ARG D 30 1 15 HELIX 29 29 SER D 43 GLN D 56 1 14 HELIX 30 30 SER D 59 MET D 63 5 5 HELIX 31 31 GLN D 73 GLU D 93 1 21 HELIX 32 32 SER D 96 ARG D 104 1 9 HELIX 33 33 GLN D 139 GLU D 159 1 21 HELIX 34 34 HIS D 170 GLY D 179 1 10 HELIX 35 35 PRO D 202 LYS D 207 1 6 HELIX 36 36 PRO D 214 ASP D 217 5 4 HELIX 37 37 SER E 16 ARG E 30 1 15 HELIX 38 38 SER E 43 GLN E 56 1 14 HELIX 39 39 SER E 59 MET E 63 5 5 HELIX 40 40 GLN E 73 GLU E 93 1 21 HELIX 41 41 SER E 96 LEU E 106 1 11 HELIX 42 42 GLN E 139 GLU E 159 1 21 HELIX 43 43 HIS E 170 GLY E 179 1 10 HELIX 44 44 PRO E 202 LYS E 207 1 6 HELIX 45 45 PRO E 214 ASP E 217 5 4 HELIX 46 46 SER F 16 ARG F 30 1 15 HELIX 47 47 SER F 43 GLN F 56 1 14 HELIX 48 48 SER F 59 MET F 63 5 5 HELIX 49 49 GLN F 73 ALA F 92 1 20 HELIX 50 50 GLU F 93 PHE F 95 5 3 HELIX 51 51 SER F 96 SER F 105 1 10 HELIX 52 52 GLN F 139 GLU F 159 1 21 HELIX 53 53 HIS F 170 GLY F 179 1 10 HELIX 54 54 PRO F 202 LYS F 207 1 6 HELIX 55 55 PRO F 214 LEU F 218 1 5 HELIX 56 56 SER G 16 ARG G 30 1 15 HELIX 57 57 SER G 43 GLN G 56 1 14 HELIX 58 58 SER G 59 MET G 63 5 5 HELIX 59 59 GLN G 73 GLU G 93 1 21 HELIX 60 60 SER G 96 SER G 105 1 10 HELIX 61 61 GLN G 139 GLU G 159 1 21 HELIX 62 62 HIS G 170 GLY G 179 1 10 HELIX 63 63 PRO G 202 LYS G 207 1 6 HELIX 64 64 PRO G 214 LEU G 218 1 5 HELIX 65 65 SER H 16 ARG H 30 1 15 HELIX 66 66 SER H 43 GLN H 56 1 14 HELIX 67 67 SER H 59 MET H 63 5 5 HELIX 68 68 GLN H 73 GLU H 93 1 21 HELIX 69 69 SER H 96 ARG H 104 1 9 HELIX 70 70 GLN H 139 GLU H 159 1 21 HELIX 71 71 HIS H 170 GLY H 179 1 10 HELIX 72 72 PRO H 202 LYS H 207 1 6 HELIX 73 73 PRO H 214 ASP H 217 5 4 SHEET 1 A 2 THR A 10 ALA A 11 0 SHEET 2 A 2 ARG B 197 LEU B 198 -1 O LEU B 198 N THR A 10 SHEET 1 B 5 VAL A 161 VAL A 166 0 SHEET 2 B 5 VAL A 184 PHE A 194 -1 O CYS A 191 N GLY A 164 SHEET 3 B 5 LEU A 116 ASP A 123 -1 N LEU A 116 O LEU A 192 SHEET 4 B 5 TRP A 66 VAL A 71 -1 N VAL A 71 O SER A 117 SHEET 5 B 5 VAL B 219 GLU B 221 1 O PHE B 220 N LEU A 70 SHEET 1 C 2 ARG A 197 LEU A 198 0 SHEET 2 C 2 THR B 10 ALA B 11 -1 O THR B 10 N LEU A 198 SHEET 1 D 5 VAL A 219 GLU A 221 0 SHEET 2 D 5 TRP B 66 VAL B 71 1 O PHE B 68 N PHE A 220 SHEET 3 D 5 LEU B 116 ASP B 123 -1 O SER B 117 N VAL B 71 SHEET 4 D 5 VAL B 184 PHE B 194 -1 O LEU B 192 N LEU B 116 SHEET 5 D 5 VAL B 161 VAL B 166 -1 N GLY B 162 O GLY B 193 SHEET 1 E 2 THR C 10 ALA C 11 0 SHEET 2 E 2 ARG D 197 LEU D 198 -1 O LEU D 198 N THR C 10 SHEET 1 F 5 VAL C 161 VAL C 166 0 SHEET 2 F 5 VAL C 184 PHE C 194 -1 O GLY C 193 N GLY C 162 SHEET 3 F 5 LEU C 116 ASP C 123 -1 N LEU C 116 O LEU C 192 SHEET 4 F 5 TRP C 66 VAL C 71 -1 N VAL C 71 O SER C 117 SHEET 5 F 5 VAL D 219 GLU D 221 1 O PHE D 220 N PHE C 68 SHEET 1 G 2 ARG C 197 LEU C 198 0 SHEET 2 G 2 THR D 10 ALA D 11 -1 O THR D 10 N LEU C 198 SHEET 1 H 5 VAL C 219 GLU C 221 0 SHEET 2 H 5 TRP D 66 VAL D 71 1 O PHE D 68 N PHE C 220 SHEET 3 H 5 LEU D 116 ASP D 123 -1 O SER D 117 N VAL D 71 SHEET 4 H 5 VAL D 184 PHE D 194 -1 O LEU D 192 N LEU D 116 SHEET 5 H 5 VAL D 161 VAL D 166 -1 N GLY D 164 O CYS D 191 SHEET 1 I 2 THR E 10 ALA E 11 0 SHEET 2 I 2 ARG F 197 LEU F 198 -1 O LEU F 198 N THR E 10 SHEET 1 J 5 VAL E 161 VAL E 166 0 SHEET 2 J 5 VAL E 184 PHE E 194 -1 O GLY E 193 N GLY E 162 SHEET 3 J 5 LEU E 116 ASP E 123 -1 N CYS E 122 O GLU E 185 SHEET 4 J 5 TRP E 66 VAL E 71 -1 N VAL E 71 O SER E 117 SHEET 5 J 5 VAL F 219 GLU F 221 1 O PHE F 220 N PHE E 68 SHEET 1 K 2 ARG E 197 LEU E 198 0 SHEET 2 K 2 THR F 10 ALA F 11 -1 O THR F 10 N LEU E 198 SHEET 1 L 5 VAL E 219 GLU E 221 0 SHEET 2 L 5 TRP F 66 VAL F 71 1 O PHE F 68 N PHE E 220 SHEET 3 L 5 LEU F 116 ASP F 123 -1 O SER F 117 N VAL F 71 SHEET 4 L 5 VAL F 184 PHE F 194 -1 O LEU F 192 N LEU F 116 SHEET 5 L 5 VAL F 161 VAL F 166 -1 N GLY F 164 O CYS F 191 SHEET 1 M 2 THR G 10 ALA G 11 0 SHEET 2 M 2 ARG H 197 LEU H 198 -1 O LEU H 198 N THR G 10 SHEET 1 N 5 VAL G 161 TRP G 165 0 SHEET 2 N 5 VAL G 184 PHE G 194 -1 O CYS G 191 N GLY G 164 SHEET 3 N 5 LEU G 116 ASP G 123 -1 N LEU G 116 O LEU G 192 SHEET 4 N 5 TRP G 66 VAL G 71 -1 N VAL G 71 O SER G 117 SHEET 5 N 5 VAL H 219 GLU H 221 1 O PHE H 220 N PHE G 68 SHEET 1 O 2 ARG G 197 LEU G 198 0 SHEET 2 O 2 THR H 10 ALA H 11 -1 O THR H 10 N LEU G 198 SHEET 1 P 5 VAL G 219 GLU G 221 0 SHEET 2 P 5 TRP H 66 VAL H 71 1 O PHE H 68 N PHE G 220 SHEET 3 P 5 LEU H 116 ASP H 123 -1 O SER H 117 N VAL H 71 SHEET 4 P 5 VAL H 184 PHE H 194 -1 O LEU H 192 N LEU H 116 SHEET 5 P 5 VAL H 161 TRP H 165 -1 N GLY H 164 O CYS H 191 SITE 1 AC1 21 PRO A 58 SER A 59 VAL A 60 PHE A 62 SITE 2 AC1 21 MET A 140 SER A 144 ARG B 30 ARG B 31 SITE 3 AC1 21 ASP B 32 ARG B 34 LEU B 108 TRP B 165 SITE 4 AC1 21 VAL B 166 SER B 167 ILE B 168 PRO B 202 SITE 5 AC1 21 LEU B 204 HOH B 525 HOH B 527 HOH B 563 SITE 6 AC1 21 HOH B 583 SITE 1 AC2 20 ARG A 30 ARG A 31 ASP A 32 ARG A 34 SITE 2 AC2 20 LEU A 108 TRP A 165 VAL A 166 SER A 167 SITE 3 AC2 20 ILE A 168 PRO A 202 LEU A 204 HOH A 509 SITE 4 AC2 20 HOH A 511 HOH A 517 HOH A 908 PRO B 58 SITE 5 AC2 20 SER B 59 VAL B 60 MET B 140 SER B 144 SITE 1 AC3 20 PRO C 58 SER C 59 VAL C 60 PHE C 62 SITE 2 AC3 20 MET C 140 SER C 144 ARG D 30 ARG D 31 SITE 3 AC3 20 ASP D 32 ARG D 34 LEU D 108 TRP D 165 SITE 4 AC3 20 VAL D 166 SER D 167 PRO D 202 LEU D 204 SITE 5 AC3 20 HOH D 510 HOH D 539 HOH D 555 HOH D 778 SITE 1 AC4 21 ARG C 30 ARG C 31 ASP C 32 ARG C 34 SITE 2 AC4 21 LEU C 108 TRP C 165 VAL C 166 SER C 167 SITE 3 AC4 21 ILE C 168 PRO C 202 LEU C 204 HOH C 524 SITE 4 AC4 21 HOH C1088 PRO D 58 SER D 59 VAL D 60 SITE 5 AC4 21 GLY D 61 PHE D 62 MET D 140 SER D 144 SITE 6 AC4 21 HOH D 522 SITE 1 AC5 21 PRO E 58 SER E 59 VAL E 60 GLY E 61 SITE 2 AC5 21 PHE E 62 MET E 140 SER E 144 ARG F 30 SITE 3 AC5 21 ARG F 31 ASP F 32 ARG F 34 LEU F 108 SITE 4 AC5 21 TRP F 165 VAL F 166 SER F 167 ILE F 168 SITE 5 AC5 21 PRO F 202 LEU F 204 HOH F 591 HOH F 804 SITE 6 AC5 21 HOH F1018 SITE 1 AC6 19 ARG E 30 ARG E 31 ASP E 32 ARG E 34 SITE 2 AC6 19 LEU E 108 TRP E 165 VAL E 166 SER E 167 SITE 3 AC6 19 ILE E 168 PRO E 202 LEU E 204 HOH E 519 SITE 4 AC6 19 HOH E 912 PRO F 58 SER F 59 VAL F 60 SITE 5 AC6 19 PHE F 62 MET F 140 SER F 144 SITE 1 AC7 20 PRO G 58 SER G 59 VAL G 60 GLY G 61 SITE 2 AC7 20 PHE G 62 MET G 140 SER G 144 HOH G1089 SITE 3 AC7 20 ARG H 30 ARG H 31 ASP H 32 ARG H 34 SITE 4 AC7 20 LEU H 108 TRP H 165 VAL H 166 SER H 167 SITE 5 AC7 20 PRO H 202 LEU H 204 HOH H 611 HOH H 764 SITE 1 AC8 18 ARG G 30 ARG G 31 ASP G 32 ARG G 34 SITE 2 AC8 18 LEU G 108 TRP G 165 VAL G 166 SER G 167 SITE 3 AC8 18 ILE G 168 PRO G 202 LEU G 204 HOH G 602 SITE 4 AC8 18 PRO H 58 SER H 59 VAL H 60 MET H 140 SITE 5 AC8 18 SER H 144 HOH H1090 CRYST1 65.149 172.724 92.063 90.00 90.06 90.00 P 1 21 1 16 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 0.015349 0.000000 0.000016 0.00000 SCALE2 0.000000 0.005790 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010862 0.00000 (ATOM LINES ARE NOT SHOWN.) END
HEADER FLAVOPROTEIN 17-OCT-06 2ISK TITLE BLUB BOUND TO FLAVIN ANION (CHARGE TRANSFER COMPLEX) COMPND MOL_ID: 1; COMPND 2 MOLECULE: BLUB; COMPND 3 CHAIN: A, B, C, D, E, F, G, H; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SINORHIZOBIUM MELILOTI; SOURCE 3 ORGANISM_TAXID: 382; SOURCE 4 GENE: BLUB; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-28B KEYWDS OXIDOREDUCTASE, FLAVIN, MONOOXYGENASE, FLAVIN DESTRUCTASE, VITAMIN KEYWDS 2 B12, DITHIONITE, CHARGE TRANSFER COMPLEX, FLAVOPROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR N.A.LARSEN,M.E.TAGA,A.R.HOWARD-JONES,C.T.WALSH,G.C.WALKER REVDAT 3 21-FEB-24 2ISK 1 REMARK SEQADV REVDAT 2 24-FEB-09 2ISK 1 VERSN REVDAT 1 27-MAR-07 2ISK 0 JRNL AUTH M.E.TAGA,N.A.LARSEN,A.R.HOWARD-JONES,C.T.WALSH,G.C.WALKER JRNL TITL BLUB CANNIBALIZES FLAVIN TO FORM THE LOWER LIGAND OF VITAMIN JRNL TITL 2 B12. JRNL REF NATURE V. 446 449 2007 JRNL REFN ISSN 0028-0836 JRNL PMID 17377583 JRNL DOI 10.1038/NATURE05611 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 TITL SINORHIZOBIUM MELILOTI BLUB IS NECESSARY FOR PRODUCTION OF REMARK 1 TITL 2 5,6-DIMETHYLBENZIMIDAZOLE, THE LOWER LIGAND OF B12. REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 103 4634 2006 REMARK 1 REFN ISSN 0027-8424 REMARK 1 PMID 16537439 REMARK 1 DOI 10.1073/PNAS.0509384103 REMARK 2 REMARK 2 RESOLUTION. 2.10 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 : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 80.2 REMARK 3 NUMBER OF REFLECTIONS : 89676 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) : 0.204 REMARK 3 FREE R VALUE : 0.250 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 4513 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 : 13928 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 248 REMARK 3 SOLVENT ATOMS : 951 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.20 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -11.13000 REMARK 3 B22 (A**2) : 3.40000 REMARK 3 B33 (A**2) : 7.73000 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) : 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) : NULL REMARK 3 BOND ANGLES (DEGREES) : NULL REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 1.138 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.657 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 1.941 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.702 ; 2.500 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 : PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 3 : FNR.PAR REMARK 3 PARAMETER FILE 4 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 TOPOLOGY FILE 2 : NULL REMARK 3 TOPOLOGY FILE 3 : NULL REMARK 3 TOPOLOGY FILE 4 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2ISK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-OCT-06. REMARK 100 THE DEPOSITION ID IS D_1000039962. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 02-JUN-06 REMARK 200 TEMPERATURE (KELVIN) : 120 REMARK 200 PH : 5.6 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 8.2.2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9919 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 94174 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.100 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 84.6 REMARK 200 DATA REDUNDANCY : 2.900 REMARK 200 R MERGE (I) : 0.08400 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18 REMARK 200 COMPLETENESS FOR SHELL (%) : 82.9 REMARK 200 DATA REDUNDANCY IN SHELL : 2.70 REMARK 200 R MERGE FOR SHELL (I) : 0.21200 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 48.14 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8 M AMMONIUM SULFATE, 100 MM CITRATE REMARK 280 SOAKED IN SATURATED DITHIONITE PRIOR TO FREEZING, PH 5.6, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-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 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 84.93600 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4 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 ASSEMBLY CONSISTS OF A HOMODIMER. THERE ARE FOUR REMARK 300 HOMODIMERS IN THE ASSYMETRIC UNIT. DIMER 1 = CHAIN A/B, DIMER 2 = REMARK 300 CHAIN C/D, DIMER 3 = CHAIN E/F, DIMER 4 = CHAIN G/H 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: 11640 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 15830 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -69.0 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 350 REMARK 350 BIOMOLECULE: 2 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: 11590 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 15710 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D 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 REMARK 350 BIOMOLECULE: 3 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: 11590 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 15750 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -70.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F 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 REMARK 350 BIOMOLECULE: 4 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: 11540 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 15800 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H 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 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 LEU A 2 REMARK 465 PRO A 3 REMARK 465 ASP A 4 REMARK 465 PRO A 5 REMARK 465 ASN A 6 REMARK 465 GLY A 7 REMARK 465 CYS A 8 REMARK 465 GLY B -2 REMARK 465 SER B -1 REMARK 465 HIS B 0 REMARK 465 MET B 1 REMARK 465 LEU B 2 REMARK 465 PRO B 3 REMARK 465 ASP B 4 REMARK 465 PRO B 5 REMARK 465 ASN B 6 REMARK 465 GLY B 7 REMARK 465 CYS B 8 REMARK 465 GLY C -2 REMARK 465 SER C -1 REMARK 465 HIS C 0 REMARK 465 MET C 1 REMARK 465 LEU C 2 REMARK 465 PRO C 3 REMARK 465 ASP C 4 REMARK 465 PRO C 5 REMARK 465 ASN C 6 REMARK 465 GLY C 7 REMARK 465 CYS C 8 REMARK 465 GLY D -2 REMARK 465 SER D -1 REMARK 465 HIS D 0 REMARK 465 MET D 1 REMARK 465 LEU D 2 REMARK 465 PRO D 3 REMARK 465 ASP D 4 REMARK 465 PRO D 5 REMARK 465 ASN D 6 REMARK 465 GLY D 7 REMARK 465 CYS D 8 REMARK 465 GLY E -2 REMARK 465 SER E -1 REMARK 465 HIS E 0 REMARK 465 MET E 1 REMARK 465 LEU E 2 REMARK 465 PRO E 3 REMARK 465 ASP E 4 REMARK 465 PRO E 5 REMARK 465 ASN E 6 REMARK 465 GLY E 7 REMARK 465 CYS E 8 REMARK 465 GLY F -2 REMARK 465 SER F -1 REMARK 465 HIS F 0 REMARK 465 MET F 1 REMARK 465 LEU F 2 REMARK 465 PRO F 3 REMARK 465 ASP F 4 REMARK 465 PRO F 5 REMARK 465 ASN F 6 REMARK 465 GLY F 7 REMARK 465 CYS F 8 REMARK 465 GLY G -2 REMARK 465 SER G -1 REMARK 465 HIS G 0 REMARK 465 MET G 1 REMARK 465 LEU G 2 REMARK 465 PRO G 3 REMARK 465 ASP G 4 REMARK 465 PRO G 5 REMARK 465 ASN G 6 REMARK 465 GLY G 7 REMARK 465 CYS G 8 REMARK 465 GLY H -2 REMARK 465 SER H -1 REMARK 465 HIS H 0 REMARK 465 MET H 1 REMARK 465 LEU H 2 REMARK 465 PRO H 3 REMARK 465 ASP H 4 REMARK 465 PRO H 5 REMARK 465 ASN H 6 REMARK 465 GLY H 7 REMARK 465 CYS H 8 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O VAL F 130 O HOH F 758 2.10 REMARK 500 O ALA B 14 O HOH B 790 2.16 REMARK 500 REMARK 500 REMARK: NULL 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 109 156.38 179.63 REMARK 500 PHE A 169 166.15 177.53 REMARK 500 GLU A 222 -32.94 65.55 REMARK 500 GLU B 222 -33.14 67.71 REMARK 500 GLU C 109 155.58 179.55 REMARK 500 PHE C 169 168.08 173.86 REMARK 500 GLU C 222 -39.64 69.98 REMARK 500 GLU D 109 150.26 179.62 REMARK 500 GLU D 222 -36.73 69.74 REMARK 500 GLU E 109 156.57 177.25 REMARK 500 GLU E 222 -33.95 68.41 REMARK 500 GLU F 222 -42.72 66.36 REMARK 500 PHE G 169 168.71 170.59 REMARK 500 GLU G 222 -39.53 69.29 REMARK 500 GLU H 222 -39.81 70.27 REMARK 500 REMARK 500 REMARK: NULL REMARK 600 REMARK 600 HETEROGEN REMARK 600 THE FLAVIN IS IN THE ANION STATE REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FNR B 501 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FNR A 502 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FNR D 503 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FNR C 504 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FNR F 505 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FNR E 506 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FNR H 507 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FNR G 508 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2ISJ RELATED DB: PDB REMARK 900 BLUB BOUND TO OXIDIZED FMN REMARK 900 RELATED ID: 2ISL RELATED DB: PDB REMARK 900 BLUB BOUND TO REDUCED FMNH2 AND MOLECULAR OXYGEN. DBREF 2ISK A 1 227 UNP Q92PC8 Q92PC8_RHIME 1 227 DBREF 2ISK B 1 227 UNP Q92PC8 Q92PC8_RHIME 1 227 DBREF 2ISK C 1 227 UNP Q92PC8 Q92PC8_RHIME 1 227 DBREF 2ISK D 1 227 UNP Q92PC8 Q92PC8_RHIME 1 227 DBREF 2ISK E 1 227 UNP Q92PC8 Q92PC8_RHIME 1 227 DBREF 2ISK F 1 227 UNP Q92PC8 Q92PC8_RHIME 1 227 DBREF 2ISK G 1 227 UNP Q92PC8 Q92PC8_RHIME 1 227 DBREF 2ISK H 1 227 UNP Q92PC8 Q92PC8_RHIME 1 227 SEQADV 2ISK GLY A -2 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISK SER A -1 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISK HIS A 0 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISK GLY B -2 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISK SER B -1 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISK HIS B 0 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISK GLY C -2 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISK SER C -1 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISK HIS C 0 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISK GLY D -2 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISK SER D -1 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISK HIS D 0 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISK GLY E -2 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISK SER E -1 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISK HIS E 0 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISK GLY F -2 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISK SER F -1 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISK HIS F 0 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISK GLY G -2 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISK SER G -1 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISK HIS G 0 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISK GLY H -2 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISK SER H -1 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISK HIS H 0 UNP Q92PC8 CLONING ARTIFACT SEQRES 1 A 230 GLY SER HIS MET LEU PRO ASP PRO ASN GLY CYS LEU THR SEQRES 2 A 230 ALA ALA GLY ALA PHE SER SER ASP GLU ARG ALA ALA VAL SEQRES 3 A 230 TYR ARG ALA ILE GLU THR ARG ARG ASP VAL ARG ASP GLU SEQRES 4 A 230 PHE LEU PRO GLU PRO LEU SER GLU GLU LEU ILE ALA ARG SEQRES 5 A 230 LEU LEU GLY ALA ALA HIS GLN ALA PRO SER VAL GLY PHE SEQRES 6 A 230 MET GLN PRO TRP ASN PHE VAL LEU VAL ARG GLN ASP GLU SEQRES 7 A 230 THR ARG GLU LYS VAL TRP GLN ALA PHE GLN ARG ALA ASN SEQRES 8 A 230 ASP GLU ALA ALA GLU MET PHE SER GLY GLU ARG GLN ALA SEQRES 9 A 230 LYS TYR ARG SER LEU LYS LEU GLU GLY ILE ARG LYS ALA SEQRES 10 A 230 PRO LEU SER ILE CYS VAL THR CYS ASP ARG THR ARG GLY SEQRES 11 A 230 GLY ALA VAL VAL LEU GLY ARG THR HIS ASN PRO GLN MET SEQRES 12 A 230 ASP LEU TYR SER THR VAL CYS ALA VAL GLN ASN LEU TRP SEQRES 13 A 230 LEU ALA ALA ARG ALA GLU GLY VAL GLY VAL GLY TRP VAL SEQRES 14 A 230 SER ILE PHE HIS GLU SER GLU ILE LYS ALA ILE LEU GLY SEQRES 15 A 230 ILE PRO ASP HIS VAL GLU ILE VAL ALA TRP LEU CYS LEU SEQRES 16 A 230 GLY PHE VAL ASP ARG LEU TYR GLN GLU PRO GLU LEU ALA SEQRES 17 A 230 ALA LYS GLY TRP ARG GLN ARG LEU PRO LEU GLU ASP LEU SEQRES 18 A 230 VAL PHE GLU GLU GLY TRP GLY VAL ARG SEQRES 1 B 230 GLY SER HIS MET LEU PRO ASP PRO ASN GLY CYS LEU THR SEQRES 2 B 230 ALA ALA GLY ALA PHE SER SER ASP GLU ARG ALA ALA VAL SEQRES 3 B 230 TYR ARG ALA ILE GLU THR ARG ARG ASP VAL ARG ASP GLU SEQRES 4 B 230 PHE LEU PRO GLU PRO LEU SER GLU GLU LEU ILE ALA ARG SEQRES 5 B 230 LEU LEU GLY ALA ALA HIS GLN ALA PRO SER VAL GLY PHE SEQRES 6 B 230 MET GLN PRO TRP ASN PHE VAL LEU VAL ARG GLN ASP GLU SEQRES 7 B 230 THR ARG GLU LYS VAL TRP GLN ALA PHE GLN ARG ALA ASN SEQRES 8 B 230 ASP GLU ALA ALA GLU MET PHE SER GLY GLU ARG GLN ALA SEQRES 9 B 230 LYS TYR ARG SER LEU LYS LEU GLU GLY ILE ARG LYS ALA SEQRES 10 B 230 PRO LEU SER ILE CYS VAL THR CYS ASP ARG THR ARG GLY SEQRES 11 B 230 GLY ALA VAL VAL LEU GLY ARG THR HIS ASN PRO GLN MET SEQRES 12 B 230 ASP LEU TYR SER THR VAL CYS ALA VAL GLN ASN LEU TRP SEQRES 13 B 230 LEU ALA ALA ARG ALA GLU GLY VAL GLY VAL GLY TRP VAL SEQRES 14 B 230 SER ILE PHE HIS GLU SER GLU ILE LYS ALA ILE LEU GLY SEQRES 15 B 230 ILE PRO ASP HIS VAL GLU ILE VAL ALA TRP LEU CYS LEU SEQRES 16 B 230 GLY PHE VAL ASP ARG LEU TYR GLN GLU PRO GLU LEU ALA SEQRES 17 B 230 ALA LYS GLY TRP ARG GLN ARG LEU PRO LEU GLU ASP LEU SEQRES 18 B 230 VAL PHE GLU GLU GLY TRP GLY VAL ARG SEQRES 1 C 230 GLY SER HIS MET LEU PRO ASP PRO ASN GLY CYS LEU THR SEQRES 2 C 230 ALA ALA GLY ALA PHE SER SER ASP GLU ARG ALA ALA VAL SEQRES 3 C 230 TYR ARG ALA ILE GLU THR ARG ARG ASP VAL ARG ASP GLU SEQRES 4 C 230 PHE LEU PRO GLU PRO LEU SER GLU GLU LEU ILE ALA ARG SEQRES 5 C 230 LEU LEU GLY ALA ALA HIS GLN ALA PRO SER VAL GLY PHE SEQRES 6 C 230 MET GLN PRO TRP ASN PHE VAL LEU VAL ARG GLN ASP GLU SEQRES 7 C 230 THR ARG GLU LYS VAL TRP GLN ALA PHE GLN ARG ALA ASN SEQRES 8 C 230 ASP GLU ALA ALA GLU MET PHE SER GLY GLU ARG GLN ALA SEQRES 9 C 230 LYS TYR ARG SER LEU LYS LEU GLU GLY ILE ARG LYS ALA SEQRES 10 C 230 PRO LEU SER ILE CYS VAL THR CYS ASP ARG THR ARG GLY SEQRES 11 C 230 GLY ALA VAL VAL LEU GLY ARG THR HIS ASN PRO GLN MET SEQRES 12 C 230 ASP LEU TYR SER THR VAL CYS ALA VAL GLN ASN LEU TRP SEQRES 13 C 230 LEU ALA ALA ARG ALA GLU GLY VAL GLY VAL GLY TRP VAL SEQRES 14 C 230 SER ILE PHE HIS GLU SER GLU ILE LYS ALA ILE LEU GLY SEQRES 15 C 230 ILE PRO ASP HIS VAL GLU ILE VAL ALA TRP LEU CYS LEU SEQRES 16 C 230 GLY PHE VAL ASP ARG LEU TYR GLN GLU PRO GLU LEU ALA SEQRES 17 C 230 ALA LYS GLY TRP ARG GLN ARG LEU PRO LEU GLU ASP LEU SEQRES 18 C 230 VAL PHE GLU GLU GLY TRP GLY VAL ARG SEQRES 1 D 230 GLY SER HIS MET LEU PRO ASP PRO ASN GLY CYS LEU THR SEQRES 2 D 230 ALA ALA GLY ALA PHE SER SER ASP GLU ARG ALA ALA VAL SEQRES 3 D 230 TYR ARG ALA ILE GLU THR ARG ARG ASP VAL ARG ASP GLU SEQRES 4 D 230 PHE LEU PRO GLU PRO LEU SER GLU GLU LEU ILE ALA ARG SEQRES 5 D 230 LEU LEU GLY ALA ALA HIS GLN ALA PRO SER VAL GLY PHE SEQRES 6 D 230 MET GLN PRO TRP ASN PHE VAL LEU VAL ARG GLN ASP GLU SEQRES 7 D 230 THR ARG GLU LYS VAL TRP GLN ALA PHE GLN ARG ALA ASN SEQRES 8 D 230 ASP GLU ALA ALA GLU MET PHE SER GLY GLU ARG GLN ALA SEQRES 9 D 230 LYS TYR ARG SER LEU LYS LEU GLU GLY ILE ARG LYS ALA SEQRES 10 D 230 PRO LEU SER ILE CYS VAL THR CYS ASP ARG THR ARG GLY SEQRES 11 D 230 GLY ALA VAL VAL LEU GLY ARG THR HIS ASN PRO GLN MET SEQRES 12 D 230 ASP LEU TYR SER THR VAL CYS ALA VAL GLN ASN LEU TRP SEQRES 13 D 230 LEU ALA ALA ARG ALA GLU GLY VAL GLY VAL GLY TRP VAL SEQRES 14 D 230 SER ILE PHE HIS GLU SER GLU ILE LYS ALA ILE LEU GLY SEQRES 15 D 230 ILE PRO ASP HIS VAL GLU ILE VAL ALA TRP LEU CYS LEU SEQRES 16 D 230 GLY PHE VAL ASP ARG LEU TYR GLN GLU PRO GLU LEU ALA SEQRES 17 D 230 ALA LYS GLY TRP ARG GLN ARG LEU PRO LEU GLU ASP LEU SEQRES 18 D 230 VAL PHE GLU GLU GLY TRP GLY VAL ARG SEQRES 1 E 230 GLY SER HIS MET LEU PRO ASP PRO ASN GLY CYS LEU THR SEQRES 2 E 230 ALA ALA GLY ALA PHE SER SER ASP GLU ARG ALA ALA VAL SEQRES 3 E 230 TYR ARG ALA ILE GLU THR ARG ARG ASP VAL ARG ASP GLU SEQRES 4 E 230 PHE LEU PRO GLU PRO LEU SER GLU GLU LEU ILE ALA ARG SEQRES 5 E 230 LEU LEU GLY ALA ALA HIS GLN ALA PRO SER VAL GLY PHE SEQRES 6 E 230 MET GLN PRO TRP ASN PHE VAL LEU VAL ARG GLN ASP GLU SEQRES 7 E 230 THR ARG GLU LYS VAL TRP GLN ALA PHE GLN ARG ALA ASN SEQRES 8 E 230 ASP GLU ALA ALA GLU MET PHE SER GLY GLU ARG GLN ALA SEQRES 9 E 230 LYS TYR ARG SER LEU LYS LEU GLU GLY ILE ARG LYS ALA SEQRES 10 E 230 PRO LEU SER ILE CYS VAL THR CYS ASP ARG THR ARG GLY SEQRES 11 E 230 GLY ALA VAL VAL LEU GLY ARG THR HIS ASN PRO GLN MET SEQRES 12 E 230 ASP LEU TYR SER THR VAL CYS ALA VAL GLN ASN LEU TRP SEQRES 13 E 230 LEU ALA ALA ARG ALA GLU GLY VAL GLY VAL GLY TRP VAL SEQRES 14 E 230 SER ILE PHE HIS GLU SER GLU ILE LYS ALA ILE LEU GLY SEQRES 15 E 230 ILE PRO ASP HIS VAL GLU ILE VAL ALA TRP LEU CYS LEU SEQRES 16 E 230 GLY PHE VAL ASP ARG LEU TYR GLN GLU PRO GLU LEU ALA SEQRES 17 E 230 ALA LYS GLY TRP ARG GLN ARG LEU PRO LEU GLU ASP LEU SEQRES 18 E 230 VAL PHE GLU GLU GLY TRP GLY VAL ARG SEQRES 1 F 230 GLY SER HIS MET LEU PRO ASP PRO ASN GLY CYS LEU THR SEQRES 2 F 230 ALA ALA GLY ALA PHE SER SER ASP GLU ARG ALA ALA VAL SEQRES 3 F 230 TYR ARG ALA ILE GLU THR ARG ARG ASP VAL ARG ASP GLU SEQRES 4 F 230 PHE LEU PRO GLU PRO LEU SER GLU GLU LEU ILE ALA ARG SEQRES 5 F 230 LEU LEU GLY ALA ALA HIS GLN ALA PRO SER VAL GLY PHE SEQRES 6 F 230 MET GLN PRO TRP ASN PHE VAL LEU VAL ARG GLN ASP GLU SEQRES 7 F 230 THR ARG GLU LYS VAL TRP GLN ALA PHE GLN ARG ALA ASN SEQRES 8 F 230 ASP GLU ALA ALA GLU MET PHE SER GLY GLU ARG GLN ALA SEQRES 9 F 230 LYS TYR ARG SER LEU LYS LEU GLU GLY ILE ARG LYS ALA SEQRES 10 F 230 PRO LEU SER ILE CYS VAL THR CYS ASP ARG THR ARG GLY SEQRES 11 F 230 GLY ALA VAL VAL LEU GLY ARG THR HIS ASN PRO GLN MET SEQRES 12 F 230 ASP LEU TYR SER THR VAL CYS ALA VAL GLN ASN LEU TRP SEQRES 13 F 230 LEU ALA ALA ARG ALA GLU GLY VAL GLY VAL GLY TRP VAL SEQRES 14 F 230 SER ILE PHE HIS GLU SER GLU ILE LYS ALA ILE LEU GLY SEQRES 15 F 230 ILE PRO ASP HIS VAL GLU ILE VAL ALA TRP LEU CYS LEU SEQRES 16 F 230 GLY PHE VAL ASP ARG LEU TYR GLN GLU PRO GLU LEU ALA SEQRES 17 F 230 ALA LYS GLY TRP ARG GLN ARG LEU PRO LEU GLU ASP LEU SEQRES 18 F 230 VAL PHE GLU GLU GLY TRP GLY VAL ARG SEQRES 1 G 230 GLY SER HIS MET LEU PRO ASP PRO ASN GLY CYS LEU THR SEQRES 2 G 230 ALA ALA GLY ALA PHE SER SER ASP GLU ARG ALA ALA VAL SEQRES 3 G 230 TYR ARG ALA ILE GLU THR ARG ARG ASP VAL ARG ASP GLU SEQRES 4 G 230 PHE LEU PRO GLU PRO LEU SER GLU GLU LEU ILE ALA ARG SEQRES 5 G 230 LEU LEU GLY ALA ALA HIS GLN ALA PRO SER VAL GLY PHE SEQRES 6 G 230 MET GLN PRO TRP ASN PHE VAL LEU VAL ARG GLN ASP GLU SEQRES 7 G 230 THR ARG GLU LYS VAL TRP GLN ALA PHE GLN ARG ALA ASN SEQRES 8 G 230 ASP GLU ALA ALA GLU MET PHE SER GLY GLU ARG GLN ALA SEQRES 9 G 230 LYS TYR ARG SER LEU LYS LEU GLU GLY ILE ARG LYS ALA SEQRES 10 G 230 PRO LEU SER ILE CYS VAL THR CYS ASP ARG THR ARG GLY SEQRES 11 G 230 GLY ALA VAL VAL LEU GLY ARG THR HIS ASN PRO GLN MET SEQRES 12 G 230 ASP LEU TYR SER THR VAL CYS ALA VAL GLN ASN LEU TRP SEQRES 13 G 230 LEU ALA ALA ARG ALA GLU GLY VAL GLY VAL GLY TRP VAL SEQRES 14 G 230 SER ILE PHE HIS GLU SER GLU ILE LYS ALA ILE LEU GLY SEQRES 15 G 230 ILE PRO ASP HIS VAL GLU ILE VAL ALA TRP LEU CYS LEU SEQRES 16 G 230 GLY PHE VAL ASP ARG LEU TYR GLN GLU PRO GLU LEU ALA SEQRES 17 G 230 ALA LYS GLY TRP ARG GLN ARG LEU PRO LEU GLU ASP LEU SEQRES 18 G 230 VAL PHE GLU GLU GLY TRP GLY VAL ARG SEQRES 1 H 230 GLY SER HIS MET LEU PRO ASP PRO ASN GLY CYS LEU THR SEQRES 2 H 230 ALA ALA GLY ALA PHE SER SER ASP GLU ARG ALA ALA VAL SEQRES 3 H 230 TYR ARG ALA ILE GLU THR ARG ARG ASP VAL ARG ASP GLU SEQRES 4 H 230 PHE LEU PRO GLU PRO LEU SER GLU GLU LEU ILE ALA ARG SEQRES 5 H 230 LEU LEU GLY ALA ALA HIS GLN ALA PRO SER VAL GLY PHE SEQRES 6 H 230 MET GLN PRO TRP ASN PHE VAL LEU VAL ARG GLN ASP GLU SEQRES 7 H 230 THR ARG GLU LYS VAL TRP GLN ALA PHE GLN ARG ALA ASN SEQRES 8 H 230 ASP GLU ALA ALA GLU MET PHE SER GLY GLU ARG GLN ALA SEQRES 9 H 230 LYS TYR ARG SER LEU LYS LEU GLU GLY ILE ARG LYS ALA SEQRES 10 H 230 PRO LEU SER ILE CYS VAL THR CYS ASP ARG THR ARG GLY SEQRES 11 H 230 GLY ALA VAL VAL LEU GLY ARG THR HIS ASN PRO GLN MET SEQRES 12 H 230 ASP LEU TYR SER THR VAL CYS ALA VAL GLN ASN LEU TRP SEQRES 13 H 230 LEU ALA ALA ARG ALA GLU GLY VAL GLY VAL GLY TRP VAL SEQRES 14 H 230 SER ILE PHE HIS GLU SER GLU ILE LYS ALA ILE LEU GLY SEQRES 15 H 230 ILE PRO ASP HIS VAL GLU ILE VAL ALA TRP LEU CYS LEU SEQRES 16 H 230 GLY PHE VAL ASP ARG LEU TYR GLN GLU PRO GLU LEU ALA SEQRES 17 H 230 ALA LYS GLY TRP ARG GLN ARG LEU PRO LEU GLU ASP LEU SEQRES 18 H 230 VAL PHE GLU GLU GLY TRP GLY VAL ARG HET FNR A 502 31 HET FNR B 501 31 HET FNR C 504 31 HET FNR D 503 31 HET FNR E 506 31 HET FNR F 505 31 HET FNR G 508 31 HET FNR H 507 31 HETNAM FNR 1-DEOXY-1-(7,8-DIMETHYL-2,4-DIOXO-3,4-DIHYDRO-2H- HETNAM 2 FNR BENZO[G]PTERIDIN-1-ID-10(5H)-YL)-5-O-PHOSPHONATO-D- HETNAM 3 FNR RIBITOL HETSYN FNR TWO ELECTRON REDUCED FLAVIN MONONUCLEOTIDE FORMUL 9 FNR 8(C17 H23 N4 O9 P) FORMUL 17 HOH *951(H2 O) HELIX 1 1 SER A 16 ARG A 30 1 15 HELIX 2 2 SER A 43 GLN A 56 1 14 HELIX 3 3 SER A 59 MET A 63 5 5 HELIX 4 4 GLN A 73 MET A 94 1 22 HELIX 5 5 SER A 96 LEU A 106 1 11 HELIX 6 6 GLN A 139 GLY A 160 1 22 HELIX 7 7 HIS A 170 GLY A 179 1 10 HELIX 8 8 PRO A 202 LYS A 207 1 6 HELIX 9 9 PRO A 214 LEU A 218 1 5 HELIX 10 10 SER B 16 ARG B 30 1 15 HELIX 11 11 SER B 43 GLN B 56 1 14 HELIX 12 12 SER B 59 MET B 63 5 5 HELIX 13 13 GLN B 73 GLU B 93 1 21 HELIX 14 14 SER B 96 LEU B 106 1 11 HELIX 15 15 GLN B 139 GLU B 159 1 21 HELIX 16 16 HIS B 170 GLY B 179 1 10 HELIX 17 17 PRO B 202 LYS B 207 1 6 HELIX 18 18 PRO B 214 ASP B 217 5 4 HELIX 19 19 SER C 16 ARG C 30 1 15 HELIX 20 20 SER C 43 GLN C 56 1 14 HELIX 21 21 SER C 59 MET C 63 5 5 HELIX 22 22 GLN C 73 GLU C 93 1 21 HELIX 23 23 SER C 96 LEU C 106 1 11 HELIX 24 24 GLN C 139 GLU C 159 1 21 HELIX 25 25 HIS C 170 GLY C 179 1 10 HELIX 26 26 PRO C 202 LYS C 207 1 6 HELIX 27 27 PRO C 214 ASP C 217 5 4 HELIX 28 28 SER D 16 ARG D 30 1 15 HELIX 29 29 SER D 43 HIS D 55 1 13 HELIX 30 30 SER D 59 MET D 63 5 5 HELIX 31 31 GLN D 73 GLU D 93 1 21 HELIX 32 32 SER D 96 LEU D 106 1 11 HELIX 33 33 GLN D 139 GLU D 159 1 21 HELIX 34 34 HIS D 170 GLY D 179 1 10 HELIX 35 35 PRO D 202 LYS D 207 1 6 HELIX 36 36 PRO D 214 LEU D 218 1 5 HELIX 37 37 SER E 16 ARG E 30 1 15 HELIX 38 38 SER E 43 GLN E 56 1 14 HELIX 39 39 SER E 59 MET E 63 5 5 HELIX 40 40 GLN E 73 GLU E 93 1 21 HELIX 41 41 SER E 96 LEU E 106 1 11 HELIX 42 42 GLN E 139 GLU E 159 1 21 HELIX 43 43 HIS E 170 GLY E 179 1 10 HELIX 44 44 PRO E 202 LYS E 207 1 6 HELIX 45 45 PRO E 214 ASP E 217 5 4 HELIX 46 46 SER F 16 ARG F 30 1 15 HELIX 47 47 SER F 43 HIS F 55 1 13 HELIX 48 48 SER F 59 MET F 63 5 5 HELIX 49 49 GLN F 73 GLU F 93 1 21 HELIX 50 50 SER F 96 LEU F 106 1 11 HELIX 51 51 GLN F 139 GLU F 159 1 21 HELIX 52 52 HIS F 170 GLY F 179 1 10 HELIX 53 53 PRO F 202 LYS F 207 1 6 HELIX 54 54 PRO F 214 ASP F 217 5 4 HELIX 55 55 SER G 16 ARG G 30 1 15 HELIX 56 56 SER G 43 GLN G 56 1 14 HELIX 57 57 SER G 59 MET G 63 5 5 HELIX 58 58 GLN G 73 GLU G 93 1 21 HELIX 59 59 SER G 96 SER G 105 1 10 HELIX 60 60 GLN G 139 GLU G 159 1 21 HELIX 61 61 HIS G 170 GLY G 179 1 10 HELIX 62 62 PRO G 202 LYS G 207 1 6 HELIX 63 63 PRO G 214 ASP G 217 5 4 HELIX 64 64 SER H 16 ARG H 30 1 15 HELIX 65 65 SER H 43 GLN H 56 1 14 HELIX 66 66 SER H 59 MET H 63 5 5 HELIX 67 67 GLN H 73 GLU H 93 1 21 HELIX 68 68 SER H 96 SER H 105 1 10 HELIX 69 69 GLN H 139 GLU H 159 1 21 HELIX 70 70 HIS H 170 GLY H 179 1 10 HELIX 71 71 PRO H 202 LYS H 207 1 6 HELIX 72 72 PRO H 214 ASP H 217 5 4 SHEET 1 A 2 THR A 10 ALA A 11 0 SHEET 2 A 2 ARG B 197 LEU B 198 -1 O LEU B 198 N THR A 10 SHEET 1 B 5 VAL A 161 TRP A 165 0 SHEET 2 B 5 VAL A 184 PHE A 194 -1 O GLY A 193 N GLY A 162 SHEET 3 B 5 LEU A 116 ASP A 123 -1 N LEU A 116 O LEU A 192 SHEET 4 B 5 TRP A 66 VAL A 71 -1 N VAL A 71 O SER A 117 SHEET 5 B 5 VAL B 219 GLU B 221 1 O PHE B 220 N LEU A 70 SHEET 1 C 2 ARG A 197 LEU A 198 0 SHEET 2 C 2 THR B 10 ALA B 11 -1 O THR B 10 N LEU A 198 SHEET 1 D 5 VAL A 219 GLU A 221 0 SHEET 2 D 5 TRP B 66 VAL B 71 1 O PHE B 68 N PHE A 220 SHEET 3 D 5 LEU B 116 ASP B 123 -1 O SER B 117 N VAL B 71 SHEET 4 D 5 VAL B 184 PHE B 194 -1 O LEU B 192 N LEU B 116 SHEET 5 D 5 VAL B 161 VAL B 166 -1 N GLY B 162 O GLY B 193 SHEET 1 E 2 THR C 10 ALA C 11 0 SHEET 2 E 2 ARG D 197 LEU D 198 -1 O LEU D 198 N THR C 10 SHEET 1 F 5 VAL C 161 TRP C 165 0 SHEET 2 F 5 VAL C 184 PHE C 194 -1 O GLY C 193 N GLY C 162 SHEET 3 F 5 LEU C 116 ASP C 123 -1 N LEU C 116 O LEU C 192 SHEET 4 F 5 TRP C 66 VAL C 71 -1 N VAL C 71 O SER C 117 SHEET 5 F 5 VAL D 219 GLU D 221 1 O PHE D 220 N PHE C 68 SHEET 1 G 2 ARG C 197 LEU C 198 0 SHEET 2 G 2 THR D 10 ALA D 11 -1 O THR D 10 N LEU C 198 SHEET 1 H 5 VAL C 219 GLU C 221 0 SHEET 2 H 5 TRP D 66 VAL D 71 1 O PHE D 68 N PHE C 220 SHEET 3 H 5 LEU D 116 ASP D 123 -1 O SER D 117 N VAL D 71 SHEET 4 H 5 VAL D 184 PHE D 194 -1 O LEU D 192 N LEU D 116 SHEET 5 H 5 VAL D 161 VAL D 166 -1 N GLY D 162 O GLY D 193 SHEET 1 I 2 THR E 10 ALA E 11 0 SHEET 2 I 2 ARG F 197 LEU F 198 -1 O LEU F 198 N THR E 10 SHEET 1 J 5 VAL E 161 VAL E 166 0 SHEET 2 J 5 VAL E 184 PHE E 194 -1 O GLY E 193 N GLY E 162 SHEET 3 J 5 LEU E 116 ASP E 123 -1 N LEU E 116 O LEU E 192 SHEET 4 J 5 TRP E 66 VAL E 71 -1 N VAL E 71 O SER E 117 SHEET 5 J 5 VAL F 219 GLU F 221 1 O PHE F 220 N PHE E 68 SHEET 1 K 2 ARG E 197 LEU E 198 0 SHEET 2 K 2 THR F 10 ALA F 11 -1 O THR F 10 N LEU E 198 SHEET 1 L 5 VAL E 219 GLU E 221 0 SHEET 2 L 5 TRP F 66 VAL F 71 1 O PHE F 68 N PHE E 220 SHEET 3 L 5 LEU F 116 ASP F 123 -1 O SER F 117 N VAL F 71 SHEET 4 L 5 VAL F 184 PHE F 194 -1 O LEU F 192 N LEU F 116 SHEET 5 L 5 VAL F 161 VAL F 166 -1 N GLY F 162 O GLY F 193 SHEET 1 M 2 THR G 10 ALA G 11 0 SHEET 2 M 2 ARG H 197 LEU H 198 -1 O LEU H 198 N THR G 10 SHEET 1 N 5 VAL G 161 TRP G 165 0 SHEET 2 N 5 VAL G 184 PHE G 194 -1 O GLY G 193 N GLY G 162 SHEET 3 N 5 LEU G 116 ASP G 123 -1 N LEU G 116 O LEU G 192 SHEET 4 N 5 TRP G 66 VAL G 71 -1 N VAL G 71 O SER G 117 SHEET 5 N 5 VAL H 219 GLU H 221 1 O PHE H 220 N LEU G 70 SHEET 1 O 2 ARG G 197 LEU G 198 0 SHEET 2 O 2 THR H 10 ALA H 11 -1 O THR H 10 N LEU G 198 SHEET 1 P 5 VAL G 219 GLU G 221 0 SHEET 2 P 5 TRP H 66 VAL H 71 1 O PHE H 68 N PHE G 220 SHEET 3 P 5 LEU H 116 ASP H 123 -1 O SER H 117 N VAL H 71 SHEET 4 P 5 VAL H 184 PHE H 194 -1 O LEU H 192 N LEU H 116 SHEET 5 P 5 VAL H 161 TRP H 165 -1 N GLY H 162 O GLY H 193 SITE 1 AC1 21 PRO A 58 SER A 59 VAL A 60 PHE A 62 SITE 2 AC1 21 MET A 140 SER A 144 ARG B 30 ARG B 31 SITE 3 AC1 21 ASP B 32 ARG B 34 LEU B 108 TRP B 165 SITE 4 AC1 21 VAL B 166 SER B 167 ILE B 168 PRO B 202 SITE 5 AC1 21 LEU B 204 HOH B 543 HOH B 782 HOH B 842 SITE 6 AC1 21 HOH B1644 SITE 1 AC2 20 ARG A 30 ARG A 31 ASP A 32 ARG A 34 SITE 2 AC2 20 LEU A 108 TRP A 165 VAL A 166 SER A 167 SITE 3 AC2 20 ILE A 168 PRO A 202 LEU A 204 HOH A 512 SITE 4 AC2 20 HOH A 524 HOH A 542 PRO B 58 SER B 59 SITE 5 AC2 20 VAL B 60 GLY B 61 MET B 140 SER B 144 SITE 1 AC3 20 PRO C 58 SER C 59 VAL C 60 PHE C 62 SITE 2 AC3 20 MET C 140 SER C 144 ARG D 30 ARG D 31 SITE 3 AC3 20 ASP D 32 ARG D 34 LEU D 108 TRP D 165 SITE 4 AC3 20 VAL D 166 SER D 167 ILE D 168 PRO D 202 SITE 5 AC3 20 LEU D 204 HOH D 513 HOH D 536 HOH D 791 SITE 1 AC4 20 ARG C 30 ARG C 31 ASP C 32 ARG C 34 SITE 2 AC4 20 LEU C 108 TRP C 165 VAL C 166 SER C 167 SITE 3 AC4 20 ILE C 168 PRO C 202 LEU C 204 HOH C 511 SITE 4 AC4 20 HOH C 577 HOH C 579 HOH C1090 PRO D 58 SITE 5 AC4 20 SER D 59 VAL D 60 MET D 140 SER D 144 SITE 1 AC5 22 PRO E 58 SER E 59 VAL E 60 PHE E 62 SITE 2 AC5 22 MET E 140 SER E 144 ARG F 30 ARG F 31 SITE 3 AC5 22 ASP F 32 ARG F 34 LEU F 108 TRP F 165 SITE 4 AC5 22 VAL F 166 SER F 167 ILE F 168 PRO F 202 SITE 5 AC5 22 LEU F 204 HOH F 529 HOH F 550 HOH F 671 SITE 6 AC5 22 HOH F1359 HOH F1645 SITE 1 AC6 21 ARG E 30 ARG E 31 ASP E 32 ARG E 34 SITE 2 AC6 21 LEU E 108 TRP E 165 VAL E 166 SER E 167 SITE 3 AC6 21 ILE E 168 PRO E 202 LEU E 204 HOH E 510 SITE 4 AC6 21 HOH E 534 HOH E 662 HOH E1266 PRO F 58 SITE 5 AC6 21 SER F 59 VAL F 60 PHE F 62 MET F 140 SITE 6 AC6 21 SER F 144 SITE 1 AC7 21 PRO G 58 SER G 59 VAL G 60 PHE G 62 SITE 2 AC7 21 MET G 140 SER G 144 ARG H 30 ARG H 31 SITE 3 AC7 21 ASP H 32 ARG H 34 LEU H 108 TRP H 165 SITE 4 AC7 21 VAL H 166 SER H 167 ILE H 168 PRO H 202 SITE 5 AC7 21 LEU H 204 HOH H 509 HOH H 592 HOH H 636 SITE 6 AC7 21 HOH H 642 SITE 1 AC8 19 ARG G 30 ARG G 31 ASP G 32 ARG G 34 SITE 2 AC8 19 LEU G 108 TRP G 165 VAL G 166 SER G 167 SITE 3 AC8 19 ILE G 168 PRO G 202 LEU G 204 HOH G 514 SITE 4 AC8 19 HOH G1144 PRO H 58 SER H 59 VAL H 60 SITE 5 AC8 19 GLY H 61 MET H 140 SER H 144 CRYST1 63.449 169.872 90.954 90.00 89.99 90.00 P 1 21 1 16 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 0.015761 0.000000 -0.000003 0.00000 SCALE2 0.000000 0.005887 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010995 0.00000 (ATOM LINES ARE NOT SHOWN.) END
HEADER FLAVOPROTEIN 17-OCT-06 2ISL TITLE BLUB BOUND TO REDUCED FLAVIN (FMNH2) AND MOLECULAR OXYGEN. (CLEAR TITLE 2 CRYSTAL FORM) COMPND MOL_ID: 1; COMPND 2 MOLECULE: BLUB; COMPND 3 CHAIN: A, B, C, D, E, F, G, H; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SINORHIZOBIUM MELILOTI; SOURCE 3 ORGANISM_TAXID: 382; SOURCE 4 GENE: BLUB; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-28B KEYWDS FLAVIN, OXIDOREDUCTASE, MONOOXYGENASE, FLAVIN DESTRUCTASE, MOLECULAR KEYWDS 2 OXYGEN, FLAVOPROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR N.A.LARSEN,M.E.TAGA,A.R.HOWARD-JONES,C.T.WALSH,G.C.WALKER REVDAT 3 21-FEB-24 2ISL 1 REMARK SEQADV REVDAT 2 24-FEB-09 2ISL 1 VERSN REVDAT 1 27-MAR-07 2ISL 0 JRNL AUTH M.E.TAGA,N.A.LARSEN,A.R.HOWARD-JONES,C.T.WALSH,G.C.WALKER JRNL TITL BLUB CANNIBALIZES FLAVIN TO FORM THE LOWER LIGAND OF VITAMIN JRNL TITL 2 B12. JRNL REF NATURE V. 446 449 2007 JRNL REFN ISSN 0028-0836 JRNL PMID 17377583 JRNL DOI 10.1038/NATURE05611 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 TITL SINORHIZOBIUM MELILOTI BLUB IS NECESSARY FOR PRODUCTION OF REMARK 1 TITL 2 5,6-DIMETHYLBENZIMIDAZOLE, THE LOWER LIGAND OF B12. REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 103 4634 2006 REMARK 1 REFN ISSN 0027-8424 REMARK 1 PMID 16537439 REMARK 1 DOI 10.1073/PNAS.0509384103 REMARK 2 REMARK 2 RESOLUTION. 2.90 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 : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.7 REMARK 3 NUMBER OF REFLECTIONS : 43289 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) : 0.217 REMARK 3 FREE R VALUE : 0.285 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 2170 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 : 13928 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 264 REMARK 3 SOLVENT ATOMS : 63 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.00 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -3.67200 REMARK 3 B22 (A**2) : 0.12700 REMARK 3 B33 (A**2) : 3.54500 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) : 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) : NULL REMARK 3 BOND ANGLES (DEGREES) : NULL REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 1.264 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.199 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 1.606 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.475 ; 2.500 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 : PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 3 : FMNH2.PAR REMARK 3 PARAMETER FILE 4 : OXY.PARAM REMARK 3 PARAMETER FILE 5 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 TOPOLOGY FILE 2 : NULL REMARK 3 TOPOLOGY FILE 3 : NULL REMARK 3 TOPOLOGY FILE 4 : NULL REMARK 3 TOPOLOGY FILE 5 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2ISL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-OCT-06. REMARK 100 THE DEPOSITION ID IS D_1000039963. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 02-JUN-06 REMARK 200 TEMPERATURE (KELVIN) : 120 REMARK 200 PH : 5.6 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 8.2.2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9919 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44966 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.300 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 3.800 REMARK 200 R MERGE (I) : 0.07900 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 3.70 REMARK 200 R MERGE FOR SHELL (I) : 0.31500 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 51.14 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8 AMMONIUM SULFATE, 100 MM CITRATE REMARK 280 SOAKED IN SATURATED DITHIONITE, AND THEN BACKSOAKED IN REMARK 280 OXYGENATED MOTHER LIQUOR PRIOR TO FREEZING, PH 5.6, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-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 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 86.91800 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4 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 CONSISTS OF A HOMODIMER. THERE ARE REMARK 300 4 DIMERS IN THE ASYMMETRIC UNIT. DIMER1 = CHAIN A/B, DIMER2 = CHAIN REMARK 300 C/D, DIMER3 = CHAIN E/F, DIMER4 = CHAIN G/H 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: 11810 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 15840 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.0 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 350 REMARK 350 BIOMOLECULE: 2 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: 11790 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 15960 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D 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 REMARK 350 BIOMOLECULE: 3 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: 11740 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 15980 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -70.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F 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 REMARK 350 BIOMOLECULE: 4 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: 11830 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 15760 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -71.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H 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 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 LEU A 2 REMARK 465 PRO A 3 REMARK 465 ASP A 4 REMARK 465 PRO A 5 REMARK 465 ASN A 6 REMARK 465 GLY A 7 REMARK 465 CYS A 8 REMARK 465 GLY B -2 REMARK 465 SER B -1 REMARK 465 HIS B 0 REMARK 465 MET B 1 REMARK 465 LEU B 2 REMARK 465 PRO B 3 REMARK 465 ASP B 4 REMARK 465 PRO B 5 REMARK 465 ASN B 6 REMARK 465 GLY B 7 REMARK 465 CYS B 8 REMARK 465 GLY C -2 REMARK 465 SER C -1 REMARK 465 HIS C 0 REMARK 465 MET C 1 REMARK 465 LEU C 2 REMARK 465 PRO C 3 REMARK 465 ASP C 4 REMARK 465 PRO C 5 REMARK 465 ASN C 6 REMARK 465 GLY C 7 REMARK 465 CYS C 8 REMARK 465 GLY D -2 REMARK 465 SER D -1 REMARK 465 HIS D 0 REMARK 465 MET D 1 REMARK 465 LEU D 2 REMARK 465 PRO D 3 REMARK 465 ASP D 4 REMARK 465 PRO D 5 REMARK 465 ASN D 6 REMARK 465 GLY D 7 REMARK 465 CYS D 8 REMARK 465 GLY E -2 REMARK 465 SER E -1 REMARK 465 HIS E 0 REMARK 465 MET E 1 REMARK 465 LEU E 2 REMARK 465 PRO E 3 REMARK 465 ASP E 4 REMARK 465 PRO E 5 REMARK 465 ASN E 6 REMARK 465 GLY E 7 REMARK 465 CYS E 8 REMARK 465 GLY F -2 REMARK 465 SER F -1 REMARK 465 HIS F 0 REMARK 465 MET F 1 REMARK 465 LEU F 2 REMARK 465 PRO F 3 REMARK 465 ASP F 4 REMARK 465 PRO F 5 REMARK 465 ASN F 6 REMARK 465 GLY F 7 REMARK 465 CYS F 8 REMARK 465 GLY G -2 REMARK 465 SER G -1 REMARK 465 HIS G 0 REMARK 465 MET G 1 REMARK 465 LEU G 2 REMARK 465 PRO G 3 REMARK 465 ASP G 4 REMARK 465 PRO G 5 REMARK 465 ASN G 6 REMARK 465 GLY G 7 REMARK 465 CYS G 8 REMARK 465 GLY H -2 REMARK 465 SER H -1 REMARK 465 HIS H 0 REMARK 465 MET H 1 REMARK 465 LEU H 2 REMARK 465 PRO H 3 REMARK 465 ASP H 4 REMARK 465 PRO H 5 REMARK 465 ASN H 6 REMARK 465 GLY H 7 REMARK 465 CYS H 8 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 GLY B 13 N - CA - C ANGL. DEV. = 16.0 DEGREES REMARK 500 PRO D 138 C - N - CA ANGL. DEV. = 9.2 DEGREES REMARK 500 PRO G 181 C - N - CA ANGL. DEV. = 9.2 DEGREES REMARK 500 REMARK 500 REMARK: NULL 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 THR A 10 139.85 153.65 REMARK 500 SER A 59 124.04 -175.06 REMARK 500 GLU A 93 7.04 -62.24 REMARK 500 ARG A 104 4.65 -54.27 REMARK 500 GLU A 109 161.31 179.46 REMARK 500 THR A 135 -37.97 121.79 REMARK 500 HIS A 136 30.46 -91.26 REMARK 500 ASN A 137 112.94 146.75 REMARK 500 PRO A 181 -179.76 -53.15 REMARK 500 ARG A 210 138.53 -172.11 REMARK 500 GLU A 222 -33.45 63.72 REMARK 500 THR B 10 152.30 159.51 REMARK 500 ALA B 11 121.06 68.47 REMARK 500 ALA B 12 -130.65 -65.20 REMARK 500 PRO B 65 1.73 -69.70 REMARK 500 ARG B 86 -63.44 97.35 REMARK 500 ARG B 104 -8.62 -56.28 REMARK 500 GLU B 109 159.08 171.08 REMARK 500 VAL B 131 159.93 166.18 REMARK 500 PHE B 169 148.90 174.71 REMARK 500 LYS B 207 17.20 -69.35 REMARK 500 ARG B 210 139.98 -172.32 REMARK 500 GLU B 222 -12.59 63.25 REMARK 500 SER C 59 127.77 -170.79 REMARK 500 PHE C 95 -169.71 -119.75 REMARK 500 ARG C 104 -12.29 -46.34 REMARK 500 ARG C 134 53.23 -93.15 REMARK 500 GLU C 222 -34.01 65.63 REMARK 500 ALA D 11 137.59 -20.74 REMARK 500 ALA D 12 -151.86 0.49 REMARK 500 ALA D 14 107.88 113.07 REMARK 500 GLN D 64 60.88 34.99 REMARK 500 SER D 96 -147.59 -119.05 REMARK 500 ARG D 104 22.60 -70.02 REMARK 500 GLU D 109 159.54 165.72 REMARK 500 ARG D 124 -4.12 -53.85 REMARK 500 THR D 135 -32.03 -149.70 REMARK 500 PRO D 181 -160.27 -53.74 REMARK 500 ARG D 210 128.21 -173.43 REMARK 500 GLU D 222 -10.87 70.27 REMARK 500 THR E 10 -165.16 -73.91 REMARK 500 SER E 16 -139.68 -64.40 REMARK 500 SER E 17 -69.86 -99.81 REMARK 500 PRO E 39 66.51 -45.13 REMARK 500 SER E 59 138.90 -176.03 REMARK 500 GLN E 64 52.55 35.47 REMARK 500 ASP E 74 -80.41 -43.39 REMARK 500 ALA E 92 27.57 -67.53 REMARK 500 GLU E 98 0.82 -57.71 REMARK 500 ARG E 99 -61.11 -90.14 REMARK 500 REMARK 500 THIS ENTRY HAS 123 RAMACHANDRAN OUTLIERS. 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 FNR B 501 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FNR A 502 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FNR D 503 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FNR C 504 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FNR F 505 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FNR E 506 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FNR H 507 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FNR G 508 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXY D 601 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXY B 602 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXY G 603 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXY H 604 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXY C 605 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXY A 606 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXY E 607 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXY F 608 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2ISJ RELATED DB: PDB REMARK 900 BLUB BOUND TO OXIDIZED FLAVIN (FMN). (YELLOW CRYSTAL FORM) REMARK 900 RELATED ID: 2ISK RELATED DB: PDB REMARK 900 BLUB BOUND TO REDUCED FLAVIN ANION. (PURPLE CRYSTAL FORM) DBREF 2ISL A 1 227 UNP Q92PC8 Q92PC8_RHIME 1 227 DBREF 2ISL B 1 227 UNP Q92PC8 Q92PC8_RHIME 1 227 DBREF 2ISL C 1 227 UNP Q92PC8 Q92PC8_RHIME 1 227 DBREF 2ISL D 1 227 UNP Q92PC8 Q92PC8_RHIME 1 227 DBREF 2ISL E 1 227 UNP Q92PC8 Q92PC8_RHIME 1 227 DBREF 2ISL F 1 227 UNP Q92PC8 Q92PC8_RHIME 1 227 DBREF 2ISL G 1 227 UNP Q92PC8 Q92PC8_RHIME 1 227 DBREF 2ISL H 1 227 UNP Q92PC8 Q92PC8_RHIME 1 227 SEQADV 2ISL GLY A -2 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISL SER A -1 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISL HIS A 0 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISL GLY B -2 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISL SER B -1 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISL HIS B 0 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISL GLY C -2 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISL SER C -1 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISL HIS C 0 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISL GLY D -2 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISL SER D -1 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISL HIS D 0 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISL GLY E -2 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISL SER E -1 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISL HIS E 0 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISL GLY F -2 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISL SER F -1 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISL HIS F 0 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISL GLY G -2 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISL SER G -1 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISL HIS G 0 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISL GLY H -2 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISL SER H -1 UNP Q92PC8 CLONING ARTIFACT SEQADV 2ISL HIS H 0 UNP Q92PC8 CLONING ARTIFACT SEQRES 1 A 230 GLY SER HIS MET LEU PRO ASP PRO ASN GLY CYS LEU THR SEQRES 2 A 230 ALA ALA GLY ALA PHE SER SER ASP GLU ARG ALA ALA VAL SEQRES 3 A 230 TYR ARG ALA ILE GLU THR ARG ARG ASP VAL ARG ASP GLU SEQRES 4 A 230 PHE LEU PRO GLU PRO LEU SER GLU GLU LEU ILE ALA ARG SEQRES 5 A 230 LEU LEU GLY ALA ALA HIS GLN ALA PRO SER VAL GLY PHE SEQRES 6 A 230 MET GLN PRO TRP ASN PHE VAL LEU VAL ARG GLN ASP GLU SEQRES 7 A 230 THR ARG GLU LYS VAL TRP GLN ALA PHE GLN ARG ALA ASN SEQRES 8 A 230 ASP GLU ALA ALA GLU MET PHE SER GLY GLU ARG GLN ALA SEQRES 9 A 230 LYS TYR ARG SER LEU LYS LEU GLU GLY ILE ARG LYS ALA SEQRES 10 A 230 PRO LEU SER ILE CYS VAL THR CYS ASP ARG THR ARG GLY SEQRES 11 A 230 GLY ALA VAL VAL LEU GLY ARG THR HIS ASN PRO GLN MET SEQRES 12 A 230 ASP LEU TYR SER THR VAL CYS ALA VAL GLN ASN LEU TRP SEQRES 13 A 230 LEU ALA ALA ARG ALA GLU GLY VAL GLY VAL GLY TRP VAL SEQRES 14 A 230 SER ILE PHE HIS GLU SER GLU ILE LYS ALA ILE LEU GLY SEQRES 15 A 230 ILE PRO ASP HIS VAL GLU ILE VAL ALA TRP LEU CYS LEU SEQRES 16 A 230 GLY PHE VAL ASP ARG LEU TYR GLN GLU PRO GLU LEU ALA SEQRES 17 A 230 ALA LYS GLY TRP ARG GLN ARG LEU PRO LEU GLU ASP LEU SEQRES 18 A 230 VAL PHE GLU GLU GLY TRP GLY VAL ARG SEQRES 1 B 230 GLY SER HIS MET LEU PRO ASP PRO ASN GLY CYS LEU THR SEQRES 2 B 230 ALA ALA GLY ALA PHE SER SER ASP GLU ARG ALA ALA VAL SEQRES 3 B 230 TYR ARG ALA ILE GLU THR ARG ARG ASP VAL ARG ASP GLU SEQRES 4 B 230 PHE LEU PRO GLU PRO LEU SER GLU GLU LEU ILE ALA ARG SEQRES 5 B 230 LEU LEU GLY ALA ALA HIS GLN ALA PRO SER VAL GLY PHE SEQRES 6 B 230 MET GLN PRO TRP ASN PHE VAL LEU VAL ARG GLN ASP GLU SEQRES 7 B 230 THR ARG GLU LYS VAL TRP GLN ALA PHE GLN ARG ALA ASN SEQRES 8 B 230 ASP GLU ALA ALA GLU MET PHE SER GLY GLU ARG GLN ALA SEQRES 9 B 230 LYS TYR ARG SER LEU LYS LEU GLU GLY ILE ARG LYS ALA SEQRES 10 B 230 PRO LEU SER ILE CYS VAL THR CYS ASP ARG THR ARG GLY SEQRES 11 B 230 GLY ALA VAL VAL LEU GLY ARG THR HIS ASN PRO GLN MET SEQRES 12 B 230 ASP LEU TYR SER THR VAL CYS ALA VAL GLN ASN LEU TRP SEQRES 13 B 230 LEU ALA ALA ARG ALA GLU GLY VAL GLY VAL GLY TRP VAL SEQRES 14 B 230 SER ILE PHE HIS GLU SER GLU ILE LYS ALA ILE LEU GLY SEQRES 15 B 230 ILE PRO ASP HIS VAL GLU ILE VAL ALA TRP LEU CYS LEU SEQRES 16 B 230 GLY PHE VAL ASP ARG LEU TYR GLN GLU PRO GLU LEU ALA SEQRES 17 B 230 ALA LYS GLY TRP ARG GLN ARG LEU PRO LEU GLU ASP LEU SEQRES 18 B 230 VAL PHE GLU GLU GLY TRP GLY VAL ARG SEQRES 1 C 230 GLY SER HIS MET LEU PRO ASP PRO ASN GLY CYS LEU THR SEQRES 2 C 230 ALA ALA GLY ALA PHE SER SER ASP GLU ARG ALA ALA VAL SEQRES 3 C 230 TYR ARG ALA ILE GLU THR ARG ARG ASP VAL ARG ASP GLU SEQRES 4 C 230 PHE LEU PRO GLU PRO LEU SER GLU GLU LEU ILE ALA ARG SEQRES 5 C 230 LEU LEU GLY ALA ALA HIS GLN ALA PRO SER VAL GLY PHE SEQRES 6 C 230 MET GLN PRO TRP ASN PHE VAL LEU VAL ARG GLN ASP GLU SEQRES 7 C 230 THR ARG GLU LYS VAL TRP GLN ALA PHE GLN ARG ALA ASN SEQRES 8 C 230 ASP GLU ALA ALA GLU MET PHE SER GLY GLU ARG GLN ALA SEQRES 9 C 230 LYS TYR ARG SER LEU LYS LEU GLU GLY ILE ARG LYS ALA SEQRES 10 C 230 PRO LEU SER ILE CYS VAL THR CYS ASP ARG THR ARG GLY SEQRES 11 C 230 GLY ALA VAL VAL LEU GLY ARG THR HIS ASN PRO GLN MET SEQRES 12 C 230 ASP LEU TYR SER THR VAL CYS ALA VAL GLN ASN LEU TRP SEQRES 13 C 230 LEU ALA ALA ARG ALA GLU GLY VAL GLY VAL GLY TRP VAL SEQRES 14 C 230 SER ILE PHE HIS GLU SER GLU ILE LYS ALA ILE LEU GLY SEQRES 15 C 230 ILE PRO ASP HIS VAL GLU ILE VAL ALA TRP LEU CYS LEU SEQRES 16 C 230 GLY PHE VAL ASP ARG LEU TYR GLN GLU PRO GLU LEU ALA SEQRES 17 C 230 ALA LYS GLY TRP ARG GLN ARG LEU PRO LEU GLU ASP LEU SEQRES 18 C 230 VAL PHE GLU GLU GLY TRP GLY VAL ARG SEQRES 1 D 230 GLY SER HIS MET LEU PRO ASP PRO ASN GLY CYS LEU THR SEQRES 2 D 230 ALA ALA GLY ALA PHE SER SER ASP GLU ARG ALA ALA VAL SEQRES 3 D 230 TYR ARG ALA ILE GLU THR ARG ARG ASP VAL ARG ASP GLU SEQRES 4 D 230 PHE LEU PRO GLU PRO LEU SER GLU GLU LEU ILE ALA ARG SEQRES 5 D 230 LEU LEU GLY ALA ALA HIS GLN ALA PRO SER VAL GLY PHE SEQRES 6 D 230 MET GLN PRO TRP ASN PHE VAL LEU VAL ARG GLN ASP GLU SEQRES 7 D 230 THR ARG GLU LYS VAL TRP GLN ALA PHE GLN ARG ALA ASN SEQRES 8 D 230 ASP GLU ALA ALA GLU MET PHE SER GLY GLU ARG GLN ALA SEQRES 9 D 230 LYS TYR ARG SER LEU LYS LEU GLU GLY ILE ARG LYS ALA SEQRES 10 D 230 PRO LEU SER ILE CYS VAL THR CYS ASP ARG THR ARG GLY SEQRES 11 D 230 GLY ALA VAL VAL LEU GLY ARG THR HIS ASN PRO GLN MET SEQRES 12 D 230 ASP LEU TYR SER THR VAL CYS ALA VAL GLN ASN LEU TRP SEQRES 13 D 230 LEU ALA ALA ARG ALA GLU GLY VAL GLY VAL GLY TRP VAL SEQRES 14 D 230 SER ILE PHE HIS GLU SER GLU ILE LYS ALA ILE LEU GLY SEQRES 15 D 230 ILE PRO ASP HIS VAL GLU ILE VAL ALA TRP LEU CYS LEU SEQRES 16 D 230 GLY PHE VAL ASP ARG LEU TYR GLN GLU PRO GLU LEU ALA SEQRES 17 D 230 ALA LYS GLY TRP ARG GLN ARG LEU PRO LEU GLU ASP LEU SEQRES 18 D 230 VAL PHE GLU GLU GLY TRP GLY VAL ARG SEQRES 1 E 230 GLY SER HIS MET LEU PRO ASP PRO ASN GLY CYS LEU THR SEQRES 2 E 230 ALA ALA GLY ALA PHE SER SER ASP GLU ARG ALA ALA VAL SEQRES 3 E 230 TYR ARG ALA ILE GLU THR ARG ARG ASP VAL ARG ASP GLU SEQRES 4 E 230 PHE LEU PRO GLU PRO LEU SER GLU GLU LEU ILE ALA ARG SEQRES 5 E 230 LEU LEU GLY ALA ALA HIS GLN ALA PRO SER VAL GLY PHE SEQRES 6 E 230 MET GLN PRO TRP ASN PHE VAL LEU VAL ARG GLN ASP GLU SEQRES 7 E 230 THR ARG GLU LYS VAL TRP GLN ALA PHE GLN ARG ALA ASN SEQRES 8 E 230 ASP GLU ALA ALA GLU MET PHE SER GLY GLU ARG GLN ALA SEQRES 9 E 230 LYS TYR ARG SER LEU LYS LEU GLU GLY ILE ARG LYS ALA SEQRES 10 E 230 PRO LEU SER ILE CYS VAL THR CYS ASP ARG THR ARG GLY SEQRES 11 E 230 GLY ALA VAL VAL LEU GLY ARG THR HIS ASN PRO GLN MET SEQRES 12 E 230 ASP LEU TYR SER THR VAL CYS ALA VAL GLN ASN LEU TRP SEQRES 13 E 230 LEU ALA ALA ARG ALA GLU GLY VAL GLY VAL GLY TRP VAL SEQRES 14 E 230 SER ILE PHE HIS GLU SER GLU ILE LYS ALA ILE LEU GLY SEQRES 15 E 230 ILE PRO ASP HIS VAL GLU ILE VAL ALA TRP LEU CYS LEU SEQRES 16 E 230 GLY PHE VAL ASP ARG LEU TYR GLN GLU PRO GLU LEU ALA SEQRES 17 E 230 ALA LYS GLY TRP ARG GLN ARG LEU PRO LEU GLU ASP LEU SEQRES 18 E 230 VAL PHE GLU GLU GLY TRP GLY VAL ARG SEQRES 1 F 230 GLY SER HIS MET LEU PRO ASP PRO ASN GLY CYS LEU THR SEQRES 2 F 230 ALA ALA GLY ALA PHE SER SER ASP GLU ARG ALA ALA VAL SEQRES 3 F 230 TYR ARG ALA ILE GLU THR ARG ARG ASP VAL ARG ASP GLU SEQRES 4 F 230 PHE LEU PRO GLU PRO LEU SER GLU GLU LEU ILE ALA ARG SEQRES 5 F 230 LEU LEU GLY ALA ALA HIS GLN ALA PRO SER VAL GLY PHE SEQRES 6 F 230 MET GLN PRO TRP ASN PHE VAL LEU VAL ARG GLN ASP GLU SEQRES 7 F 230 THR ARG GLU LYS VAL TRP GLN ALA PHE GLN ARG ALA ASN SEQRES 8 F 230 ASP GLU ALA ALA GLU MET PHE SER GLY GLU ARG GLN ALA SEQRES 9 F 230 LYS TYR ARG SER LEU LYS LEU GLU GLY ILE ARG LYS ALA SEQRES 10 F 230 PRO LEU SER ILE CYS VAL THR CYS ASP ARG THR ARG GLY SEQRES 11 F 230 GLY ALA VAL VAL LEU GLY ARG THR HIS ASN PRO GLN MET SEQRES 12 F 230 ASP LEU TYR SER THR VAL CYS ALA VAL GLN ASN LEU TRP SEQRES 13 F 230 LEU ALA ALA ARG ALA GLU GLY VAL GLY VAL GLY TRP VAL SEQRES 14 F 230 SER ILE PHE HIS GLU SER GLU ILE LYS ALA ILE LEU GLY SEQRES 15 F 230 ILE PRO ASP HIS VAL GLU ILE VAL ALA TRP LEU CYS LEU SEQRES 16 F 230 GLY PHE VAL ASP ARG LEU TYR GLN GLU PRO GLU LEU ALA SEQRES 17 F 230 ALA LYS GLY TRP ARG GLN ARG LEU PRO LEU GLU ASP LEU SEQRES 18 F 230 VAL PHE GLU GLU GLY TRP GLY VAL ARG SEQRES 1 G 230 GLY SER HIS MET LEU PRO ASP PRO ASN GLY CYS LEU THR SEQRES 2 G 230 ALA ALA GLY ALA PHE SER SER ASP GLU ARG ALA ALA VAL SEQRES 3 G 230 TYR ARG ALA ILE GLU THR ARG ARG ASP VAL ARG ASP GLU SEQRES 4 G 230 PHE LEU PRO GLU PRO LEU SER GLU GLU LEU ILE ALA ARG SEQRES 5 G 230 LEU LEU GLY ALA ALA HIS GLN ALA PRO SER VAL GLY PHE SEQRES 6 G 230 MET GLN PRO TRP ASN PHE VAL LEU VAL ARG GLN ASP GLU SEQRES 7 G 230 THR ARG GLU LYS VAL TRP GLN ALA PHE GLN ARG ALA ASN SEQRES 8 G 230 ASP GLU ALA ALA GLU MET PHE SER GLY GLU ARG GLN ALA SEQRES 9 G 230 LYS TYR ARG SER LEU LYS LEU GLU GLY ILE ARG LYS ALA SEQRES 10 G 230 PRO LEU SER ILE CYS VAL THR CYS ASP ARG THR ARG GLY SEQRES 11 G 230 GLY ALA VAL VAL LEU GLY ARG THR HIS ASN PRO GLN MET SEQRES 12 G 230 ASP LEU TYR SER THR VAL CYS ALA VAL GLN ASN LEU TRP SEQRES 13 G 230 LEU ALA ALA ARG ALA GLU GLY VAL GLY VAL GLY TRP VAL SEQRES 14 G 230 SER ILE PHE HIS GLU SER GLU ILE LYS ALA ILE LEU GLY SEQRES 15 G 230 ILE PRO ASP HIS VAL GLU ILE VAL ALA TRP LEU CYS LEU SEQRES 16 G 230 GLY PHE VAL ASP ARG LEU TYR GLN GLU PRO GLU LEU ALA SEQRES 17 G 230 ALA LYS GLY TRP ARG GLN ARG LEU PRO LEU GLU ASP LEU SEQRES 18 G 230 VAL PHE GLU GLU GLY TRP GLY VAL ARG SEQRES 1 H 230 GLY SER HIS MET LEU PRO ASP PRO ASN GLY CYS LEU THR SEQRES 2 H 230 ALA ALA GLY ALA PHE SER SER ASP GLU ARG ALA ALA VAL SEQRES 3 H 230 TYR ARG ALA ILE GLU THR ARG ARG ASP VAL ARG ASP GLU SEQRES 4 H 230 PHE LEU PRO GLU PRO LEU SER GLU GLU LEU ILE ALA ARG SEQRES 5 H 230 LEU LEU GLY ALA ALA HIS GLN ALA PRO SER VAL GLY PHE SEQRES 6 H 230 MET GLN PRO TRP ASN PHE VAL LEU VAL ARG GLN ASP GLU SEQRES 7 H 230 THR ARG GLU LYS VAL TRP GLN ALA PHE GLN ARG ALA ASN SEQRES 8 H 230 ASP GLU ALA ALA GLU MET PHE SER GLY GLU ARG GLN ALA SEQRES 9 H 230 LYS TYR ARG SER LEU LYS LEU GLU GLY ILE ARG LYS ALA SEQRES 10 H 230 PRO LEU SER ILE CYS VAL THR CYS ASP ARG THR ARG GLY SEQRES 11 H 230 GLY ALA VAL VAL LEU GLY ARG THR HIS ASN PRO GLN MET SEQRES 12 H 230 ASP LEU TYR SER THR VAL CYS ALA VAL GLN ASN LEU TRP SEQRES 13 H 230 LEU ALA ALA ARG ALA GLU GLY VAL GLY VAL GLY TRP VAL SEQRES 14 H 230 SER ILE PHE HIS GLU SER GLU ILE LYS ALA ILE LEU GLY SEQRES 15 H 230 ILE PRO ASP HIS VAL GLU ILE VAL ALA TRP LEU CYS LEU SEQRES 16 H 230 GLY PHE VAL ASP ARG LEU TYR GLN GLU PRO GLU LEU ALA SEQRES 17 H 230 ALA LYS GLY TRP ARG GLN ARG LEU PRO LEU GLU ASP LEU SEQRES 18 H 230 VAL PHE GLU GLU GLY TRP GLY VAL ARG HET FNR A 502 31 HET OXY A 606 2 HET FNR B 501 31 HET OXY B 602 2 HET FNR C 504 31 HET OXY C 605 2 HET FNR D 503 31 HET OXY D 601 2 HET FNR E 506 31 HET OXY E 607 2 HET FNR F 505 31 HET OXY F 608 2 HET FNR G 508 31 HET OXY G 603 2 HET FNR H 507 31 HET OXY H 604 2 HETNAM FNR 1-DEOXY-1-(7,8-DIMETHYL-2,4-DIOXO-3,4-DIHYDRO-2H- HETNAM 2 FNR BENZO[G]PTERIDIN-1-ID-10(5H)-YL)-5-O-PHOSPHONATO-D- HETNAM 3 FNR RIBITOL HETNAM OXY OXYGEN MOLECULE HETSYN FNR TWO ELECTRON REDUCED FLAVIN MONONUCLEOTIDE FORMUL 9 FNR 8(C17 H23 N4 O9 P) FORMUL 10 OXY 8(O2) FORMUL 25 HOH *63(H2 O) HELIX 1 1 SER A 16 ARG A 30 1 15 HELIX 2 2 SER A 43 GLN A 56 1 14 HELIX 3 3 SER A 59 MET A 63 5 5 HELIX 4 4 GLN A 73 GLU A 93 1 21 HELIX 5 5 MET A 94 SER A 96 5 3 HELIX 6 6 GLY A 97 ARG A 104 1 8 HELIX 7 7 GLN A 139 GLU A 159 1 21 HELIX 8 8 HIS A 170 GLY A 179 1 10 HELIX 9 9 PRO A 202 LYS A 207 1 6 HELIX 10 10 PRO A 214 ASP A 217 5 4 HELIX 11 11 SER B 16 ARG B 30 1 15 HELIX 12 12 SER B 43 HIS B 55 1 13 HELIX 13 13 SER B 59 MET B 63 5 5 HELIX 14 14 GLN B 73 GLU B 93 1 21 HELIX 15 15 SER B 96 ARG B 104 1 9 HELIX 16 16 GLN B 139 GLY B 160 1 22 HELIX 17 17 HIS B 170 GLY B 179 1 10 HELIX 18 18 PRO B 202 LYS B 207 1 6 HELIX 19 19 PRO B 214 ASP B 217 5 4 HELIX 20 20 SER C 16 ARG C 30 1 15 HELIX 21 21 SER C 43 GLN C 56 1 14 HELIX 22 22 SER C 59 MET C 63 5 5 HELIX 23 23 GLN C 73 GLU C 93 1 21 HELIX 24 24 GLY C 97 LEU C 106 1 10 HELIX 25 25 GLN C 139 GLU C 159 1 21 HELIX 26 26 HIS C 170 GLY C 179 1 10 HELIX 27 27 PRO C 202 LYS C 207 1 6 HELIX 28 28 PRO C 214 ASP C 217 5 4 HELIX 29 29 SER D 16 ARG D 30 1 15 HELIX 30 30 SER D 43 HIS D 55 1 13 HELIX 31 31 SER D 59 MET D 63 5 5 HELIX 32 32 GLN D 73 GLU D 93 1 21 HELIX 33 33 SER D 96 ARG D 104 1 9 HELIX 34 34 GLN D 139 GLU D 159 1 21 HELIX 35 35 HIS D 170 GLY D 179 1 10 HELIX 36 36 PRO D 202 LYS D 207 1 6 HELIX 37 37 PRO D 214 LEU D 218 1 5 HELIX 38 38 SER E 17 ARG E 30 1 14 HELIX 39 39 SER E 43 GLN E 56 1 14 HELIX 40 40 SER E 59 MET E 63 5 5 HELIX 41 41 GLN E 73 ALA E 92 1 20 HELIX 42 42 ARG E 99 ARG E 104 1 6 HELIX 43 43 GLN E 139 GLU E 159 1 21 HELIX 44 44 HIS E 170 GLY E 179 1 10 HELIX 45 45 PRO E 202 LYS E 207 1 6 HELIX 46 46 PRO E 214 ASP E 217 5 4 HELIX 47 47 SER F 16 ARG F 30 1 15 HELIX 48 48 SER F 43 GLN F 56 1 14 HELIX 49 49 SER F 59 MET F 63 5 5 HELIX 50 50 GLN F 73 GLU F 93 1 21 HELIX 51 51 GLU F 98 TYR F 103 1 6 HELIX 52 52 GLN F 139 GLU F 159 1 21 HELIX 53 53 HIS F 170 LEU F 178 1 9 HELIX 54 54 PRO F 202 LYS F 207 1 6 HELIX 55 55 PRO F 214 VAL F 219 1 6 HELIX 56 56 SER G 16 ARG G 30 1 15 HELIX 57 57 SER G 43 GLN G 56 1 14 HELIX 58 58 SER G 59 MET G 63 5 5 HELIX 59 59 GLN G 73 ALA G 92 1 20 HELIX 60 60 LYS G 102 LEU G 106 5 5 HELIX 61 61 GLN G 139 GLU G 159 1 21 HELIX 62 62 HIS G 170 GLY G 179 1 10 HELIX 63 63 PRO G 202 LYS G 207 1 6 HELIX 64 64 PRO G 214 ASP G 217 5 4 HELIX 65 65 SER H 16 ARG H 30 1 15 HELIX 66 66 SER H 43 GLN H 56 1 14 HELIX 67 67 SER H 59 MET H 63 5 5 HELIX 68 68 ASP H 74 GLU H 93 1 20 HELIX 69 69 SER H 96 LEU H 106 1 11 HELIX 70 70 GLN H 139 GLU H 159 1 21 HELIX 71 71 HIS H 170 LEU H 178 1 9 HELIX 72 72 PRO H 202 LYS H 207 1 6 HELIX 73 73 PRO H 214 VAL H 219 1 6 SHEET 1 A 5 VAL A 161 VAL A 166 0 SHEET 2 A 5 VAL A 184 PHE A 194 -1 O TRP A 189 N VAL A 166 SHEET 3 A 5 LEU A 116 ASP A 123 -1 N ILE A 118 O LEU A 190 SHEET 4 A 5 TRP A 66 VAL A 71 -1 N VAL A 71 O SER A 117 SHEET 5 A 5 VAL B 219 GLU B 221 1 O PHE B 220 N PHE A 68 SHEET 1 B 5 VAL A 219 GLU A 221 0 SHEET 2 B 5 TRP B 66 VAL B 71 1 O PHE B 68 N PHE A 220 SHEET 3 B 5 LEU B 116 ASP B 123 -1 O SER B 117 N VAL B 71 SHEET 4 B 5 VAL B 184 PHE B 194 -1 O GLU B 185 N CYS B 122 SHEET 5 B 5 VAL B 161 VAL B 166 -1 N GLY B 162 O GLY B 193 SHEET 1 C 2 THR C 10 ALA C 11 0 SHEET 2 C 2 ARG D 197 LEU D 198 -1 O LEU D 198 N THR C 10 SHEET 1 D 3 PHE C 37 LEU C 38 0 SHEET 2 D 3 VAL C 184 VAL C 195 -1 O PHE C 194 N LEU C 38 SHEET 3 D 3 VAL C 161 VAL C 166 -1 N GLY C 164 O CYS C 191 SHEET 1 E 5 PHE C 37 LEU C 38 0 SHEET 2 E 5 VAL C 184 VAL C 195 -1 O PHE C 194 N LEU C 38 SHEET 3 E 5 LEU C 116 ASP C 123 -1 N ILE C 118 O LEU C 190 SHEET 4 E 5 TRP C 66 VAL C 71 -1 N ASN C 67 O THR C 121 SHEET 5 E 5 VAL D 219 GLU D 221 1 O PHE D 220 N PHE C 68 SHEET 1 F 2 ARG C 197 LEU C 198 0 SHEET 2 F 2 THR D 10 ALA D 11 -1 O THR D 10 N LEU C 198 SHEET 1 G 5 VAL C 219 GLU C 221 0 SHEET 2 G 5 TRP D 66 VAL D 71 1 O PHE D 68 N PHE C 220 SHEET 3 G 5 LEU D 116 ASP D 123 -1 O SER D 117 N VAL D 71 SHEET 4 G 5 VAL D 184 PHE D 194 -1 O LEU D 192 N LEU D 116 SHEET 5 G 5 VAL D 161 VAL D 166 -1 N GLY D 162 O GLY D 193 SHEET 1 H 4 TRP E 66 ASN E 67 0 SHEET 2 H 4 LEU E 116 ASP E 123 -1 O THR E 121 N ASN E 67 SHEET 3 H 4 VAL E 184 PHE E 194 -1 O LEU E 192 N LEU E 116 SHEET 4 H 4 VAL E 161 VAL E 166 -1 N GLY E 162 O GLY E 193 SHEET 1 I 4 TRP E 66 ASN E 67 0 SHEET 2 I 4 LEU E 116 ASP E 123 -1 O THR E 121 N ASN E 67 SHEET 3 I 4 VAL E 69 VAL E 71 -1 N VAL E 71 O SER E 117 SHEET 4 I 4 PHE F 220 GLU F 221 1 O PHE F 220 N LEU E 70 SHEET 1 J 5 VAL E 219 GLU E 221 0 SHEET 2 J 5 TRP F 66 VAL F 71 1 O PHE F 68 N PHE E 220 SHEET 3 J 5 LEU F 116 ASP F 123 -1 O SER F 117 N VAL F 71 SHEET 4 J 5 VAL F 184 PHE F 194 -1 O LEU F 192 N LEU F 116 SHEET 5 J 5 VAL F 161 TRP F 165 -1 N GLY F 162 O GLY F 193 SHEET 1 K 4 TRP G 66 VAL G 71 0 SHEET 2 K 4 LEU G 116 ASP G 123 -1 O CYS G 119 N VAL G 69 SHEET 3 K 4 VAL G 184 PHE G 194 -1 O LEU G 192 N LEU G 116 SHEET 4 K 4 VAL G 161 VAL G 166 -1 N GLY G 162 O GLY G 193 SHEET 1 L 5 VAL G 219 GLU G 221 0 SHEET 2 L 5 TRP H 66 VAL H 71 1 O PHE H 68 N PHE G 220 SHEET 3 L 5 LEU H 116 ASP H 123 -1 O SER H 117 N VAL H 71 SHEET 4 L 5 VAL H 184 PHE H 194 -1 O LEU H 192 N LEU H 116 SHEET 5 L 5 VAL H 161 TRP H 165 -1 N GLY H 162 O GLY H 193 SITE 1 AC1 19 PRO A 58 SER A 59 VAL A 60 PHE A 62 SITE 2 AC1 19 MET A 140 SER A 144 OXY A 606 ARG B 30 SITE 3 AC1 19 ARG B 31 ASP B 32 ARG B 34 LEU B 108 SITE 4 AC1 19 TRP B 165 VAL B 166 SER B 167 ILE B 168 SITE 5 AC1 19 PRO B 202 LEU B 204 HOH B 516 SITE 1 AC2 18 ARG A 30 ARG A 31 ASP A 32 ARG A 34 SITE 2 AC2 18 LEU A 108 TRP A 165 VAL A 166 SER A 167 SITE 3 AC2 18 ILE A 168 PRO A 202 LEU A 204 HOH A 562 SITE 4 AC2 18 PRO B 58 SER B 59 VAL B 60 MET B 140 SITE 5 AC2 18 SER B 144 OXY B 602 SITE 1 AC3 18 PRO C 58 SER C 59 VAL C 60 PHE C 62 SITE 2 AC3 18 MET C 140 SER C 144 OXY C 605 ARG D 30 SITE 3 AC3 18 ARG D 31 ASP D 32 ARG D 34 LEU D 108 SITE 4 AC3 18 TRP D 165 VAL D 166 SER D 167 ILE D 168 SITE 5 AC3 18 PRO D 202 LEU D 204 SITE 1 AC4 16 ARG C 30 ARG C 31 ASP C 32 ARG C 34 SITE 2 AC4 16 LEU C 108 TRP C 165 VAL C 166 SER C 167 SITE 3 AC4 16 ILE C 168 LEU C 204 PRO D 58 SER D 59 SITE 4 AC4 16 VAL D 60 MET D 140 SER D 144 OXY D 601 SITE 1 AC5 19 PRO E 58 SER E 59 VAL E 60 PHE E 62 SITE 2 AC5 19 MET E 140 SER E 144 OXY E 607 ARG F 30 SITE 3 AC5 19 ARG F 31 ASP F 32 ARG F 34 LYS F 107 SITE 4 AC5 19 LEU F 108 TRP F 165 VAL F 166 SER F 167 SITE 5 AC5 19 ILE F 168 PRO F 202 LEU F 204 SITE 1 AC6 17 ARG E 30 ARG E 31 ASP E 32 ARG E 34 SITE 2 AC6 17 LEU E 108 TRP E 165 VAL E 166 SER E 167 SITE 3 AC6 17 PRO E 202 PRO F 58 SER F 59 VAL F 60 SITE 4 AC6 17 PHE F 62 MET F 140 TYR F 143 SER F 144 SITE 5 AC6 17 OXY F 608 SITE 1 AC7 18 PRO G 58 SER G 59 VAL G 60 PHE G 62 SITE 2 AC7 18 MET G 140 SER G 144 OXY G 603 ARG H 30 SITE 3 AC7 18 ARG H 31 ASP H 32 ARG H 34 LEU H 108 SITE 4 AC7 18 TRP H 165 VAL H 166 SER H 167 ILE H 168 SITE 5 AC7 18 PRO H 202 LEU H 204 SITE 1 AC8 18 ARG G 30 ARG G 31 ASP G 32 ARG G 34 SITE 2 AC8 18 LEU G 108 TRP G 165 VAL G 166 SER G 167 SITE 3 AC8 18 PRO G 202 LEU G 204 HOH G 564 PRO H 58 SITE 4 AC8 18 SER H 59 VAL H 60 PHE H 62 MET H 140 SITE 5 AC8 18 SER H 144 OXY H 604 SITE 1 AC9 4 FNR C 504 GLY D 61 LEU D 132 GLY D 133 SITE 1 BC1 3 FNR A 502 GLY B 61 LEU B 132 SITE 1 BC2 4 GLY G 61 LEU G 132 GLY G 133 FNR H 507 SITE 1 BC3 3 FNR G 508 GLY H 61 LEU H 132 SITE 1 BC4 3 GLY C 61 LEU C 132 FNR D 503 SITE 1 BC5 4 GLY A 61 LEU A 132 GLY A 133 FNR B 501 SITE 1 BC6 3 GLY E 61 LEU E 132 FNR F 505 SITE 1 BC7 4 LEU E 108 FNR E 506 GLY F 61 LEU F 132 CRYST1 65.073 173.836 91.977 90.00 89.96 90.00 P 1 21 1 16 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 0.015367 0.000000 -0.000011 0.00000 SCALE2 0.000000 0.005753 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010872 0.00000 (ATOM LINES ARE NOT SHOWN.) END