HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 15-JUN-11 3SGZ
TITLE HIGH RESOLUTION CRYSTAL STRUCTURE OF RAT LONG CHAIN HYDROXY ACID
TITLE 2 OXIDASE IN COMPLEX WITH THE INHIBITOR 4-CARBOXY-5-[(4-CHIOROPHENYL)
TITLE 3 SULFANYL]-1, 2, 3-THIADIAZOLE.
CAVEAT 3SGZ C-N BOND DISTANCE OUTSIDE OF THE NORMAL RANGE FOR RESIDUE
CAVEAT 2 3SGZ 142 GLN AND 143 ARG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYDROXYACID OXIDASE 2;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: HAOX2, (S)-2-HYDROXY-ACID OXIDASE, PEROXISOMAL, LONG CHAIN
COMPND 5 ALPHA-HYDROXY ACID OXIDASE, LONG-CHAIN L-2-HYDROXY ACID OXIDASE;
COMPND 6 EC: 1.1.3.15;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: HAO2, HAO3, HAOX2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FLAVOPROTEIN, HOMOLOGY, LONG CHAIN HYDROXY ACID OXIDASE, INHIBITOR,
KEYWDS 2 OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.CHEN,C.VIGNAUD,A.JAAFAR,F.GUERITTE,D.GUENARD,F.LEDERER,F.S.MATHEWS
REVDAT 3 13-SEP-23 3SGZ 1 REMARK SEQADV
REVDAT 2 25-APR-12 3SGZ 1 JRNL
REVDAT 1 07-MAR-12 3SGZ 0
JRNL AUTH Z.W.CHEN,C.VIGNAUD,A.JAAFAR,B.LEVY,F.GUERITTE,D.GUENARD,
JRNL AUTH 2 F.LEDERER,F.S.MATHEWS
JRNL TITL HIGH RESOLUTION CRYSTAL STRUCTURE OF RAT LONG CHAIN HYDROXY
JRNL TITL 2 ACID OXIDASE IN COMPLEX WITH THE INHIBITOR
JRNL TITL 3 4-CARBOXY-5-[(4-CHLOROPHENYL)SULFANYL]-1, 2, 3-THIADIAZOLE.
JRNL TITL 4 IMPLICATIONS FOR INHIBITOR SPECIFICITY AND DRUG DESIGN.
JRNL REF BIOCHIMIE V. 94 1172 2012
JRNL REFN ISSN 0300-9084
JRNL PMID 22342614
JRNL DOI 10.1016/J.BIOCHI.2012.02.003
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.M.CUNANE,J.D.BARTON,Z.CHEN,K.H.DIEP LE,F.LEDERER,
REMARK 1 AUTH 2 F.S.MATHEWS
REMARK 1 TITL CRYSTAL STRUCTURE ANALYSIS OF RECOMBINANT RAT KIDNEY
REMARK 1 TITL 2 LONG-CHAIN HYDROXY ACID OXIDASE
REMARK 1 REF BIOCHEMISTRY V. 44 1521 2005
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. 1.35 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) : 1.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.91
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 342133.650
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 311329
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) : 0.185
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 15480
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.002
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.43
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 45811
REMARK 3 BIN R VALUE (WORKING SET) : 0.2890
REMARK 3 BIN FREE R VALUE : 0.2940
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 2373
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.006
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7814
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 141
REMARK 3 SOLVENT ATOMS : 1104
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.15
REMARK 3 ESD FROM SIGMAA (A) : 0.17
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.16
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.18
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.013
REMARK 3 BOND ANGLES (DEGREES) : 1.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.230
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3SGZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUN-11.
REMARK 100 THE DEPOSITION ID IS D_1000066189.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-AUG-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 14-BM-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
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 : 311329
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.350
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 11.20
REMARK 200 R MERGE (I) : 0.08700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : 0.33400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP FROM CCP4
REMARK 200 STARTING MODEL: PDB ENTRY 1TB3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.8M NACL AND 100 MM BIS-TRIS, PH 6.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 11555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 12555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 13555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 14555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 15555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 16555 -Y+1/2,-X+1/2,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 54.22500
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 54.22500
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 245.83850
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 54.22500
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 54.22500
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 245.83850
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 54.22500
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 54.22500
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 245.83850
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 54.22500
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 54.22500
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 245.83850
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 54.22500
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 54.22500
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 245.83850
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 54.22500
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 54.22500
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 245.83850
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 54.22500
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 54.22500
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 245.83850
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 54.22500
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 54.22500
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 245.83850
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 47660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 BIOMT1 2 -1.000000 0.000000 0.000000 108.45000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 -108.45000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 -108.45000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 108.45000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 47450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -60.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 -108.45000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 -108.45000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 -108.45000
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 -108.45000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 35080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 89950 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -164.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 5 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 6 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 7 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 7 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 34910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 88900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -151.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 BIOMT1 2 -1.000000 0.000000 0.000000 108.45000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 -108.45000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 -108.45000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 108.45000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 5 1.000000 0.000000 0.000000 108.45000
REMARK 350 BIOMT2 5 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 6 0.000000 -1.000000 0.000000 -108.45000
REMARK 350 BIOMT3 6 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 7 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 7 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 7 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 8 0.000000 1.000000 0.000000 108.45000
REMARK 350 BIOMT2 8 -1.000000 0.000000 0.000000 -108.45000
REMARK 350 BIOMT3 8 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 LEU A 183
REMARK 465 ARG A 184
REMARK 465 ALA A 185
REMARK 465 LEU A 186
REMARK 465 LYS A 187
REMARK 465 GLU A 188
REMARK 465 GLU A 189
REMARK 465 LYS A 190
REMARK 465 PRO A 191
REMARK 465 THR A 192
REMARK 465 GLN A 193
REMARK 465 SER A 194
REMARK 465 VAL A 195
REMARK 465 PRO A 196
REMARK 465 VAL A 197
REMARK 465 LEU A 352
REMARK 465 LEU B 183
REMARK 465 ARG B 184
REMARK 465 ALA B 185
REMARK 465 LEU B 186
REMARK 465 LYS B 187
REMARK 465 GLU B 188
REMARK 465 GLU B 189
REMARK 465 LYS B 190
REMARK 465 PRO B 191
REMARK 465 THR B 192
REMARK 465 GLN B 193
REMARK 465 SER B 194
REMARK 465 VAL B 195
REMARK 465 PRO B 196
REMARK 465 VAL B 197
REMARK 465 SER B 350
REMARK 465 ARG B 351
REMARK 465 LEU B 352
REMARK 465 LEU C 183
REMARK 465 ARG C 184
REMARK 465 ALA C 185
REMARK 465 LEU C 186
REMARK 465 LYS C 187
REMARK 465 GLU C 188
REMARK 465 GLU C 189
REMARK 465 LYS C 190
REMARK 465 PRO C 191
REMARK 465 THR C 192
REMARK 465 GLN C 193
REMARK 465 SER C 194
REMARK 465 VAL C 195
REMARK 465 PRO C 196
REMARK 465 VAL C 197
REMARK 465 LEU C 352
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LEU A 198 CG CD1 CD2
REMARK 470 LEU B 198 CG CD1 CD2
REMARK 470 PRO B 200 CG CD
REMARK 470 LEU C 198 CG CD1 CD2
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 PRO C 344 CB ARG C 351 2.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLN A 142 C ARG A 143 N -0.154
REMARK 500 GLN B 142 C ARG B 143 N -0.278
REMARK 500 GLN C 142 C ARG C 143 N -0.214
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 PHE A 199 C - N - CA ANGL. DEV. = 16.9 DEGREES
REMARK 500 PHE A 199 N - CA - CB ANGL. DEV. = -12.9 DEGREES
REMARK 500 PHE A 199 N - CA - C ANGL. DEV. = 26.8 DEGREES
REMARK 500 PRO A 200 C - N - CA ANGL. DEV. = 18.1 DEGREES
REMARK 500 LYS A 201 N - CA - C ANGL. DEV. = 22.7 DEGREES
REMARK 500 SER A 350 N - CA - C ANGL. DEV. = -28.8 DEGREES
REMARK 500 ARG B 164 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 PRO C 200 C - N - CD ANGL. DEV. = -13.5 DEGREES
REMARK 500 LYS C 201 C - N - CA ANGL. DEV. = 15.7 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 GLU A 25 -70.86 -69.24
REMARK 500 ASP A 29 -122.62 48.02
REMARK 500 ALA A 119 74.77 -152.58
REMARK 500 ALA A 181 -68.04 -102.16
REMARK 500 PHE A 199 -98.41 -69.64
REMARK 500 PRO A 200 38.54 -150.98
REMARK 500 LYS A 201 56.00 -52.41
REMARK 500 GLN A 251 -112.88 -114.11
REMARK 500 LYS A 311 21.70 -150.10
REMARK 500 PHE A 349 96.20 19.43
REMARK 500 SER A 350 -130.77 161.68
REMARK 500 ASP B 29 -123.70 48.49
REMARK 500 ALA B 119 75.88 -153.44
REMARK 500 GLN B 251 -115.60 -113.47
REMARK 500 LYS B 311 24.67 -150.53
REMARK 500 ASP C 29 -123.44 48.94
REMARK 500 ALA C 119 73.29 -154.16
REMARK 500 PHE C 199 -107.06 -70.75
REMARK 500 LYS C 201 -84.04 -66.00
REMARK 500 ALA C 202 -19.04 66.76
REMARK 500 GLN C 251 -112.89 -115.64
REMARK 500 LYS C 311 23.19 -148.26
REMARK 500 PHE C 349 93.66 22.68
REMARK 500 SER C 350 -33.73 154.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PHE C 199 PRO C 200 -72.29
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 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HO6 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HO6 B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HO6 C 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TB3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF RECOMBINANT RAT KIDNEY LONG-CHAIN
REMARK 900 HYDROXY ACID OXIDASE
DBREF 3SGZ A 1 352 UNP Q07523 HAOX2_RAT 2 353
DBREF 3SGZ B 1 352 UNP Q07523 HAOX2_RAT 2 353
DBREF 3SGZ C 1 352 UNP Q07523 HAOX2_RAT 2 353
SEQADV 3SGZ LYS A 180 UNP Q07523 LEU 181 CONFLICT
SEQADV 3SGZ ALA A 181 UNP Q07523 LYS 182 CONFLICT
SEQADV 3SGZ ALA A 182 UNP Q07523 ASP 183 CONFLICT
SEQADV 3SGZ LEU A 198 UNP Q07523 SER 199 CONFLICT
SEQADV 3SGZ LYS B 180 UNP Q07523 LEU 181 CONFLICT
SEQADV 3SGZ ALA B 181 UNP Q07523 LYS 182 CONFLICT
SEQADV 3SGZ ALA B 182 UNP Q07523 ASP 183 CONFLICT
SEQADV 3SGZ LEU B 198 UNP Q07523 SER 199 CONFLICT
SEQADV 3SGZ LYS C 180 UNP Q07523 LEU 181 CONFLICT
SEQADV 3SGZ ALA C 181 UNP Q07523 LYS 182 CONFLICT
SEQADV 3SGZ ALA C 182 UNP Q07523 ASP 183 CONFLICT
SEQADV 3SGZ LEU C 198 UNP Q07523 SER 199 CONFLICT
SEQRES 1 A 352 PRO LEU VAL CYS LEU ALA ASP PHE LYS ALA HIS ALA GLN
SEQRES 2 A 352 LYS GLN LEU SER LYS THR SER TRP ASP PHE ILE GLU GLY
SEQRES 3 A 352 GLU ALA ASP ASP GLY ILE THR TYR SER GLU ASN ILE ALA
SEQRES 4 A 352 ALA PHE LYS ARG ILE ARG LEU ARG PRO ARG TYR LEU ARG
SEQRES 5 A 352 ASP MET SER LYS VAL ASP THR ARG THR THR ILE GLN GLY
SEQRES 6 A 352 GLN GLU ILE SER ALA PRO ILE CYS ILE SER PRO THR ALA
SEQRES 7 A 352 PHE HIS SER ILE ALA TRP PRO ASP GLY GLU LYS SER THR
SEQRES 8 A 352 ALA ARG ALA ALA GLN GLU ALA ASN ILE CYS TYR VAL ILE
SEQRES 9 A 352 SER SER TYR ALA SER TYR SER LEU GLU ASP ILE VAL ALA
SEQRES 10 A 352 ALA ALA PRO GLU GLY PHE ARG TRP PHE GLN LEU TYR MET
SEQRES 11 A 352 LYS SER ASP TRP ASP PHE ASN LYS GLN MET VAL GLN ARG
SEQRES 12 A 352 ALA GLU ALA LEU GLY PHE LYS ALA LEU VAL ILE THR ILE
SEQRES 13 A 352 ASP THR PRO VAL LEU GLY ASN ARG ARG ARG ASP LYS ARG
SEQRES 14 A 352 ASN GLN LEU ASN LEU GLU ALA ASN ILE LEU LYS ALA ALA
SEQRES 15 A 352 LEU ARG ALA LEU LYS GLU GLU LYS PRO THR GLN SER VAL
SEQRES 16 A 352 PRO VAL LEU PHE PRO LYS ALA SER PHE CYS TRP ASN ASP
SEQRES 17 A 352 LEU SER LEU LEU GLN SER ILE THR ARG LEU PRO ILE ILE
SEQRES 18 A 352 LEU LYS GLY ILE LEU THR LYS GLU ASP ALA GLU LEU ALA
SEQRES 19 A 352 MET LYS HIS ASN VAL GLN GLY ILE VAL VAL SER ASN HIS
SEQRES 20 A 352 GLY GLY ARG GLN LEU ASP GLU VAL SER ALA SER ILE ASP
SEQRES 21 A 352 ALA LEU ARG GLU VAL VAL ALA ALA VAL LYS GLY LYS ILE
SEQRES 22 A 352 GLU VAL TYR MET ASP GLY GLY VAL ARG THR GLY THR ASP
SEQRES 23 A 352 VAL LEU LYS ALA LEU ALA LEU GLY ALA ARG CYS ILE PHE
SEQRES 24 A 352 LEU GLY ARG PRO ILE LEU TRP GLY LEU ALA CYS LYS GLY
SEQRES 25 A 352 GLU ASP GLY VAL LYS GLU VAL LEU ASP ILE LEU THR ALA
SEQRES 26 A 352 GLU LEU HIS ARG CYS MET THR LEU SER GLY CYS GLN SER
SEQRES 27 A 352 VAL ALA GLU ILE SER PRO ASP LEU ILE GLN PHE SER ARG
SEQRES 28 A 352 LEU
SEQRES 1 B 352 PRO LEU VAL CYS LEU ALA ASP PHE LYS ALA HIS ALA GLN
SEQRES 2 B 352 LYS GLN LEU SER LYS THR SER TRP ASP PHE ILE GLU GLY
SEQRES 3 B 352 GLU ALA ASP ASP GLY ILE THR TYR SER GLU ASN ILE ALA
SEQRES 4 B 352 ALA PHE LYS ARG ILE ARG LEU ARG PRO ARG TYR LEU ARG
SEQRES 5 B 352 ASP MET SER LYS VAL ASP THR ARG THR THR ILE GLN GLY
SEQRES 6 B 352 GLN GLU ILE SER ALA PRO ILE CYS ILE SER PRO THR ALA
SEQRES 7 B 352 PHE HIS SER ILE ALA TRP PRO ASP GLY GLU LYS SER THR
SEQRES 8 B 352 ALA ARG ALA ALA GLN GLU ALA ASN ILE CYS TYR VAL ILE
SEQRES 9 B 352 SER SER TYR ALA SER TYR SER LEU GLU ASP ILE VAL ALA
SEQRES 10 B 352 ALA ALA PRO GLU GLY PHE ARG TRP PHE GLN LEU TYR MET
SEQRES 11 B 352 LYS SER ASP TRP ASP PHE ASN LYS GLN MET VAL GLN ARG
SEQRES 12 B 352 ALA GLU ALA LEU GLY PHE LYS ALA LEU VAL ILE THR ILE
SEQRES 13 B 352 ASP THR PRO VAL LEU GLY ASN ARG ARG ARG ASP LYS ARG
SEQRES 14 B 352 ASN GLN LEU ASN LEU GLU ALA ASN ILE LEU LYS ALA ALA
SEQRES 15 B 352 LEU ARG ALA LEU LYS GLU GLU LYS PRO THR GLN SER VAL
SEQRES 16 B 352 PRO VAL LEU PHE PRO LYS ALA SER PHE CYS TRP ASN ASP
SEQRES 17 B 352 LEU SER LEU LEU GLN SER ILE THR ARG LEU PRO ILE ILE
SEQRES 18 B 352 LEU LYS GLY ILE LEU THR LYS GLU ASP ALA GLU LEU ALA
SEQRES 19 B 352 MET LYS HIS ASN VAL GLN GLY ILE VAL VAL SER ASN HIS
SEQRES 20 B 352 GLY GLY ARG GLN LEU ASP GLU VAL SER ALA SER ILE ASP
SEQRES 21 B 352 ALA LEU ARG GLU VAL VAL ALA ALA VAL LYS GLY LYS ILE
SEQRES 22 B 352 GLU VAL TYR MET ASP GLY GLY VAL ARG THR GLY THR ASP
SEQRES 23 B 352 VAL LEU LYS ALA LEU ALA LEU GLY ALA ARG CYS ILE PHE
SEQRES 24 B 352 LEU GLY ARG PRO ILE LEU TRP GLY LEU ALA CYS LYS GLY
SEQRES 25 B 352 GLU ASP GLY VAL LYS GLU VAL LEU ASP ILE LEU THR ALA
SEQRES 26 B 352 GLU LEU HIS ARG CYS MET THR LEU SER GLY CYS GLN SER
SEQRES 27 B 352 VAL ALA GLU ILE SER PRO ASP LEU ILE GLN PHE SER ARG
SEQRES 28 B 352 LEU
SEQRES 1 C 352 PRO LEU VAL CYS LEU ALA ASP PHE LYS ALA HIS ALA GLN
SEQRES 2 C 352 LYS GLN LEU SER LYS THR SER TRP ASP PHE ILE GLU GLY
SEQRES 3 C 352 GLU ALA ASP ASP GLY ILE THR TYR SER GLU ASN ILE ALA
SEQRES 4 C 352 ALA PHE LYS ARG ILE ARG LEU ARG PRO ARG TYR LEU ARG
SEQRES 5 C 352 ASP MET SER LYS VAL ASP THR ARG THR THR ILE GLN GLY
SEQRES 6 C 352 GLN GLU ILE SER ALA PRO ILE CYS ILE SER PRO THR ALA
SEQRES 7 C 352 PHE HIS SER ILE ALA TRP PRO ASP GLY GLU LYS SER THR
SEQRES 8 C 352 ALA ARG ALA ALA GLN GLU ALA ASN ILE CYS TYR VAL ILE
SEQRES 9 C 352 SER SER TYR ALA SER TYR SER LEU GLU ASP ILE VAL ALA
SEQRES 10 C 352 ALA ALA PRO GLU GLY PHE ARG TRP PHE GLN LEU TYR MET
SEQRES 11 C 352 LYS SER ASP TRP ASP PHE ASN LYS GLN MET VAL GLN ARG
SEQRES 12 C 352 ALA GLU ALA LEU GLY PHE LYS ALA LEU VAL ILE THR ILE
SEQRES 13 C 352 ASP THR PRO VAL LEU GLY ASN ARG ARG ARG ASP LYS ARG
SEQRES 14 C 352 ASN GLN LEU ASN LEU GLU ALA ASN ILE LEU LYS ALA ALA
SEQRES 15 C 352 LEU ARG ALA LEU LYS GLU GLU LYS PRO THR GLN SER VAL
SEQRES 16 C 352 PRO VAL LEU PHE PRO LYS ALA SER PHE CYS TRP ASN ASP
SEQRES 17 C 352 LEU SER LEU LEU GLN SER ILE THR ARG LEU PRO ILE ILE
SEQRES 18 C 352 LEU LYS GLY ILE LEU THR LYS GLU ASP ALA GLU LEU ALA
SEQRES 19 C 352 MET LYS HIS ASN VAL GLN GLY ILE VAL VAL SER ASN HIS
SEQRES 20 C 352 GLY GLY ARG GLN LEU ASP GLU VAL SER ALA SER ILE ASP
SEQRES 21 C 352 ALA LEU ARG GLU VAL VAL ALA ALA VAL LYS GLY LYS ILE
SEQRES 22 C 352 GLU VAL TYR MET ASP GLY GLY VAL ARG THR GLY THR ASP
SEQRES 23 C 352 VAL LEU LYS ALA LEU ALA LEU GLY ALA ARG CYS ILE PHE
SEQRES 24 C 352 LEU GLY ARG PRO ILE LEU TRP GLY LEU ALA CYS LYS GLY
SEQRES 25 C 352 GLU ASP GLY VAL LYS GLU VAL LEU ASP ILE LEU THR ALA
SEQRES 26 C 352 GLU LEU HIS ARG CYS MET THR LEU SER GLY CYS GLN SER
SEQRES 27 C 352 VAL ALA GLU ILE SER PRO ASP LEU ILE GLN PHE SER ARG
SEQRES 28 C 352 LEU
HET FMN A 401 31
HET HO6 A 402 16
HET FMN B 401 31
HET HO6 B 402 16
HET FMN C 401 31
HET HO6 C 402 16
HETNAM FMN FLAVIN MONONUCLEOTIDE
HETNAM HO6 5-[(4-METHYLPHENYL)SULFANYL]-1,2,3-THIADIAZOLE-4-
HETNAM 2 HO6 CARBOXYLIC ACID
HETSYN FMN RIBOFLAVIN MONOPHOSPHATE
HETSYN HO6 4-CARBOXY-5-[(4-CHLOROPHENYL)SULFANYL]-1, 2, 3-
HETSYN 2 HO6 THIADIAZOLE
FORMUL 4 FMN 3(C17 H21 N4 O9 P)
FORMUL 5 HO6 3(C10 H8 N2 O2 S2)
FORMUL 10 HOH *1104(H2 O)
HELIX 1 1 CYS A 4 GLN A 15 1 12
HELIX 2 2 SER A 17 GLY A 26 1 10
HELIX 3 3 GLY A 31 ARG A 43 1 13
HELIX 4 4 PHE A 79 ALA A 83 5 5
HELIX 5 5 ASP A 86 ASN A 99 1 14
HELIX 6 6 SER A 111 ALA A 119 1 9
HELIX 7 7 ASP A 133 LEU A 147 1 15
HELIX 8 8 ARG A 164 LEU A 174 1 11
HELIX 9 9 GLU A 175 LYS A 180 1 6
HELIX 10 10 CYS A 205 THR A 216 1 12
HELIX 11 11 THR A 227 HIS A 237 1 11
HELIX 12 12 ASN A 246 ARG A 250 5 5
HELIX 13 13 ALA A 257 LYS A 270 1 14
HELIX 14 14 THR A 283 LEU A 293 1 11
HELIX 15 15 GLY A 301 GLY A 335 1 35
HELIX 16 16 SER A 338 ILE A 342 5 5
HELIX 17 17 SER A 343 ILE A 347 5 5
HELIX 18 18 CYS B 4 LEU B 16 1 13
HELIX 19 19 SER B 17 GLY B 26 1 10
HELIX 20 20 GLY B 31 ILE B 44 1 14
HELIX 21 21 PHE B 79 ALA B 83 5 5
HELIX 22 22 ASP B 86 ASN B 99 1 14
HELIX 23 23 SER B 111 ALA B 119 1 9
HELIX 24 24 ASP B 133 LEU B 147 1 15
HELIX 25 25 ARG B 164 LEU B 174 1 11
HELIX 26 26 GLU B 175 LYS B 180 1 6
HELIX 27 27 CYS B 205 THR B 216 1 12
HELIX 28 28 THR B 227 HIS B 237 1 11
HELIX 29 29 ASN B 246 ARG B 250 5 5
HELIX 30 30 ALA B 257 LYS B 270 1 14
HELIX 31 31 THR B 283 LEU B 293 1 11
HELIX 32 32 GLY B 301 GLY B 335 1 35
HELIX 33 33 SER B 338 ILE B 342 5 5
HELIX 34 34 SER B 343 ILE B 347 5 5
HELIX 35 35 CYS C 4 LEU C 16 1 13
HELIX 36 36 SER C 17 GLY C 26 1 10
HELIX 37 37 GLY C 31 ARG C 43 1 13
HELIX 38 38 PHE C 79 ALA C 83 5 5
HELIX 39 39 ASP C 86 ASN C 99 1 14
HELIX 40 40 SER C 111 ALA C 119 1 9
HELIX 41 41 ASP C 133 LEU C 147 1 15
HELIX 42 42 ARG C 164 LEU C 174 1 11
HELIX 43 43 GLU C 175 LYS C 180 1 6
HELIX 44 44 CYS C 205 ASN C 207 5 3
HELIX 45 45 ASP C 208 THR C 216 1 9
HELIX 46 46 THR C 227 HIS C 237 1 11
HELIX 47 47 ASN C 246 ARG C 250 5 5
HELIX 48 48 ALA C 257 LYS C 270 1 14
HELIX 49 49 THR C 283 LEU C 293 1 11
HELIX 50 50 GLY C 301 GLY C 335 1 35
HELIX 51 51 SER C 338 ILE C 342 5 5
HELIX 52 52 SER C 343 ILE C 347 5 5
SHEET 1 A 2 THR A 61 ILE A 63 0
SHEET 2 A 2 GLN A 66 ILE A 68 -1 O ILE A 68 N THR A 61
SHEET 1 B 9 ILE A 72 ILE A 74 0
SHEET 2 B 9 CYS A 101 ILE A 104 1 O CYS A 101 N ILE A 74
SHEET 3 B 9 PHE A 123 GLN A 127 1 O GLN A 127 N ILE A 104
SHEET 4 B 9 LEU A 152 THR A 155 1 O VAL A 153 N PHE A 126
SHEET 5 B 9 ILE A 220 ILE A 225 1 O LYS A 223 N ILE A 154
SHEET 6 B 9 GLY A 241 VAL A 244 1 O VAL A 243 N LEU A 222
SHEET 7 B 9 GLU A 274 ASP A 278 1 O TYR A 276 N ILE A 242
SHEET 8 B 9 CYS A 297 LEU A 300 1 O PHE A 299 N MET A 277
SHEET 9 B 9 ILE A 72 ILE A 74 1 N CYS A 73 O ILE A 298
SHEET 1 C 2 THR B 61 ILE B 63 0
SHEET 2 C 2 GLN B 66 ILE B 68 -1 O ILE B 68 N THR B 61
SHEET 1 D 9 ILE B 72 ILE B 74 0
SHEET 2 D 9 CYS B 101 ILE B 104 1 O CYS B 101 N ILE B 74
SHEET 3 D 9 PHE B 123 GLN B 127 1 O GLN B 127 N ILE B 104
SHEET 4 D 9 LEU B 152 THR B 155 1 O VAL B 153 N PHE B 126
SHEET 5 D 9 ILE B 220 ILE B 225 1 O LYS B 223 N ILE B 154
SHEET 6 D 9 GLY B 241 VAL B 244 1 O VAL B 243 N LEU B 222
SHEET 7 D 9 GLU B 274 ASP B 278 1 O TYR B 276 N ILE B 242
SHEET 8 D 9 ILE B 298 LEU B 300 1 O PHE B 299 N MET B 277
SHEET 9 D 9 ILE B 72 ILE B 74 1 N CYS B 73 O LEU B 300
SHEET 1 E 2 THR C 61 ILE C 63 0
SHEET 2 E 2 GLN C 66 ILE C 68 -1 O ILE C 68 N THR C 61
SHEET 1 F 9 ILE C 72 ILE C 74 0
SHEET 2 F 9 CYS C 101 ILE C 104 1 O CYS C 101 N ILE C 74
SHEET 3 F 9 PHE C 123 GLN C 127 1 O GLN C 127 N ILE C 104
SHEET 4 F 9 LEU C 152 THR C 155 1 O VAL C 153 N PHE C 126
SHEET 5 F 9 ILE C 220 ILE C 225 1 O ILE C 221 N LEU C 152
SHEET 6 F 9 GLY C 241 VAL C 244 1 O VAL C 243 N LEU C 222
SHEET 7 F 9 GLU C 274 ASP C 278 1 O TYR C 276 N ILE C 242
SHEET 8 F 9 ILE C 298 LEU C 300 1 O PHE C 299 N MET C 277
SHEET 9 F 9 ILE C 72 ILE C 74 1 N CYS C 73 O ILE C 298
CISPEP 1 PHE A 199 PRO A 200 0 0.22
SITE 1 AC1 26 PHE A 23 ILE A 24 SER A 75 PRO A 76
SITE 2 AC1 26 THR A 77 ALA A 78 SER A 105 GLN A 127
SITE 3 AC1 26 TYR A 129 THR A 155 LYS A 223 SER A 245
SITE 4 AC1 26 HIS A 247 GLY A 248 ARG A 250 ASP A 278
SITE 5 AC1 26 GLY A 279 GLY A 280 ARG A 282 GLY A 301
SITE 6 AC1 26 ARG A 302 PRO A 303 LEU A 305 HO6 A 402
SITE 7 AC1 26 HOH A 503 HOH A 504
SITE 1 AC2 9 PHE A 23 PHE A 79 TYR A 107 TYR A 129
SITE 2 AC2 9 ARG A 164 LEU A 198 HIS A 247 ARG A 250
SITE 3 AC2 9 FMN A 401
SITE 1 AC3 26 PHE B 23 ILE B 24 SER B 75 PRO B 76
SITE 2 AC3 26 THR B 77 ALA B 78 SER B 105 GLN B 127
SITE 3 AC3 26 TYR B 129 THR B 155 LYS B 223 SER B 245
SITE 4 AC3 26 HIS B 247 GLY B 248 ARG B 250 ASP B 278
SITE 5 AC3 26 GLY B 279 GLY B 280 ARG B 282 GLY B 301
SITE 6 AC3 26 ARG B 302 PRO B 303 LEU B 305 HO6 B 402
SITE 7 AC3 26 HOH B 503 HOH B 509
SITE 1 AC4 11 PHE B 23 PHE B 79 TYR B 107 TYR B 129
SITE 2 AC4 11 LEU B 161 ARG B 164 LEU B 198 PHE B 199
SITE 3 AC4 11 HIS B 247 ARG B 250 FMN B 401
SITE 1 AC5 26 PHE C 23 ILE C 24 SER C 75 PRO C 76
SITE 2 AC5 26 THR C 77 ALA C 78 SER C 105 GLN C 127
SITE 3 AC5 26 TYR C 129 THR C 155 LYS C 223 SER C 245
SITE 4 AC5 26 HIS C 247 GLY C 248 ARG C 250 ASP C 278
SITE 5 AC5 26 GLY C 279 GLY C 280 ARG C 282 GLY C 301
SITE 6 AC5 26 ARG C 302 PRO C 303 LEU C 305 HO6 C 402
SITE 7 AC5 26 HOH C1002 HOH C1006
SITE 1 AC6 9 PHE C 23 PHE C 79 TYR C 107 TYR C 129
SITE 2 AC6 9 ARG C 164 LEU C 198 HIS C 247 ARG C 250
SITE 3 AC6 9 FMN C 401
CRYST1 108.450 108.450 491.677 90.00 90.00 90.00 I 4 2 2 48
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 0.009221 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009221 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002034 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
