HEADER OXIDOREDUCTASE 07-MAR-03 1OQC
TITLE THE CRYSTAL STRUCTURE OF AUGMENTER OF LIVER REGENERATION: A MAMMALIAN
TITLE 2 FAD DEPENDENT SULFHYDRYL OXIDASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AUGMENTER OF LIVER REGENERATION;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: ALR;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: ALR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET16
KEYWDS SULFHYDRYL OXIDASE, LIVER REGENERATION, ALR, HELIX-TURN-HELIX,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.P.ROSE,C.-K.WU,B.-C.WANG
REVDAT 5 13-JUL-11 1OQC 1 VERSN
REVDAT 4 24-FEB-09 1OQC 1 VERSN
REVDAT 3 28-FEB-06 1OQC 1 REMARK
REVDAT 2 27-APR-04 1OQC 1 JRNL
REVDAT 1 15-APR-03 1OQC 0
JRNL AUTH C.-K.WU,T.A.DAILEY,H.A.DAILEY,B.-C.WANG,J.P.ROSE
JRNL TITL THE REFINED CRYSTAL STRUCTURE OF AUGMENTER OF LIVER
JRNL TITL 2 REGENERATION
JRNL REF INT.UNION CRYST.(MEETING) V. 1 293 1999
JRNL REFN ISSN 1067-0696
JRNL DOI 10.1109/ACC.1999.782787
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.-K.WU,T.A.DAILEY,H.A.DAILEY,B.C.WANG,J.P.ROSE
REMARK 1 TITL THE CRYSTAL STRUCTURE OF AUGMENTER OF LIVER REGENERATION: A
REMARK 1 TITL 2 MAMMALIAN FAD-DEPENDENT SULFHYDRYL OXIDASE
REMARK 1 REF PROTEIN SCI. V. 12 1109 2003
REMARK 1 REFN ISSN 0961-8368
REMARK 1 PMID 12717032
REMARK 1 DOI 10.1110/PS.0238103
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.-K.WU,T.DAILEY,H.DAILEY,A.FRANCAVILLA,T.E.STARZL,
REMARK 1 AUTH 2 B.-C.WANG,J.P.ROSE
REMARK 1 TITL EXPRESSION, PURIFICATION, CRYSTALLIZATION AND PRELIMINARY
REMARK 1 TITL 2 X-RAY ANALYSIS OF THE AUGMENTER OF LIVER REGENERATION
REMARK 1 REF PROTEIN PEPT.LETT. V. 7 25 2000
REMARK 1 REFN ISSN 0929-8665
REMARK 1 REFERENCE 3
REMARK 1 AUTH J.P.ROSE,C.-K.WU,A.FRANCAVILLA,J.G.PRELICH,A.IACOBELLIS,
REMARK 1 AUTH 2 M.HAGIYA,A.S.RAO,T.E.STARZL,B.C.WANG
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC DATA FOR
REMARK 1 TITL 2 THE AUGMENTER OF LIVER REGENERATION
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 53 331 1997
REMARK 1 REFN ISSN 0907-4449
REMARK 1 DOI 10.1107/S0907444996014084
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.65
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1754209.160
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 88.1
REMARK 3 NUMBER OF REFLECTIONS : 41788
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) : 0.202
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2100
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 74.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5503
REMARK 3 BIN R VALUE (WORKING SET) : 0.2110
REMARK 3 BIN FREE R VALUE : 0.2680
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 279
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.016
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3728
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 212
REMARK 3 SOLVENT ATOMS : 623
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.94000
REMARK 3 B22 (A**2) : -1.47000
REMARK 3 B33 (A**2) : 0.53000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.19
REMARK 3 ESD FROM SIGMAA (A) : 0.08
REMARK 3 LOW RESOLUTION CUTOFF (A) : 6.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.14
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.50
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 18.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.32
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 : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 44.19
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.PARAM
REMARK 3 PARAMETER FILE 3 : FAD.PAR
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : FAD.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1OQC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAR-03.
REMARK 100 THE RCSB ID CODE IS RCSB018560.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-SEP-98; 25-JUN-98
REMARK 200 TEMPERATURE (KELVIN) : 120; 120
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : NSLS; APS
REMARK 200 BEAMLINE : X12C; 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95, 0.979, 0.978; 0.979
REMARK 200 MONOCHROMATOR : GRAPHITE CRYSTAL; GRAPHITE
REMARK 200 CRYSTAL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : CUSTOM-MADE; SIEMENS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, SAINT
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, SAINT
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41788
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 27.650
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 76.5
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 40.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.02
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.17300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.880
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: PHASING DATA (SE-MAD) WERE COLLECTED ON X12C, NSLS TO 2.5
REMARK 200 ANGSTROMS. REFINEMENT DATA WERE COLLECTED ON 17ID, APS TO 1.5
REMARK 200 ANGSTROMS.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, MAGNESIUM CHLORIDE, PH 6.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 300K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 53.49350
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 61.56500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 53.49350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 61.56500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: DISULFIDE LINKED HOMO DIMER
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 5740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 5580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 MET A 1
REMARK 465 ARG A 2
REMARK 465 THR A 3
REMARK 465 GLN A 4
REMARK 465 GLN A 5
REMARK 465 LYS A 6
REMARK 465 ARG A 7
REMARK 465 ASP A 8
REMARK 465 ILE A 9
REMARK 465 LYS A 10
REMARK 465 PHE A 11
REMARK 465 ARG A 12
REMARK 465 ASP A 125
REMARK 465 MET B 1
REMARK 465 ARG B 2
REMARK 465 THR B 3
REMARK 465 GLN B 4
REMARK 465 GLN B 5
REMARK 465 LYS B 6
REMARK 465 ARG B 7
REMARK 465 ASP B 8
REMARK 465 ILE B 9
REMARK 465 LYS B 10
REMARK 465 PHE B 11
REMARK 465 ARG B 12
REMARK 465 GLU B 13
REMARK 465 ASP B 125
REMARK 465 MET C 1
REMARK 465 ARG C 2
REMARK 465 THR C 3
REMARK 465 GLN C 4
REMARK 465 GLN C 5
REMARK 465 LYS C 6
REMARK 465 ARG C 7
REMARK 465 ASP C 8
REMARK 465 ILE C 9
REMARK 465 LYS C 10
REMARK 465 PHE C 11
REMARK 465 ARG C 12
REMARK 465 ASP C 125
REMARK 465 MET D 1
REMARK 465 ARG D 2
REMARK 465 THR D 3
REMARK 465 GLN D 4
REMARK 465 GLN D 5
REMARK 465 LYS D 6
REMARK 465 ARG D 7
REMARK 465 ASP D 8
REMARK 465 ILE D 9
REMARK 465 LYS D 10
REMARK 465 PHE D 11
REMARK 465 ARG D 12
REMARK 465 ASP D 125
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 LYS A 120 CG CD CE NZ
REMARK 470 SER A 123 OG
REMARK 470 GLU C 13 CB CG CD OE1 OE2
REMARK 470 GLU D 13 CB CG CD OE1 OE2
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 PRO B 61 C - N - CA ANGL. DEV. = 11.0 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 PRO A 61 -14.81 -41.21
REMARK 500 ARG A 116 -58.50 -132.03
REMARK 500 PRO B 61 13.91 -52.35
REMARK 500 ARG B 116 -56.23 -126.54
REMARK 500 ASP C 14 -8.66 -149.38
REMARK 500 MET C 40 63.11 -119.74
REMARK 500 CYS C 62 108.85 -58.26
REMARK 500 ARG C 116 -55.42 -131.33
REMARK 500 CYS D 62 109.29 -57.19
REMARK 500 ARG D 116 -62.18 -124.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 273 DISTANCE = 5.20 ANGSTROMS
REMARK 525 HOH D 273 DISTANCE = 5.29 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CTA
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: PUTATIVE CATALYTIC SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: CTB
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: PUTATIVE CATALYTIC SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: CTC
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: PUTATIVE CATALYTIC SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: CTD
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: PUTATIVE CATALYTIC SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 126
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 126
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD C 126
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD D 126
DBREF 1OQC A 1 125 UNP Q63042 ALR_RAT 1 125
DBREF 1OQC B 1 125 UNP Q63042 ALR_RAT 1 125
DBREF 1OQC C 1 125 UNP Q63042 ALR_RAT 1 125
DBREF 1OQC D 1 125 UNP Q63042 ALR_RAT 1 125
SEQRES 1 A 125 MET ARG THR GLN GLN LYS ARG ASP ILE LYS PHE ARG GLU
SEQRES 2 A 125 ASP CYS PRO GLN ASP ARG GLU GLU LEU GLY ARG ASN THR
SEQRES 3 A 125 TRP ALA PHE LEU HIS THR LEU ALA ALA TYR TYR PRO ASP
SEQRES 4 A 125 MET PRO THR PRO GLU GLN GLN GLN ASP MET ALA GLN PHE
SEQRES 5 A 125 ILE HIS ILE PHE SER LYS PHE TYR PRO CYS GLU GLU CYS
SEQRES 6 A 125 ALA GLU ASP ILE ARG LYS ARG ILE ASP ARG SER GLN PRO
SEQRES 7 A 125 ASP THR SER THR ARG VAL SER PHE SER GLN TRP LEU CYS
SEQRES 8 A 125 ARG LEU HIS ASN GLU VAL ASN ARG LYS LEU GLY LYS PRO
SEQRES 9 A 125 ASP PHE ASP CYS SER ARG VAL ASP GLU ARG TRP ARG ASP
SEQRES 10 A 125 GLY TRP LYS ASP GLY SER CYS ASP
SEQRES 1 B 125 MET ARG THR GLN GLN LYS ARG ASP ILE LYS PHE ARG GLU
SEQRES 2 B 125 ASP CYS PRO GLN ASP ARG GLU GLU LEU GLY ARG ASN THR
SEQRES 3 B 125 TRP ALA PHE LEU HIS THR LEU ALA ALA TYR TYR PRO ASP
SEQRES 4 B 125 MET PRO THR PRO GLU GLN GLN GLN ASP MET ALA GLN PHE
SEQRES 5 B 125 ILE HIS ILE PHE SER LYS PHE TYR PRO CYS GLU GLU CYS
SEQRES 6 B 125 ALA GLU ASP ILE ARG LYS ARG ILE ASP ARG SER GLN PRO
SEQRES 7 B 125 ASP THR SER THR ARG VAL SER PHE SER GLN TRP LEU CYS
SEQRES 8 B 125 ARG LEU HIS ASN GLU VAL ASN ARG LYS LEU GLY LYS PRO
SEQRES 9 B 125 ASP PHE ASP CYS SER ARG VAL ASP GLU ARG TRP ARG ASP
SEQRES 10 B 125 GLY TRP LYS ASP GLY SER CYS ASP
SEQRES 1 C 125 MET ARG THR GLN GLN LYS ARG ASP ILE LYS PHE ARG GLU
SEQRES 2 C 125 ASP CYS PRO GLN ASP ARG GLU GLU LEU GLY ARG ASN THR
SEQRES 3 C 125 TRP ALA PHE LEU HIS THR LEU ALA ALA TYR TYR PRO ASP
SEQRES 4 C 125 MET PRO THR PRO GLU GLN GLN GLN ASP MET ALA GLN PHE
SEQRES 5 C 125 ILE HIS ILE PHE SER LYS PHE TYR PRO CYS GLU GLU CYS
SEQRES 6 C 125 ALA GLU ASP ILE ARG LYS ARG ILE ASP ARG SER GLN PRO
SEQRES 7 C 125 ASP THR SER THR ARG VAL SER PHE SER GLN TRP LEU CYS
SEQRES 8 C 125 ARG LEU HIS ASN GLU VAL ASN ARG LYS LEU GLY LYS PRO
SEQRES 9 C 125 ASP PHE ASP CYS SER ARG VAL ASP GLU ARG TRP ARG ASP
SEQRES 10 C 125 GLY TRP LYS ASP GLY SER CYS ASP
SEQRES 1 D 125 MET ARG THR GLN GLN LYS ARG ASP ILE LYS PHE ARG GLU
SEQRES 2 D 125 ASP CYS PRO GLN ASP ARG GLU GLU LEU GLY ARG ASN THR
SEQRES 3 D 125 TRP ALA PHE LEU HIS THR LEU ALA ALA TYR TYR PRO ASP
SEQRES 4 D 125 MET PRO THR PRO GLU GLN GLN GLN ASP MET ALA GLN PHE
SEQRES 5 D 125 ILE HIS ILE PHE SER LYS PHE TYR PRO CYS GLU GLU CYS
SEQRES 6 D 125 ALA GLU ASP ILE ARG LYS ARG ILE ASP ARG SER GLN PRO
SEQRES 7 D 125 ASP THR SER THR ARG VAL SER PHE SER GLN TRP LEU CYS
SEQRES 8 D 125 ARG LEU HIS ASN GLU VAL ASN ARG LYS LEU GLY LYS PRO
SEQRES 9 D 125 ASP PHE ASP CYS SER ARG VAL ASP GLU ARG TRP ARG ASP
SEQRES 10 D 125 GLY TRP LYS ASP GLY SER CYS ASP
HET FAD A 126 53
HET FAD B 126 53
HET FAD C 126 53
HET FAD D 126 53
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
FORMUL 5 FAD 4(C27 H33 N9 O15 P2)
FORMUL 9 HOH *623(H2 O)
HELIX 1 1 ASP A 18 TYR A 36 1 19
HELIX 2 2 THR A 42 TYR A 60 1 19
HELIX 3 3 CYS A 62 SER A 76 1 15
HELIX 4 4 THR A 82 LEU A 101 1 20
HELIX 5 5 ASP A 107 SER A 109 5 3
HELIX 6 6 ARG A 110 ARG A 116 1 7
HELIX 7 7 ASP B 18 TYR B 36 1 19
HELIX 8 8 THR B 42 TYR B 60 1 19
HELIX 9 9 CYS B 62 SER B 76 1 15
HELIX 10 10 THR B 82 LEU B 101 1 20
HELIX 11 11 ASP B 107 SER B 109 5 3
HELIX 12 12 ARG B 110 ARG B 116 1 7
HELIX 13 13 ASP C 18 TYR C 36 1 19
HELIX 14 14 THR C 42 TYR C 60 1 19
HELIX 15 15 CYS C 62 SER C 76 1 15
HELIX 16 16 THR C 82 LEU C 101 1 20
HELIX 17 17 ASP C 107 SER C 109 5 3
HELIX 18 18 ARG C 110 ARG C 116 1 7
HELIX 19 19 ASP D 18 TYR D 36 1 19
HELIX 20 20 THR D 42 TYR D 60 1 19
HELIX 21 21 CYS D 62 SER D 76 1 15
HELIX 22 22 THR D 82 LEU D 101 1 20
HELIX 23 23 ASP D 107 SER D 109 5 3
HELIX 24 24 ARG D 110 ARG D 116 1 7
SSBOND 1 CYS A 15 CYS C 124 1555 1555 2.02
SSBOND 2 CYS A 62 CYS A 65 1555 1555 2.03
SSBOND 3 CYS A 91 CYS A 108 1555 1555 2.03
SSBOND 4 CYS A 124 CYS C 15 1555 1555 2.03
SSBOND 5 CYS B 15 CYS D 124 1555 1555 2.03
SSBOND 6 CYS B 62 CYS B 65 1555 1555 2.03
SSBOND 7 CYS B 91 CYS B 108 1555 1555 2.03
SSBOND 8 CYS B 124 CYS D 15 1555 1555 2.03
SSBOND 9 CYS C 62 CYS C 65 1555 1555 2.03
SSBOND 10 CYS C 91 CYS C 108 1555 1555 2.03
SSBOND 11 CYS D 62 CYS D 65 1555 1555 2.03
SSBOND 12 CYS D 91 CYS D 108 1555 1555 2.03
SITE 1 CTA 3 CYS A 62 CYS A 65 FAD A 126
SITE 1 CTB 3 CYS B 62 CYS B 65 FAD B 126
SITE 1 CTC 3 CYS C 62 CYS C 65 FAD C 126
SITE 1 CTD 3 CYS D 62 CYS D 65 FAD D 126
SITE 1 AC1 30 ARG A 19 GLU A 20 GLY A 23 ARG A 24
SITE 2 AC1 30 TRP A 27 HIS A 31 PHE A 56 TYR A 60
SITE 3 AC1 30 CYS A 65 ILE A 69 CYS A 91 HIS A 94
SITE 4 AC1 30 ASN A 95 VAL A 97 ASN A 98 LYS A 100
SITE 5 AC1 30 LEU A 101 LYS A 103 PHE A 106 ARG A 114
SITE 6 AC1 30 TRP A 115 HOH A 131 HOH A 148 HOH A 150
SITE 7 AC1 30 HOH A 165 HOH A 195 HOH A 201 HOH A 203
SITE 8 AC1 30 HOH A 252 HOH A 266
SITE 1 AC2 29 ARG B 19 GLU B 20 GLY B 23 ARG B 24
SITE 2 AC2 29 TRP B 27 HIS B 31 PHE B 56 TYR B 60
SITE 3 AC2 29 CYS B 65 CYS B 91 HIS B 94 ASN B 95
SITE 4 AC2 29 VAL B 97 ASN B 98 LYS B 100 LEU B 101
SITE 5 AC2 29 LYS B 103 PHE B 106 ARG B 114 TRP B 115
SITE 6 AC2 29 HOH B 135 HOH B 152 HOH B 167 HOH B 174
SITE 7 AC2 29 HOH B 192 HOH B 198 HOH B 215 HOH B 232
SITE 8 AC2 29 HOH B 276
SITE 1 AC3 29 ARG C 19 GLU C 20 GLY C 23 ARG C 24
SITE 2 AC3 29 TRP C 27 HIS C 31 PHE C 56 TYR C 60
SITE 3 AC3 29 CYS C 65 ILE C 69 CYS C 91 HIS C 94
SITE 4 AC3 29 ASN C 95 VAL C 97 ASN C 98 LYS C 100
SITE 5 AC3 29 LEU C 101 LYS C 103 PHE C 106 ARG C 114
SITE 6 AC3 29 TRP C 115 HOH C 139 HOH C 162 HOH C 179
SITE 7 AC3 29 HOH C 185 HOH C 189 HOH C 233 HOH C 263
SITE 8 AC3 29 HOH C 274
SITE 1 AC4 32 ARG D 19 GLU D 20 GLY D 23 ARG D 24
SITE 2 AC4 32 TRP D 27 HIS D 31 PHE D 56 TYR D 60
SITE 3 AC4 32 CYS D 65 ASP D 68 ILE D 69 CYS D 91
SITE 4 AC4 32 HIS D 94 ASN D 95 VAL D 97 ASN D 98
SITE 5 AC4 32 LYS D 100 LEU D 101 LYS D 103 PHE D 106
SITE 6 AC4 32 ARG D 114 TRP D 115 HOH D 144 HOH D 148
SITE 7 AC4 32 HOH D 159 HOH D 162 HOH D 164 HOH D 183
SITE 8 AC4 32 HOH D 187 HOH D 193 HOH D 261 HOH D 269
CRYST1 106.987 123.130 37.930 90.00 90.00 90.00 P 21 21 2 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 0.009347 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008121 0.000000 0.00000
SCALE3 0.000000 0.000000 0.026364 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
