HEADER OXIDOREDUCTASE 08-JUL-03 1OJ9
TITLE HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH
TITLE 2 1,4-DIPHENYL-2-BUTENE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AMINE OXIDASE [FLAVIN-CONTAINING] B;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: MONOAMINE OXIDASE, MAO-B;
COMPND 5 EC: 1.4.3.4;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922
KEYWDS OXIDOREDUCTASE, FAD-CONTAINING AMINE OXIDASE, MAOB
EXPDTA X-RAY DIFFRACTION
AUTHOR C.BINDA,D.E.EDMONDSON,A.MATTEVI
REVDAT 3 24-FEB-09 1OJ9 1 VERSN
REVDAT 2 21-AUG-03 1OJ9 1 JRNL
REVDAT 1 15-AUG-03 1OJ9 0
JRNL AUTH C.BINDA,M.LI,F.HUBALEK,N.RESTELLI,D.E.EDMONDSON,
JRNL AUTH 2 A.MATTEVI
JRNL TITL INSIGHTS INTO THE MODE OF INHIBITION OF HUMAN
JRNL TITL 2 MITOCHONDRIAL MONOAMINE OXIDASE B FROM
JRNL TITL 3 HIGH-RESOLUTION CRYSTAL STRUCTURES
JRNL REF PROC.NATL.ACAD.SCI.USA V. 100 9750 2003
JRNL REFN ISSN 0027-8424
JRNL PMID 12913124
JRNL DOI 10.1073/PNAS.1633804100
REMARK 2
REMARK 2 RESOLUTION. 2.3 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.3
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.6
REMARK 3 NUMBER OF REFLECTIONS : 49954
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 + TEST SET) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.6
REMARK 3 FREE R VALUE TEST SET COUNT : 1326
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7911
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 138
REMARK 3 SOLVENT ATOMS : 230
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.632
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.44
REMARK 3 B22 (A**2) : -0.98
REMARK 3 B33 (A**2) : -1.46
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.341
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.234
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.150
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.155
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1OJ9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-JUL-03.
REMARK 100 THE PDBE ID CODE IS EBI-13009.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 302811
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.6
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.10700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.8000
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) : 2.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 66.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : 0.20200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 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 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z
REMARK 290 7555 -X+1/2,Y+1/2,-Z
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 66.05200
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 112.01100
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 66.05200
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 112.01100
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 66.05200
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 112.01100
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 66.05200
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 112.01100
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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: PQS
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 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 SER A 2
REMARK 465 PHE A 502
REMARK 465 SER A 503
REMARK 465 ALA A 504
REMARK 465 THR A 505
REMARK 465 ALA A 506
REMARK 465 LEU A 507
REMARK 465 GLY A 508
REMARK 465 PHE A 509
REMARK 465 LEU A 510
REMARK 465 ALA A 511
REMARK 465 HIS A 512
REMARK 465 LYS A 513
REMARK 465 ARG A 514
REMARK 465 GLY A 515
REMARK 465 LEU A 516
REMARK 465 LEU A 517
REMARK 465 VAL A 518
REMARK 465 ARG A 519
REMARK 465 VAL A 520
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 GLY B 497
REMARK 465 LEU B 498
REMARK 465 THR B 499
REMARK 465 THR B 500
REMARK 465 ILE B 501
REMARK 465 PHE B 502
REMARK 465 SER B 503
REMARK 465 ALA B 504
REMARK 465 THR B 505
REMARK 465 ALA B 506
REMARK 465 LEU B 507
REMARK 465 GLY B 508
REMARK 465 PHE B 509
REMARK 465 LEU B 510
REMARK 465 ALA B 511
REMARK 465 HIS B 512
REMARK 465 LYS B 513
REMARK 465 ARG B 514
REMARK 465 GLY B 515
REMARK 465 LEU B 516
REMARK 465 LEU B 517
REMARK 465 VAL B 518
REMARK 465 ARG B 519
REMARK 465 VAL B 520
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 ILE A 501 CG1 CG2 CD1
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 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PB A1503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B1497
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PB B1498
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GOS RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE B
REMARK 900 RELATED ID: 1H8R RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE TYPE B (TRUNCATED)
REMARK 900 RELATED ID: 1OJB RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH TRANYLCYPROMINE
REMARK 900 RELATED ID: 1OJA RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH ISATIN
REMARK 900 RELATED ID: 1OJC RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH
REMARK 900 2 N-(2-AMINOETHYL)-P-CHLOROBENZAMIDE
REMARK 900 RELATED ID: 1OJD RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH
REMARK 900 LAURYLDIMETHYLAMINE-N-OXIDE (LDAO)
DBREF 1OJ9 A 1 1 PDB 1OJ9 1OJ9 1 1
DBREF 1OJ9 A 2 520 UNP P27338 AOFB_HUMAN 1 519
DBREF 1OJ9 B 1 1 PDB 1OJ9 1OJ9 1 1
DBREF 1OJ9 B 2 520 UNP P27338 AOFB_HUMAN 1 519
SEQRES 1 A 520 MET SER ASN LYS CYS ASP VAL VAL VAL VAL GLY GLY GLY
SEQRES 2 A 520 ILE SER GLY MET ALA ALA ALA LYS LEU LEU HIS ASP SER
SEQRES 3 A 520 GLY LEU ASN VAL VAL VAL LEU GLU ALA ARG ASP ARG VAL
SEQRES 4 A 520 GLY GLY ARG THR TYR THR LEU ARG ASN GLN LYS VAL LYS
SEQRES 5 A 520 TYR VAL ASP LEU GLY GLY SER TYR VAL GLY PRO THR GLN
SEQRES 6 A 520 ASN ARG ILE LEU ARG LEU ALA LYS GLU LEU GLY LEU GLU
SEQRES 7 A 520 THR TYR LYS VAL ASN GLU VAL GLU ARG LEU ILE HIS HIS
SEQRES 8 A 520 VAL LYS GLY LYS SER TYR PRO PHE ARG GLY PRO PHE PRO
SEQRES 9 A 520 PRO VAL TRP ASN PRO ILE THR TYR LEU ASP HIS ASN ASN
SEQRES 10 A 520 PHE TRP ARG THR MET ASP ASP MET GLY ARG GLU ILE PRO
SEQRES 11 A 520 SER ASP ALA PRO TRP LYS ALA PRO LEU ALA GLU GLU TRP
SEQRES 12 A 520 ASP ASN MET THR MET LYS GLU LEU LEU ASP LYS LEU CYS
SEQRES 13 A 520 TRP THR GLU SER ALA LYS GLN LEU ALA THR LEU PHE VAL
SEQRES 14 A 520 ASN LEU CYS VAL THR ALA GLU THR HIS GLU VAL SER ALA
SEQRES 15 A 520 LEU TRP PHE LEU TRP TYR VAL LYS GLN CYS GLY GLY THR
SEQRES 16 A 520 THR ARG ILE ILE SER THR THR ASN GLY GLY GLN GLU ARG
SEQRES 17 A 520 LYS PHE VAL GLY GLY SER GLY GLN VAL SER GLU ARG ILE
SEQRES 18 A 520 MET ASP LEU LEU GLY ASP ARG VAL LYS LEU GLU ARG PRO
SEQRES 19 A 520 VAL ILE TYR ILE ASP GLN THR ARG GLU ASN VAL LEU VAL
SEQRES 20 A 520 GLU THR LEU ASN HIS GLU MET TYR GLU ALA LYS TYR VAL
SEQRES 21 A 520 ILE SER ALA ILE PRO PRO THR LEU GLY MET LYS ILE HIS
SEQRES 22 A 520 PHE ASN PRO PRO LEU PRO MET MET ARG ASN GLN MET ILE
SEQRES 23 A 520 THR ARG VAL PRO LEU GLY SER VAL ILE LYS CYS ILE VAL
SEQRES 24 A 520 TYR TYR LYS GLU PRO PHE TRP ARG LYS LYS ASP TYR CYS
SEQRES 25 A 520 GLY THR MET ILE ILE ASP GLY GLU GLU ALA PRO VAL ALA
SEQRES 26 A 520 TYR THR LEU ASP ASP THR LYS PRO GLU GLY ASN TYR ALA
SEQRES 27 A 520 ALA ILE MET GLY PHE ILE LEU ALA HIS LYS ALA ARG LYS
SEQRES 28 A 520 LEU ALA ARG LEU THR LYS GLU GLU ARG LEU LYS LYS LEU
SEQRES 29 A 520 CYS GLU LEU TYR ALA LYS VAL LEU GLY SER LEU GLU ALA
SEQRES 30 A 520 LEU GLU PRO VAL HIS TYR GLU GLU LYS ASN TRP CYS GLU
SEQRES 31 A 520 GLU GLN TYR SER GLY GLY CYS TYR THR THR TYR PHE PRO
SEQRES 32 A 520 PRO GLY ILE LEU THR GLN TYR GLY ARG VAL LEU ARG GLN
SEQRES 33 A 520 PRO VAL ASP ARG ILE TYR PHE ALA GLY THR GLU THR ALA
SEQRES 34 A 520 THR HIS TRP SER GLY TYR MET GLU GLY ALA VAL GLU ALA
SEQRES 35 A 520 GLY GLU ARG ALA ALA ARG GLU ILE LEU HIS ALA MET GLY
SEQRES 36 A 520 LYS ILE PRO GLU ASP GLU ILE TRP GLN SER GLU PRO GLU
SEQRES 37 A 520 SER VAL ASP VAL PRO ALA GLN PRO ILE THR THR THR PHE
SEQRES 38 A 520 LEU GLU ARG HIS LEU PRO SER VAL PRO GLY LEU LEU ARG
SEQRES 39 A 520 LEU ILE GLY LEU THR THR ILE PHE SER ALA THR ALA LEU
SEQRES 40 A 520 GLY PHE LEU ALA HIS LYS ARG GLY LEU LEU VAL ARG VAL
SEQRES 1 B 520 MET SER ASN LYS CYS ASP VAL VAL VAL VAL GLY GLY GLY
SEQRES 2 B 520 ILE SER GLY MET ALA ALA ALA LYS LEU LEU HIS ASP SER
SEQRES 3 B 520 GLY LEU ASN VAL VAL VAL LEU GLU ALA ARG ASP ARG VAL
SEQRES 4 B 520 GLY GLY ARG THR TYR THR LEU ARG ASN GLN LYS VAL LYS
SEQRES 5 B 520 TYR VAL ASP LEU GLY GLY SER TYR VAL GLY PRO THR GLN
SEQRES 6 B 520 ASN ARG ILE LEU ARG LEU ALA LYS GLU LEU GLY LEU GLU
SEQRES 7 B 520 THR TYR LYS VAL ASN GLU VAL GLU ARG LEU ILE HIS HIS
SEQRES 8 B 520 VAL LYS GLY LYS SER TYR PRO PHE ARG GLY PRO PHE PRO
SEQRES 9 B 520 PRO VAL TRP ASN PRO ILE THR TYR LEU ASP HIS ASN ASN
SEQRES 10 B 520 PHE TRP ARG THR MET ASP ASP MET GLY ARG GLU ILE PRO
SEQRES 11 B 520 SER ASP ALA PRO TRP LYS ALA PRO LEU ALA GLU GLU TRP
SEQRES 12 B 520 ASP ASN MET THR MET LYS GLU LEU LEU ASP LYS LEU CYS
SEQRES 13 B 520 TRP THR GLU SER ALA LYS GLN LEU ALA THR LEU PHE VAL
SEQRES 14 B 520 ASN LEU CYS VAL THR ALA GLU THR HIS GLU VAL SER ALA
SEQRES 15 B 520 LEU TRP PHE LEU TRP TYR VAL LYS GLN CYS GLY GLY THR
SEQRES 16 B 520 THR ARG ILE ILE SER THR THR ASN GLY GLY GLN GLU ARG
SEQRES 17 B 520 LYS PHE VAL GLY GLY SER GLY GLN VAL SER GLU ARG ILE
SEQRES 18 B 520 MET ASP LEU LEU GLY ASP ARG VAL LYS LEU GLU ARG PRO
SEQRES 19 B 520 VAL ILE TYR ILE ASP GLN THR ARG GLU ASN VAL LEU VAL
SEQRES 20 B 520 GLU THR LEU ASN HIS GLU MET TYR GLU ALA LYS TYR VAL
SEQRES 21 B 520 ILE SER ALA ILE PRO PRO THR LEU GLY MET LYS ILE HIS
SEQRES 22 B 520 PHE ASN PRO PRO LEU PRO MET MET ARG ASN GLN MET ILE
SEQRES 23 B 520 THR ARG VAL PRO LEU GLY SER VAL ILE LYS CYS ILE VAL
SEQRES 24 B 520 TYR TYR LYS GLU PRO PHE TRP ARG LYS LYS ASP TYR CYS
SEQRES 25 B 520 GLY THR MET ILE ILE ASP GLY GLU GLU ALA PRO VAL ALA
SEQRES 26 B 520 TYR THR LEU ASP ASP THR LYS PRO GLU GLY ASN TYR ALA
SEQRES 27 B 520 ALA ILE MET GLY PHE ILE LEU ALA HIS LYS ALA ARG LYS
SEQRES 28 B 520 LEU ALA ARG LEU THR LYS GLU GLU ARG LEU LYS LYS LEU
SEQRES 29 B 520 CYS GLU LEU TYR ALA LYS VAL LEU GLY SER LEU GLU ALA
SEQRES 30 B 520 LEU GLU PRO VAL HIS TYR GLU GLU LYS ASN TRP CYS GLU
SEQRES 31 B 520 GLU GLN TYR SER GLY GLY CYS TYR THR THR TYR PHE PRO
SEQRES 32 B 520 PRO GLY ILE LEU THR GLN TYR GLY ARG VAL LEU ARG GLN
SEQRES 33 B 520 PRO VAL ASP ARG ILE TYR PHE ALA GLY THR GLU THR ALA
SEQRES 34 B 520 THR HIS TRP SER GLY TYR MET GLU GLY ALA VAL GLU ALA
SEQRES 35 B 520 GLY GLU ARG ALA ALA ARG GLU ILE LEU HIS ALA MET GLY
SEQRES 36 B 520 LYS ILE PRO GLU ASP GLU ILE TRP GLN SER GLU PRO GLU
SEQRES 37 B 520 SER VAL ASP VAL PRO ALA GLN PRO ILE THR THR THR PHE
SEQRES 38 B 520 LEU GLU ARG HIS LEU PRO SER VAL PRO GLY LEU LEU ARG
SEQRES 39 B 520 LEU ILE GLY LEU THR THR ILE PHE SER ALA THR ALA LEU
SEQRES 40 B 520 GLY PHE LEU ALA HIS LYS ARG GLY LEU LEU VAL ARG VAL
HET FAD A1502 53
HET 1PB A1503 16
HET FAD B1497 53
HET 1PB B1498 16
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM 1PB 1,4-DIPHENYL-2-BUTENE
HETSYN 1PB [(1E)-4-PHENYLBUT-1-ENYL]BENZENE
FORMUL 3 FAD 2(C27 H33 N9 O15 P2)
FORMUL 4 1PB 2(C16 H16)
FORMUL 7 HOH *230(H2 O1)
HELIX 1 1 GLY A 13 SER A 26 1 14
HELIX 2 2 GLN A 65 LEU A 75 1 11
HELIX 3 3 ASN A 108 ARG A 127 1 20
HELIX 4 4 ALA A 133 ALA A 137 5 5
HELIX 5 5 LEU A 139 ASN A 145 1 7
HELIX 6 6 THR A 147 CYS A 156 1 10
HELIX 7 7 THR A 158 THR A 174 1 17
HELIX 8 8 SER A 181 GLN A 191 1 11
HELIX 9 9 GLY A 194 SER A 200 1 7
HELIX 10 10 GLY A 215 GLY A 226 1 12
HELIX 11 11 PRO A 265 ILE A 272 5 8
HELIX 12 12 PRO A 279 ILE A 286 1 8
HELIX 13 13 PRO A 304 LYS A 309 5 6
HELIX 14 14 ALA A 346 ALA A 353 1 8
HELIX 15 15 THR A 356 GLY A 373 1 18
HELIX 16 16 SER A 374 GLU A 379 5 6
HELIX 17 17 CYS A 389 GLU A 391 5 3
HELIX 18 18 GLY A 405 GLY A 411 1 7
HELIX 19 19 ARG A 412 LEU A 414 5 3
HELIX 20 20 GLY A 425 ALA A 429 5 5
HELIX 21 21 TYR A 435 MET A 454 1 20
HELIX 22 22 PRO A 458 ILE A 462 5 5
HELIX 23 23 THR A 480 LEU A 486 1 7
HELIX 24 24 SER A 488 THR A 500 1 13
HELIX 25 25 GLY B 13 SER B 26 1 14
HELIX 26 26 GLN B 65 LEU B 75 1 11
HELIX 27 27 ASN B 108 ARG B 127 1 20
HELIX 28 28 ALA B 133 ALA B 137 5 5
HELIX 29 29 LEU B 139 ASN B 145 1 7
HELIX 30 30 THR B 147 CYS B 156 1 10
HELIX 31 31 THR B 158 THR B 174 1 17
HELIX 32 32 SER B 181 GLN B 191 1 11
HELIX 33 33 GLY B 194 SER B 200 1 7
HELIX 34 34 GLY B 215 GLY B 226 1 12
HELIX 35 35 PRO B 265 ILE B 272 5 8
HELIX 36 36 PRO B 279 ILE B 286 1 8
HELIX 37 37 PRO B 304 LYS B 309 5 6
HELIX 38 38 ALA B 346 ALA B 353 1 8
HELIX 39 39 THR B 356 GLY B 373 1 18
HELIX 40 40 SER B 374 GLU B 379 5 6
HELIX 41 41 CYS B 389 GLU B 391 5 3
HELIX 42 42 GLY B 405 GLY B 411 1 7
HELIX 43 43 ARG B 412 LEU B 414 5 3
HELIX 44 44 GLY B 425 ALA B 429 5 5
HELIX 45 45 TYR B 435 MET B 454 1 20
HELIX 46 46 PRO B 458 ILE B 462 5 5
HELIX 47 47 THR B 480 LEU B 486 1 7
HELIX 48 48 SER B 488 ILE B 496 1 9
SHEET 1 AA 5 VAL A 229 LYS A 230 0
SHEET 2 AA 5 VAL A 30 LEU A 33 1 O VAL A 32 N LYS A 230
SHEET 3 AA 5 VAL A 7 VAL A 10 1 O VAL A 7 N VAL A 31
SHEET 4 AA 5 TYR A 259 SER A 262 1 O TYR A 259 N VAL A 8
SHEET 5 AA 5 ILE A 421 PHE A 423 1 O TYR A 422 N SER A 262
SHEET 1 AB 2 THR A 45 LEU A 46 0
SHEET 2 AB 2 VAL A 54 ASP A 55 -1 O VAL A 54 N LEU A 46
SHEET 1 AC 3 TYR A 60 VAL A 61 0
SHEET 2 AC 3 ARG A 208 PHE A 210 -1 O ARG A 208 N VAL A 61
SHEET 3 AC 3 THR A 79 LYS A 81 -1 O TYR A 80 N LYS A 209
SHEET 1 AD 7 LYS A 95 PHE A 99 0
SHEET 2 AD 7 ARG A 87 VAL A 92 -1 O LEU A 88 N PHE A 99
SHEET 3 AD 7 TYR A 311 ILE A 317 1 N CYS A 312 O ARG A 87
SHEET 4 AD 7 TYR A 326 ASP A 329 -1 O THR A 327 N MET A 315
SHEET 5 AD 7 ALA A 339 LEU A 345 -1 O MET A 341 N LEU A 328
SHEET 6 AD 7 VAL A 294 TYR A 300 -1 O ILE A 295 N ILE A 344
SHEET 7 AD 7 HIS A 382 ASN A 387 -1 O HIS A 382 N TYR A 300
SHEET 1 AE 4 MET A 254 ALA A 257 0
SHEET 2 AE 4 VAL A 245 THR A 249 -1 O VAL A 245 N ALA A 257
SHEET 3 AE 4 VAL A 235 ASP A 239 -1 N ILE A 236 O GLU A 248
SHEET 4 AE 4 HIS A 273 ASN A 275 1 O HIS A 273 N ILE A 238
SHEET 1 BA 5 VAL B 229 LYS B 230 0
SHEET 2 BA 5 VAL B 30 LEU B 33 1 O VAL B 32 N LYS B 230
SHEET 3 BA 5 VAL B 7 VAL B 10 1 O VAL B 7 N VAL B 31
SHEET 4 BA 5 TYR B 259 SER B 262 1 O TYR B 259 N VAL B 8
SHEET 5 BA 5 ILE B 421 PHE B 423 1 O TYR B 422 N SER B 262
SHEET 1 BB 2 THR B 45 LEU B 46 0
SHEET 2 BB 2 VAL B 54 ASP B 55 -1 O VAL B 54 N LEU B 46
SHEET 1 BC 3 TYR B 60 VAL B 61 0
SHEET 2 BC 3 ARG B 208 PHE B 210 -1 O ARG B 208 N VAL B 61
SHEET 3 BC 3 THR B 79 LYS B 81 -1 O TYR B 80 N LYS B 209
SHEET 1 BD 7 LYS B 95 PHE B 99 0
SHEET 2 BD 7 ARG B 87 VAL B 92 -1 O LEU B 88 N PHE B 99
SHEET 3 BD 7 TYR B 311 ILE B 317 1 N CYS B 312 O ARG B 87
SHEET 4 BD 7 TYR B 326 ASP B 329 -1 O THR B 327 N MET B 315
SHEET 5 BD 7 ALA B 339 LEU B 345 -1 O MET B 341 N LEU B 328
SHEET 6 BD 7 VAL B 294 TYR B 300 -1 O ILE B 295 N ILE B 344
SHEET 7 BD 7 HIS B 382 ASN B 387 -1 O HIS B 382 N TYR B 300
SHEET 1 BE 4 MET B 254 ALA B 257 0
SHEET 2 BE 4 VAL B 245 THR B 249 -1 O VAL B 245 N ALA B 257
SHEET 3 BE 4 VAL B 235 ASP B 239 -1 N ILE B 236 O GLU B 248
SHEET 4 BE 4 HIS B 273 ASN B 275 1 O HIS B 273 N ILE B 238
LINK SG CYS A 397 C8M FAD A1502 1555 1555 1.64
LINK SG CYS B 397 C8M FAD B1497 1555 1555 1.62
CISPEP 1 ASN A 275 PRO A 276 0 2.11
CISPEP 2 CYS A 397 TYR A 398 0 -0.75
CISPEP 3 ASN B 275 PRO B 276 0 2.70
CISPEP 4 CYS B 397 TYR B 398 0 0.55
SITE 1 AC1 39 VAL A 10 GLY A 11 GLY A 13 ILE A 14
SITE 2 AC1 39 SER A 15 LEU A 33 GLU A 34 ALA A 35
SITE 3 AC1 39 ARG A 36 GLY A 40 GLY A 41 ARG A 42
SITE 4 AC1 39 THR A 43 GLY A 57 GLY A 58 SER A 59
SITE 5 AC1 39 TYR A 60 PRO A 234 VAL A 235 ALA A 263
SITE 6 AC1 39 ILE A 264 TRP A 388 TYR A 393 CYS A 397
SITE 7 AC1 39 TYR A 398 GLY A 425 THR A 426 GLY A 434
SITE 8 AC1 39 TYR A 435 MET A 436 ALA A 439 HOH A2001
SITE 9 AC1 39 HOH A2009 HOH A2052 HOH A2096 HOH A2097
SITE 10 AC1 39 HOH A2098 HOH A2099 HOH A2100
SITE 1 AC2 3 LEU A 171 ILE A 199 GLN A 206
SITE 1 AC3 40 VAL B 10 GLY B 11 GLY B 13 ILE B 14
SITE 2 AC3 40 SER B 15 LEU B 33 GLU B 34 ALA B 35
SITE 3 AC3 40 ARG B 36 GLY B 40 GLY B 41 ARG B 42
SITE 4 AC3 40 THR B 43 GLY B 57 GLY B 58 SER B 59
SITE 5 AC3 40 TYR B 60 ARG B 233 PRO B 234 VAL B 235
SITE 6 AC3 40 ALA B 263 ILE B 264 TRP B 388 TYR B 393
SITE 7 AC3 40 CYS B 397 TYR B 398 GLY B 425 THR B 426
SITE 8 AC3 40 GLY B 434 TYR B 435 MET B 436 ALA B 439
SITE 9 AC3 40 HOH B2017 HOH B2074 HOH B2102 HOH B2126
SITE 10 AC3 40 HOH B2127 HOH B2128 HOH B2129 HOH B2130
SITE 1 AC4 3 LEU B 171 ILE B 199 GLN B 206
CRYST1 132.104 224.022 86.833 90.00 90.00 90.00 C 2 2 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 0.007570 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004464 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011516 0.00000
MTRIX1 1 -0.530150 -0.493700 -0.689350 140.08148 1
MTRIX2 1 -0.495400 -0.479440 0.724370 209.34830 1
MTRIX3 1 -0.688120 0.725530 0.009590 -54.66193 1
(ATOM LINES ARE NOT SHOWN.)
END