HEADER OXIDOREDUCTASE 29-AUG-11 3ZYX
TITLE CRYSTAL STRUCTURE OF HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH
TITLE 2 METHYLENE BLUE AND BEARING THE DOUBLE MUTATION I199A-Y326A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AMINE OXIDASE [FLAVIN-CONTAINING] B;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: MONOAMINE OXIDASE B, MONOAMINE OXIDASE TYPE B, MAO-B;
COMPND 5 EC: 1.4.3.4;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: 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;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: KM71
KEYWDS OXIDOREDUCTASE, INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR E.M.MILCZEK,C.BINDA,S.ROVIDA,A.MATTEVI,D.E.EDMONDSON
REVDAT 3 20-DEC-23 3ZYX 1 REMARK LINK
REVDAT 2 01-APR-15 3ZYX 1 REMARK
REVDAT 1 14-DEC-11 3ZYX 0
JRNL AUTH E.M.MILCZEK,C.BINDA,S.ROVIDA,A.MATTEVI,D.E.EDMONDSON
JRNL TITL THE 'GATING' RESIDUES ILE199 AND TYR326 IN HUMAN MONOAMINE
JRNL TITL 2 OXIDASE B FUNCTION IN SUBSTRATE AND INHIBITOR RECOGNITION.
JRNL REF FEBS J. V. 278 4860 2011
JRNL REFN ISSN 1742-464X
JRNL PMID 21978362
JRNL DOI 10.1111/J.1742-4658.2011.08386.X
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.31
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 62656
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) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.600
REMARK 3 FREE R VALUE TEST SET COUNT : 1667
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3988
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.32
REMARK 3 BIN R VALUE (WORKING SET) : 0.2410
REMARK 3 BIN FREE R VALUE SET COUNT : 92
REMARK 3 BIN FREE R VALUE : 0.3220
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7894
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 146
REMARK 3 SOLVENT ATOMS : 350
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.78
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.11000
REMARK 3 B22 (A**2) : 0.53000
REMARK 3 B33 (A**2) : -0.64000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.229
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.200
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.131
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.036
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.931
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.882
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8246 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11209 ; 1.379 ; 1.988
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 991 ; 6.081 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 356 ;35.261 ;23.539
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1404 ;15.450 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 58 ;16.518 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1218 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6222 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4942 ; 0.630 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8004 ; 1.194 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3304 ; 1.989 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3205 ; 3.196 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 3ZYX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-AUG-11.
REMARK 100 THE DEPOSITION ID IS D_1290049478.
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
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64424
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2V5Z
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG4000, 100 MM ADA PH 6.5, 70 MM
REMARK 280 LITHIUM SULPHATE, 8.5 MM ZWITTERGENT 3-12
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 65.95000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 112.48000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 65.95000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 112.48000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 65.95000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 112.48000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 65.95000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 112.48000
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 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: 8580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B2049 LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ILE 199 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, TYR 326 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, ILE 199 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, TYR 326 TO ALA
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 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 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 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 448 NE - CZ - NH2 ANGL. DEV. = -3.1 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 ASP A 37 20.69 -78.32
REMARK 500 LYS A 52 -70.37 67.08
REMARK 500 SER A 59 -53.29 -143.55
REMARK 500 THR A 64 -2.90 76.44
REMARK 500 ALA A 133 67.49 -164.19
REMARK 500 THR A 201 -78.21 -88.20
REMARK 500 ALA A 346 -119.49 50.56
REMARK 500 GLU A 379 59.26 -115.93
REMARK 500 ASP A 419 -97.92 56.33
REMARK 500 ALA A 424 -150.85 -107.97
REMARK 500 ASP A 460 4.17 -67.99
REMARK 500 TYR B 44 119.65 -160.51
REMARK 500 LYS B 52 -74.19 60.12
REMARK 500 SER B 59 -45.94 -144.03
REMARK 500 THR B 64 -11.10 74.97
REMARK 500 ALA B 133 69.18 -162.15
REMARK 500 THR B 201 -80.94 -85.59
REMARK 500 ASN B 251 24.32 -77.43
REMARK 500 PRO B 277 150.70 -49.20
REMARK 500 ALA B 346 -124.99 62.16
REMARK 500 ASP B 419 -100.15 59.62
REMARK 500 ALA B 424 -155.49 -106.76
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 FAD A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MBT A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MBT B 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2C67 RELATED DB: PDB
REMARK 900 MAO INHIBITION BY RASAGILINE ANALOGUES
REMARK 900 RELATED ID: 1S3E RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MAOB IN COMPLEX WITH 6-HYDROXY- N-PROPARGYL-
REMARK 900 1(R)-AMINOINDAN
REMARK 900 RELATED ID: 2C73 RELATED DB: PDB
REMARK 900 FUNCTIONAL ROLE OF THE AROMATIC CAGE IN HUMAN MONOAMINE OXIDASE B:
REMARK 900 STRUCTURES AND CATALYTIC PROPERTIES OF TYR435 MUTANT PROTEINS
REMARK 900 RELATED ID: 2V60 RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN MAO B IN COMPLEX WITH THE SELECTIVE INHIBITOR 7-
REMARK 900 (3-CHLOROBENZYLOXY)-4-CARBOXALDEHYDE -COUMARIN
REMARK 900 RELATED ID: 1OJ9 RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH 1,4- DIPHENYL-2-BUTENE
REMARK 900 RELATED ID: 2VZ2 RELATED DB: PDB
REMARK 900 HUMAN MAO B IN COMPLEX WITH MOFEGILINE
REMARK 900 RELATED ID: 1OJD RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH LAURYLDIMETHYLAMINE-N-
REMARK 900 OXIDE (LDAO)
REMARK 900 RELATED ID: 1S3B RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MAOB IN COMPLEX WITH N-METHYL-N -PROPARGYL-1(R)
REMARK 900 -AMINOINDAN
REMARK 900 RELATED ID: 2C66 RELATED DB: PDB
REMARK 900 MAO INHIBITION BY RASAGILINE ANALOGUES
REMARK 900 RELATED ID: 2XFO RELATED DB: PDB
REMARK 900 TRANYLCYPROMINE-INHIBITED HUMAN MONOAMINE OXIDASE B ILE199ALA
REMARK 900 MUTANT IN COMPLEX WITH 2-(2-BENZOFURANYL)-2 -IMIDAZOLINE
REMARK 900 RELATED ID: 2BK5 RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE B: I199F MUTANT IN COMPLEX WITH ISATIN
REMARK 900 RELATED ID: 1H8R RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE TYPE B (TRUNCATED)
REMARK 900 RELATED ID: 2C70 RELATED DB: PDB
REMARK 900 FUNCTIONAL ROLE OF THE AROMATIC CAGE IN HUMAN MONOAMINE OXIDASE B:
REMARK 900 STRUCTURES AND CATALYTIC PROPERTIES OF TYR435 MUTANT PROTEINS
REMARK 900 RELATED ID: 2XFN RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH 2-(2- BENZOFURANYL)-2-
REMARK 900 IMIDAZOLINE
REMARK 900 RELATED ID: 2BK3 RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH FARNESOL
REMARK 900 RELATED ID: 2C76 RELATED DB: PDB
REMARK 900 FUNCTIONAL ROLE OF THE AROMATIC CAGE IN HUMAN MONOAMINE OXIDASE B:
REMARK 900 STRUCTURES AND CATALYTIC PROPERTIES OF TYR435 MUTANT PROTEINS
REMARK 900 RELATED ID: 2VRL RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN MAO B IN COMPLEX WITH BENZYLHYDRAZINE
REMARK 900 RELATED ID: 1OJA RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH ISATIN
REMARK 900 RELATED ID: 2V5Z RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN MAO B IN COMPLEX WITH THE SELECTIVE INHIBITOR
REMARK 900 SAFINAMIDE
REMARK 900 RELATED ID: 2XFU RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE B WITH TRANYLCYPROMINE
REMARK 900 RELATED ID: 2BYB RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH DEPRENYL
REMARK 900 RELATED ID: 2VRM RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN MAO B IN COMPLEX WITH PHENYETHYLHYDRAZINE
REMARK 900 RELATED ID: 2C65 RELATED DB: PDB
REMARK 900 MAO INHIBITION BY RASAGILINE ANALOGUES
REMARK 900 RELATED ID: 2C64 RELATED DB: PDB
REMARK 900 MAO INHIBITION BY RASAGILINE ANALOGUES
REMARK 900 RELATED ID: 2XCG RELATED DB: PDB
REMARK 900 TRANYLCYPROMINE-INHIBITED HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH
REMARK 900 2-(2-BENZOFURANYL)-2-IMIDAZOLINE
REMARK 900 RELATED ID: 2XFP RELATED DB: PDB
REMARK 900 ISATIN-INHIBITED HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH 2-(2-
REMARK 900 BENZOFURANYL)-2-IMIDAZOLINE
REMARK 900 RELATED ID: 2BK4 RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE B: I199F MUTANT IN COMPLEX WITH RASAGILINE
REMARK 900 RELATED ID: 2C75 RELATED DB: PDB
REMARK 900 FUNCTIONAL ROLE OF THE AROMATIC CAGE IN HUMAN MONOAMINE OXIDASE B:
REMARK 900 STRUCTURES AND CATALYTIC PROPERTIES OF TYR435 MUTANT PROTEINS
REMARK 900 RELATED ID: 2V61 RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN MAO B IN COMPLEX WITH THE SELECTIVE INHIBITOR 7-
REMARK 900 (3-CHLOROBENZYLOXY)-4-(METHYLAMINO) METHYL-COUMARIN
REMARK 900 RELATED ID: 1S2Y RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MAOB IN COMPLEX WITH N-PROPARGYL -1(S)-
REMARK 900 AMINOINDAN
REMARK 900 RELATED ID: 2C72 RELATED DB: PDB
REMARK 900 FUNCTIONAL ROLE OF THE AROMATIC CAGE IN HUMAN MONOAMINE OXIDASE B:
REMARK 900 STRUCTURES AND CATALYTIC PROPERTIES OF TYR435 MUTANT PROTEINS
REMARK 900 RELATED ID: 1GOS RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE B
REMARK 900 RELATED ID: 1S2Q RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MAOB IN COMPLEX WITH N-PROPARGYL -1(R)-
REMARK 900 AMINOINDAN (RASAGILINE)
REMARK 900 RELATED ID: 2XFQ RELATED DB: PDB
REMARK 900 RASAGILINE-INHIBITED HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH 2-(2-
REMARK 900 BENZOFURANYL)-2-IMIDAZOLINE
REMARK 900 RELATED ID: 1OJC RELATED DB: PDB
REMARK 900 HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH N-(2- AMINOETHYL)-P-
REMARK 900 CHLOROBENZAMIDE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 DISCREPANCIES OCCUR AT SITES 199 AND 326 BECAUSE SITE-
REMARK 999 DIRECTED MUTAGENESIS HAS BEEN PERFORMED IN ORDER TO STUDY
REMARK 999 THESE GATING RESIDUES
DBREF 3ZYX A 2 520 UNP P27338 AOFB_HUMAN 2 520
DBREF 3ZYX B 2 520 UNP P27338 AOFB_HUMAN 2 520
SEQADV 3ZYX ALA A 199 UNP P27338 ILE 199 ENGINEERED MUTATION
SEQADV 3ZYX ALA A 326 UNP P27338 TYR 326 ENGINEERED MUTATION
SEQADV 3ZYX ALA B 199 UNP P27338 ILE 199 ENGINEERED MUTATION
SEQADV 3ZYX ALA B 326 UNP P27338 TYR 326 ENGINEERED MUTATION
SEQRES 1 A 519 SER ASN LYS CYS ASP VAL VAL VAL VAL GLY GLY GLY ILE
SEQRES 2 A 519 SER GLY MET ALA ALA ALA LYS LEU LEU HIS ASP SER GLY
SEQRES 3 A 519 LEU ASN VAL VAL VAL LEU GLU ALA ARG ASP ARG VAL GLY
SEQRES 4 A 519 GLY ARG THR TYR THR LEU ARG ASN GLN LYS VAL LYS TYR
SEQRES 5 A 519 VAL ASP LEU GLY GLY SER TYR VAL GLY PRO THR GLN ASN
SEQRES 6 A 519 ARG ILE LEU ARG LEU ALA LYS GLU LEU GLY LEU GLU THR
SEQRES 7 A 519 TYR LYS VAL ASN GLU VAL GLU ARG LEU ILE HIS HIS VAL
SEQRES 8 A 519 LYS GLY LYS SER TYR PRO PHE ARG GLY PRO PHE PRO PRO
SEQRES 9 A 519 VAL TRP ASN PRO ILE THR TYR LEU ASP HIS ASN ASN PHE
SEQRES 10 A 519 TRP ARG THR MET ASP ASP MET GLY ARG GLU ILE PRO SER
SEQRES 11 A 519 ASP ALA PRO TRP LYS ALA PRO LEU ALA GLU GLU TRP ASP
SEQRES 12 A 519 ASN MET THR MET LYS GLU LEU LEU ASP LYS LEU CYS TRP
SEQRES 13 A 519 THR GLU SER ALA LYS GLN LEU ALA THR LEU PHE VAL ASN
SEQRES 14 A 519 LEU CYS VAL THR ALA GLU THR HIS GLU VAL SER ALA LEU
SEQRES 15 A 519 TRP PHE LEU TRP TYR VAL LYS GLN CYS GLY GLY THR THR
SEQRES 16 A 519 ARG ILE ALA SER THR THR ASN GLY GLY GLN GLU ARG LYS
SEQRES 17 A 519 PHE VAL GLY GLY SER GLY GLN VAL SER GLU ARG ILE MET
SEQRES 18 A 519 ASP LEU LEU GLY ASP ARG VAL LYS LEU GLU ARG PRO VAL
SEQRES 19 A 519 ILE TYR ILE ASP GLN THR ARG GLU ASN VAL LEU VAL GLU
SEQRES 20 A 519 THR LEU ASN HIS GLU MET TYR GLU ALA LYS TYR VAL ILE
SEQRES 21 A 519 SER ALA ILE PRO PRO THR LEU GLY MET LYS ILE HIS PHE
SEQRES 22 A 519 ASN PRO PRO LEU PRO MET MET ARG ASN GLN MET ILE THR
SEQRES 23 A 519 ARG VAL PRO LEU GLY SER VAL ILE LYS CYS ILE VAL TYR
SEQRES 24 A 519 TYR LYS GLU PRO PHE TRP ARG LYS LYS ASP TYR CYS GLY
SEQRES 25 A 519 THR MET ILE ILE ASP GLY GLU GLU ALA PRO VAL ALA ALA
SEQRES 26 A 519 THR LEU ASP ASP THR LYS PRO GLU GLY ASN TYR ALA ALA
SEQRES 27 A 519 ILE MET GLY PHE ILE LEU ALA HIS LYS ALA ARG LYS LEU
SEQRES 28 A 519 ALA ARG LEU THR LYS GLU GLU ARG LEU LYS LYS LEU CYS
SEQRES 29 A 519 GLU LEU TYR ALA LYS VAL LEU GLY SER LEU GLU ALA LEU
SEQRES 30 A 519 GLU PRO VAL HIS TYR GLU GLU LYS ASN TRP CYS GLU GLU
SEQRES 31 A 519 GLN TYR SER GLY GLY CYS TYR THR THR TYR PHE PRO PRO
SEQRES 32 A 519 GLY ILE LEU THR GLN TYR GLY ARG VAL LEU ARG GLN PRO
SEQRES 33 A 519 VAL ASP ARG ILE TYR PHE ALA GLY THR GLU THR ALA THR
SEQRES 34 A 519 HIS TRP SER GLY TYR MET GLU GLY ALA VAL GLU ALA GLY
SEQRES 35 A 519 GLU ARG ALA ALA ARG GLU ILE LEU HIS ALA MET GLY LYS
SEQRES 36 A 519 ILE PRO GLU ASP GLU ILE TRP GLN SER GLU PRO GLU SER
SEQRES 37 A 519 VAL ASP VAL PRO ALA GLN PRO ILE THR THR THR PHE LEU
SEQRES 38 A 519 GLU ARG HIS LEU PRO SER VAL PRO GLY LEU LEU ARG LEU
SEQRES 39 A 519 ILE GLY LEU THR THR ILE PHE SER ALA THR ALA LEU GLY
SEQRES 40 A 519 PHE LEU ALA HIS LYS ARG GLY LEU LEU VAL ARG VAL
SEQRES 1 B 519 SER ASN LYS CYS ASP VAL VAL VAL VAL GLY GLY GLY ILE
SEQRES 2 B 519 SER GLY MET ALA ALA ALA LYS LEU LEU HIS ASP SER GLY
SEQRES 3 B 519 LEU ASN VAL VAL VAL LEU GLU ALA ARG ASP ARG VAL GLY
SEQRES 4 B 519 GLY ARG THR TYR THR LEU ARG ASN GLN LYS VAL LYS TYR
SEQRES 5 B 519 VAL ASP LEU GLY GLY SER TYR VAL GLY PRO THR GLN ASN
SEQRES 6 B 519 ARG ILE LEU ARG LEU ALA LYS GLU LEU GLY LEU GLU THR
SEQRES 7 B 519 TYR LYS VAL ASN GLU VAL GLU ARG LEU ILE HIS HIS VAL
SEQRES 8 B 519 LYS GLY LYS SER TYR PRO PHE ARG GLY PRO PHE PRO PRO
SEQRES 9 B 519 VAL TRP ASN PRO ILE THR TYR LEU ASP HIS ASN ASN PHE
SEQRES 10 B 519 TRP ARG THR MET ASP ASP MET GLY ARG GLU ILE PRO SER
SEQRES 11 B 519 ASP ALA PRO TRP LYS ALA PRO LEU ALA GLU GLU TRP ASP
SEQRES 12 B 519 ASN MET THR MET LYS GLU LEU LEU ASP LYS LEU CYS TRP
SEQRES 13 B 519 THR GLU SER ALA LYS GLN LEU ALA THR LEU PHE VAL ASN
SEQRES 14 B 519 LEU CYS VAL THR ALA GLU THR HIS GLU VAL SER ALA LEU
SEQRES 15 B 519 TRP PHE LEU TRP TYR VAL LYS GLN CYS GLY GLY THR THR
SEQRES 16 B 519 ARG ILE ALA SER THR THR ASN GLY GLY GLN GLU ARG LYS
SEQRES 17 B 519 PHE VAL GLY GLY SER GLY GLN VAL SER GLU ARG ILE MET
SEQRES 18 B 519 ASP LEU LEU GLY ASP ARG VAL LYS LEU GLU ARG PRO VAL
SEQRES 19 B 519 ILE TYR ILE ASP GLN THR ARG GLU ASN VAL LEU VAL GLU
SEQRES 20 B 519 THR LEU ASN HIS GLU MET TYR GLU ALA LYS TYR VAL ILE
SEQRES 21 B 519 SER ALA ILE PRO PRO THR LEU GLY MET LYS ILE HIS PHE
SEQRES 22 B 519 ASN PRO PRO LEU PRO MET MET ARG ASN GLN MET ILE THR
SEQRES 23 B 519 ARG VAL PRO LEU GLY SER VAL ILE LYS CYS ILE VAL TYR
SEQRES 24 B 519 TYR LYS GLU PRO PHE TRP ARG LYS LYS ASP TYR CYS GLY
SEQRES 25 B 519 THR MET ILE ILE ASP GLY GLU GLU ALA PRO VAL ALA ALA
SEQRES 26 B 519 THR LEU ASP ASP THR LYS PRO GLU GLY ASN TYR ALA ALA
SEQRES 27 B 519 ILE MET GLY PHE ILE LEU ALA HIS LYS ALA ARG LYS LEU
SEQRES 28 B 519 ALA ARG LEU THR LYS GLU GLU ARG LEU LYS LYS LEU CYS
SEQRES 29 B 519 GLU LEU TYR ALA LYS VAL LEU GLY SER LEU GLU ALA LEU
SEQRES 30 B 519 GLU PRO VAL HIS TYR GLU GLU LYS ASN TRP CYS GLU GLU
SEQRES 31 B 519 GLN TYR SER GLY GLY CYS TYR THR THR TYR PHE PRO PRO
SEQRES 32 B 519 GLY ILE LEU THR GLN TYR GLY ARG VAL LEU ARG GLN PRO
SEQRES 33 B 519 VAL ASP ARG ILE TYR PHE ALA GLY THR GLU THR ALA THR
SEQRES 34 B 519 HIS TRP SER GLY TYR MET GLU GLY ALA VAL GLU ALA GLY
SEQRES 35 B 519 GLU ARG ALA ALA ARG GLU ILE LEU HIS ALA MET GLY LYS
SEQRES 36 B 519 ILE PRO GLU ASP GLU ILE TRP GLN SER GLU PRO GLU SER
SEQRES 37 B 519 VAL ASP VAL PRO ALA GLN PRO ILE THR THR THR PHE LEU
SEQRES 38 B 519 GLU ARG HIS LEU PRO SER VAL PRO GLY LEU LEU ARG LEU
SEQRES 39 B 519 ILE GLY LEU THR THR ILE PHE SER ALA THR ALA LEU GLY
SEQRES 40 B 519 PHE LEU ALA HIS LYS ARG GLY LEU LEU VAL ARG VAL
HET FAD A 600 53
HET MBT A 601 20
HET FAD B 600 53
HET MBT B 601 20
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM MBT 3,7-BIS(DIMETHYLAMINO)PHENOTHIAZIN-5-IUM
HETSYN MBT METHYLENE BLUE
FORMUL 3 FAD 2(C27 H33 N9 O15 P2)
FORMUL 4 MBT 2(C16 H18 N3 S 1+)
FORMUL 7 HOH *350(H2 O)
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 CYS A 192 1 12
HELIX 9 9 GLY A 194 SER A 200 1 7
HELIX 10 10 SER A 214 GLY A 226 1 13
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 LEU A 372 1 17
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 SER B 214 GLY B 226 1 13
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 LEU B 495 1 8
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 ALA 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 ASN B 48 0
SHEET 2 BB 2 LYS B 52 ASP B 55 -1 O LYS B 52 N ASN B 48
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 ALA 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 A 600 1555 1555 1.64
LINK SG CYS B 397 C8M FAD B 600 1555 1555 1.65
CISPEP 1 ASN A 275 PRO A 276 0 -3.48
CISPEP 2 CYS A 397 TYR A 398 0 2.98
CISPEP 3 ASN B 275 PRO B 276 0 -2.08
CISPEP 4 CYS B 397 TYR B 398 0 -1.02
SITE 1 AC1 39 GLY A 11 GLY A 13 ILE A 14 SER A 15
SITE 2 AC1 39 LEU A 33 GLU A 34 ALA A 35 ARG A 36
SITE 3 AC1 39 GLY A 40 GLY A 41 ARG A 42 THR A 43
SITE 4 AC1 39 GLY A 58 SER A 59 TYR A 60 ARG A 233
SITE 5 AC1 39 PRO A 234 VAL A 235 ALA A 263 ILE A 264
SITE 6 AC1 39 TRP A 388 TYR A 393 CYS A 397 TYR A 398
SITE 7 AC1 39 GLY A 425 THR A 426 GLY A 434 TYR A 435
SITE 8 AC1 39 MET A 436 ALA A 439 MBT A 601 HOH A2001
SITE 9 AC1 39 HOH A2002 HOH A2007 HOH A2009 HOH A2014
SITE 10 AC1 39 HOH A2030 HOH A2035 HOH A2110
SITE 1 AC2 13 LEU A 171 ALA A 199 GLN A 206 THR A 314
SITE 2 AC2 13 ILE A 316 THR A 327 LEU A 328 PHE A 343
SITE 3 AC2 13 TYR A 398 TYR A 435 FAD A 600 HOH A2103
SITE 4 AC2 13 HOH A2166
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 58 SER B 59 TYR B 60
SITE 5 AC3 40 ARG B 233 PRO B 234 VAL B 235 ALA B 263
SITE 6 AC3 40 ILE B 264 TRP B 388 TYR B 393 CYS B 397
SITE 7 AC3 40 TYR B 398 GLY B 425 THR B 426 GLY B 434
SITE 8 AC3 40 TYR B 435 MET B 436 ALA B 439 MBT B 601
SITE 9 AC3 40 HOH B2001 HOH B2002 HOH B2009 HOH B2012
SITE 10 AC3 40 HOH B2015 HOH B2032 HOH B2039 HOH B2117
SITE 1 AC4 10 LEU B 171 ALA B 199 GLN B 206 THR B 314
SITE 2 AC4 10 ILE B 316 LEU B 328 PHE B 343 FAD B 600
SITE 3 AC4 10 HOH B2107 HOH B2162
CRYST1 131.900 224.960 86.630 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 0.007582 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004445 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011543 0.00000
MTRIX1 1 -0.525000 -0.497000 -0.691000 140.71869 1
MTRIX2 1 0.498000 -0.479000 0.723000 210.38109 1
MTRIX3 1 -0.690000 0.724000 0.004000 -54.78398 1
(ATOM LINES ARE NOT SHOWN.)
END
