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PDBsum entry 2xfq

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Top Page protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
2xfq
Jmol
Contents
Protein chain
499 a.a.
Ligands
FAD-RAS ×2
XCG ×2
C15
Waters ×472
HEADER    OXIDOREDUCTASE                          26-MAY-10   2XFQ
TITLE     RASAGILINE-INHIBITED HUMAN MONOAMINE OXIDASE B IN COMPLEX
TITLE    2 WITH 2-(2-BENZOFURANYL)-2-IMIDAZOLINE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: AMINE OXIDASE [FLAVIN-CONTAINING] B;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: MONOAMINE OXIDASE TYPE B, MAO-B;
COMPND   5 EC: 1.4.3.4
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606
KEYWDS    FLAVOPROTEIN, OXIDOREDUCTASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.BONIVENTO,E.M.MILCZEK,G.R.MCDONALD,C.BINDA,A.HOLT,D.E.EDMONDSON,
AUTHOR   2 A.MATTEVI
REVDAT   3   29-FEB-12 2XFQ    1       REMARK VERSN  HETNAM HETSYN
REVDAT   3 2                           FORMUL
REVDAT   2   24-NOV-10 2XFQ    1       JRNL
REVDAT   1   06-OCT-10 2XFQ    0
JRNL        AUTH   D.BONIVENTO,E.M.MILCZEK,G.R.MCDONALD,C.BINDA,A.HOLT,
JRNL        AUTH 2 D.E.EDMONDSON,A.MATTEVI
JRNL        TITL   POTENTIATION OF LIGAND BINDING THROUGH COOPERATIVE EFFECTS
JRNL        TITL 2 IN MONOAMINE OXIDASE B.
JRNL        REF    J.BIOL.CHEM.                  V. 285 36849 2010
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   20855894
JRNL        DOI    10.1074/JBC.M110.169482
REMARK   2
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0109
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
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) : 40.4
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9
REMARK   3   NUMBER OF REFLECTIONS             : 62931
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) : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.159
REMARK   3   FREE R VALUE                     : NULL
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   REFLECTION IN BIN     (WORKING SET) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE SET COUNT          : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 7933
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 182
REMARK   3   SOLVENT ATOMS            : 472
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
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 OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK   3
REMARK   3  CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : NULL
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  NULL ;  NULL ;  NULL
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
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):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN ANGLE REFINED 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 : NULL
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : NULL
REMARK   3   ION PROBE RADIUS   : NULL
REMARK   3   SHRINKAGE RADIUS   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3   RIDING POSITIONS.
REMARK   4
REMARK   4 2XFQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-MAY-10.
REMARK 100 THE PDBE ID CODE IS EBI-43801.
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                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 64575
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.20
REMARK 200  RESOLUTION RANGE LOW       (A) : 50
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1
REMARK 200  DATA REDUNDANCY                : 4.1
REMARK 200  R MERGE                    (I) : 0.09
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.31
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.0
REMARK 200  R MERGE FOR SHELL          (I) : 0.206
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 6.7
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: REFMAC5
REMARK 200 STARTING MODEL: PDB ENTRY 1S2Q
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 54.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
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       65.75500
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      111.69000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       65.75500
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      111.69000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       65.75500
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      111.69000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       65.75500
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      111.69000
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: 8370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 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 A2003   LIES ON A SPECIAL POSITION.
REMARK 375      HOH B2154   LIES ON A SPECIAL POSITION.
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 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    GLU B 150   CD    GLU B 150   OE2     0.068
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ARG A  47   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES
REMARK 500    ARG A  47   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES
REMARK 500    ARG A 445   NE  -  CZ  -  NH1 ANGL. DEV. =   5.1 DEGREES
REMARK 500    ARG A 445   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.4 DEGREES
REMARK 500    ARG A 448   NE  -  CZ  -  NH1 ANGL. DEV. =   7.0 DEGREES
REMARK 500    ARG A 448   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.4 DEGREES
REMARK 500    ARG B  47   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES
REMARK 500    ARG B  47   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES
REMARK 500    ARG B 445   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES
REMARK 500    ARG B 445   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.2 DEGREES
REMARK 500    ARG B 448   NE  -  CZ  -  NH1 ANGL. DEV. =   6.6 DEGREES
REMARK 500    ARG B 448   NE  -  CZ  -  NH2 ANGL. DEV. =  -8.0 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    LYS A  52      -69.69     66.70
REMARK 500    SER A  59      -51.28   -152.52
REMARK 500    THR A  64       -5.10     80.50
REMARK 500    ALA A 133       68.50   -161.48
REMARK 500    THR A 201      -81.20    -91.17
REMARK 500    ALA A 346     -124.99     55.23
REMARK 500    GLU A 379       56.16   -116.14
REMARK 500    ASP A 419     -101.62     63.13
REMARK 500    ALA A 424     -147.51   -109.20
REMARK 500    THR A 500       33.34    -68.45
REMARK 500    LYS B  52      -74.20     69.37
REMARK 500    SER B  59      -51.24   -146.14
REMARK 500    THR B  64       -4.27     81.31
REMARK 500    LYS B  93       54.91     38.43
REMARK 500    ALA B 133       70.50   -160.86
REMARK 500    THR B 201      -74.11    -89.21
REMARK 500    ALA B 346     -126.67     57.16
REMARK 500    ASP B 419     -102.13     60.78
REMARK 500    ALA B 424     -149.98   -109.14
REMARK 500    LEU B 495       43.74    -83.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    HIS B 252        25.0      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 FLAVIN-ADENINE DINUCLEOTIDE (FAD): N5 ATOM OF FAD IS
REMARK 600  COVALENTLY ATTACHED TO C13 ATOM OF RAS
REMARK 600 N-PROPARGYL-1(R)-AMINOINDAN (RASAGILINE) (RAS): C13 ATOM OF
REMARK 600  RAS IS COVALENTLY ATTACHED TO N5 ATOM OF FAD
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XCG A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C15 A1503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XCG B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF
REMARK 800     RESIDUES  600 TO  601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF
REMARK 800     RESIDUES  600 TO  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: 1OJA   RELATED DB: PDB
REMARK 900  HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH
REMARK 900  ISATIN
REMARK 900 RELATED ID: 2V5Z   RELATED DB: PDB
REMARK 900  STRUCTURE OF HUMAN MAO B IN COMPLEX WITH
REMARK 900  THE SELECTIVE INHIBITOR SAFINAMIDE
REMARK 900 RELATED ID: 1S3E   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF MAOB IN COMPLEX WITH
REMARK 900  6-HYDROXY-N-PROPARGYL-1(R)-AMINOINDAN
REMARK 900 RELATED ID: 2C73   RELATED DB: PDB
REMARK 900  FUNCTIONAL ROLE OF THE AROMATIC CAGE IN
REMARK 900  HUMAN MONOAMINE OXIDASE B: STRUCTURES AND
REMARK 900  CATALYTIC PROPERTIES OF TYR435 MUTANT PROTEINS
REMARK 900 RELATED ID: 1OJB   RELATED DB: PDB
REMARK 900  HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH
REMARK 900  TRANYLCYPROMINE
REMARK 900 RELATED ID: 2V60   RELATED DB: PDB
REMARK 900  STRUCTURE OF HUMAN MAO B IN COMPLEX WITH
REMARK 900  THE SELECTIVE INHIBITOR 7-(3-CHLOROBENZYLOXY
REMARK 900  )-4-CARBOXALDEHYDE-COUMARIN
REMARK 900 RELATED ID: 2BYB   RELATED DB: PDB
REMARK 900  HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH
REMARK 900  DEPRENYL
REMARK 900 RELATED ID: 2VRM   RELATED DB: PDB
REMARK 900  STRUCTURE OF HUMAN MAO B IN COMPLEX WITH
REMARK 900  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
REMARK 900  OXIDASE B IN COMPLEX WITH 2-(2-
REMARK 900  BENZOFURANYL)-2-IMIDAZOLINE
REMARK 900 RELATED ID: 1OJ9   RELATED DB: PDB
REMARK 900  HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH
REMARK 900  1,4-DIPHENYL-2-BUTENE
REMARK 900 RELATED ID: 1OJD   RELATED DB: PDB
REMARK 900  HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH
REMARK 900  LAURYLDIMETHYLAMINE-N-OXIDE (LDAO)
REMARK 900 RELATED ID: 2VZ2   RELATED DB: PDB
REMARK 900  HUMAN MAO B IN COMPLEX WITH MOFEGILINE
REMARK 900 RELATED ID: 1S3B   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF MAOB IN COMPLEX WITH
REMARK 900  N-METHYL-N-PROPARGYL-1(R)-AMINOINDAN
REMARK 900 RELATED ID: 2C66   RELATED DB: PDB
REMARK 900  MAO INHIBITION BY RASAGILINE ANALOGUES
REMARK 900 RELATED ID: 2BK4   RELATED DB: PDB
REMARK 900  HUMAN MONOAMINE OXIDASE B: I199F MUTANT IN
REMARK 900  COMPLEX WITH RASAGILINE
REMARK 900 RELATED ID: 2BK5   RELATED DB: PDB
REMARK 900  HUMAN MONOAMINE OXIDASE B: I199F MUTANT IN
REMARK 900  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
REMARK 900  HUMAN MONOAMINE OXIDASE B: STRUCTURES AND
REMARK 900  CATALYTIC PROPERTIES OF TYR435 MUTANT PROTEINS
REMARK 900 RELATED ID: 2C75   RELATED DB: PDB
REMARK 900  FUNCTIONAL ROLE OF THE AROMATIC CAGE IN
REMARK 900  HUMAN MONOAMINE OXIDASE B: STRUCTURES AND
REMARK 900  CATALYTIC PROPERTIES OF TYR435 MUTANT PROTEINS
REMARK 900 RELATED ID: 2BK3   RELATED DB: PDB
REMARK 900  HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH
REMARK 900  FARNESOL
REMARK 900 RELATED ID: 2V61   RELATED DB: PDB
REMARK 900  STRUCTURE OF HUMAN MAO B IN COMPLEX WITH
REMARK 900  THE SELECTIVE INHIBITOR 7-(3-CHLOROBENZYLOXY
REMARK 900  )-4-(METHYLAMINO)METHYL-COUMARIN
REMARK 900 RELATED ID: 2C72   RELATED DB: PDB
REMARK 900  FUNCTIONAL ROLE OF THE AROMATIC CAGE IN
REMARK 900  HUMAN MONOAMINE OXIDASE B: STRUCTURES AND
REMARK 900  CATALYTIC PROPERTIES OF TYR435 MUTANT PROTEINS
REMARK 900 RELATED ID: 1S2Y   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF MAOB IN COMPLEX WITH
REMARK 900  N-PROPARGYL-1(S)-AMINOINDAN
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
REMARK 900  N-PROPARGYL-1(R)-AMINOINDAN (RASAGILINE)
REMARK 900 RELATED ID: 2C76   RELATED DB: PDB
REMARK 900  FUNCTIONAL ROLE OF THE AROMATIC CAGE IN
REMARK 900  HUMAN MONOAMINE OXIDASE B: STRUCTURES AND
REMARK 900  CATALYTIC PROPERTIES OF TYR435 MUTANT PROTEINS
REMARK 900 RELATED ID: 2VRL   RELATED DB: PDB
REMARK 900  STRUCTURE OF HUMAN MAO B IN COMPLEX WITH
REMARK 900  BENZYLHYDRAZINE
REMARK 900 RELATED ID: 1OJC   RELATED DB: PDB
REMARK 900  HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH
REMARK 900  N-(2-AMINOETHYL)-P-CHLOROBENZAMIDE
REMARK 900 RELATED ID: 2XFO   RELATED DB: PDB
REMARK 900  TRANYLCYPROMINE-INHIBITED HUMAN MONOAMINE
REMARK 900  OXIDASE B ILE199ALA MUTANT IN COMPLEX WITH
REMARK 900  2-(2-BENZOFURANYL)-2-IMIDAZOLINE
REMARK 900 RELATED ID: 2XFN   RELATED DB: PDB
REMARK 900  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
REMARK 900  IN COMPLEX WITH 2-(2-BENZOFURANYL)-2-
REMARK 900  IMIDAZOLINE
DBREF  2XFQ A    1   520  UNP    P27338   AOFB_HUMAN       1    520
DBREF  2XFQ B    1   520  UNP    P27338   AOFB_HUMAN       1    520
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  A 600      53
HET    RAS  A 601      13
HET    XCG  A 602      14
HET    C15  A1503      22
HET    FAD  B 600      53
HET    RAS  B 601      13
HET    XCG  B 602      14
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM     RAS (1R)-N-(PROP-2-EN-1-YL)-2,3-DIHYDRO-1H-INDEN-
HETNAM   2 RAS  1-AMINE
HETNAM     XCG 2-(2-BENZOFURANYL)-2-IMIDAZOLINE
HETNAM     C15 N-DODECYL-N,N-DIMETHYL-3-AMMONIO-1-
HETNAM   2 C15  PROPANESULFONATE
HETSYN     RAS RASAGILINE, BOUND FORM
FORMUL   3  FAD    2(C27 H33 N9 O15 P2)
FORMUL   4  RAS    2(C12 H15 N)
FORMUL   5  XCG    2(C11 H8 N2 O)
FORMUL   6  C15    C17 H38 N O3 S 1+
FORMUL   7  HOH   *472(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  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  1                                   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 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  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 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  LEU B 231  0
SHEET    2  BA 5 VAL B  30  GLU B  34  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 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 A 600     1555   1555  1.65
LINK         N5  FAD A 600                 C13 RAS A 601     1555   1555  1.67
LINK         SG  CYS B 397                 C8M FAD B 600     1555   1555  1.67
LINK         N5  FAD B 600                 C13 RAS B 601     1555   1555  1.64
CISPEP   1 ASN A  275    PRO A  276          0         1.78
CISPEP   2 CYS A  397    TYR A  398          0        -1.36
CISPEP   3 ASN B  275    PRO B  276          0        -1.73
CISPEP   4 CYS B  397    TYR B  398          0        -2.88
SITE     1 AC1  7 LEU A  88  PRO A 102  LEU A 164  LEU A 167
SITE     2 AC1  7 ILE A 199  ILE A 316  TYR A 326
SITE     1 AC2  5 TRP A 107  ASP A 153  LYS A 154  CYS A 156
SITE     2 AC2  5 TRP A 157
SITE     1 AC3  9 LEU B  88  PRO B 102  LEU B 164  LEU B 167
SITE     2 AC3  9 LEU B 171  ILE B 199  ILE B 316  TYR B 326
SITE     3 AC3  9 HOH B2049
SITE     1 AC4 42 GLY A  11  GLY A  13  ILE A  14  SER A  15
SITE     2 AC4 42 LEU A  33  GLU A  34  ALA A  35  ARG A  36
SITE     3 AC4 42 GLY A  41  ARG A  42  THR A  43  GLY A  57
SITE     4 AC4 42 GLY A  58  SER A  59  TYR A  60  LEU A 171
SITE     5 AC4 42 CYS A 172  ILE A 198  GLN A 206  PRO A 234
SITE     6 AC4 42 VAL A 235  ALA A 263  ILE A 264  TYR A 326
SITE     7 AC4 42 TRP A 388  TYR A 393  CYS A 397  TYR A 398
SITE     8 AC4 42 GLY A 425  THR A 426  GLY A 434  TYR A 435
SITE     9 AC4 42 MET A 436  ALA A 439  HOH A2009  HOH A2030
SITE    10 AC4 42 HOH A2123  HOH A2208  HOH A2209  HOH A2210
SITE    11 AC4 42 HOH A2211  HOH A2212
SITE     1 AC5 43 VAL B  10  GLY B  11  GLY B  13  ILE B  14
SITE     2 AC5 43 SER B  15  LEU B  33  GLU B  34  ALA B  35
SITE     3 AC5 43 ARG B  36  GLY B  40  GLY B  41  ARG B  42
SITE     4 AC5 43 GLY B  57  GLY B  58  SER B  59  TYR B  60
SITE     5 AC5 43 CYS B 172  ILE B 198  ILE B 199  GLN B 206
SITE     6 AC5 43 PRO B 234  VAL B 235  ALA B 263  ILE B 264
SITE     7 AC5 43 TYR B 326  TRP B 388  TYR B 393  CYS B 397
SITE     8 AC5 43 TYR B 398  GLY B 425  THR B 426  GLY B 434
SITE     9 AC5 43 TYR B 435  MET B 436  ALA B 439  HOH B2017
SITE    10 AC5 43 HOH B2254  HOH B2255  HOH B2256  HOH B2257
SITE    11 AC5 43 HOH B2258  HOH B2259  HOH B2260
CRYST1  131.510  223.380   86.550  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      0.007604  0.000000  0.000000        0.00000
SCALE2      0.000000  0.004477  0.000000        0.00000
SCALE3      0.000000  0.000000  0.011554        0.00000
      
PROCHECK
Go to PROCHECK summary
 References