GenomeNet

Database: PDB
Entry: 2Z5U
LinkDB: 2Z5U
Original site: 2Z5U 
HEADER    OXIDOREDUCTASE                          17-JUL-07   2Z5U              
TITLE     CRYSTAL STRUCTURE OF LYSINE-SPECIFIC HISTONE DEMETHYLASE 1            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LYSINE-SPECIFIC HISTONE DEMETHYLASE 1;                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: LSD1, RESIDUES 172-833;                                    
COMPND   5 SYNONYM: FLAVIN-CONTAINING AMINE OXIDASE DOMAIN-CONTAINING PROTEIN 2,
COMPND   6 BRAF35-HDAC COMPLEX PROTEIN BHC110;                                  
COMPND   7 EC: 1.-.-.-;                                                         
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: KIAA0601, LSD1;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX-HS-6P                                
KEYWDS    CHROMATIN, HISTONE DEMETHYLASE, NUCLEOSOME, TRANSCRIPTION, LSD1,      
KEYWDS   2 LYSINE-SPECIFIC, CHROMATIN REGULATOR, FAD, NUCLEUS, OXIDOREDUCTASE,  
KEYWDS   3 PHOSPHORYLATION, REPRESSOR, TRANSCRIPTION REGULATION, STRUCTURAL     
KEYWDS   4 GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND         
KEYWDS   5 FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS            
KEYWDS   6 INITIATIVE, RSGI                                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.MIMASU,T.SENGOKU,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS    
AUTHOR   2 INITIATIVE (RSGI)                                                    
REVDAT   7   01-NOV-23 2Z5U    1       REMARK                                   
REVDAT   6   25-DEC-19 2Z5U    1       REMARK                                   
REVDAT   5   27-MAR-13 2Z5U    1       HET    HETATM HETNAM VERSN               
REVDAT   4   24-FEB-09 2Z5U    1       VERSN                                    
REVDAT   3   24-JUN-08 2Z5U    1       JRNL                                     
REVDAT   2   15-APR-08 2Z5U    1       HETATM                                   
REVDAT   1   01-APR-08 2Z5U    0                                                
JRNL        AUTH   S.MIMASU,T.SENGOKU,S.FUKUZAWA,T.UMEHARA,S.YOKOYAMA           
JRNL        TITL   CRYSTAL STRUCTURE OF HISTONE DEMETHYLASE LSD1 AND            
JRNL        TITL 2 TRANYLCYPROMINE AT 2.25 A                                    
JRNL        REF    BIOCHEM.BIOPHYS.RES.COMMUN.   V. 366    15 2008              
JRNL        REFN                   ISSN 0006-291X                               
JRNL        PMID   18039463                                                     
JRNL        DOI    10.1016/J.BBRC.2007.11.066                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.36                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 48969                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.225                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2551                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 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) : 2.25                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.39                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3130                       
REMARK   3   BIN FREE R VALUE                    : 0.3220                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 381                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5044                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 63                                      
REMARK   3   SOLVENT ATOMS            : 130                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 31.40                          
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.32                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.34                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.33                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.50                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.950                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.350 ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2Z5U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-JUL-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000027558.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-MAY-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
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                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 51520                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.9100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.39                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.32000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 11.30                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 2EJR                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.55                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.68                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1MM HEPES-NA, 5% MPD, 3-4.5% PEG       
REMARK 280  MONOMETHYLETHER 2000, 1MM DTT, PH 7.5, VAPOR DIFFUSION, HANGING     
REMARK 280  DROP, TEMPERATURE 277.0K                                            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       36.24733            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       72.49467            
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       54.37100            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       90.61833            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       18.12367            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       36.24733            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       72.49467            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       90.61833            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       54.37100            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       18.12367            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ALA A   465                                                      
REMARK 465     SER A   466                                                      
REMARK 465     GLU A   467                                                      
REMARK 465     VAL A   468                                                      
REMARK 465     LYS A   469                                                      
REMARK 465     PRO A   470                                                      
REMARK 465     PRO A   471                                                      
REMARK 465     ARG A   472                                                      
REMARK 465     ASP A   473                                                      
REMARK 465     GLY A   783                                                      
REMARK 465     PRO A   784                                                      
REMARK 465     SER A   785                                                      
REMARK 465     ILE A   786                                                      
REMARK 465     PRO A   787                                                      
REMARK 465     GLY A   788                                                      
REMARK 465     ALA A   789                                                      
REMARK 465     PRO A   790                                                      
REMARK 465     GLN A   791                                                      
REMARK 465     ALA A   832                                                      
REMARK 465     MET A   833                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 782   C   -  N   -  CA  ANGL. DEV. = -10.3 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    SER A 201       68.80   -100.01                                   
REMARK 500    ASN A 224       74.28   -153.20                                   
REMARK 500    LYS A 271       79.76   -106.87                                   
REMARK 500    THR A 335       45.62    -85.75                                   
REMARK 500    HIS A 394       49.62    -98.19                                   
REMARK 500    GLN A 395      -53.49   -169.88                                   
REMARK 500    ASP A 397       49.99     37.04                                   
REMARK 500    ASN A 403       -0.56     66.32                                   
REMARK 500    GLN A 460      147.08    169.86                                   
REMARK 500    GLN A 461      -57.27     81.07                                   
REMARK 500    TYR A 462       93.21    -59.33                                   
REMARK 500    LYS A 463       48.47    158.29                                   
REMARK 500    ALA A 476      -30.64    -39.60                                   
REMARK 500    TYR A 494      -78.28    -59.59                                   
REMARK 500    ASP A 495       -9.25    -53.33                                   
REMARK 500    THR A 500        1.93    -69.85                                   
REMARK 500    GLU A 512        6.08    -67.74                                   
REMARK 500    GLU A 559      150.58    -49.95                                   
REMARK 500    SER A 598       34.92   -141.69                                   
REMARK 500    SER A 609       78.25   -157.51                                   
REMARK 500    THR A 610       -0.33    -52.21                                   
REMARK 500    PRO A 701       81.39    -67.28                                   
REMARK 500    SER A 738      -21.46     79.98                                   
REMARK 500    ALA A 757      -53.97   -133.15                                   
REMARK 500    PRO A 794      120.39    -35.07                                   
REMARK 500    TYR A 807       47.53   -142.02                                   
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 FAJ A 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2EJR   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH ANOTHER DRAG                         
REMARK 900 RELATED ID: 2Z3Y   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH ANOTHER DRAG                         
DBREF  2Z5U A  172   833  UNP    O60341   LSD1_HUMAN     172    833             
SEQRES   1 A  662  SER GLY VAL GLU GLY ALA ALA PHE GLN SER ARG LEU PRO          
SEQRES   2 A  662  HIS ASP ARG MET THR SER GLN GLU ALA ALA CYS PHE PRO          
SEQRES   3 A  662  ASP ILE ILE SER GLY PRO GLN GLN THR GLN LYS VAL PHE          
SEQRES   4 A  662  LEU PHE ILE ARG ASN ARG THR LEU GLN LEU TRP LEU ASP          
SEQRES   5 A  662  ASN PRO LYS ILE GLN LEU THR PHE GLU ALA THR LEU GLN          
SEQRES   6 A  662  GLN LEU GLU ALA PRO TYR ASN SER ASP THR VAL LEU VAL          
SEQRES   7 A  662  HIS ARG VAL HIS SER TYR LEU GLU ARG HIS GLY LEU ILE          
SEQRES   8 A  662  ASN PHE GLY ILE TYR LYS ARG ILE LYS PRO LEU PRO THR          
SEQRES   9 A  662  LYS LYS THR GLY LYS VAL ILE ILE ILE GLY SER GLY VAL          
SEQRES  10 A  662  SER GLY LEU ALA ALA ALA ARG GLN LEU GLN SER PHE GLY          
SEQRES  11 A  662  MET ASP VAL THR LEU LEU GLU ALA ARG ASP ARG VAL GLY          
SEQRES  12 A  662  GLY ARG VAL ALA THR PHE ARG LYS GLY ASN TYR VAL ALA          
SEQRES  13 A  662  ASP LEU GLY ALA MET VAL VAL THR GLY LEU GLY GLY ASN          
SEQRES  14 A  662  PRO MET ALA VAL VAL SER LYS GLN VAL ASN MET GLU LEU          
SEQRES  15 A  662  ALA LYS ILE LYS GLN LYS CYS PRO LEU TYR GLU ALA ASN          
SEQRES  16 A  662  GLY GLN ALA VAL PRO LYS GLU LYS ASP GLU MET VAL GLU          
SEQRES  17 A  662  GLN GLU PHE ASN ARG LEU LEU GLU ALA THR SER TYR LEU          
SEQRES  18 A  662  SER HIS GLN LEU ASP PHE ASN VAL LEU ASN ASN LYS PRO          
SEQRES  19 A  662  VAL SER LEU GLY GLN ALA LEU GLU VAL VAL ILE GLN LEU          
SEQRES  20 A  662  GLN GLU LYS HIS VAL LYS ASP GLU GLN ILE GLU HIS TRP          
SEQRES  21 A  662  LYS LYS ILE VAL LYS THR GLN GLU GLU LEU LYS GLU LEU          
SEQRES  22 A  662  LEU ASN LYS MET VAL ASN LEU LYS GLU LYS ILE LYS GLU          
SEQRES  23 A  662  LEU HIS GLN GLN TYR LYS GLU ALA SER GLU VAL LYS PRO          
SEQRES  24 A  662  PRO ARG ASP ILE THR ALA GLU PHE LEU VAL LYS SER LYS          
SEQRES  25 A  662  HIS ARG ASP LEU THR ALA LEU CYS LYS GLU TYR ASP GLU          
SEQRES  26 A  662  LEU ALA GLU THR GLN GLY LYS LEU GLU GLU LYS LEU GLN          
SEQRES  27 A  662  GLU LEU GLU ALA ASN PRO PRO SER ASP VAL TYR LEU SER          
SEQRES  28 A  662  SER ARG ASP ARG GLN ILE LEU ASP TRP HIS PHE ALA ASN          
SEQRES  29 A  662  LEU GLU PHE ALA ASN ALA THR PRO LEU SER THR LEU SER          
SEQRES  30 A  662  LEU LYS HIS TRP ASP GLN ASP ASP ASP PHE GLU PHE THR          
SEQRES  31 A  662  GLY SER HIS LEU THR VAL ARG ASN GLY TYR SER CYS VAL          
SEQRES  32 A  662  PRO VAL ALA LEU ALA GLU GLY LEU ASP ILE LYS LEU ASN          
SEQRES  33 A  662  THR ALA VAL ARG GLN VAL ARG TYR THR ALA SER GLY CYS          
SEQRES  34 A  662  GLU VAL ILE ALA VAL ASN THR ARG SER THR SER GLN THR          
SEQRES  35 A  662  PHE ILE TYR LYS CYS ASP ALA VAL LEU CYS THR LEU PRO          
SEQRES  36 A  662  LEU GLY VAL LEU LYS GLN GLN PRO PRO ALA VAL GLN PHE          
SEQRES  37 A  662  VAL PRO PRO LEU PRO GLU TRP LYS THR SER ALA VAL GLN          
SEQRES  38 A  662  ARG MET GLY PHE GLY ASN LEU ASN LYS VAL VAL LEU CYS          
SEQRES  39 A  662  PHE ASP ARG VAL PHE TRP ASP PRO SER VAL ASN LEU PHE          
SEQRES  40 A  662  GLY HIS VAL GLY SER THR THR ALA SER ARG GLY GLU LEU          
SEQRES  41 A  662  PHE LEU PHE TRP ASN LEU TYR LYS ALA PRO ILE LEU LEU          
SEQRES  42 A  662  ALA LEU VAL ALA GLY GLU ALA ALA GLY ILE MET GLU ASN          
SEQRES  43 A  662  ILE SER ASP ASP VAL ILE VAL GLY ARG CYS LEU ALA ILE          
SEQRES  44 A  662  LEU LYS GLY ILE PHE GLY SER SER ALA VAL PRO GLN PRO          
SEQRES  45 A  662  LYS GLU THR VAL VAL SER ARG TRP ARG ALA ASP PRO TRP          
SEQRES  46 A  662  ALA ARG GLY SER TYR SER TYR VAL ALA ALA GLY SER SER          
SEQRES  47 A  662  GLY ASN ASP TYR ASP LEU MET ALA GLN PRO ILE THR PRO          
SEQRES  48 A  662  GLY PRO SER ILE PRO GLY ALA PRO GLN PRO ILE PRO ARG          
SEQRES  49 A  662  LEU PHE PHE ALA GLY GLU HIS THR ILE ARG ASN TYR PRO          
SEQRES  50 A  662  ALA THR VAL HIS GLY ALA LEU LEU SER GLY LEU ARG GLU          
SEQRES  51 A  662  ALA GLY ARG ILE ALA ASP GLN PHE LEU GLY ALA MET              
HET    FAJ  A   1      63                                                       
HETNAM     FAJ FAD-TRANS-2-PHENYLCYCLOPROPYLAMINE ADDUCT                        
HETSYN     FAJ FAD-PCPA ADDUCT                                                  
FORMUL   2  FAJ    C36 H43 N9 O16 P2                                            
FORMUL   3  HOH   *130(H2 O)                                                    
HELIX    1   1 SER A  172  SER A  181  1                                  10    
HELIX    2   2 THR A  189  PHE A  196  1                                   8    
HELIX    3   3 PHE A  196  SER A  201  1                                   6    
HELIX    4   4 PRO A  203  ASP A  223  1                                  21    
HELIX    5   5 THR A  230  LEU A  238  1                                   9    
HELIX    6   6 PRO A  241  SER A  244  5                                   4    
HELIX    7   7 ASP A  245  HIS A  259  1                                  15    
HELIX    8   8 GLY A  287  PHE A  300  1                                  14    
HELIX    9   9 ASN A  340  ASN A  350  1                                  11    
HELIX   10  10 PRO A  371  HIS A  394  1                                  24    
HELIX   11  11 SER A  407  GLU A  457  1                                  51    
HELIX   12  12 THR A  475  THR A  488  1                                  14    
HELIX   13  13 LEU A  490  ALA A  498  1                                   9    
HELIX   14  14 ALA A  498  GLU A  512  1                                  15    
HELIX   15  15 SER A  522  ALA A  541  1                                  20    
HELIX   16  16 PRO A  543  LEU A  547  5                                   5    
HELIX   17  17 ASP A  555  GLU A  559  5                                   5    
HELIX   18  18 SER A  572  ALA A  579  1                                   8    
HELIX   19  19 PRO A  626  GLN A  632  1                                   7    
HELIX   20  20 PRO A  644  MET A  654  1                                  11    
HELIX   21  21 ALA A  708  GLU A  716  1                                   9    
HELIX   22  22 SER A  719  GLY A  736  1                                  18    
HELIX   23  23 GLY A  770  GLN A  778  1                                   9    
HELIX   24  24 GLY A  800  ILE A  804  5                                   5    
HELIX   25  25 THR A  810  LEU A  830  1                                  21    
SHEET    1   A 5 ILE A 584  LYS A 585  0                                        
SHEET    2   A 5 ASP A 303  LEU A 307  1  N  LEU A 306   O  LYS A 585           
SHEET    3   A 5 LYS A 280  ILE A 284  1  N  VAL A 281   O  ASP A 303           
SHEET    4   A 5 ALA A 620  CYS A 623  1  O  LEU A 622   N  ILE A 284           
SHEET    5   A 5 LEU A 796  PHE A 798  1  O  PHE A 797   N  VAL A 621           
SHEET    1   B 2 THR A 319  LYS A 322  0                                        
SHEET    2   B 2 TYR A 325  ASP A 328 -1  O  ALA A 327   N  PHE A 320           
SHEET    1   C 3 VAL A 333  VAL A 334  0                                        
SHEET    2   C 3 LEU A 565  VAL A 567 -1  O  LEU A 565   N  VAL A 334           
SHEET    3   C 3 LEU A 353  LYS A 355 -1  N  ALA A 354   O  THR A 566           
SHEET    1   D 6 LEU A 362  TYR A 363  0                                        
SHEET    2   D 6 LEU A 677  HIS A 680  1  O  GLY A 679   N  TYR A 363           
SHEET    3   D 6 LEU A 693  ASN A 696 -1  O  PHE A 694   N  PHE A 678           
SHEET    4   D 6 ILE A 702  VAL A 707 -1  O  LEU A 704   N  TRP A 695           
SHEET    5   D 6 ASN A 660  CYS A 665 -1  N  LEU A 664   O  LEU A 703           
SHEET    6   D 6 GLU A 745  VAL A 748 -1  O  VAL A 747   N  VAL A 663           
SHEET    1   E 2 VAL A 400  LEU A 401  0                                        
SHEET    2   E 2 LYS A 404  PRO A 405 -1  O  LYS A 404   N  LEU A 401           
SHEET    1   F 4 THR A 613  CYS A 618  0                                        
SHEET    2   F 4 GLY A 599  ASN A 606 -1  N  CYS A 600   O  CYS A 618           
SHEET    3   F 4 THR A 588  THR A 596 -1  N  ARG A 594   O  GLU A 601           
SHEET    4   F 4 GLN A 638  VAL A 640  1  O  GLN A 638   N  ARG A 591           
SHEET    1   G 2 GLY A 655  PHE A 656  0                                        
SHEET    2   G 2 SER A 762  TYR A 763 -1  O  TYR A 763   N  GLY A 655           
CISPEP   1 ALA A  240    PRO A  241          0        -0.02                     
CISPEP   2 GLN A  633    PRO A  634          0        -0.18                     
CISPEP   3 VAL A  640    PRO A  641          0         0.01                     
SITE     1 AC1 38 ILE A 284  GLY A 285  GLY A 287  VAL A 288                    
SITE     2 AC1 38 SER A 289  LEU A 307  GLU A 308  ALA A 309                    
SITE     3 AC1 38 ARG A 310  GLY A 314  GLY A 315  ARG A 316                    
SITE     4 AC1 38 LEU A 329  GLY A 330  ALA A 331  MET A 332                    
SITE     5 AC1 38 VAL A 333  THR A 335  THR A 588  VAL A 590                    
SITE     6 AC1 38 THR A 624  LEU A 625  PRO A 626  VAL A 637                    
SITE     7 AC1 38 TRP A 751  TRP A 756  TYR A 761  GLY A 800                    
SITE     8 AC1 38 GLU A 801  ALA A 809  THR A 810  VAL A 811                    
SITE     9 AC1 38 ALA A 814  HOH A 839  HOH A 847  HOH A 891                    
SITE    10 AC1 38 HOH A 892  HOH A 916                                          
CRYST1  185.759  185.759  108.742  90.00  90.00 120.00 P 61 2 2     12          
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      0.005383  0.003108  0.000000        0.00000                         
SCALE2      0.000000  0.006216  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009196        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system