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Database: PDB
Entry: 2V1D
LinkDB: 2V1D
Original site: 2V1D 
HEADER    OXIDOREDUCTASE/REPRESSOR                23-MAY-07   2V1D              
TITLE     STRUCTURAL BASIS OF LSD1-COREST SELECTIVITY IN HISTONE H3 RECOGNITION 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LYSINE-SPECIFIC HISTONE DEMETHYLASE 1;                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 123-852;                                          
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;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: REST COREPRESSOR 1;                                        
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: 305-482;                                                   
COMPND  13 SYNONYM: PROTEIN COREST, COREST;                                     
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 3;                                                           
COMPND  16 MOLECULE: HISTONE H3.1T;                                             
COMPND  17 CHAIN: C;                                                            
COMPND  18 FRAGMENT: RESIDUES 2-22;                                             
COMPND  19 SYNONYM: HISTONE H3 K4M PEPTIDE;                                     
COMPND  20 ENGINEERED: YES;                                                     
COMPND  21 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: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 SYNTHETIC: YES;                                                      
SOURCE  15 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  16 ORGANISM_COMMON: HUMAN;                                              
SOURCE  17 ORGANISM_TAXID: 9606                                                 
KEYWDS    OXIDOREDUCTASE REPRESSOR COMPLEX, ALTERNATIVE SPLICING,               
KEYWDS   2 OXIDOREDUCTASE, FLAVIN, REPRESSOR, TRANSCRIPTION REGULATION,         
KEYWDS   3 CHROMATIN REMODELLING, HOST-VIRUS INTERACTION, NUCLEAR PROTEIN,      
KEYWDS   4 PHOSPHORYLATION, CHROMATIN REGULATOR, OXIDOREDUCTASE-REPRESSOR       
KEYWDS   5 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.FORNERIS,C.BINDA,A.ADAMO,E.BATTAGLIOLI,A.MATTEVI                    
REVDAT   5   13-DEC-23 2V1D    1       REMARK                                   
REVDAT   4   29-DEC-09 2V1D    1       VERSN                                    
REVDAT   3   24-FEB-09 2V1D    1       VERSN                                    
REVDAT   2   17-JUL-07 2V1D    1       JRNL                                     
REVDAT   1   29-MAY-07 2V1D    0                                                
JRNL        AUTH   F.FORNERIS,C.BINDA,A.ADAMO,E.BATTAGLIOLI,A.MATTEVI           
JRNL        TITL   STRUCTURAL BASIS OF LSD1-COREST SELECTIVITY IN HISTONE H3    
JRNL        TITL 2 RECOGNITION.                                                 
JRNL        REF    J.BIOL.CHEM.                  V. 282 20070 2007              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   17537733                                                     
JRNL        DOI    10.1074/JBC.C700100200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 76.03                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 43224                          
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) : 0.224                           
REMARK   3   R VALUE            (WORKING SET) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 860                             
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) : 3.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.18                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3242                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3250                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 61                           
REMARK   3   BIN FREE R VALUE                    : 0.3780                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6407                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 53                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 84.85                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 6.79000                                              
REMARK   3    B22 (A**2) : -4.24000                                             
REMARK   3    B33 (A**2) : -2.55000                                             
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): 0.432         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.293         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.243         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.687        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.930                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.923                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6594 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8942 ; 1.670 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   812 ; 6.933 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   298 ;37.413 ;24.396       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1153 ;21.988 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    44 ;19.234 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1001 ; 0.107 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4952 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3336 ; 0.263 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4553 ; 0.328 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   269 ; 0.172 ; 0.200       
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):    53 ; 0.257 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     1 ; 0.309 ; 0.200       
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):  4120 ; 0.831 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6559 ; 1.503 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2771 ; 1.710 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2383 ; 2.998 ; 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 2V1D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-MAY-07.                  
REMARK 100 THE DEPOSITION ID IS D_1290032651.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 44088                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.27                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 2IW5                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 80.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 7.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 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+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
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       60.02850            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       90.24800            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      116.69350            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       60.02850            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       90.24800            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      116.69350            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       60.02850            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       90.24800            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      116.69350            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       60.02850            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       90.24800            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      116.69350            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8940 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 37570 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.3 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, LYS 5 TO MET                          
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   123                                                      
REMARK 465     ASP A   124                                                      
REMARK 465     GLU A   125                                                      
REMARK 465     SER A   126                                                      
REMARK 465     LEU A   127                                                      
REMARK 465     ALA A   128                                                      
REMARK 465     ASN A   129                                                      
REMARK 465     LEU A   130                                                      
REMARK 465     SER A   131                                                      
REMARK 465     GLU A   132                                                      
REMARK 465     ASP A   133                                                      
REMARK 465     GLU A   134                                                      
REMARK 465     TYR A   135                                                      
REMARK 465     TYR A   136                                                      
REMARK 465     SER A   137                                                      
REMARK 465     GLU A   138                                                      
REMARK 465     GLU A   139                                                      
REMARK 465     GLU A   140                                                      
REMARK 465     ARG A   141                                                      
REMARK 465     ASN A   142                                                      
REMARK 465     ALA A   143                                                      
REMARK 465     LYS A   144                                                      
REMARK 465     ALA A   145                                                      
REMARK 465     GLU A   146                                                      
REMARK 465     LYS A   147                                                      
REMARK 465     GLU A   148                                                      
REMARK 465     LYS A   149                                                      
REMARK 465     LYS A   150                                                      
REMARK 465     LEU A   151                                                      
REMARK 465     PRO A   152                                                      
REMARK 465     PRO A   153                                                      
REMARK 465     PRO A   154                                                      
REMARK 465     PRO A   155                                                      
REMARK 465     PRO A   156                                                      
REMARK 465     GLN A   157                                                      
REMARK 465     ALA A   158                                                      
REMARK 465     PRO A   159                                                      
REMARK 465     PRO A   160                                                      
REMARK 465     GLU A   161                                                      
REMARK 465     GLU A   162                                                      
REMARK 465     GLU A   163                                                      
REMARK 465     ASN A   164                                                      
REMARK 465     GLU A   165                                                      
REMARK 465     SER A   166                                                      
REMARK 465     GLU A   167                                                      
REMARK 465     PRO A   168                                                      
REMARK 465     GLU A   169                                                      
REMARK 465     GLU A   170                                                      
REMARK 465     PRO A   837                                                      
REMARK 465     ARG A   838                                                      
REMARK 465     GLN A   839                                                      
REMARK 465     ALA A   840                                                      
REMARK 465     THR A   841                                                      
REMARK 465     PRO A   842                                                      
REMARK 465     GLY A   843                                                      
REMARK 465     VAL A   844                                                      
REMARK 465     PRO A   845                                                      
REMARK 465     ALA A   846                                                      
REMARK 465     GLN A   847                                                      
REMARK 465     GLN A   848                                                      
REMARK 465     SER A   849                                                      
REMARK 465     PRO A   850                                                      
REMARK 465     SER A   851                                                      
REMARK 465     MET A   852                                                      
REMARK 465     ARG B   305                                                      
REMARK 465     ALA B   306                                                      
REMARK 465     LYS B   307                                                      
REMARK 465     HIS B   441                                                      
REMARK 465     GLY B   442                                                      
REMARK 465     LYS B   443                                                      
REMARK 465     GLU B   444                                                      
REMARK 465     GLU B   445                                                      
REMARK 465     THR B   446                                                      
REMARK 465     ASN B   447                                                      
REMARK 465     GLY B   448                                                      
REMARK 465     PRO B   449                                                      
REMARK 465     SER B   450                                                      
REMARK 465     ASN B   451                                                      
REMARK 465     GLN B   452                                                      
REMARK 465     LYS B   453                                                      
REMARK 465     PRO B   454                                                      
REMARK 465     VAL B   455                                                      
REMARK 465     LYS B   456                                                      
REMARK 465     SER B   457                                                      
REMARK 465     PRO B   458                                                      
REMARK 465     ASP B   459                                                      
REMARK 465     ASN B   460                                                      
REMARK 465     SER B   461                                                      
REMARK 465     ILE B   462                                                      
REMARK 465     LYS B   463                                                      
REMARK 465     MET B   464                                                      
REMARK 465     PRO B   465                                                      
REMARK 465     GLU B   466                                                      
REMARK 465     GLU B   467                                                      
REMARK 465     GLU B   468                                                      
REMARK 465     ASP B   469                                                      
REMARK 465     GLU B   470                                                      
REMARK 465     ALA B   471                                                      
REMARK 465     PRO B   472                                                      
REMARK 465     VAL B   473                                                      
REMARK 465     LEU B   474                                                      
REMARK 465     ASP B   475                                                      
REMARK 465     VAL B   476                                                      
REMARK 465     ARG B   477                                                      
REMARK 465     TYR B   478                                                      
REMARK 465     ALA B   479                                                      
REMARK 465     SER B   480                                                      
REMARK 465     ALA B   481                                                      
REMARK 465     SER B   482                                                      
REMARK 465     ARG C    17                                                      
REMARK 465     LYS C    18                                                      
REMARK 465     GLN C    19                                                      
REMARK 465     LEU C    20                                                      
REMARK 465     ALA C    21                                                      
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 274   C   -  N   -  CA  ANGL. DEV. =   9.0 DEGREES          
REMARK 500    ARG A 795   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 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    ASN A 224       85.34   -155.37                                   
REMARK 500    ASN A 243       22.98    -64.69                                   
REMARK 500    LEU A 248      -76.11    -53.52                                   
REMARK 500    ILE A 270      -60.17    -95.67                                   
REMARK 500    PRO A 274      102.63    -18.70                                   
REMARK 500    ARG A 316       15.28    -66.13                                   
REMARK 500    LYS A 322      124.52   -172.77                                   
REMARK 500    MET A 332      -31.14   -144.23                                   
REMARK 500    ASN A 350       78.74    -64.68                                   
REMARK 500    TYR A 363       84.19   -156.80                                   
REMARK 500    GLU A 364      168.93    -43.24                                   
REMARK 500    ASP A 375      -60.46    -29.02                                   
REMARK 500    PHE A 398       89.21    -67.37                                   
REMARK 500    ASN A 403      -13.66     84.13                                   
REMARK 500    LEU A 418      -19.36    -48.19                                   
REMARK 500    GLN A 438      -10.34    -38.52                                   
REMARK 500    LYS A 456      -60.73    -26.83                                   
REMARK 500    VAL A 468       91.52    -40.04                                   
REMARK 500    GLN A 501      -29.90    -38.73                                   
REMARK 500    LYS A 507        2.39    -60.42                                   
REMARK 500    GLU A 510      -76.63    -75.54                                   
REMARK 500    GLU A 512      -19.39    -49.61                                   
REMARK 500    ASN A 514       76.99   -110.09                                   
REMARK 500    ALA A 541       50.24     35.05                                   
REMARK 500    THR A 542      147.89   -170.71                                   
REMARK 500    PRO A 543      117.90    -37.49                                   
REMARK 500    GLN A 554       -7.47    -55.41                                   
REMARK 500    ASN A 569       31.81    -98.78                                   
REMARK 500    CYS A 573      -18.25    -35.25                                   
REMARK 500    VAL A 574      -64.81    -94.16                                   
REMARK 500    ARG A 608      -77.71    -71.14                                   
REMARK 500    PHE A 678      126.17   -176.03                                   
REMARK 500    PRO A 701       74.12    -65.25                                   
REMARK 500    ALA A 729      -72.85    -34.71                                   
REMARK 500    ASP A 754      115.41    -39.97                                   
REMARK 500    ALA A 757      -52.62   -124.99                                   
REMARK 500    SER A 760      -55.14   -120.98                                   
REMARK 500    SER A 785      -77.87    -69.04                                   
REMARK 500    ILE A 804       73.38   -118.08                                   
REMARK 500    ARG A 805      -49.50    -20.41                                   
REMARK 500    TYR A 807       48.61   -152.19                                   
REMARK 500    ALA A 809       33.60     39.09                                   
REMARK 500    PRO B 310      176.28    -52.55                                   
REMARK 500    ALA B 326      -41.01    -27.53                                   
REMARK 500    THR B 333      -72.23    -49.57                                   
REMARK 500    ILE B 367       47.78   -105.13                                   
REMARK 500    PRO B 369       29.24    -76.16                                   
REMARK 500    PRO B 373     -177.33    -42.92                                   
REMARK 500    ALA B 391      -73.74    -42.18                                   
REMARK 500    VAL B 392      -38.24    -37.73                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      55 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ALA C   15     PRO C   16                  133.02                    
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 FAD A 1837                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2X0L   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A NEURO-SPECIFIC SPLICING VARIANT OF HUMAN      
REMARK 900 HISTONE LYSINE DEMETHYLASE LSD1.                                     
REMARK 900 RELATED ID: 2UXX   RELATED DB: PDB                                   
REMARK 900 HUMAN LSD1 HISTONE DEMETHYLASE-COREST IN COMPLEX WITH AN FAD-        
REMARK 900 TRANYLCYPROMINE ADDUCT                                               
REMARK 900 RELATED ID: 2IW5   RELATED DB: PDB                                   
REMARK 900 STRUCTURAL BASIS FOR COREST-DEPENDENT DEMETHYLATION OF NUCLEOSOMES   
REMARK 900 BY THE HUMAN LSD1 HISTONE DEMETHYLASE                                
REMARK 900 RELATED ID: 2UXN   RELATED DB: PDB                                   
REMARK 900 STRUCTURAL BASIS OF HISTONE DEMETHYLATION BY LSD1 REVEALED BY        
REMARK 900 SUICIDE INACTIVATION                                                 
REMARK 900 RELATED ID: 2COM   RELATED DB: PDB                                   
REMARK 900 THE SOLUTION STRUCTURE OF THE 33RD FIBRONECTIN TYPE IIIDOMAIN OF     
REMARK 900 HUMAN TENASCIN- X                                                    
REMARK 900 RELATED ID: 2H94   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE AND MECHANISM OF HUMAN LYSINE-SPECIFICDEMETHYLASE- 
REMARK 900 1                                                                    
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 TRUNCATED MUTANT LACKING THE FIRST 122 N-TERMINAL RESIDUES           
REMARK 999 TRUNCATED MUTANT LACKING THE FIRST 304 N-TERMINAL RESIDUES           
REMARK 999 SYNTHETIC PEPTIDE CORRESPONDING TO THE FIRST 21 N-TERMINAL           
REMARK 999 AMINO ACIDS OF HISTONE H3 BEARING POINT MUTATION LYS4MET             
DBREF  2V1D A  123   852  UNP    O60341   KDM1_HUMAN     123    852             
DBREF  2V1D B  305   482  UNP    Q9UKL0   RCOR1_HUMAN    305    482             
DBREF  2V1D C    1    21  UNP    Q16695   H31T_HUMAN       2     22             
SEQADV 2V1D MET C    4  UNP  Q16695    LYS     5 ENGINEERED MUTATION            
SEQRES   1 A  730  MET ASP GLU SER LEU ALA ASN LEU SER GLU ASP GLU TYR          
SEQRES   2 A  730  TYR SER GLU GLU GLU ARG ASN ALA LYS ALA GLU LYS GLU          
SEQRES   3 A  730  LYS LYS LEU PRO PRO PRO PRO PRO GLN ALA PRO PRO GLU          
SEQRES   4 A  730  GLU GLU ASN GLU SER GLU PRO GLU GLU PRO SER GLY VAL          
SEQRES   5 A  730  GLU GLY ALA ALA PHE GLN SER ARG LEU PRO HIS ASP ARG          
SEQRES   6 A  730  MET THR SER GLN GLU ALA ALA CYS PHE PRO ASP ILE ILE          
SEQRES   7 A  730  SER GLY PRO GLN GLN THR GLN LYS VAL PHE LEU PHE ILE          
SEQRES   8 A  730  ARG ASN ARG THR LEU GLN LEU TRP LEU ASP ASN PRO LYS          
SEQRES   9 A  730  ILE GLN LEU THR PHE GLU ALA THR LEU GLN GLN LEU GLU          
SEQRES  10 A  730  ALA PRO TYR ASN SER ASP THR VAL LEU VAL HIS ARG VAL          
SEQRES  11 A  730  HIS SER TYR LEU GLU ARG HIS GLY LEU ILE ASN PHE GLY          
SEQRES  12 A  730  ILE TYR LYS ARG ILE LYS PRO LEU PRO THR LYS LYS THR          
SEQRES  13 A  730  GLY LYS VAL ILE ILE ILE GLY SER GLY VAL SER GLY LEU          
SEQRES  14 A  730  ALA ALA ALA ARG GLN LEU GLN SER PHE GLY MET ASP VAL          
SEQRES  15 A  730  THR LEU LEU GLU ALA ARG ASP ARG VAL GLY GLY ARG VAL          
SEQRES  16 A  730  ALA THR PHE ARG LYS GLY ASN TYR VAL ALA ASP LEU GLY          
SEQRES  17 A  730  ALA MET VAL VAL THR GLY LEU GLY GLY ASN PRO MET ALA          
SEQRES  18 A  730  VAL VAL SER LYS GLN VAL ASN MET GLU LEU ALA LYS ILE          
SEQRES  19 A  730  LYS GLN LYS CYS PRO LEU TYR GLU ALA ASN GLY GLN ALA          
SEQRES  20 A  730  VAL PRO LYS GLU LYS ASP GLU MET VAL GLU GLN GLU PHE          
SEQRES  21 A  730  ASN ARG LEU LEU GLU ALA THR SER TYR LEU SER HIS GLN          
SEQRES  22 A  730  LEU ASP PHE ASN VAL LEU ASN ASN LYS PRO VAL SER LEU          
SEQRES  23 A  730  GLY GLN ALA LEU GLU VAL VAL ILE GLN LEU GLN GLU LYS          
SEQRES  24 A  730  HIS VAL LYS ASP GLU GLN ILE GLU HIS TRP LYS LYS ILE          
SEQRES  25 A  730  VAL LYS THR GLN GLU GLU LEU LYS GLU LEU LEU ASN LYS          
SEQRES  26 A  730  MET VAL ASN LEU LYS GLU LYS ILE LYS GLU LEU HIS GLN          
SEQRES  27 A  730  GLN TYR LYS GLU ALA SER GLU VAL LYS PRO PRO ARG ASP          
SEQRES  28 A  730  ILE THR ALA GLU PHE LEU VAL LYS SER LYS HIS ARG ASP          
SEQRES  29 A  730  LEU THR ALA LEU CYS LYS GLU TYR ASP GLU LEU ALA GLU          
SEQRES  30 A  730  THR GLN GLY LYS LEU GLU GLU LYS LEU GLN GLU LEU GLU          
SEQRES  31 A  730  ALA ASN PRO PRO SER ASP VAL TYR LEU SER SER ARG ASP          
SEQRES  32 A  730  ARG GLN ILE LEU ASP TRP HIS PHE ALA ASN LEU GLU PHE          
SEQRES  33 A  730  ALA ASN ALA THR PRO LEU SER THR LEU SER LEU LYS HIS          
SEQRES  34 A  730  TRP ASP GLN ASP ASP ASP PHE GLU PHE THR GLY SER HIS          
SEQRES  35 A  730  LEU THR VAL ARG ASN GLY TYR SER CYS VAL PRO VAL ALA          
SEQRES  36 A  730  LEU ALA GLU GLY LEU ASP ILE LYS LEU ASN THR ALA VAL          
SEQRES  37 A  730  ARG GLN VAL ARG TYR THR ALA SER GLY CYS GLU VAL ILE          
SEQRES  38 A  730  ALA VAL ASN THR ARG SER THR SER GLN THR PHE ILE TYR          
SEQRES  39 A  730  LYS CYS ASP ALA VAL LEU CYS THR LEU PRO LEU GLY VAL          
SEQRES  40 A  730  LEU LYS GLN GLN PRO PRO ALA VAL GLN PHE VAL PRO PRO          
SEQRES  41 A  730  LEU PRO GLU TRP LYS THR SER ALA VAL GLN ARG MET GLY          
SEQRES  42 A  730  PHE GLY ASN LEU ASN LYS VAL VAL LEU CYS PHE ASP ARG          
SEQRES  43 A  730  VAL PHE TRP ASP PRO SER VAL ASN LEU PHE GLY HIS VAL          
SEQRES  44 A  730  GLY SER THR THR ALA SER ARG GLY GLU LEU PHE LEU PHE          
SEQRES  45 A  730  TRP ASN LEU TYR LYS ALA PRO ILE LEU LEU ALA LEU VAL          
SEQRES  46 A  730  ALA GLY GLU ALA ALA GLY ILE MET GLU ASN ILE SER ASP          
SEQRES  47 A  730  ASP VAL ILE VAL GLY ARG CYS LEU ALA ILE LEU LYS GLY          
SEQRES  48 A  730  ILE PHE GLY SER SER ALA VAL PRO GLN PRO LYS GLU THR          
SEQRES  49 A  730  VAL VAL SER ARG TRP ARG ALA ASP PRO TRP ALA ARG GLY          
SEQRES  50 A  730  SER TYR SER TYR VAL ALA ALA GLY SER SER GLY ASN ASP          
SEQRES  51 A  730  TYR ASP LEU MET ALA GLN PRO ILE THR PRO GLY PRO SER          
SEQRES  52 A  730  ILE PRO GLY ALA PRO GLN PRO ILE PRO ARG LEU PHE PHE          
SEQRES  53 A  730  ALA GLY GLU HIS THR ILE ARG ASN TYR PRO ALA THR VAL          
SEQRES  54 A  730  HIS GLY ALA LEU LEU SER GLY LEU ARG GLU ALA GLY ARG          
SEQRES  55 A  730  ILE ALA ASP GLN PHE LEU GLY ALA MET TYR THR LEU PRO          
SEQRES  56 A  730  ARG GLN ALA THR PRO GLY VAL PRO ALA GLN GLN SER PRO          
SEQRES  57 A  730  SER MET                                                      
SEQRES   1 B  178  ARG ALA LYS ARG LYS PRO PRO LYS GLY MET PHE LEU SER          
SEQRES   2 B  178  GLN GLU ASP VAL GLU ALA VAL SER ALA ASN ALA THR ALA          
SEQRES   3 B  178  ALA THR THR VAL LEU ARG GLN LEU ASP MET GLU LEU VAL          
SEQRES   4 B  178  SER VAL LYS ARG GLN ILE GLN ASN ILE LYS GLN THR ASN          
SEQRES   5 B  178  SER ALA LEU LYS GLU LYS LEU ASP GLY GLY ILE GLU PRO          
SEQRES   6 B  178  TYR ARG LEU PRO GLU VAL ILE GLN LYS CYS ASN ALA ARG          
SEQRES   7 B  178  TRP THR THR GLU GLU GLN LEU LEU ALA VAL GLN ALA ILE          
SEQRES   8 B  178  ARG LYS TYR GLY ARG ASP PHE GLN ALA ILE SER ASP VAL          
SEQRES   9 B  178  ILE GLY ASN LYS SER VAL VAL GLN VAL LYS ASN PHE PHE          
SEQRES  10 B  178  VAL ASN TYR ARG ARG ARG PHE ASN ILE ASP GLU VAL LEU          
SEQRES  11 B  178  GLN GLU TRP GLU ALA GLU HIS GLY LYS GLU GLU THR ASN          
SEQRES  12 B  178  GLY PRO SER ASN GLN LYS PRO VAL LYS SER PRO ASP ASN          
SEQRES  13 B  178  SER ILE LYS MET PRO GLU GLU GLU ASP GLU ALA PRO VAL          
SEQRES  14 B  178  LEU ASP VAL ARG TYR ALA SER ALA SER                          
SEQRES   1 C   21  ALA ARG THR MET GLN THR ALA ARG LYS SER THR GLY GLY          
SEQRES   2 C   21  LYS ALA PRO ARG LYS GLN LEU ALA                              
HET    FAD  A1837      53                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
FORMUL   4  FAD    C27 H33 N9 O15 P2                                            
HELIX    1   1 GLY A  173  SER A  181  1                                   9    
HELIX    2   2 THR A  189  PHE A  196  1                                   8    
HELIX    3   3 PHE A  196  GLY A  202  1                                   7    
HELIX    4   4 PRO A  203  ASN A  224  1                                  22    
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  VAL A  349  1                                  10    
HELIX   10  10 PRO A  371  GLN A  395  1                                  25    
HELIX   11  11 SER A  407  VAL A  468  1                                  62    
HELIX   12  12 ASP A  473  GLU A  512  1                                  40    
HELIX   13  13 SER A  522  ASN A  540  1                                  19    
HELIX   14  14 ASP A  555  GLU A  559  5                                   5    
HELIX   15  15 SER A  572  GLU A  580  1                                   9    
HELIX   16  16 PRO A  626  GLN A  632  1                                   7    
HELIX   17  17 PRO A  644  MET A  654  1                                  11    
HELIX   18  18 ALA A  708  GLU A  716  1                                   9    
HELIX   19  19 SER A  719  GLY A  736  1                                  18    
HELIX   20  20 SER A  769  GLN A  778  1                                  10    
HELIX   21  21 GLY A  800  ILE A  804  5                                   5    
HELIX   22  22 THR A  810  LEU A  830  1                                  21    
HELIX   23  23 ALA A  832  LEU A  836  5                                   5    
HELIX   24  24 SER B  317  ALA B  326  1                                  10    
HELIX   25  25 THR B  329  LEU B  363  1                                  35    
HELIX   26  26 ILE B  367  ARG B  371  5                                   5    
HELIX   27  27 THR B  384  GLY B  399  1                                  16    
HELIX   28  28 ASP B  401  GLY B  410  1                                  10    
HELIX   29  29 SER B  413  TYR B  424  1                                  12    
HELIX   30  30 ASN B  429  ALA B  439  1                                  11    
HELIX   31  31 ALA C    1  GLN C    5  5                                   5    
SHEET    1  AA 5 ILE A 584  LYS A 585  0                                        
SHEET    2  AA 5 ASP A 303  LEU A 307  1  O  LEU A 306   N  LYS A 585           
SHEET    3  AA 5 LYS A 280  ILE A 284  1  O  VAL A 281   N  THR A 305           
SHEET    4  AA 5 ALA A 620  CYS A 623  1  O  ALA A 620   N  ILE A 282           
SHEET    5  AA 5 LEU A 796  PHE A 798  1  O  PHE A 797   N  CYS A 623           
SHEET    1  AB 2 THR A 319  LYS A 322  0                                        
SHEET    2  AB 2 TYR A 325  ASP A 328 -1  O  TYR A 325   N  LYS A 322           
SHEET    1  AC 3 VAL A 333  VAL A 334  0                                        
SHEET    2  AC 3 LEU A 565  VAL A 567 -1  O  LEU A 565   N  VAL A 334           
SHEET    3  AC 3 LEU A 353  LYS A 355 -1  O  ALA A 354   N  THR A 566           
SHEET    1  AD 2 VAL A 400  LEU A 401  0                                        
SHEET    2  AD 2 LYS A 404  PRO A 405 -1  O  LYS A 404   N  LEU A 401           
SHEET    1  AE 4 THR A 613  CYS A 618  0                                        
SHEET    2  AE 4 GLY A 599  ASN A 606 -1  O  CYS A 600   N  CYS A 618           
SHEET    3  AE 4 THR A 588  THR A 596 -1  O  ALA A 589   N  VAL A 605           
SHEET    4  AE 4 GLN A 638  VAL A 640  1  O  GLN A 638   N  VAL A 593           
SHEET    1  AF 2 GLY A 655  PHE A 656  0                                        
SHEET    2  AF 2 SER A 762  TYR A 763 -1  O  TYR A 763   N  GLY A 655           
SHEET    1  AG 5 LEU A 677  GLY A 679  0                                        
SHEET    2  AG 5 LEU A 693  ASN A 696 -1  O  PHE A 694   N  PHE A 678           
SHEET    3  AG 5 ILE A 702  VAL A 707 -1  O  LEU A 704   N  TRP A 695           
SHEET    4  AG 5 ASN A 660  CYS A 665 -1  O  ASN A 660   N  VAL A 707           
SHEET    5  AG 5 GLU A 745  VAL A 748 -1  O  GLU A 745   N  CYS A 665           
CISPEP   1 ALA A  240    PRO A  241          0         2.94                     
CISPEP   2 PRO A  470    PRO A  471          0         2.63                     
CISPEP   3 GLN A  633    PRO A  634          0         2.26                     
CISPEP   4 VAL A  640    PRO A  641          0         3.04                     
SITE     1 AC1 30 GLY A 285  GLY A 287  VAL A 288  SER A 289                    
SITE     2 AC1 30 LEU A 307  GLU A 308  ALA A 309  ARG A 310                    
SITE     3 AC1 30 GLY A 315  ARG A 316  LEU A 329  GLY A 330                    
SITE     4 AC1 30 ALA A 331  MET A 332  VAL A 333  THR A 588                    
SITE     5 AC1 30 VAL A 590  THR A 624  LEU A 625  PRO A 626                    
SITE     6 AC1 30 TRP A 756  SER A 760  TYR A 761  GLY A 800                    
SITE     7 AC1 30 GLU A 801  ALA A 809  THR A 810  VAL A 811                    
SITE     8 AC1 30 ALA A 814  MET C   4                                          
CRYST1  120.057  180.496  233.387  90.00  90.00  90.00 I 2 2 2       8          
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      0.008329  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005540  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004285        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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