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Database: PDB
Entry: 2X0L
LinkDB: 2X0L
Original site: 2X0L 
HEADER    TRANSCRIPTION                           15-DEC-09   2X0L              
TITLE     CRYSTAL STRUCTURE OF A NEURO-SPECIFIC SPLICING VARIANT OF HUMAN       
TITLE    2 HISTONE LYSINE DEMETHYLASE LSD1.                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LYSINE-SPECIFIC HISTONE DEMETHYLASE 1;                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: FLAVIN-CONTAINING AMINE OXIDASE DOMAIN-CONTAINING PROTEIN 2,
COMPND   5 BRAF35-HDAC COMPLEX PROTEIN BHC110;                                  
COMPND   6 EC: 1.-.-.-;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: REST COREPRESSOR 1;                                        
COMPND  10 CHAIN: B;                                                            
COMPND  11 SYNONYM: PROTEIN COREST, COREPRESSOR COREST;                         
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: HISTONE H3 PEPTIDE;                                        
COMPND  15 CHAIN: C;                                                            
COMPND  16 FRAGMENT: RESIDUES 2-17;                                             
COMPND  17 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: 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    REPRESSOR COMPLEX, CHROMATIN REMODELLING, AMINE OXIDASE,              
KEYWDS   2 TRANSCRIPTION, HOST-VIRUS INTERACTION, TRANSCRIPTION REGULATION,     
KEYWDS   3 PHOSPHOPROTEIN, OXIDOREDUCTASE, NUCLEAR PROTEIN, CHROMATIN           
KEYWDS   4 REGULATOR, DEVELOPMENTAL PROTEIN                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.ZIBETTI,A.ADAMO,C.BINDA,F.FORNERIS,C.VERPELLI,E.GINELLI,A.MATTEVI,  
AUTHOR   2 C.SALA,E.BATTAGLIOLI                                                 
REVDAT   3   20-DEC-23 2X0L    1       REMARK                                   
REVDAT   2   14-DEC-16 2X0L    1       COMPND SOURCE REMARK VERSN               
REVDAT   2 2                   1       DBREF  SEQADV                            
REVDAT   1   02-MAR-10 2X0L    0                                                
JRNL        AUTH   C.ZIBETTI,A.ADAMO,C.BINDA,F.FORNERIS,E.TOFFOLO,C.VERPELLI,   
JRNL        AUTH 2 E.GINELLI,A.MATTEVI,C.SALA,E.BATTAGLIOLI                     
JRNL        TITL   ALTERNATIVE SPLICING OF THE HISTONE DEMETHYLASE LSD1/KDM1    
JRNL        TITL 2 CONTRIBUTES TO THE MODULATION OF NEURITE MORPHOGENESIS IN    
JRNL        TITL 3 THE MAMMALIAN NERVOUS SYSTEM.                                
JRNL        REF    J.NEUROSCI.                   V.  30  2521 2010              
JRNL        REFN                   ISSN 0270-6474                               
JRNL        PMID   20164337                                                     
JRNL        DOI    10.1523/JNEUROSCI.5500-09.2010                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.4.0078                                      
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) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 71.50                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 49397                          
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) : 0.213                           
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 960                             
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) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.08                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3635                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.65                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3130                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 67                           
REMARK   3   BIN FREE R VALUE                    : 0.3210                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6438                                    
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) : 64.13                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.37000                                              
REMARK   3    B22 (A**2) : -3.03000                                             
REMARK   3    B33 (A**2) : -1.34000                                             
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): 0.339         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.277         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.217         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.819        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.928                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.868                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6625 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8984 ; 1.571 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   816 ; 6.895 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   299 ;37.450 ;24.415       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1160 ;21.296 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    44 ;20.361 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1007 ; 0.103 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4973 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4082 ; 0.727 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6593 ; 1.396 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2543 ; 1.716 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2391 ; 3.079 ; 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   : 1.20                                          
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 2X0L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-DEC-09.                  
REMARK 100 THE DEPOSITION ID IS D_1290042093.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49397                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 70.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.11300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 2IW5                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 78.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.70                     
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       59.84500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       90.60500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      116.72500            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       59.84500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       90.60500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      116.72500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       59.84500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       90.60500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      116.72500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       59.84500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       90.60500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      116.72500            
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: 9020 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 38130 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.7 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 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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD1  ASN A   660     OG   SER A   749              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 635   C   -  N   -  CA  ANGL. DEV. =  10.2 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    PHE A 196       50.67   -147.20                                   
REMARK 500    ASN A 224       86.03   -164.51                                   
REMARK 500    SER A 244      -71.28    -70.39                                   
REMARK 500    PRO A 274      128.27    -28.91                                   
REMARK 500    SER A 286       47.87   -108.18                                   
REMARK 500    LYS A 322      111.11    168.74                                   
REMARK 500    MET A 332      -29.11   -142.66                                   
REMARK 500    THR A 335       56.15    -90.92                                   
REMARK 500    ASN A 350       74.32    -52.52                                   
REMARK 500    ASN A 366       65.57   -116.20                                   
REMARK 500    ALA A 369     -161.28    -62.15                                   
REMARK 500    LYS A 372        0.42    -51.73                                   
REMARK 500    ASN A 402       36.69     77.67                                   
REMARK 500    GLN A 438       -6.78    -55.58                                   
REMARK 500    SER A 466      -38.31   -130.95                                   
REMARK 500    GLU A 467      -79.30     61.87                                   
REMARK 500    VAL A 468       96.23    -69.83                                   
REMARK 500    TYR A 494       -8.06    -56.18                                   
REMARK 500    LYS A 503      -76.89    -49.36                                   
REMARK 500    GLU A 510      -81.58    -64.19                                   
REMARK 500    ASN A 514       68.84   -107.91                                   
REMARK 500    ALA A 541       58.01     35.37                                   
REMARK 500    THR A 542      146.25   -174.83                                   
REMARK 500    PRO A 543      121.58    -37.07                                   
REMARK 500    ASN A 587       28.98     45.96                                   
REMARK 500    THR A 610       21.64    -76.35                                   
REMARK 500    ASN A 717       34.83    -89.63                                   
REMARK 500    ALA A 729      -75.79    -43.75                                   
REMARK 500    SER A 737      -33.46    -26.09                                   
REMARK 500    ALA A 757      -59.82   -138.28                                   
REMARK 500    SER A 768     -167.44   -105.97                                   
REMARK 500    SER A 785      -74.27    -61.89                                   
REMARK 500    GLN A 791      121.25    -35.37                                   
REMARK 500    ILE A 793      147.27    -21.49                                   
REMARK 500    TYR A 807       45.71   -145.30                                   
REMARK 500    ALA A 809       14.65     49.84                                   
REMARK 500    TYR A 834       -4.16    -51.46                                   
REMARK 500    PRO B 310      173.57    -53.03                                   
REMARK 500    ALA B 326      -19.77    -44.14                                   
REMARK 500    MET B 340      -60.19    -90.80                                   
REMARK 500    GLU B 341      -35.31    -31.99                                   
REMARK 500    LEU B 363        7.01    -67.95                                   
REMARK 500    PRO B 369       22.80    -73.35                                   
REMARK 500    PRO B 373      147.05    -31.52                                   
REMARK 500    ASP B 401       72.01    -67.69                                   
REMARK 500    ASN B 429       61.44     13.00                                   
REMARK 500    ALA B 439       12.47    -60.33                                   
REMARK 500    THR C  11      -35.86   -137.65                                   
REMARK 500    ALA C  15       66.10   -103.45                                   
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 PRO A  274     THR A  275                 -147.23                    
REMARK 500 SER A  466     GLU A  467                   51.74                    
REMARK 500 PRO A  792     ILE A  793                  145.40                    
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 900                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
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: 2V1D   RELATED DB: PDB                                   
REMARK 900 STRUCTURAL BASIS OF LSD1-COREST SELECTIVITY IN HISTONE H3            
REMARK 900 RECOGNITION                                                          
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 SPLICING VARIANT FORM OF THE PROTEIN LSD1: BETWEEN                   
REMARK 999 RESIDUE 369 AND 370 OF CHAIN A THERE ARE 4 ADDITIONAL (DTVK)         
REMARK 999 RESIDUES THAT HAVE BEEN MARKED AS 369A, 369B, 369C, 369D.            
DBREF  2X0L A  123   852  UNP    O60341   KDM1_HUMAN     123    852             
DBREF  2X0L B  308   440  UNP    Q9UKL0   RCOR1_HUMAN    308    440             
DBREF  2X0L C    1    16  UNP    Q5TEC6   Q5TEC6_HUMAN     2     17             
SEQADV 2X0L ASP A  369A UNP  O60341              INSERTION                      
SEQADV 2X0L THR A  369B UNP  O60341              INSERTION                      
SEQADV 2X0L VAL A  369C UNP  O60341              INSERTION                      
SEQADV 2X0L LYS A  369D UNP  O60341              INSERTION                      
SEQADV 2X0L MET C    4  UNP  Q5TEC6    LYS     5 ENGINEERED MUTATION            
SEQRES   1 A  734  MET ASP GLU SER LEU ALA ASN LEU SER GLU ASP GLU TYR          
SEQRES   2 A  734  TYR SER GLU GLU GLU ARG ASN ALA LYS ALA GLU LYS GLU          
SEQRES   3 A  734  LYS LYS LEU PRO PRO PRO PRO PRO GLN ALA PRO PRO GLU          
SEQRES   4 A  734  GLU GLU ASN GLU SER GLU PRO GLU GLU PRO SER GLY VAL          
SEQRES   5 A  734  GLU GLY ALA ALA PHE GLN SER ARG LEU PRO HIS ASP ARG          
SEQRES   6 A  734  MET THR SER GLN GLU ALA ALA CYS PHE PRO ASP ILE ILE          
SEQRES   7 A  734  SER GLY PRO GLN GLN THR GLN LYS VAL PHE LEU PHE ILE          
SEQRES   8 A  734  ARG ASN ARG THR LEU GLN LEU TRP LEU ASP ASN PRO LYS          
SEQRES   9 A  734  ILE GLN LEU THR PHE GLU ALA THR LEU GLN GLN LEU GLU          
SEQRES  10 A  734  ALA PRO TYR ASN SER ASP THR VAL LEU VAL HIS ARG VAL          
SEQRES  11 A  734  HIS SER TYR LEU GLU ARG HIS GLY LEU ILE ASN PHE GLY          
SEQRES  12 A  734  ILE TYR LYS ARG ILE LYS PRO LEU PRO THR LYS LYS THR          
SEQRES  13 A  734  GLY LYS VAL ILE ILE ILE GLY SER GLY VAL SER GLY LEU          
SEQRES  14 A  734  ALA ALA ALA ARG GLN LEU GLN SER PHE GLY MET ASP VAL          
SEQRES  15 A  734  THR LEU LEU GLU ALA ARG ASP ARG VAL GLY GLY ARG VAL          
SEQRES  16 A  734  ALA THR PHE ARG LYS GLY ASN TYR VAL ALA ASP LEU GLY          
SEQRES  17 A  734  ALA MET VAL VAL THR GLY LEU GLY GLY ASN PRO MET ALA          
SEQRES  18 A  734  VAL VAL SER LYS GLN VAL ASN MET GLU LEU ALA LYS ILE          
SEQRES  19 A  734  LYS GLN LYS CYS PRO LEU TYR GLU ALA ASN GLY GLN ALA          
SEQRES  20 A  734  ASP THR VAL LYS VAL PRO LYS GLU LYS ASP GLU MET VAL          
SEQRES  21 A  734  GLU GLN GLU PHE ASN ARG LEU LEU GLU ALA THR SER TYR          
SEQRES  22 A  734  LEU SER HIS GLN LEU ASP PHE ASN VAL LEU ASN ASN LYS          
SEQRES  23 A  734  PRO VAL SER LEU GLY GLN ALA LEU GLU VAL VAL ILE GLN          
SEQRES  24 A  734  LEU GLN GLU LYS HIS VAL LYS ASP GLU GLN ILE GLU HIS          
SEQRES  25 A  734  TRP LYS LYS ILE VAL LYS THR GLN GLU GLU LEU LYS GLU          
SEQRES  26 A  734  LEU LEU ASN LYS MET VAL ASN LEU LYS GLU LYS ILE LYS          
SEQRES  27 A  734  GLU LEU HIS GLN GLN TYR LYS GLU ALA SER GLU VAL LYS          
SEQRES  28 A  734  PRO PRO ARG ASP ILE THR ALA GLU PHE LEU VAL LYS SER          
SEQRES  29 A  734  LYS HIS ARG ASP LEU THR ALA LEU CYS LYS GLU TYR ASP          
SEQRES  30 A  734  GLU LEU ALA GLU THR GLN GLY LYS LEU GLU GLU LYS LEU          
SEQRES  31 A  734  GLN GLU LEU GLU ALA ASN PRO PRO SER ASP VAL TYR LEU          
SEQRES  32 A  734  SER SER ARG ASP ARG GLN ILE LEU ASP TRP HIS PHE ALA          
SEQRES  33 A  734  ASN LEU GLU PHE ALA ASN ALA THR PRO LEU SER THR LEU          
SEQRES  34 A  734  SER LEU LYS HIS TRP ASP GLN ASP ASP ASP PHE GLU PHE          
SEQRES  35 A  734  THR GLY SER HIS LEU THR VAL ARG ASN GLY TYR SER CYS          
SEQRES  36 A  734  VAL PRO VAL ALA LEU ALA GLU GLY LEU ASP ILE LYS LEU          
SEQRES  37 A  734  ASN THR ALA VAL ARG GLN VAL ARG TYR THR ALA SER GLY          
SEQRES  38 A  734  CYS GLU VAL ILE ALA VAL ASN THR ARG SER THR SER GLN          
SEQRES  39 A  734  THR PHE ILE TYR LYS CYS ASP ALA VAL LEU CYS THR LEU          
SEQRES  40 A  734  PRO LEU GLY VAL LEU LYS GLN GLN PRO PRO ALA VAL GLN          
SEQRES  41 A  734  PHE VAL PRO PRO LEU PRO GLU TRP LYS THR SER ALA VAL          
SEQRES  42 A  734  GLN ARG MET GLY PHE GLY ASN LEU ASN LYS VAL VAL LEU          
SEQRES  43 A  734  CYS PHE ASP ARG VAL PHE TRP ASP PRO SER VAL ASN LEU          
SEQRES  44 A  734  PHE GLY HIS VAL GLY SER THR THR ALA SER ARG GLY GLU          
SEQRES  45 A  734  LEU PHE LEU PHE TRP ASN LEU TYR LYS ALA PRO ILE LEU          
SEQRES  46 A  734  LEU ALA LEU VAL ALA GLY GLU ALA ALA GLY ILE MET GLU          
SEQRES  47 A  734  ASN ILE SER ASP ASP VAL ILE VAL GLY ARG CYS LEU ALA          
SEQRES  48 A  734  ILE LEU LYS GLY ILE PHE GLY SER SER ALA VAL PRO GLN          
SEQRES  49 A  734  PRO LYS GLU THR VAL VAL SER ARG TRP ARG ALA ASP PRO          
SEQRES  50 A  734  TRP ALA ARG GLY SER TYR SER TYR VAL ALA ALA GLY SER          
SEQRES  51 A  734  SER GLY ASN ASP TYR ASP LEU MET ALA GLN PRO ILE THR          
SEQRES  52 A  734  PRO GLY PRO SER ILE PRO GLY ALA PRO GLN PRO ILE PRO          
SEQRES  53 A  734  ARG LEU PHE PHE ALA GLY GLU HIS THR ILE ARG ASN TYR          
SEQRES  54 A  734  PRO ALA THR VAL HIS GLY ALA LEU LEU SER GLY LEU ARG          
SEQRES  55 A  734  GLU ALA GLY ARG ILE ALA ASP GLN PHE LEU GLY ALA MET          
SEQRES  56 A  734  TYR THR LEU PRO ARG GLN ALA THR PRO GLY VAL PRO ALA          
SEQRES  57 A  734  GLN GLN SER PRO SER MET                                      
SEQRES   1 B  133  ARG LYS PRO PRO LYS GLY MET PHE LEU SER GLN GLU ASP          
SEQRES   2 B  133  VAL GLU ALA VAL SER ALA ASN ALA THR ALA ALA THR THR          
SEQRES   3 B  133  VAL LEU ARG GLN LEU ASP MET GLU LEU VAL SER VAL LYS          
SEQRES   4 B  133  ARG GLN ILE GLN ASN ILE LYS GLN THR ASN SER ALA LEU          
SEQRES   5 B  133  LYS GLU LYS LEU ASP GLY GLY ILE GLU PRO TYR ARG LEU          
SEQRES   6 B  133  PRO GLU VAL ILE GLN LYS CYS ASN ALA ARG TRP THR THR          
SEQRES   7 B  133  GLU GLU GLN LEU LEU ALA VAL GLN ALA ILE ARG LYS TYR          
SEQRES   8 B  133  GLY ARG ASP PHE GLN ALA ILE SER ASP VAL ILE GLY ASN          
SEQRES   9 B  133  LYS SER VAL VAL GLN VAL LYS ASN PHE PHE VAL ASN TYR          
SEQRES  10 B  133  ARG ARG ARG PHE ASN ILE ASP GLU VAL LEU GLN GLU TRP          
SEQRES  11 B  133  GLU ALA GLU                                                  
SEQRES   1 C   16  ALA ARG THR MET GLN THR ALA ARG LYS SER THR GLY GLY          
SEQRES   2 C   16  LYS ALA PRO                                                  
HET    FAD  A 900      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  ASP A  223  1                                  21    
HELIX    5   5 THR A  230  GLN A  237  1                                   8    
HELIX    6   6 ASP A  245  HIS A  259  1                                  15    
HELIX    7   7 GLY A  287  PHE A  300  1                                  14    
HELIX    8   8 ASN A  340  VAL A  349  1                                  10    
HELIX    9   9 GLU A  373  GLN A  395  1                                  23    
HELIX   10  10 SER A  407  ALA A  465  1                                  59    
HELIX   11  11 ASP A  473  GLU A  512  1                                  40    
HELIX   12  12 SER A  522  ASN A  540  1                                  19    
HELIX   13  13 ASP A  555  GLU A  559  5                                   5    
HELIX   14  14 SER A  572  GLU A  580  1                                   9    
HELIX   15  15 PRO A  626  LYS A  631  1                                   6    
HELIX   16  16 PRO A  644  MET A  654  1                                  11    
HELIX   17  17 THR A  684  ARG A  688  5                                   5    
HELIX   18  18 ALA A  708  MET A  715  1                                   8    
HELIX   19  19 GLU A  716  ILE A  718  5                                   3    
HELIX   20  20 SER A  719  GLY A  736  1                                  18    
HELIX   21  21 ASN A  771  GLN A  778  1                                   8    
HELIX   22  22 GLY A  800  ILE A  804  5                                   5    
HELIX   23  23 THR A  810  GLY A  831  1                                  22    
HELIX   24  24 ALA A  832  LEU A  836  5                                   5    
HELIX   25  25 SER B  317  VAL B  324  1                                   8    
HELIX   26  26 THR B  329  LEU B  363  1                                  35    
HELIX   27  27 ILE B  367  ARG B  371  5                                   5    
HELIX   28  28 THR B  384  GLY B  399  1                                  16    
HELIX   29  29 ASP B  401  GLY B  410  1                                  10    
HELIX   30  30 SER B  413  TYR B  424  1                                  12    
HELIX   31  31 ASN B  429  ALA B  439  1                                  11    
HELIX   32  32 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 TYR A 363  GLU A 364  0                                        
SHEET    2  AD 2 VAL A 369C LYS A 369D-1  O  VAL A 369C  N  GLU A 364           
SHEET    1  AE 4 SER A 609  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  TRP A 695 -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        -5.29                     
CISPEP   2 PRO A  470    PRO A  471          0         4.20                     
CISPEP   3 GLN A  633    PRO A  634          0        10.69                     
CISPEP   4 VAL A  640    PRO A  641          0        -1.39                     
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 314  GLY A 315  ARG A 316  LEU A 329                    
SITE     4 AC1 30 GLY A 330  ALA A 331  MET A 332  VAL A 333                    
SITE     5 AC1 30 THR A 588  VAL A 590  THR A 624  LEU A 625                    
SITE     6 AC1 30 PRO A 626  TRP A 756  SER A 760  TYR A 761                    
SITE     7 AC1 30 GLY A 800  GLU A 801  ALA A 809  THR A 810                    
SITE     8 AC1 30 VAL A 811  MET C   4                                          
CRYST1  119.690  181.210  233.450  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      0.008355  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005518  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004284        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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