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Database: PDB
Entry: 1N6A
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Original site: 1N6A 
HEADER    TRANSFERASE                             09-NOV-02   1N6A              
TITLE     STRUCTURE OF SET7/9                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SET DOMAIN-CONTAINING PROTEIN 7;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 108-366;                                          
COMPND   5 SYNONYM: SET7/9 METHYLTRANSFERASE;                                   
COMPND   6 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 EXPRESSION_SYSTEM_STRAIN: B834;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET-28A                                   
KEYWDS    PROTEIN-LIGAND COMPLEX, TRANSFERASE                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.W.KWON,J.H.CHANG,E.KWAK,C.W.LEE,A.JOACHIMIAK,Y.C.KIM,               
AUTHOR   2 J.LEE,Y.CHO                                                          
REVDAT   2   24-FEB-09 1N6A    1       VERSN                                    
REVDAT   1   04-FEB-03 1N6A    0                                                
JRNL        AUTH   T.KWON,J.H.CHANG,E.KWAK,C.W.LEE,A.JOACHIMIAK,                
JRNL        AUTH 2 Y.C.KIM,J.LEE,Y.CHO                                          
JRNL        TITL   MECHANISM OF HISTONE LYSINE METHYL TRANSFER                  
JRNL        TITL 2 REVEALED BY THE STRUCTURE OF SET7/9-ADOMET                   
JRNL        REF    EMBO J.                       V.  22   292 2003              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   12514135                                                     
JRNL        DOI    10.1093/EMBOJ/CDG025                                         
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.98                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 409242.100                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 29506                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.194                           
REMARK   3   FREE R VALUE                     : 0.217                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2713                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.81                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.20                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 8198                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2200                       
REMARK   3   BIN FREE R VALUE                    : 0.2540                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 415                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.012                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1834                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 27                                      
REMARK   3   SOLVENT ATOMS            : 212                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 14.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.08000                                              
REMARK   3    B22 (A**2) : -0.35000                                             
REMARK   3    B33 (A**2) : -1.73000                                             
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.18                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.09                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.21                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.12                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.90                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.310 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.090 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.100 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.110 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.43                                                 
REMARK   3   BSOL        : 64.28                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : FSAM.PARAM                                     
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : FSAM.TOP                                       
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1N6A COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-NOV-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB017571.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 103                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792, 0.9791, 0.9464             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29713                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
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: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.31                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG6000, TRIS-HCL, DTT, PH 8.0,          
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       51.11550            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       19.33400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       51.11550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       19.33400            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   108                                                      
REMARK 465     GLN A   109                                                      
REMARK 465     TYR A   110                                                      
REMARK 465     LYS A   111                                                      
REMARK 465     ASP A   112                                                      
REMARK 465     ASN A   113                                                      
REMARK 465     ILE A   114                                                      
REMARK 465     ARG A   115                                                      
REMARK 465     ASP A   338                                                      
REMARK 465     HIS A   339                                                      
REMARK 465     SER A   340                                                      
REMARK 465     PRO A   341                                                      
REMARK 465     PRO A   342                                                      
REMARK 465     GLY A   343                                                      
REMARK 465     LYS A   344                                                      
REMARK 465     SER A   345                                                      
REMARK 465     GLY A   346                                                      
REMARK 465     PRO A   347                                                      
REMARK 465     GLU A   348                                                      
REMARK 465     ALA A   349                                                      
REMARK 465     ALA A   362                                                      
REMARK 465     THR A   363                                                      
REMARK 465     GLN A   364                                                      
REMARK 465     GLN A   365                                                      
REMARK 465     LYS A   366                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     TRP A 260    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 260    CZ3  CH2                                            
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 134     -178.63    -63.90                                   
REMARK 500    ARG A 152      -47.62   -138.81                                   
REMARK 500    ASP A 194       50.69   -145.55                                   
REMARK 500    THR A 197     -168.54   -123.39                                   
REMARK 500    ALA A 261       -9.66    -59.41                                   
REMARK 500    GLU A 279      -71.57    -10.58                                   
REMARK 500    CYS A 288       18.87   -142.12                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1102        DISTANCE = 12.15 ANGSTROMS                       
REMARK 525    HOH A1241        DISTANCE = 10.09 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAM A 402                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1N6C   RELATED DB: PDB                                   
REMARK 900 RESIDUES 70-366 OF THE SAME PROTEIN                                  
DBREF  1N6A A  108   366  UNP    Q8WTS6   SET7_HUMAN     108    366             
SEQADV 1N6A MSE A  139  UNP  Q8WTS6    MET   139 MODIFIED RESIDUE               
SEQADV 1N6A MSE A  164  UNP  Q8WTS6    MET   164 MODIFIED RESIDUE               
SEQADV 1N6A MSE A  173  UNP  Q8WTS6    MET   173 MODIFIED RESIDUE               
SEQADV 1N6A MSE A  185  UNP  Q8WTS6    MET   185 MODIFIED RESIDUE               
SEQADV 1N6A MSE A  242  UNP  Q8WTS6    MET   242 MODIFIED RESIDUE               
SEQADV 1N6A MSE A  307  UNP  Q8WTS6    MET   307 MODIFIED RESIDUE               
SEQRES   1 A  259  GLY GLN TYR LYS ASP ASN ILE ARG HIS GLY VAL CYS TRP          
SEQRES   2 A  259  ILE TYR TYR PRO ASP GLY GLY SER LEU VAL GLY GLU VAL          
SEQRES   3 A  259  ASN GLU ASP GLY GLU MSE THR GLY GLU LYS ILE ALA TYR          
SEQRES   4 A  259  VAL TYR PRO ASP GLU ARG THR ALA LEU TYR GLY LYS PHE          
SEQRES   5 A  259  ILE ASP GLY GLU MSE ILE GLU GLY LYS LEU ALA THR LEU          
SEQRES   6 A  259  MSE SER THR GLU GLU GLY ARG PRO HIS PHE GLU LEU MSE          
SEQRES   7 A  259  PRO GLY ASN SER VAL TYR HIS PHE ASP LYS SER THR SER          
SEQRES   8 A  259  SER CYS ILE SER THR ASN ALA LEU LEU PRO ASP PRO TYR          
SEQRES   9 A  259  GLU SER GLU ARG VAL TYR VAL ALA GLU SER LEU ILE SER          
SEQRES  10 A  259  SER ALA GLY GLU GLY LEU PHE SER LYS VAL ALA VAL GLY          
SEQRES  11 A  259  PRO ASN THR VAL MSE SER PHE TYR ASN GLY VAL ARG ILE          
SEQRES  12 A  259  THR HIS GLN GLU VAL ASP SER ARG ASP TRP ALA LEU ASN          
SEQRES  13 A  259  GLY ASN THR LEU SER LEU ASP GLU GLU THR VAL ILE ASP          
SEQRES  14 A  259  VAL PRO GLU PRO TYR ASN HIS VAL SER LYS TYR CYS ALA          
SEQRES  15 A  259  SER LEU GLY HIS LYS ALA ASN HIS SER PHE THR PRO ASN          
SEQRES  16 A  259  CYS ILE TYR ASP MSE PHE VAL HIS PRO ARG PHE GLY PRO          
SEQRES  17 A  259  ILE LYS CYS ILE ARG THR LEU ARG ALA VAL GLU ALA ASP          
SEQRES  18 A  259  GLU GLU LEU THR VAL ALA TYR GLY TYR ASP HIS SER PRO          
SEQRES  19 A  259  PRO GLY LYS SER GLY PRO GLU ALA PRO GLU TRP TYR GLN          
SEQRES  20 A  259  VAL GLU LEU LYS ALA PHE GLN ALA THR GLN GLN LYS              
MODRES 1N6A MSE A  139  MET  SELENOMETHIONINE                                   
MODRES 1N6A MSE A  164  MET  SELENOMETHIONINE                                   
MODRES 1N6A MSE A  173  MET  SELENOMETHIONINE                                   
MODRES 1N6A MSE A  185  MET  SELENOMETHIONINE                                   
MODRES 1N6A MSE A  242  MET  SELENOMETHIONINE                                   
MODRES 1N6A MSE A  307  MET  SELENOMETHIONINE                                   
HET    MSE  A 139       8                                                       
HET    MSE  A 164       8                                                       
HET    MSE  A 173       8                                                       
HET    MSE  A 185       8                                                       
HET    MSE  A 242       8                                                       
HET    MSE  A 307       8                                                       
HET    SAM  A 402      27                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
FORMUL   1  MSE    6(C5 H11 N O2 SE)                                            
FORMUL   2  SAM    C15 H22 N6 O5 S                                              
FORMUL   3  HOH   *212(H2 O)                                                    
HELIX    1   1 ASP A  209  GLU A  214  1                                   6    
HELIX    2   2 THR A  251  ARG A  258  1                                   8    
HELIX    3   3 PRO A  278  HIS A  283  5                                   6    
HELIX    4   4 LEU A  291  ALA A  295  5                                   5    
HELIX    5   5 PRO A  350  GLN A  361  1                                  12    
SHEET    1   A 6 VAL A 118  TYR A 122  0                                        
SHEET    2   A 6 SER A 128  GLU A 132 -1  O  LEU A 129   N  ILE A 121           
SHEET    3   A 6 GLY A 141  VAL A 147 -1  O  VAL A 147   N  SER A 128           
SHEET    4   A 6 THR A 153  ILE A 160 -1  O  GLY A 157   N  ILE A 144           
SHEET    5   A 6 GLU A 163  GLU A 176 -1  O  LYS A 168   N  TYR A 156           
SHEET    6   A 6 ARG A 179  LEU A 184 -1  O  HIS A 181   N  SER A 174           
SHEET    1   B 6 VAL A 118  TYR A 122  0                                        
SHEET    2   B 6 SER A 128  GLU A 132 -1  O  LEU A 129   N  ILE A 121           
SHEET    3   B 6 GLY A 141  VAL A 147 -1  O  VAL A 147   N  SER A 128           
SHEET    4   B 6 THR A 153  ILE A 160 -1  O  GLY A 157   N  ILE A 144           
SHEET    5   B 6 GLU A 163  GLU A 176 -1  O  LYS A 168   N  TYR A 156           
SHEET    6   B 6 VAL A 190  TYR A 191 -1  O  TYR A 191   N  GLY A 167           
SHEET    1   C 4 VAL A 216  GLU A 220  0                                        
SHEET    2   C 4 GLU A 228  SER A 232 -1  O  GLY A 229   N  ALA A 219           
SHEET    3   C 4 GLU A 330  VAL A 333 -1  O  LEU A 331   N  LEU A 230           
SHEET    4   C 4 ASN A 296  HIS A 297  1  N  ASN A 296   O  VAL A 333           
SHEET    1   D 3 VAL A 241  TYR A 245  0                                        
SHEET    2   D 3 GLY A 314  THR A 321 -1  O  LYS A 317   N  TYR A 245           
SHEET    3   D 3 CYS A 303  HIS A 310 -1  N  ASP A 306   O  CYS A 318           
SHEET    1   E 3 VAL A 248  ILE A 250  0                                        
SHEET    2   E 3 VAL A 274  ASP A 276 -1  O  VAL A 274   N  ILE A 250           
SHEET    3   E 3 LEU A 267  SER A 268 -1  N  LEU A 267   O  ILE A 275           
LINK         C   GLU A 138                 N   MSE A 139     1555   1555  1.33  
LINK         C   MSE A 139                 N   THR A 140     1555   1555  1.33  
LINK         C   GLU A 163                 N   MSE A 164     1555   1555  1.33  
LINK         C   MSE A 164                 N   ILE A 165     1555   1555  1.33  
LINK         C   LEU A 172                 N   MSE A 173     1555   1555  1.33  
LINK         C   MSE A 173                 N   SER A 174     1555   1555  1.33  
LINK         C   LEU A 184                 N   MSE A 185     1555   1555  1.33  
LINK         C   MSE A 185                 N   PRO A 186     1555   1555  1.34  
LINK         C   VAL A 241                 N   MSE A 242     1555   1555  1.33  
LINK         C   MSE A 242                 N   SER A 243     1555   1555  1.33  
LINK         C   ASP A 306                 N   MSE A 307     1555   1555  1.33  
LINK         C   MSE A 307                 N   PHE A 308     1555   1555  1.33  
SITE     1 AC1 19 ALA A 226  GLU A 228  GLY A 264  ASN A 265                    
SITE     2 AC1 19 HIS A 293  LYS A 294  ALA A 295  ASN A 296                    
SITE     3 AC1 19 HIS A 297  TYR A 335  TRP A 352  GLU A 356                    
SITE     4 AC1 19 HOH A1030  HOH A1118  HOH A1130  HOH A1153                    
SITE     5 AC1 19 HOH A1159  HOH A1161  HOH A1219                               
CRYST1  102.231   38.668   66.596  90.00  90.00  90.00 P 21 21 2     4          
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      0.009782  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.025861  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015016        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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