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Database: PDB
Entry: 3K9J
LinkDB: 3K9J
Original site: 3K9J 
HEADER    TRANSFERASE                             15-OCT-09   3K9J              
TITLE     TRANSPOSASE DOMAIN OF METNASE                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE SETMAR;                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: SET DOMAIN AND MARINER TRANSPOSASE FUSION GENE-CONTAINING   
COMPND   5 PROTEIN, METNASE, HSMAR1, HISTONE-LYSINE N-METHYLTRANSFERASE, MARINER
COMPND   6 TRANSPOSASE HSMAR1;                                                  
COMPND   7 EC: 2.1.1.43;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SETMAR;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET15B                                    
KEYWDS    TRANSPOSASE, CHROMATIN REGULATOR, DNA DAMAGE, DNA REPAIR, DNA-        
KEYWDS   2 BINDING, METHYLTRANSFERASE, NUCLEUS, PHOSPHOPROTEIN, TRANSFERASE     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.D.GOODWIN,H.HE,T.IMASAKI,S.-H.LEE,M.M.GEORGIADIS                    
REVDAT   2   21-JUL-10 3K9J    1       JRNL                                     
REVDAT   1   14-JUL-10 3K9J    0                                                
JRNL        AUTH   K.D.GOODWIN,H.HE,T.IMASAKI,S.H.LEE,M.M.GEORGIADIS            
JRNL        TITL   CRYSTAL STRUCTURE OF THE HUMAN HSMAR1-DERIVED TRANSPOSASE    
JRNL        TITL 2 DOMAIN IN THE DNA REPAIR ENZYME METNASE.                     
JRNL        REF    BIOCHEMISTRY                  V.  49  5705 2010              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   20521842                                                     
JRNL        DOI    10.1021/BI100171X                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.4_4)                        
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.59                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.040                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 41365                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.950                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2047                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 44.5969 -  4.6904    0.97     2976   172  0.2139 0.2136        
REMARK   3     2  4.6904 -  3.7235    0.99     2999   144  0.1699 0.1941        
REMARK   3     3  3.7235 -  3.2530    1.00     2949   149  0.1900 0.2167        
REMARK   3     4  3.2530 -  2.9556    0.99     2945   170  0.2190 0.2521        
REMARK   3     5  2.9556 -  2.7438    0.98     2892   148  0.2148 0.2713        
REMARK   3     6  2.7438 -  2.5821    0.97     2904   130  0.1983 0.2317        
REMARK   3     7  2.5821 -  2.4528    0.95     2805   144  0.2027 0.2384        
REMARK   3     8  2.4528 -  2.3460    0.94     2791   137  0.2076 0.2567        
REMARK   3     9  2.3460 -  2.2557    0.92     2687   139  0.2118 0.2607        
REMARK   3    10  2.2557 -  2.1779    0.89     2668   113  0.2067 0.2533        
REMARK   3    11  2.1779 -  2.1098    0.85     2489   130  0.2117 0.2460        
REMARK   3    12  2.1098 -  2.0495    0.80     2354   140  0.2257 0.2666        
REMARK   3    13  2.0495 -  1.9955    0.74     2159   124  0.2281 0.2565        
REMARK   3    14  1.9955 -  1.9468    0.69     1986   120  0.2471 0.2692        
REMARK   3    15  1.9468 -  1.9030    0.58     1714    87  0.2587 0.2700        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.37                                          
REMARK   3   B_SOL              : 59.65                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : -0.000           
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.040           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.22290                                              
REMARK   3    B22 (A**2) : -6.32610                                             
REMARK   3    B33 (A**2) : 2.10320                                              
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : 12.44070                                             
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           3506                                  
REMARK   3   ANGLE     :  1.052           4748                                  
REMARK   3   CHIRALITY :  0.078            497                                  
REMARK   3   PLANARITY :  0.004            616                                  
REMARK   3   DIHEDRAL  : 18.868           1286                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3K9J COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-OCT-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB055716.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JUL-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
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                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.10546                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL CRYO-COOLED         
REMARK 200                                   SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43992                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.2                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : 0.04600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.93                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 71.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42500                            
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: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.04                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NH4OAC, CACL2, PEG4000, PH 8.0, VAPOR    
REMARK 280  DIFFUSION, TEMPERATURE 293K                                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       22.70550            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     HIS A   433                                                      
REMARK 465     LEU A   434                                                      
REMARK 465     LYS A   435                                                      
REMARK 465     GLN A   436                                                      
REMARK 465     ILE A   437                                                      
REMARK 465     GLY A   438                                                      
REMARK 465     LYS A   439                                                      
REMARK 465     VAL A   440                                                      
REMARK 465     LYS A   441                                                      
REMARK 465     LYS A   442                                                      
REMARK 465     LEU A   443                                                      
REMARK 465     ASP A   444                                                      
REMARK 465     LYS A   445                                                      
REMARK 465     TRP A   446                                                      
REMARK 465     VAL A   447                                                      
REMARK 465     ARG A   492                                                      
REMARK 465     ARG A   493                                                      
REMARK 465     ARG A   494                                                      
REMARK 465     SER A   495                                                      
REMARK 465     ALA A   496                                                      
REMARK 465     GLN A   497                                                      
REMARK 465     TRP A   498                                                      
REMARK 465     LEU A   499                                                      
REMARK 465     ASP A   500                                                      
REMARK 465     GLN A   501                                                      
REMARK 465     GLU A   502                                                      
REMARK 465     GLU A   503                                                      
REMARK 465     ALA A   504                                                      
REMARK 465     PRO A   505                                                      
REMARK 465     LYS A   506                                                      
REMARK 465     HIS A   507                                                      
REMARK 465     PHE A   508                                                      
REMARK 465     PRO A   509                                                      
REMARK 465     LYS A   510                                                      
REMARK 465     PRO A   511                                                      
REMARK 465     ILE A   512                                                      
REMARK 465     LEU A   513                                                      
REMARK 465     HIS A   514                                                      
REMARK 465     HIS B   433                                                      
REMARK 465     LEU B   434                                                      
REMARK 465     LYS B   435                                                      
REMARK 465     GLN B   436                                                      
REMARK 465     ILE B   437                                                      
REMARK 465     GLY B   438                                                      
REMARK 465     LYS B   439                                                      
REMARK 465     ARG B   492                                                      
REMARK 465     ARG B   493                                                      
REMARK 465     ARG B   494                                                      
REMARK 465     SER B   495                                                      
REMARK 465     ALA B   496                                                      
REMARK 465     GLN B   497                                                      
REMARK 465     TRP B   498                                                      
REMARK 465     LEU B   499                                                      
REMARK 465     ASP B   500                                                      
REMARK 465     GLN B   501                                                      
REMARK 465     GLU B   502                                                      
REMARK 465     GLU B   503                                                      
REMARK 465     ALA B   504                                                      
REMARK 465     PRO B   505                                                      
REMARK 465     LYS B   506                                                      
REMARK 465     HIS B   507                                                      
REMARK 465     PHE B   508                                                      
REMARK 465     PRO B   509                                                      
REMARK 465     LYS B   510                                                      
REMARK 465     PRO B   511                                                      
REMARK 465     ILE B   512                                                      
REMARK 465     LEU B   513                                                      
REMARK 465     HIS B   514                                                      
REMARK 465     ALA B   563                                                      
REMARK 465     LEU B   564                                                      
REMARK 465     VAL B   565                                                      
REMARK 465     ARG B   566                                                      
REMARK 465     ARG B   567                                                      
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     ARG A 567    CG   CD   NE   CZ   NH1  NH2                        
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   O    HOH B    65     O    HOH B   238              1.97            
REMARK 500   O    HOH A   267     O    HOH A   268              2.16            
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    GLN A 622      106.88    -50.81                                   
REMARK 500    ASP B 444      -16.76     75.36                                   
REMARK 500    HIS B 531      143.82   -170.18                                   
REMARK 500    ALA B 582     -164.72   -109.58                                   
REMARK 500    HIS B 612      -71.13   -119.77                                   
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 A 161        DISTANCE =  5.64 ANGSTROMS                       
REMARK 525    HOH A 163        DISTANCE =  9.00 ANGSTROMS                       
REMARK 525    HOH B 199        DISTANCE =  6.53 ANGSTROMS                       
REMARK 525    HOH A 246        DISTANCE =  6.49 ANGSTROMS                       
REMARK 525    HOH A 253        DISTANCE =  5.08 ANGSTROMS                       
REMARK 525    HOH A 254        DISTANCE =  7.59 ANGSTROMS                       
REMARK 525    HOH A 258        DISTANCE =  7.27 ANGSTROMS                       
REMARK 525    HOH A 259        DISTANCE =  5.71 ANGSTROMS                       
REMARK 525    HOH A 260        DISTANCE =  5.45 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A   1  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 483   OD1                                                    
REMARK 620 2 ASP A 483   OD2  45.1                                              
REMARK 620 3 HOH A 148   O   103.8 108.3                                        
REMARK 620 4 HOH A 144   O    69.9 114.5  91.9                                  
REMARK 620 5 HOH A 240   O   155.7 113.4  93.8 126.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 672                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 5                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 4                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3K9K   RELATED DB: PDB                                   
DBREF  3K9J A  433   671  UNP    Q53H47   SETMR_HUMAN    433    671             
DBREF  3K9J B  433   671  UNP    Q53H47   SETMR_HUMAN    433    671             
SEQADV 3K9J ARG A  566  UNP  Q53H47    ASN   566 ENGINEERED                     
SEQADV 3K9J ARG A  569  UNP  Q53H47    GLY   569 ENGINEERED                     
SEQADV 3K9J TRP A  649  UNP  Q53H47    ALA   649 ENGINEERED                     
SEQADV 3K9J ARG B  566  UNP  Q53H47    ASN   566 ENGINEERED                     
SEQADV 3K9J ARG B  569  UNP  Q53H47    GLY   569 ENGINEERED                     
SEQADV 3K9J TRP B  649  UNP  Q53H47    ALA   649 ENGINEERED                     
SEQRES   1 A  239  HIS LEU LYS GLN ILE GLY LYS VAL LYS LYS LEU ASP LYS          
SEQRES   2 A  239  TRP VAL PRO HIS GLU LEU THR GLU ASN GLN LYS ASN ARG          
SEQRES   3 A  239  ARG PHE GLU VAL SER SER SER LEU ILE LEU ARG ASN HIS          
SEQRES   4 A  239  ASN GLU PRO PHE LEU ASP ARG ILE VAL THR CYS ASP GLU          
SEQRES   5 A  239  LYS TRP ILE LEU TYR ASP ASN ARG ARG ARG SER ALA GLN          
SEQRES   6 A  239  TRP LEU ASP GLN GLU GLU ALA PRO LYS HIS PHE PRO LYS          
SEQRES   7 A  239  PRO ILE LEU HIS PRO LYS LYS VAL MET VAL THR ILE TRP          
SEQRES   8 A  239  TRP SER ALA ALA GLY LEU ILE HIS TYR SER PHE LEU ASN          
SEQRES   9 A  239  PRO GLY GLU THR ILE THR SER GLU LYS TYR ALA GLN GLU          
SEQRES  10 A  239  ILE ASP GLU MET ASN GLN LYS LEU GLN ARG LEU GLN LEU          
SEQRES  11 A  239  ALA LEU VAL ARG ARG LYS ARG PRO ILE LEU LEU HIS ASP          
SEQRES  12 A  239  ASN ALA ARG PRO HIS VAL ALA GLN PRO THR LEU GLN LYS          
SEQRES  13 A  239  LEU ASN GLU LEU GLY TYR GLU VAL LEU PRO HIS PRO PRO          
SEQRES  14 A  239  TYR SER PRO ASP LEU LEU PRO THR ASN TYR HIS VAL PHE          
SEQRES  15 A  239  LYS HIS LEU ASN ASN PHE LEU GLN GLY LYS ARG PHE HIS          
SEQRES  16 A  239  ASN GLN GLN ASP ALA GLU ASN ALA PHE GLN GLU PHE VAL          
SEQRES  17 A  239  GLU SER GLN SER THR ASP PHE TYR TRP THR GLY ILE ASN          
SEQRES  18 A  239  GLN LEU ILE SER ARG TRP GLN LYS CYS VAL ASP CYS ASN          
SEQRES  19 A  239  GLY SER TYR PHE ASP                                          
SEQRES   1 B  239  HIS LEU LYS GLN ILE GLY LYS VAL LYS LYS LEU ASP LYS          
SEQRES   2 B  239  TRP VAL PRO HIS GLU LEU THR GLU ASN GLN LYS ASN ARG          
SEQRES   3 B  239  ARG PHE GLU VAL SER SER SER LEU ILE LEU ARG ASN HIS          
SEQRES   4 B  239  ASN GLU PRO PHE LEU ASP ARG ILE VAL THR CYS ASP GLU          
SEQRES   5 B  239  LYS TRP ILE LEU TYR ASP ASN ARG ARG ARG SER ALA GLN          
SEQRES   6 B  239  TRP LEU ASP GLN GLU GLU ALA PRO LYS HIS PHE PRO LYS          
SEQRES   7 B  239  PRO ILE LEU HIS PRO LYS LYS VAL MET VAL THR ILE TRP          
SEQRES   8 B  239  TRP SER ALA ALA GLY LEU ILE HIS TYR SER PHE LEU ASN          
SEQRES   9 B  239  PRO GLY GLU THR ILE THR SER GLU LYS TYR ALA GLN GLU          
SEQRES  10 B  239  ILE ASP GLU MET ASN GLN LYS LEU GLN ARG LEU GLN LEU          
SEQRES  11 B  239  ALA LEU VAL ARG ARG LYS ARG PRO ILE LEU LEU HIS ASP          
SEQRES  12 B  239  ASN ALA ARG PRO HIS VAL ALA GLN PRO THR LEU GLN LYS          
SEQRES  13 B  239  LEU ASN GLU LEU GLY TYR GLU VAL LEU PRO HIS PRO PRO          
SEQRES  14 B  239  TYR SER PRO ASP LEU LEU PRO THR ASN TYR HIS VAL PHE          
SEQRES  15 B  239  LYS HIS LEU ASN ASN PHE LEU GLN GLY LYS ARG PHE HIS          
SEQRES  16 B  239  ASN GLN GLN ASP ALA GLU ASN ALA PHE GLN GLU PHE VAL          
SEQRES  17 B  239  GLU SER GLN SER THR ASP PHE TYR TRP THR GLY ILE ASN          
SEQRES  18 B  239  GLN LEU ILE SER ARG TRP GLN LYS CYS VAL ASP CYS ASN          
SEQRES  19 B  239  GLY SER TYR PHE ASP                                          
HET     CA  A   1       1                                                       
HET    EDO  A 672       4                                                       
HET    EDO  A   2       4                                                       
HET    EDO  A   3       4                                                       
HET    EDO  A   5       4                                                       
HET    EDO  B   4       4                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3   CA    CA 2+                                                        
FORMUL   4  EDO    5(C2 H6 O2)                                                  
FORMUL   9  HOH   *251(H2 O)                                                    
HELIX    1   1 THR A  452  GLU A  473  1                                  22    
HELIX    2   2 PHE A  475  ASP A  477  5                                   3    
HELIX    3   3 THR A  542  GLN A  561  1                                  20    
HELIX    4   4 LEU A  562  LEU A  564  5                                   3    
HELIX    5   5 ALA A  577  VAL A  581  5                                   5    
HELIX    6   6 ALA A  582  GLY A  593  1                                  12    
HELIX    7   7 SER A  603  LEU A  606  5                                   4    
HELIX    8   8 LEU A  607  HIS A  612  1                                   6    
HELIX    9   9 HIS A  612  GLN A  622  1                                  11    
HELIX   10  10 ASN A  628  GLN A  643  1                                  16    
HELIX   11  11 ASP A  646  GLN A  654  1                                   9    
HELIX   12  12 GLN A  654  CYS A  665  1                                  12    
HELIX   13  13 THR B  452  GLU B  473  1                                  22    
HELIX   14  14 PHE B  475  ASP B  477  5                                   3    
HELIX   15  15 THR B  542  GLN B  561  1                                  20    
HELIX   16  16 ALA B  582  LEU B  592  1                                  11    
HELIX   17  17 SER B  603  LEU B  606  5                                   4    
HELIX   18  18 LEU B  607  HIS B  612  1                                   6    
HELIX   19  19 HIS B  612  GLN B  622  1                                  11    
HELIX   20  20 ASN B  628  GLN B  643  1                                  16    
HELIX   21  21 SER B  644  GLN B  654  1                                  11    
HELIX   22  22 GLN B  654  CYS B  665  1                                  12    
SHEET    1   A 5 GLY A 528  PHE A 534  0                                        
SHEET    2   A 5 LYS A 517  SER A 525 -1  N  TRP A 523   O  HIS A 531           
SHEET    3   A 5 ILE A 479  LEU A 488 -1  N  THR A 481   O  TRP A 524           
SHEET    4   A 5 ILE A 571  LEU A 573  1  O  ILE A 571   N  VAL A 480           
SHEET    5   A 5 GLU A 595  VAL A 596  1  O  GLU A 595   N  LEU A 572           
SHEET    1   B 2 LYS B 441  LYS B 442  0                                        
SHEET    2   B 2 LYS B 445  TRP B 446 -1  O  LYS B 445   N  LYS B 442           
SHEET    1   C 5 GLY B 528  PHE B 534  0                                        
SHEET    2   C 5 LYS B 517  SER B 525 -1  N  SER B 525   O  GLY B 528           
SHEET    3   C 5 ILE B 479  LEU B 488 -1  N  THR B 481   O  TRP B 524           
SHEET    4   C 5 ILE B 571  LEU B 573  1  O  ILE B 571   N  VAL B 480           
SHEET    5   C 5 GLU B 595  VAL B 596  1  O  GLU B 595   N  LEU B 572           
LINK         OD1 ASP A 483                CA    CA A   1     1555   1555  2.75  
LINK         OD2 ASP A 483                CA    CA A   1     1555   1555  2.95  
LINK        CA    CA A   1                 O   HOH A 148     1555   1555  2.58  
LINK        CA    CA A   1                 O   HOH A 144     1555   1555  2.71  
LINK        CA    CA A   1                 O   HOH A 240     1555   1555  2.85  
SITE     1 AC1  4 HOH A 144  HOH A 148  HOH A 240  ASP A 483                    
SITE     1 AC2  4 ILE A 530  HIS A 531  TYR A 532  LYS A 556                    
SITE     1 AC3  9 EDO A   3  HOH A 128  HOH A 160  HOH A 250                    
SITE     2 AC3  9 HOH A 267  ASP A 575  ASN A 576  PRO A 601                    
SITE     3 AC3  9 TYR A 602                                                     
SITE     1 AC4  4 EDO A   2  HOH A 236  HOH A 252  TYR A 602                    
SITE     1 AC5  2 THR A 542  SER A 543                                          
SITE     1 AC6  2 HOH B 264  GLN B 643                                          
CRYST1   79.158   45.411   90.678  90.00 113.81  90.00 P 1 21 1      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      0.012633  0.000000  0.005574        0.00000                         
SCALE2      0.000000  0.022021  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012054        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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