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Database: PDB
Entry: 2J8A
LinkDB: 2J8A
Original site: 2J8A 
HEADER    TRANSFERASE                             24-OCT-06   2J8A              
TITLE     X-RAY STRUCTURE OF THE N-TERMINUS RRM DOMAIN OF SET1                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-4            
COMPND   3  SPECIFIC;                                                           
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: N-TERMINUS RRM DOMAIN, RESIDUES 247-375;                   
COMPND   6 SYNONYM: COMPASS COMPONENT SET1, SET DOMAIN-CONTAINING               
COMPND   7  PROTEIN 1, SET1 HISTONE METHYLTRANSFERASE;                          
COMPND   8 EC: 2.1.1.43;                                                        
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 STRAIN: S228C;                                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: GOLD;                                      
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET-9                                     
KEYWDS    HISTONE METHYLTRANSFERASE, RRM FOLD, TELOMERE, TRANSFERASE,           
KEYWDS   2 NUCLEAR PROTEIN, METHYLTRANSFERASE, CHROMOSOMAL PROTEIN              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.TRESAUGUES,P.M.DEHE,R.GUEROIS,A.RODRIGUEZ-GIL,I.VARLET,             
AUTHOR   2 P.SALAH,M.PAMBLANCO,P.LUCIANO,S.QUEVILLON-CHERUEL,                   
AUTHOR   3 J.SOLLIER,N.LEULLIOT,J.COUPRIE,V.TORDERA,S.ZINN-JUSTIN,              
AUTHOR   4 S.CHAVEZ,H.VAN TILBEURGH,V.GELI                                      
REVDAT   3   24-FEB-09 2J8A    1       VERSN                                    
REVDAT   2   03-APR-07 2J8A    1       REMARK                                   
REVDAT   1   20-MAR-07 2J8A    0                                                
JRNL        AUTH   L.TRESAUGUES,P.M.DEHE,R.GUEROIS,A.RODRIGUEZ-GIL,             
JRNL        AUTH 2 I.VARLET,P.SALAH,M.PAMBLANCO,P.LUCIANO,                      
JRNL        AUTH 3 S.QUEVILLON-CHERUEL,J.SOLLIER,N.LEULLIOT,J.COUPRIE,          
JRNL        AUTH 4 V.TORDERA,S.ZINN-JUSTIN,S.CHAVEZ,H.VAN TILBEURGH,            
JRNL        AUTH 5 V.GELI                                                       
JRNL        TITL   X-RAY STRUCTURE OF THE N-TERMINUS RRM DOMAIN OF              
JRNL        TITL 2 SET1                                                         
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   L.TRESAUGUES,P.M.DEHE,R.GUEROIS,A.RODRIGUEZ-GIL,             
REMARK   1  AUTH 2 I.VARLET,P.SALAH,M.PAMBLANCO,P.LUCIANO,                      
REMARK   1  AUTH 3 S.QUEVILLON-CHERUEL,J.SOLLIER,N.LEULLIOT,J.COUPRIE,          
REMARK   1  AUTH 4 V.TORDERA,S.ZINN-JUSTIN,S.CHAVEZ,H.VAN TILBEURGH,            
REMARK   1  AUTH 5 V.GELI                                                       
REMARK   1  TITL   STRUCTURAL CHARACTERIZATION OF SET1 RNA                      
REMARK   1  TITL 2 RECOGNITION MOTIFS AND THEIR ROLE IN HISTONE H3              
REMARK   1  TITL 3 LYSINE 4 METHYLATION.                                        
REMARK   1  REF    J.MOL.BIOL.                   V. 359  1170 2006              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  PMID   16787775                                                     
REMARK   1  DOI    10.1016/J.JMB.2006.04.050                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.0  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
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) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 6381                           
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) : 0.247                           
REMARK   3   R VALUE            (WORKING SET) : 0.246                           
REMARK   3   FREE R VALUE                     : 0.277                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 321                             
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) : 3.07                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 443                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3660                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 23                           
REMARK   3   BIN FREE R VALUE                    : 0.4300                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 915                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          :                                         
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) : 67.85                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.435         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.320         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.234         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.120        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.914                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.877                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):   933 ; 0.054 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1255 ; 4.097 ; 1.943       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   112 ;12.832 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    43 ;31.879 ;25.581       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   173 ;25.179 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     1 ; 6.192 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   141 ; 0.335 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   685 ; 0.016 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   520 ; 0.348 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   651 ; 0.392 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    50 ; 0.232 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    44 ; 0.297 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     2 ; 0.096 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   586 ; 2.273 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   919 ; 3.563 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   403 ; 5.078 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   336 ; 7.741 ; 4.500       
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          
REMARK   3  RIDING POSITIONS. RESIDUES 302-306 AND 367-CTERMINUS ARE            
REMARK   3  DISORDERED                                                          
REMARK   4                                                                      
REMARK   4 2J8A COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-OCT-06.                  
REMARK 100 THE PDBE ID CODE IS EBI-30296.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-NOV-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 4.60                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 7192                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 9.400                              
REMARK 200  R MERGE                    (I) : 0.01000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.31000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS                        
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 75.2                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.67                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.15M AMMONIUM SULFATE,50MM              
REMARK 280  NACITRATE PH4.6,4% POLYPROPYLENE-GLYCOL 400,3% GLYCEROL             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 3 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z+1/2,-X+1/2,-Y                                         
REMARK 290       7555   -Z+1/2,-X,Y+1/2                                         
REMARK 290       8555   -Z,X+1/2,-Y+1/2                                         
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z+1/2,-X+1/2                                         
REMARK 290      11555   Y+1/2,-Z+1/2,-X                                         
REMARK 290      12555   -Y+1/2,-Z,X+1/2                                         
REMARK 290      13555   Y+1/4,X+3/4,-Z+3/4                                      
REMARK 290      14555   -Y+1/4,-X+1/4,-Z+1/4                                    
REMARK 290      15555   Y+3/4,-X+3/4,Z+1/4                                      
REMARK 290      16555   -Y+3/4,X+1/4,Z+3/4                                      
REMARK 290      17555   X+1/4,Z+3/4,-Y+3/4                                      
REMARK 290      18555   -X+3/4,Z+1/4,Y+3/4                                      
REMARK 290      19555   -X+1/4,-Z+1/4,-Y+1/4                                    
REMARK 290      20555   X+3/4,-Z+3/4,Y+1/4                                      
REMARK 290      21555   Z+1/4,Y+3/4,-X+3/4                                      
REMARK 290      22555   Z+3/4,-Y+3/4,X+1/4                                      
REMARK 290      23555   -Z+3/4,Y+1/4,X+3/4                                      
REMARK 290      24555   -Z+1/4,-Y+1/4,-X+1/4                                    
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       61.89500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       61.89500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       61.89500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       61.89500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       61.89500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       61.89500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000       61.89500            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000       61.89500            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000       61.89500            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000       61.89500            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000       61.89500            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000       61.89500            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000       61.89500            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000       61.89500            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000       61.89500            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000       61.89500            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000       61.89500            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000       61.89500            
REMARK 290   SMTRY1  13  0.000000  1.000000  0.000000       30.94750            
REMARK 290   SMTRY2  13  1.000000  0.000000  0.000000       92.84250            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       92.84250            
REMARK 290   SMTRY1  14  0.000000 -1.000000  0.000000       30.94750            
REMARK 290   SMTRY2  14 -1.000000  0.000000  0.000000       30.94750            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       30.94750            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       92.84250            
REMARK 290   SMTRY2  15 -1.000000  0.000000  0.000000       92.84250            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000       30.94750            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       92.84250            
REMARK 290   SMTRY2  16  1.000000  0.000000  0.000000       30.94750            
REMARK 290   SMTRY3  16  0.000000  0.000000  1.000000       92.84250            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000       30.94750            
REMARK 290   SMTRY2  17  0.000000  0.000000  1.000000       92.84250            
REMARK 290   SMTRY3  17  0.000000 -1.000000  0.000000       92.84250            
REMARK 290   SMTRY1  18 -1.000000  0.000000  0.000000       92.84250            
REMARK 290   SMTRY2  18  0.000000  0.000000  1.000000       30.94750            
REMARK 290   SMTRY3  18  0.000000  1.000000  0.000000       92.84250            
REMARK 290   SMTRY1  19 -1.000000  0.000000  0.000000       30.94750            
REMARK 290   SMTRY2  19  0.000000  0.000000 -1.000000       30.94750            
REMARK 290   SMTRY3  19  0.000000 -1.000000  0.000000       30.94750            
REMARK 290   SMTRY1  20  1.000000  0.000000  0.000000       92.84250            
REMARK 290   SMTRY2  20  0.000000  0.000000 -1.000000       92.84250            
REMARK 290   SMTRY3  20  0.000000  1.000000  0.000000       30.94750            
REMARK 290   SMTRY1  21  0.000000  0.000000  1.000000       30.94750            
REMARK 290   SMTRY2  21  0.000000  1.000000  0.000000       92.84250            
REMARK 290   SMTRY3  21 -1.000000  0.000000  0.000000       92.84250            
REMARK 290   SMTRY1  22  0.000000  0.000000  1.000000       92.84250            
REMARK 290   SMTRY2  22  0.000000 -1.000000  0.000000       92.84250            
REMARK 290   SMTRY3  22  1.000000  0.000000  0.000000       30.94750            
REMARK 290   SMTRY1  23  0.000000  0.000000 -1.000000       92.84250            
REMARK 290   SMTRY2  23  0.000000  1.000000  0.000000       30.94750            
REMARK 290   SMTRY3  23  1.000000  0.000000  0.000000       92.84250            
REMARK 290   SMTRY1  24  0.000000  0.000000 -1.000000       30.94750            
REMARK 290   SMTRY2  24  0.000000 -1.000000  0.000000       30.94750            
REMARK 290   SMTRY3  24 -1.000000  0.000000  0.000000       30.94750            
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 GENERATING THE BIOMOLECULE                                           
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE:  1                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
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     MET A   246                                                      
REMARK 465     SER A   302                                                      
REMARK 465     SER A   303                                                      
REMARK 465     ASP A   304                                                      
REMARK 465     GLY A   305                                                      
REMARK 465     LYS A   306                                                      
REMARK 465     ILE A   307                                                      
REMARK 465     LYS A   367                                                      
REMARK 465     ALA A   368                                                      
REMARK 465     LYS A   369                                                      
REMARK 465     GLU A   370                                                      
REMARK 465     LYS A   371                                                      
REMARK 465     GLU A   372                                                      
REMARK 465     ALA A   373                                                      
REMARK 465     GLU A   374                                                      
REMARK 465     ASN A   375                                                      
REMARK 465     HIS A   376                                                      
REMARK 465     HIS A   377                                                      
REMARK 465     HIS A   378                                                      
REMARK 465     HIS A   379                                                      
REMARK 465     HIS A   380                                                      
REMARK 465     HIS A   381                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS A 248   CB    CYS A 248   SG     -0.130                       
REMARK 500    GLU A 249   CB    GLU A 249   CG     -0.175                       
REMARK 500    TYR A 253   CD2   TYR A 253   CE2     0.117                       
REMARK 500    THR A 260   CA    THR A 260   CB      0.173                       
REMARK 500    TYR A 271   CB    TYR A 271   CG     -0.110                       
REMARK 500    TYR A 271   CD2   TYR A 271   CE2     0.106                       
REMARK 500    PHE A 281   CE2   PHE A 281   CZ      0.116                       
REMARK 500    GLU A 282   CB    GLU A 282   CG     -0.154                       
REMARK 500    PHE A 284   CE2   PHE A 284   CZ      0.127                       
REMARK 500    VAL A 295   C     VAL A 295   O       0.118                       
REMARK 500    ALA A 301   CA    ALA A 301   CB      0.153                       
REMARK 500    SER A 323   CA    SER A 323   CB      0.113                       
REMARK 500    SER A 324   CA    SER A 324   CB      0.102                       
REMARK 500    PHE A 327   CA    PHE A 327   CB     -0.137                       
REMARK 500    PHE A 327   CB    PHE A 327   CG     -0.121                       
REMARK 500    PHE A 331   CD2   PHE A 331   CE2     0.128                       
REMARK 500    PHE A 331   CE1   PHE A 331   CZ      0.117                       
REMARK 500    LEU A 343   C     LEU A 343   O       0.123                       
REMARK 500    SER A 348   C     SER A 348   O       0.131                       
REMARK 500    LYS A 349   CD    LYS A 349   CE      0.210                       
REMARK 500    LYS A 349   CE    LYS A 349   NZ      0.228                       
REMARK 500    VAL A 351   CA    VAL A 351   CB     -0.134                       
REMARK 500    GLU A 352   CG    GLU A 352   CD      0.132                       
REMARK 500    ILE A 353   CA    ILE A 353   CB     -0.161                       
REMARK 500    ASN A 354   N     ASN A 354   CA     -0.120                       
REMARK 500    LYS A 356   CE    LYS A 356   NZ      0.183                       
REMARK 500    LYS A 366   CD    LYS A 366   CE      0.190                       
REMARK 500    LYS A 366   CE    LYS A 366   NZ      0.172                       
REMARK 500    LYS A 366   CG    LYS A 366   CD      0.235                       
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    CYS A 248   CA  -  CB  -  SG  ANGL. DEV. =  -8.5 DEGREES          
REMARK 500    ASP A 257   CB  -  CG  -  OD1 ANGL. DEV. =   8.7 DEGREES          
REMARK 500    ASP A 257   CB  -  CG  -  OD2 ANGL. DEV. = -10.5 DEGREES          
REMARK 500    THR A 259   N   -  CA  -  C   ANGL. DEV. =  19.7 DEGREES          
REMARK 500    LYS A 269   CD  -  CE  -  NZ  ANGL. DEV. = -20.5 DEGREES          
REMARK 500    LYS A 273   CD  -  CE  -  NZ  ANGL. DEV. =  14.4 DEGREES          
REMARK 500    GLU A 277   N   -  CA  -  C   ANGL. DEV. = -16.4 DEGREES          
REMARK 500    LEU A 293   CB  -  CG  -  CD2 ANGL. DEV. = -10.7 DEGREES          
REMARK 500    HIS A 321   N   -  CA  -  C   ANGL. DEV. =  18.1 DEGREES          
REMARK 500    MET A 329   CG  -  SD  -  CE  ANGL. DEV. =  10.6 DEGREES          
REMARK 500    VAL A 335   CB  -  CA  -  C   ANGL. DEV. = -12.1 DEGREES          
REMARK 500    LEU A 343   CB  -  CG  -  CD1 ANGL. DEV. = -16.1 DEGREES          
REMARK 500    GLU A 352   N   -  CA  -  CB  ANGL. DEV. = -11.4 DEGREES          
REMARK 500    GLU A 352   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.2 DEGREES          
REMARK 500    LEU A 365   CA  -  CB  -  CG  ANGL. DEV. =  18.7 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 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    CYS A 248      -34.34   -136.32                                   
REMARK 500    ASP A 257      -74.04    -28.35                                   
REMARK 500    ASN A 262       35.93   -146.20                                   
REMARK 500    ASP A 265      -72.62    -43.49                                   
REMARK 500    ILE A 266      -74.82    -16.52                                   
REMARK 500    SER A 267      -28.10    -27.56                                   
REMARK 500    ASN A 270      -83.95    -33.51                                   
REMARK 500    TYR A 271      -49.21    -28.05                                   
REMARK 500    LYS A 273      -41.87    -25.73                                   
REMARK 500    LYS A 274       39.53    -63.80                                   
REMARK 500    HIS A 280      132.75    171.35                                   
REMARK 500    ALA A 290       -2.83     63.55                                   
REMARK 500    HIS A 294       53.66     71.69                                   
REMARK 500    ALA A 310      -75.15    -47.46                                   
REMARK 500    ALA A 311      -35.88    -32.71                                   
REMARK 500    ALA A 313      -78.71    -39.79                                   
REMARK 500    ALA A 314      -62.07    -26.14                                   
REMARK 500    SER A 323      -86.47    -35.85                                   
REMARK 500    ASN A 364      -36.23    -31.63                                   
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 SER A  247     CYS A  248                 -139.77                    
REMARK 500 THR A  260     THR A  261                  147.48                    
REMARK 500 TYR A  300     ALA A  301                  144.58                    
REMARK 500 ASP A  309     ALA A  310                  138.33                    
REMARK 500 GLU A  363     ASN A  364                  146.54                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    THR A 259         5.2      L          D   EXPECTING SP3           
REMARK 500    GLN A 264        19.1      L          L   OUTSIDE RANGE           
REMARK 500    PHE A 272        22.4      L          L   OUTSIDE RANGE           
REMARK 500    GLU A 277        46.7      L          L   OUTSIDE RANGE           
REMARK 500    HIS A 321        12.0      L          L   OUTSIDE RANGE           
REMARK 500    GLU A 363        23.6      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  2J8A A  246   246  PDB    2J8A     2J8A           246    246             
DBREF  2J8A A  247   375  UNP    P38827   SET1_YEAST     247    375             
DBREF  2J8A A  376   381  PDB    2J8A     2J8A           376    381             
SEQRES   1 A  136  MET SER CYS GLU ILE VAL VAL TYR PRO ALA GLN ASP SER          
SEQRES   2 A  136  THR THR THR ASN ILE GLN ASP ILE SER ILE LYS ASN TYR          
SEQRES   3 A  136  PHE LYS LYS TYR GLY GLU ILE SER HIS PHE GLU ALA PHE          
SEQRES   4 A  136  ASN ASP PRO ASN SER ALA LEU PRO LEU HIS VAL TYR LEU          
SEQRES   5 A  136  ILE LYS TYR ALA SER SER ASP GLY LYS ILE ASN ASP ALA          
SEQRES   6 A  136  ALA LYS ALA ALA PHE SER ALA VAL ARG LYS HIS GLU SER          
SEQRES   7 A  136  SER GLY CYS PHE ILE MET GLY PHE LYS PHE GLU VAL ILE          
SEQRES   8 A  136  LEU ASN LYS HIS SER ILE LEU ASN ASN ILE ILE SER LYS          
SEQRES   9 A  136  PHE VAL GLU ILE ASN VAL LYS LYS LEU GLN LYS LEU GLN          
SEQRES  10 A  136  GLU ASN LEU LYS LYS ALA LYS GLU LYS GLU ALA GLU ASN          
SEQRES  11 A  136  HIS HIS HIS HIS HIS HIS                                      
HELIX    1   1 GLN A  264  LYS A  274  1                                  11    
HELIX    2   2 ASP A  309  HIS A  321  1                                  13    
HELIX    3   3 SER A  341  LEU A  365  1                                  25    
SHEET    1  AA 5 HIS A 280  ASN A 285  0                                        
SHEET    2  AA 5 PRO A 292  LYS A 299 -1  N  LEU A 293   O  PHE A 284           
SHEET    3  AA 5 GLU A 249  PRO A 254 -1  O  ILE A 250   N  ILE A 298           
SHEET    4  AA 5 PHE A 331  LEU A 337 -1  O  GLU A 334   N  TYR A 253           
SHEET    5  AA 5 CYS A 326  ILE A 328 -1  O  CYS A 326   N  PHE A 333           
CRYST1  123.790  123.790  123.790  90.00  90.00  90.00 P 43 3 2     24          
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      0.008078  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008078  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008078        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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