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Database: PDB
Entry: 1LJM
LinkDB: 1LJM
Original site: 1LJM 
HEADER    TRANSCRIPTION                           22-APR-02   1LJM              
TITLE     DNA RECOGNITION IS MEDIATED BY CONFORMATIONAL TRANSITION              
TITLE    2 AND BY DNA BENDING                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RUNX1 TRANSCRIPTION FACTOR;                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RUNT DOMAIN;                                               
COMPND   5 SYNONYM: RUNT-RELATED TRANSCRIPTION FACTOR 1, ACUTE                  
COMPND   6 MYELOID LEUKEMIA 1 PROTEIN, CORE-BINDING FACTOR, ALPHA 2             
COMPND   7 SUBUNIT;                                                             
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HUMAN;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: PHS2;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PV/8+LAMBDAPL+RBS;                    
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: RUNT-PV-8                                 
KEYWDS    IMMUNOGLOBULIN FOLD, BETA-SANDWICH, TRANSCRIPTION                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.BARTFELD,L.SHIMON,G.C.COUTURE,D.RABINOVICH,F.FROLOW,                
AUTHOR   2 D.LEVANON,Y.GRONER,Z.SHAKKED                                         
REVDAT   2   24-FEB-09 1LJM    1       VERSN                                    
REVDAT   1   06-NOV-02 1LJM    0                                                
JRNL        AUTH   D.BARTFELD,L.SHIMON,G.COUTURE,D.RABINOVICH,                  
JRNL        AUTH 2 F.FROLOW,D.LEVANON,Y.GRONER,Z.SHAKKED                        
JRNL        TITL   DNA RECOGNITION BY THE RUNX1 TRANSCRIPTION FACTOR            
JRNL        TITL 2 IS MEDIATED BY AN ALLOSTERIC TRANSITION IN THE               
JRNL        TITL 3 RUNT DOMAIN AND BY DNA BENDING.                              
JRNL        REF    STRUCTURE                     V.  10  1395                   
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   12377125                                                     
JRNL        DOI    10.1016/S0969-2126(02)00853-5                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 17379                          
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) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 842                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1759                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 201                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 31.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.50                          
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.29                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.36                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 43.00                           
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.39                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.39                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.50                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.78                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 3.800 ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1LJM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-APR-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB016000.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-JAN-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU ULTRAX 18                   
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : OSMIC MIRRORS                      
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17379                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 13.900                             
REMARK 200  R MERGE                    (I) : 0.07100                            
REMARK 200  R SYM                      (I) : 0.07100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.29500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.29500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MTF, ULTIMA                                           
REMARK 200 STARTING MODEL: PDB ENTRY 1E50                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 72.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.52                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: ETHANOL, SODIUM CHLORIDE, TRIS-HCL,      
REMARK 280  HEPES, DTT, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE      
REMARK 280  292K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-Z                                              
REMARK 290       7555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       8555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       9555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290      10555   Y+2/3,X+1/3,-Z+1/3                                      
REMARK 290      11555   X-Y+2/3,-Y+1/3,-Z+1/3                                   
REMARK 290      12555   -X+2/3,-X+Y+1/3,-Z+1/3                                  
REMARK 290      13555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290      14555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290      15555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290      16555   Y+1/3,X+2/3,-Z+2/3                                      
REMARK 290      17555   X-Y+1/3,-Y+2/3,-Z+2/3                                   
REMARK 290      18555   -X+1/3,-X+Y+2/3,-Z+2/3                                  
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000       60.61500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       34.99609            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       62.11000            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000       60.61500            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       34.99609            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       62.11000            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000       60.61500            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       34.99609            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       62.11000            
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000       60.61500            
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       34.99609            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       62.11000            
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000       60.61500            
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       34.99609            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       62.11000            
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000       60.61500            
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       34.99609            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       62.11000            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       69.99217            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000      124.22000            
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000       69.99217            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000      124.22000            
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000       69.99217            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000      124.22000            
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000       69.99217            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      124.22000            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000       69.99217            
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000      124.22000            
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000       69.99217            
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000      124.22000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 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: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5810 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20950 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -119.0 KCAL/MOL                       
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   BIOMT1   2 -0.500000  0.866025  0.000000      -60.61500            
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000       34.99609            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       62.11000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1860 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -88.0 KCAL/MOL                        
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 350   BIOMT1   2 -0.500000  0.866025  0.000000      -60.61500            
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000       34.99609            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       62.11000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A3114  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B3112  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B3148  LIES ON A SPECIAL POSITION.                          
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  1051                                                      
REMARK 465     VAL A  1052                                                      
REMARK 465     GLU A  1053                                                      
REMARK 465     VAL A  1054                                                      
REMARK 465     LEU A  1055                                                      
REMARK 465     ALA A  1056                                                      
REMARK 465     ASP A  1057                                                      
REMARK 465     HIS A  1058                                                      
REMARK 465     PRO A  1059                                                      
REMARK 465     GLY A  1060                                                      
REMARK 465     GLU A  1175                                                      
REMARK 465     PRO A  1176                                                      
REMARK 465     ARG A  1177                                                      
REMARK 465     ARG A  1178                                                      
REMARK 465     HIS A  1179                                                      
REMARK 465     ARG A  1180                                                      
REMARK 465     GLN A  1181                                                      
REMARK 465     MET B  2051                                                      
REMARK 465     VAL B  2052                                                      
REMARK 465     GLU B  2053                                                      
REMARK 465     VAL B  2054                                                      
REMARK 465     LEU B  2055                                                      
REMARK 465     ALA B  2056                                                      
REMARK 465     ASP B  2057                                                      
REMARK 465     HIS B  2058                                                      
REMARK 465     PRO B  2059                                                      
REMARK 465     ARG B  2174                                                      
REMARK 465     GLU B  2175                                                      
REMARK 465     PRO B  2176                                                      
REMARK 465     ARG B  2177                                                      
REMARK 465     ARG B  2178                                                      
REMARK 465     HIS B  2179                                                      
REMARK 465     ARG B  2180                                                      
REMARK 465     GLN B  2181                                                      
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    THR A1065     -166.72   -103.10                                   
REMARK 500    ASN A1082       11.93     57.27                                   
REMARK 500    THR B2065     -168.58   -116.15                                   
REMARK 500    ASP B2096       84.62     61.79                                   
REMARK 500    SER B2114       98.15   -164.46                                   
REMARK 500    ASP B2133       70.13     49.30                                   
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 B3147        DISTANCE =  7.15 ANGSTROMS                       
REMARK 525    HOH B3177        DISTANCE =  7.17 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 4001                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 4002                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 4003                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 4004                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 4005                 
DBREF  1LJM A 1051  1181  UNP    Q01196   RUNX1_HUMAN     51    181             
DBREF  1LJM B 2051  2181  UNP    Q01196   RUNX1_HUMAN     51    181             
SEQRES   1 A  131  MET VAL GLU VAL LEU ALA ASP HIS PRO GLY GLU LEU VAL          
SEQRES   2 A  131  ARG THR ASP SER PRO ASN PHE LEU CYS SER VAL LEU PRO          
SEQRES   3 A  131  THR HIS TRP ARG CYS ASN LYS THR LEU PRO ILE ALA PHE          
SEQRES   4 A  131  LYS VAL VAL ALA LEU GLY ASP VAL PRO ASP GLY THR LEU          
SEQRES   5 A  131  VAL THR VAL MET ALA GLY ASN ASP GLU ASN TYR SER ALA          
SEQRES   6 A  131  GLU LEU ARG ASN ALA THR ALA ALA MET LYS ASN GLN VAL          
SEQRES   7 A  131  ALA ARG PHE ASN ASP LEU ARG PHE VAL GLY ARG SER GLY          
SEQRES   8 A  131  ARG GLY LYS SER PHE THR LEU THR ILE THR VAL PHE THR          
SEQRES   9 A  131  ASN PRO PRO GLN VAL ALA THR TYR HIS ARG ALA ILE LYS          
SEQRES  10 A  131  ILE THR VAL ASP GLY PRO ARG GLU PRO ARG ARG HIS ARG          
SEQRES  11 A  131  GLN                                                          
SEQRES   1 B  131  MET VAL GLU VAL LEU ALA ASP HIS PRO GLY GLU LEU VAL          
SEQRES   2 B  131  ARG THR ASP SER PRO ASN PHE LEU CYS SER VAL LEU PRO          
SEQRES   3 B  131  THR HIS TRP ARG CYS ASN LYS THR LEU PRO ILE ALA PHE          
SEQRES   4 B  131  LYS VAL VAL ALA LEU GLY ASP VAL PRO ASP GLY THR LEU          
SEQRES   5 B  131  VAL THR VAL MET ALA GLY ASN ASP GLU ASN TYR SER ALA          
SEQRES   6 B  131  GLU LEU ARG ASN ALA THR ALA ALA MET LYS ASN GLN VAL          
SEQRES   7 B  131  ALA ARG PHE ASN ASP LEU ARG PHE VAL GLY ARG SER GLY          
SEQRES   8 B  131  ARG GLY LYS SER PHE THR LEU THR ILE THR VAL PHE THR          
SEQRES   9 B  131  ASN PRO PRO GLN VAL ALA THR TYR HIS ARG ALA ILE LYS          
SEQRES  10 B  131  ILE THR VAL ASP GLY PRO ARG GLU PRO ARG ARG HIS ARG          
SEQRES  11 B  131  GLN                                                          
HET     CL  B4001       1                                                       
HET     CL  B4002       1                                                       
HET     CL  A4003       1                                                       
HET     CL  B4004       1                                                       
HET     CL  B4005       1                                                       
HETNAM      CL CHLORIDE ION                                                     
FORMUL   3   CL    5(CL 1-)                                                     
FORMUL   8  HOH   *201(H2 O)                                                    
SHEET    1   A 4 LEU A1062  ARG A1064  0                                        
SHEET    2   A 4 PHE A1070  SER A1073 -1  O  CYS A1072   N  VAL A1063           
SHEET    3   A 4 LYS A1090  ALA A1093 -1  O  VAL A1092   N  LEU A1071           
SHEET    4   A 4 VAL A1128  ARG A1130 -1  O  ALA A1129   N  VAL A1091           
SHEET    1   B 2 HIS A1078  ARG A1080  0                                        
SHEET    2   B 2 LYS A1167  THR A1169  1  O  LYS A1167   N  TRP A1079           
SHEET    1   C 4 THR A1121  ALA A1123  0                                        
SHEET    2   C 4 LEU A1102  GLY A1108 -1  N  VAL A1103   O  ALA A1122           
SHEET    3   C 4 THR A1147  VAL A1152 -1  O  THR A1149   N  MET A1106           
SHEET    4   C 4 GLN A1158  THR A1161 -1  O  ALA A1160   N  ILE A1150           
SHEET    1   D 2 LEU A1117  ARG A1118  0                                        
SHEET    2   D 2 ARG A1135  PHE A1136 -1  O  ARG A1135   N  ARG A1118           
SHEET    1   E 4 VAL B2063  ARG B2064  0                                        
SHEET    2   E 4 PHE B2070  CYS B2072 -1  O  CYS B2072   N  VAL B2063           
SHEET    3   E 4 LYS B2090  ALA B2093 -1  O  VAL B2092   N  LEU B2071           
SHEET    4   E 4 VAL B2128  ARG B2130 -1  O  ALA B2129   N  VAL B2091           
SHEET    1   F 2 HIS B2078  ARG B2080  0                                        
SHEET    2   F 2 LYS B2167  THR B2169  1  O  LYS B2167   N  TRP B2079           
SHEET    1   G 4 THR B2121  ALA B2123  0                                        
SHEET    2   G 4 LEU B2102  GLY B2108 -1  N  VAL B2103   O  ALA B2122           
SHEET    3   G 4 THR B2147  VAL B2152 -1  O  THR B2147   N  GLY B2108           
SHEET    4   G 4 GLN B2158  THR B2161 -1  O  ALA B2160   N  ILE B2150           
CISPEP   1 ASN A 1155    PRO A 1156          0         0.78                     
CISPEP   2 ASN B 2155    PRO B 2156          0         0.12                     
SITE     1 AC1  2 THR B2154  ASN B2155                                          
SITE     1 AC2  2 GLN B2158  HOH B3056                                          
SITE     1 AC3  3 ALA A1115  GLU A1116  GLY A1138                               
SITE     1 AC4  4 ASN B2112  ALA B2115  GLU B2116  GLY B2138                    
SITE     1 AC5  3 ARG B2142  THR B2169  VAL B2170                               
CRYST1  121.230  121.230  186.330  90.00  90.00 120.00 H 3 2        36          
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      0.008249  0.004762  0.000000        0.00000                         
SCALE2      0.000000  0.009525  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005367        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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