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Database: PDB
Entry: 1IO4
LinkDB: 1IO4
Original site: 1IO4 
HEADER    TRANSCRIPTION/DNA                       10-JAN-01   1IO4              
TITLE     CRYSTAL STRUCTURE OF RUNX-1/AML1/CBFALPHA RUNT DOMAIN-                
TITLE    2 CBFBETA CORE DOMAIN HETERODIMER AND C/EBPBETA BZIP                   
TITLE    3 HOMODIMER BOUND TO A DNA FRAGMENT FROM THE CSF-1R PROMOTER           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CSF-1R PROMOTER;                                           
COMPND   3 CHAIN: E;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: CSF-1R PROMOTER;                                           
COMPND   7 CHAIN: F;                                                            
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: CAAT/ENHANCER BINDING PROTEIN BETA;                        
COMPND  11 CHAIN: A, B;                                                         
COMPND  12 FRAGMENT: BZIP DOMAIN;                                               
COMPND  13 SYNONYM: C/EBP BETA;                                                 
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 4;                                                           
COMPND  16 MOLECULE: RUNT-RELATED TRANSCRIPTION FACTOR 1;                       
COMPND  17 CHAIN: C;                                                            
COMPND  18 FRAGMENT: RUNT DOMAIN;                                               
COMPND  19 SYNONYM: CORE-BINDING FACTOR, ALPHA B SUBUNIT, PEPB2-ALPHA           
COMPND  20 B;                                                                   
COMPND  21 ENGINEERED: YES;                                                     
COMPND  22 MOL_ID: 5;                                                           
COMPND  23 MOLECULE: CORE-BINDING FACTOR, BETA SUBUNIT;                         
COMPND  24 CHAIN: D;                                                            
COMPND  25 FRAGMENT: CORE DOMAIN;                                               
COMPND  26 SYNONYM: PEBP2-BETA, CBF-BETA;                                       
COMPND  27 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 MOL_ID: 2;                                                           
SOURCE   4 SYNTHETIC: YES;                                                      
SOURCE   5 MOL_ID: 3;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   7 ORGANISM_COMMON: HUMAN;                                              
SOURCE   8 ORGANISM_TAXID: 9606;                                                
SOURCE   9 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  10 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  11 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  12 EXPRESSION_SYSTEM_VECTOR: PLASMID;                                   
SOURCE  13 EXPRESSION_SYSTEM_PLASMID: PAR2156;                                  
SOURCE  14 MOL_ID: 4;                                                           
SOURCE  15 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  16 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  17 ORGANISM_TAXID: 10090;                                               
SOURCE  18 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  20 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  21 EXPRESSION_SYSTEM_VECTOR: PLASMID;                                   
SOURCE  22 EXPRESSION_SYSTEM_PLASMID: PAR2156;                                  
SOURCE  23 MOL_ID: 5;                                                           
SOURCE  24 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  25 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  26 ORGANISM_TAXID: 10090;                                               
SOURCE  27 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  28 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  29 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  30 EXPRESSION_SYSTEM_VECTOR: PLASMID;                                   
SOURCE  31 EXPRESSION_SYSTEM_PLASMID: PAR2156                                   
KEYWDS    PROTEIN-DNA COMPLEX, TRANSCRIPTION FACTOR, BZIP, RUNX, RUNT,          
KEYWDS   2 C/EBP, CBF, CORE BINDING FACTOR, AML1, AML,                          
KEYWDS   3 TRANSCRIPTION/DNA COMPLEX                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.H.TAHIROV,K.OGATA                                                   
REVDAT   2   24-FEB-09 1IO4    1       VERSN                                    
REVDAT   1   12-MAR-01 1IO4    0                                                
JRNL        AUTH   T.H.TAHIROV,T.INOUE-BUNGO,H.MORII,A.FUJIKAWA,                
JRNL        AUTH 2 M.SASAKI,K.KIMURA,M.SHIINA,K.SATO,T.KUMASAKA,                
JRNL        AUTH 3 M.YAMAMOTO,S.ISHII,K.OGATA                                   
JRNL        TITL   STRUCTURAL ANALYSES OF DNA RECOGNITION BY THE                
JRNL        TITL 2 AML1/RUNX-1 RUNT DOMAIN AND ITS ALLOSTERIC CONTROL           
JRNL        TITL 3 BY CBFBETA.                                                  
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 104   755 2001              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   11257229                                                     
JRNL        DOI    10.1016/S0092-8674(01)00271-9                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   T.H.TAHIROV,T.INOUE,M.SASAKI,M.SHIINA,K.KIMURA,              
REMARK   1  AUTH 2 K.SATO,T.KUMASAKA,M.YAMAMOTO,N.KAMIYA,K.OGATA                
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSES OF            
REMARK   1  TITL 2 QUATERNARY, TERNARY AND BINARY PROTEIN-DNA                   
REMARK   1  TITL 3 COMPLEXES WITH INVOLVEMENT OF AML1/RUNX-1/CBFALPHA           
REMARK   1  TITL 4 RUNT DOMAIN, CBFBETA AND THE C/EBPBETA BZIP REGION           
REMARK   1  REF    TO BE PUBLISHED                                              
REMARK   1  REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.9                                              
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) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.95                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 461658.950                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 21111                          
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) : 0.247                           
REMARK   3   FREE R VALUE                     : 0.299                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1038                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.009                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.19                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3090                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4470                       
REMARK   3   BIN FREE R VALUE                    : 0.4640                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.60                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 150                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.038                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3126                                    
REMARK   3   NUCLEIC ACID ATOMS       : 1060                                    
REMARK   3   HETEROGEN ATOMS          : 3                                       
REMARK   3   SOLVENT ATOMS            : 8                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 45.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 82.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 29.96000                                             
REMARK   3    B22 (A**2) : -15.30000                                            
REMARK   3    B33 (A**2) : -14.66000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.45                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.64                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 20.00                           
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.57                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.64                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.10                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 14.090; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 18.800; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 20.260; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 23.660; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.20                                                 
REMARK   3   BSOL        : 25.00                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : DNA-RNA_REP.PARAM                              
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA.TOP                                    
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1IO4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JAN-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB005111.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-APR-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.60                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL45XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : DIAMOND                            
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   : 21113                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.1                               
REMARK 200  DATA REDUNDANCY                : 3.173                              
REMARK 200  R MERGE                    (I) : 0.06200                            
REMARK 200  R SYM                      (I) : 6.20000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.5000                            
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) : 3.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.25                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37200                            
REMARK 200  R SYM FOR SHELL            (I) : 37.20000                           
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: THREE WAVELENGTH FROM GOLD DERIVATIVE          
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: CNS 0.9                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M POTASSIUM CHLORIDE, 0.01 M         
REMARK 280  MAGNESIUM CHLORIDE, 0.01 M DTT, 4.5% V/V PEG 8000, 1% V/V           
REMARK 280  GLYCEROL, 1% V/V MPD, 0.05 M MES BUFFER PH 5.6, PH 5.60, VAPOR      
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 297K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       54.66300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       54.66300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       60.55400            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       81.80000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       60.55400            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       81.80000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       54.66300            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       60.55400            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       81.80000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       54.66300            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       60.55400            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       81.80000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, A, B, C, D                      
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     VAL A   259                                                      
REMARK 465     LYS A   260                                                      
REMARK 465     SER A   261                                                      
REMARK 465     LYS A   262                                                      
REMARK 465     ALA A   263                                                      
REMARK 465     LYS A   264                                                      
REMARK 465     LYS A   265                                                      
REMARK 465     THR A   266                                                      
REMARK 465     VAL A   267                                                      
REMARK 465     ASP A   268                                                      
REMARK 465     LYS A   332                                                      
REMARK 465     GLN A   333                                                      
REMARK 465     LEU A   334                                                      
REMARK 465     PRO A   335                                                      
REMARK 465     GLU A   336                                                      
REMARK 465     VAL B   259                                                      
REMARK 465     LYS B   260                                                      
REMARK 465     SER B   261                                                      
REMARK 465     LYS B   262                                                      
REMARK 465     ALA B   263                                                      
REMARK 465     LYS B   264                                                      
REMARK 465     PRO B   335                                                      
REMARK 465     GLU B   336                                                      
REMARK 465     ARG C   180                                                      
REMARK 465     GLN C   181                                                      
REMARK 465     LYS C   182                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ALA D    71                                                      
REMARK 465     SER D    72                                                      
REMARK 465     TRP D    73                                                      
REMARK 465     GLN D    74                                                      
REMARK 465     GLY D    75                                                      
REMARK 465     GLU D    76                                                      
REMARK 465     GLN D    77                                                      
REMARK 465     ARG D    78                                                      
REMARK 465     GLN D    79                                                      
REMARK 465     THR D    80                                                      
REMARK 465     PRO D    81                                                      
REMARK 465     GLN D   141                                                      
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    GLY C    95     NE2  GLN C   127              2.12            
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    SER A 271      155.25    -40.51                                   
REMARK 500    ILE A 276      -62.17    -96.66                                   
REMARK 500    LYS B 269        1.95    -66.84                                   
REMARK 500    SER B 271     -176.99    -50.14                                   
REMARK 500    PRO C  68        2.20    -63.77                                   
REMARK 500    ASN C  82        9.80     53.72                                   
REMARK 500    ASN C 109      137.95    171.42                                   
REMARK 500    ASN C 119       61.17     62.75                                   
REMARK 500    ASP C 133       60.32     66.54                                   
REMARK 500    ARG C 164       67.80     28.26                                   
REMARK 500    ARG D   9      -84.67    -32.89                                   
REMARK 500    GLU D  15      106.83    -46.62                                   
REMARK 500    GLU D  24      139.99    -27.28                                   
REMARK 500    HIS D  37      -49.80    -23.30                                   
REMARK 500    GLU D  38      -75.39    -41.99                                   
REMARK 500    PHE D  57       98.68    -68.41                                   
REMARK 500    ALA D  59      -77.28    -57.16                                   
REMARK 500    GLU D  89      -22.46    104.10                                   
REMARK 500    LEU D 116        2.43    -62.31                                   
REMARK 500    PHE D 127      100.14    -59.20                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500     DA F   6         0.06    SIDE_CHAIN                              
REMARK 500     DC F   7         0.07    SIDE_CHAIN                              
REMARK 500     DG F  18         0.05    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AU C 200                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AU D 200                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AU D 201                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1CL3   RELATED DB: PDB                                   
REMARK 900 MOLECULAR INSIGHTS INTO PEBP2/CBF-SMMHC ASSOCIATED ACUTE             
REMARK 900 LEUKEMIA REVEALED FROM THE THREE-DIMENSIONAL STRUCTURE OF            
REMARK 900 PEBP2/CBF BETA                                                       
REMARK 900 RELATED ID: 2JHB   RELATED DB: PDB                                   
REMARK 900 CORE BINDING FACTOR BETA                                             
REMARK 900 RELATED ID: 1CMO   RELATED DB: PDB                                   
REMARK 900 IMMUNOGLOBULIN MOTIF DEOXYRIBONUCLEIC ACID- RECOGNITION AND          
REMARK 900 HETERODIMERIZATION FOR THE PEBP2/CBF RUNT-DOMAIN                     
REMARK 900 RELATED ID: 1CO1   RELATED DB: PDB                                   
REMARK 900 FOLD OF THE CBFA                                                     
REMARK 900 RELATED ID: 1E50   RELATED DB: PDB                                   
REMARK 900 AML1/CBFBETA COMPLEX                                                 
REMARK 900 RELATED ID: 1HJB   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF RUNX-1/AML1/CBFALPHA RUNT DOMAIN AND            
REMARK 900 C/EBPBETA BZIP HOMODIMER BOUND TO A DNA FRAGMENT FROM THE            
REMARK 900 CSF-1R PROMOTER                                                      
REMARK 900 RELATED ID: 1HJC   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF RUNX-1/AML1/CBFALPHA RUNT DOMAIN BOUND          
REMARK 900 TO A DNA FRAGMENT FROM THE CSF-1R PROMOTER                           
DBREF  1IO4 A  259   336  UNP    P17676   CEBPB_HUMAN    259    336             
DBREF  1IO4 B  259   336  UNP    P17676   CEBPB_HUMAN    259    336             
DBREF  1IO4 C   60   182  UNP    Q03347   RUNX1_MOUSE     60    182             
DBREF  1IO4 D    1   141  UNP    Q08024   PEBB_MOUSE       1    141             
DBREF  1IO4 E    1    26  PDB    1IO4     1IO4             1     26             
DBREF  1IO4 F    1    26  PDB    1IO4     1IO4             1     26             
SEQRES   1 E   26   DG  DA  DA  DG  DA  DT  DT  DT  DC  DC  DA  DA  DA          
SEQRES   2 E   26   DC  DT  DC  DT  DG  DT  DG  DG  DT  DT  DG  DC  DG          
SEQRES   1 F   26   DC  DC  DG  DC  DA  DA  DC  DC  DA  DC  DA  DG  DA          
SEQRES   2 F   26   DG  DT  DT  DT  DG  DG  DA  DA  DA  DT  DC  DT  DT          
SEQRES   1 A   78  VAL LYS SER LYS ALA LYS LYS THR VAL ASP LYS HIS SER          
SEQRES   2 A   78  ASP GLU TYR LYS ILE ARG ARG GLU ARG ASN ASN ILE ALA          
SEQRES   3 A   78  VAL ARG LYS SER ARG ASP LYS ALA LYS MET ARG ASN LEU          
SEQRES   4 A   78  GLU THR GLN HIS LYS VAL LEU GLU LEU THR ALA GLU ASN          
SEQRES   5 A   78  GLU ARG LEU GLN LYS LYS VAL GLU GLN LEU SER ARG GLU          
SEQRES   6 A   78  LEU SER THR LEU ARG ASN LEU PHE LYS GLN LEU PRO GLU          
SEQRES   1 B   78  VAL LYS SER LYS ALA LYS LYS THR VAL ASP LYS HIS SER          
SEQRES   2 B   78  ASP GLU TYR LYS ILE ARG ARG GLU ARG ASN ASN ILE ALA          
SEQRES   3 B   78  VAL ARG LYS SER ARG ASP LYS ALA LYS MET ARG ASN LEU          
SEQRES   4 B   78  GLU THR GLN HIS LYS VAL LEU GLU LEU THR ALA GLU ASN          
SEQRES   5 B   78  GLU ARG LEU GLN LYS LYS VAL GLU GLN LEU SER ARG GLU          
SEQRES   6 B   78  LEU SER THR LEU ARG ASN LEU PHE LYS GLN LEU PRO GLU          
SEQRES   1 C  123  GLY GLU LEU VAL ARG THR ASP SER PRO ASN PHE LEU CYS          
SEQRES   2 C  123  SER VAL LEU PRO THR HIS TRP ARG CYS ASN LYS THR LEU          
SEQRES   3 C  123  PRO ILE ALA PHE LYS VAL VAL ALA LEU GLY ASP VAL PRO          
SEQRES   4 C  123  ASP GLY THR LEU VAL THR VAL MET ALA GLY ASN ASP GLU          
SEQRES   5 C  123  ASN TYR SER ALA GLU LEU ARG ASN ALA THR ALA ALA MET          
SEQRES   6 C  123  LYS ASN GLN VAL ALA ARG PHE ASN ASP LEU ARG PHE VAL          
SEQRES   7 C  123  GLY ARG SER GLY ARG GLY LYS SER PHE THR LEU THR ILE          
SEQRES   8 C  123  THR VAL PHE THR ASN PRO PRO GLN VAL ALA THR TYR HIS          
SEQRES   9 C  123  ARG ALA ILE LYS ILE THR VAL ASP GLY PRO ARG GLU PRO          
SEQRES  10 C  123  ARG ARG HIS ARG GLN LYS                                      
SEQRES   1 D  141  MET PRO ARG VAL VAL PRO ASP GLN ARG SER LYS PHE GLU          
SEQRES   2 D  141  ASN GLU GLU PHE PHE ARG LYS LEU SER ARG GLU CYS GLU          
SEQRES   3 D  141  ILE LYS TYR THR GLY PHE ARG ASP ARG PRO HIS GLU GLU          
SEQRES   4 D  141  ARG GLN THR ARG PHE GLN ASN ALA CYS ARG ASP GLY ARG          
SEQRES   5 D  141  SER GLU ILE ALA PHE VAL ALA THR GLY THR ASN LEU SER          
SEQRES   6 D  141  LEU GLN PHE PHE PRO ALA SER TRP GLN GLY GLU GLN ARG          
SEQRES   7 D  141  GLN THR PRO SER ARG GLU TYR VAL ASP LEU GLU ARG GLU          
SEQRES   8 D  141  ALA GLY LYS VAL TYR LEU LYS ALA PRO MET ILE LEU ASN          
SEQRES   9 D  141  GLY VAL CYS VAL ILE TRP LYS GLY TRP ILE ASP LEU HIS          
SEQRES  10 D  141  ARG LEU ASP GLY MET GLY CYS LEU GLU PHE ASP GLU GLU          
SEQRES  11 D  141  ARG ALA GLN GLN GLU ASP ALA LEU ALA GLN GLN                  
HET     AU  C 200       1                                                       
HET     AU  D 200       1                                                       
HET     AU  D 201       1                                                       
HETNAM      AU GOLD ION                                                         
FORMUL   7   AU    3(AU 1+)                                                     
FORMUL  10  HOH   *8(H2 O)                                                      
HELIX    1   1 SER A  271  LEU A  330  1                                  60    
HELIX    2   2 ASP B  272  LEU B  334  1                                  63    
HELIX    3   3 ASP D    7  GLU D   15  1                                   9    
HELIX    4   4 GLU D   15  ARG D   23  1                                   9    
HELIX    5   5 PRO D   36  GLY D   51  1                                  16    
HELIX    6   6 ASP D  128  ALA D  139  1                                  12    
SHEET    1   A14 ASN D  63  GLN D  67  0                                        
SHEET    2   A14 ARG D  52  PHE D  57 -1  O  SER D  53   N  LEU D  66           
SHEET    3   A14 CYS D  25  TYR D  29 -1  N  LYS D  28   O  ALA D  56           
SHEET    4   A14 ASP D 120  GLU D 126 -1  N  GLY D 121   O  ILE D  27           
SHEET    5   A14 CYS D 107  ASP D 115 -1  O  ILE D 109   N  GLU D 126           
SHEET    6   A14 VAL D  95  LEU D 103 -1  N  VAL D  95   O  ILE D 114           
SHEET    7   A14 GLN C 158  TYR C 162  1  N  VAL C 159   O  ILE D 102           
SHEET    8   A14 THR C 147  VAL C 152 -1  N  LEU C 148   O  TYR C 162           
SHEET    9   A14 LEU C 102  GLY C 108 -1  O  THR C 104   N  THR C 151           
SHEET   10   A14 THR C 121  LYS C 125 -1  N  ALA C 122   O  VAL C 103           
SHEET   11   A14 VAL C 128  ARG C 130 -1  O  VAL C 128   N  LYS C 125           
SHEET   12   A14 LYS C  90  ALA C  93 -1  O  VAL C  91   N  ALA C 129           
SHEET   13   A14 PHE C  70  SER C  73 -1  O  LEU C  71   N  VAL C  92           
SHEET   14   A14 LEU C  62  ARG C  64 -1  N  VAL C  63   O  CYS C  72           
SHEET    1   B 7 ASN D  63  GLN D  67  0                                        
SHEET    2   B 7 ARG D  52  PHE D  57 -1  O  SER D  53   N  LEU D  66           
SHEET    3   B 7 CYS D  25  TYR D  29 -1  N  LYS D  28   O  ALA D  56           
SHEET    4   B 7 ASP D 120  GLU D 126 -1  N  GLY D 121   O  ILE D  27           
SHEET    5   B 7 CYS D 107  ASP D 115 -1  O  ILE D 109   N  GLU D 126           
SHEET    6   B 7 VAL D  95  LEU D 103 -1  N  VAL D  95   O  ILE D 114           
SHEET    7   B 7 VAL D  86  ASP D  87 -1  N  ASP D  87   O  TYR D  96           
SHEET    1   C 2 HIS C  78  ARG C  80  0                                        
SHEET    2   C 2 LYS C 167  THR C 169  1  O  LYS C 167   N  TRP C  79           
SHEET    1   D 2 LEU C 117  ARG C 118  0                                        
SHEET    2   D 2 ARG C 135  PHE C 136 -1  O  ARG C 135   N  ARG C 118           
CISPEP   1 ASN C  155    PRO C  156          0         0.01                     
SITE     1 AC1  1 CYS C  81                                                     
SITE     1 AC2  2 GLU D  24  CYS D 124                                          
SITE     1 AC3  2 GLN D  45  CYS D  48                                          
CRYST1  121.108  163.600  109.326  90.00  90.00  90.00 C 2 2 21     16          
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      0.008257  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006112  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009147        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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