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Database: PDB
Entry: 1H8A
LinkDB: 1H8A
Original site: 1H8A 
HEADER    TRANSCRIPTION/DNA                       31-JAN-01   1H8A              
TITLE     CRYSTAL STRUCTURE OF TERNARY PROTEIN-DNA COMPLEX3                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAAT/ENHANCER BINDING PROTEIN BETA;                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 259-336;                                          
COMPND   5 SYNONYM: C/EBP BETA, NFIL-6;                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: MYB TRANSFORMING PROTEIN;                                  
COMPND   9 CHAIN: C;                                                            
COMPND  10 FRAGMENT: RESIDUES 1-128;                                            
COMPND  11 SYNONYM: AMV V-MYB;                                                  
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: DNA(5'-(*GP*AP*TP*GP*TP*GP*GP*CP*GP*CP*AP*                 
COMPND  15 AP*TP*CP*CP*TP*TP*AP*AP*CP*GP*GP*AP*CP*TP*G)-3');                    
COMPND  16 CHAIN: D;                                                            
COMPND  17 FRAGMENT: FRAGMENT FROM TOM-1A PROMOTER;                             
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 MOL_ID: 4;                                                           
COMPND  20 MOLECULE: DNA(5'-(*CP*CP*AP*GP*TP*CP*CP*GP*TP*TP*AP*                 
COMPND  21 AP*GP*GP*AP*TP*TP*GP*CP*GP*CP*CP*AP*CP*AP*T)-3');                    
COMPND  22 CHAIN: E;                                                            
COMPND  23 FRAGMENT: FRAGMENT FROM TOM-1A PROMOTER;                             
COMPND  24 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PAR2156;                                  
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: AVIAN MYELOBLASTOSIS VIRUS;                     
SOURCE  12 ORGANISM_TAXID: 11866;                                               
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  15 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  17 EXPRESSION_SYSTEM_PLASMID: PAR2156;                                  
SOURCE  18 MOL_ID: 3;                                                           
SOURCE  19 SYNTHETIC: YES;                                                      
SOURCE  20 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  21 ORGANISM_TAXID: 9606;                                                
SOURCE  22 MOL_ID: 4;                                                           
SOURCE  23 SYNTHETIC: YES;                                                      
SOURCE  24 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  25 ORGANISM_TAXID: 9606                                                 
KEYWDS    TRANSCRIPTION/DNA, PROTEIN-DNA COMPLEX, TRANSCRIPTION REGULATION,     
KEYWDS   2 BZIP, V-MYB, C-MYB, AMV, C/EBP, AVIAN MYELOBLASTOSIS VIRUS,          
KEYWDS   3 TRANSFORMING PROTEIN, TRANSCRIPTION-DNA COMPLEX                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.H.TAHIROV,K.OGATA                                                   
REVDAT   3   08-MAY-19 1H8A    1       SOURCE REMARK                            
REVDAT   2   24-FEB-09 1H8A    1       VERSN                                    
REVDAT   1   28-JAN-02 1H8A    0                                                
JRNL        AUTH   T.H.TAHIROV,K.SATO,E.ICHIKAWA-IWATA,M.SASAKI,T.INOUE-BUNGO,  
JRNL        AUTH 2 M.SHIINA,K.KIMURA,S.TAKATA,A.FUJIKAWA,H.MORII,T.KUMASAKA,    
JRNL        AUTH 3 M.YAMAMOTO,S.ISHII,K.OGATA                                   
JRNL        TITL   MECHANISM OF C-MYB-C/EBPBETA COOPERATION FROM SEPARATED      
JRNL        TITL 2 SITES ON A PROMOTER                                          
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 108    57 2002              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   11792321                                                     
JRNL        DOI    10.1016/S0092-8674(01)00636-5                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   T.H.TAHIROV,T.INOUE,M.SASAKI,M.SHIINA,K.KIMURA,K.SATO,       
REMARK   1  AUTH 2 T.KUMASAKA,M.YAMAMOTO,N.KAMIYA,K.OGATA                       
REMARK   1  TITL   CRYSTALS OF TERNARY PROTEIN-DNA COMPLEXES COMPOSED OF        
REMARK   1  TITL 2 DNA-BINDING DOMAINS C-MYB OR V-MYB, C/EBPALPHA OR C/EBPBETA  
REMARK   1  TITL 3 AND TOM-1A PROMOTER FRAGMENT                                 
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  57  1655 2001              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   1  PMID   11679735                                                     
REMARK   1  DOI    10.1107/S0907444901011982                                    
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   T.H.TAHIROV,H.MORII,H.UEDAIRA,M.SASAKI,A.SARAI,S.ADACHI,     
REMARK   1  AUTH 2 S.Y.PARK,N.KAMIYA,K.OGATA                                    
REMARK   1  TITL   CRYSTAL STRUCTURES OF C-MYB DNA-BINDING DOMAIN IN FREE       
REMARK   1  TITL 2 STATE: AN EVIDENCE FOR BINDING OF NA+ AND COMPARISON WITH    
REMARK   1  TITL 3 SOLUTION STRUCTURE                                           
REMARK   1  REF    TO BE PUBLISHED                                              
REMARK   1  REFN                                                                
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   T.H.TAHIROV,T.INOUE-BUNGO,H.MORII,A.FUJIKAWA,M.SASAKI,       
REMARK   1  AUTH 2 K.KIMURA,M.SHIINA,K.SATO,T.KUMASAKA,M.YAMAMOTO,S.ISHII,      
REMARK   1  AUTH 3 K.OGATA                                                      
REMARK   1  TITL   STRUCTURAL ANALYSES OF DNA RECOGNITION BY THE AML1/ RUNX-1   
REMARK   1  TITL 2 RUNT DOMAIN AND ITS ALLOSTERIC CONTROL BY CBFBETA            
REMARK   1  REF    CELL(CAMBRIDGE,MASS.)         V. 104   755 2001              
REMARK   1  REFN                   ISSN 0092-8674                               
REMARK   1  PMID   11257229                                                     
REMARK   1  DOI    10.1016/S0092-8674(01)00271-9                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.23 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 : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.23                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.85                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2363401.120                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 35692                          
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) : 0.245                           
REMARK   3   FREE R VALUE                     : 0.288                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1765                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
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) : 2.23                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.37                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5429                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3760                       
REMARK   3   BIN FREE R VALUE                    : 0.3760                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 275                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.023                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2045                                    
REMARK   3   NUCLEIC ACID ATOMS       : 1060                                    
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 171                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 67.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 64.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.93000                                             
REMARK   3    B22 (A**2) : -12.25000                                            
REMARK   3    B33 (A**2) : 14.18000                                             
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) : 0.37                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.37                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 20.0                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.44                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.37                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.100                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 17.80                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.190                           
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) : 6.190 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 7.980 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 8.450 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 10.510; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.28                                                 
REMARK   3   BSOL        : 39.30                                                
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: BULK SOLVENT MODEL USED. ATOMS C, O, N,   
REMARK   3  CA AND CB ARE HARMONICALLY RESTRAINED DURING REFINEMENT WITH        
REMARK   3  HARMONIC RESTRAINT CONSTANT OF 20 TWO DATA SETS WERE COLLECTED      
REMARK   3  FROM ONE CRYSTAL. FIRST 120 IMAGES WERE OBTAINED WITH EXPOSURE      
REMARK   3  TIME OF 200 SEC, OSCILLATION ANGLE OF 1 DEGREE AND CRYSTAL TO       
REMARK   3  DETECTOR DISTANCE OF 240 MM. ANOTHER 60 IMAGES WERE OBTAINED        
REMARK   3  WITH EXPOSURE TIME OF 30 SEC, OSCILLATION ANGLE OF 1.5 DEGREES      
REMARK   3  AND CRYSTAL TO DETECTOR DISTANCE OF 420 MM.                         
REMARK   4                                                                      
REMARK   4 1H8A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-JAN-01.                  
REMARK 100 THE DEPOSITION ID IS D_1290005852.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-APR-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.00                               
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) : 1.020                              
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   : 42104                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
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     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY                : 3.868                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.9495                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.17                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.56                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.38900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.784                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS 0.9                                               
REMARK 200 STARTING MODEL: 1H88                                                 
REMARK 200                                                                      
REMARK 200 REMARK: LEUCINE ZIPPER OF C/EBP BETA AND C-MYB REPEAT 1 WERE         
REMARK 200  EXCLUDED FROM STARTING MODEL.                                       
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.61                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.04 M MAGNESIUM CHLORIDE, 20% V/V       
REMARK 280  MPD, 0.05 M SODIUM CACODYLATE BUFFER PH 6.0 AT 24 DEGREES C, PH     
REMARK 280  6.00, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 297K               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       54.93000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       83.35000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       54.93000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       83.35000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: OF C/EBP BETA AND MONOMER OF MYB                             
REMARK 300  TRANSFORMING PROTEINBOUND TO A DUPLEX DNA                           
REMARK 300  FRAGMENTFOR THE HETERO-ASSEMBLY DESCRIBED BY REMARK                 
REMARK 300   350.                                                               
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: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E                         
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 C/EBP BETA IS IMPORTANT TRANSCRIPTIONAL ACTIVATOR IN THE REGULATION  
REMARK 400  OF GENES INVOLVED IN IMMUNE AND INFLAMMATORY RESPONSES. SPECIFICALL 
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     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     LYS B   265                                                      
REMARK 465     THR B   266                                                      
REMARK 465     VAL B   267                                                      
REMARK 465     PRO B   335                                                      
REMARK 465     GLU B   336                                                      
REMARK 465     MET C    66                                                      
REMARK 465     GLU C    67                                                      
REMARK 465     ALA C    68                                                      
REMARK 465     VAL C    69                                                      
REMARK 465     ILE C    70                                                      
REMARK 465     LYS C    71                                                      
REMARK 465     ASN C    72                                                      
REMARK 465     ARG C    73                                                      
REMARK 465     THR C    74                                                      
REMARK 465     ASP C    75                                                      
REMARK 465     VAL C    76                                                      
REMARK 465     GLN C    77                                                      
REMARK 465     CYS C    78                                                      
REMARK 465     GLN C    79                                                      
REMARK 465     HIS C    80                                                      
REMARK 465     ARG C    81                                                      
REMARK 465     TRP C    82                                                      
REMARK 465     GLN C    83                                                      
REMARK 465     LYS C    84                                                      
REMARK 465     VAL C    85                                                      
REMARK 465     LEU C    86                                                      
REMARK 465     LYS C   192                                                      
REMARK 465     VAL C   193                                                      
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     DT D  13   O4' -  C1' -  N1  ANGL. DEV. =   2.9 DEGREES          
REMARK 500     DG E  13   O4' -  C1' -  N9  ANGL. DEV. =   1.9 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                                                                      
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 B 271     -175.89    -62.69                                   
REMARK 500    LYS C 160       41.34    -83.81                                   
REMARK 500    ARG C 161      -36.00   -157.24                                   
REMARK 500    ASN C 164       40.85    -67.91                                   
REMARK 500    SER C 187      -81.64   -103.26                                   
REMARK 500    THR C 188      -77.39    -58.11                                   
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     DG D   1         0.07    SIDE CHAIN                              
REMARK 500     DA D   2         0.07    SIDE CHAIN                              
REMARK 500     DC E   1         0.06    SIDE CHAIN                              
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 A2008        DISTANCE =  5.92 ANGSTROMS                       
REMARK 525    HOH B2016        DISTANCE =  5.90 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1H88   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF TERNARY PROTEIN-DNA COMPLEX1                    
REMARK 900 RELATED ID: 1H89   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF TERNARY PROTEIN-DNA COMPLEX2                    
REMARK 900 RELATED ID: 1HJB   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF RUNX-1/AML1/CBFALPHA RUNT DOMAIN AND C/EBPBETA  
REMARK 900 BZIP DIMERIC BOUND TO A DNA FRAGMENT FROM THE CSF-1R PROMOTER        
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 NUMBERING OF AMV V-MYB AMINO ACID                                    
REMARK 999 SEQUENCE WAS CHANGED IN ORDER TO MAKE THE                            
REMARK 999 COMPARISON WITH STRUCTURES OF MOUSE                                  
REMARK 999 C-MYB MORE CONVENIENT                                                
DBREF  1H8A A  259   336  UNP    P17676   CEBB_HUMAN     259    336             
DBREF  1H8A B  259   336  UNP    P17676   CEBB_HUMAN     259    336             
DBREF  1H8A C   66    71  PDB    1H8A     1H8A            66     71             
DBREF  1H8A C   72   193  UNP    P01104   MYB_AVIMB        1    122             
DBREF  1H8A D    1    26  PDB    1H8A     1H8A             1     26             
DBREF  1H8A E    1    26  PDB    1H8A     1H8A             1     26             
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  128  MET GLU ALA VAL ILE LYS ASN ARG THR ASP VAL GLN CYS          
SEQRES   2 C  128  GLN HIS ARG TRP GLN LYS VAL LEU ASN PRO GLU LEU ASN          
SEQRES   3 C  128  LYS GLY PRO TRP THR LYS GLU GLU ASP GLN ARG VAL ILE          
SEQRES   4 C  128  GLU HIS VAL GLN LYS TYR GLY PRO LYS ARG TRP SER ASP          
SEQRES   5 C  128  ILE ALA LYS HIS LEU LYS GLY ARG ILE GLY LYS GLN CYS          
SEQRES   6 C  128  ARG GLU ARG TRP HIS ASN HIS LEU ASN PRO GLU VAL LYS          
SEQRES   7 C  128  LYS THR SER TRP THR GLU GLU GLU ASP ARG ILE ILE TYR          
SEQRES   8 C  128  GLN ALA HIS LYS ARG LEU GLY ASN ARG TRP ALA GLU ILE          
SEQRES   9 C  128  ALA LYS LEU LEU PRO GLY ARG THR ASP ASN ALA VAL LYS          
SEQRES  10 C  128  ASN HIS TRP ASN SER THR MET ARG ARG LYS VAL                  
SEQRES   1 D   26   DG  DA  DT  DG  DT  DG  DG  DC  DG  DC  DA  DA  DT          
SEQRES   2 D   26   DC  DC  DT  DT  DA  DA  DC  DG  DG  DA  DC  DT  DG          
SEQRES   1 E   26   DC  DC  DA  DG  DT  DC  DC  DG  DT  DT  DA  DA  DG          
SEQRES   2 E   26   DG  DA  DT  DT  DG  DC  DG  DC  DC  DA  DC  DA  DT          
FORMUL   6  HOH   *171(H2 O)                                                    
HELIX    1   1 SER A  271  ASN A  329  1                                  59    
HELIX    2   2 LEU A  330  LYS A  332  5                                   3    
HELIX    3   3 SER B  271  GLN B  333  1                                  63    
HELIX    4   4 THR C   96  TYR C  110  1                                  15    
HELIX    5   5 ARG C  114  LEU C  122  1                                   9    
HELIX    6   6 ILE C  126  HIS C  137  1                                  12    
HELIX    7   7 THR C  148  GLY C  163  1                                  16    
HELIX    8   8 ARG C  165  ALA C  170  1                                   6    
HELIX    9   9 LYS C  171  LEU C  173  5                                   3    
HELIX   10  10 THR C  177  SER C  187  1                                  11    
CRYST1  109.860  166.700   39.600  90.00  90.00  90.00 P 21 21 2     8          
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      0.009102  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005999  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.025253        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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