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Database: PDB
Entry: 1H9D
LinkDB: 1H9D
Original site: 1H9D 
HEADER    TRANSCRIPTION FACTOR                    07-MAR-01   1H9D              
TITLE     AML1/CBF-BETA/DNA COMPLEX                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CORE-BINDING FACTOR ALPHA SUBUNIT1;                        
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: RUNT DOMAIN RESIDUES 50-183;                               
COMPND   5 SYNONYM: CBFA2/PEPBP2AB/RUNX1, AML-1;                                
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CORE-BINDING FACTOR CBF-BETA;                              
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 FRAGMENT: HETERODIMERISATION DOMAIN RESIDUES 2-135;                  
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: DNA (5'-(*GP*TP*TP*GP*CP*GP*GP*TP*TP*G)-3');               
COMPND  14 CHAIN: E, G;                                                         
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MOL_ID: 4;                                                           
COMPND  17 MOLECULE: DNA (5'-(*CP*AP*AP*CP*CP*GP*CP*AP*AP*C)-3');               
COMPND  18 CHAIN: F, H;                                                         
COMPND  19 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: AML1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: C41;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PRSET;                                    
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: CBFB;                                                          
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_VARIANT: C41;                                      
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PRSET;                                    
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 SYNTHETIC: YES;                                                      
SOURCE  23 MOL_ID: 4;                                                           
SOURCE  24 SYNTHETIC: YES                                                       
KEYWDS    TRANSCRIPTION FACTOR                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.BRAVO,A.J.WARREN                                                    
REVDAT   6   24-JAN-18 1H9D    1       SOURCE REMARK                            
REVDAT   5   24-FEB-09 1H9D    1       VERSN                                    
REVDAT   4   05-MAR-03 1H9D    1       REMARK HETATM                            
REVDAT   3   02-JUL-02 1H9D    1       ATOM                                     
REVDAT   2   16-AUG-01 1H9D    1       REMARK SHEET  MASTER                     
REVDAT   1   31-MAR-01 1H9D    0                                                
JRNL        AUTH   J.BRAVO,Z.LI,N.A.SPECK,A.J.WARREN                            
JRNL        TITL   THE LEUKEMIA-ASSOCIATED AML1 (RUNX1)-CBFBETA COMPLEX         
JRNL        TITL 2 FUNCTIONS AS A DNA-INDUCED MOLECULAR CLAMP                   
JRNL        REF    NAT.STRUCT.BIOL.              V.   8   371 2001              
JRNL        REFN                   ISSN 1072-8368                               
JRNL        PMID   11276260                                                     
JRNL        DOI    10.1038/86264                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.02                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1104447.410                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 27926                          
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) : 0.237                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2272                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
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) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.76                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4174                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3600                       
REMARK   3   BIN FREE R VALUE                    : 0.4070                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 8.10                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 367                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.021                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4003                                    
REMARK   3   NUCLEIC ACID ATOMS       : 808                                     
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 56                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 60.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 48.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 8.93000                                              
REMARK   3    B22 (A**2) : 8.93000                                              
REMARK   3    B33 (A**2) : -17.85000                                            
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) : 0.36                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.39                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
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) : 0.44                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.017                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.900                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.540                           
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) : 1.210 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.090 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.820 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.750 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.38                                                 
REMARK   3   BSOL        : 44.39                                                
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   : &_1_TOPOLOGY_INFILE_1                          
REMARK   3  TOPOLOGY FILE  2   : &_1_TOPOLOGY_INFILE_2                          
REMARK   3  TOPOLOGY FILE  3   : &_1_TOPOLOGY_INFILE_3                          
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1H9D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-MAR-01.                  
REMARK 100 THE DEPOSITION ID IS D_1290005776.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-OCT-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 110.0                              
REMARK 200  PH                             : 6.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-3                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9366                             
REMARK 200  MONOCHROMATOR                  : DIAMOND (111)                      
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27926                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 6.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.12600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.38000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1E50                                       
REMARK 200                                                                      
REMARK 200 REMARK: ON HOLD                                                      
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.50                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
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   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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       66.96250            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       57.51650            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       57.51650            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      100.44375            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       57.51650            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       57.51650            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       33.48125            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       57.51650            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       57.51650            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      100.44375            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       57.51650            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       57.51650            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       33.48125            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       66.96250            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 4800 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18270 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 4830 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18390 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.5 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, G, H                            
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     SER A    50                                                      
REMARK 465     MET A    51                                                      
REMARK 465     VAL A    52                                                      
REMARK 465     GLU A    53                                                      
REMARK 465     HIS A   179                                                      
REMARK 465     ARG A   180                                                      
REMARK 465     GLN A   181                                                      
REMARK 465     LYS A   182                                                      
REMARK 465     LEU A   183                                                      
REMARK 465     ALA B    71                                                      
REMARK 465     SER B    72                                                      
REMARK 465     TRP B    73                                                      
REMARK 465     GLN B    74                                                      
REMARK 465     GLY B    75                                                      
REMARK 465     GLU B    76                                                      
REMARK 465     GLN B    77                                                      
REMARK 465     ARG B    78                                                      
REMARK 465     GLN B    79                                                      
REMARK 465     SER C    50                                                      
REMARK 465     MET C    51                                                      
REMARK 465     VAL C    52                                                      
REMARK 465     GLU C    53                                                      
REMARK 465     HIS C   179                                                      
REMARK 465     ARG C   180                                                      
REMARK 465     GLN C   181                                                      
REMARK 465     LYS C   182                                                      
REMARK 465     LEU C   183                                                      
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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     VAL A  54    CG1  CG2                                            
REMARK 470     LEU A  55    CG   CD1  CD2                                       
REMARK 470     ASP A  57    CG   OD1  OD2                                       
REMARK 470     ARG A 178    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL C  54    CG1  CG2                                            
REMARK 470     LEU C  55    CG   CD1  CD2                                       
REMARK 470     ASP C  57    CG   OD1  OD2                                       
REMARK 470     ARG C 178    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TRP D  73    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP D  73    CZ3  CH2                                            
REMARK 470     GLN D  74    CG   CD   OE1  NE2                                  
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C  SSEQI                                                     
REMARK 475     VAL A    54                                                      
REMARK 475     LEU A    55                                                      
REMARK 475     ALA A    56                                                      
REMARK 475     ARG A   178                                                      
REMARK 475     VAL C    54                                                      
REMARK 475     LEU C    55                                                      
REMARK 475     ARG C   178                                                      
REMARK 475     TRP D    73                                                      
REMARK 475     GLN D    74                                                      
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   N1    DA H     8     O    HOH H  2002              2.14            
REMARK 500   OH   TYR C   113     NH1  ARG D    33              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS A  81   CB    CYS A  81   SG     -0.110                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500     DT E   2   O5' -  P   -  OP1 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500     DC F   1   O5' -  C5' -  C4' ANGL. DEV. =  -5.2 DEGREES          
REMARK 500     DA F   3   N9  -  C1' -  C2' ANGL. DEV. = -11.7 DEGREES          
REMARK 500     DC F   7   O4' -  C1' -  N1  ANGL. DEV. =   2.4 DEGREES          
REMARK 500     DC G   5   N1  -  C1' -  C2' ANGL. DEV. =   9.3 DEGREES          
REMARK 500     DC G   5   O4' -  C1' -  N1  ANGL. DEV. =   1.8 DEGREES          
REMARK 500     DA H   3   C4' -  C3' -  O3' ANGL. DEV. =  12.3 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    ALA A  56      114.02     74.27                                   
REMARK 500    ASP A  57       86.13    152.38                                   
REMARK 500    HIS A  58      -21.35   -148.17                                   
REMARK 500    LEU A  94      -72.22    -79.05                                   
REMARK 500    ARG A 142      139.00    -39.79                                   
REMARK 500    PHE B  32       50.36     36.18                                   
REMARK 500    GLU B  89      -79.00    -72.04                                   
REMARK 500    ARG B  90      -54.73      3.15                                   
REMARK 500    ALA C  56      110.32     71.94                                   
REMARK 500    ASP C  57       87.87    156.30                                   
REMARK 500    HIS C  58      -26.19   -149.27                                   
REMARK 500    ASP C  66        0.94    -68.25                                   
REMARK 500    ASN C 109     -176.98   -173.37                                   
REMARK 500    ALA C 120       36.31    -86.70                                   
REMARK 500    SER D  72      108.36    103.08                                   
REMARK 500    GLU D  89      -77.93    -73.84                                   
REMARK 500    ARG D  90      -53.97      4.04                                   
REMARK 500    LEU D 116       -5.08    -59.23                                   
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     DC F   4         0.09    SIDE CHAIN                              
REMARK 500     DG F   6         0.06    SIDE CHAIN                              
REMARK 500     DC F  10         0.07    SIDE CHAIN                              
REMARK 500     DG G   1         0.05    SIDE CHAIN                              
REMARK 500     DC H   4         0.12    SIDE CHAIN                              
REMARK 500     DA H   8         0.06    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
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/CBF-BETA COMPLEX                                                
REMARK 900 RELATED ID: 1CL3   RELATED DB: PDB                                   
REMARK 900 MOLECULAR INSIGHTS INTO PEBP2/CBF-SMMHC ASSOCIATED ACUTE LEUKEMIA    
REMARK 900 REVEALED FROM THE THREE-DIMENSIONAL STRUCTURE OF PEBP2/CBF BETA      
DBREF  1H9D A   50   183  UNP    Q01196   AML1_HUMAN      50    183             
DBREF  1H9D B    2   135  UNP    Q13951   PEBB_HUMAN       2    135             
DBREF  1H9D C   50   183  UNP    Q01196   AML1_HUMAN      50    183             
DBREF  1H9D D    2   135  UNP    Q13951   PEBB_HUMAN       2    135             
DBREF  1H9D E    1    10  PDB    1H9D     1H9D             1     10             
DBREF  1H9D F    1    10  PDB    1H9D     1H9D             1     10             
DBREF  1H9D G    1    10  PDB    1H9D     1H9D             1     10             
DBREF  1H9D H    1    10  PDB    1H9D     1H9D             1     10             
SEQRES   1 A  134  SER MET VAL GLU VAL LEU ALA ASP HIS PRO GLY GLU LEU          
SEQRES   2 A  134  VAL ARG THR ASP SER PRO ASN PHE LEU CYS SER VAL LEU          
SEQRES   3 A  134  PRO THR HIS TRP ARG CYS ASN LYS THR LEU PRO ILE ALA          
SEQRES   4 A  134  PHE LYS VAL VAL ALA LEU GLY ASP VAL PRO ASP GLY THR          
SEQRES   5 A  134  LEU VAL THR VAL MET ALA GLY ASN ASP GLU ASN TYR SER          
SEQRES   6 A  134  ALA GLU LEU ARG ASN ALA THR ALA ALA MET LYS ASN GLN          
SEQRES   7 A  134  VAL ALA ARG PHE ASN ASP LEU ARG PHE VAL GLY ARG SER          
SEQRES   8 A  134  GLY ARG GLY LYS SER PHE THR LEU THR ILE THR VAL PHE          
SEQRES   9 A  134  THR ASN PRO PRO GLN VAL ALA THR TYR HIS ARG ALA ILE          
SEQRES  10 A  134  LYS ILE THR VAL ASP GLY PRO ARG GLU PRO ARG ARG HIS          
SEQRES  11 A  134  ARG GLN LYS LEU                                              
SEQRES   1 B  134  PRO ARG VAL VAL PRO ASP GLN ARG SER LYS PHE GLU ASN          
SEQRES   2 B  134  GLU GLU PHE PHE ARG LYS LEU SER ARG GLU CYS GLU ILE          
SEQRES   3 B  134  LYS TYR THR GLY PHE ARG ASP ARG PRO HIS GLU GLU ARG          
SEQRES   4 B  134  GLN ALA ARG PHE GLN ASN ALA CYS ARG ASP GLY ARG SER          
SEQRES   5 B  134  GLU ILE ALA PHE VAL ALA THR GLY THR ASN LEU SER LEU          
SEQRES   6 B  134  GLN PHE PHE PRO ALA SER TRP GLN GLY GLU GLN ARG GLN          
SEQRES   7 B  134  THR PRO SER ARG GLU TYR VAL ASP LEU GLU ARG GLU ALA          
SEQRES   8 B  134  GLY LYS VAL TYR LEU LYS ALA PRO MET ILE LEU ASN GLY          
SEQRES   9 B  134  VAL CYS VAL ILE TRP LYS GLY TRP ILE ASP LEU GLN ARG          
SEQRES  10 B  134  LEU ASP GLY MET GLY CYS LEU GLU PHE ASP GLU GLU ARG          
SEQRES  11 B  134  ALA GLN GLN GLU                                              
SEQRES   1 C  134  SER MET VAL GLU VAL LEU ALA ASP HIS PRO GLY GLU LEU          
SEQRES   2 C  134  VAL ARG THR ASP SER PRO ASN PHE LEU CYS SER VAL LEU          
SEQRES   3 C  134  PRO THR HIS TRP ARG CYS ASN LYS THR LEU PRO ILE ALA          
SEQRES   4 C  134  PHE LYS VAL VAL ALA LEU GLY ASP VAL PRO ASP GLY THR          
SEQRES   5 C  134  LEU VAL THR VAL MET ALA GLY ASN ASP GLU ASN TYR SER          
SEQRES   6 C  134  ALA GLU LEU ARG ASN ALA THR ALA ALA MET LYS ASN GLN          
SEQRES   7 C  134  VAL ALA ARG PHE ASN ASP LEU ARG PHE VAL GLY ARG SER          
SEQRES   8 C  134  GLY ARG GLY LYS SER PHE THR LEU THR ILE THR VAL PHE          
SEQRES   9 C  134  THR ASN PRO PRO GLN VAL ALA THR TYR HIS ARG ALA ILE          
SEQRES  10 C  134  LYS ILE THR VAL ASP GLY PRO ARG GLU PRO ARG ARG HIS          
SEQRES  11 C  134  ARG GLN LYS LEU                                              
SEQRES   1 D  134  PRO ARG VAL VAL PRO ASP GLN ARG SER LYS PHE GLU ASN          
SEQRES   2 D  134  GLU GLU PHE PHE ARG LYS LEU SER ARG GLU CYS GLU ILE          
SEQRES   3 D  134  LYS TYR THR GLY PHE ARG ASP ARG PRO HIS GLU GLU ARG          
SEQRES   4 D  134  GLN ALA ARG PHE GLN ASN ALA CYS ARG ASP GLY ARG SER          
SEQRES   5 D  134  GLU ILE ALA PHE VAL ALA THR GLY THR ASN LEU SER LEU          
SEQRES   6 D  134  GLN PHE PHE PRO ALA SER TRP GLN GLY GLU GLN ARG GLN          
SEQRES   7 D  134  THR PRO SER ARG GLU TYR VAL ASP LEU GLU ARG GLU ALA          
SEQRES   8 D  134  GLY LYS VAL TYR LEU LYS ALA PRO MET ILE LEU ASN GLY          
SEQRES   9 D  134  VAL CYS VAL ILE TRP LYS GLY TRP ILE ASP LEU GLN ARG          
SEQRES  10 D  134  LEU ASP GLY MET GLY CYS LEU GLU PHE ASP GLU GLU ARG          
SEQRES  11 D  134  ALA GLN GLN GLU                                              
SEQRES   1 E   10   DG  DT  DT  DG  DC  DG  DG  DT  DT  DG                      
SEQRES   1 F   10   DC  DA  DA  DC  DC  DG  DC  DA  DA  DC                      
SEQRES   1 G   10   DG  DT  DT  DG  DC  DG  DG  DT  DT  DG                      
SEQRES   1 H   10   DC  DA  DA  DC  DC  DG  DC  DA  DA  DC                      
FORMUL   9  HOH   *56(H2 O)                                                     
HELIX    1   1 ASP B    7  GLU B   15  1                                   9    
HELIX    2   2 GLU B   15  LYS B   20  1                                   6    
HELIX    3   3 PRO B   36  ASP B   50  1                                  15    
HELIX    4   4 ASP B  128  GLU B  135  1                                   8    
HELIX    5   5 ASP D    7  GLU D   15  1                                   9    
HELIX    6   6 GLU D   15  ARG D   23  1                                   9    
HELIX    7   7 PRO D   36  ASP D   50  1                                  15    
HELIX    8   8 ASP D  128  GLU D  135  1                                   8    
SHEET    1  AA 9 LEU A  62  ARG A  64  0                                        
SHEET    2  AA 9 PHE A  70  SER A  73 -1  O  CYS A  72   N  VAL A  63           
SHEET    3  AA 9 LYS A  90  ALA A  93 -1  O  LYS A  90   N  SER A  73           
SHEET    4  AA 9 VAL A 128  ARG A 130 -1  O  ALA A 129   N  VAL A  91           
SHEET    5  AA 9 THR A 121  LYS A 125 -1  O  ALA A 123   N  ARG A 130           
SHEET    6  AA 9 LEU A 102  GLY A 108 -1  O  VAL A 103   N  ALA A 122           
SHEET    7  AA 9 PHE A 146  VAL A 152 -1  O  THR A 147   N  GLY A 108           
SHEET    8  AA 9 GLN A 158  THR A 169 -1  O  GLN A 158   N  VAL A 152           
SHEET    9  AA 9 HIS A  78  ARG A  80  1  O  TRP A  79   N  THR A 169           
SHEET    1  AB 9 LEU A  62  ARG A  64  0                                        
SHEET    2  AB 9 PHE A  70  SER A  73 -1  O  CYS A  72   N  VAL A  63           
SHEET    3  AB 9 LYS A  90  ALA A  93 -1  O  LYS A  90   N  SER A  73           
SHEET    4  AB 9 VAL A 128  ARG A 130 -1  O  ALA A 129   N  VAL A  91           
SHEET    5  AB 9 THR A 121  LYS A 125 -1  O  ALA A 123   N  ARG A 130           
SHEET    6  AB 9 LEU A 102  GLY A 108 -1  O  VAL A 103   N  ALA A 122           
SHEET    7  AB 9 PHE A 146  VAL A 152 -1  O  THR A 147   N  GLY A 108           
SHEET    8  AB 9 GLN A 158  THR A 169 -1  O  GLN A 158   N  VAL A 152           
SHEET    9  AB 9 LYS B  94  LEU B 103  1  O  ILE B 102   N  VAL A 159           
SHEET    1  AC 2 LEU A 117  ARG A 118  0                                        
SHEET    2  AC 2 ARG A 135  PHE A 136 -1  O  ARG A 135   N  ARG A 118           
SHEET    1  CA 9 LEU C  62  ARG C  64  0                                        
SHEET    2  CA 9 PHE C  70  SER C  73 -1  O  CYS C  72   N  VAL C  63           
SHEET    3  CA 9 LYS C  90  ALA C  93 -1  O  LYS C  90   N  SER C  73           
SHEET    4  CA 9 VAL C 128  ARG C 130 -1  O  ALA C 129   N  VAL C  91           
SHEET    5  CA 9 THR C 121  LYS C 125 -1  O  ALA C 123   N  ARG C 130           
SHEET    6  CA 9 LEU C 102  GLY C 108 -1  O  VAL C 103   N  ALA C 122           
SHEET    7  CA 9 PHE C 146  VAL C 152 -1  O  THR C 147   N  GLY C 108           
SHEET    8  CA 9 GLN C 158  THR C 169 -1  O  GLN C 158   N  VAL C 152           
SHEET    9  CA 9 HIS C  78  ARG C  80  1  O  TRP C  79   N  THR C 169           
SHEET    1  CB 9 LEU C  62  ARG C  64  0                                        
SHEET    2  CB 9 PHE C  70  SER C  73 -1  O  CYS C  72   N  VAL C  63           
SHEET    3  CB 9 LYS C  90  ALA C  93 -1  O  LYS C  90   N  SER C  73           
SHEET    4  CB 9 VAL C 128  ARG C 130 -1  O  ALA C 129   N  VAL C  91           
SHEET    5  CB 9 THR C 121  LYS C 125 -1  O  ALA C 123   N  ARG C 130           
SHEET    6  CB 9 LEU C 102  GLY C 108 -1  O  VAL C 103   N  ALA C 122           
SHEET    7  CB 9 PHE C 146  VAL C 152 -1  O  THR C 147   N  GLY C 108           
SHEET    8  CB 9 GLN C 158  THR C 169 -1  O  GLN C 158   N  VAL C 152           
SHEET    9  CB 9 LYS D  94  LEU D 103  1  O  ILE D 102   N  VAL C 159           
SHEET    1  CC 2 LEU C 117  ARG C 118  0                                        
SHEET    2  CC 2 ARG C 135  PHE C 136 -1  O  ARG C 135   N  ARG C 118           
CISPEP   1 ASN A  155    PRO A  156          0        -0.15                     
CISPEP   2 ASN C  155    PRO C  156          0        -0.31                     
CRYST1  115.033  115.033  133.925  90.00  90.00  90.00 P 43 21 2    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      0.008693  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008693  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007467        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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