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Database: PDB
Entry: 1HJB
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Original site: 1HJB 
HEADER    TRANSCRIPTION/DNA                       11-JAN-01   1HJB              
TITLE     CRYSTAL STRUCTURE OF RUNX-1/AML1/CBFALPHA RUNT DOMAIN AND C/EBPBETA   
TITLE    2 BZIP HOMODIMER BOUND TO A DNA FRAGMENT FROM THE CSF-1R PROMOTER      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CCAAT/ENHANCER BINDING PROTEIN BETA;                       
COMPND   3 CHAIN: A, B, D, E;                                                   
COMPND   4 FRAGMENT: RESIDUES 259-345;                                          
COMPND   5 SYNONYM: C/EBP BETA, NFIL-6;                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: RUNT-RELATED TRANSCRIPTION FACTOR 1;                       
COMPND   9 CHAIN: C, F;                                                         
COMPND  10 FRAGMENT: RESIDUES 60-182;                                           
COMPND  11 SYNONYM: CORE BINDING FACTOR ALPHA, RUNX-1, AML1, PEBP2ALPHAB, CBFA2;
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: DNA (5'-(*GP*AP*AP*GP*AP*TP*TP*TP*CP*CP*                   
COMPND  15 AP*AP*AP*CP*TP*CP*TP*GP*TP*GP*GP*TP*TP*GP*CP*G)-3');                 
COMPND  16 CHAIN: G, I;                                                         
COMPND  17 FRAGMENT: FRAGMENT FROM CSF-1R PROMOTER;                             
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 MOL_ID: 4;                                                           
COMPND  20 MOLECULE: DNA (5'-(*CP*CP*GP*CP*AP*AP*CP*CP*AP*CP*                   
COMPND  21 AP*GP*AP*GP*TP*TP*TP*GP*GP*AP*AP*AP*TP*CP*TP*T)-3');                 
COMPND  22 CHAIN: H, J;                                                         
COMPND  23 FRAGMENT: FRAGMENT FROM CSF-1R 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: MUS MUSCULUS;                                   
SOURCE  12 ORGANISM_COMMON: MOUSE;                                              
SOURCE  13 ORGANISM_TAXID: 10090;                                               
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PAR2156;                                  
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 SYNTHETIC: YES;                                                      
SOURCE  21 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  22 ORGANISM_COMMON: HUMAN;                                              
SOURCE  23 ORGANISM_TAXID: 9606;                                                
SOURCE  24 MOL_ID: 4;                                                           
SOURCE  25 SYNTHETIC: YES;                                                      
SOURCE  26 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  27 ORGANISM_COMMON: HUMAN;                                              
SOURCE  28 ORGANISM_TAXID: 9606                                                 
KEYWDS    TRANSCRIPTION/DNA, PROTEIN-DNA COMPLEX, TRANSCRIPTION FACTOR, BZIP,   
KEYWDS   2 RUNX, RUNT, C/EBP, CBF, CORE BINDING FACTOR, AML1, AML,              
KEYWDS   3 TRANSCRIPTION-DNA COMPLEX                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.H.TAHIROV,K.OGATA                                                   
REVDAT   4   08-MAY-19 1HJB    1       REMARK                                   
REVDAT   3   24-FEB-09 1HJB    1       VERSN                                    
REVDAT   2   21-JUN-01 1HJB    1       REMARK MASTER                            
REVDAT   1   09-MAR-01 1HJB    0                                                
JRNL        AUTH   T.H.TAHIROV,T.INOUE-BUNGO,H.MORII,A.FUJIKAWA,M.SASAKI,       
JRNL        AUTH 2 K.KIMURA,M.SHIINA,K.SATO,T.KUMASAKA,M.YAMAMOTO,S.ISHII,      
JRNL        AUTH 3 K.OGATA                                                      
JRNL        TITL   STRUCTURAL ANALYSES OF DNA RECOGNITION BY THE AML1/RUNX-1    
JRNL        TITL 2 RUNT DOMAIN AND ITS ALLOSTERIC CONTROL BY CBFBETA            
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 104   755 2001              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   11257229                                                     
JRNL        DOI    10.1016/S0092-8674(01)00271-9                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   T.H.TAHIROV,T.INOUE-BUNGO,M.SASAKI,M.SHIINA,K.KIMURA,K.SATO, 
REMARK   1  AUTH 2 T.KUMASAKA,M.YAMAMOTO,N.KAMIYA,K.OGATA                       
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSES OF            
REMARK   1  TITL 2 QUATERNARY, TERNARY AND BINARY PROTEIN-DNA COMPLEXES WITH    
REMARK   1  TITL 3 INVOLVEMENT OF AML1/RUNX-1/CBFALPHA RUNT DOMAIN, CBFBETA AND 
REMARK   1  TITL 4 THE C/EBPBETA BZIP REGION                                    
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  57   850 2001              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   1  PMID   11375505                                                     
REMARK   1  DOI    10.1107/S0907444901003900                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.9                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 173187.840                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 89.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 26157                          
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) : 0.244                           
REMARK   3   FREE R VALUE                     : 0.313                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1264                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.009                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.19                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 69.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3154                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3600                       
REMARK   3   BIN FREE R VALUE                    : 0.4250                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.10                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 170                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.033                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4150                                    
REMARK   3   NUCLEIC ACID ATOMS       : 2120                                    
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 46.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 72.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 23.49000                                             
REMARK   3    B22 (A**2) : -38.31000                                            
REMARK   3    B33 (A**2) : 14.82000                                             
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) : 0.44                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.49                            
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) : 0.60                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.63                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 20.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.130                           
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) : 21.580; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 26.380; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 32.320; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 35.120; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.20                                                 
REMARK   3   BSOL        : 19.00                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : DNA-RNA_REP.PARAM                              
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA.TOP                                    
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED, BSOL IS          
REMARK   3  DETERMINED MANUALLY AND FIXED. ATOMS C, O, N, AND CA ARE            
REMARK   3  HARMONICALLY RESTRAINED DURING REFINEMENT WITH HARMONIC             
REMARK   3  RESTRAINT CONSTANT OF 20                                            
REMARK   4                                                                      
REMARK   4 1HJB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-JAN-01.                  
REMARK 100 THE DEPOSITION ID IS D_1290005785.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAR-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.60                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.7085                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26407                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.3                               
REMARK 200  DATA REDUNDANCY                : 4.456                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 71.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.91                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.30200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
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: 1IO4                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 5 MM MGSO4, 3% W/V PEG 4000, 1% V/V      
REMARK 280  DIOXANE, 50 MM MES BUFFER, PH 5.6 AT 24 DEGREES C, PH 5.60,         
REMARK 280  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       51.08250            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       54.63650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       51.08250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       54.63650            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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 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, 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: D, E, F, I, J                         
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 400  THE CORE BINDING FACTOR ALPHA SUBUNIT BINDS DNA AND APPEARS TO HAVE 
REMARK 400  A ROLE IN THE DEVELOPMENT OF NORMAL HEMATOPOIESIS.                  
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     VAL A   259                                                      
REMARK 465     LYS A   260                                                      
REMARK 465     SER A   261                                                      
REMARK 465     LYS A   262                                                      
REMARK 465     ALA A   263                                                      
REMARK 465     LYS A   264                                                      
REMARK 465     LYS A   265                                                      
REMARK 465     THR A   266                                                      
REMARK 465     VAL A   267                                                      
REMARK 465     LEU A   334                                                      
REMARK 465     PRO A   335                                                      
REMARK 465     GLU A   336                                                      
REMARK 465     PRO A   337                                                      
REMARK 465     LEU A   338                                                      
REMARK 465     LEU A   339                                                      
REMARK 465     ALA A   340                                                      
REMARK 465     SER A   341                                                      
REMARK 465     SER A   342                                                      
REMARK 465     GLY A   343                                                      
REMARK 465     HIS A   344                                                      
REMARK 465     CYS A   345                                                      
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     PRO B   337                                                      
REMARK 465     LEU B   338                                                      
REMARK 465     LEU B   339                                                      
REMARK 465     ALA B   340                                                      
REMARK 465     SER B   341                                                      
REMARK 465     SER B   342                                                      
REMARK 465     GLY B   343                                                      
REMARK 465     HIS B   344                                                      
REMARK 465     CYS B   345                                                      
REMARK 465     ARG C   180                                                      
REMARK 465     GLN C   181                                                      
REMARK 465     LYS C   182                                                      
REMARK 465     VAL D   259                                                      
REMARK 465     LYS D   260                                                      
REMARK 465     SER D   261                                                      
REMARK 465     LYS D   262                                                      
REMARK 465     ALA D   263                                                      
REMARK 465     LYS D   264                                                      
REMARK 465     LYS D   265                                                      
REMARK 465     THR D   266                                                      
REMARK 465     VAL D   267                                                      
REMARK 465     GLU D   336                                                      
REMARK 465     PRO D   337                                                      
REMARK 465     LEU D   338                                                      
REMARK 465     LEU D   339                                                      
REMARK 465     ALA D   340                                                      
REMARK 465     SER D   341                                                      
REMARK 465     SER D   342                                                      
REMARK 465     GLY D   343                                                      
REMARK 465     HIS D   344                                                      
REMARK 465     CYS D   345                                                      
REMARK 465     VAL E   259                                                      
REMARK 465     LYS E   260                                                      
REMARK 465     SER E   261                                                      
REMARK 465     LYS E   262                                                      
REMARK 465     ALA E   263                                                      
REMARK 465     LYS E   264                                                      
REMARK 465     LYS E   265                                                      
REMARK 465     THR E   266                                                      
REMARK 465     VAL E   267                                                      
REMARK 465     GLU E   336                                                      
REMARK 465     PRO E   337                                                      
REMARK 465     LEU E   338                                                      
REMARK 465     LEU E   339                                                      
REMARK 465     ALA E   340                                                      
REMARK 465     SER E   341                                                      
REMARK 465     SER E   342                                                      
REMARK 465     GLY E   343                                                      
REMARK 465     HIS E   344                                                      
REMARK 465     CYS E   345                                                      
REMARK 465     ARG F   180                                                      
REMARK 465     GLN F   181                                                      
REMARK 465     LYS F   182                                                      
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     GLN A 333    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 273    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 273    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CB   GLU F   111     CB   GLU F   111     2575     2.13            
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    PRO C  98   C   -  N   -  CA  ANGL. DEV. =   9.4 DEGREES          
REMARK 500     DC H  10   O4' -  C1' -  N1  ANGL. DEV. =   1.8 DEGREES          
REMARK 500     DC J  10   O4' -  C1' -  N1  ANGL. DEV. =   2.9 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    LYS A 269        8.07    -63.68                                   
REMARK 500    HIS A 270       46.25   -140.62                                   
REMARK 500    ASP A 272      -59.91     -2.37                                   
REMARK 500    THR A 299      -72.47    -51.46                                   
REMARK 500    VAL A 303      -72.41    -48.36                                   
REMARK 500    THR A 307      -39.10    -36.88                                   
REMARK 500    TYR B 274      -70.83    -28.25                                   
REMARK 500    GLU B 305      -62.87    -29.70                                   
REMARK 500    GLU C  61      140.91    -27.86                                   
REMARK 500    ASN C 109      145.38   -178.10                                   
REMARK 500    GLU C 111      -78.25    -51.64                                   
REMARK 500    ASN C 119       42.49     80.58                                   
REMARK 500    ALA C 129       77.34   -119.83                                   
REMARK 500    ASP C 133       66.67     34.37                                   
REMARK 500    ASN D 282      -70.85    -56.34                                   
REMARK 500    LYS D 287      -71.25    -39.00                                   
REMARK 500    SER D 321      -74.05    -53.00                                   
REMARK 500    LYS E 275      -77.10    -42.88                                   
REMARK 500    THR F  65     -165.88   -106.45                                   
REMARK 500    ASN F  82       26.22     30.43                                   
REMARK 500    SER F 114       85.36   -158.37                                   
REMARK 500    ALA F 120       13.91    -59.09                                   
REMARK 500    ASP F 133       75.88     51.64                                   
REMARK 500    ARG F 142      131.34    -36.53                                   
REMARK 500    ARG F 164       64.44     34.02                                   
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 G  18         0.05    SIDE CHAIN                              
REMARK 500     DC J   1         0.06    SIDE CHAIN                              
REMARK 500     DC J   2         0.06    SIDE CHAIN                              
REMARK 500     DA J   6         0.06    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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/CBFBETA 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      
REMARK 900 RELATED ID: 1JHB   RELATED DB: PDB                                   
REMARK 900 CORE BINDING FACTOR BETA                                             
REMARK 900 RELATED ID: 1HJC   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF RUNX-1/AML1/CBFALPHA RUNT DOMAIN BOUND TO A     
REMARK 900 DNA FRAGMENT FROM THE CSF-1R PROMOTER                                
REMARK 900 RELATED ID: 1IO4   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF RUNX-1/AML1/CBFALPHA RUNT DOMAIN-CBFBETA CORE   
REMARK 900 DOMAIN DIMERIC AND C/EBPBETA BZIP DIMERIC BOUND TO A DNA FRAGMENT    
REMARK 900 FROM THE CSF-1R PROMOTER                                             
DBREF  1HJB A  259   345  UNP    P17676   CEBB_HUMAN     259    345             
DBREF  1HJB B  259   345  UNP    P17676   CEBB_HUMAN     259    345             
DBREF  1HJB C   60   182  UNP    Q03347   AML1_MOUSE      60    182             
DBREF  1HJB D  259   345  UNP    P17676   CEBB_HUMAN     259    345             
DBREF  1HJB E  259   345  UNP    P17676   CEBB_HUMAN     259    345             
DBREF  1HJB F   60   182  UNP    Q03347   AML1_MOUSE      60    182             
DBREF  1HJB G    1    26  PDB    1HJB     1HJB             1     26             
DBREF  1HJB H    1    26  PDB    1HJB     1HJB             1     26             
DBREF  1HJB I    1    26  PDB    1HJB     1HJB             1     26             
DBREF  1HJB J    1    26  PDB    1HJB     1HJB             1     26             
SEQRES   1 A   87  VAL LYS SER LYS ALA LYS LYS THR VAL ASP LYS HIS SER          
SEQRES   2 A   87  ASP GLU TYR LYS ILE ARG ARG GLU ARG ASN ASN ILE ALA          
SEQRES   3 A   87  VAL ARG LYS SER ARG ASP LYS ALA LYS MET ARG ASN LEU          
SEQRES   4 A   87  GLU THR GLN HIS LYS VAL LEU GLU LEU THR ALA GLU ASN          
SEQRES   5 A   87  GLU ARG LEU GLN LYS LYS VAL GLU GLN LEU SER ARG GLU          
SEQRES   6 A   87  LEU SER THR LEU ARG ASN LEU PHE LYS GLN LEU PRO GLU          
SEQRES   7 A   87  PRO LEU LEU ALA SER SER GLY HIS CYS                          
SEQRES   1 B   87  VAL LYS SER LYS ALA LYS LYS THR VAL ASP LYS HIS SER          
SEQRES   2 B   87  ASP GLU TYR LYS ILE ARG ARG GLU ARG ASN ASN ILE ALA          
SEQRES   3 B   87  VAL ARG LYS SER ARG ASP LYS ALA LYS MET ARG ASN LEU          
SEQRES   4 B   87  GLU THR GLN HIS LYS VAL LEU GLU LEU THR ALA GLU ASN          
SEQRES   5 B   87  GLU ARG LEU GLN LYS LYS VAL GLU GLN LEU SER ARG GLU          
SEQRES   6 B   87  LEU SER THR LEU ARG ASN LEU PHE LYS GLN LEU PRO GLU          
SEQRES   7 B   87  PRO LEU LEU ALA SER SER GLY HIS CYS                          
SEQRES   1 C  123  GLY GLU LEU VAL ARG THR ASP SER PRO ASN PHE LEU CYS          
SEQRES   2 C  123  SER VAL LEU PRO THR HIS TRP ARG CYS ASN LYS THR LEU          
SEQRES   3 C  123  PRO ILE ALA PHE LYS VAL VAL ALA LEU GLY ASP VAL PRO          
SEQRES   4 C  123  ASP GLY THR LEU VAL THR VAL MET ALA GLY ASN ASP GLU          
SEQRES   5 C  123  ASN TYR SER ALA GLU LEU ARG ASN ALA THR ALA ALA MET          
SEQRES   6 C  123  LYS ASN GLN VAL ALA ARG PHE ASN ASP LEU ARG PHE VAL          
SEQRES   7 C  123  GLY ARG SER GLY ARG GLY LYS SER PHE THR LEU THR ILE          
SEQRES   8 C  123  THR VAL PHE THR ASN PRO PRO GLN VAL ALA THR TYR HIS          
SEQRES   9 C  123  ARG ALA ILE LYS ILE THR VAL ASP GLY PRO ARG GLU PRO          
SEQRES  10 C  123  ARG ARG HIS ARG GLN LYS                                      
SEQRES   1 D   87  VAL LYS SER LYS ALA LYS LYS THR VAL ASP LYS HIS SER          
SEQRES   2 D   87  ASP GLU TYR LYS ILE ARG ARG GLU ARG ASN ASN ILE ALA          
SEQRES   3 D   87  VAL ARG LYS SER ARG ASP LYS ALA LYS MET ARG ASN LEU          
SEQRES   4 D   87  GLU THR GLN HIS LYS VAL LEU GLU LEU THR ALA GLU ASN          
SEQRES   5 D   87  GLU ARG LEU GLN LYS LYS VAL GLU GLN LEU SER ARG GLU          
SEQRES   6 D   87  LEU SER THR LEU ARG ASN LEU PHE LYS GLN LEU PRO GLU          
SEQRES   7 D   87  PRO LEU LEU ALA SER SER GLY HIS CYS                          
SEQRES   1 E   87  VAL LYS SER LYS ALA LYS LYS THR VAL ASP LYS HIS SER          
SEQRES   2 E   87  ASP GLU TYR LYS ILE ARG ARG GLU ARG ASN ASN ILE ALA          
SEQRES   3 E   87  VAL ARG LYS SER ARG ASP LYS ALA LYS MET ARG ASN LEU          
SEQRES   4 E   87  GLU THR GLN HIS LYS VAL LEU GLU LEU THR ALA GLU ASN          
SEQRES   5 E   87  GLU ARG LEU GLN LYS LYS VAL GLU GLN LEU SER ARG GLU          
SEQRES   6 E   87  LEU SER THR LEU ARG ASN LEU PHE LYS GLN LEU PRO GLU          
SEQRES   7 E   87  PRO LEU LEU ALA SER SER GLY HIS CYS                          
SEQRES   1 F  123  GLY GLU LEU VAL ARG THR ASP SER PRO ASN PHE LEU CYS          
SEQRES   2 F  123  SER VAL LEU PRO THR HIS TRP ARG CYS ASN LYS THR LEU          
SEQRES   3 F  123  PRO ILE ALA PHE LYS VAL VAL ALA LEU GLY ASP VAL PRO          
SEQRES   4 F  123  ASP GLY THR LEU VAL THR VAL MET ALA GLY ASN ASP GLU          
SEQRES   5 F  123  ASN TYR SER ALA GLU LEU ARG ASN ALA THR ALA ALA MET          
SEQRES   6 F  123  LYS ASN GLN VAL ALA ARG PHE ASN ASP LEU ARG PHE VAL          
SEQRES   7 F  123  GLY ARG SER GLY ARG GLY LYS SER PHE THR LEU THR ILE          
SEQRES   8 F  123  THR VAL PHE THR ASN PRO PRO GLN VAL ALA THR TYR HIS          
SEQRES   9 F  123  ARG ALA ILE LYS ILE THR VAL ASP GLY PRO ARG GLU PRO          
SEQRES  10 F  123  ARG ARG HIS ARG GLN LYS                                      
SEQRES   1 G   26   DG  DA  DA  DG  DA  DT  DT  DT  DC  DC  DA  DA  DA          
SEQRES   2 G   26   DC  DT  DC  DT  DG  DT  DG  DG  DT  DT  DG  DC  DG          
SEQRES   1 H   26   DC  DC  DG  DC  DA  DA  DC  DC  DA  DC  DA  DG  DA          
SEQRES   2 H   26   DG  DT  DT  DT  DG  DG  DA  DA  DA  DT  DC  DT  DT          
SEQRES   1 I   26   DG  DA  DA  DG  DA  DT  DT  DT  DC  DC  DA  DA  DA          
SEQRES   2 I   26   DC  DT  DC  DT  DG  DT  DG  DG  DT  DT  DG  DC  DG          
SEQRES   1 J   26   DC  DC  DG  DC  DA  DA  DC  DC  DA  DC  DA  DG  DA          
SEQRES   2 J   26   DG  DT  DT  DT  DG  DG  DA  DA  DA  DT  DC  DT  DT          
HELIX    1   1 SER A  271  GLN A  333  1                                  63    
HELIX    2   2 SER B  271  LEU B  334  1                                  64    
HELIX    3   3 SER D  271  LEU D  334  1                                  64    
HELIX    4   4 SER E  271  LEU E  334  1                                  64    
SHEET    1  CA 4 LEU C  62  ARG C  64  0                                        
SHEET    2  CA 4 PHE C  70  SER C  73 -1  O  CYS C  72   N  VAL C  63           
SHEET    3  CA 4 LYS C  90  ALA C  93 -1  O  LYS C  90   N  SER C  73           
SHEET    4  CA 4 VAL C 128  ARG C 130 -1  O  ALA C 129   N  VAL C  91           
SHEET    1  CB 5 HIS C  78  ARG C  80  0                                        
SHEET    2  CB 5 GLN C 158  THR C 169  1  O  LYS C 167   N  TRP C  79           
SHEET    3  CB 5 PHE C 146  VAL C 152 -1  O  PHE C 146   N  ALA C 165           
SHEET    4  CB 5 LEU C 102  GLY C 108 -1  O  THR C 104   N  THR C 151           
SHEET    5  CB 5 THR C 121  ALA C 123 -1  O  ALA C 122   N  VAL C 103           
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           
SHEET    1  FA 4 LEU F  62  ARG F  64  0                                        
SHEET    2  FA 4 PHE F  70  SER F  73 -1  O  CYS F  72   N  VAL F  63           
SHEET    3  FA 4 PHE F  89  ALA F  93 -1  O  LYS F  90   N  SER F  73           
SHEET    4  FA 4 VAL F 128  PHE F 131 -1  O  ALA F 129   N  VAL F  91           
SHEET    1  FB 2 HIS F  78  ARG F  80  0                                        
SHEET    2  FB 2 LYS F 167  THR F 169  1  O  LYS F 167   N  TRP F  79           
SHEET    1  FC 4 THR F 121  ALA F 123  0                                        
SHEET    2  FC 4 LEU F 102  GLY F 108 -1  O  VAL F 103   N  ALA F 122           
SHEET    3  FC 4 THR F 147  VAL F 152 -1  O  THR F 147   N  GLY F 108           
SHEET    4  FC 4 GLN F 158  TYR F 162 -1  O  GLN F 158   N  VAL F 152           
SHEET    1  FD 2 LEU F 117  ARG F 118  0                                        
SHEET    2  FD 2 ARG F 135  PHE F 136 -1  O  ARG F 135   N  ARG F 118           
CISPEP   1 ASN C  155    PRO C  156          0         0.03                     
CISPEP   2 ASN F  155    PRO F  156          0        -0.12                     
CRYST1  102.165  109.273  127.405  90.00  90.00  90.00 P 21 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      0.009788  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009151  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007849        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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