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Database: PDB
Entry: 4L18
LinkDB: 4L18
Original site: 4L18 
HEADER    TRANSCRIPTION/DNA                       02-JUN-13   4L18              
TITLE     CRYSTAL STRUCTURE OF RUNX1 AND ETS1 BOUND TO TCR ALPHA PROMOTER       
TITLE    2 (CRYSTAL FORM 3)                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RUNT-RELATED TRANSCRIPTION FACTOR 1;                       
COMPND   3 CHAIN: A, E;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 48-214;                                       
COMPND   5 SYNONYM: RUNX1, ACUTE MYELOID LEUKEMIA 1 PROTEIN, CORE-BINDING FACTOR
COMPND   6 SUBUNIT ALPHA-2, CBF-ALPHA-2, ONCOGENE AML-1, POLYOMAVIRUS ENHANCER- 
COMPND   7 BINDING PROTEIN 2 ALPHA B SUBUNIT, PEA2-ALPHA B, PEBP2-ALPHA B, SL3-3
COMPND   8 ENHANCER FACTOR 1 ALPHA B SUBUNIT, SL3/AKV CORE-BINDING FACTOR ALPHA 
COMPND   9 B SUBUNIT;                                                           
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: PROTEIN C-ETS-1;                                           
COMPND  13 CHAIN: B, F;                                                         
COMPND  14 FRAGMENT: UNP RESIDUES 296-441;                                      
COMPND  15 SYNONYM: ETS1, P54;                                                  
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 3;                                                           
COMPND  18 MOLECULE: 5'-D(*GP*GP*AP*AP*GP*CP*CP*AP*CP*AP*TP*CP*CP*TP*CP*T)-3';  
COMPND  19 CHAIN: C, G;                                                         
COMPND  20 ENGINEERED: YES;                                                     
COMPND  21 OTHER_DETAILS: TCR ALPHA DNA STRAND 1;                               
COMPND  22 MOL_ID: 4;                                                           
COMPND  23 MOLECULE: 5'-D(*CP*AP*GP*AP*GP*GP*AP*TP*GP*TP*GP*GP*CP*TP*TP*C)-3';  
COMPND  24 CHAIN: D, H;                                                         
COMPND  25 ENGINEERED: YES;                                                     
COMPND  26 OTHER_DETAILS: TCR ALPHA DNA STRAND 2                                
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: RUNX1, AML1, CBFA2, PEBP2AB;                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: ETS1, EWSR2;                                                   
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 SYNTHETIC: YES;                                                      
SOURCE  17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  18 ORGANISM_COMMON: HUMAN;                                              
SOURCE  19 ORGANISM_TAXID: 9606;                                                
SOURCE  20 MOL_ID: 4;                                                           
SOURCE  21 SYNTHETIC: YES;                                                      
SOURCE  22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  23 ORGANISM_COMMON: HUMAN;                                              
SOURCE  24 ORGANISM_TAXID: 9606                                                 
KEYWDS    RUNT DOMAIN, ETS DOMAIN, TRANSCRIPTION-DNA COMPLEX                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.H.TAHIROV                                                           
REVDAT   3   22-OCT-14 4L18    1       JRNL                                     
REVDAT   2   02-APR-14 4L18    1       JRNL                                     
REVDAT   1   26-MAR-14 4L18    0                                                
JRNL        AUTH   T.SHRIVASTAVA,K.MINO,N.D.BABAYEVA,O.I.BARANOVSKAYA,          
JRNL        AUTH 2 A.RIZZINO,T.H.TAHIROV                                        
JRNL        TITL   STRUCTURAL BASIS OF ETS1 ACTIVATION BY RUNX1.                
JRNL        REF    LEUKEMIA                      V.  28  2040 2014              
JRNL        REFN                   ISSN 0887-6924                               
JRNL        PMID   24646888                                                     
JRNL        DOI    10.1038/LEU.2014.111                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.64                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1680438.940                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 87.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 33721                          
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) : 0.231                           
REMARK   3   FREE R VALUE                     : 0.280                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1665                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.44                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 50.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3167                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4870                       
REMARK   3   BIN FREE R VALUE                    : 0.4450                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.60                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 154                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.036                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3982                                    
REMARK   3   NUCLEIC ACID ATOMS       : 1300                                    
REMARK   3   HETEROGEN ATOMS          : 6                                       
REMARK   3   SOLVENT ATOMS            : 143                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 49.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 52.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.22000                                             
REMARK   3    B22 (A**2) : 1.00000                                              
REMARK   3    B33 (A**2) : 0.22000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.92000                                              
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) : 0.60                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 20.00                           
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.51                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.67                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.400                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.900                          
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.070                           
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) : 3.490 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 5.320 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 5.180 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 6.840 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 42.73                                                
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  : GOL.PAR                                        
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA.TOP                                    
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : GOL.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4L18 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUN-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB080052.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9                                
REMARK 200  MONOCHROMATOR                  : CRYOGENICALLY-COOLED SINGLE        
REMARK 200                                   CRYSTAL SI(220) SIDE BOUNCE        
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35376                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -2.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.4                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.05600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.34                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 60.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.5% W/V PEG4000, 5 MM MAGNESIUM         
REMARK 280  CHLORIDE HEXAHYDRATE, 25 MM MES, PH 5.6, 5% V/V GLYCEROL, VAPOR     
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       50.01600            
REMARK 290   SMTRY3   2  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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6020 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17370 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, C                            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5680 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17070 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, H, G                            
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     ASP A    48                                                      
REMARK 465     ARG A    49                                                      
REMARK 465     SER A    50                                                      
REMARK 465     MET A    51                                                      
REMARK 465     VAL A    52                                                      
REMARK 465     ARG A   178                                                      
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     ASP A   184                                                      
REMARK 465     ASP A   185                                                      
REMARK 465     GLN A   186                                                      
REMARK 465     THR A   187                                                      
REMARK 465     LYS A   188                                                      
REMARK 465     ARG A   206                                                      
REMARK 465     THR A   207                                                      
REMARK 465     ALA A   208                                                      
REMARK 465     MET A   209                                                      
REMARK 465     ARG A   210                                                      
REMARK 465     VAL A   211                                                      
REMARK 465     SER A   212                                                      
REMARK 465     PRO A   213                                                      
REMARK 465     HIS A   214                                                      
REMARK 465     PRO B   296                                                      
REMARK 465     ASN B   297                                                      
REMARK 465     HIS B   298                                                      
REMARK 465     LYS B   299                                                      
REMARK 465     PRO B   300                                                      
REMARK 465     LYS B   301                                                      
REMARK 465     GLY B   302                                                      
REMARK 465     THR B   303                                                      
REMARK 465     PHE B   304                                                      
REMARK 465     LYS B   305                                                      
REMARK 465     ASP B   306                                                      
REMARK 465     TYR B   307                                                      
REMARK 465     VAL B   308                                                      
REMARK 465     ARG B   309                                                      
REMARK 465     ASP B   310                                                      
REMARK 465     ARG B   311                                                      
REMARK 465     ALA B   312                                                      
REMARK 465     ASP B   313                                                      
REMARK 465     LEU B   314                                                      
REMARK 465     ASN B   315                                                      
REMARK 465     LYS B   316                                                      
REMARK 465     ASP B   317                                                      
REMARK 465     LYS B   318                                                      
REMARK 465     PRO B   319                                                      
REMARK 465     VAL B   320                                                      
REMARK 465     ILE B   321                                                      
REMARK 465     PRO B   322                                                      
REMARK 465     ALA B   323                                                      
REMARK 465     ALA B   324                                                      
REMARK 465     ALA B   325                                                      
REMARK 465     LEU B   326                                                      
REMARK 465     ALA B   327                                                      
REMARK 465     GLY B   328                                                      
REMARK 465     TYR B   329                                                      
REMARK 465     THR B   330                                                      
REMARK 465     GLY B   331                                                      
REMARK 465     SER B   332                                                      
REMARK 465     ASP B   440                                                      
REMARK 465     GLU B   441                                                      
REMARK 465     ASP E    48                                                      
REMARK 465     ARG E    49                                                      
REMARK 465     SER E    50                                                      
REMARK 465     MET E    51                                                      
REMARK 465     ARG E   178                                                      
REMARK 465     HIS E   179                                                      
REMARK 465     ARG E   180                                                      
REMARK 465     GLN E   181                                                      
REMARK 465     LYS E   182                                                      
REMARK 465     LEU E   183                                                      
REMARK 465     ASP E   184                                                      
REMARK 465     ASP E   185                                                      
REMARK 465     GLN E   186                                                      
REMARK 465     THR E   187                                                      
REMARK 465     LYS E   188                                                      
REMARK 465     PRO E   189                                                      
REMARK 465     ARG E   205                                                      
REMARK 465     ARG E   206                                                      
REMARK 465     THR E   207                                                      
REMARK 465     ALA E   208                                                      
REMARK 465     MET E   209                                                      
REMARK 465     ARG E   210                                                      
REMARK 465     VAL E   211                                                      
REMARK 465     SER E   212                                                      
REMARK 465     PRO E   213                                                      
REMARK 465     HIS E   214                                                      
REMARK 465     PRO F   296                                                      
REMARK 465     ASN F   297                                                      
REMARK 465     HIS F   298                                                      
REMARK 465     LYS F   299                                                      
REMARK 465     PRO F   300                                                      
REMARK 465     LYS F   301                                                      
REMARK 465     GLY F   302                                                      
REMARK 465     THR F   303                                                      
REMARK 465     PHE F   304                                                      
REMARK 465     LYS F   305                                                      
REMARK 465     ASP F   306                                                      
REMARK 465     TYR F   307                                                      
REMARK 465     VAL F   308                                                      
REMARK 465     ARG F   309                                                      
REMARK 465     ASP F   310                                                      
REMARK 465     ARG F   311                                                      
REMARK 465     ALA F   312                                                      
REMARK 465     ASP F   313                                                      
REMARK 465     LEU F   314                                                      
REMARK 465     ASN F   315                                                      
REMARK 465     LYS F   316                                                      
REMARK 465     ASP F   317                                                      
REMARK 465     LYS F   318                                                      
REMARK 465     PRO F   319                                                      
REMARK 465     VAL F   320                                                      
REMARK 465     ILE F   321                                                      
REMARK 465     PRO F   322                                                      
REMARK 465     ALA F   323                                                      
REMARK 465     ALA F   324                                                      
REMARK 465     ALA F   325                                                      
REMARK 465     LEU F   326                                                      
REMARK 465     ALA F   327                                                      
REMARK 465     GLY F   328                                                      
REMARK 465     TYR F   329                                                      
REMARK 465     THR F   330                                                      
REMARK 465     GLY F   331                                                      
REMARK 465     ASP F   438                                                      
REMARK 465     ALA F   439                                                      
REMARK 465     ASP F   440                                                      
REMARK 465     GLU F   441                                                      
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     DA C   8   O4' -  C1' -  N9  ANGL. DEV. =   2.2 DEGREES          
REMARK 500     DG D 103   O4' -  C1' -  N9  ANGL. DEV. =   2.2 DEGREES          
REMARK 500    LEU E  55   N   -  CA  -  C   ANGL. DEV. = -18.6 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    ASN A 109     -165.51   -173.86                                   
REMARK 500    ALA A 120       23.50    -79.78                                   
REMARK 500    GLN A 127       -0.31     68.20                                   
REMARK 500    PHE A 153       55.09    -68.51                                   
REMARK 500    LEU A 204      -80.62     -3.53                                   
REMARK 500    GLN B 351       -8.57    -54.11                                   
REMARK 500    ASN B 380       62.87     61.22                                   
REMARK 500    ASN E 109     -162.16   -173.49                                   
REMARK 500    PHE E 153       56.08    -67.58                                   
REMARK 500    ARG E 164       55.75     38.40                                   
REMARK 500    GLN F 351       -6.15    -57.54                                   
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 C   5         0.08    SIDE CHAIN                              
REMARK 500     DC C  13         0.06    SIDE CHAIN                              
REMARK 500     DG D 103         0.06    SIDE CHAIN                              
REMARK 500     DG G 205         0.06    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 516        DISTANCE =  5.37 ANGSTROMS                       
REMARK 525    HOH F 513        DISTANCE =  5.58 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 201                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4L0Y   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4L0Z   RELATED DB: PDB                                   
DBREF  4L18 A   48   214  UNP    Q03347   RUNX1_MOUSE     48    214             
DBREF  4L18 B  296   441  UNP    P14921   ETS1_HUMAN     296    441             
DBREF  4L18 E   48   214  UNP    Q03347   RUNX1_MOUSE     48    214             
DBREF  4L18 F  296   441  UNP    P14921   ETS1_HUMAN     296    441             
DBREF  4L18 C    1    16  PDB    4L18     4L18             1     16             
DBREF  4L18 G  201   216  PDB    4L18     4L18           201    216             
DBREF  4L18 D  101   116  PDB    4L18     4L18           101    116             
DBREF  4L18 H  301   316  PDB    4L18     4L18           301    316             
SEQRES   1 A  167  ASP ARG SER MET VAL GLU VAL LEU ALA ASP HIS PRO GLY          
SEQRES   2 A  167  GLU LEU VAL ARG THR ASP SER PRO ASN PHE LEU CYS SER          
SEQRES   3 A  167  VAL LEU PRO THR HIS TRP ARG CYS ASN LYS THR LEU PRO          
SEQRES   4 A  167  ILE ALA PHE LYS VAL VAL ALA LEU GLY ASP VAL PRO ASP          
SEQRES   5 A  167  GLY THR LEU VAL THR VAL MET ALA GLY ASN ASP GLU ASN          
SEQRES   6 A  167  TYR SER ALA GLU LEU ARG ASN ALA THR ALA ALA MET LYS          
SEQRES   7 A  167  ASN GLN VAL ALA ARG PHE ASN ASP LEU ARG PHE VAL GLY          
SEQRES   8 A  167  ARG SER GLY ARG GLY LYS SER PHE THR LEU THR ILE THR          
SEQRES   9 A  167  VAL PHE THR ASN PRO PRO GLN VAL ALA THR TYR HIS ARG          
SEQRES  10 A  167  ALA ILE LYS ILE THR VAL ASP GLY PRO ARG GLU PRO ARG          
SEQRES  11 A  167  ARG HIS ARG GLN LYS LEU ASP ASP GLN THR LYS PRO GLY          
SEQRES  12 A  167  SER LEU SER PHE SER GLU ARG LEU SER GLU LEU GLU GLN          
SEQRES  13 A  167  LEU ARG ARG THR ALA MET ARG VAL SER PRO HIS                  
SEQRES   1 B  146  PRO ASN HIS LYS PRO LYS GLY THR PHE LYS ASP TYR VAL          
SEQRES   2 B  146  ARG ASP ARG ALA ASP LEU ASN LYS ASP LYS PRO VAL ILE          
SEQRES   3 B  146  PRO ALA ALA ALA LEU ALA GLY TYR THR GLY SER GLY PRO          
SEQRES   4 B  146  ILE GLN LEU TRP GLN PHE LEU LEU GLU LEU LEU THR ASP          
SEQRES   5 B  146  LYS SER CYS GLN SER PHE ILE SER TRP THR GLY ASP GLY          
SEQRES   6 B  146  TRP GLU PHE LYS LEU SER ASP PRO ASP GLU VAL ALA ARG          
SEQRES   7 B  146  ARG TRP GLY LYS ARG LYS ASN LYS PRO LYS MET ASN TYR          
SEQRES   8 B  146  GLU LYS LEU SER ARG GLY LEU ARG TYR TYR TYR ASP LYS          
SEQRES   9 B  146  ASN ILE ILE HIS LYS THR ALA GLY LYS ARG TYR VAL TYR          
SEQRES  10 B  146  ARG PHE VAL CYS ASP LEU GLN SER LEU LEU GLY TYR THR          
SEQRES  11 B  146  PRO GLU GLU LEU HIS ALA MET LEU ASP VAL LYS PRO ASP          
SEQRES  12 B  146  ALA ASP GLU                                                  
SEQRES   1 C   16   DG  DG  DA  DA  DG  DC  DC  DA  DC  DA  DT  DC  DC          
SEQRES   2 C   16   DT  DC  DT                                                  
SEQRES   1 D   16   DC  DA  DG  DA  DG  DG  DA  DT  DG  DT  DG  DG  DC          
SEQRES   2 D   16   DT  DT  DC                                                  
SEQRES   1 E  167  ASP ARG SER MET VAL GLU VAL LEU ALA ASP HIS PRO GLY          
SEQRES   2 E  167  GLU LEU VAL ARG THR ASP SER PRO ASN PHE LEU CYS SER          
SEQRES   3 E  167  VAL LEU PRO THR HIS TRP ARG CYS ASN LYS THR LEU PRO          
SEQRES   4 E  167  ILE ALA PHE LYS VAL VAL ALA LEU GLY ASP VAL PRO ASP          
SEQRES   5 E  167  GLY THR LEU VAL THR VAL MET ALA GLY ASN ASP GLU ASN          
SEQRES   6 E  167  TYR SER ALA GLU LEU ARG ASN ALA THR ALA ALA MET LYS          
SEQRES   7 E  167  ASN GLN VAL ALA ARG PHE ASN ASP LEU ARG PHE VAL GLY          
SEQRES   8 E  167  ARG SER GLY ARG GLY LYS SER PHE THR LEU THR ILE THR          
SEQRES   9 E  167  VAL PHE THR ASN PRO PRO GLN VAL ALA THR TYR HIS ARG          
SEQRES  10 E  167  ALA ILE LYS ILE THR VAL ASP GLY PRO ARG GLU PRO ARG          
SEQRES  11 E  167  ARG HIS ARG GLN LYS LEU ASP ASP GLN THR LYS PRO GLY          
SEQRES  12 E  167  SER LEU SER PHE SER GLU ARG LEU SER GLU LEU GLU GLN          
SEQRES  13 E  167  LEU ARG ARG THR ALA MET ARG VAL SER PRO HIS                  
SEQRES   1 F  146  PRO ASN HIS LYS PRO LYS GLY THR PHE LYS ASP TYR VAL          
SEQRES   2 F  146  ARG ASP ARG ALA ASP LEU ASN LYS ASP LYS PRO VAL ILE          
SEQRES   3 F  146  PRO ALA ALA ALA LEU ALA GLY TYR THR GLY SER GLY PRO          
SEQRES   4 F  146  ILE GLN LEU TRP GLN PHE LEU LEU GLU LEU LEU THR ASP          
SEQRES   5 F  146  LYS SER CYS GLN SER PHE ILE SER TRP THR GLY ASP GLY          
SEQRES   6 F  146  TRP GLU PHE LYS LEU SER ASP PRO ASP GLU VAL ALA ARG          
SEQRES   7 F  146  ARG TRP GLY LYS ARG LYS ASN LYS PRO LYS MET ASN TYR          
SEQRES   8 F  146  GLU LYS LEU SER ARG GLY LEU ARG TYR TYR TYR ASP LYS          
SEQRES   9 F  146  ASN ILE ILE HIS LYS THR ALA GLY LYS ARG TYR VAL TYR          
SEQRES  10 F  146  ARG PHE VAL CYS ASP LEU GLN SER LEU LEU GLY TYR THR          
SEQRES  11 F  146  PRO GLU GLU LEU HIS ALA MET LEU ASP VAL LYS PRO ASP          
SEQRES  12 F  146  ALA ASP GLU                                                  
SEQRES   1 G   16   DG  DG  DA  DA  DG  DC  DC  DA  DC  DA  DT  DC  DC          
SEQRES   2 G   16   DT  DC  DT                                                  
SEQRES   1 H   16   DC  DA  DG  DA  DG  DG  DA  DT  DG  DT  DG  DG  DC          
SEQRES   2 H   16   DT  DT  DC                                                  
HET    GOL  D 201       6                                                       
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   9  GOL    C3 H8 O3                                                     
FORMUL  10  HOH   *143(H2 O)                                                    
HELIX    1   1 SER A  193  LEU A  204  1                                  12    
HELIX    2   2 GLN B  336  LEU B  345  1                                  10    
HELIX    3   3 THR B  346  GLN B  351  5                                   6    
HELIX    4   4 ASP B  367  ASN B  380  1                                  14    
HELIX    5   5 ASN B  385  LYS B  399  1                                  15    
HELIX    6   6 ASP B  417  GLY B  423  1                                   7    
HELIX    7   7 THR B  425  LEU B  433  1                                   9    
HELIX    8   8 SER E  193  GLU E  202  1                                  10    
HELIX    9   9 GLN F  336  THR F  346  1                                  11    
HELIX   10  10 ASP F  347  GLN F  351  5                                   5    
HELIX   11  11 ASP F  367  ASN F  380  1                                  14    
HELIX   12  12 ASN F  385  LYS F  399  1                                  15    
HELIX   13  13 ASP F  417  GLY F  423  1                                   7    
HELIX   14  14 THR F  425  LEU F  433  1                                   9    
SHEET    1   A 9 LEU A  62  ARG A  64  0                                        
SHEET    2   A 9 PHE A  70  SER A  73 -1  O  CYS A  72   N  VAL A  63           
SHEET    3   A 9 LYS A  90  ALA A  93 -1  O  VAL A  92   N  LEU A  71           
SHEET    4   A 9 VAL A 128  ARG A 130 -1  O  ALA A 129   N  VAL A  91           
SHEET    5   A 9 THR A 121  LYS A 125 -1  N  LYS A 125   O  VAL A 128           
SHEET    6   A 9 LEU A 102  GLY A 108 -1  N  VAL A 103   O  ALA A 122           
SHEET    7   A 9 PHE A 146  VAL A 152 -1  O  THR A 147   N  GLY A 108           
SHEET    8   A 9 GLN A 158  THR A 169 -1  O  ALA A 160   N  ILE A 150           
SHEET    9   A 9 HIS A  78  ARG A  80  1  N  TRP A  79   O  LYS A 167           
SHEET    1   B 2 LEU A 117  ARG A 118  0                                        
SHEET    2   B 2 ARG A 135  PHE A 136 -1  O  ARG A 135   N  ARG A 118           
SHEET    1   C 4 SER B 355  TRP B 356  0                                        
SHEET    2   C 4 GLU B 362  LYS B 364 -1  O  LYS B 364   N  SER B 355           
SHEET    3   C 4 VAL B 411  PHE B 414 -1  O  TYR B 412   N  PHE B 363           
SHEET    4   C 4 ILE B 402  LYS B 404 -1  N  HIS B 403   O  ARG B 413           
SHEET    1   D 9 LEU E  62  ARG E  64  0                                        
SHEET    2   D 9 PHE E  70  SER E  73 -1  O  CYS E  72   N  VAL E  63           
SHEET    3   D 9 LYS E  90  ALA E  93 -1  O  VAL E  92   N  LEU E  71           
SHEET    4   D 9 VAL E 128  ARG E 130 -1  O  ALA E 129   N  VAL E  91           
SHEET    5   D 9 THR E 121  LYS E 125 -1  N  LYS E 125   O  VAL E 128           
SHEET    6   D 9 LEU E 102  GLY E 108 -1  N  VAL E 103   O  ALA E 122           
SHEET    7   D 9 PHE E 146  VAL E 152 -1  O  THR E 147   N  GLY E 108           
SHEET    8   D 9 GLN E 158  THR E 169 -1  O  ALA E 160   N  ILE E 150           
SHEET    9   D 9 HIS E  78  ARG E  80  1  N  TRP E  79   O  LYS E 167           
SHEET    1   E 2 LEU E 117  ARG E 118  0                                        
SHEET    2   E 2 ARG E 135  PHE E 136 -1  O  ARG E 135   N  ARG E 118           
SHEET    1   F 4 SER F 355  TRP F 356  0                                        
SHEET    2   F 4 GLU F 362  LYS F 364 -1  O  LYS F 364   N  SER F 355           
SHEET    3   F 4 VAL F 411  PHE F 414 -1  O  TYR F 412   N  PHE F 363           
SHEET    4   F 4 ILE F 402  LYS F 404 -1  N  HIS F 403   O  ARG F 413           
CISPEP   1 ASN A  155    PRO A  156          0         0.04                     
CISPEP   2 ASN E  155    PRO E  156          0         0.10                     
SITE     1 AC1  3  DT C  14   DG D 103   DA D 104                               
CRYST1   66.153  100.032   72.064  90.00 110.23  90.00 P 1 21 1      4          
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      0.015116  0.000000  0.005570        0.00000                         
SCALE2      0.000000  0.009997  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014789        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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