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Database: PDB
Entry: 3WTT
LinkDB: 3WTT
Original site: 3WTT 
HEADER    TRANSCRIPTION/DNA                       21-APR-14   3WTT              
TITLE     CRYSTAL STRUCTURE OF THE COMPLEX COMPRISED OF PHOSPHORYLATED ETS1,    
TITLE    2 RUNX1, CBFBETA, AND THE TCRALPHA GENE ENHANCER DNA                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RUNT-RELATED TRANSCRIPTION FACTOR 1;                       
COMPND   3 CHAIN: A, F;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 60-263;                                       
COMPND   5 SYNONYM: 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 MUTATION: YES;                                                       
COMPND  12 MOL_ID: 2;                                                           
COMPND  13 MOLECULE: CORE-BINDING FACTOR SUBUNIT BETA;                          
COMPND  14 CHAIN: B, G;                                                         
COMPND  15 FRAGMENT: UNP RESIDUES 1-142;                                        
COMPND  16 SYNONYM: CBF-BETA, POLYOMAVIRUS ENHANCER-BINDING PROTEIN 2 BETA      
COMPND  17 SUBUNIT, PEA2-BETA, PEBP2-BETA, SL3-3 ENHANCER FACTOR 1 SUBUNIT BETA,
COMPND  18 SL3/AKV CORE-BINDING FACTOR BETA SUBUNIT;                            
COMPND  19 ENGINEERED: YES;                                                     
COMPND  20 MOL_ID: 3;                                                           
COMPND  21 MOLECULE: PROTEIN C-ETS-1;                                           
COMPND  22 CHAIN: C, H;                                                         
COMPND  23 FRAGMENT: UNP RESIDUES 276-441;                                      
COMPND  24 SYNONYM: P54;                                                        
COMPND  25 ENGINEERED: YES;                                                     
COMPND  26 MOL_ID: 4;                                                           
COMPND  27 MOLECULE: 5'-D(*GP*AP*AP*GP*CP*CP*AP*CP*AP*TP*CP*CP*TP*CP*T)-3';     
COMPND  28 CHAIN: D, I;                                                         
COMPND  29 ENGINEERED: YES;                                                     
COMPND  30 MOL_ID: 5;                                                           
COMPND  31 MOLECULE: 5'-D(*AP*GP*AP*GP*GP*AP*TP*GP*TP*GP*GP*CP*TP*TP*C)-3';     
COMPND  32 CHAIN: E, J;                                                         
COMPND  33 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: AML1, CBFA2, PEBP2AB, RUNX1;                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET23A;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  13 ORGANISM_COMMON: MOUSE;                                              
SOURCE  14 ORGANISM_TAXID: 10090;                                               
SOURCE  15 GENE: CBFB, PEBP2B, PEBPB2;                                          
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET23A;                                   
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  23 ORGANISM_COMMON: HUMAN;                                              
SOURCE  24 ORGANISM_TAXID: 9606;                                                
SOURCE  25 GENE: ETS1, EWSR2;                                                   
SOURCE  26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  27 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  28 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  30 EXPRESSION_SYSTEM_PLASMID: PET23A;                                   
SOURCE  31 MOL_ID: 4;                                                           
SOURCE  32 SYNTHETIC: YES;                                                      
SOURCE  33 MOL_ID: 5;                                                           
SOURCE  34 SYNTHETIC: YES                                                       
KEYWDS    PROTEIN-DNA COMPLEX, TRANSCRIPTION-DNA COMPLEX                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.SHIINA,K.HAMADA,K.OGATA                                             
REVDAT   2   22-NOV-17 3WTT    1       REMARK                                   
REVDAT   1   13-AUG-14 3WTT    0                                                
JRNL        AUTH   M.SHIINA,K.HAMADA,T.INOUE-BUNGO,M.SHIMAMURA,A.UCHIYAMA,      
JRNL        AUTH 2 S.BABA,K.SATO,M.YAMAMOTO,K.OGATA                             
JRNL        TITL   A NOVEL ALLOSTERIC MECHANISM ON PROTEIN-DNA INTERACTIONS     
JRNL        TITL 2 UNDERLYING THE PHOSPHORYLATION-DEPENDENT REGULATION OF ETS1  
JRNL        TITL 3 TARGET GENE EXPRESSIONS                                      
JRNL        REF    J.MOL.BIOL.                                2014              
JRNL        REFN                   ESSN 1089-8638                               
JRNL        PMID   25083921                                                     
JRNL        DOI    10.1016/J.JMB.2014.07.020                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.2                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.68                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2354630.000                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 64625                          
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) : 0.241                           
REMARK   3   FREE R VALUE                     : 0.277                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 6531                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
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) : 2.35                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.50                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 9042                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4350                       
REMARK   3   BIN FREE R VALUE                    : 0.4580                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.50                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 1058                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.014                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5738                                    
REMARK   3   NUCLEIC ACID ATOMS       : 1218                                    
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 127                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 71.49                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.69000                                              
REMARK   3    B22 (A**2) : 4.13000                                              
REMARK   3    B33 (A**2) : -6.82000                                             
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) : 0.53                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.50                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.59                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.012                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.500                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.80                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.250                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.420 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.460 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.070 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.180 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 53.18                                                
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  : ION.PARAM                                      
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   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 3WTT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-MAY-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000096783.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-MAY-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
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) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
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, DENZO                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 64857                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : 0.06100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.43                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3WTS                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.03                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 4000, 0.25M AMMONIUM ACETATE,    
REMARK 280  0.05M SODIUM ACETATE, PH 5.5, VAPOR DIFFUSION, SITTING DROP,        
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       39.30900            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       97.36050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       50.85900            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       97.36050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.30900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       50.85900            
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: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7130 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6810 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20840 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, G, H, 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 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     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     PRO A   189                                                      
REMARK 465     GLY A   190                                                      
REMARK 465     SER A   191                                                      
REMARK 465     LEU A   192                                                      
REMARK 465     SER A   193                                                      
REMARK 465     PHE A   194                                                      
REMARK 465     SER A   195                                                      
REMARK 465     GLU A   196                                                      
REMARK 465     ARG A   197                                                      
REMARK 465     LEU A   198                                                      
REMARK 465     SER A   199                                                      
REMARK 465     GLU A   200                                                      
REMARK 465     LEU A   201                                                      
REMARK 465     GLU A   202                                                      
REMARK 465     GLN A   203                                                      
REMARK 465     LEU A   204                                                      
REMARK 465     ARG A   205                                                      
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     HIS A   215                                                      
REMARK 465     PRO A   216                                                      
REMARK 465     ALA A   217                                                      
REMARK 465     PRO A   218                                                      
REMARK 465     THR A   219                                                      
REMARK 465     PRO A   220                                                      
REMARK 465     ASN A   221                                                      
REMARK 465     PRO A   222                                                      
REMARK 465     ARG A   223                                                      
REMARK 465     ALA A   224                                                      
REMARK 465     SER A   225                                                      
REMARK 465     LEU A   226                                                      
REMARK 465     ASN A   227                                                      
REMARK 465     HIS A   228                                                      
REMARK 465     SER A   229                                                      
REMARK 465     THR A   230                                                      
REMARK 465     ALA A   231                                                      
REMARK 465     PHE A   232                                                      
REMARK 465     ASN A   233                                                      
REMARK 465     PRO A   234                                                      
REMARK 465     GLN A   235                                                      
REMARK 465     PRO A   236                                                      
REMARK 465     GLN A   237                                                      
REMARK 465     SER A   238                                                      
REMARK 465     GLN A   239                                                      
REMARK 465     MET A   240                                                      
REMARK 465     GLN A   241                                                      
REMARK 465     ASP A   242                                                      
REMARK 465     ALA A   243                                                      
REMARK 465     ARG A   244                                                      
REMARK 465     GLN A   245                                                      
REMARK 465     ILE A   246                                                      
REMARK 465     GLN A   247                                                      
REMARK 465     PRO A   248                                                      
REMARK 465     SER A   249                                                      
REMARK 465     PRO A   250                                                      
REMARK 465     PRO A   251                                                      
REMARK 465     TRP A   252                                                      
REMARK 465     SER A   253                                                      
REMARK 465     TYR A   254                                                      
REMARK 465     ASP A   255                                                      
REMARK 465     GLN A   256                                                      
REMARK 465     SER A   257                                                      
REMARK 465     TYR A   258                                                      
REMARK 465     GLN A   259                                                      
REMARK 465     TYR A   260                                                      
REMARK 465     LEU A   261                                                      
REMARK 465     GLY A   262                                                      
REMARK 465     SER A   263                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B    72                                                      
REMARK 465     TRP B    73                                                      
REMARK 465     GLN B    74                                                      
REMARK 465     GLY B    75                                                      
REMARK 465     GLU B    76                                                      
REMARK 465     GLN B    77                                                      
REMARK 465     ARG B    78                                                      
REMARK 465     GLN B    79                                                      
REMARK 465     GLN B   141                                                      
REMARK 465     ALA B   142                                                      
REMARK 465     SER C   276                                                      
REMARK 465     LEU C   277                                                      
REMARK 465     GLN C   278                                                      
REMARK 465     ARG C   279                                                      
REMARK 465     VAL C   280                                                      
REMARK 465     PRO C   281                                                      
REMARK 465     SER C   282                                                      
REMARK 465     TYR C   283                                                      
REMARK 465     ASP C   284                                                      
REMARK 465     SER C   285                                                      
REMARK 465     PHE C   286                                                      
REMARK 465     ASP C   287                                                      
REMARK 465     SER C   288                                                      
REMARK 465     GLU C   289                                                      
REMARK 465     ASP C   290                                                      
REMARK 465     TYR C   291                                                      
REMARK 465     PRO C   292                                                      
REMARK 465     ALA C   293                                                      
REMARK 465     ALA C   294                                                      
REMARK 465     LEU C   295                                                      
REMARK 465     PRO C   296                                                      
REMARK 465     ASN C   297                                                      
REMARK 465     HIS C   298                                                      
REMARK 465     LYS C   299                                                      
REMARK 465     PRO C   300                                                      
REMARK 465     LYS C   301                                                      
REMARK 465     GLY C   302                                                      
REMARK 465     THR C   303                                                      
REMARK 465     PHE C   304                                                      
REMARK 465     LYS C   305                                                      
REMARK 465     ASP C   306                                                      
REMARK 465     TYR C   307                                                      
REMARK 465     VAL C   308                                                      
REMARK 465     ARG C   309                                                      
REMARK 465     ASP C   310                                                      
REMARK 465     ARG C   311                                                      
REMARK 465     ALA C   312                                                      
REMARK 465     ASP C   313                                                      
REMARK 465     LEU C   314                                                      
REMARK 465     ASN C   315                                                      
REMARK 465     LYS C   316                                                      
REMARK 465     ASP C   317                                                      
REMARK 465     LYS C   318                                                      
REMARK 465     PRO C   437                                                      
REMARK 465     ASP C   438                                                      
REMARK 465     ALA C   439                                                      
REMARK 465     ASP C   440                                                      
REMARK 465     GLU C   441                                                      
REMARK 465     ARG F   178                                                      
REMARK 465     HIS F   179                                                      
REMARK 465     ARG F   180                                                      
REMARK 465     GLN F   181                                                      
REMARK 465     LYS F   182                                                      
REMARK 465     LEU F   183                                                      
REMARK 465     ASP F   184                                                      
REMARK 465     ASP F   185                                                      
REMARK 465     GLN F   186                                                      
REMARK 465     THR F   187                                                      
REMARK 465     LYS F   188                                                      
REMARK 465     PRO F   189                                                      
REMARK 465     GLY F   190                                                      
REMARK 465     SER F   191                                                      
REMARK 465     LEU F   192                                                      
REMARK 465     SER F   193                                                      
REMARK 465     PHE F   194                                                      
REMARK 465     SER F   195                                                      
REMARK 465     GLU F   196                                                      
REMARK 465     ARG F   197                                                      
REMARK 465     LEU F   198                                                      
REMARK 465     SER F   199                                                      
REMARK 465     GLU F   200                                                      
REMARK 465     LEU F   201                                                      
REMARK 465     GLU F   202                                                      
REMARK 465     GLN F   203                                                      
REMARK 465     LEU F   204                                                      
REMARK 465     ARG F   205                                                      
REMARK 465     ARG F   206                                                      
REMARK 465     THR F   207                                                      
REMARK 465     ALA F   208                                                      
REMARK 465     MET F   209                                                      
REMARK 465     ARG F   210                                                      
REMARK 465     VAL F   211                                                      
REMARK 465     SER F   212                                                      
REMARK 465     PRO F   213                                                      
REMARK 465     HIS F   214                                                      
REMARK 465     HIS F   215                                                      
REMARK 465     PRO F   216                                                      
REMARK 465     ALA F   217                                                      
REMARK 465     PRO F   218                                                      
REMARK 465     THR F   219                                                      
REMARK 465     PRO F   220                                                      
REMARK 465     ASN F   221                                                      
REMARK 465     PRO F   222                                                      
REMARK 465     ARG F   223                                                      
REMARK 465     ALA F   224                                                      
REMARK 465     SER F   225                                                      
REMARK 465     LEU F   226                                                      
REMARK 465     ASN F   227                                                      
REMARK 465     HIS F   228                                                      
REMARK 465     SER F   229                                                      
REMARK 465     THR F   230                                                      
REMARK 465     ALA F   231                                                      
REMARK 465     PHE F   232                                                      
REMARK 465     ASN F   233                                                      
REMARK 465     PRO F   234                                                      
REMARK 465     GLN F   235                                                      
REMARK 465     PRO F   236                                                      
REMARK 465     GLN F   237                                                      
REMARK 465     SER F   238                                                      
REMARK 465     GLN F   239                                                      
REMARK 465     MET F   240                                                      
REMARK 465     GLN F   241                                                      
REMARK 465     ASP F   242                                                      
REMARK 465     ALA F   243                                                      
REMARK 465     ARG F   244                                                      
REMARK 465     GLN F   245                                                      
REMARK 465     ILE F   246                                                      
REMARK 465     GLN F   247                                                      
REMARK 465     PRO F   248                                                      
REMARK 465     SER F   249                                                      
REMARK 465     PRO F   250                                                      
REMARK 465     PRO F   251                                                      
REMARK 465     TRP F   252                                                      
REMARK 465     SER F   253                                                      
REMARK 465     TYR F   254                                                      
REMARK 465     ASP F   255                                                      
REMARK 465     GLN F   256                                                      
REMARK 465     SER F   257                                                      
REMARK 465     TYR F   258                                                      
REMARK 465     GLN F   259                                                      
REMARK 465     TYR F   260                                                      
REMARK 465     LEU F   261                                                      
REMARK 465     GLY F   262                                                      
REMARK 465     SER F   263                                                      
REMARK 465     MET G     1                                                      
REMARK 465     SER G    72                                                      
REMARK 465     TRP G    73                                                      
REMARK 465     GLN G    74                                                      
REMARK 465     GLY G    75                                                      
REMARK 465     GLU G    76                                                      
REMARK 465     GLN G    77                                                      
REMARK 465     ARG G    78                                                      
REMARK 465     GLN G    79                                                      
REMARK 465     THR G    80                                                      
REMARK 465     GLN G   141                                                      
REMARK 465     ALA G   142                                                      
REMARK 465     SER H   276                                                      
REMARK 465     LEU H   277                                                      
REMARK 465     GLN H   278                                                      
REMARK 465     ARG H   279                                                      
REMARK 465     VAL H   280                                                      
REMARK 465     PRO H   281                                                      
REMARK 465     SER H   282                                                      
REMARK 465     TYR H   283                                                      
REMARK 465     ASP H   284                                                      
REMARK 465     SER H   285                                                      
REMARK 465     PHE H   286                                                      
REMARK 465     ASP H   287                                                      
REMARK 465     SER H   288                                                      
REMARK 465     GLU H   289                                                      
REMARK 465     ASP H   290                                                      
REMARK 465     TYR H   291                                                      
REMARK 465     PRO H   292                                                      
REMARK 465     ALA H   293                                                      
REMARK 465     ALA H   294                                                      
REMARK 465     LEU H   295                                                      
REMARK 465     PRO H   296                                                      
REMARK 465     ASN H   297                                                      
REMARK 465     HIS H   298                                                      
REMARK 465     LYS H   299                                                      
REMARK 465     PRO H   300                                                      
REMARK 465     LYS H   301                                                      
REMARK 465     GLY H   302                                                      
REMARK 465     THR H   303                                                      
REMARK 465     PHE H   304                                                      
REMARK 465     LYS H   305                                                      
REMARK 465     ASP H   306                                                      
REMARK 465     TYR H   307                                                      
REMARK 465     VAL H   308                                                      
REMARK 465     ARG H   309                                                      
REMARK 465     ASP H   310                                                      
REMARK 465     ARG H   311                                                      
REMARK 465     ALA H   312                                                      
REMARK 465     ASP H   313                                                      
REMARK 465     LEU H   314                                                      
REMARK 465     ASN H   315                                                      
REMARK 465     LYS H   316                                                      
REMARK 465     ASP H   317                                                      
REMARK 465     LYS H   318                                                      
REMARK 465     PRO H   319                                                      
REMARK 465     VAL H   320                                                      
REMARK 465     ILE H   321                                                      
REMARK 465     PRO H   322                                                      
REMARK 465     ALA H   323                                                      
REMARK 465     ALA H   324                                                      
REMARK 465     ALA H   325                                                      
REMARK 465     LEU H   326                                                      
REMARK 465     ALA H   327                                                      
REMARK 465     GLY H   328                                                      
REMARK 465     TYR H   329                                                      
REMARK 465     THR H   330                                                      
REMARK 465     GLY H   331                                                      
REMARK 465     SER H   332                                                      
REMARK 465     PRO H   426                                                      
REMARK 465     GLU H   427                                                      
REMARK 465     GLU H   428                                                      
REMARK 465     LEU H   429                                                      
REMARK 465     HIS H   430                                                      
REMARK 465     ALA H   431                                                      
REMARK 465     MET H   432                                                      
REMARK 465     LEU H   433                                                      
REMARK 465     ASP H   434                                                      
REMARK 465     VAL H   435                                                      
REMARK 465     LYS H   436                                                      
REMARK 465     PRO H   437                                                      
REMARK 465     ASP H   438                                                      
REMARK 465     ALA H   439                                                      
REMARK 465     ASP H   440                                                      
REMARK 465     GLU H   441                                                      
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     ARG A 178    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500     DG D   4   O3'    DG D   4   C3'    -0.041                       
REMARK 500     DG I   4   O3'    DG I   4   C3'    -0.038                       
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     DG D   4   N9  -  C1' -  C2' ANGL. DEV. = -14.6 DEGREES          
REMARK 500     DC D   5   O4' -  C1' -  N1  ANGL. DEV. =   2.3 DEGREES          
REMARK 500     DA I   3   O4' -  C1' -  N9  ANGL. DEV. =   1.9 DEGREES          
REMARK 500     DG I   4   N9  -  C1' -  C2' ANGL. DEV. = -13.2 DEGREES          
REMARK 500     DC I   5   O4' -  C1' -  N1  ANGL. DEV. =   2.5 DEGREES          
REMARK 500     DC I   8   O4' -  C1' -  N1  ANGL. DEV. =   2.1 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    GLU A  61       75.29     71.81                                   
REMARK 500    LYS A  94      -70.41    -84.06                                   
REMARK 500    ASN A 109     -175.18   -172.39                                   
REMARK 500    ASN B  14      -65.49    -98.07                                   
REMARK 500    GLU B  24       78.82    -65.93                                   
REMARK 500    PHE B  32       53.06     28.16                                   
REMARK 500    PRO B  36      150.76    -48.46                                   
REMARK 500    PRO B  81     -121.04    -85.39                                   
REMARK 500    ARG B  83      -72.84   -101.05                                   
REMARK 500    ARG B  90        0.05    -66.59                                   
REMARK 500    GLU B  91      120.38    173.98                                   
REMARK 500    ASN B 104       56.07     39.97                                   
REMARK 500    LEU B 116       -5.58    -47.34                                   
REMARK 500    PHE B 127      155.90    -43.86                                   
REMARK 500    GLU B 130      -75.71    -60.61                                   
REMARK 500    TYR C 410       19.81     57.89                                   
REMARK 500    ASP C 434       70.50     51.88                                   
REMARK 500    ASN F 109     -165.36   -167.00                                   
REMARK 500    ASP F 110      -70.17    -53.36                                   
REMARK 500    GLU G  13       56.66   -111.37                                   
REMARK 500    ASN G  14      -24.90   -170.85                                   
REMARK 500    GLU G  24      137.96    -22.62                                   
REMARK 500    PHE G  32       63.66     34.93                                   
REMARK 500    VAL G  58      -56.45    -17.81                                   
REMARK 500    SER G  82      -50.59    174.00                                   
REMARK 500    ARG G  83      -45.77     76.53                                   
REMARK 500    ARG G  90      -44.36    -24.19                                   
REMARK 500    ALA G  92      -78.79    -86.86                                   
REMARK 500    LEU G 116       -4.89    -54.49                                   
REMARK 500    ASP G 128       74.20   -108.89                                   
REMARK 500    GLU G 130      -75.51    -51.50                                   
REMARK 500    PRO H 334      -72.16    -44.71                                   
REMARK 500    ILE H 335      117.28    177.72                                   
REMARK 500    PHE H 353     -105.75   -131.32                                   
REMARK 500    THR H 357      -47.61   -138.26                                   
REMARK 500    TRP H 361       -1.16   -157.66                                   
REMARK 500    LEU H 365       73.41   -112.67                                   
REMARK 500    ASP H 369        2.91    -62.62                                   
REMARK 500    GLU H 370      -65.97    -96.30                                   
REMARK 500    PRO H 382      -78.81    -56.41                                   
REMARK 500    LYS H 383       -7.98    -51.00                                   
REMARK 500    ARG H 409      -82.77    -82.60                                   
REMARK 500    LEU H 422      -30.93   -152.18                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500     DG D   4         0.05    SIDE CHAIN                              
REMARK 500     DC D   5         0.07    SIDE CHAIN                              
REMARK 500     DC D  12         0.09    SIDE CHAIN                              
REMARK 500     DT D  15         0.07    SIDE CHAIN                              
REMARK 500     DT E  13         0.08    SIDE CHAIN                              
REMARK 500     DG I   4         0.06    SIDE CHAIN                              
REMARK 500     DC I   5         0.07    SIDE CHAIN                              
REMARK 500     DA I   9         0.07    SIDE CHAIN                              
REMARK 500     DC I  12         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3WTS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3WTU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3WTV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3WTW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3WTX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3WTY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3WTZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3WU0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3WU1   RELATED DB: PDB                                   
DBREF  3WTT A   60   263  UNP    Q03347   RUNX1_MOUSE     60    263             
DBREF  3WTT B    1   142  UNP    Q08024   PEBB_MOUSE       1    142             
DBREF  3WTT C  276   441  UNP    P14921   ETS1_HUMAN     276    441             
DBREF  3WTT F   60   263  UNP    Q03347   RUNX1_MOUSE     60    263             
DBREF  3WTT G    1   142  UNP    Q08024   PEBB_MOUSE       1    142             
DBREF  3WTT H  276   441  UNP    P14921   ETS1_HUMAN     276    441             
DBREF  3WTT D    1    15  PDB    3WTT     3WTT             1     15             
DBREF  3WTT I    1    15  PDB    3WTT     3WTT             1     15             
DBREF  3WTT E    1    15  PDB    3WTT     3WTT             1     15             
DBREF  3WTT J    1    15  PDB    3WTT     3WTT             1     15             
SEQADV 3WTT LYS A   94  UNP  Q03347    LEU    94 ENGINEERED MUTATION            
SEQADV 3WTT LYS F   94  UNP  Q03347    LEU    94 ENGINEERED MUTATION            
SEQRES   1 A  204  GLY GLU LEU VAL ARG THR ASP SER PRO ASN PHE LEU CYS          
SEQRES   2 A  204  SER VAL LEU PRO THR HIS TRP ARG CYS ASN LYS THR LEU          
SEQRES   3 A  204  PRO ILE ALA PHE LYS VAL VAL ALA LYS GLY ASP VAL PRO          
SEQRES   4 A  204  ASP GLY THR LEU VAL THR VAL MET ALA GLY ASN ASP GLU          
SEQRES   5 A  204  ASN TYR SER ALA GLU LEU ARG ASN ALA THR ALA ALA MET          
SEQRES   6 A  204  LYS ASN GLN VAL ALA ARG PHE ASN ASP LEU ARG PHE VAL          
SEQRES   7 A  204  GLY ARG SER GLY ARG GLY LYS SER PHE THR LEU THR ILE          
SEQRES   8 A  204  THR VAL PHE THR ASN PRO PRO GLN VAL ALA THR TYR HIS          
SEQRES   9 A  204  ARG ALA ILE LYS ILE THR VAL ASP GLY PRO ARG GLU PRO          
SEQRES  10 A  204  ARG ARG HIS ARG GLN LYS LEU ASP ASP GLN THR LYS PRO          
SEQRES  11 A  204  GLY SER LEU SER PHE SER GLU ARG LEU SER GLU LEU GLU          
SEQRES  12 A  204  GLN LEU ARG ARG THR ALA MET ARG VAL SER PRO HIS HIS          
SEQRES  13 A  204  PRO ALA PRO THR PRO ASN PRO ARG ALA SER LEU ASN HIS          
SEQRES  14 A  204  SER THR ALA PHE ASN PRO GLN PRO GLN SER GLN MET GLN          
SEQRES  15 A  204  ASP ALA ARG GLN ILE GLN PRO SER PRO PRO TRP SER TYR          
SEQRES  16 A  204  ASP GLN SER TYR GLN TYR LEU GLY SER                          
SEQRES   1 B  142  MET PRO ARG VAL VAL PRO ASP GLN ARG SER LYS PHE GLU          
SEQRES   2 B  142  ASN GLU GLU PHE PHE ARG LYS LEU SER ARG GLU CYS GLU          
SEQRES   3 B  142  ILE LYS TYR THR GLY PHE ARG ASP ARG PRO HIS GLU GLU          
SEQRES   4 B  142  ARG GLN THR ARG PHE GLN ASN ALA CYS ARG ASP GLY ARG          
SEQRES   5 B  142  SER GLU ILE ALA PHE VAL ALA THR GLY THR ASN LEU SER          
SEQRES   6 B  142  LEU GLN PHE PHE PRO ALA SER TRP GLN GLY GLU GLN ARG          
SEQRES   7 B  142  GLN THR PRO SER ARG GLU TYR VAL ASP LEU GLU ARG GLU          
SEQRES   8 B  142  ALA GLY LYS VAL TYR LEU LYS ALA PRO MET ILE LEU ASN          
SEQRES   9 B  142  GLY VAL CYS VAL ILE TRP LYS GLY TRP ILE ASP LEU HIS          
SEQRES  10 B  142  ARG LEU ASP GLY MET GLY CYS LEU GLU PHE ASP GLU GLU          
SEQRES  11 B  142  ARG ALA GLN GLN GLU ASP ALA LEU ALA GLN GLN ALA              
SEQRES   1 C  166  SER LEU GLN ARG VAL PRO SER TYR ASP SER PHE ASP SER          
SEQRES   2 C  166  GLU ASP TYR PRO ALA ALA LEU PRO ASN HIS LYS PRO LYS          
SEQRES   3 C  166  GLY THR PHE LYS ASP TYR VAL ARG ASP ARG ALA ASP LEU          
SEQRES   4 C  166  ASN LYS ASP LYS PRO VAL ILE PRO ALA ALA ALA LEU ALA          
SEQRES   5 C  166  GLY TYR THR GLY SER GLY PRO ILE GLN LEU TRP GLN PHE          
SEQRES   6 C  166  LEU LEU GLU LEU LEU THR ASP LYS SER CYS GLN SER PHE          
SEQRES   7 C  166  ILE SER TRP THR GLY ASP GLY TRP GLU PHE LYS LEU SER          
SEQRES   8 C  166  ASP PRO ASP GLU VAL ALA ARG ARG TRP GLY LYS ARG LYS          
SEQRES   9 C  166  ASN LYS PRO LYS MET ASN TYR GLU LYS LEU SER ARG GLY          
SEQRES  10 C  166  LEU ARG TYR TYR TYR ASP LYS ASN ILE ILE HIS LYS THR          
SEQRES  11 C  166  ALA GLY LYS ARG TYR VAL TYR ARG PHE VAL CYS ASP LEU          
SEQRES  12 C  166  GLN SER LEU LEU GLY TYR THR PRO GLU GLU LEU HIS ALA          
SEQRES  13 C  166  MET LEU ASP VAL LYS PRO ASP ALA ASP GLU                      
SEQRES   1 F  204  GLY GLU LEU VAL ARG THR ASP SER PRO ASN PHE LEU CYS          
SEQRES   2 F  204  SER VAL LEU PRO THR HIS TRP ARG CYS ASN LYS THR LEU          
SEQRES   3 F  204  PRO ILE ALA PHE LYS VAL VAL ALA LYS GLY ASP VAL PRO          
SEQRES   4 F  204  ASP GLY THR LEU VAL THR VAL MET ALA GLY ASN ASP GLU          
SEQRES   5 F  204  ASN TYR SER ALA GLU LEU ARG ASN ALA THR ALA ALA MET          
SEQRES   6 F  204  LYS ASN GLN VAL ALA ARG PHE ASN ASP LEU ARG PHE VAL          
SEQRES   7 F  204  GLY ARG SER GLY ARG GLY LYS SER PHE THR LEU THR ILE          
SEQRES   8 F  204  THR VAL PHE THR ASN PRO PRO GLN VAL ALA THR TYR HIS          
SEQRES   9 F  204  ARG ALA ILE LYS ILE THR VAL ASP GLY PRO ARG GLU PRO          
SEQRES  10 F  204  ARG ARG HIS ARG GLN LYS LEU ASP ASP GLN THR LYS PRO          
SEQRES  11 F  204  GLY SER LEU SER PHE SER GLU ARG LEU SER GLU LEU GLU          
SEQRES  12 F  204  GLN LEU ARG ARG THR ALA MET ARG VAL SER PRO HIS HIS          
SEQRES  13 F  204  PRO ALA PRO THR PRO ASN PRO ARG ALA SER LEU ASN HIS          
SEQRES  14 F  204  SER THR ALA PHE ASN PRO GLN PRO GLN SER GLN MET GLN          
SEQRES  15 F  204  ASP ALA ARG GLN ILE GLN PRO SER PRO PRO TRP SER TYR          
SEQRES  16 F  204  ASP GLN SER TYR GLN TYR LEU GLY SER                          
SEQRES   1 G  142  MET PRO ARG VAL VAL PRO ASP GLN ARG SER LYS PHE GLU          
SEQRES   2 G  142  ASN GLU GLU PHE PHE ARG LYS LEU SER ARG GLU CYS GLU          
SEQRES   3 G  142  ILE LYS TYR THR GLY PHE ARG ASP ARG PRO HIS GLU GLU          
SEQRES   4 G  142  ARG GLN THR ARG PHE GLN ASN ALA CYS ARG ASP GLY ARG          
SEQRES   5 G  142  SER GLU ILE ALA PHE VAL ALA THR GLY THR ASN LEU SER          
SEQRES   6 G  142  LEU GLN PHE PHE PRO ALA SER TRP GLN GLY GLU GLN ARG          
SEQRES   7 G  142  GLN THR PRO SER ARG GLU TYR VAL ASP LEU GLU ARG GLU          
SEQRES   8 G  142  ALA GLY LYS VAL TYR LEU LYS ALA PRO MET ILE LEU ASN          
SEQRES   9 G  142  GLY VAL CYS VAL ILE TRP LYS GLY TRP ILE ASP LEU HIS          
SEQRES  10 G  142  ARG LEU ASP GLY MET GLY CYS LEU GLU PHE ASP GLU GLU          
SEQRES  11 G  142  ARG ALA GLN GLN GLU ASP ALA LEU ALA GLN GLN ALA              
SEQRES   1 H  166  SER LEU GLN ARG VAL PRO SER TYR ASP SER PHE ASP SER          
SEQRES   2 H  166  GLU ASP TYR PRO ALA ALA LEU PRO ASN HIS LYS PRO LYS          
SEQRES   3 H  166  GLY THR PHE LYS ASP TYR VAL ARG ASP ARG ALA ASP LEU          
SEQRES   4 H  166  ASN LYS ASP LYS PRO VAL ILE PRO ALA ALA ALA LEU ALA          
SEQRES   5 H  166  GLY TYR THR GLY SER GLY PRO ILE GLN LEU TRP GLN PHE          
SEQRES   6 H  166  LEU LEU GLU LEU LEU THR ASP LYS SER CYS GLN SER PHE          
SEQRES   7 H  166  ILE SER TRP THR GLY ASP GLY TRP GLU PHE LYS LEU SER          
SEQRES   8 H  166  ASP PRO ASP GLU VAL ALA ARG ARG TRP GLY LYS ARG LYS          
SEQRES   9 H  166  ASN LYS PRO LYS MET ASN TYR GLU LYS LEU SER ARG GLY          
SEQRES  10 H  166  LEU ARG TYR TYR TYR ASP LYS ASN ILE ILE HIS LYS THR          
SEQRES  11 H  166  ALA GLY LYS ARG TYR VAL TYR ARG PHE VAL CYS ASP LEU          
SEQRES  12 H  166  GLN SER LEU LEU GLY TYR THR PRO GLU GLU LEU HIS ALA          
SEQRES  13 H  166  MET LEU ASP VAL LYS PRO ASP ALA ASP GLU                      
SEQRES   1 D   15   DG  DA  DA  DG  DC  DC  DA  DC  DA  DT  DC  DC  DT          
SEQRES   2 D   15   DC  DT                                                      
SEQRES   1 E   15   DA  DG  DA  DG  DG  DA  DT  DG  DT  DG  DG  DC  DT          
SEQRES   2 E   15   DT  DC                                                      
SEQRES   1 I   15   DG  DA  DA  DG  DC  DC  DA  DC  DA  DT  DC  DC  DT          
SEQRES   2 I   15   DC  DT                                                      
SEQRES   1 J   15   DA  DG  DA  DG  DG  DA  DT  DG  DT  DG  DG  DC  DT          
SEQRES   2 J   15   DT  DC                                                      
FORMUL  11  HOH   *127(H2 O)                                                    
HELIX    1   1 ASP B    7  GLU B   15  1                                   9    
HELIX    2   2 GLU B   15  LYS B   20  1                                   6    
HELIX    3   3 PRO B   36  ASP B   50  1                                  15    
HELIX    4   4 ASP B  128  GLU B  135  1                                   8    
HELIX    5   5 GLU B  135  GLN B  140  1                                   6    
HELIX    6   6 PRO C  322  ALA C  327  1                                   6    
HELIX    7   7 GLN C  336  THR C  346  1                                  11    
HELIX    8   8 ASP C  347  PHE C  353  5                                   7    
HELIX    9   9 ASP C  367  ASN C  380  1                                  14    
HELIX   10  10 ASN C  385  TYR C  396  1                                  12    
HELIX   11  11 ASP C  417  GLY C  423  1                                   7    
HELIX   12  12 THR C  425  LEU C  433  1                                   9    
HELIX   13  13 ASP G    7  GLU G   13  1                                   7    
HELIX   14  14 GLU G   15  ARG G   23  1                                   9    
HELIX   15  15 PRO G   36  GLY G   51  1                                  16    
HELIX   16  16 ASP G  128  ALA G  139  1                                  12    
HELIX   17  17 GLN H  336  THR H  346  1                                  11    
HELIX   18  18 ASP H  367  LYS H  379  1                                  13    
HELIX   19  19 ASN H  385  TYR H  395  1                                  11    
HELIX   20  20 TYR H  395  ASN H  400  1                                   6    
SHEET    1   A14 LEU A  62  ARG A  64  0                                        
SHEET    2   A14 PHE A  70  SER A  73 -1  O  CYS A  72   N  VAL A  63           
SHEET    3   A14 LYS A  90  ALA A  93 -1  O  VAL A  92   N  LEU A  71           
SHEET    4   A14 VAL A 128  ARG A 130 -1  O  ALA A 129   N  VAL A  91           
SHEET    5   A14 THR A 121  LYS A 125 -1  N  LYS A 125   O  VAL A 128           
SHEET    6   A14 LEU A 102  GLY A 108 -1  N  VAL A 103   O  ALA A 122           
SHEET    7   A14 PHE A 146  VAL A 152 -1  O  THR A 147   N  GLY A 108           
SHEET    8   A14 GLN A 158  THR A 169 -1  O  GLN A 158   N  VAL A 152           
SHEET    9   A14 LYS B  94  LEU B 103  1  O  ILE B 102   N  VAL A 159           
SHEET   10   A14 VAL B 106  ASP B 115 -1  O  TRP B 110   N  ALA B  99           
SHEET   11   A14 ASP B 120  PHE B 127 -1  O  ASP B 120   N  ASP B 115           
SHEET   12   A14 CYS B  25  TYR B  29 -1  N  ILE B  27   O  GLY B 121           
SHEET   13   A14 ARG B  52  ALA B  56 -1  O  ALA B  56   N  LYS B  28           
SHEET   14   A14 ASN B  63  GLN B  67 -1  O  LEU B  66   N  SER B  53           
SHEET    1   B 4 HIS A  78  ARG A  80  0                                        
SHEET    2   B 4 GLN A 158  THR A 169  1  O  LYS A 167   N  TRP A  79           
SHEET    3   B 4 LYS B  94  LEU B 103  1  O  ILE B 102   N  VAL A 159           
SHEET    4   B 4 VAL B  86  ASP B  87 -1  N  ASP B  87   O  TYR B  96           
SHEET    1   C 2 LEU A 117  ARG A 118  0                                        
SHEET    2   C 2 ARG A 135  PHE A 136 -1  O  ARG A 135   N  ARG A 118           
SHEET    1   D 4 SER C 355  TRP C 356  0                                        
SHEET    2   D 4 GLU C 362  LYS C 364 -1  O  LYS C 364   N  SER C 355           
SHEET    3   D 4 VAL C 411  PHE C 414 -1  O  TYR C 412   N  PHE C 363           
SHEET    4   D 4 ILE C 402  LYS C 404 -1  N  HIS C 403   O  ARG C 413           
SHEET    1   E14 LEU F  62  ARG F  64  0                                        
SHEET    2   E14 PHE F  70  SER F  73 -1  O  CYS F  72   N  VAL F  63           
SHEET    3   E14 LYS F  90  ALA F  93 -1  O  VAL F  92   N  LEU F  71           
SHEET    4   E14 VAL F 128  ARG F 130 -1  O  ALA F 129   N  VAL F  91           
SHEET    5   E14 THR F 121  LYS F 125 -1  N  LYS F 125   O  VAL F 128           
SHEET    6   E14 LEU F 102  GLY F 108 -1  N  VAL F 103   O  ALA F 122           
SHEET    7   E14 PHE F 146  VAL F 152 -1  O  THR F 149   N  MET F 106           
SHEET    8   E14 GLN F 158  THR F 169 -1  O  ILE F 166   N  PHE F 146           
SHEET    9   E14 LYS G  94  LEU G 103  1  O  ILE G 102   N  VAL F 159           
SHEET   10   E14 VAL G 106  ASP G 115 -1  O  TRP G 110   N  ALA G  99           
SHEET   11   E14 ASP G 120  PHE G 127 -1  O  ASP G 120   N  ASP G 115           
SHEET   12   E14 CYS G  25  TYR G  29 -1  N  ILE G  27   O  GLY G 121           
SHEET   13   E14 ARG G  52  ALA G  56 -1  O  ALA G  56   N  LYS G  28           
SHEET   14   E14 ASN G  63  GLN G  67 -1  O  LEU G  66   N  SER G  53           
SHEET    1   F 4 HIS F  78  ARG F  80  0                                        
SHEET    2   F 4 GLN F 158  THR F 169  1  O  LYS F 167   N  TRP F  79           
SHEET    3   F 4 LYS G  94  LEU G 103  1  O  ILE G 102   N  VAL F 159           
SHEET    4   F 4 VAL G  86  ASP G  87 -1  N  ASP G  87   O  TYR G  96           
SHEET    1   G 2 LEU F 117  ARG F 118  0                                        
SHEET    2   G 2 ARG F 135  PHE F 136 -1  O  ARG F 135   N  ARG F 118           
SHEET    1   H 4 ILE H 354  TRP H 356  0                                        
SHEET    2   H 4 GLU H 362  LEU H 365 -1  O  LYS H 364   N  SER H 355           
SHEET    3   H 4 VAL H 411  ARG H 413 -1  O  TYR H 412   N  PHE H 363           
SHEET    4   H 4 HIS H 403  LYS H 404 -1  N  HIS H 403   O  ARG H 413           
CISPEP   1 ASN A  155    PRO A  156          0         1.51                     
CISPEP   2 THR B   80    PRO B   81          0         0.83                     
CISPEP   3 ASN F  155    PRO F  156          0        -0.16                     
CRYST1   78.618  101.718  194.721  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012720  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009831  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005136        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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