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Database: PDB
Entry: 3WTZ
LinkDB: 3WTZ
Original site: 3WTZ 
HEADER    TRANSCRIPTION                           21-APR-14   3WTZ              
TITLE     CRYSTAL STRUCTURE OF ETS-1 DNA BINDING AND AUTOINHIBITORY DOMAINS     
TITLE    2 (276-441)                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN C-ETS-1;                                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 276-441;                                      
COMPND   5 SYNONYM: P54;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ETS1, EWSR2;                                                   
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                                    
KEYWDS    TRANSCRIPTION, ETS-1, AUTOINHIBITION, ETS DOMAIN, DNA-BINDING,        
KEYWDS   2 ISOPEPTIDE BOND, NUCLEUS, PHOSPHOPROTEIN, PROTO-ONCOGENE,            
KEYWDS   3 TRANSCRIPTION REGULATION                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.SHIINA,K.HAMADA,K.OGATA                                             
REVDAT   2   22-NOV-17 3WTZ    1       REMARK                                   
REVDAT   1   20-AUG-14 3WTZ    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.    2.61 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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) : 2.61                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.42                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 821361.000                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 11947                          
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) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.300                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1232                            
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) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.76                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1688                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3090                       
REMARK   3   BIN FREE R VALUE                    : 0.3320                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.20                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 192                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.024                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2223                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 22                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 85.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 10.00000                                             
REMARK   3    B22 (A**2) : 10.00000                                             
REMARK   3    B33 (A**2) : -20.00000                                            
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) : 0.33                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.36                            
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) : 0.39                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.41                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.000                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.750                           
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) : 1.730 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.080 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.010 ; 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        : 0.40                                                 
REMARK   3   BSOL        : 80.99                                                
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  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 3WTZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-MAY-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000096789.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-MAR-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : AR-NW12A                           
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 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000, DENZO                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11974                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : 0.05900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32500                            
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: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1GVJ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.62                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 9% MPD, 6% PEG 6000, 0.1M HEPES, PH      
REMARK 280  7.8, VAPOR DIFFUSION, SITTING DROP                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       35.61767            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       71.23533            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15540 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A   276                                                      
REMARK 465     LEU A   277                                                      
REMARK 465     GLN A   278                                                      
REMARK 465     ARG A   279                                                      
REMARK 465     VAL A   280                                                      
REMARK 465     PRO A   281                                                      
REMARK 465     SER A   282                                                      
REMARK 465     TYR A   283                                                      
REMARK 465     ASP A   284                                                      
REMARK 465     SER A   285                                                      
REMARK 465     PHE A   286                                                      
REMARK 465     ASP A   287                                                      
REMARK 465     SER A   288                                                      
REMARK 465     GLU A   289                                                      
REMARK 465     ASP A   290                                                      
REMARK 465     TYR A   291                                                      
REMARK 465     PRO A   292                                                      
REMARK 465     ALA A   293                                                      
REMARK 465     ALA A   294                                                      
REMARK 465     LEU A   295                                                      
REMARK 465     PRO A   296                                                      
REMARK 465     ASN A   297                                                      
REMARK 465     HIS A   298                                                      
REMARK 465     LYS A   299                                                      
REMARK 465     PRO A   300                                                      
REMARK 465     ARG A   311                                                      
REMARK 465     ALA A   312                                                      
REMARK 465     ASP A   313                                                      
REMARK 465     LEU A   314                                                      
REMARK 465     ASN A   315                                                      
REMARK 465     GLU A   441                                                      
REMARK 465     SER B   276                                                      
REMARK 465     LEU B   277                                                      
REMARK 465     GLN B   278                                                      
REMARK 465     ARG B   279                                                      
REMARK 465     VAL B   280                                                      
REMARK 465     PRO B   281                                                      
REMARK 465     SER B   282                                                      
REMARK 465     TYR B   283                                                      
REMARK 465     ASP B   284                                                      
REMARK 465     SER B   285                                                      
REMARK 465     PHE B   286                                                      
REMARK 465     ASP B   287                                                      
REMARK 465     SER B   288                                                      
REMARK 465     GLU B   289                                                      
REMARK 465     ASP B   290                                                      
REMARK 465     TYR B   291                                                      
REMARK 465     PRO B   292                                                      
REMARK 465     ALA B   293                                                      
REMARK 465     ALA B   294                                                      
REMARK 465     LEU B   295                                                      
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     PRO B   437                                                      
REMARK 465     ASP B   438                                                      
REMARK 465     ALA B   439                                                      
REMARK 465     ASP B   440                                                      
REMARK 465     GLU B   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     ASP A 440    CG   OD1  OD2                                       
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    ILE A 321       78.22   -112.61                                   
REMARK 500    GLN A 351       -6.99    -55.58                                   
REMARK 500    ASN A 380       61.06     64.05                                   
REMARK 500    LYS A 383       20.81    -77.00                                   
REMARK 500    ASP A 438     -170.76    -62.63                                   
REMARK 500    LEU B 314      -64.62    -96.18                                   
REMARK 500    ASP B 317       74.95   -167.28                                   
REMARK 500    GLN B 351        0.52    -58.12                                   
REMARK 500    TRP B 361       30.75    -88.90                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3WTS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3WTT   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: 3WU0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3WU1   RELATED DB: PDB                                   
DBREF  3WTZ A  276   441  UNP    P14921   ETS1_HUMAN     276    441             
DBREF  3WTZ B  276   441  UNP    P14921   ETS1_HUMAN     276    441             
SEQRES   1 A  166  SER LEU GLN ARG VAL PRO SER TYR ASP SER PHE ASP SER          
SEQRES   2 A  166  GLU ASP TYR PRO ALA ALA LEU PRO ASN HIS LYS PRO LYS          
SEQRES   3 A  166  GLY THR PHE LYS ASP TYR VAL ARG ASP ARG ALA ASP LEU          
SEQRES   4 A  166  ASN LYS ASP LYS PRO VAL ILE PRO ALA ALA ALA LEU ALA          
SEQRES   5 A  166  GLY TYR THR GLY SER GLY PRO ILE GLN LEU TRP GLN PHE          
SEQRES   6 A  166  LEU LEU GLU LEU LEU THR ASP LYS SER CYS GLN SER PHE          
SEQRES   7 A  166  ILE SER TRP THR GLY ASP GLY TRP GLU PHE LYS LEU SER          
SEQRES   8 A  166  ASP PRO ASP GLU VAL ALA ARG ARG TRP GLY LYS ARG LYS          
SEQRES   9 A  166  ASN LYS PRO LYS MET ASN TYR GLU LYS LEU SER ARG GLY          
SEQRES  10 A  166  LEU ARG TYR TYR TYR ASP LYS ASN ILE ILE HIS LYS THR          
SEQRES  11 A  166  ALA GLY LYS ARG TYR VAL TYR ARG PHE VAL CYS ASP LEU          
SEQRES  12 A  166  GLN SER LEU LEU GLY TYR THR PRO GLU GLU LEU HIS ALA          
SEQRES  13 A  166  MET LEU ASP VAL LYS PRO ASP ALA ASP GLU                      
SEQRES   1 B  166  SER LEU GLN ARG VAL PRO SER TYR ASP SER PHE ASP SER          
SEQRES   2 B  166  GLU ASP TYR PRO ALA ALA LEU PRO ASN HIS LYS PRO LYS          
SEQRES   3 B  166  GLY THR PHE LYS ASP TYR VAL ARG ASP ARG ALA ASP LEU          
SEQRES   4 B  166  ASN LYS ASP LYS PRO VAL ILE PRO ALA ALA ALA LEU ALA          
SEQRES   5 B  166  GLY TYR THR GLY SER GLY PRO ILE GLN LEU TRP GLN PHE          
SEQRES   6 B  166  LEU LEU GLU LEU LEU THR ASP LYS SER CYS GLN SER PHE          
SEQRES   7 B  166  ILE SER TRP THR GLY ASP GLY TRP GLU PHE LYS LEU SER          
SEQRES   8 B  166  ASP PRO ASP GLU VAL ALA ARG ARG TRP GLY LYS ARG LYS          
SEQRES   9 B  166  ASN LYS PRO LYS MET ASN TYR GLU LYS LEU SER ARG GLY          
SEQRES  10 B  166  LEU ARG TYR TYR TYR ASP LYS ASN ILE ILE HIS LYS THR          
SEQRES  11 B  166  ALA GLY LYS ARG TYR VAL TYR ARG PHE VAL CYS ASP LEU          
SEQRES  12 B  166  GLN SER LEU LEU GLY TYR THR PRO GLU GLU LEU HIS ALA          
SEQRES  13 B  166  MET LEU ASP VAL LYS PRO ASP ALA ASP GLU                      
FORMUL   3  HOH   *22(H2 O)                                                     
HELIX    1   1 THR A  303  ASP A  310  1                                   8    
HELIX    2   2 PRO A  322  GLY A  331  1                                  10    
HELIX    3   3 GLN A  336  THR A  346  1                                  11    
HELIX    4   4 ASP A  347  GLN A  351  5                                   5    
HELIX    5   5 ASP A  367  ASN A  380  1                                  14    
HELIX    6   6 ASN A  385  LYS A  399  1                                  15    
HELIX    7   7 ASP A  417  GLY A  423  1                                   7    
HELIX    8   8 THR A  425  LEU A  433  1                                   9    
HELIX    9   9 THR B  303  ASN B  315  1                                  13    
HELIX   10  10 PRO B  322  THR B  330  1                                   9    
HELIX   11  11 GLN B  336  THR B  346  1                                  11    
HELIX   12  12 ASP B  347  GLN B  351  5                                   5    
HELIX   13  13 ASP B  367  LYS B  377  1                                  11    
HELIX   14  14 TYR B  386  LYS B  399  1                                  14    
HELIX   15  15 ASP B  417  GLY B  423  1                                   7    
HELIX   16  16 THR B  425  LEU B  433  1                                   9    
SHEET    1   A 4 ILE A 354  TRP A 356  0                                        
SHEET    2   A 4 GLU A 362  LEU A 365 -1  O  LYS A 364   N  SER A 355           
SHEET    3   A 4 VAL A 411  PHE A 414 -1  O  TYR A 412   N  PHE A 363           
SHEET    4   A 4 ILE A 402  LYS A 404 -1  N  HIS A 403   O  ARG A 413           
SHEET    1   B 4 ILE B 354  TRP B 356  0                                        
SHEET    2   B 4 GLU B 362  LEU B 365 -1  O  LYS B 364   N  SER B 355           
SHEET    3   B 4 VAL B 411  PHE B 414 -1  O  TYR B 412   N  PHE B 363           
SHEET    4   B 4 ILE B 402  LYS B 404 -1  N  HIS B 403   O  ARG B 413           
CRYST1   57.484   57.484  106.853  90.00  90.00 120.00 P 31          6          
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      0.017396  0.010044  0.000000        0.00000                         
SCALE2      0.000000  0.020087  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009359        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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