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Database: PDB
Entry: 2NNY
LinkDB: 2NNY
Original site: 2NNY 
HEADER    TRANSCRIPTION/DNA                       24-OCT-06   2NNY              
TITLE     CRYSTAL STRUCTURE OF THE ETS1 DIMER DNA COMPLEX.                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 5'-                                                        
COMPND   3 D(*T*AP*GP*AP*CP*AP*GP*GP*AP*AP*GP*CP*AP*CP*TP*TP*CP*CP*TP*          
COMPND   4 GP*GP*AP*G)-3';                                                      
COMPND   5 CHAIN: C;                                                            
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: 5'-                                                        
COMPND   9 D(*A*CP*TP*CP*CP*AP*GP*GP*AP*AP*GP*TP*GP*CP*TP*TP*CP*CP*TP*          
COMPND  10 GP*TP*CP*T)-3';                                                      
COMPND  11 CHAIN: D;                                                            
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: C-ETS-1 PROTEIN;                                           
COMPND  15 CHAIN: A, B;                                                         
COMPND  16 FRAGMENT: RESIDUES 280-441;                                          
COMPND  17 SYNONYM: P54;                                                        
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 MOL_ID: 2;                                                           
SOURCE   4 SYNTHETIC: YES;                                                      
SOURCE   5 MOL_ID: 3;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   7 ORGANISM_COMMON: HUMAN;                                              
SOURCE   8 ORGANISM_TAXID: 9606;                                                
SOURCE   9 GENE: ETS1;                                                          
SOURCE  10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  11 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  12 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) RIL;                             
SOURCE  13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  14 EXPRESSION_SYSTEM_PLASMID: PETM10                                    
KEYWDS    ETS-1, PROTEIN-DNA COMPLEX, TRANSCRIPTION/DNA COMPLEX                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.P.LAMBER,G.S.KACHALOVA,M.WILMANNS                                   
REVDAT   3   24-FEB-09 2NNY    1       VERSN                                    
REVDAT   2   09-SEP-08 2NNY    1       JRNL                                     
REVDAT   1   04-MAR-08 2NNY    0                                                
JRNL        AUTH   E.P.LAMBER,L.VANHILLE,L.C.TEXTOR,G.S.KACHALOVA,              
JRNL        AUTH 2 M.H.SIEWEKE,M.WILMANNS                                       
JRNL        TITL   REGULATION OF THE TRANSCRIPTION FACTOR ETS-1 BY              
JRNL        TITL 2 DNA-MEDIATED HOMO-DIMERIZATION.                              
JRNL        REF    EMBO J.                       V.  27  2006 2008              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   18566588                                                     
JRNL        DOI    10.1038/EMBOJ.2008.117                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.58 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.58                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.69                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 19446                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : R-FREE                          
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.235                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1041                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2118                                    
REMARK   3   NUCLEIC ACID ATOMS       : 896                                     
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 46                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2NNY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-OCT-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB040093.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-SEP-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9756                             
REMARK 200  MONOCHROMATOR                  : SI(311)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20507                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.580                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.960                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY                : 2.700                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.4500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1K79                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.31                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE   28% PEG         
REMARK 280  2000 0.1 M SODIUM CITRATE, PH 5.6, VAPOR DIFFUSION, SITTING         
REMARK 280  DROP, TEMPERATURE 100K, TEMPERATURE 298K                            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       46.77800            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       50.41900            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       46.77800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       50.41900            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, 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      DT C     1                                                      
REMARK 465      DA D     1                                                      
REMARK 465     MET A   271                                                      
REMARK 465     LYS A   272                                                      
REMARK 465     HIS A   273                                                      
REMARK 465     HIS A   274                                                      
REMARK 465     HIS A   275                                                      
REMARK 465     HIS A   276                                                      
REMARK 465     HIS A   277                                                      
REMARK 465     PRO A   278                                                      
REMARK 465     MET 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     LYS A   301                                                      
REMARK 465     GLY A   302                                                      
REMARK 465     THR A   303                                                      
REMARK 465     PHE A   304                                                      
REMARK 465     LYS A   305                                                      
REMARK 465     ASP A   306                                                      
REMARK 465     TYR A   307                                                      
REMARK 465     PRO A   437                                                      
REMARK 465     ASP A   438                                                      
REMARK 465     ALA A   439                                                      
REMARK 465     ASP A   440                                                      
REMARK 465     GLU A   441                                                      
REMARK 465     MET B   271                                                      
REMARK 465     LYS B   272                                                      
REMARK 465     HIS B   273                                                      
REMARK 465     HIS B   274                                                      
REMARK 465     HIS B   275                                                      
REMARK 465     HIS B   276                                                      
REMARK 465     HIS B   277                                                      
REMARK 465     PRO B   278                                                      
REMARK 465     MET 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     LYS B   301                                                      
REMARK 465     GLY B   302                                                      
REMARK 465     THR B   303                                                      
REMARK 465     PHE B   304                                                      
REMARK 465     LYS B   305                                                      
REMARK 465     ASP B   306                                                      
REMARK 465     TYR B   307                                                      
REMARK 465     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      DA C   2    P    OP1  OP2                                       
REMARK 470      DC D   2    P    OP1  OP2                                       
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    ASP A 310       88.44    -49.92                                   
REMARK 500    LEU A 314     -136.68     31.02                                   
REMARK 500    ASN A 315     -101.68    -85.39                                   
REMARK 500    LYS A 316     -121.73   -179.78                                   
REMARK 500    GLN A 351       -6.45    -51.57                                   
REMARK 500    ASN A 400       74.65     38.22                                   
REMARK 500    ILE A 401      -47.18   -132.67                                   
REMARK 500    LEU A 433     -131.73    -87.18                                   
REMARK 500    ASP A 434       88.12   -160.05                                   
REMARK 500    ASP B 310       38.52    -69.76                                   
REMARK 500    ASN B 315       44.55   -149.50                                   
REMARK 500    LYS B 316     -156.71    -62.13                                   
REMARK 500    PRO B 334      150.16    -48.06                                   
REMARK 500    GLN B 351        6.58    -61.61                                   
REMARK 500    ASP B 434       72.86   -115.37                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 451        DISTANCE =  7.46 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1K78   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1GVJ   RELATED DB: PDB                                   
DBREF  2NNY A  280   441  UNP    P14921   ETS1_HUMAN     280    441             
DBREF  2NNY B  280   441  UNP    P14921   ETS1_HUMAN     280    441             
DBREF  2NNY C    1    23  PDB    2NNY     2NNY             1     23             
DBREF  2NNY D    1    23  PDB    2NNY     2NNY             1     23             
SEQADV 2NNY MET A  271  UNP  P14921              EXPRESSION TAG                 
SEQADV 2NNY LYS A  272  UNP  P14921              EXPRESSION TAG                 
SEQADV 2NNY HIS A  273  UNP  P14921              EXPRESSION TAG                 
SEQADV 2NNY HIS A  274  UNP  P14921              EXPRESSION TAG                 
SEQADV 2NNY HIS A  275  UNP  P14921              EXPRESSION TAG                 
SEQADV 2NNY HIS A  276  UNP  P14921              EXPRESSION TAG                 
SEQADV 2NNY HIS A  277  UNP  P14921              EXPRESSION TAG                 
SEQADV 2NNY PRO A  278  UNP  P14921              EXPRESSION TAG                 
SEQADV 2NNY MET A  279  UNP  P14921              EXPRESSION TAG                 
SEQADV 2NNY SER A  350  UNP  P14921    CYS   350 ENGINEERED                     
SEQADV 2NNY SER A  416  UNP  P14921    CYS   416 ENGINEERED                     
SEQADV 2NNY MET B  271  UNP  P14921              EXPRESSION TAG                 
SEQADV 2NNY LYS B  272  UNP  P14921              EXPRESSION TAG                 
SEQADV 2NNY HIS B  273  UNP  P14921              EXPRESSION TAG                 
SEQADV 2NNY HIS B  274  UNP  P14921              EXPRESSION TAG                 
SEQADV 2NNY HIS B  275  UNP  P14921              EXPRESSION TAG                 
SEQADV 2NNY HIS B  276  UNP  P14921              EXPRESSION TAG                 
SEQADV 2NNY HIS B  277  UNP  P14921              EXPRESSION TAG                 
SEQADV 2NNY PRO B  278  UNP  P14921              EXPRESSION TAG                 
SEQADV 2NNY MET B  279  UNP  P14921              EXPRESSION TAG                 
SEQADV 2NNY SER B  350  UNP  P14921    CYS   350 ENGINEERED                     
SEQADV 2NNY SER B  416  UNP  P14921    CYS   416 ENGINEERED                     
SEQRES   1 C   23   DT  DA  DG  DA  DC  DA  DG  DG  DA  DA  DG  DC  DA          
SEQRES   2 C   23   DC  DT  DT  DC  DC  DT  DG  DG  DA  DG                      
SEQRES   1 D   23   DA  DC  DT  DC  DC  DA  DG  DG  DA  DA  DG  DT  DG          
SEQRES   2 D   23   DC  DT  DT  DC  DC  DT  DG  DT  DC  DT                      
SEQRES   1 A  171  MET LYS HIS HIS HIS HIS HIS PRO MET VAL PRO SER TYR          
SEQRES   2 A  171  ASP SER PHE ASP SER GLU ASP TYR PRO ALA ALA LEU PRO          
SEQRES   3 A  171  ASN HIS LYS PRO LYS GLY THR PHE LYS ASP TYR VAL ARG          
SEQRES   4 A  171  ASP ARG ALA ASP LEU ASN LYS ASP LYS PRO VAL ILE PRO          
SEQRES   5 A  171  ALA ALA ALA LEU ALA GLY TYR THR GLY SER GLY PRO ILE          
SEQRES   6 A  171  GLN LEU TRP GLN PHE LEU LEU GLU LEU LEU THR ASP LYS          
SEQRES   7 A  171  SER SER GLN SER PHE ILE SER TRP THR GLY ASP GLY TRP          
SEQRES   8 A  171  GLU PHE LYS LEU SER ASP PRO ASP GLU VAL ALA ARG ARG          
SEQRES   9 A  171  TRP GLY LYS ARG LYS ASN LYS PRO LYS MET ASN TYR GLU          
SEQRES  10 A  171  LYS LEU SER ARG GLY LEU ARG TYR TYR TYR ASP LYS ASN          
SEQRES  11 A  171  ILE ILE HIS LYS THR ALA GLY LYS ARG TYR VAL TYR ARG          
SEQRES  12 A  171  PHE VAL SER ASP LEU GLN SER LEU LEU GLY TYR THR PRO          
SEQRES  13 A  171  GLU GLU LEU HIS ALA MET LEU ASP VAL LYS PRO ASP ALA          
SEQRES  14 A  171  ASP GLU                                                      
SEQRES   1 B  171  MET LYS HIS HIS HIS HIS HIS PRO MET VAL PRO SER TYR          
SEQRES   2 B  171  ASP SER PHE ASP SER GLU ASP TYR PRO ALA ALA LEU PRO          
SEQRES   3 B  171  ASN HIS LYS PRO LYS GLY THR PHE LYS ASP TYR VAL ARG          
SEQRES   4 B  171  ASP ARG ALA ASP LEU ASN LYS ASP LYS PRO VAL ILE PRO          
SEQRES   5 B  171  ALA ALA ALA LEU ALA GLY TYR THR GLY SER GLY PRO ILE          
SEQRES   6 B  171  GLN LEU TRP GLN PHE LEU LEU GLU LEU LEU THR ASP LYS          
SEQRES   7 B  171  SER SER GLN SER PHE ILE SER TRP THR GLY ASP GLY TRP          
SEQRES   8 B  171  GLU PHE LYS LEU SER ASP PRO ASP GLU VAL ALA ARG ARG          
SEQRES   9 B  171  TRP GLY LYS ARG LYS ASN LYS PRO LYS MET ASN TYR GLU          
SEQRES  10 B  171  LYS LEU SER ARG GLY LEU ARG TYR TYR TYR ASP LYS ASN          
SEQRES  11 B  171  ILE ILE HIS LYS THR ALA GLY LYS ARG TYR VAL TYR ARG          
SEQRES  12 B  171  PHE VAL SER ASP LEU GLN SER LEU LEU GLY TYR THR PRO          
SEQRES  13 B  171  GLU GLU LEU HIS ALA MET LEU ASP VAL LYS PRO ASP ALA          
SEQRES  14 B  171  ASP GLU                                                      
FORMUL   5  HOH   *46(H2 O)                                                     
HELIX    1   1 PRO A  322  GLY A  331  1                                  10    
HELIX    2   2 GLN A  336  THR A  346  1                                  11    
HELIX    3   3 ASP A  347  PHE A  353  5                                   7    
HELIX    4   4 ASP A  367  ASN A  380  1                                  14    
HELIX    5   5 ASN A  385  TYR A  395  1                                  11    
HELIX    6   6 TYR A  396  ASP A  398  5                                   3    
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 PRO B  322  GLY B  331  1                                  10    
HELIX   10  10 GLN B  336  THR B  346  1                                  11    
HELIX   11  11 ASP B  347  GLN B  351  5                                   5    
HELIX   12  12 ASP B  367  ASN B  380  1                                  14    
HELIX   13  13 ASN B  385  TYR B  395  1                                  11    
HELIX   14  14 LEU B  418  GLY B  423  1                                   6    
HELIX   15  15 THR B  425  LEU B  433  1                                   9    
SHEET    1   A 4 SER A 355  TRP A 356  0                                        
SHEET    2   A 4 GLU A 362  LYS A 364 -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   93.556  100.838   69.800  90.00  90.00  90.00 P 21 21 2     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      0.010689  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009917  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014327        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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