GenomeNet

Database: PDB
Entry: 4LG0
LinkDB: 4LG0
Original site: 4LG0 
HEADER    TRANSCRIPTION/DNA                       27-JUN-13   4LG0              
TITLE     STRUCTURE OF A TERNARY FOXO1-ETS1 DNA COMPLEX                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FORKHEAD BOX PROTEIN O1;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: DNA BINDING DOMAIN, UNP RESIDUES 143-270;                  
COMPND   5 SYNONYM: FORKHEAD BOX PROTEIN O1A, FORKHEAD IN RHABDOMYOSARCOMA;     
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PROTEIN C-ETS-1;                                           
COMPND   9 CHAIN: B;                                                            
COMPND  10 FRAGMENT: DNA BINDING DOMAIN, UNP RESIDUES 331-440;                  
COMPND  11 SYNONYM: P54;                                                        
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: DNA (5'-                                                   
COMPND  15 D(*DTP*DTP*DCP*DAP*DCP*DGP*DGP*DTP*DTP*DTP*DCP*DCP*DTP*DGP*DTP*DTP*DA
COMPND  16 P*DTP*DTP*DGP*DT)-3');                                               
COMPND  17 CHAIN: C;                                                            
COMPND  18 FRAGMENT: FOX-ETS SITE FROM VE-CADHERIN;                             
COMPND  19 ENGINEERED: YES;                                                     
COMPND  20 MOL_ID: 4;                                                           
COMPND  21 MOLECULE: DNA (5'-                                                   
COMPND  22 D(*DAP*DAP*DAP*DCP*DAP*DAP*DTP*DAP*DAP*DCP*DAP*DGP*DGP*DAP*DAP*DAP*DC
COMPND  23 P*DCP*DGP*DTP*DG)-3');                                               
COMPND  24 CHAIN: D;                                                            
COMPND  25 FRAGMENT: FOX-ETS SITE FROM VE-CADHERIN;                             
COMPND  26 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: FKHR, FOXO1, FOXO1A;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-50B;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: C-ETS-1, ETS1, EWSR2;                                          
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET-19;                                   
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 SYNTHETIC: YES;                                                      
SOURCE  23 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS.;            
SOURCE  24 MOL_ID: 4;                                                           
SOURCE  25 SYNTHETIC: YES;                                                      
SOURCE  26 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS.             
KEYWDS    DEOXYRIBONUCLEIC ACID, COMPLEX (DNA-BINDING PROTEIN-DNA),             
KEYWDS   2 PHOSPHOPROTEIN, PROTO-ONCOGENE, TRANSCRIPTION-DNA COMPLEX, WINGED    
KEYWDS   3 HELIX, FORKHEAD DOMAIN, ETS BINDING DOMAIN, HELIX-TURN-HELIX,        
KEYWDS   4 TRANSCRIPTION, TRANSCRIPTION REGULATION, DNA-BINDING,                
KEYWDS   5 PHOSPHORYLATION, NUCLEUS                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.BIRRANE,W.C.CHOY,D.DATTA,C.A.GEIGER,M.A.GRANT                       
REVDAT   1   02-JUL-14 4LG0    0                                                
JRNL        AUTH   G.BIRRANE,W.C.CHOY,D.DATTA,C.A.GEIGER,M.A.GRANT              
JRNL        TITL   STRUCTURE OF A TERNARY FOXO1-ETS1 DNA COMPLEX                
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.19 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0047                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.19                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.94                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 25814                          
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 + TEST SET) : 0.197                           
REMARK   3   R VALUE            (WORKING SET) : 0.194                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1407                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.19                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.25                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1460                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 74.89                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3060                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 76                           
REMARK   3   BIN FREE R VALUE                    : 0.3890                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1609                                    
REMARK   3   NUCLEIC ACID ATOMS       : 855                                     
REMARK   3   HETEROGEN ATOMS          : 14                                      
REMARK   3   SOLVENT ATOMS            : 70                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 49.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 79.24                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.69000                                             
REMARK   3    B22 (A**2) : -3.85000                                             
REMARK   3    B33 (A**2) : 5.54000                                              
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.181         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.174         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.156         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.355        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.927                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2695 ; 0.013 ; 0.016       
REMARK   3   BOND LENGTHS OTHERS               (A):  2106 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3812 ; 1.584 ; 1.646       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4891 ; 1.079 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   204 ; 6.502 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    82 ;36.702 ;23.415       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   311 ;14.535 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;15.152 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   358 ; 0.090 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2432 ; 0.010 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   623 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   819 ; 4.628 ; 5.282       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   818 ; 4.626 ; 5.273       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1022 ; 6.732 ; 7.874       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1023 ; 6.729 ; 7.886       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1876 ; 4.414 ; 4.988       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1876 ; 4.414 ; 4.987       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2791 ; 6.589 ; 7.376       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  3337 ;10.127 ;40.935       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  3338 ;10.125 ;40.954       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   156        A   244                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.7640  23.2270  18.2970              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2107 T22:   0.6493                                     
REMARK   3      T33:   0.1093 T12:   0.0395                                     
REMARK   3      T13:   0.0383 T23:   0.0421                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2999 L22:   0.3195                                     
REMARK   3      L33:   3.9836 L12:   0.1010                                     
REMARK   3      L13:  -0.0206 L23:  -0.9490                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1278 S12:  -0.3204 S13:  -0.0605                       
REMARK   3      S21:  -0.1677 S22:   0.2017 S23:  -0.0166                       
REMARK   3      S31:   0.1658 S32:  -0.7185 S33:  -0.0739                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   333        B   438                          
REMARK   3    ORIGIN FOR THE GROUP (A):  69.5700  24.9600  12.2310              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0287 T22:   0.5005                                     
REMARK   3      T33:   0.2764 T12:   0.0932                                     
REMARK   3      T13:   0.0463 T23:   0.1063                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5332 L22:   1.8094                                     
REMARK   3      L33:   0.7639 L12:   1.1574                                     
REMARK   3      L13:   0.0727 L23:   0.0951                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1239 S12:   0.0255 S13:  -0.0808                       
REMARK   3      S21:  -0.0554 S22:  -0.1045 S23:  -0.2970                       
REMARK   3      S31:   0.0958 S32:   0.2765 S33:   0.2284                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C    21                          
REMARK   3    ORIGIN FOR THE GROUP (A):  54.1430  16.7580  15.3440              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0896 T22:   0.3447                                     
REMARK   3      T33:   0.3176 T12:   0.1468                                     
REMARK   3      T13:   0.0652 T23:   0.0717                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6654 L22:   1.0365                                     
REMARK   3      L33:   0.8819 L12:  -1.0166                                     
REMARK   3      L13:   0.2531 L23:   0.4166                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0454 S12:   0.1004 S13:  -0.0525                       
REMARK   3      S21:   0.0398 S22:  -0.1233 S23:  -0.0047                       
REMARK   3      S31:   0.1366 S32:  -0.0261 S33:   0.0778                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     1        D    21                          
REMARK   3    ORIGIN FOR THE GROUP (A):  50.9450  21.5580  15.2030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2513 T22:   0.4834                                     
REMARK   3      T33:   0.3056 T12:   0.0389                                     
REMARK   3      T13:   0.0566 T23:   0.0220                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1521 L22:   0.0626                                     
REMARK   3      L33:   1.4295 L12:  -0.0486                                     
REMARK   3      L13:  -1.3257 L23:  -0.1043                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0466 S12:   0.1913 S13:  -0.1835                       
REMARK   3      S21:   0.0515 S22:  -0.1657 S23:   0.0626                       
REMARK   3      S31:  -0.1744 S32:   0.2840 S33:   0.2123                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4LG0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-JUL-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB080582.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-JUN-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.075,0.9793,0.979                 
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27722                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.190                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 12.000                             
REMARK 200  R MERGE                    (I) : 0.11100                            
REMARK 200  R SYM                      (I) : 0.11000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.4                               
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: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHELXS                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.64                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 400, 0.05M 2-AMINO-2-            
REMARK 280  HYDROXYMETHYL-PROPANE-1,3-DIOL, 0.1M POTASSIUM CHLORIDE, 0.01M      
REMARK 280  MAGNESIUM CHLORIDE, PH 8.5, VAPOR DIFFUSION, SITTING DROP,          
REMARK 280  TEMPERATURE 291K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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       68.16250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       68.16250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       34.32900            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       57.47200            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       34.32900            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       57.47200            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       68.16250            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       34.32900            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       57.47200            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       68.16250            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       34.32900            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       57.47200            
REMARK 290   SMTRY3   8  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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5810 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16410 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D, 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     GLY A   138                                                      
REMARK 465     PRO A   139                                                      
REMARK 465     GLY A   140                                                      
REMARK 465     TYR A   141                                                      
REMARK 465     PRO A   142                                                      
REMARK 465     GLY A   143                                                      
REMARK 465     PRO A   144                                                      
REMARK 465     LEU A   145                                                      
REMARK 465     ALA A   146                                                      
REMARK 465     GLY A   147                                                      
REMARK 465     GLN A   148                                                      
REMARK 465     PRO A   149                                                      
REMARK 465     ARG A   150                                                      
REMARK 465     LYS A   151                                                      
REMARK 465     SER A   152                                                      
REMARK 465     SER A   153                                                      
REMARK 465     SER A   154                                                      
REMARK 465     SER A   155                                                      
REMARK 465     LYS A   245                                                      
REMARK 465     SER A   246                                                      
REMARK 465     GLY A   247                                                      
REMARK 465     LYS A   248                                                      
REMARK 465     SER A   249                                                      
REMARK 465     PRO A   250                                                      
REMARK 465     ARG A   251                                                      
REMARK 465     ARG A   252                                                      
REMARK 465     ARG A   253                                                      
REMARK 465     ALA A   254                                                      
REMARK 465     ALA A   255                                                      
REMARK 465     SER A   256                                                      
REMARK 465     MET A   257                                                      
REMARK 465     ASP A   258                                                      
REMARK 465     ASN A   259                                                      
REMARK 465     ASN A   260                                                      
REMARK 465     SER A   261                                                      
REMARK 465     LYS A   262                                                      
REMARK 465     PHE A   263                                                      
REMARK 465     ALA A   264                                                      
REMARK 465     LYS A   265                                                      
REMARK 465     SER A   266                                                      
REMARK 465     ARG A   267                                                      
REMARK 465     SER A   268                                                      
REMARK 465     ARG A   269                                                      
REMARK 465     ALA A   270                                                      
REMARK 465     MET B   329                                                      
REMARK 465     GLY B   330                                                      
REMARK 465     GLY B   331                                                      
REMARK 465     SER B   332                                                      
REMARK 465     ALA B   439                                                      
REMARK 465     ASP B   440                                                      
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     DT C  19   O5' -  P   -  OP2 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500     DT D   7   C1' -  O4' -  C4' ANGL. DEV. =  -7.3 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 229      -84.65    -48.85                                   
REMARK 500    LYS A 233       78.88    135.25                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 301  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHE A 223   O                                                      
REMARK 620 2 HIS A 220   O    74.3                                              
REMARK 620 3 LEU A 217   O   100.2  87.2                                        
REMARK 620 4 HOH C 105   O   108.6 176.4  90.2                                  
REMARK 620 5 SER A 218   O   170.4  96.1  79.5  81.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 501                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3COA   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF FOXO1 DBD BOUND TO IRE DNA ELEMENT              
REMARK 900 RELATED ID: 3CO6   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF FOXO1 DBD BOUND TO DBE1 DNA                     
REMARK 900 RELATED ID: 1K79   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ETS1 DBD BOUND TO LOW (GGAG) AND HIGH           
REMARK 900 (GGAA) AFFINITY DNA                                                  
REMARK 900 RELATED ID: 2STT   RELATED DB: PDB                                   
REMARK 900 NMR STRUCTURE OF ETS1 BOUND TO DNA                                   
DBREF  4LG0 A  143   270  UNP    Q12778   FOXO1_HUMAN    143    270             
DBREF  4LG0 B  331   440  UNP    P14921   ETS1_HUMAN     331    440             
DBREF  4LG0 C    1    21  PDB    4LG0     4LG0             1     21             
DBREF  4LG0 D    1    21  PDB    4LG0     4LG0             1     21             
SEQADV 4LG0 GLY A  138  UNP  Q12778              EXPRESSION TAG                 
SEQADV 4LG0 PRO A  139  UNP  Q12778              EXPRESSION TAG                 
SEQADV 4LG0 GLY A  140  UNP  Q12778              EXPRESSION TAG                 
SEQADV 4LG0 TYR A  141  UNP  Q12778              EXPRESSION TAG                 
SEQADV 4LG0 PRO A  142  UNP  Q12778              EXPRESSION TAG                 
SEQADV 4LG0 MET B  329  UNP  P14921              EXPRESSION TAG                 
SEQADV 4LG0 GLY B  330  UNP  P14921              EXPRESSION TAG                 
SEQRES   1 A  133  GLY PRO GLY TYR PRO GLY PRO LEU ALA GLY GLN PRO ARG          
SEQRES   2 A  133  LYS SER SER SER SER ARG ARG ASN ALA TRP GLY ASN LEU          
SEQRES   3 A  133  SER TYR ALA ASP LEU ILE THR LYS ALA ILE GLU SER SER          
SEQRES   4 A  133  ALA GLU LYS ARG LEU THR LEU SER GLN ILE TYR GLU TRP          
SEQRES   5 A  133  MET VAL LYS SER VAL PRO TYR PHE LYS ASP LYS GLY ASP          
SEQRES   6 A  133  SER ASN SER SER ALA GLY TRP LYS ASN SER ILE ARG HIS          
SEQRES   7 A  133  ASN LEU SER LEU HIS SER LYS PHE ILE ARG VAL GLN ASN          
SEQRES   8 A  133  GLU GLY THR GLY LYS SER SER TRP TRP MET LEU ASN PRO          
SEQRES   9 A  133  GLU GLY GLY LYS SER GLY LYS SER PRO ARG ARG ARG ALA          
SEQRES  10 A  133  ALA SER MET ASP ASN ASN SER LYS PHE ALA LYS SER ARG          
SEQRES  11 A  133  SER ARG ALA                                                  
SEQRES   1 B  112  MET GLY GLY SER GLY PRO ILE GLN LEU TRP GLN PHE LEU          
SEQRES   2 B  112  LEU GLU LEU LEU THR ASP LYS SER CYS GLN SER PHE ILE          
SEQRES   3 B  112  SER TRP THR GLY ASP GLY TRP GLU PHE LYS LEU SER ASP          
SEQRES   4 B  112  PRO ASP GLU VAL ALA ARG ARG TRP GLY LYS ARG LYS ASN          
SEQRES   5 B  112  LYS PRO LYS MET ASN TYR GLU LYS LEU SER ARG GLY LEU          
SEQRES   6 B  112  ARG TYR TYR TYR ASP LYS ASN ILE ILE HIS LYS THR ALA          
SEQRES   7 B  112  GLY LYS ARG TYR VAL TYR ARG PHE VAL CYS ASP LEU GLN          
SEQRES   8 B  112  SER LEU LEU GLY TYR THR PRO GLU GLU LEU HIS ALA MET          
SEQRES   9 B  112  LEU ASP VAL LYS PRO ASP ALA ASP                              
SEQRES   1 C   21   DT  DT  DC  DA  DC  DG  DG  DT  DT  DT  DC  DC  DT          
SEQRES   2 C   21   DG  DT  DT  DA  DT  DT  DG  DT                              
SEQRES   1 D   21   DA  DA  DA  DC  DA  DA  DT  DA  DA  DC  DA  DG  DG          
SEQRES   2 D   21   DA  DA  DA  DC  DC  DG  DT  DG                              
HET     CA  A 301       1                                                       
HET    PG4  B 501      13                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
FORMUL   5   CA    CA 2+                                                        
FORMUL   6  PG4    C8 H18 O5                                                    
FORMUL   7  HOH   *70(H2 O)                                                     
HELIX    1   1 SER A  164  SER A  175  1                                  12    
HELIX    2   2 THR A  182  VAL A  194  1                                  13    
HELIX    3   3 PRO A  195  LYS A  200  5                                   6    
HELIX    4   4 ALA A  207  HIS A  220  1                                  14    
HELIX    5   5 GLN B  336  THR B  346  1                                  11    
HELIX    6   6 ASP B  347  GLN B  351  5                                   5    
HELIX    7   7 ASP B  367  ASN B  380  1                                  14    
HELIX    8   8 ASN B  385  TYR B  396  1                                  12    
HELIX    9   9 ASP B  417  GLY B  423  1                                   7    
HELIX   10  10 THR B  425  LEU B  433  1                                   9    
SHEET    1   A 2 PHE A 223  VAL A 226  0                                        
SHEET    2   A 2 TRP A 236  LEU A 239 -1  O  TRP A 236   N  VAL A 226           
SHEET    1   B 4 SER B 355  TRP B 356  0                                        
SHEET    2   B 4 GLU B 362  LYS B 364 -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           
LINK         O   PHE A 223                CA    CA A 301     1555   1555  2.70  
LINK         O   HIS A 220                CA    CA A 301     1555   1555  2.72  
LINK         O   LEU A 217                CA    CA A 301     1555   1555  2.74  
LINK        CA    CA A 301                 O   HOH C 105     1555   1555  2.87  
LINK         O   SER A 218                CA    CA A 301     1555   1555  3.13  
CISPEP   1 GLY A  232    LYS A  233          0        12.99                     
SITE     1 AC1  6 LEU A 217  SER A 218  HIS A 220  PHE A 223                    
SITE     2 AC1  6 HOH A 408  HOH C 105                                          
SITE     1 AC2  4 TRP B 338  VAL B 415  CYS B 416  ASP B 417                    
CRYST1   68.658  114.944  136.325  90.00  90.00  90.00 C 2 2 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      0.014565  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008700  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007335        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system