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Database: PDB
Entry: 4CO8
LinkDB: 4CO8
Original site: 4CO8 
HEADER    TRANSCRIPTION                           27-JAN-14   4CO8              
TITLE     STRUCTURE OF THE DNA BINDING ETS DOMAIN OF HUMAN ETV4                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ETS TRANSLOCATION VARIANT 4;                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: ETS DOMAIN, RESIDUES 338-470;                              
COMPND   5 SYNONYM: ADENOVIRUS E1A ENHANCER-BINDING PROTEIN, E1A-F,             
COMPND   6  POLYOMAVIRUS ENHANCER ACTIVATOR 3 HOMOLOG, PROTEIN PEA3;            
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21                                       
KEYWDS    TRANSCRIPTION                                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.A.NEWMAN,C.D.O.COOPER,L.SHRESTHA,N.BURGESS-BROWN,J.KOPEC,           
AUTHOR   2 F.VON DELFT,C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,O.GILEADI           
REVDAT   3   10-JUN-15 4CO8    1       JRNL                                     
REVDAT   2   29-APR-15 4CO8    1       JRNL                                     
REVDAT   1   05-FEB-14 4CO8    0                                                
JRNL        AUTH   C.D.O.COOPER,J.A.NEWMAN,H.AITKENHEAD,C.K.ALLERSTON,          
JRNL        AUTH 2 O.GILEADI                                                    
JRNL        TITL   STRUCTURES OF THE ETS DOMAINS OF TRANSCRIPTION FACTORS ETV1, 
JRNL        TITL 2 ETV4, ETV5 AND FEV: DETERMINANTS OF DNA BINDING AND REDOX    
JRNL        TITL 3 REGULATION BY DISULFIDE BOND FORMATION.                      
JRNL        REF    J.BIOL.CHEM.                  V. 290 13692 2015              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   25866208                                                     
JRNL        DOI    10.1074/JBC.M115.646737                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,                      
REMARK   3                 STEINER,NICHOLLS,WINN,LONG,VAGIN                     
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.99                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.46                          
REMARK   3   NUMBER OF REFLECTIONS             : 43771                          
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) : 0.11727                         
REMARK   3   R VALUE            (WORKING SET) : 0.11654                         
REMARK   3   FREE R VALUE                     : 0.13201                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.9                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 2245                            
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) : 1.050                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.077                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2316                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 69.61                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.227                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 112                          
REMARK   3   BIN FREE R VALUE                    : 0.226                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 800                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 12                                      
REMARK   3   SOLVENT ATOMS            : 117                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.559                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.22                                                 
REMARK   3    B22 (A**2) : 0.22                                                 
REMARK   3    B33 (A**2) : -0.70                                                
REMARK   3    B12 (A**2) : 0.11                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.022         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.022         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.012         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.547         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.982                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.978                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):   936 ; 0.007 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):   880 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1276 ; 1.348 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2031 ; 0.814 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   117 ; 5.462 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    47 ;34.056 ;23.830       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   160 ;12.117 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     6 ;19.917 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   129 ; 0.089 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1074 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   226 ; 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):   435 ; 1.323 ; 1.342       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   433 ; 1.321 ; 1.333       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   549 ; 1.927 ; 2.013       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):   550 ; 1.933 ; 2.015       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   501 ; 1.806 ; 1.500       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):   501 ; 1.793 ; 1.499       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):   721 ; 2.257 ; 2.175       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  1150 ; 3.545 ;11.882       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  1151 ; 3.544 ;11.894       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  1816 ; 1.340 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):    34 ;32.534 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  1870 ; 8.663 ; 5.000       
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  : NULL                                       
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          
REMARK   3   RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY                    
REMARK   4                                                                      
REMARK   4 4CO8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-JAN-14.                  
REMARK 100 THE PDBE ID CODE IS EBI-59598.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-JAN-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL (PILATUS 6M)                 
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46056                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.05                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 26.80                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.5                               
REMARK 200  DATA REDUNDANCY                : 8.8                                
REMARK 200  R MERGE                    (I) : 0.04                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.10                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 67.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.7                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.67                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.10                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4BNC                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8 M SODIUM CITRATE TRIBASIC,           
REMARK 280  0.1 M CACODYLATE PH 6.5.                                            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
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       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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       22.55333            
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       45.10667            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  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        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       45.10667            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       22.55333            
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: 2600 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.7 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -22.55333            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A2111   LIES ON A SPECIAL POSITION.                         
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   336                                                      
REMARK 465     ASN A   435                                                      
REMARK 465     GLN A   436                                                      
REMARK 465     ARG A   437                                                      
REMARK 465     PRO A   438                                                      
REMARK 465     ALA A   439                                                      
REMARK 465     LEU A   440                                                      
REMARK 465     LYS A   441                                                      
REMARK 465     ALA A   442                                                      
REMARK 465     GLU A   443                                                      
REMARK 465     PHE A   444                                                      
REMARK 465     ASP A   445                                                      
REMARK 465     ARG A   446                                                      
REMARK 465     PRO A   447                                                      
REMARK 465     VAL A   448                                                      
REMARK 465     SER A   449                                                      
REMARK 465     GLU A   450                                                      
REMARK 465     GLU A   451                                                      
REMARK 465     ASP A   452                                                      
REMARK 465     THR A   453                                                      
REMARK 465     VAL A   454                                                      
REMARK 465     PRO A   455                                                      
REMARK 465     LEU A   456                                                      
REMARK 465     SER A   457                                                      
REMARK 465     HIS A   458                                                      
REMARK 465     LEU A   459                                                      
REMARK 465     ASP A   460                                                      
REMARK 465     GLU A   461                                                      
REMARK 465     SER A   462                                                      
REMARK 465     PRO A   463                                                      
REMARK 465     ALA A   464                                                      
REMARK 465     TYR A   465                                                      
REMARK 465     LEU A   466                                                      
REMARK 465     PRO A   467                                                      
REMARK 465     GLU A   468                                                      
REMARK 465     LEU A   469                                                      
REMARK 465     ALA A   470                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 338    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 370    NZ                                                  
REMARK 470     ARG A 415    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 419    NZ                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   CE B MET A   367     SG B CYS A   422              2.20            
REMARK 500   OE1B GLU A   423     O  B HOH A  2112              2.00            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  2026     O    HOH A  2026     5554     1.47            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1435                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1436                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1437                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 FIRST TWO RESIDUES ARE REMAINING FROM CLEAVAGE OF N-                 
REMARK 999 TERMINAL HIS TAG                                                     
DBREF  4CO8 A  338   470  UNP    P43268   ETV4_HUMAN     338    470             
SEQADV 4CO8 SER A  336  UNP  P43268              EXPRESSION TAG                 
SEQADV 4CO8 MET A  337  UNP  P43268              EXPRESSION TAG                 
SEQRES   1 A  135  SER MET ARG GLY ALA LEU GLN LEU TRP GLN PHE LEU VAL          
SEQRES   2 A  135  ALA LEU LEU ASP ASP PRO THR ASN ALA HIS PHE ILE ALA          
SEQRES   3 A  135  TRP THR GLY ARG GLY MET GLU PHE LYS LEU ILE GLU PRO          
SEQRES   4 A  135  GLU GLU VAL ALA ARG LEU TRP GLY ILE GLN LYS ASN ARG          
SEQRES   5 A  135  PRO ALA MET ASN TYR ASP LYS LEU SER ARG SER LEU ARG          
SEQRES   6 A  135  TYR TYR TYR GLU LYS GLY ILE MET GLN LYS VAL ALA GLY          
SEQRES   7 A  135  GLU ARG TYR VAL TYR LYS PHE VAL CYS GLU PRO GLU ALA          
SEQRES   8 A  135  LEU PHE SER LEU ALA PHE PRO ASP ASN GLN ARG PRO ALA          
SEQRES   9 A  135  LEU LYS ALA GLU PHE ASP ARG PRO VAL SER GLU GLU ASP          
SEQRES  10 A  135  THR VAL PRO LEU SER HIS LEU ASP GLU SER PRO ALA TYR          
SEQRES  11 A  135  LEU PRO GLU LEU ALA                                          
HET    EDO  A1435       4                                                       
HET    EDO  A1436       4                                                       
HET    EDO  A1437       4                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  EDO    3(C2 H6 O2)                                                  
FORMUL   3  HOH   *117(H2 O)                                                    
HELIX    1   1 GLN A  342  ASP A  353  1                                  12    
HELIX    2   2 PRO A  354  ALA A  357  5                                   4    
HELIX    3   3 GLU A  373  ASN A  386  1                                  14    
HELIX    4   4 ASN A  391  LYS A  405  1                                  15    
HELIX    5   5 GLU A  423  PHE A  432  1                                  10    
SHEET    1  AA 4 ILE A 360  TRP A 362  0                                        
SHEET    2  AA 4 GLU A 368  LEU A 371 -1  O  LYS A 370   N  ALA A 361           
SHEET    3  AA 4 VAL A 417  PHE A 420 -1  O  TYR A 418   N  PHE A 369           
SHEET    4  AA 4 MET A 408  LYS A 410 -1  O  GLN A 409   N  LYS A 419           
SSBOND   1 CYS A  422    CYS A  422                          1555   5554  2.19  
SITE     1 AC1  7 ALA A 340  LEU A 341  TRP A 362  EDO A1437                    
SITE     2 AC1  7 HOH A2025  HOH A2039  HOH A2067                               
SITE     1 AC2  6 GLN A 342  TRP A 344  SER A 429  PRO A 433                    
SITE     2 AC2  6 HOH A2033  HOH A2034                                          
SITE     1 AC3  8 LEU A 351  ASP A 352  ARG A 387  GLU A 425                    
SITE     2 AC3  8 EDO A1435  HOH A2028  HOH A2067  HOH A2085                    
CRYST1   50.801   50.801   67.660  90.00  90.00 120.00 P 31 2 1      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      0.019685  0.011365  0.000000        0.00000                         
SCALE2      0.000000  0.022730  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014780        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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