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Database: PDB
Entry: 4UUV
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Original site: 4UUV 
HEADER    TRANSCRIPTION                           31-JUL-14   4UUV              
TITLE     STRUCTURE OF THE DNA BINDING ETS DOMAIN OF HUMAN ETV4 IN              
TITLE    2 COMPLEX WITH DNA                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ETS TRANSLOCATION VARIANT 4;                               
COMPND   3 CHAIN: A, D, G, J, M, P, S, V;                                       
COMPND   4 FRAGMENT: ETS DOMAIN, RESIDUES 338-435;                              
COMPND   5 SYNONYM: ADENOVIRUS E1A ENHANCER-BINDING PROTEIN, E1A-F,             
COMPND   6  POLYOMAVIRUS;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: 5'-D(*AP*CP*CP*GP*GP*AP*AP*GP*TP*GP)-3';                   
COMPND  10 CHAIN: B, E, H, K, N, Q, T, W;                                       
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: 5'-D(*AP*CP*TP*TP*CP*CP*GP*GP*TP*CP)-3';                   
COMPND  13 CHAIN: C, F, I, L, O, R, U;                                          
COMPND  14 MOL_ID: 4;                                                           
COMPND  15 MOLECULE: 5'-D(*AP*CP*TP*TP*CP*CP*GP*GP*TP*CP)-3';                   
COMPND  16 CHAIN: X                                                             
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;                                      
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  11 ORGANISM_TAXID: 32630;                                               
SOURCE  12 MOL_ID: 3;                                                           
SOURCE  13 SYNTHETIC: YES;                                                      
SOURCE  14 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  15 ORGANISM_TAXID: 32630;                                               
SOURCE  16 MOL_ID: 4;                                                           
SOURCE  17 SYNTHETIC: YES;                                                      
SOURCE  18 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  19 ORGANISM_TAXID: 32630                                                
KEYWDS    TRANSCRIPTION                                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.A.NEWMAN,H.AITKENHEAD,C.D.O.COOPER,L.SHRESTHA,N.BURGESS-BROWN,      
AUTHOR   2 J.KOPEC,F.VON DELFT,C.H.ARROWSMITH,C.BOUNTRA,A.M.EDWARDS,O.GILEADI   
REVDAT   3   10-JUN-15 4UUV    1       JRNL                                     
REVDAT   2   29-APR-15 4UUV    1       JRNL                                     
REVDAT   1   13-AUG-14 4UUV    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.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.970                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.34                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.61                          
REMARK   3   NUMBER OF REFLECTIONS             : 32675                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.2052                          
REMARK   3   R VALUE            (WORKING SET) : 0.2030                          
REMARK   3   FREE R VALUE                     : 0.2480                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.7                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1534                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 40.9745 -  6.2209    0.94     2971   146  0.1650 0.1833        
REMARK   3     2  6.2209 -  4.9404    0.95     2866   145  0.1830 0.2042        
REMARK   3     3  4.9404 -  4.3167    0.94     2797   128  0.1804 0.2298        
REMARK   3     4  4.3167 -  3.9223    0.94     2809   128  0.1949 0.2390        
REMARK   3     5  3.9223 -  3.6414    0.92     2732   147  0.2276 0.2640        
REMARK   3     6  3.6414 -  3.4268    0.95     2839   135  0.2266 0.3393        
REMARK   3     7  3.4268 -  3.2553    0.96     2826   144  0.2239 0.3350        
REMARK   3     8  3.2553 -  3.1136    0.97     2852   171  0.2548 0.3153        
REMARK   3     9  3.1136 -  2.9938    0.98     2932   149  0.2827 0.3383        
REMARK   3    10  2.9938 -  2.8905    0.99     2885   127  0.2888 0.3652        
REMARK   3    11  2.8905 -  2.8001    0.88     2632   114  0.3357 0.3814        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.42             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.33            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 80.38                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 78.8                           
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           9904                                  
REMARK   3   ANGLE     :  0.521          14035                                  
REMARK   3   CHIRALITY :  0.022           1485                                  
REMARK   3   PLANARITY :  0.002           1262                                  
REMARK   3   DIHEDRAL  : 21.813           3822                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4UUV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-JUL-14.                  
REMARK 100 THE PDBE ID CODE IS EBI-61425.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-JUN-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 10                                 
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                       : I24                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9686                             
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   : 32705                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.80                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.26                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.9                               
REMARK 200  DATA REDUNDANCY                : 2.5                                
REMARK 200  R MERGE                    (I) : 0.05                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.60                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.5                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.46                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.80                               
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 4UNO                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG3350, 0.2M MG CL, 0.1M BIS TRIS   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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       88.32550            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       23.06650            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       88.32550            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       23.06650            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7020 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14160 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.6 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, V, K, L, W, X                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6980 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, G, E, F, H, I                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6910 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14270 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.6 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, S, T, U, N, O                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7050 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14610 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.4 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, P, B, C, Q, R                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A   336                                                      
REMARK 465     MET A   337                                                      
REMARK 465     ARG A   338                                                      
REMARK 465     ASN A   435                                                      
REMARK 465     SER D   336                                                      
REMARK 465     MET D   337                                                      
REMARK 465     ARG D   338                                                      
REMARK 465     GLY D   339                                                      
REMARK 465     ASN D   435                                                      
REMARK 465     SER G   336                                                      
REMARK 465     MET G   337                                                      
REMARK 465     ARG G   338                                                      
REMARK 465     GLY G   339                                                      
REMARK 465     ASN G   435                                                      
REMARK 465     SER J   336                                                      
REMARK 465     MET J   337                                                      
REMARK 465     ARG J   338                                                      
REMARK 465     GLY J   339                                                      
REMARK 465     ALA J   340                                                      
REMARK 465     ASN J   435                                                      
REMARK 465     SER M   336                                                      
REMARK 465     MET M   337                                                      
REMARK 465     ARG M   338                                                      
REMARK 465     GLY M   339                                                      
REMARK 465     ALA M   340                                                      
REMARK 465     ASN M   435                                                      
REMARK 465     SER P   336                                                      
REMARK 465     MET P   337                                                      
REMARK 465     ARG P   338                                                      
REMARK 465     ASN P   435                                                      
REMARK 465     SER S   336                                                      
REMARK 465     MET S   337                                                      
REMARK 465     ARG S   338                                                      
REMARK 465     GLY S   339                                                      
REMARK 465     ASN S   435                                                      
REMARK 465     SER V   336                                                      
REMARK 465     MET V   337                                                      
REMARK 465     ARG V   338                                                      
REMARK 465     GLY V   339                                                      
REMARK 465     ALA V   340                                                      
REMARK 465     ASN V   435                                                      
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      DC C  11    C5'  C4'  O4'  C3'  C2'  C1'  N1   C2               
REMARK 470      DC C  11    O2   N3   C4   N4   C5   C6                         
REMARK 470     ARG D 365    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 373    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 394    CG   CD   CE   NZ                                   
REMARK 470      DG E  10    C5'  C4'  O4'  C3'  C2'  C1'  N9   C8               
REMARK 470      DG E  10    N7   C5   C6   O6   N1   C2   N2   N3               
REMARK 470      DG E  10    C4                                                  
REMARK 470     ARG G 387    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG G 415    CD   NE   CZ   NH1  NH2                             
REMARK 470      DC I  10    C5'  C4'  O4'  C3'  C2'  C1'  N1   C2               
REMARK 470      DC I  10    O2   N3   C4   N4   C5   C6                         
REMARK 470      DG K  10    C5'  C4'  O4'  C3'  C2'  C1'  N9   C8               
REMARK 470      DG K  10    N7   C5   C6   O6   N1   C2   N2   N3               
REMARK 470      DG K  10    C4                                                  
REMARK 470      DC L  10    C5'  C4'  O4'  C3'  C2'  C1'  N1   C2               
REMARK 470      DC L  10    O2   N3   C4   N4   C5   C6                         
REMARK 470     ARG M 387    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470      DG N  10    C5'  C4'  O4'  C3'  C2'  C1'  N9   C8               
REMARK 470      DG N  10    N7   C5   C6   O6   N1   C2   N2   N3               
REMARK 470      DG N  10    C4                                                  
REMARK 470      DC O  10    C5'  C4'  O4'  C3'  C2'  C1'  N1   C2               
REMARK 470      DC O  10    O2   N3   C4   N4   C5   C6                         
REMARK 470     ASN S 386    CG   OD1  ND2                                       
REMARK 470     ARG V 365    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS V 370    CG   CD   CE   NZ                                   
REMARK 470     GLU V 373    CG   CD   OE1  OE2                                  
REMARK 470     LYS V 394    CG   CD   CE   NZ                                   
REMARK 470     GLU V 404    CG   CD   OE1  OE2                                  
REMARK 470     LYS V 405    CG   CD   CE   NZ                                   
REMARK 470     LYS V 410    CG   CD   CE   NZ                                   
REMARK 470      DG X  10    C5'  C4'  O4'  C3'  C2'  C1'  N9   C8   N7   C5   C6
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500     DG H  10   O3' -  P   -  OP1 ANGL. DEV. =   7.2 DEGREES          
REMARK 500     DG H  10   O3' -  P   -  OP2 ANGL. DEV. =   7.2 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    ALA A 340       83.63   -156.36                                   
REMARK 500    MET A 367       41.99    -93.87                                   
REMARK 500    PHE D 359      -13.70   -148.52                                   
REMARK 500    MET D 367       57.66    -95.12                                   
REMARK 500    ALA D 389       36.38    -88.40                                   
REMARK 500    CYS D 422       55.73    -98.50                                   
REMARK 500    PHE G 359       -6.67   -141.98                                   
REMARK 500    ALA G 389       59.38    -99.28                                   
REMARK 500    CYS G 422       68.24   -100.69                                   
REMARK 500    ASP M 352       31.89    -97.76                                   
REMARK 500    VAL M 411       97.92    -65.28                                   
REMARK 500    PHE P 359       -6.48   -150.29                                   
REMARK 500    ALA P 389       54.01   -106.11                                   
REMARK 500    MET S 367       54.80    -90.73                                   
REMARK 500    CYS S 422       71.55   -101.12                                   
REMARK 500    MET V 367       57.09   -107.44                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 FIRST 2 RESIDUES REMAIN AFTER CLEAVAGE OF PURIFICATION TAG           
DBREF  4UUV A  338   435  UNP    P43268   ETV4_HUMAN     338    435             
DBREF  4UUV D  338   435  UNP    P43268   ETV4_HUMAN     338    435             
DBREF  4UUV G  338   435  UNP    P43268   ETV4_HUMAN     338    435             
DBREF  4UUV J  338   435  UNP    P43268   ETV4_HUMAN     338    435             
DBREF  4UUV M  338   435  UNP    P43268   ETV4_HUMAN     338    435             
DBREF  4UUV P  338   435  UNP    P43268   ETV4_HUMAN     338    435             
DBREF  4UUV S  338   435  UNP    P43268   ETV4_HUMAN     338    435             
DBREF  4UUV V  338   435  UNP    P43268   ETV4_HUMAN     338    435             
DBREF  4UUV B    1    10  PDB    4UUV     4UUV             1     10             
DBREF  4UUV C    2    11  PDB    4UUV     4UUV             2     11             
DBREF  4UUV E    1    10  PDB    4UUV     4UUV             1     10             
DBREF  4UUV F    1    10  PDB    4UUV     4UUV             1     10             
DBREF  4UUV H    1    10  PDB    4UUV     4UUV             1     10             
DBREF  4UUV I    1    10  PDB    4UUV     4UUV             1     10             
DBREF  4UUV K    1    10  PDB    4UUV     4UUV             1     10             
DBREF  4UUV L    1    10  PDB    4UUV     4UUV             1     10             
DBREF  4UUV N    1    10  PDB    4UUV     4UUV             1     10             
DBREF  4UUV O    1    10  PDB    4UUV     4UUV             1     10             
DBREF  4UUV Q    1    10  PDB    4UUV     4UUV             1     10             
DBREF  4UUV R    1    10  PDB    4UUV     4UUV             1     10             
DBREF  4UUV T    1    10  PDB    4UUV     4UUV             1     10             
DBREF  4UUV U    1    10  PDB    4UUV     4UUV             1     10             
DBREF  4UUV W    1    10  PDB    4UUV     4UUV             1     10             
DBREF  4UUV X    1    10  PDB    4UUV     4UUV             1     10             
SEQADV 4UUV SER A  336  UNP  P43268              EXPRESSION TAG                 
SEQADV 4UUV MET A  337  UNP  P43268              EXPRESSION TAG                 
SEQADV 4UUV SER D  336  UNP  P43268              EXPRESSION TAG                 
SEQADV 4UUV MET D  337  UNP  P43268              EXPRESSION TAG                 
SEQADV 4UUV SER G  336  UNP  P43268              EXPRESSION TAG                 
SEQADV 4UUV MET G  337  UNP  P43268              EXPRESSION TAG                 
SEQADV 4UUV SER J  336  UNP  P43268              EXPRESSION TAG                 
SEQADV 4UUV MET J  337  UNP  P43268              EXPRESSION TAG                 
SEQADV 4UUV SER M  336  UNP  P43268              EXPRESSION TAG                 
SEQADV 4UUV MET M  337  UNP  P43268              EXPRESSION TAG                 
SEQADV 4UUV SER P  336  UNP  P43268              EXPRESSION TAG                 
SEQADV 4UUV MET P  337  UNP  P43268              EXPRESSION TAG                 
SEQADV 4UUV SER S  336  UNP  P43268              EXPRESSION TAG                 
SEQADV 4UUV MET S  337  UNP  P43268              EXPRESSION TAG                 
SEQADV 4UUV SER V  336  UNP  P43268              EXPRESSION TAG                 
SEQADV 4UUV MET V  337  UNP  P43268              EXPRESSION TAG                 
SEQRES   1 A  100  SER MET ARG GLY ALA LEU GLN LEU TRP GLN PHE LEU VAL          
SEQRES   2 A  100  ALA LEU LEU ASP ASP PRO THR ASN ALA HIS PHE ILE ALA          
SEQRES   3 A  100  TRP THR GLY ARG GLY MET GLU PHE LYS LEU ILE GLU PRO          
SEQRES   4 A  100  GLU GLU VAL ALA ARG LEU TRP GLY ILE GLN LYS ASN ARG          
SEQRES   5 A  100  PRO ALA MET ASN TYR ASP LYS LEU SER ARG SER LEU ARG          
SEQRES   6 A  100  TYR TYR TYR GLU LYS GLY ILE MET GLN LYS VAL ALA GLY          
SEQRES   7 A  100  GLU ARG TYR VAL TYR LYS PHE VAL CYS GLU PRO ASP ALA          
SEQRES   8 A  100  LEU PHE SER MET ALA PHE PRO ASP ASN                          
SEQRES   1 D  100  SER MET ARG GLY ALA LEU GLN LEU TRP GLN PHE LEU VAL          
SEQRES   2 D  100  ALA LEU LEU ASP ASP PRO THR ASN ALA HIS PHE ILE ALA          
SEQRES   3 D  100  TRP THR GLY ARG GLY MET GLU PHE LYS LEU ILE GLU PRO          
SEQRES   4 D  100  GLU GLU VAL ALA ARG LEU TRP GLY ILE GLN LYS ASN ARG          
SEQRES   5 D  100  PRO ALA MET ASN TYR ASP LYS LEU SER ARG SER LEU ARG          
SEQRES   6 D  100  TYR TYR TYR GLU LYS GLY ILE MET GLN LYS VAL ALA GLY          
SEQRES   7 D  100  GLU ARG TYR VAL TYR LYS PHE VAL CYS GLU PRO ASP ALA          
SEQRES   8 D  100  LEU PHE SER MET ALA PHE PRO ASP ASN                          
SEQRES   1 G  100  SER MET ARG GLY ALA LEU GLN LEU TRP GLN PHE LEU VAL          
SEQRES   2 G  100  ALA LEU LEU ASP ASP PRO THR ASN ALA HIS PHE ILE ALA          
SEQRES   3 G  100  TRP THR GLY ARG GLY MET GLU PHE LYS LEU ILE GLU PRO          
SEQRES   4 G  100  GLU GLU VAL ALA ARG LEU TRP GLY ILE GLN LYS ASN ARG          
SEQRES   5 G  100  PRO ALA MET ASN TYR ASP LYS LEU SER ARG SER LEU ARG          
SEQRES   6 G  100  TYR TYR TYR GLU LYS GLY ILE MET GLN LYS VAL ALA GLY          
SEQRES   7 G  100  GLU ARG TYR VAL TYR LYS PHE VAL CYS GLU PRO ASP ALA          
SEQRES   8 G  100  LEU PHE SER MET ALA PHE PRO ASP ASN                          
SEQRES   1 J  100  SER MET ARG GLY ALA LEU GLN LEU TRP GLN PHE LEU VAL          
SEQRES   2 J  100  ALA LEU LEU ASP ASP PRO THR ASN ALA HIS PHE ILE ALA          
SEQRES   3 J  100  TRP THR GLY ARG GLY MET GLU PHE LYS LEU ILE GLU PRO          
SEQRES   4 J  100  GLU GLU VAL ALA ARG LEU TRP GLY ILE GLN LYS ASN ARG          
SEQRES   5 J  100  PRO ALA MET ASN TYR ASP LYS LEU SER ARG SER LEU ARG          
SEQRES   6 J  100  TYR TYR TYR GLU LYS GLY ILE MET GLN LYS VAL ALA GLY          
SEQRES   7 J  100  GLU ARG TYR VAL TYR LYS PHE VAL CYS GLU PRO ASP ALA          
SEQRES   8 J  100  LEU PHE SER MET ALA PHE PRO ASP ASN                          
SEQRES   1 M  100  SER MET ARG GLY ALA LEU GLN LEU TRP GLN PHE LEU VAL          
SEQRES   2 M  100  ALA LEU LEU ASP ASP PRO THR ASN ALA HIS PHE ILE ALA          
SEQRES   3 M  100  TRP THR GLY ARG GLY MET GLU PHE LYS LEU ILE GLU PRO          
SEQRES   4 M  100  GLU GLU VAL ALA ARG LEU TRP GLY ILE GLN LYS ASN ARG          
SEQRES   5 M  100  PRO ALA MET ASN TYR ASP LYS LEU SER ARG SER LEU ARG          
SEQRES   6 M  100  TYR TYR TYR GLU LYS GLY ILE MET GLN LYS VAL ALA GLY          
SEQRES   7 M  100  GLU ARG TYR VAL TYR LYS PHE VAL CYS GLU PRO ASP ALA          
SEQRES   8 M  100  LEU PHE SER MET ALA PHE PRO ASP ASN                          
SEQRES   1 P  100  SER MET ARG GLY ALA LEU GLN LEU TRP GLN PHE LEU VAL          
SEQRES   2 P  100  ALA LEU LEU ASP ASP PRO THR ASN ALA HIS PHE ILE ALA          
SEQRES   3 P  100  TRP THR GLY ARG GLY MET GLU PHE LYS LEU ILE GLU PRO          
SEQRES   4 P  100  GLU GLU VAL ALA ARG LEU TRP GLY ILE GLN LYS ASN ARG          
SEQRES   5 P  100  PRO ALA MET ASN TYR ASP LYS LEU SER ARG SER LEU ARG          
SEQRES   6 P  100  TYR TYR TYR GLU LYS GLY ILE MET GLN LYS VAL ALA GLY          
SEQRES   7 P  100  GLU ARG TYR VAL TYR LYS PHE VAL CYS GLU PRO ASP ALA          
SEQRES   8 P  100  LEU PHE SER MET ALA PHE PRO ASP ASN                          
SEQRES   1 S  100  SER MET ARG GLY ALA LEU GLN LEU TRP GLN PHE LEU VAL          
SEQRES   2 S  100  ALA LEU LEU ASP ASP PRO THR ASN ALA HIS PHE ILE ALA          
SEQRES   3 S  100  TRP THR GLY ARG GLY MET GLU PHE LYS LEU ILE GLU PRO          
SEQRES   4 S  100  GLU GLU VAL ALA ARG LEU TRP GLY ILE GLN LYS ASN ARG          
SEQRES   5 S  100  PRO ALA MET ASN TYR ASP LYS LEU SER ARG SER LEU ARG          
SEQRES   6 S  100  TYR TYR TYR GLU LYS GLY ILE MET GLN LYS VAL ALA GLY          
SEQRES   7 S  100  GLU ARG TYR VAL TYR LYS PHE VAL CYS GLU PRO ASP ALA          
SEQRES   8 S  100  LEU PHE SER MET ALA PHE PRO ASP ASN                          
SEQRES   1 V  100  SER MET ARG GLY ALA LEU GLN LEU TRP GLN PHE LEU VAL          
SEQRES   2 V  100  ALA LEU LEU ASP ASP PRO THR ASN ALA HIS PHE ILE ALA          
SEQRES   3 V  100  TRP THR GLY ARG GLY MET GLU PHE LYS LEU ILE GLU PRO          
SEQRES   4 V  100  GLU GLU VAL ALA ARG LEU TRP GLY ILE GLN LYS ASN ARG          
SEQRES   5 V  100  PRO ALA MET ASN TYR ASP LYS LEU SER ARG SER LEU ARG          
SEQRES   6 V  100  TYR TYR TYR GLU LYS GLY ILE MET GLN LYS VAL ALA GLY          
SEQRES   7 V  100  GLU ARG TYR VAL TYR LYS PHE VAL CYS GLU PRO ASP ALA          
SEQRES   8 V  100  LEU PHE SER MET ALA PHE PRO ASP ASN                          
SEQRES   1 B   10   DA  DC  DC  DG  DG  DA  DA  DG  DT  DG                      
SEQRES   1 C   10   DA  DC  DT  DT  DC  DC  DG  DG  DT  DC                      
SEQRES   1 E   10   DA  DC  DC  DG  DG  DA  DA  DG  DT  DG                      
SEQRES   1 F   10   DA  DC  DT  DT  DC  DC  DG  DG  DT  DC                      
SEQRES   1 H   10   DA  DC  DC  DG  DG  DA  DA  DG  DT  DG                      
SEQRES   1 I   10   DA  DC  DT  DT  DC  DC  DG  DG  DT  DC                      
SEQRES   1 K   10   DA  DC  DC  DG  DG  DA  DA  DG  DT  DG                      
SEQRES   1 L   10   DA  DC  DT  DT  DC  DC  DG  DG  DT  DC                      
SEQRES   1 N   10   DA  DC  DC  DG  DG  DA  DA  DG  DT  DG                      
SEQRES   1 O   10   DA  DC  DT  DT  DC  DC  DG  DG  DT  DC                      
SEQRES   1 Q   10   DA  DC  DC  DG  DG  DA  DA  DG  DT  DG                      
SEQRES   1 R   10   DA  DC  DT  DT  DC  DC  DG  DG  DT  DC                      
SEQRES   1 T   10   DA  DC  DC  DG  DG  DA  DA  DG  DT  DG                      
SEQRES   1 U   10   DA  DC  DT  DT  DC  DC  DG  DG  DT  DC                      
SEQRES   1 W   10   DA  DC  DC  DG  DG  DA  DA  DG  DT  DG                      
SEQRES   1 X   10   DA  DC  DT  DT  DC  DC  DG  DG  DT  DG                      
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  LYS A  385  1                                  13    
HELIX    4   4 ASN A  391  LYS A  405  1                                  15    
HELIX    5   5 GLU A  423  PHE A  432  1                                  10    
HELIX    6   6 GLN D  342  ASP D  353  1                                  12    
HELIX    7   7 PRO D  354  ALA D  357  5                                   4    
HELIX    8   8 GLU D  373  LYS D  385  1                                  13    
HELIX    9   9 ASN D  391  LYS D  405  1                                  15    
HELIX   10  10 GLU D  423  PHE D  432  1                                  10    
HELIX   11  11 GLN G  342  ASP G  353  1                                  12    
HELIX   12  12 PRO G  354  ALA G  357  5                                   4    
HELIX   13  13 GLU G  373  LYS G  385  1                                  13    
HELIX   14  14 ASN G  391  LYS G  405  1                                  15    
HELIX   15  15 GLU G  423  PHE G  432  1                                  10    
HELIX   16  16 GLN J  342  ASP J  353  1                                  12    
HELIX   17  17 PRO J  354  ALA J  357  5                                   4    
HELIX   18  18 GLU J  373  LYS J  385  1                                  13    
HELIX   19  19 ASN J  391  LYS J  405  1                                  15    
HELIX   20  20 GLU J  423  PHE J  432  1                                  10    
HELIX   21  21 GLN M  342  ASP M  352  1                                  11    
HELIX   22  22 ASP M  353  ALA M  357  5                                   5    
HELIX   23  23 GLU M  373  LYS M  385  1                                  13    
HELIX   24  24 ASN M  391  LYS M  405  1                                  15    
HELIX   25  25 GLU M  423  PHE M  432  1                                  10    
HELIX   26  26 GLN P  342  ASP P  353  1                                  12    
HELIX   27  27 PRO P  354  ALA P  357  5                                   4    
HELIX   28  28 GLU P  373  LYS P  385  1                                  13    
HELIX   29  29 ASN P  391  GLY P  406  1                                  16    
HELIX   30  30 GLU P  423  PHE P  432  1                                  10    
HELIX   31  31 GLN S  342  ASP S  352  1                                  11    
HELIX   32  32 ASP S  353  ALA S  357  5                                   5    
HELIX   33  33 GLU S  373  LYS S  385  1                                  13    
HELIX   34  34 ASN S  391  LYS S  405  1                                  15    
HELIX   35  35 GLU S  423  PHE S  432  1                                  10    
HELIX   36  36 GLN V  342  ASP V  353  1                                  12    
HELIX   37  37 PRO V  354  ALA V  357  5                                   4    
HELIX   38  38 GLU V  373  LYS V  385  1                                  13    
HELIX   39  39 ASN V  391  TYR V  402  1                                  12    
HELIX   40  40 GLU V  423  PHE V  432  1                                  10    
SHEET    1  AA 4 ALA A 361  TRP A 362  0                                        
SHEET    2  AA 4 GLU A 368  LYS A 370 -1  N  LYS A 370   O  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           
SHEET    1  DA 4 ALA D 361  TRP D 362  0                                        
SHEET    2  DA 4 GLU D 368  LYS D 370 -1  O  LYS D 370   N  ALA D 361           
SHEET    3  DA 4 VAL D 417  PHE D 420 -1  O  TYR D 418   N  PHE D 369           
SHEET    4  DA 4 MET D 408  LYS D 410 -1  O  GLN D 409   N  LYS D 419           
SHEET    1  GA 4 ALA G 361  TRP G 362  0                                        
SHEET    2  GA 4 GLU G 368  LYS G 370 -1  N  LYS G 370   O  ALA G 361           
SHEET    3  GA 4 VAL G 417  PHE G 420 -1  O  TYR G 418   N  PHE G 369           
SHEET    4  GA 4 MET G 408  LYS G 410 -1  O  GLN G 409   N  LYS G 419           
SHEET    1  JA 4 ALA J 361  TRP J 362  0                                        
SHEET    2  JA 4 GLU J 368  LYS J 370 -1  O  LYS J 370   N  ALA J 361           
SHEET    3  JA 4 VAL J 417  PHE J 420 -1  O  TYR J 418   N  PHE J 369           
SHEET    4  JA 4 MET J 408  LYS J 410 -1  O  GLN J 409   N  LYS J 419           
SHEET    1  MA 4 ALA M 361  TRP M 362  0                                        
SHEET    2  MA 4 GLU M 368  LYS M 370 -1  O  LYS M 370   N  ALA M 361           
SHEET    3  MA 4 VAL M 417  PHE M 420 -1  O  TYR M 418   N  PHE M 369           
SHEET    4  MA 4 MET M 408  LYS M 410 -1  O  GLN M 409   N  LYS M 419           
SHEET    1  PA 4 ALA P 361  TRP P 362  0                                        
SHEET    2  PA 4 GLU P 368  LYS P 370 -1  O  LYS P 370   N  ALA P 361           
SHEET    3  PA 4 VAL P 417  PHE P 420 -1  O  TYR P 418   N  PHE P 369           
SHEET    4  PA 4 MET P 408  LYS P 410 -1  O  GLN P 409   N  LYS P 419           
SHEET    1  SA 4 ALA S 361  TRP S 362  0                                        
SHEET    2  SA 4 GLU S 368  LYS S 370 -1  O  LYS S 370   N  ALA S 361           
SHEET    3  SA 4 VAL S 417  PHE S 420 -1  O  TYR S 418   N  PHE S 369           
SHEET    4  SA 4 MET S 408  LYS S 410 -1  O  GLN S 409   N  LYS S 419           
SHEET    1  VA 4 ALA V 361  TRP V 362  0                                        
SHEET    2  VA 4 GLU V 368  LYS V 370 -1  O  LYS V 370   N  ALA V 361           
SHEET    3  VA 4 VAL V 417  PHE V 420 -1  O  TYR V 418   N  PHE V 369           
SHEET    4  VA 4 MET V 408  LYS V 410 -1  O  GLN V 409   N  LYS V 419           
SSBOND   1 CYS A  422    CYS P  422                          1555   1555  2.03  
SSBOND   2 CYS D  422    CYS G  422                          1555   1555  2.03  
SSBOND   3 CYS J  422    CYS V  422                          1555   1555  2.03  
SSBOND   4 CYS M  422    CYS S  422                          1555   1555  2.03  
CRYST1  176.651   46.133  171.150  90.00  96.69  90.00 C 1 2 1      32          
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      0.005661  0.000000  0.000664        0.00000                         
SCALE2      0.000000  0.021676  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005883        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system