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Database: PDB
Entry: 3US0
LinkDB: 3US0
Original site: 3US0 
HEADER    TRANSCRIPTION ACTIVATOR/DNA             22-NOV-11   3US0              
TITLE     STRUCTURE OF P63 DNA BINDING DOMAIN IN COMPLEX WITH A 22 BASE PAIR A/T
TITLE    2 RICH RESPONSE ELEMENT CONTAINING A TWO BASE PAIR "AT" SPACER BETWEEN 
TITLE    3 HALF SITES                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TUMOR PROTEIN 63;                                          
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: DNA BINDING DOMAIN (UNP RESIDUES 166-362);                 
COMPND   5 SYNONYM: TP63, P63, CHRONIC ULCERATIVE STOMATITIS PROTEIN, CUSP,     
COMPND   6 KERATINOCYTE TRANSCRIPTION FACTOR KET, TRANSFORMATION-RELATED PROTEIN
COMPND   7 63, TUMOR PROTEIN P73-LIKE, P73L, P40, P51;                          
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: 5'-D(*AP*AP*AP*CP*AP*TP*GP*TP*TP*TP*AP*TP*AP*AP*AP*CP*AP*TP
COMPND  11 *GP*TP*TP*T)-3';                                                     
COMPND  12 CHAIN: E, F;                                                         
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 OTHER_DETAILS: P63 RESPONSE ELEMENT WITH AT SPACER                   
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: KET, P63, P73H, P73L, TP63, TP73L;                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2(DE3);                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-28A;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES                                                       
KEYWDS    B-DNA DOUBLE HELIX, ZINC BINDING, BETA SANDWICH, GREEK KEY,           
KEYWDS   2 TRANSCRIPTION FACTOR, NUCLEUS, TRANSCRIPTION ACTIVATOR-DNA COMPLEX   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.CHEN,O.HERZBERG                                                     
REVDAT   4   13-SEP-23 3US0    1       REMARK SEQADV LINK                       
REVDAT   3   08-NOV-17 3US0    1       REMARK                                   
REVDAT   2   21-MAR-12 3US0    1       JRNL                                     
REVDAT   1   01-FEB-12 3US0    0                                                
JRNL        AUTH   C.CHEN,N.GORLATOVA,O.HERZBERG                                
JRNL        TITL   PLIABLE DNA CONFORMATION OF RESPONSE ELEMENTS BOUND TO       
JRNL        TITL 2 TRANSCRIPTION FACTOR P63.                                    
JRNL        REF    J.BIOL.CHEM.                  V. 287  7477 2012              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   22247550                                                     
JRNL        DOI    10.1074/JBC.M111.315820                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7_650)                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 59.80                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.500                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 47224                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.208                           
REMARK   3   R VALUE            (WORKING SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.130                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2424                            
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 59.8191 -  6.4257    1.00     2700   146  0.1705 0.2178        
REMARK   3     2  6.4257 -  5.1012    1.00     2650   158  0.1497 0.1852        
REMARK   3     3  5.1012 -  4.4566    1.00     2646   147  0.1389 0.1712        
REMARK   3     4  4.4566 -  4.0492    1.00     2633   137  0.1525 0.1748        
REMARK   3     5  4.0492 -  3.7590    1.00     2659   132  0.1879 0.2116        
REMARK   3     6  3.7590 -  3.5374    1.00     2627   143  0.2002 0.2144        
REMARK   3     7  3.5374 -  3.3603    1.00     2634   144  0.2186 0.2782        
REMARK   3     8  3.3603 -  3.2140    1.00     2654   114  0.1862 0.2188        
REMARK   3     9  3.2140 -  3.0903    1.00     2609   140  0.2286 0.2480        
REMARK   3    10  3.0903 -  2.9837    1.00     2623   155  0.2577 0.2958        
REMARK   3    11  2.9837 -  2.8904    1.00     2631   144  0.2856 0.3286        
REMARK   3    12  2.8904 -  2.8078    1.00     2629   145  0.3044 0.2826        
REMARK   3    13  2.8078 -  2.7338    1.00     2614   136  0.3297 0.3569        
REMARK   3    14  2.7338 -  2.6671    1.00     2647   155  0.3430 0.4028        
REMARK   3    15  2.6671 -  2.6065    1.00     2603   144  0.3564 0.3833        
REMARK   3    16  2.6065 -  2.5510    1.00     2648   132  0.3585 0.3865        
REMARK   3    17  2.5510 -  2.5000    1.00     2593   152  0.3841 0.4090        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.00                                          
REMARK   3   SHRINKAGE RADIUS   : 0.72                                          
REMARK   3   K_SOL              : 0.28                                          
REMARK   3   B_SOL              : 44.18                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.390            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.660           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 50.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 8.46190                                              
REMARK   3    B22 (A**2) : 8.46190                                              
REMARK   3    B33 (A**2) : -16.92370                                            
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  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      :  0.011           7136                                  
REMARK   3   ANGLE     :  1.643           9894                                  
REMARK   3   CHIRALITY :  0.102           1105                                  
REMARK   3   PLANARITY :  0.007           1151                                  
REMARK   3   DIHEDRAL  : 20.344           2741                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -59.5023   6.3936  22.6970              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4795 T22:   0.3339                                     
REMARK   3      T33:   0.3942 T12:   0.0834                                     
REMARK   3      T13:  -0.0829 T23:  -0.0112                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3233 L22:   1.9618                                     
REMARK   3      L33:   1.0346 L12:  -0.7895                                     
REMARK   3      L13:  -0.4857 L23:   1.2166                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1244 S12:   0.1673 S13:   0.0185                       
REMARK   3      S21:  -0.4610 S22:  -0.2554 S23:   0.1854                       
REMARK   3      S31:  -0.4676 S32:  -0.2446 S33:  -0.0096                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -49.0776 -19.9373 -10.3005              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3867 T22:   0.3590                                     
REMARK   3      T33:   0.3896 T12:   0.0565                                     
REMARK   3      T13:  -0.0216 T23:  -0.0058                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9242 L22:   1.3274                                     
REMARK   3      L33:   1.7992 L12:  -0.3418                                     
REMARK   3      L13:  -0.1141 L23:   0.5051                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0782 S12:   0.1531 S13:  -0.0466                       
REMARK   3      S21:  -0.2589 S22:  -0.2435 S23:   0.0165                       
REMARK   3      S31:  -0.2100 S32:  -0.0858 S33:   0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN C                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -57.3275  20.3927 -43.4989              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5143 T22:   0.6061                                     
REMARK   3      T33:   0.5374 T12:  -0.1772                                     
REMARK   3      T13:   0.1144 T23:  -0.0737                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2189 L22:   0.5266                                     
REMARK   3      L33:   0.4326 L12:   0.7979                                     
REMARK   3      L13:   0.2527 L23:   0.2818                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3692 S12:  -0.5754 S13:   0.1146                       
REMARK   3      S21:   0.4752 S22:  -0.3367 S23:   0.3738                       
REMARK   3      S31:   0.1902 S32:  -0.3664 S33:   0.0715                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN D                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -36.2543  39.5497 -10.1073              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5069 T22:   0.4718                                     
REMARK   3      T33:   0.3283 T12:  -0.1331                                     
REMARK   3      T13:   0.0436 T23:  -0.0161                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0813 L22:   1.2884                                     
REMARK   3      L33:   1.1955 L12:   0.4056                                     
REMARK   3      L13:   0.1126 L23:   0.6055                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2012 S12:  -0.3891 S13:   0.0031                       
REMARK   3      S21:   0.4466 S22:  -0.3031 S23:  -0.0032                       
REMARK   3      S31:   0.2986 S32:  -0.2738 S33:  -0.0011                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN E OR CHAIN F                                     
REMARK   3    ORIGIN FOR THE GROUP (A): -36.4120   8.2543 -10.1442              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8691 T22:   0.5263                                     
REMARK   3      T33:   0.3928 T12:  -0.1412                                     
REMARK   3      T13:   0.0320 T23:   0.0815                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.3125 L22:   1.3089                                     
REMARK   3      L33:   1.4612 L12:   0.4698                                     
REMARK   3      L13:  -0.8458 L23:  -2.9506                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0855 S12:   0.0026 S13:  -0.0516                       
REMARK   3      S21:  -0.1963 S22:  -0.0042 S23:  -0.0275                       
REMARK   3      S31:   0.2337 S32:   0.6154 S33:   0.0503                       
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 3US0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-NOV-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000069136.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-NOV-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.03320357                         
REMARK 200  MONOCHROMATOR                  : SI(111) CHANNEL                    
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 47258                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.500                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 12.80                              
REMARK 200  R MERGE                    (I) : 0.08200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.56                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.45100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.500                              
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 3QYN                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.07                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG3350, 0.2 M AMMONIUM ACETATE,     
REMARK 280  0.1 M BIS-TRIS, PH 6.8, VAPOR DIFFUSION, HANGING DROP,              
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,Z+1/2                                             
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        0.00000            
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        0.00000            
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       59.80200            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       59.80200            
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       59.80200            
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: HEXAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F                      
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   121                                                      
REMARK 465     SER A   122                                                      
REMARK 465     HIS A   123                                                      
REMARK 465     MET A   124                                                      
REMARK 465     ALA A   125                                                      
REMARK 465     ARG A   321                                                      
REMARK 465     LYS A   322                                                      
REMARK 465     GLN A   323                                                      
REMARK 465     GLY B   121                                                      
REMARK 465     SER B   122                                                      
REMARK 465     HIS B   123                                                      
REMARK 465     GLN B   144                                                      
REMARK 465     SER B   145                                                      
REMARK 465     SER B   146                                                      
REMARK 465     THR B   147                                                      
REMARK 465     ALA B   148                                                      
REMARK 465     LYS B   149                                                      
REMARK 465     GLN B   323                                                      
REMARK 465     GLY C   121                                                      
REMARK 465     SER C   122                                                      
REMARK 465     HIS C   123                                                      
REMARK 465     MET C   124                                                      
REMARK 465     ARG C   321                                                      
REMARK 465     LYS C   322                                                      
REMARK 465     GLN C   323                                                      
REMARK 465     GLY D   121                                                      
REMARK 465     SER D   122                                                      
REMARK 465     HIS D   123                                                      
REMARK 465     GLN D   144                                                      
REMARK 465     SER D   145                                                      
REMARK 465     SER D   146                                                      
REMARK 465     THR D   147                                                      
REMARK 465     ALA D   148                                                      
REMARK 465     LYS D   149                                                      
REMARK 465     SER D   150                                                      
REMARK 465     GLN D   323                                                      
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     LYS A 149    CE   NZ                                             
REMARK 470     LYS A 160    CD   CE   NZ                                        
REMARK 470     GLN A 182    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 194    CD   CE   NZ                                        
REMARK 470     GLU A 216    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 219    CG1  CD1                                            
REMARK 470     LYS A 314    CE   NZ                                             
REMARK 470     GLN B 182    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 212    NE   CZ   NH1  NH2                                  
REMARK 470     ILE B 219    CG1  CD1                                            
REMARK 470     GLN B 294    CD   OE1  NE2                                       
REMARK 470     LYS B 314    CG   CD   CE   NZ                                   
REMARK 470     ARG B 321    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 149    CD   CE   NZ                                        
REMARK 470     LYS C 194    CD   CE   NZ                                        
REMARK 470     ARG C 212    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN C 218    CD   OE1  NE2                                       
REMARK 470     ARG C 279    NE   CZ   NH1  NH2                                  
REMARK 470     LYS D 160    CE   NZ                                             
REMARK 470     LYS D 194    CD   CE   NZ                                        
REMARK 470     ARG D 212    NE   CZ   NH1  NH2                                  
REMARK 470     ILE D 219    CG1  CD1                                            
REMARK 470     ARG D 291    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 314    CD   CE   NZ                                        
REMARK 470     ARG D 321    CG   CD   NE   CZ   NH1  NH2                        
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   OP2   DA F    11     O    HOH F   373              1.81            
REMARK 500   N    GLN B   143     O    HOH B   380              1.87            
REMARK 500   O    PRO B   133     O    HOH B   368              1.91            
REMARK 500   OG1  THR B   199     O    HOH B   392              1.95            
REMARK 500   O2    DT F    10     O    HOH F   371              1.99            
REMARK 500   N7    DA E    11     O    HOH E   369              2.02            
REMARK 500   O    ILE A   166     O    HOH A   383              2.04            
REMARK 500   OE1  GLN B   143     O    HOH B   380              2.06            
REMARK 500   OG   SER B   211     O    HOH B   370              2.15            
REMARK 500   O    HOH B    97     O    HOH B   392              2.16            
REMARK 500   N6    DA E    11     O    HOH E   369              2.17            
REMARK 500   O    LYS C   203     O    HOH C     5              2.17            
REMARK 500   OP2   DT F    12     O    HOH F   374              2.18            
REMARK 500   N    SER C   128     O    HOH C   377              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    PRO A 181   C   -  N   -  CA  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    PRO C 127   C   -  N   -  CA  ANGL. DEV. =  11.2 DEGREES          
REMARK 500    PRO C 181   C   -  N   -  CA  ANGL. DEV. =  10.2 DEGREES          
REMARK 500     DA E   5   O4' -  C1' -  N9  ANGL. DEV. =  -5.6 DEGREES          
REMARK 500     DT E  10   O4' -  C1' -  N1  ANGL. DEV. =   3.3 DEGREES          
REMARK 500     DT E  18   O4' -  C1' -  N1  ANGL. DEV. =   2.7 DEGREES          
REMARK 500     DA F   5   O4' -  C1' -  N9  ANGL. DEV. =  -5.3 DEGREES          
REMARK 500     DT F   6   O4' -  C1' -  C2' ANGL. DEV. =  -4.9 DEGREES          
REMARK 500     DA F  15   O4' -  C1' -  C2' ANGL. DEV. =  -5.0 DEGREES          
REMARK 500     DC F  16   O4' -  C1' -  N1  ANGL. DEV. =   2.7 DEGREES          
REMARK 500     DT F  18   P   -  O5' -  C5' ANGL. DEV. = -11.7 DEGREES          
REMARK 500     DT F  18   O4' -  C1' -  N1  ANGL. DEV. =   3.3 DEGREES          
REMARK 500     DT F  21   O4' -  C1' -  N1  ANGL. DEV. =  -4.5 DEGREES          
REMARK 500     DT F  21   N3  -  C4  -  O4  ANGL. DEV. =   3.7 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    PRO A 135       -8.40    -54.70                                   
REMARK 500    SER A 137       53.21     38.40                                   
REMARK 500    SER A 146       97.74    -40.45                                   
REMARK 500    THR A 147       13.42    -65.14                                   
REMARK 500    ALA A 148       77.64    -69.04                                   
REMARK 500    LYS A 149      -59.27     22.45                                   
REMARK 500    SER A 150       37.28    -91.95                                   
REMARK 500    ALA A 167      -29.53     68.33                                   
REMARK 500    PRO A 181     -168.89    -53.72                                   
REMARK 500    GLN A 182      -78.15    -46.58                                   
REMARK 500    ALA A 184      163.13    -48.12                                   
REMARK 500    VAL A 198      -27.64    -36.12                                   
REMARK 500    SER A 211      160.08    -44.20                                   
REMARK 500    PHE A 214      -17.31     76.98                                   
REMARK 500    GLU A 216      -85.86     -1.50                                   
REMARK 500    ILE A 219       23.68    -70.17                                   
REMARK 500    PRO A 222       -8.37    -46.52                                   
REMARK 500    SER A 271       32.68    -81.87                                   
REMARK 500    SER A 272       13.01   -151.95                                   
REMARK 500    ASN A 278       50.72     32.37                                   
REMARK 500    ALA B 125      157.10    -37.02                                   
REMARK 500    SER B 137       56.62     38.84                                   
REMARK 500    ALA B 151     -173.03    -54.49                                   
REMARK 500    THR B 154      148.45   -174.13                                   
REMARK 500    ALA B 167      -16.59     61.98                                   
REMARK 500    PRO B 181     -154.85    -56.20                                   
REMARK 500    GLN B 182      -95.76    -63.67                                   
REMARK 500    PHE B 214       -3.01     73.41                                   
REMARK 500    GLU B 216      -91.34    -52.80                                   
REMARK 500    GLN B 218      136.37   -171.72                                   
REMARK 500    PRO B 253      170.44    -55.08                                   
REMARK 500    ARG B 321       33.14    -71.45                                   
REMARK 500    PRO C 127      138.69    -32.49                                   
REMARK 500    SER C 146       22.40     30.09                                   
REMARK 500    THR C 147      -66.49     18.18                                   
REMARK 500    ALA C 148      -12.15     43.72                                   
REMARK 500    LYS C 149      -21.54     78.50                                   
REMARK 500    ALA C 167      -21.68     72.82                                   
REMARK 500    PRO C 181     -156.58    -38.28                                   
REMARK 500    GLN C 182      -80.75    -81.92                                   
REMARK 500    ALA C 184      131.76    -37.48                                   
REMARK 500    GLU C 196      -18.51    -47.33                                   
REMARK 500    VAL C 198      -23.21    -37.42                                   
REMARK 500    PHE C 214      -19.25     82.76                                   
REMARK 500    GLU C 216      -75.16    -24.02                                   
REMARK 500    SER C 272        0.46    -62.79                                   
REMARK 500    ASN C 278       52.66     36.21                                   
REMARK 500    LYS D 160       46.85     37.19                                   
REMARK 500    ALA D 167      -22.89     57.89                                   
REMARK 500    PRO D 181     -148.14    -57.52                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      55 RAMACHANDRAN OUTLIERS.                        
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                              ZN A 901  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 205   SG                                                     
REMARK 620 2 HIS A 208   ND1 108.6                                              
REMARK 620 3 CYS A 269   SG  107.7 115.6                                        
REMARK 620 4 CYS A 273   SG  103.9 103.5 116.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 901  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 205   SG                                                     
REMARK 620 2 HIS B 208   ND1 102.6                                              
REMARK 620 3 CYS B 269   SG  105.9 110.4                                        
REMARK 620 4 CYS B 273   SG  121.5 105.6 110.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 901  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 205   SG                                                     
REMARK 620 2 HIS C 208   ND1 106.0                                              
REMARK 620 3 CYS C 269   SG  112.7 111.9                                        
REMARK 620 4 CYS C 273   SG  107.9 102.9 114.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 901  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 205   SG                                                     
REMARK 620 2 HIS D 208   ND1 100.5                                              
REMARK 620 3 CYS D 269   SG  110.9 112.6                                        
REMARK 620 4 CYS D 273   SG  117.7 100.8 113.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 901                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 901                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 901                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 901                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3QYM   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF P63 DNA BINDING DOMAIN IN COMPLEX WITH A 10 BASE PAIR   
REMARK 900 A/T RICH RESPONSE ELEMENT HALF SITE                                  
REMARK 900 RELATED ID: 3QYN   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF P63 DNA BINDING DOMAIN IN COMPLEX WITH A 22 BASE PAIR   
REMARK 900 A/T RICH RESPONSE ELEMENT CONTAINING 2 BASE PAIR SPACER BETWEEN      
REMARK 900 HALF SITES                                                           
REMARK 900 RELATED ID: 3US1   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF P63 DNA BINDING DOMAIN IN COMPLEX WITH A 22 BASE PAIR   
REMARK 900 RESPONSE ELEMENT CONTAINING A TWO BASE PAIR "GC" SPACER BETWEEN      
REMARK 900 HALF SITES                                                           
REMARK 900 RELATED ID: 3US2   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF P63 DNA BINDING DOMAIN IN COMPLEX WITH A 19 BASE PAIR   
REMARK 900 A/T RICH RESPONSE ELEMENT CONTAINING TWO HALF SITES WITH A SINGLE    
REMARK 900 BASE PAIR OVERLAP                                                    
DBREF  3US0 A  127   323  UNP    Q9H3D4   P63_HUMAN      166    362             
DBREF  3US0 B  127   323  UNP    Q9H3D4   P63_HUMAN      166    362             
DBREF  3US0 C  127   323  UNP    Q9H3D4   P63_HUMAN      166    362             
DBREF  3US0 D  127   323  UNP    Q9H3D4   P63_HUMAN      166    362             
DBREF  3US0 E    1    22  PDB    3US0     3US0             1     22             
DBREF  3US0 F    1    22  PDB    3US0     3US0             1     22             
SEQADV 3US0 GLY A  121  UNP  Q9H3D4              EXPRESSION TAG                 
SEQADV 3US0 SER A  122  UNP  Q9H3D4              EXPRESSION TAG                 
SEQADV 3US0 HIS A  123  UNP  Q9H3D4              EXPRESSION TAG                 
SEQADV 3US0 MET A  124  UNP  Q9H3D4              EXPRESSION TAG                 
SEQADV 3US0 ALA A  125  UNP  Q9H3D4              EXPRESSION TAG                 
SEQADV 3US0 SER A  126  UNP  Q9H3D4              EXPRESSION TAG                 
SEQADV 3US0 GLY B  121  UNP  Q9H3D4              EXPRESSION TAG                 
SEQADV 3US0 SER B  122  UNP  Q9H3D4              EXPRESSION TAG                 
SEQADV 3US0 HIS B  123  UNP  Q9H3D4              EXPRESSION TAG                 
SEQADV 3US0 MET B  124  UNP  Q9H3D4              EXPRESSION TAG                 
SEQADV 3US0 ALA B  125  UNP  Q9H3D4              EXPRESSION TAG                 
SEQADV 3US0 SER B  126  UNP  Q9H3D4              EXPRESSION TAG                 
SEQADV 3US0 GLY C  121  UNP  Q9H3D4              EXPRESSION TAG                 
SEQADV 3US0 SER C  122  UNP  Q9H3D4              EXPRESSION TAG                 
SEQADV 3US0 HIS C  123  UNP  Q9H3D4              EXPRESSION TAG                 
SEQADV 3US0 MET C  124  UNP  Q9H3D4              EXPRESSION TAG                 
SEQADV 3US0 ALA C  125  UNP  Q9H3D4              EXPRESSION TAG                 
SEQADV 3US0 SER C  126  UNP  Q9H3D4              EXPRESSION TAG                 
SEQADV 3US0 GLY D  121  UNP  Q9H3D4              EXPRESSION TAG                 
SEQADV 3US0 SER D  122  UNP  Q9H3D4              EXPRESSION TAG                 
SEQADV 3US0 HIS D  123  UNP  Q9H3D4              EXPRESSION TAG                 
SEQADV 3US0 MET D  124  UNP  Q9H3D4              EXPRESSION TAG                 
SEQADV 3US0 ALA D  125  UNP  Q9H3D4              EXPRESSION TAG                 
SEQADV 3US0 SER D  126  UNP  Q9H3D4              EXPRESSION TAG                 
SEQRES   1 A  203  GLY SER HIS MET ALA SER PRO SER ASN THR ASP TYR PRO          
SEQRES   2 A  203  GLY PRO HIS SER PHE ASP VAL SER PHE GLN GLN SER SER          
SEQRES   3 A  203  THR ALA LYS SER ALA THR TRP THR TYR SER THR GLU LEU          
SEQRES   4 A  203  LYS LYS LEU TYR CYS GLN ILE ALA LYS THR CYS PRO ILE          
SEQRES   5 A  203  GLN ILE LYS VAL MET THR PRO PRO PRO GLN GLY ALA VAL          
SEQRES   6 A  203  ILE ARG ALA MET PRO VAL TYR LYS LYS ALA GLU HIS VAL          
SEQRES   7 A  203  THR GLU VAL VAL LYS ARG CYS PRO ASN HIS GLU LEU SER          
SEQRES   8 A  203  ARG GLU PHE ASN GLU GLY GLN ILE ALA PRO PRO SER HIS          
SEQRES   9 A  203  LEU ILE ARG VAL GLU GLY ASN SER HIS ALA GLN TYR VAL          
SEQRES  10 A  203  GLU ASP PRO ILE THR GLY ARG GLN SER VAL LEU VAL PRO          
SEQRES  11 A  203  TYR GLU PRO PRO GLN VAL GLY THR GLU PHE THR THR VAL          
SEQRES  12 A  203  LEU TYR ASN PHE MET CYS ASN SER SER CYS VAL GLY GLY          
SEQRES  13 A  203  MET ASN ARG ARG PRO ILE LEU ILE ILE VAL THR LEU GLU          
SEQRES  14 A  203  THR ARG ASP GLY GLN VAL LEU GLY ARG ARG CYS PHE GLU          
SEQRES  15 A  203  ALA ARG ILE CYS ALA CYS PRO GLY ARG ASP ARG LYS ALA          
SEQRES  16 A  203  ASP GLU ASP SER ILE ARG LYS GLN                              
SEQRES   1 B  203  GLY SER HIS MET ALA SER PRO SER ASN THR ASP TYR PRO          
SEQRES   2 B  203  GLY PRO HIS SER PHE ASP VAL SER PHE GLN GLN SER SER          
SEQRES   3 B  203  THR ALA LYS SER ALA THR TRP THR TYR SER THR GLU LEU          
SEQRES   4 B  203  LYS LYS LEU TYR CYS GLN ILE ALA LYS THR CYS PRO ILE          
SEQRES   5 B  203  GLN ILE LYS VAL MET THR PRO PRO PRO GLN GLY ALA VAL          
SEQRES   6 B  203  ILE ARG ALA MET PRO VAL TYR LYS LYS ALA GLU HIS VAL          
SEQRES   7 B  203  THR GLU VAL VAL LYS ARG CYS PRO ASN HIS GLU LEU SER          
SEQRES   8 B  203  ARG GLU PHE ASN GLU GLY GLN ILE ALA PRO PRO SER HIS          
SEQRES   9 B  203  LEU ILE ARG VAL GLU GLY ASN SER HIS ALA GLN TYR VAL          
SEQRES  10 B  203  GLU ASP PRO ILE THR GLY ARG GLN SER VAL LEU VAL PRO          
SEQRES  11 B  203  TYR GLU PRO PRO GLN VAL GLY THR GLU PHE THR THR VAL          
SEQRES  12 B  203  LEU TYR ASN PHE MET CYS ASN SER SER CYS VAL GLY GLY          
SEQRES  13 B  203  MET ASN ARG ARG PRO ILE LEU ILE ILE VAL THR LEU GLU          
SEQRES  14 B  203  THR ARG ASP GLY GLN VAL LEU GLY ARG ARG CYS PHE GLU          
SEQRES  15 B  203  ALA ARG ILE CYS ALA CYS PRO GLY ARG ASP ARG LYS ALA          
SEQRES  16 B  203  ASP GLU ASP SER ILE ARG LYS GLN                              
SEQRES   1 C  203  GLY SER HIS MET ALA SER PRO SER ASN THR ASP TYR PRO          
SEQRES   2 C  203  GLY PRO HIS SER PHE ASP VAL SER PHE GLN GLN SER SER          
SEQRES   3 C  203  THR ALA LYS SER ALA THR TRP THR TYR SER THR GLU LEU          
SEQRES   4 C  203  LYS LYS LEU TYR CYS GLN ILE ALA LYS THR CYS PRO ILE          
SEQRES   5 C  203  GLN ILE LYS VAL MET THR PRO PRO PRO GLN GLY ALA VAL          
SEQRES   6 C  203  ILE ARG ALA MET PRO VAL TYR LYS LYS ALA GLU HIS VAL          
SEQRES   7 C  203  THR GLU VAL VAL LYS ARG CYS PRO ASN HIS GLU LEU SER          
SEQRES   8 C  203  ARG GLU PHE ASN GLU GLY GLN ILE ALA PRO PRO SER HIS          
SEQRES   9 C  203  LEU ILE ARG VAL GLU GLY ASN SER HIS ALA GLN TYR VAL          
SEQRES  10 C  203  GLU ASP PRO ILE THR GLY ARG GLN SER VAL LEU VAL PRO          
SEQRES  11 C  203  TYR GLU PRO PRO GLN VAL GLY THR GLU PHE THR THR VAL          
SEQRES  12 C  203  LEU TYR ASN PHE MET CYS ASN SER SER CYS VAL GLY GLY          
SEQRES  13 C  203  MET ASN ARG ARG PRO ILE LEU ILE ILE VAL THR LEU GLU          
SEQRES  14 C  203  THR ARG ASP GLY GLN VAL LEU GLY ARG ARG CYS PHE GLU          
SEQRES  15 C  203  ALA ARG ILE CYS ALA CYS PRO GLY ARG ASP ARG LYS ALA          
SEQRES  16 C  203  ASP GLU ASP SER ILE ARG LYS GLN                              
SEQRES   1 D  203  GLY SER HIS MET ALA SER PRO SER ASN THR ASP TYR PRO          
SEQRES   2 D  203  GLY PRO HIS SER PHE ASP VAL SER PHE GLN GLN SER SER          
SEQRES   3 D  203  THR ALA LYS SER ALA THR TRP THR TYR SER THR GLU LEU          
SEQRES   4 D  203  LYS LYS LEU TYR CYS GLN ILE ALA LYS THR CYS PRO ILE          
SEQRES   5 D  203  GLN ILE LYS VAL MET THR PRO PRO PRO GLN GLY ALA VAL          
SEQRES   6 D  203  ILE ARG ALA MET PRO VAL TYR LYS LYS ALA GLU HIS VAL          
SEQRES   7 D  203  THR GLU VAL VAL LYS ARG CYS PRO ASN HIS GLU LEU SER          
SEQRES   8 D  203  ARG GLU PHE ASN GLU GLY GLN ILE ALA PRO PRO SER HIS          
SEQRES   9 D  203  LEU ILE ARG VAL GLU GLY ASN SER HIS ALA GLN TYR VAL          
SEQRES  10 D  203  GLU ASP PRO ILE THR GLY ARG GLN SER VAL LEU VAL PRO          
SEQRES  11 D  203  TYR GLU PRO PRO GLN VAL GLY THR GLU PHE THR THR VAL          
SEQRES  12 D  203  LEU TYR ASN PHE MET CYS ASN SER SER CYS VAL GLY GLY          
SEQRES  13 D  203  MET ASN ARG ARG PRO ILE LEU ILE ILE VAL THR LEU GLU          
SEQRES  14 D  203  THR ARG ASP GLY GLN VAL LEU GLY ARG ARG CYS PHE GLU          
SEQRES  15 D  203  ALA ARG ILE CYS ALA CYS PRO GLY ARG ASP ARG LYS ALA          
SEQRES  16 D  203  ASP GLU ASP SER ILE ARG LYS GLN                              
SEQRES   1 E   22   DA  DA  DA  DC  DA  DT  DG  DT  DT  DT  DA  DT  DA          
SEQRES   2 E   22   DA  DA  DC  DA  DT  DG  DT  DT  DT                          
SEQRES   1 F   22   DA  DA  DA  DC  DA  DT  DG  DT  DT  DT  DA  DT  DA          
SEQRES   2 F   22   DA  DA  DC  DA  DT  DG  DT  DT  DT                          
HET     ZN  A 901       1                                                       
HET     ZN  B 901       1                                                       
HET     ZN  C 901       1                                                       
HET     ZN  D 901       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   7   ZN    4(ZN 2+)                                                     
FORMUL  11  HOH   *394(H2 O)                                                    
HELIX    1   1 PRO A  133  SER A  137  5                                   5    
HELIX    2   2 CYS A  205  SER A  211  1                                   7    
HELIX    3   3 CYS A  308  GLU A  317  1                                  10    
HELIX    4   4 CYS B  205  SER B  211  1                                   7    
HELIX    5   5 CYS B  308  ILE B  320  1                                  13    
HELIX    6   6 CYS C  205  SER C  211  1                                   7    
HELIX    7   7 CYS C  308  SER C  319  1                                  12    
HELIX    8   8 CYS D  205  SER D  211  1                                   7    
HELIX    9   9 CYS D  308  ARG D  321  1                                  14    
SHEET    1   A 4 ASP A 139  SER A 141  0                                        
SHEET    2   A 4 THR A 169  LYS A 175 -1  O  GLN A 173   N  SER A 141           
SHEET    3   A 4 THR A 261  PHE A 267 -1  O  VAL A 263   N  ILE A 172           
SHEET    4   A 4 ILE A 226  GLU A 229 -1  N  ARG A 227   O  ASN A 266           
SHEET    1   B 7 TRP A 153  SER A 156  0                                        
SHEET    2   B 7 LYS A 161  CYS A 164 -1  O  TYR A 163   N  THR A 154           
SHEET    3   B 7 VAL A 295  ILE A 305  1  O  ARG A 304   N  LEU A 162           
SHEET    4   B 7 ILE A 282  GLU A 289 -1  N  LEU A 288   O  GLY A 297           
SHEET    5   B 7 VAL A 185  TYR A 192 -1  N  VAL A 185   O  GLU A 289           
SHEET    6   B 7 GLN A 245  PRO A 250 -1  O  VAL A 249   N  ILE A 186           
SHEET    7   B 7 GLN A 235  GLU A 238 -1  N  GLN A 235   O  LEU A 248           
SHEET    1   C 4 ASP B 139  SER B 141  0                                        
SHEET    2   C 4 THR B 169  LYS B 175 -1  O  GLN B 173   N  SER B 141           
SHEET    3   C 4 THR B 261  PHE B 267 -1  O  TYR B 265   N  CYS B 170           
SHEET    4   C 4 ILE B 226  VAL B 228 -1  N  ARG B 227   O  ASN B 266           
SHEET    1   D 7 TRP B 153  SER B 156  0                                        
SHEET    2   D 7 LYS B 161  CYS B 164 -1  O  TYR B 163   N  THR B 154           
SHEET    3   D 7 VAL B 295  ILE B 305  1  O  GLU B 302   N  LEU B 162           
SHEET    4   D 7 ILE B 282  GLU B 289 -1  N  ILE B 284   O  PHE B 301           
SHEET    5   D 7 VAL B 185  TYR B 192 -1  N  MET B 189   O  ILE B 285           
SHEET    6   D 7 GLN B 245  PRO B 250 -1  O  VAL B 249   N  ILE B 186           
SHEET    7   D 7 GLN B 235  GLU B 238 -1  N  GLN B 235   O  LEU B 248           
SHEET    1   E 4 ASP C 139  SER C 141  0                                        
SHEET    2   E 4 THR C 169  LYS C 175 -1  O  GLN C 173   N  SER C 141           
SHEET    3   E 4 THR C 261  PHE C 267 -1  O  THR C 261   N  ILE C 174           
SHEET    4   E 4 ILE C 226  VAL C 228 -1  N  ARG C 227   O  ASN C 266           
SHEET    1   F 7 TRP C 153  SER C 156  0                                        
SHEET    2   F 7 LYS C 161  CYS C 164 -1  O  TYR C 163   N  THR C 154           
SHEET    3   F 7 VAL C 295  ARG C 304  1  O  GLU C 302   N  LEU C 162           
SHEET    4   F 7 ILE C 282  GLU C 289 -1  N  LEU C 288   O  LEU C 296           
SHEET    5   F 7 VAL C 185  TYR C 192 -1  N  VAL C 185   O  GLU C 289           
SHEET    6   F 7 GLN C 245  PRO C 250 -1  O  VAL C 249   N  ILE C 186           
SHEET    7   F 7 GLN C 235  GLU C 238 -1  N  VAL C 237   O  SER C 246           
SHEET    1   G 4 ASP D 139  SER D 141  0                                        
SHEET    2   G 4 THR D 169  LYS D 175 -1  O  GLN D 173   N  SER D 141           
SHEET    3   G 4 THR D 261  PHE D 267 -1  O  TYR D 265   N  CYS D 170           
SHEET    4   G 4 ILE D 226  VAL D 228 -1  N  ARG D 227   O  ASN D 266           
SHEET    1   H 7 TRP D 153  SER D 156  0                                        
SHEET    2   H 7 LYS D 161  GLN D 165 -1  O  TYR D 163   N  THR D 154           
SHEET    3   H 7 VAL D 295  CYS D 306  1  O  ARG D 304   N  LEU D 162           
SHEET    4   H 7 ILE D 282  GLU D 289 -1  N  ILE D 284   O  PHE D 301           
SHEET    5   H 7 VAL D 185  TYR D 192 -1  N  ARG D 187   O  THR D 287           
SHEET    6   H 7 GLN D 245  PRO D 250 -1  O  VAL D 249   N  ILE D 186           
SHEET    7   H 7 GLN D 235  GLU D 238 -1  N  GLN D 235   O  LEU D 248           
LINK         SG  CYS A 205                ZN    ZN A 901     1555   1555  2.38  
LINK         ND1 HIS A 208                ZN    ZN A 901     1555   1555  2.09  
LINK         SG  CYS A 269                ZN    ZN A 901     1555   1555  2.31  
LINK         SG  CYS A 273                ZN    ZN A 901     1555   1555  2.30  
LINK         SG  CYS B 205                ZN    ZN B 901     1555   1555  2.31  
LINK         ND1 HIS B 208                ZN    ZN B 901     1555   1555  2.12  
LINK         SG  CYS B 269                ZN    ZN B 901     1555   1555  2.36  
LINK         SG  CYS B 273                ZN    ZN B 901     1555   1555  2.35  
LINK         SG  CYS C 205                ZN    ZN C 901     1555   1555  2.36  
LINK         ND1 HIS C 208                ZN    ZN C 901     1555   1555  2.12  
LINK         SG  CYS C 269                ZN    ZN C 901     1555   1555  2.35  
LINK         SG  CYS C 273                ZN    ZN C 901     1555   1555  2.31  
LINK         SG  CYS D 205                ZN    ZN D 901     1555   1555  2.32  
LINK         ND1 HIS D 208                ZN    ZN D 901     1555   1555  2.15  
LINK         SG  CYS D 269                ZN    ZN D 901     1555   1555  2.34  
LINK         SG  CYS D 273                ZN    ZN D 901     1555   1555  2.32  
SITE     1 AC1  4 CYS A 205  HIS A 208  CYS A 269  CYS A 273                    
SITE     1 AC2  4 CYS B 205  HIS B 208  CYS B 269  CYS B 273                    
SITE     1 AC3  4 CYS C 205  HIS C 208  CYS C 269  CYS C 273                    
SITE     1 AC4  4 CYS D 205  HIS D 208  CYS D 269  CYS D 273                    
CRYST1  141.806  141.806  119.604  90.00  90.00 120.00 P 63         24          
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      0.007052  0.004071  0.000000        0.00000                         
SCALE2      0.000000  0.008143  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008361        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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