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Database: PDB
Entry: 2OZO
LinkDB: 2OZO
Original site: 2OZO 
HEADER    TRANSFERASE                             26-FEB-07   2OZO              
TITLE     AUTOINHIBITED INTACT HUMAN ZAP-70                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE ZAP-70;                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: INACTIVE ZAP-70 (RESIDUES 1-606);                          
COMPND   5 SYNONYM: 70 KDA ZETA-ASSOCIATED PROTEIN, SYK-RELATED                 
COMPND   6 TYROSINE KINASE;                                                     
COMPND   7 EC: 2.7.10.2;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ZAP70, SRK;                                                    
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: TRIEX SF9;                                 
SOURCE  10 EXPRESSION_SYSTEM_CELL: BACULOVIRUS-INFECTED INSECT CELLS            
SOURCE  11 SF9;                                                                 
SOURCE  12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  13 EXPRESSION_SYSTEM_PLASMID: PFASTBAC-1                                
KEYWDS    INACTIVE ZAP-70, TANDEM SH2, AUTOINHIBITION, ITAM, HYDROGEN           
KEYWDS   2 BONDING NETWORK, TCR SIGNALING, TRANSFERASE                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.DEINDL,T.A.KADLECEK,T.BRDICKA,X.CAO,A.WEISS,J.KURIYAN               
REVDAT   3   24-FEB-09 2OZO    1       VERSN                                    
REVDAT   2   05-JUN-07 2OZO    1       JRNL                                     
REVDAT   1   22-MAY-07 2OZO    0                                                
JRNL        AUTH   S.DEINDL,T.A.KADLECEK,T.BRDICKA,X.CAO,A.WEISS,               
JRNL        AUTH 2 J.KURIYAN                                                    
JRNL        TITL   STRUCTURAL BASIS FOR THE INHIBITION OF TYROSINE              
JRNL        TITL 2 KINASE ACTIVITY OF ZAP-70.                                   
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 129   735 2007              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   17512407                                                     
JRNL        DOI    10.1016/J.CELL.2007.03.039                                   
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 500.00                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 88.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 17302                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.290                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.300                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1622                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4226                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 32                                      
REMARK   3   SOLVENT ATOMS            : 69                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.42                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.86400                                             
REMARK   3    B22 (A**2) : 3.76500                                              
REMARK   3    B33 (A**2) : -1.90100                                             
REMARK   3    B12 (A**2) : 2.51500                                              
REMARK   3    B13 (A**2) : 4.25300                                              
REMARK   3    B23 (A**2) : -5.08300                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.342 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.305 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.798 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.769 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 38.89                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  3  : ANP_PAR.TXT                                    
REMARK   3  PARAMETER FILE  4  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2OZO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAR-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB041784.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-APR-06                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.115879                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : DOUBLE CRYSTAL, SI(111)            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18285                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 500.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.3                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.1800                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 78.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.34500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.05                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05 M NASCN, 21% PEG3350, PROTEIN       
REMARK 280  MIXED WITH 9 MM N-DECYL-BETA-D-THIOMALTOPYRANOSIDE, VAPOR           
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     MET A     1                                                      
REMARK 465     SER A   257                                                      
REMARK 465     SER A   258                                                      
REMARK 465     ALA A   259                                                      
REMARK 465     SER A   260                                                      
REMARK 465     ASN A   261                                                      
REMARK 465     ALA A   262                                                      
REMARK 465     SER A   263                                                      
REMARK 465     GLY A   264                                                      
REMARK 465     ALA A   265                                                      
REMARK 465     ALA A   266                                                      
REMARK 465     ALA A   267                                                      
REMARK 465     PRO A   268                                                      
REMARK 465     THR A   269                                                      
REMARK 465     LEU A   270                                                      
REMARK 465     PRO A   271                                                      
REMARK 465     ALA A   272                                                      
REMARK 465     HIS A   273                                                      
REMARK 465     PRO A   274                                                      
REMARK 465     SER A   275                                                      
REMARK 465     THR A   276                                                      
REMARK 465     LEU A   277                                                      
REMARK 465     THR A   278                                                      
REMARK 465     HIS A   279                                                      
REMARK 465     PRO A   280                                                      
REMARK 465     GLN A   281                                                      
REMARK 465     ARG A   282                                                      
REMARK 465     ARG A   283                                                      
REMARK 465     ILE A   284                                                      
REMARK 465     ASP A   285                                                      
REMARK 465     THR A   286                                                      
REMARK 465     LEU A   287                                                      
REMARK 465     ASN A   288                                                      
REMARK 465     SER A   289                                                      
REMARK 465     ASP A   290                                                      
REMARK 465     GLY A   291                                                      
REMARK 465     TYR A   292                                                      
REMARK 465     THR A   293                                                      
REMARK 465     PRO A   294                                                      
REMARK 465     GLU A   295                                                      
REMARK 465     PRO A   296                                                      
REMARK 465     ALA A   297                                                      
REMARK 465     ARG A   298                                                      
REMARK 465     ILE A   299                                                      
REMARK 465     THR A   300                                                      
REMARK 465     SER A   301                                                      
REMARK 465     PRO A   302                                                      
REMARK 465     ASP A   303                                                      
REMARK 465     LYS A   304                                                      
REMARK 465     PRO A   305                                                      
REMARK 465     ARG A   306                                                      
REMARK 465     PRO A   307                                                      
REMARK 465     MET A   308                                                      
REMARK 465     PRO A   309                                                      
REMARK 465     ALA A   488                                                      
REMARK 465     ASP A   489                                                      
REMARK 465     ASP A   490                                                      
REMARK 465     SER A   491                                                      
REMARK 465     TYR A   492                                                      
REMARK 465     TYR A   493                                                      
REMARK 465     THR A   494                                                      
REMARK 465     ALA A   495                                                      
REMARK 465     ARG A   496                                                      
REMARK 465     SER A   497                                                      
REMARK 465     ALA A   498                                                      
REMARK 465     GLY A   499                                                      
REMARK 465     LYS A   500                                                      
REMARK 465     TRP A   501                                                      
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     GLU A  22    CG   CD   OE1  OE2                                  
REMARK 470     ASP A  31    CG   OD1  OD2                                       
REMARK 470     ASP A  53    CG   OD1  OD2                                       
REMARK 470     ARG A  55    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  62    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  85    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 100    CG   CD   CE   NZ                                   
REMARK 470     ASP A 125    CG   OD1  OD2                                       
REMARK 470     GLU A 139    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 160    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET A 310    CG   SD   CE                                        
REMARK 470     THR A 312    OG1  CG2                                            
REMARK 470     GLU A 324    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 325    CG   CD1  CD2                                       
REMARK 470     LYS A 326    CG   CD   CE   NZ                                   
REMARK 470     ASP A 327    CG   OD1  OD2                                       
REMARK 470     LYS A 329    CG   CD   CE   NZ                                   
REMARK 470     ASN A 348    CG   OD1  ND2                                       
REMARK 470     ARG A 358    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 372    CG   CD   CE   NZ                                   
REMARK 470     GLN A 373    CG   CD   OE1  NE2                                  
REMARK 470     THR A 375    OG1  CG2                                            
REMARK 470     GLU A 376    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 377    CG   CD   CE   NZ                                   
REMARK 470     ARG A 385    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 431    CG   CD   OE1  OE2                                  
REMARK 470     SER A 483    OG                                                  
REMARK 470     LYS A 484    CG   CD   CE   NZ                                   
REMARK 470     LEU A 486    CG   CD1  CD2                                       
REMARK 470     LYS A 541    CG   CD   CE   NZ                                   
REMARK 470     LYS A 542    CG   CD   CE   NZ                                   
REMARK 470     GLU A 553    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 581    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 603    CB   CG   CD   CE   NZ                              
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   4        6.49    -69.35                                   
REMARK 500    SER A  14       52.87   -100.62                                   
REMARK 500    MET A  29       22.60     37.70                                   
REMARK 500    ALA A  72      124.20    -37.72                                   
REMARK 500    ASP A  90      116.22   -165.72                                   
REMARK 500    ASP A  92       35.01     32.65                                   
REMARK 500    CYS A  96      155.58    175.40                                   
REMARK 500    ARG A  99     -108.71   -110.68                                   
REMARK 500    SER A 106     -103.03     39.75                                   
REMARK 500    LYS A 132       42.61     36.89                                   
REMARK 500    SER A 167       61.38   -156.40                                   
REMARK 500    SER A 179       55.77    -92.36                                   
REMARK 500    ALA A 243       57.86   -116.13                                   
REMARK 500    LYS A 251     -103.72   -123.14                                   
REMARK 500    PHE A 315       41.56    -99.05                                   
REMARK 500    SER A 317      170.69     75.69                                   
REMARK 500    PRO A 318       85.90    -51.29                                   
REMARK 500    LEU A 325      102.42    138.25                                   
REMARK 500    ASP A 327       59.23    169.96                                   
REMARK 500    PHE A 349     -150.66    -66.46                                   
REMARK 500    LEU A 371      102.76     53.48                                   
REMARK 500    GLN A 373      -41.91    161.45                                   
REMARK 500    LYS A 377     -174.24    147.82                                   
REMARK 500    ALA A 407     -116.64   -133.39                                   
REMARK 500    ARG A 460      -19.73     80.94                                   
REMARK 500    LEU A 503       51.77   -148.01                                   
REMARK 500    PHE A 513       19.16   -140.04                                   
REMARK 500    TYR A 535       75.14     41.73                                   
REMARK 500    LYS A 542       41.49    -72.70                                   
REMARK 500    LYS A 544     -104.75   -156.32                                   
REMARK 500    PRO A 565      151.55    -48.26                                   
REMARK 500    TRP A 580      -29.33    -39.34                                   
REMARK 500    SER A 602      -50.27   -145.05                                   
REMARK 500    LYS A 603       50.09    -50.31                                   
REMARK 500    VAL A 604      -95.96     54.83                                   
REMARK 500    GLU A 605     -170.97   -178.69                                   
REMARK 500    SER A 608     -159.57     63.80                                   
REMARK 500    ALA A 609       54.86    -69.16                                   
REMARK 500    LEU A 610       51.61   -110.64                                   
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                              MG A 614  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ANP A 615   O2A                                                    
REMARK 620 2 ANP A 615   O3A  57.2                                              
REMARK 620 3 ASN A 466   OD1 173.8 129.0                                        
REMARK 620 4 ASP A 479   OD1  81.5 103.5  96.3                                  
REMARK 620 5 ANP A 615   O2G 110.3  68.8  74.2  71.2                            
REMARK 620 6 ANP A 615   O2B  98.6  56.5  86.0 152.9  83.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 614                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A 615                 
DBREF  2OZO A    1   606  UNP    P43403   ZAP70_HUMAN      1    606             
SEQADV 2OZO PHE A  315  UNP  P43403    TYR   315 ENGINEERED                     
SEQADV 2OZO PHE A  319  UNP  P43403    TYR   319 ENGINEERED                     
SEQADV 2OZO ASN A  461  UNP  P43403    ASP   461 ENGINEERED                     
SEQADV 2OZO GLY A  607  UNP  P43403              CLONING ARTIFACT               
SEQADV 2OZO SER A  608  UNP  P43403              CLONING ARTIFACT               
SEQADV 2OZO ALA A  609  UNP  P43403              CLONING ARTIFACT               
SEQADV 2OZO LEU A  610  UNP  P43403              CLONING ARTIFACT               
SEQADV 2OZO GLU A  611  UNP  P43403              CLONING ARTIFACT               
SEQADV 2OZO VAL A  612  UNP  P43403              CLONING ARTIFACT               
SEQADV 2OZO ALA A  613  UNP  P43403              CLONING ARTIFACT               
SEQRES   1 A  613  MET PRO ASP PRO ALA ALA HIS LEU PRO PHE PHE TYR GLY          
SEQRES   2 A  613  SER ILE SER ARG ALA GLU ALA GLU GLU HIS LEU LYS LEU          
SEQRES   3 A  613  ALA GLY MET ALA ASP GLY LEU PHE LEU LEU ARG GLN CYS          
SEQRES   4 A  613  LEU ARG SER LEU GLY GLY TYR VAL LEU SER LEU VAL HIS          
SEQRES   5 A  613  ASP VAL ARG PHE HIS HIS PHE PRO ILE GLU ARG GLN LEU          
SEQRES   6 A  613  ASN GLY THR TYR ALA ILE ALA GLY GLY LYS ALA HIS CYS          
SEQRES   7 A  613  GLY PRO ALA GLU LEU CYS GLU PHE TYR SER ARG ASP PRO          
SEQRES   8 A  613  ASP GLY LEU PRO CYS ASN LEU ARG LYS PRO CYS ASN ARG          
SEQRES   9 A  613  PRO SER GLY LEU GLU PRO GLN PRO GLY VAL PHE ASP CYS          
SEQRES  10 A  613  LEU ARG ASP ALA MET VAL ARG ASP TYR VAL ARG GLN THR          
SEQRES  11 A  613  TRP LYS LEU GLU GLY GLU ALA LEU GLU GLN ALA ILE ILE          
SEQRES  12 A  613  SER GLN ALA PRO GLN VAL GLU LYS LEU ILE ALA THR THR          
SEQRES  13 A  613  ALA HIS GLU ARG MET PRO TRP TYR HIS SER SER LEU THR          
SEQRES  14 A  613  ARG GLU GLU ALA GLU ARG LYS LEU TYR SER GLY ALA GLN          
SEQRES  15 A  613  THR ASP GLY LYS PHE LEU LEU ARG PRO ARG LYS GLU GLN          
SEQRES  16 A  613  GLY THR TYR ALA LEU SER LEU ILE TYR GLY LYS THR VAL          
SEQRES  17 A  613  TYR HIS TYR LEU ILE SER GLN ASP LYS ALA GLY LYS TYR          
SEQRES  18 A  613  CYS ILE PRO GLU GLY THR LYS PHE ASP THR LEU TRP GLN          
SEQRES  19 A  613  LEU VAL GLU TYR LEU LYS LEU LYS ALA ASP GLY LEU ILE          
SEQRES  20 A  613  TYR CYS LEU LYS GLU ALA CYS PRO ASN SER SER ALA SER          
SEQRES  21 A  613  ASN ALA SER GLY ALA ALA ALA PRO THR LEU PRO ALA HIS          
SEQRES  22 A  613  PRO SER THR LEU THR HIS PRO GLN ARG ARG ILE ASP THR          
SEQRES  23 A  613  LEU ASN SER ASP GLY TYR THR PRO GLU PRO ALA ARG ILE          
SEQRES  24 A  613  THR SER PRO ASP LYS PRO ARG PRO MET PRO MET ASP THR          
SEQRES  25 A  613  SER VAL PHE GLU SER PRO PHE SER ASP PRO GLU GLU LEU          
SEQRES  26 A  613  LYS ASP LYS LYS LEU PHE LEU LYS ARG ASP ASN LEU LEU          
SEQRES  27 A  613  ILE ALA ASP ILE GLU LEU GLY CYS GLY ASN PHE GLY SER          
SEQRES  28 A  613  VAL ARG GLN GLY VAL TYR ARG MET ARG LYS LYS GLN ILE          
SEQRES  29 A  613  ASP VAL ALA ILE LYS VAL LEU LYS GLN GLY THR GLU LYS          
SEQRES  30 A  613  ALA ASP THR GLU GLU MET MET ARG GLU ALA GLN ILE MET          
SEQRES  31 A  613  HIS GLN LEU ASP ASN PRO TYR ILE VAL ARG LEU ILE GLY          
SEQRES  32 A  613  VAL CYS GLN ALA GLU ALA LEU MET LEU VAL MET GLU MET          
SEQRES  33 A  613  ALA GLY GLY GLY PRO LEU HIS LYS PHE LEU VAL GLY LYS          
SEQRES  34 A  613  ARG GLU GLU ILE PRO VAL SER ASN VAL ALA GLU LEU LEU          
SEQRES  35 A  613  HIS GLN VAL SER MET GLY MET LYS TYR LEU GLU GLU LYS          
SEQRES  36 A  613  ASN PHE VAL HIS ARG ASN LEU ALA ALA ARG ASN VAL LEU          
SEQRES  37 A  613  LEU VAL ASN ARG HIS TYR ALA LYS ILE SER ASP PHE GLY          
SEQRES  38 A  613  LEU SER LYS ALA LEU GLY ALA ASP ASP SER TYR TYR THR          
SEQRES  39 A  613  ALA ARG SER ALA GLY LYS TRP PRO LEU LYS TRP TYR ALA          
SEQRES  40 A  613  PRO GLU CYS ILE ASN PHE ARG LYS PHE SER SER ARG SER          
SEQRES  41 A  613  ASP VAL TRP SER TYR GLY VAL THR MET TRP GLU ALA LEU          
SEQRES  42 A  613  SER TYR GLY GLN LYS PRO TYR LYS LYS MET LYS GLY PRO          
SEQRES  43 A  613  GLU VAL MET ALA PHE ILE GLU GLN GLY LYS ARG MET GLU          
SEQRES  44 A  613  CYS PRO PRO GLU CYS PRO PRO GLU LEU TYR ALA LEU MET          
SEQRES  45 A  613  SER ASP CYS TRP ILE TYR LYS TRP GLU ASP ARG PRO ASP          
SEQRES  46 A  613  PHE LEU THR VAL GLU GLN ARG MET ARG ALA CYS TYR TYR          
SEQRES  47 A  613  SER LEU ALA SER LYS VAL GLU GLY GLY SER ALA LEU GLU          
SEQRES  48 A  613  VAL ALA                                                      
HET     MG  A 614       1                                                       
HET    ANP  A 615      31                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
FORMUL   2   MG    MG 2+                                                        
FORMUL   3  ANP    C10 H17 N6 O12 P3                                            
FORMUL   4  HOH   *69(H2 O)                                                     
HELIX    1   1 SER A   16  LEU A   26  1                                  11    
HELIX    2   2 GLY A   79  SER A   88  1                                  10    
HELIX    3   3 GLY A  113  LYS A  132  1                                  20    
HELIX    4   4 GLU A  134  ALA A  154  1                                  21    
HELIX    5   5 THR A  169  TYR A  178  1                                  10    
HELIX    6   6 THR A  231  LYS A  242  1                                  12    
HELIX    7   7 ASP A  379  HIS A  391  1                                  13    
HELIX    8   8 PRO A  421  VAL A  427  1                                   7    
HELIX    9   9 PRO A  434  LYS A  455  1                                  22    
HELIX   10  10 ALA A  463  ARG A  465  5                                   3    
HELIX   11  11 ALA A  507  ARG A  514  1                                   8    
HELIX   12  12 SER A  517  SER A  534  1                                  18    
HELIX   13  13 GLY A  545  GLN A  554  1                                  10    
HELIX   14  14 PRO A  565  CYS A  575  1                                  11    
HELIX   15  15 ASP A  585  ALA A  601  1                                  17    
SHEET    1   A 4 LEU A  33  GLN A  38  0                                        
SHEET    2   A 4 TYR A  46  HIS A  52 -1  O  VAL A  51   N  LEU A  33           
SHEET    3   A 4 ARG A  55  ARG A  63 -1  O  PHE A  59   N  LEU A  48           
SHEET    4   A 4 TYR A  69  ILE A  71 -1  O  ALA A  70   N  GLU A  62           
SHEET    1   B 5 PHE A 187  PRO A 191  0                                        
SHEET    2   B 5 THR A 197  TYR A 204 -1  O  ALA A 199   N  ARG A 190           
SHEET    3   B 5 THR A 207  GLN A 215 -1  O  ILE A 213   N  TYR A 198           
SHEET    4   B 5 TYR A 221  CYS A 222 -1  O  CYS A 222   N  SER A 214           
SHEET    5   B 5 LYS A 228  PHE A 229 -1  O  PHE A 229   N  TYR A 221           
SHEET    1   C 5 LEU A 337  CYS A 346  0                                        
SHEET    2   C 5 SER A 351  ARG A 358 -1  O  VAL A 356   N  LEU A 338           
SHEET    3   C 5 GLN A 363  VAL A 370 -1  O  ILE A 368   N  ARG A 353           
SHEET    4   C 5 LEU A 410  GLU A 415 -1  O  LEU A 412   N  LYS A 369           
SHEET    5   C 5 LEU A 401  GLN A 406 -1  N  CYS A 405   O  MET A 411           
SHEET    1   D 2 VAL A 467  ASN A 471  0                                        
SHEET    2   D 2 TYR A 474  ILE A 477 -1  O  LYS A 476   N  LEU A 468           
LINK        MG    MG A 614                 O2A ANP A 615     1555   1555  2.50  
LINK        MG    MG A 614                 O3A ANP A 615     1555   1555  2.76  
LINK        MG    MG A 614                 OD1 ASN A 466     1555   1555  2.38  
LINK        MG    MG A 614                 OD1 ASP A 479     1555   1555  2.39  
LINK        MG    MG A 614                 O2G ANP A 615     1555   1555  2.79  
LINK        MG    MG A 614                 O2B ANP A 615     1555   1555  2.46  
SITE     1 AC1  3 ASN A 466  ASP A 479  ANP A 615                               
SITE     1 AC2 18 LEU A 344  CYS A 346  GLY A 347  ASN A 348                    
SITE     2 AC2 18 PHE A 349  VAL A 352  ALA A 367  LYS A 369                    
SITE     3 AC2 18 GLU A 415  ALA A 417  PRO A 421  ARG A 465                    
SITE     4 AC2 18 ASN A 466  LEU A 468  ASP A 479   MG A 614                    
SITE     5 AC2 18 HOH A 655  HOH A 671                                          
CRYST1   48.297   52.929   69.331 105.91  92.94 103.72 P 1           1          
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      0.020705  0.005055  0.002674        0.00000                         
SCALE2      0.000000  0.019448  0.006006        0.00000                         
SCALE3      0.000000  0.000000  0.015116        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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