GenomeNet

Database: PDB
Entry: 4K2R
LinkDB: 4K2R
Original site: 4K2R 
HEADER    TRANSFERASE                             09-APR-13   4K2R              
TITLE     STRUCTURAL BASIS FOR ACTIVATION OF ZAP-70 BY PHOSPHORYLATION OF THE   
TITLE    2 SH2-KINASE LINKER                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE ZAP-70;                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: 70 KDA ZETA-CHAIN ASSOCIATED PROTEIN, SYK-RELATED TYROSINE  
COMPND   5 KINASE;                                                              
COMPND   6 EC: 2.7.10.2;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 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                                        
KEYWDS    KINASE DOMAIN, SH2 DOMAIN, TRANSFERASE, ATP BINDING, CYTOPLAM         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Q.YAN,T.BARROS,P.R.VISPERAS,S.DEINDL,T.A.KADLECEK,A.WEISS,J.KURIYAN   
REVDAT   2   22-MAY-13 4K2R    1       JRNL                                     
REVDAT   1   08-MAY-13 4K2R    0                                                
JRNL        AUTH   Q.YAN,T.BARROS,P.R.VISPERAS,S.DEINDL,T.A.KADLECEK,A.WEISS,   
JRNL        AUTH 2 J.KURIYAN                                                    
JRNL        TITL   STRUCTURAL BASIS FOR ACTIVATION OF ZAP-70 BY PHOSPHORYLATION 
JRNL        TITL 2 OF THE SH2-KINASE LINKER.                                    
JRNL        REF    MOL.CELL.BIOL.                V.  33  2188 2013              
JRNL        REFN                   ISSN 0270-7306                               
JRNL        PMID   23530057                                                     
JRNL        DOI    10.1128/MCB.01637-12                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.09                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 11374                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.213                           
REMARK   3   R VALUE            (WORKING SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.287                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 579                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.08                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 835                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.17                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3280                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 51                           
REMARK   3   BIN FREE R VALUE                    : 0.3870                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4398                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 37                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 48.92                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.18000                                             
REMARK   3    B22 (A**2) : 0.04000                                              
REMARK   3    B33 (A**2) : 0.39000                                              
REMARK   3    B12 (A**2) : 0.36000                                              
REMARK   3    B13 (A**2) : 0.36000                                              
REMARK   3    B23 (A**2) : 0.06000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.558         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.446         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 55.031        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.906                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.827                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4544 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6141 ; 1.552 ; 1.984       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   548 ; 4.783 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   201 ;31.940 ;23.333       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   803 ;19.196 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    32 ;16.698 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   643 ; 0.088 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3422 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 10                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A    43                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.0917  -2.4825  23.3524              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1524 T22:   0.0566                                     
REMARK   3      T33:   0.1941 T12:  -0.0151                                     
REMARK   3      T13:  -0.0503 T23:  -0.0517                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6073 L22:   7.1417                                     
REMARK   3      L33:   7.9564 L12:  -1.4620                                     
REMARK   3      L13:   0.6181 L23:  -1.0923                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3767 S12:  -0.2589 S13:  -0.5618                       
REMARK   3      S21:  -0.0498 S22:  -0.0327 S23:   0.2929                       
REMARK   3      S31:   0.2349 S32:  -0.1225 S33:  -0.3440                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    44        A   114                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.5499   3.6825  23.0775              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0630 T22:   0.0454                                     
REMARK   3      T33:   0.1518 T12:   0.0210                                     
REMARK   3      T13:   0.0219 T23:   0.0381                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5523 L22:   5.9814                                     
REMARK   3      L33:   4.4126 L12:  -0.7022                                     
REMARK   3      L13:   1.1475 L23:  -1.2846                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0381 S12:   0.0210 S13:  -0.1925                       
REMARK   3      S21:   0.1342 S22:  -0.0770 S23:  -0.2614                       
REMARK   3      S31:   0.1846 S32:   0.1237 S33:   0.1151                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   115        A   174                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.4188  10.7647   0.5866              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1102 T22:   0.2189                                     
REMARK   3      T33:   0.0915 T12:  -0.0279                                     
REMARK   3      T13:   0.0254 T23:   0.0195                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9017 L22:   3.5872                                     
REMARK   3      L33:   2.7527 L12:  -1.7050                                     
REMARK   3      L13:  -1.6289 L23:   2.3832                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0626 S12:   0.1313 S13:   0.0079                       
REMARK   3      S21:  -0.2339 S22:  -0.0520 S23:   0.2323                       
REMARK   3      S31:  -0.1165 S32:  -0.2990 S33:  -0.0107                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   175        A   220                          
REMARK   3    ORIGIN FOR THE GROUP (A): -23.8860  21.4511  12.0110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1377 T22:   0.1752                                     
REMARK   3      T33:   0.1664 T12:  -0.0144                                     
REMARK   3      T13:   0.0848 T23:  -0.0859                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  14.4163 L22:   5.1897                                     
REMARK   3      L33:   3.9394 L12:   2.1074                                     
REMARK   3      L13:   3.3535 L23:  -2.7065                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1959 S12:   0.2809 S13:   1.0266                       
REMARK   3      S21:   0.0788 S22:  -0.1279 S23:   0.2233                       
REMARK   3      S31:  -0.3499 S32:   0.3418 S33:  -0.0680                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   221        A   327                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.8802   8.7172  -0.4168              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0604 T22:   0.3162                                     
REMARK   3      T33:   0.1691 T12:   0.0333                                     
REMARK   3      T13:  -0.0678 T23:  -0.0372                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2590 L22:   2.1151                                     
REMARK   3      L33:   2.7420 L12:  -0.8920                                     
REMARK   3      L13:  -1.8411 L23:   1.3739                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0679 S12:   0.1978 S13:   0.0369                       
REMARK   3      S21:  -0.2711 S22:  -0.0952 S23:   0.0894                       
REMARK   3      S31:  -0.1305 S32:  -0.2535 S33:   0.0273                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   328        A   386                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.2249  -7.5677 -32.9716              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4517 T22:   0.3439                                     
REMARK   3      T33:   0.0981 T12:  -0.0774                                     
REMARK   3      T13:  -0.0084 T23:   0.0254                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4846 L22:   9.5662                                     
REMARK   3      L33:   4.1951 L12:   1.2186                                     
REMARK   3      L13:  -0.8855 L23:  -0.1959                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0418 S12:   0.1261 S13:  -0.4827                       
REMARK   3      S21:  -0.3754 S22:  -0.1519 S23:  -0.6129                       
REMARK   3      S31:   0.4170 S32:  -0.0329 S33:   0.1936                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   387        A   479                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.7460  -5.8274 -16.3259              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0526 T22:   0.0876                                     
REMARK   3      T33:   0.1379 T12:   0.0377                                     
REMARK   3      T13:   0.0586 T23:   0.0307                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6727 L22:   3.6668                                     
REMARK   3      L33:   7.4008 L12:   0.1183                                     
REMARK   3      L13:   0.5981 L23:   0.9639                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0289 S12:   0.1033 S13:  -0.2152                       
REMARK   3      S21:  -0.0553 S22:   0.0929 S23:  -0.1322                       
REMARK   3      S31:   0.3532 S32:   0.1025 S33:  -0.0640                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   480        A   538                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.8265 -16.0314 -11.8865              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6005 T22:   0.2157                                     
REMARK   3      T33:   0.4649 T12:   0.0427                                     
REMARK   3      T13:   0.1981 T23:   0.0381                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1697 L22:   5.8470                                     
REMARK   3      L33:   2.5665 L12:  -3.0785                                     
REMARK   3      L13:   0.9355 L23:   0.3068                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3096 S12:   0.3589 S13:   0.0070                       
REMARK   3      S21:  -0.4426 S22:  -0.2228 S23:  -0.2276                       
REMARK   3      S31:   0.6459 S32:   0.4901 S33:  -0.0867                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   539        A   606                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.7553 -12.5947  -1.6503              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3699 T22:   0.1633                                     
REMARK   3      T33:   0.3074 T12:   0.0020                                     
REMARK   3      T13:  -0.1147 T23:   0.0562                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7701 L22:   4.3160                                     
REMARK   3      L33:   1.6558 L12:  -1.5206                                     
REMARK   3      L13:  -0.7661 L23:  -0.7115                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1566 S12:  -0.6113 S13:  -0.1543                       
REMARK   3      S21:   0.2488 S22:   0.1126 S23:  -0.5975                       
REMARK   3      S31:   0.3101 S32:   0.3764 S33:   0.0440                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   607        A   614                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.9381  16.6969  -4.4299              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9604 T22:   0.3616                                     
REMARK   3      T33:   0.4564 T12:   0.1319                                     
REMARK   3      T13:   0.0009 T23:  -0.0714                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  13.8604 L22:  50.5400                                     
REMARK   3      L33:   1.9200 L12: -26.3439                                     
REMARK   3      L13:  -5.0277 L23:   9.3491                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.7030 S12:   0.8587 S13:   0.2074                       
REMARK   3      S21:  -2.3035 S22:  -1.6646 S23:  -0.4330                       
REMARK   3      S31:  -1.0200 S32:  -0.3245 S33:  -0.0384                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4K2R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-APR-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB078817.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-FEB-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 9.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.3.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1159                             
REMARK 200  MONOCHROMATOR                  : KOHZU DOUBLE CRYSTAL, SI(111)      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11992                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.24000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.84                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PH 6.5, 20%               
REMARK 280  POLYETHYLENE GLYCOL MONOMETHYL ETHER 5,000, VAPOR DIFFUSION,        
REMARK 280  SITTING 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   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     LYS A   484                                                      
REMARK 465     ALA A   485                                                      
REMARK 465     LEU A   486                                                      
REMARK 465     GLY A   487                                                      
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 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     GLU A  85    OE1  OE2                                            
REMARK 470     ARG A 128    CZ   NH1  NH2                                       
REMARK 470     GLU A 139    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 244    CG   OD1  OD2                                       
REMARK 470     ASP A 327    CG   OD1  OD2                                       
REMARK 470     GLU A 431    CG   CD   OE1  OE2                                  
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   O    CYS A   596     CD1  LEU A   600              1.37            
REMARK 500   O    GLU A   194     OG1  THR A   197              1.92            
REMARK 500   O    HIS A   459     OD1  ASP A   521              2.00            
REMARK 500   O    TYR A   164     ND2  ASN A   256              2.03            
REMARK 500   O    ASN A   461     ND2  ASN A   466              2.08            
REMARK 500   OG   SER A   351     NH2  ARG A   353              2.10            
REMARK 500   OG   SER A    42     OE2  GLU A    62              2.13            
REMARK 500   NZ   LYS A   504     O    TYR A   540              2.17            
REMARK 500   O    ALA A   570     OD1  ASP A   574              2.17            
REMARK 500   O    ILE A   223     N    GLY A   226              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS A 443   CG    HIS A 443   CD2     0.064                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  72      118.21    -39.23                                   
REMARK 500    ARG A  99      -80.41   -126.71                                   
REMARK 500    PRO A 110      150.04    -47.98                                   
REMARK 500    LYS A 132       60.97     32.99                                   
REMARK 500    SER A 167       44.52   -143.73                                   
REMARK 500    GLN A 182       54.22    -91.08                                   
REMARK 500    GLU A 194      107.99    -51.48                                   
REMARK 500    LYS A 251      -88.36   -123.45                                   
REMARK 500    TYR A 319       47.74    -88.99                                   
REMARK 500    ASP A 327       72.35   -114.19                                   
REMARK 500    LYS A 328       78.35   -108.26                                   
REMARK 500    GLU A 376      -58.46     73.45                                   
REMARK 500    ALA A 378       59.75    -68.55                                   
REMARK 500    ALA A 387      -32.92    -39.19                                   
REMARK 500    ALA A 407     -123.21   -145.45                                   
REMARK 500    ALA A 417       69.66   -108.91                                   
REMARK 500    LYS A 429       34.93    -99.67                                   
REMARK 500    ASN A 461       52.42   -118.51                                   
REMARK 500    PRO A 502       10.24    -67.79                                   
REMARK 500    GLU A 509       -8.68    -54.74                                   
REMARK 500    LYS A 542        0.76     90.85                                   
REMARK 500    LYS A 544      160.94    177.52                                   
REMARK 500    PRO A 565      159.10    -48.65                                   
REMARK 500    TRP A 576       40.22   -104.84                                   
REMARK 500    SER A 608     -164.07   -104.01                                   
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 701  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ANP A 702   O2A                                                    
REMARK 620 2 ANP A 702   O2B 100.8                                              
REMARK 620 3 ASP A 479   OD2  78.5 120.5                                        
REMARK 620 4 ASN A 466   OD1 156.4  81.1  80.4                                  
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 MG A 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 703                 
DBREF  4K2R A    1   606  UNP    P43403   ZAP70_HUMAN      1    606             
SEQADV 4K2R ASN A  461  UNP  P43403    ASP   461 ENGINEERED MUTATION            
SEQADV 4K2R GLY A  607  UNP  P43403              EXPRESSION TAG                 
SEQADV 4K2R SER A  608  UNP  P43403              EXPRESSION TAG                 
SEQADV 4K2R GLY A  609  UNP  P43403              EXPRESSION TAG                 
SEQADV 4K2R LEU A  610  UNP  P43403              EXPRESSION TAG                 
SEQADV 4K2R GLU A  611  UNP  P43403              EXPRESSION TAG                 
SEQADV 4K2R VAL A  612  UNP  P43403              EXPRESSION TAG                 
SEQADV 4K2R LEU A  613  UNP  P43403              EXPRESSION TAG                 
SEQADV 4K2R PHE A  614  UNP  P43403              EXPRESSION TAG                 
SEQRES   1 A  614  MET PRO ASP PRO ALA ALA HIS LEU PRO PHE PHE TYR GLY          
SEQRES   2 A  614  SER ILE SER ARG ALA GLU ALA GLU GLU HIS LEU LYS LEU          
SEQRES   3 A  614  ALA GLY MET ALA ASP GLY LEU PHE LEU LEU ARG GLN CYS          
SEQRES   4 A  614  LEU ARG SER LEU GLY GLY TYR VAL LEU SER LEU VAL HIS          
SEQRES   5 A  614  ASP VAL ARG PHE HIS HIS PHE PRO ILE GLU ARG GLN LEU          
SEQRES   6 A  614  ASN GLY THR TYR ALA ILE ALA GLY GLY LYS ALA HIS CYS          
SEQRES   7 A  614  GLY PRO ALA GLU LEU CYS GLU PHE TYR SER ARG ASP PRO          
SEQRES   8 A  614  ASP GLY LEU PRO CYS ASN LEU ARG LYS PRO CYS ASN ARG          
SEQRES   9 A  614  PRO SER GLY LEU GLU PRO GLN PRO GLY VAL PHE ASP CYS          
SEQRES  10 A  614  LEU ARG ASP ALA MET VAL ARG ASP TYR VAL ARG GLN THR          
SEQRES  11 A  614  TRP LYS LEU GLU GLY GLU ALA LEU GLU GLN ALA ILE ILE          
SEQRES  12 A  614  SER GLN ALA PRO GLN VAL GLU LYS LEU ILE ALA THR THR          
SEQRES  13 A  614  ALA HIS GLU ARG MET PRO TRP TYR HIS SER SER LEU THR          
SEQRES  14 A  614  ARG GLU GLU ALA GLU ARG LYS LEU TYR SER GLY ALA GLN          
SEQRES  15 A  614  THR ASP GLY LYS PHE LEU LEU ARG PRO ARG LYS GLU GLN          
SEQRES  16 A  614  GLY THR TYR ALA LEU SER LEU ILE TYR GLY LYS THR VAL          
SEQRES  17 A  614  TYR HIS TYR LEU ILE SER GLN ASP LYS ALA GLY LYS TYR          
SEQRES  18 A  614  CYS ILE PRO GLU GLY THR LYS PHE ASP THR LEU TRP GLN          
SEQRES  19 A  614  LEU VAL GLU TYR LEU LYS LEU LYS ALA ASP GLY LEU ILE          
SEQRES  20 A  614  TYR CYS LEU LYS GLU ALA CYS PRO ASN SER SER ALA SER          
SEQRES  21 A  614  ASN ALA SER GLY ALA ALA ALA PRO THR LEU PRO ALA HIS          
SEQRES  22 A  614  PRO SER THR LEU THR HIS PRO GLN ARG ARG ILE ASP THR          
SEQRES  23 A  614  LEU ASN SER ASP GLY TYR THR PRO GLU PRO ALA ARG ILE          
SEQRES  24 A  614  THR SER PRO ASP LYS PRO ARG PRO MET PRO MET ASP THR          
SEQRES  25 A  614  SER VAL TYR GLU SER PRO TYR SER ASP PRO GLU GLU LEU          
SEQRES  26 A  614  LYS ASP LYS LYS LEU PHE LEU LYS ARG ASP ASN LEU LEU          
SEQRES  27 A  614  ILE ALA ASP ILE GLU LEU GLY CYS GLY ASN PHE GLY SER          
SEQRES  28 A  614  VAL ARG GLN GLY VAL TYR ARG MET ARG LYS LYS GLN ILE          
SEQRES  29 A  614  ASP VAL ALA ILE LYS VAL LEU LYS GLN GLY THR GLU LYS          
SEQRES  30 A  614  ALA ASP THR GLU GLU MET MET ARG GLU ALA GLN ILE MET          
SEQRES  31 A  614  HIS GLN LEU ASP ASN PRO TYR ILE VAL ARG LEU ILE GLY          
SEQRES  32 A  614  VAL CYS GLN ALA GLU ALA LEU MET LEU VAL MET GLU MET          
SEQRES  33 A  614  ALA GLY GLY GLY PRO LEU HIS LYS PHE LEU VAL GLY LYS          
SEQRES  34 A  614  ARG GLU GLU ILE PRO VAL SER ASN VAL ALA GLU LEU LEU          
SEQRES  35 A  614  HIS GLN VAL SER MET GLY MET LYS TYR LEU GLU GLU LYS          
SEQRES  36 A  614  ASN PHE VAL HIS ARG ASN LEU ALA ALA ARG ASN VAL LEU          
SEQRES  37 A  614  LEU VAL ASN ARG HIS TYR ALA LYS ILE SER ASP PHE GLY          
SEQRES  38 A  614  LEU SER LYS ALA LEU GLY ALA ASP ASP SER TYR TYR THR          
SEQRES  39 A  614  ALA ARG SER ALA GLY LYS TRP PRO LEU LYS TRP TYR ALA          
SEQRES  40 A  614  PRO GLU CYS ILE ASN PHE ARG LYS PHE SER SER ARG SER          
SEQRES  41 A  614  ASP VAL TRP SER TYR GLY VAL THR MET TRP GLU ALA LEU          
SEQRES  42 A  614  SER TYR GLY GLN LYS PRO TYR LYS LYS MET LYS GLY PRO          
SEQRES  43 A  614  GLU VAL MET ALA PHE ILE GLU GLN GLY LYS ARG MET GLU          
SEQRES  44 A  614  CYS PRO PRO GLU CYS PRO PRO GLU LEU TYR ALA LEU MET          
SEQRES  45 A  614  SER ASP CYS TRP ILE TYR LYS TRP GLU ASP ARG PRO ASP          
SEQRES  46 A  614  PHE LEU THR VAL GLU GLN ARG MET ARG ALA CYS TYR TYR          
SEQRES  47 A  614  SER LEU ALA SER LYS VAL GLU GLY GLY SER GLY LEU GLU          
SEQRES  48 A  614  VAL LEU PHE                                                  
HET     MG  A 701       1                                                       
HET    ANP  A 702      31                                                       
HET    PO4  A 703       5                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL   2   MG    MG 2+                                                        
FORMUL   3  ANP    C10 H17 N6 O12 P3                                            
FORMUL   4  PO4    O4 P 3-                                                      
HELIX    1   1 SER A   16  ALA A   27  1                                  12    
HELIX    2   2 GLY A   79  ASP A   90  1                                  12    
HELIX    3   3 GLY A  113  TRP A  131  1                                  19    
HELIX    4   4 GLY A  135  THR A  156  1                                  22    
HELIX    5   5 ALA A  157  MET A  161  5                                   5    
HELIX    6   6 THR A  169  GLY A  180  1                                  12    
HELIX    7   7 THR A  231  LYS A  240  1                                  10    
HELIX    8   8 MET A  308  THR A  312  5                                   5    
HELIX    9   9 SER A  317  SER A  320  5                                   4    
HELIX   10  10 ASP A  321  ASP A  327  1                                   7    
HELIX   11  11 LYS A  333  ASP A  335  5                                   3    
HELIX   12  12 ASP A  379  HIS A  391  1                                  13    
HELIX   13  13 PRO A  421  VAL A  427  1                                   7    
HELIX   14  14 PRO A  434  LYS A  455  1                                  22    
HELIX   15  15 ALA A  463  ARG A  465  5                                   3    
HELIX   16  16 ALA A  507  ARG A  514  1                                   8    
HELIX   17  17 SER A  517  SER A  534  1                                  18    
HELIX   18  18 GLY A  545  GLN A  554  1                                  10    
HELIX   19  19 PRO A  565  CYS A  575  1                                  11    
HELIX   20  20 ASP A  585  SER A  602  1                                  18    
SHEET    1   A 5 TYR A  69  ILE A  71  0                                        
SHEET    2   A 5 ARG A  55  ARG A  63 -1  N  GLU A  62   O  ALA A  70           
SHEET    3   A 5 TYR A  46  HIS A  52 -1  N  LEU A  48   O  PHE A  59           
SHEET    4   A 5 LEU A  33  GLN A  38 -1  N  ARG A  37   O  VAL A  47           
SHEET    5   A 5 LYS A 100  PRO A 101  1  O  LYS A 100   N  PHE A  34           
SHEET    1   B 5 PHE A 187  PRO A 191  0                                        
SHEET    2   B 5 TYR A 198  TYR A 204 -1  O  ALA A 199   N  ARG A 190           
SHEET    3   B 5 THR A 207  GLN A 215 -1  O  TYR A 209   N  LEU A 202           
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 GLY A 350  ARG A 358 -1  O  VAL A 356   N  LEU A 338           
SHEET    3   C 5 GLN A 363  LEU A 371 -1  O  ILE A 364   N  TYR A 357           
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  TYR A 474   N  VAL A 470           
LINK        MG    MG A 701                 O2A ANP A 702     1555   1555  2.26  
LINK        MG    MG A 701                 O2B ANP A 702     1555   1555  2.39  
LINK         OD2 ASP A 479                MG    MG A 701     1555   1555  2.43  
LINK         OD1 ASN A 466                MG    MG A 701     1555   1555  2.58  
SITE     1 AC1  4 ARG A 465  ASN A 466  ASP A 479  ANP A 702                    
SITE     1 AC2 14 LEU A 344  GLY A 347  PHE A 349  VAL A 352                    
SITE     2 AC2 14 ALA A 367  LYS A 369  GLU A 415  ALA A 417                    
SITE     3 AC2 14 PRO A 421  ARG A 465  ASN A 466  LEU A 468                    
SITE     4 AC2 14 ASP A 479   MG A 701                                          
SITE     1 AC3  4 ARG A 170  ARG A 190  ARG A 192  ALA A 199                    
CRYST1   48.530   53.150   68.960 106.10  93.26 104.40 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      0.020606  0.005291  0.002903        0.00000                         
SCALE2      0.000000  0.019425  0.006140        0.00000                         
SCALE3      0.000000  0.000000  0.015233        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system