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Database: PDB
Entry: 6N9G
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HEADER    SIGNALING PROTEIN                       03-DEC-18   6N9G              
TITLE     CRYSTAL STRUCTURE OF RGS7-GBETA5 DIMER                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: REGULATOR OF G-PROTEIN SIGNALING 7;                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: RGS7;                                                       
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN SUBUNIT BETA-5;         
COMPND   8 CHAIN: C, D;                                                         
COMPND   9 SYNONYM: GBETA5,TRANSDUCIN BETA CHAIN 5;                             
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   3 ORGANISM_COMMON: BOVINE;                                             
SOURCE   4 ORGANISM_TAXID: 9913;                                                
SOURCE   5 GENE: RGS7;                                                          
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  10 ORGANISM_COMMON: MOUSE;                                              
SOURCE  11 ORGANISM_TAXID: 10090;                                               
SOURCE  12 GENE: GNB5;                                                          
SOURCE  13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    RGS, G PROTEIN SIGNALING, SIGNALING PROTEIN                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.N.PATIL,E.RANGARAJAN,T.IZARD,K.A.MARTEMYANOV                        
REVDAT   1   09-JAN-19 6N9G    0                                                
JRNL        AUTH   D.N.PATIL,E.S.RANGARAJAN,S.J.NOVICK,B.D.PASCAL,D.J.KOJETIN,  
JRNL        AUTH 2 P.R.GRIFFIN,T.IZARD,K.A.MARTEMYANOV                          
JRNL        TITL   STRUCTURAL ORGANIZATION OF A MAJOR NEURONAL G PROTEIN        
JRNL        TITL 2 REGULATOR, THE RGS7-G BETA 5-R7BP COMPLEX.                   
JRNL        REF    ELIFE                         V.   7       2018              
JRNL        REFN                   ESSN 2050-084X                               
JRNL        PMID   30540250                                                     
JRNL        DOI    10.7554/ELIFE.42150                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.13 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.13_2998: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.13                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.54                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.370                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 46.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 54330                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.176                           
REMARK   3   R VALUE            (WORKING SET) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.217                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2610                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 37.5404 -  5.6737    0.99     5898   309  0.1664 0.1908        
REMARK   3     2  5.6737 -  4.5058    1.00     5849   314  0.1348 0.1680        
REMARK   3     3  4.5058 -  3.9369    1.00     5852   267  0.1307 0.1695        
REMARK   3     4  3.9369 -  3.5773    1.00     5831   309  0.1612 0.2217        
REMARK   3     5  3.5773 -  3.3210    0.99     5727   303  0.1886 0.2359        
REMARK   3     6  3.3210 -  3.1253    0.86     5058   262  0.2159 0.2800        
REMARK   3     7  3.1253 -  2.9689    0.72     4242   199  0.2347 0.2999        
REMARK   3     8  2.9689 -  2.8397    0.60     3516   150  0.2508 0.3125        
REMARK   3     9  2.8397 -  2.7304    0.43     2486   140  0.2648 0.2701        
REMARK   3    10  2.7304 -  2.6362    0.33     1940   100  0.2843 0.3219        
REMARK   3    11  2.6362 -  2.5538    0.27     1573    82  0.2907 0.3421        
REMARK   3    12  2.5538 -  2.4808    0.21     1206    56  0.3087 0.3702        
REMARK   3    13  2.4808 -  2.4155    0.15      906    40  0.2865 0.3497        
REMARK   3    14  2.4155 -  2.3566    0.11      634    27  0.3133 0.3557        
REMARK   3    15  2.3566 -  2.3030    0.07      425    26  0.3500 0.4515        
REMARK   3    16  2.3030 -  2.2540    0.04      250     9  0.3113 0.4426        
REMARK   3    17  2.2540 -  2.2090    0.03      149     5  0.3634 0.3425        
REMARK   3    18  2.2090 -  2.1673    0.02      103     6  0.3621 0.3935        
REMARK   3    19  2.1673 -  2.1286    0.01       75     6  0.2961 0.4508        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.250            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.930           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 50.08                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002          12336                                  
REMARK   3   ANGLE     :  0.488          16690                                  
REMARK   3   CHIRALITY :  0.040           1783                                  
REMARK   3   PLANARITY :  0.003           2160                                  
REMARK   3   DIHEDRAL  : 17.819           7421                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 14                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 18 THROUGH 107 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  10.7663  29.0425   5.8063              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3698 T22:   0.3095                                     
REMARK   3      T33:   0.5893 T12:  -0.0376                                     
REMARK   3      T13:   0.1474 T23:  -0.0994                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9999 L22:   4.8680                                     
REMARK   3      L33:   1.9795 L12:  -1.2705                                     
REMARK   3      L13:   1.3497 L23:  -1.7773                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0112 S12:  -0.4889 S13:   0.5058                       
REMARK   3      S21:   0.5727 S22:  -0.0195 S23:   0.6145                       
REMARK   3      S31:  -0.0152 S32:  -0.4707 S33:   0.0774                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 108 THROUGH 200 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   1.8323  32.1282 -15.6674              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2877 T22:   0.3761                                     
REMARK   3      T33:   0.5311 T12:  -0.0123                                     
REMARK   3      T13:  -0.0487 T23:   0.0206                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5930 L22:   1.6300                                     
REMARK   3      L33:   5.0123 L12:  -0.3384                                     
REMARK   3      L13:   0.1276 L23:  -1.0299                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0278 S12:   0.2272 S13:   0.0660                       
REMARK   3      S21:  -0.1462 S22:  -0.0747 S23:   0.3798                       
REMARK   3      S31:   0.1989 S32:  -0.8274 S33:  -0.2067                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 201 THROUGH 317 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  29.4388  -0.8427   5.7866              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5225 T22:   0.2146                                     
REMARK   3      T33:   0.3791 T12:  -0.0828                                     
REMARK   3      T13:  -0.1336 T23:  -0.0385                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9297 L22:   1.5538                                     
REMARK   3      L33:   1.1080 L12:  -0.3296                                     
REMARK   3      L13:  -0.5027 L23:  -0.8280                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0546 S12:  -0.1822 S13:  -0.0545                       
REMARK   3      S21:   0.1568 S22:  -0.0567 S23:  -0.0619                       
REMARK   3      S31:   0.2823 S32:  -0.0037 S33:   0.0412                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 318 THROUGH 450 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  50.3827 -18.9283   2.3093              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3796 T22:   0.1942                                     
REMARK   3      T33:   0.6397 T12:   0.0036                                     
REMARK   3      T13:  -0.2233 T23:   0.0822                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5034 L22:   2.9544                                     
REMARK   3      L33:   3.9714 L12:   0.1595                                     
REMARK   3      L13:   0.3800 L23:   2.0587                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0775 S12:  -0.1492 S13:  -0.2069                       
REMARK   3      S21:   0.0751 S22:   0.0262 S23:  -0.8617                       
REMARK   3      S31:  -0.0277 S32:  -0.2203 S33:  -0.1092                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 18 THROUGH 58 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  40.8406  36.9038 -45.3927              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9530 T22:   1.0790                                     
REMARK   3      T33:   1.6233 T12:   0.0338                                     
REMARK   3      T13:   0.3253 T23:   0.5235                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1647 L22:   2.5016                                     
REMARK   3      L33:   3.9983 L12:  -1.6908                                     
REMARK   3      L13:   2.3692 L23:  -0.5669                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5287 S12:   0.4956 S13:   0.0874                       
REMARK   3      S21:  -0.2478 S22:  -0.6077 S23:  -1.0883                       
REMARK   3      S31:   0.2044 S32:   1.1745 S33:   0.1492                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 59 THROUGH 182 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  33.0915  28.2588 -35.9387              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5909 T22:   0.5776                                     
REMARK   3      T33:   1.0626 T12:   0.0439                                     
REMARK   3      T13:   0.1703 T23:   0.3384                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5844 L22:   4.9356                                     
REMARK   3      L33:   3.7675 L12:   0.1241                                     
REMARK   3      L13:  -0.3481 L23:  -2.9974                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0292 S12:   0.5115 S13:   0.7826                       
REMARK   3      S21:  -0.6890 S22:  -0.3538 S23:  -1.3137                       
REMARK   3      S31:   0.2793 S32:   0.4731 S33:   0.3346                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 183 THROUGH 317 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  15.7082  52.7988 -48.4320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6677 T22:   0.5013                                     
REMARK   3      T33:   0.8258 T12:  -0.0866                                     
REMARK   3      T13:  -0.0864 T23:   0.2319                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7605 L22:   1.3467                                     
REMARK   3      L33:   1.8586 L12:  -0.4890                                     
REMARK   3      L13:  -0.2398 L23:   0.0170                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1405 S12:   0.2276 S13:   0.2159                       
REMARK   3      S21:  -0.4818 S22:  -0.2898 S23:  -0.4835                       
REMARK   3      S31:  -0.2713 S32:   0.0350 S33:   0.4442                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 318 THROUGH 450 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -12.5673  76.1520 -48.5890              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9602 T22:   0.5912                                     
REMARK   3      T33:   0.5926 T12:   0.2035                                     
REMARK   3      T13:  -0.3236 T23:   0.0200                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9171 L22:   3.9422                                     
REMARK   3      L33:   2.4644 L12:   1.4299                                     
REMARK   3      L13:   1.5915 L23:  -0.5058                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3871 S12:  -0.2850 S13:   0.3557                       
REMARK   3      S21:   0.2618 S22:   0.1724 S23:  -0.1269                       
REMARK   3      S31:  -0.4913 S32:  -0.4210 S33:   0.2161                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 3 THROUGH 118 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   9.6950  54.8294 -47.6758              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6460 T22:   0.3201                                     
REMARK   3      T33:   0.7107 T12:   0.0016                                     
REMARK   3      T13:  -0.2097 T23:   0.1934                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3260 L22:   1.2609                                     
REMARK   3      L33:   2.3840 L12:  -0.4130                                     
REMARK   3      L13:   0.4532 L23:   0.3043                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2510 S12:   0.3864 S13:   0.1634                       
REMARK   3      S21:  -0.3863 S22:  -0.2687 S23:  -0.5468                       
REMARK   3      S31:  -0.4017 S32:   0.0326 S33:   0.3457                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 119 THROUGH 216 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.5480  49.8295 -42.0136              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6044 T22:   0.3812                                     
REMARK   3      T33:   0.3780 T12:  -0.0068                                     
REMARK   3      T13:  -0.2720 T23:   0.0027                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8425 L22:   6.4556                                     
REMARK   3      L33:   6.2052 L12:  -0.4497                                     
REMARK   3      L13:  -0.6513 L23:  -0.7477                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2169 S12:  -0.0150 S13:   0.1003                       
REMARK   3      S21:  -0.4746 S22:   0.0039 S23:   0.4021                       
REMARK   3      S31:   0.0062 S32:  -0.6444 S33:   0.1254                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 217 THROUGH 353 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  14.4351  55.9221 -47.6855              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8807 T22:   0.3675                                     
REMARK   3      T33:   0.8898 T12:   0.0231                                     
REMARK   3      T13:  -0.0431 T23:   0.3514                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4308 L22:   2.0539                                     
REMARK   3      L33:   1.8708 L12:   0.1501                                     
REMARK   3      L13:  -0.0387 L23:  -0.4141                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1431 S12:   0.6949 S13:   0.1311                       
REMARK   3      S21:  -0.8998 S22:  -0.5068 S23:  -1.1558                       
REMARK   3      S31:  -0.2047 S32:   0.3300 S33:   0.3115                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 2 THROUGH 172 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  30.1886  -0.1755  -4.9594              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2889 T22:   0.1600                                     
REMARK   3      T33:   0.2414 T12:   0.0100                                     
REMARK   3      T13:  -0.1118 T23:   0.0240                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9150 L22:   2.4789                                     
REMARK   3      L33:   0.8124 L12:   0.4661                                     
REMARK   3      L13:  -0.1471 L23:  -0.1602                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1242 S12:   0.0450 S13:   0.0189                       
REMARK   3      S21:   0.0123 S22:  -0.1080 S23:  -0.2703                       
REMARK   3      S31:  -0.0715 S32:   0.0392 S33:   0.0345                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 173 THROUGH 216 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  28.9446  -9.5314  -8.3393              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4001 T22:   0.1488                                     
REMARK   3      T33:   0.2482 T12:  -0.0850                                     
REMARK   3      T13:  -0.1509 T23:   0.0382                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1174 L22:   4.7798                                     
REMARK   3      L33:   5.2315 L12:  -0.6058                                     
REMARK   3      L13:  -1.9324 L23:   1.1842                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3478 S12:  -0.0379 S13:  -0.4111                       
REMARK   3      S21:   0.0118 S22:  -0.1526 S23:   0.1845                       
REMARK   3      S31:   0.3476 S32:   0.0800 S33:  -0.1690                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 217 THROUGH 353 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  27.1120   4.9019   4.2346              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3154 T22:   0.1723                                     
REMARK   3      T33:   0.2367 T12:  -0.0702                                     
REMARK   3      T13:  -0.0622 T23:   0.0010                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8645 L22:   2.5725                                     
REMARK   3      L33:   1.3341 L12:  -0.6907                                     
REMARK   3      L13:  -0.1320 L23:  -0.2227                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0460 S12:  -0.2075 S13:   0.0629                       
REMARK   3      S21:   0.3870 S22:  -0.0802 S23:  -0.0467                       
REMARK   3      S31:   0.0800 S32:  -0.1261 S33:   0.0133                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6N9G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-DEC-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000237326.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-OCT-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 80                                 
REMARK 200  PH                             : 6.25                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-300                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AUTOPROC                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 54345                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.129                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 94.280                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.06400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.13                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.48                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.81700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 2PBI                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.54                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM MALONATE (PH 6.25) AND 10%   
REMARK 280  W/V POLYETHYLENE GLYCOL 3,350, VAPOR DIFFUSION, TEMPERATURE 277K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       81.38000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8160 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 34660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8310 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 34780 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C                                  
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     ALA A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     ASN A     5                                                      
REMARK 465     ASN A     6                                                      
REMARK 465     TYR A     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     GLN A     9                                                      
REMARK 465     THR A    10                                                      
REMARK 465     SER A    11                                                      
REMARK 465     ASN A    12                                                      
REMARK 465     GLY A    13                                                      
REMARK 465     VAL A    14                                                      
REMARK 465     ALA A    15                                                      
REMARK 465     ASP A    16                                                      
REMARK 465     GLU A    17                                                      
REMARK 465     ARG A   219                                                      
REMARK 465     MET A   220                                                      
REMARK 465     ARG A   221                                                      
REMARK 465     ASN A   222                                                      
REMARK 465     PRO A   223                                                      
REMARK 465     HIS A   224                                                      
REMARK 465     LYS A   225                                                      
REMARK 465     THR A   226                                                      
REMARK 465     ARG A   227                                                      
REMARK 465     LYS A   228                                                      
REMARK 465     SER A   229                                                      
REMARK 465     VAL A   230                                                      
REMARK 465     TYR A   231                                                      
REMARK 465     GLY A   232                                                      
REMARK 465     LEU A   233                                                      
REMARK 465     GLN A   234                                                      
REMARK 465     ASN A   235                                                      
REMARK 465     ASP A   236                                                      
REMARK 465     ILE A   237                                                      
REMARK 465     ARG A   238                                                      
REMARK 465     SER A   239                                                      
REMARK 465     HIS A   240                                                      
REMARK 465     SER A   241                                                      
REMARK 465     PRO A   242                                                      
REMARK 465     THR A   243                                                      
REMARK 465     HIS A   244                                                      
REMARK 465     THR A   245                                                      
REMARK 465     PRO A   246                                                      
REMARK 465     THR A   247                                                      
REMARK 465     PRO A   248                                                      
REMARK 465     GLU A   249                                                      
REMARK 465     THR A   250                                                      
REMARK 465     LYS A   251                                                      
REMARK 465     LYS A   451                                                      
REMARK 465     LYS A   452                                                      
REMARK 465     LYS A   453                                                      
REMARK 465     GLY A   454                                                      
REMARK 465     LYS A   455                                                      
REMARK 465     SER A   456                                                      
REMARK 465     LEU A   457                                                      
REMARK 465     THR A   458                                                      
REMARK 465     SER A   459                                                      
REMARK 465     LYS A   460                                                      
REMARK 465     ARG A   461                                                      
REMARK 465     LEU A   462                                                      
REMARK 465     THR A   463                                                      
REMARK 465     SER A   464                                                      
REMARK 465     LEU A   465                                                      
REMARK 465     VAL A   466                                                      
REMARK 465     GLN A   467                                                      
REMARK 465     SER A   468                                                      
REMARK 465     TYR A   469                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     GLN B     3                                                      
REMARK 465     GLY B     4                                                      
REMARK 465     ASN B     5                                                      
REMARK 465     ASN B     6                                                      
REMARK 465     TYR B     7                                                      
REMARK 465     GLY B     8                                                      
REMARK 465     GLN B     9                                                      
REMARK 465     THR B    10                                                      
REMARK 465     SER B    11                                                      
REMARK 465     ASN B    12                                                      
REMARK 465     GLY B    13                                                      
REMARK 465     VAL B    14                                                      
REMARK 465     ALA B    15                                                      
REMARK 465     ASP B    16                                                      
REMARK 465     GLU B    17                                                      
REMARK 465     ARG B   219                                                      
REMARK 465     MET B   220                                                      
REMARK 465     ARG B   221                                                      
REMARK 465     ASN B   222                                                      
REMARK 465     PRO B   223                                                      
REMARK 465     HIS B   224                                                      
REMARK 465     LYS B   225                                                      
REMARK 465     THR B   226                                                      
REMARK 465     ARG B   227                                                      
REMARK 465     LYS B   228                                                      
REMARK 465     SER B   229                                                      
REMARK 465     VAL B   230                                                      
REMARK 465     TYR B   231                                                      
REMARK 465     GLY B   232                                                      
REMARK 465     LEU B   233                                                      
REMARK 465     GLN B   234                                                      
REMARK 465     ASN B   235                                                      
REMARK 465     ASP B   236                                                      
REMARK 465     ILE B   237                                                      
REMARK 465     ARG B   238                                                      
REMARK 465     SER B   239                                                      
REMARK 465     HIS B   240                                                      
REMARK 465     SER B   241                                                      
REMARK 465     PRO B   242                                                      
REMARK 465     THR B   243                                                      
REMARK 465     HIS B   244                                                      
REMARK 465     THR B   245                                                      
REMARK 465     PRO B   246                                                      
REMARK 465     THR B   247                                                      
REMARK 465     PRO B   248                                                      
REMARK 465     GLU B   249                                                      
REMARK 465     THR B   250                                                      
REMARK 465     LYS B   451                                                      
REMARK 465     LYS B   452                                                      
REMARK 465     LYS B   453                                                      
REMARK 465     GLY B   454                                                      
REMARK 465     LYS B   455                                                      
REMARK 465     SER B   456                                                      
REMARK 465     LEU B   457                                                      
REMARK 465     THR B   458                                                      
REMARK 465     SER B   459                                                      
REMARK 465     LYS B   460                                                      
REMARK 465     ARG B   461                                                      
REMARK 465     LEU B   462                                                      
REMARK 465     THR B   463                                                      
REMARK 465     SER B   464                                                      
REMARK 465     LEU B   465                                                      
REMARK 465     VAL B   466                                                      
REMARK 465     GLN B   467                                                      
REMARK 465     SER B   468                                                      
REMARK 465     TYR B   469                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     MET D     1                                                      
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    ASN A 119       40.95    -93.40                                   
REMARK 500    CYS A 120       71.67     52.11                                   
REMARK 500    PHE A 160       40.89    -96.57                                   
REMARK 500    SER A 356       32.82   -149.55                                   
REMARK 500    SER A 395       59.85   -116.95                                   
REMARK 500    ASP A 433      -70.53   -130.13                                   
REMARK 500    ASP B 104     -159.47   -160.64                                   
REMARK 500    ASN B 119       35.46    -90.07                                   
REMARK 500    CYS B 120       77.96     52.45                                   
REMARK 500    PHE B 160       43.48    -99.64                                   
REMARK 500    SER B 356       37.52   -149.46                                   
REMARK 500    SER B 395       59.87   -113.97                                   
REMARK 500    ASP B 433      -68.22   -134.16                                   
REMARK 500    PHE C 136       44.71    -90.82                                   
REMARK 500    ASN C 139       33.04    -95.51                                   
REMARK 500    THR C 162     -142.70    -89.00                                   
REMARK 500    ASN C 210       48.54    -90.95                                   
REMARK 500    HIS C 347        6.00     81.61                                   
REMARK 500    ASP D   4     -149.05   -122.31                                   
REMARK 500    VAL D 149      -69.25   -109.61                                   
REMARK 500    MET D 151      116.71   -160.16                                   
REMARK 500    THR D 162     -143.08    -82.97                                   
REMARK 500    SER D 206      104.85    -58.76                                   
REMARK 500    ASN D 210       52.10    -93.71                                   
REMARK 500    HIS D 347        6.48     80.20                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  6N9G A    1   469  UNP    O46470   RGS7_BOVIN       1    469             
DBREF  6N9G B    1   469  UNP    O46470   RGS7_BOVIN       1    469             
DBREF  6N9G C    1   353  UNP    P62881   GNB5_MOUSE      43    395             
DBREF  6N9G D    1   353  UNP    P62881   GNB5_MOUSE      43    395             
SEQRES   1 A  469  MET ALA GLN GLY ASN ASN TYR GLY GLN THR SER ASN GLY          
SEQRES   2 A  469  VAL ALA ASP GLU SER PRO ASN MET LEU VAL TYR ARG LYS          
SEQRES   3 A  469  MET GLU ASP VAL ILE ALA ARG MET GLN ASP GLU LYS ASN          
SEQRES   4 A  469  GLY ILE PRO ILE ARG THR VAL LYS SER PHE LEU SER LYS          
SEQRES   5 A  469  ILE PRO SER VAL PHE SER GLY SER ASP ILE VAL GLN TRP          
SEQRES   6 A  469  LEU ILE LYS ASN LEU THR ILE GLU ASP PRO VAL GLU ALA          
SEQRES   7 A  469  LEU HIS LEU GLY THR LEU MET ALA ALA HIS GLY TYR PHE          
SEQRES   8 A  469  PHE PRO ILE SER ASP HIS VAL LEU THR LEU LYS ASP ASP          
SEQRES   9 A  469  GLY THR PHE TYR ARG PHE GLN THR PRO TYR PHE TRP PRO          
SEQRES  10 A  469  SER ASN CYS TRP GLU PRO GLU ASN THR ASP TYR ALA VAL          
SEQRES  11 A  469  TYR LEU CYS LYS ARG THR MET GLN ASN LYS ALA ARG LEU          
SEQRES  12 A  469  GLU LEU ALA ASP TYR GLU ALA GLU SER LEU ALA ARG LEU          
SEQRES  13 A  469  GLN ARG ALA PHE ALA ARG LYS TRP GLU PHE ILE PHE MET          
SEQRES  14 A  469  GLN ALA GLU ALA GLN ALA LYS VAL ASP LYS LYS ARG ASP          
SEQRES  15 A  469  LYS ILE GLU ARG LYS ILE LEU ASP SER GLN GLU ARG ALA          
SEQRES  16 A  469  PHE TRP ASP VAL HIS ARG PRO VAL PRO GLY CYS VAL ASN          
SEQRES  17 A  469  THR THR GLU VAL ASP ILE LYS LYS SER SER ARG MET ARG          
SEQRES  18 A  469  ASN PRO HIS LYS THR ARG LYS SER VAL TYR GLY LEU GLN          
SEQRES  19 A  469  ASN ASP ILE ARG SER HIS SER PRO THR HIS THR PRO THR          
SEQRES  20 A  469  PRO GLU THR LYS PRO PRO THR GLU ASP GLU LEU GLN GLN          
SEQRES  21 A  469  GLN ILE LYS TYR TRP GLN ILE GLN LEU ASP ARG HIS ARG          
SEQRES  22 A  469  LEU LYS MET SER LYS VAL ALA ASP SER LEU LEU SER TYR          
SEQRES  23 A  469  THR GLU GLN TYR VAL GLU TYR ASP PRO PHE LEU ALA PRO          
SEQRES  24 A  469  PRO ASP PRO SER ASN PRO TRP LEU SER ASP ASP THR THR          
SEQRES  25 A  469  PHE TRP GLU LEU GLU ALA SER LYS GLU PRO SER GLN GLN          
SEQRES  26 A  469  ARG VAL LYS ARG TRP GLY PHE GLY MET ASP GLU ALA LEU          
SEQRES  27 A  469  LYS ASP PRO VAL GLY ARG GLU GLN PHE LEU LYS PHE LEU          
SEQRES  28 A  469  GLU SER GLU PHE SER SER GLU ASN LEU ARG PHE TRP LEU          
SEQRES  29 A  469  ALA VAL GLU ASP LEU LYS LYS ARG PRO ILE ARG GLU VAL          
SEQRES  30 A  469  PRO SER ARG VAL GLN GLU ILE TRP GLN GLU PHE LEU ALA          
SEQRES  31 A  469  PRO GLY ALA PRO SER ALA ILE ASN LEU ASP SER LYS SER          
SEQRES  32 A  469  TYR ASP LYS THR THR GLN ASN VAL LYS GLU PRO GLY ARG          
SEQRES  33 A  469  TYR THR PHE GLU ASP ALA GLN GLU HIS ILE TYR LYS LEU          
SEQRES  34 A  469  MET LYS SER ASP SER TYR PRO ARG PHE ILE ARG SER SER          
SEQRES  35 A  469  ALA TYR GLN GLU LEU LEU GLN ALA LYS LYS LYS GLY LYS          
SEQRES  36 A  469  SER LEU THR SER LYS ARG LEU THR SER LEU VAL GLN SER          
SEQRES  37 A  469  TYR                                                          
SEQRES   1 B  469  MET ALA GLN GLY ASN ASN TYR GLY GLN THR SER ASN GLY          
SEQRES   2 B  469  VAL ALA ASP GLU SER PRO ASN MET LEU VAL TYR ARG LYS          
SEQRES   3 B  469  MET GLU ASP VAL ILE ALA ARG MET GLN ASP GLU LYS ASN          
SEQRES   4 B  469  GLY ILE PRO ILE ARG THR VAL LYS SER PHE LEU SER LYS          
SEQRES   5 B  469  ILE PRO SER VAL PHE SER GLY SER ASP ILE VAL GLN TRP          
SEQRES   6 B  469  LEU ILE LYS ASN LEU THR ILE GLU ASP PRO VAL GLU ALA          
SEQRES   7 B  469  LEU HIS LEU GLY THR LEU MET ALA ALA HIS GLY TYR PHE          
SEQRES   8 B  469  PHE PRO ILE SER ASP HIS VAL LEU THR LEU LYS ASP ASP          
SEQRES   9 B  469  GLY THR PHE TYR ARG PHE GLN THR PRO TYR PHE TRP PRO          
SEQRES  10 B  469  SER ASN CYS TRP GLU PRO GLU ASN THR ASP TYR ALA VAL          
SEQRES  11 B  469  TYR LEU CYS LYS ARG THR MET GLN ASN LYS ALA ARG LEU          
SEQRES  12 B  469  GLU LEU ALA ASP TYR GLU ALA GLU SER LEU ALA ARG LEU          
SEQRES  13 B  469  GLN ARG ALA PHE ALA ARG LYS TRP GLU PHE ILE PHE MET          
SEQRES  14 B  469  GLN ALA GLU ALA GLN ALA LYS VAL ASP LYS LYS ARG ASP          
SEQRES  15 B  469  LYS ILE GLU ARG LYS ILE LEU ASP SER GLN GLU ARG ALA          
SEQRES  16 B  469  PHE TRP ASP VAL HIS ARG PRO VAL PRO GLY CYS VAL ASN          
SEQRES  17 B  469  THR THR GLU VAL ASP ILE LYS LYS SER SER ARG MET ARG          
SEQRES  18 B  469  ASN PRO HIS LYS THR ARG LYS SER VAL TYR GLY LEU GLN          
SEQRES  19 B  469  ASN ASP ILE ARG SER HIS SER PRO THR HIS THR PRO THR          
SEQRES  20 B  469  PRO GLU THR LYS PRO PRO THR GLU ASP GLU LEU GLN GLN          
SEQRES  21 B  469  GLN ILE LYS TYR TRP GLN ILE GLN LEU ASP ARG HIS ARG          
SEQRES  22 B  469  LEU LYS MET SER LYS VAL ALA ASP SER LEU LEU SER TYR          
SEQRES  23 B  469  THR GLU GLN TYR VAL GLU TYR ASP PRO PHE LEU ALA PRO          
SEQRES  24 B  469  PRO ASP PRO SER ASN PRO TRP LEU SER ASP ASP THR THR          
SEQRES  25 B  469  PHE TRP GLU LEU GLU ALA SER LYS GLU PRO SER GLN GLN          
SEQRES  26 B  469  ARG VAL LYS ARG TRP GLY PHE GLY MET ASP GLU ALA LEU          
SEQRES  27 B  469  LYS ASP PRO VAL GLY ARG GLU GLN PHE LEU LYS PHE LEU          
SEQRES  28 B  469  GLU SER GLU PHE SER SER GLU ASN LEU ARG PHE TRP LEU          
SEQRES  29 B  469  ALA VAL GLU ASP LEU LYS LYS ARG PRO ILE ARG GLU VAL          
SEQRES  30 B  469  PRO SER ARG VAL GLN GLU ILE TRP GLN GLU PHE LEU ALA          
SEQRES  31 B  469  PRO GLY ALA PRO SER ALA ILE ASN LEU ASP SER LYS SER          
SEQRES  32 B  469  TYR ASP LYS THR THR GLN ASN VAL LYS GLU PRO GLY ARG          
SEQRES  33 B  469  TYR THR PHE GLU ASP ALA GLN GLU HIS ILE TYR LYS LEU          
SEQRES  34 B  469  MET LYS SER ASP SER TYR PRO ARG PHE ILE ARG SER SER          
SEQRES  35 B  469  ALA TYR GLN GLU LEU LEU GLN ALA LYS LYS LYS GLY LYS          
SEQRES  36 B  469  SER LEU THR SER LYS ARG LEU THR SER LEU VAL GLN SER          
SEQRES  37 B  469  TYR                                                          
SEQRES   1 C  353  MET ALA THR ASP GLY LEU HIS GLU ASN GLU THR LEU ALA          
SEQRES   2 C  353  SER LEU LYS SER GLU ALA GLU SER LEU LYS GLY LYS LEU          
SEQRES   3 C  353  GLU GLU GLU ARG ALA LYS LEU HIS ASP VAL GLU LEU HIS          
SEQRES   4 C  353  GLN VAL ALA GLU ARG VAL GLU ALA LEU GLY GLN PHE VAL          
SEQRES   5 C  353  MET LYS THR ARG ARG THR LEU LYS GLY HIS GLY ASN LYS          
SEQRES   6 C  353  VAL LEU CYS MET ASP TRP CYS LYS ASP LYS ARG ARG ILE          
SEQRES   7 C  353  VAL SER SER SER GLN ASP GLY LYS VAL ILE VAL TRP ASP          
SEQRES   8 C  353  SER PHE THR THR ASN LYS GLU HIS ALA VAL THR MET PRO          
SEQRES   9 C  353  CYS THR TRP VAL MET ALA CYS ALA TYR ALA PRO SER GLY          
SEQRES  10 C  353  CYS ALA ILE ALA CYS GLY GLY LEU ASP ASN LYS CYS SER          
SEQRES  11 C  353  VAL TYR PRO LEU THR PHE ASP LYS ASN GLU ASN MET ALA          
SEQRES  12 C  353  ALA LYS LYS LYS SER VAL ALA MET HIS THR ASN TYR LEU          
SEQRES  13 C  353  SER ALA CYS SER PHE THR ASN SER ASP MET GLN ILE LEU          
SEQRES  14 C  353  THR ALA SER GLY ASP GLY THR CYS ALA LEU TRP ASP VAL          
SEQRES  15 C  353  GLU SER GLY GLN LEU LEU GLN SER PHE HIS GLY HIS GLY          
SEQRES  16 C  353  ALA ASP VAL LEU CYS LEU ASP LEU ALA PRO SER GLU THR          
SEQRES  17 C  353  GLY ASN THR PHE VAL SER GLY GLY CYS ASP LYS LYS ALA          
SEQRES  18 C  353  MET VAL TRP ASP MET ARG SER GLY GLN CYS VAL GLN ALA          
SEQRES  19 C  353  PHE GLU THR HIS GLU SER ASP VAL ASN SER VAL ARG TYR          
SEQRES  20 C  353  TYR PRO SER GLY ASP ALA PHE ALA SER GLY SER ASP ASP          
SEQRES  21 C  353  ALA THR CYS ARG LEU TYR ASP LEU ARG ALA ASP ARG GLU          
SEQRES  22 C  353  VAL ALA ILE TYR SER LYS GLU SER ILE ILE PHE GLY ALA          
SEQRES  23 C  353  SER SER VAL ASP PHE SER LEU SER GLY ARG LEU LEU PHE          
SEQRES  24 C  353  ALA GLY TYR ASN ASP TYR THR ILE ASN VAL TRP ASP VAL          
SEQRES  25 C  353  LEU LYS GLY SER ARG VAL SER ILE LEU PHE GLY HIS GLU          
SEQRES  26 C  353  ASN ARG VAL SER THR LEU ARG VAL SER PRO ASP GLY THR          
SEQRES  27 C  353  ALA PHE CYS SER GLY SER TRP ASP HIS THR LEU ARG VAL          
SEQRES  28 C  353  TRP ALA                                                      
SEQRES   1 D  353  MET ALA THR ASP GLY LEU HIS GLU ASN GLU THR LEU ALA          
SEQRES   2 D  353  SER LEU LYS SER GLU ALA GLU SER LEU LYS GLY LYS LEU          
SEQRES   3 D  353  GLU GLU GLU ARG ALA LYS LEU HIS ASP VAL GLU LEU HIS          
SEQRES   4 D  353  GLN VAL ALA GLU ARG VAL GLU ALA LEU GLY GLN PHE VAL          
SEQRES   5 D  353  MET LYS THR ARG ARG THR LEU LYS GLY HIS GLY ASN LYS          
SEQRES   6 D  353  VAL LEU CYS MET ASP TRP CYS LYS ASP LYS ARG ARG ILE          
SEQRES   7 D  353  VAL SER SER SER GLN ASP GLY LYS VAL ILE VAL TRP ASP          
SEQRES   8 D  353  SER PHE THR THR ASN LYS GLU HIS ALA VAL THR MET PRO          
SEQRES   9 D  353  CYS THR TRP VAL MET ALA CYS ALA TYR ALA PRO SER GLY          
SEQRES  10 D  353  CYS ALA ILE ALA CYS GLY GLY LEU ASP ASN LYS CYS SER          
SEQRES  11 D  353  VAL TYR PRO LEU THR PHE ASP LYS ASN GLU ASN MET ALA          
SEQRES  12 D  353  ALA LYS LYS LYS SER VAL ALA MET HIS THR ASN TYR LEU          
SEQRES  13 D  353  SER ALA CYS SER PHE THR ASN SER ASP MET GLN ILE LEU          
SEQRES  14 D  353  THR ALA SER GLY ASP GLY THR CYS ALA LEU TRP ASP VAL          
SEQRES  15 D  353  GLU SER GLY GLN LEU LEU GLN SER PHE HIS GLY HIS GLY          
SEQRES  16 D  353  ALA ASP VAL LEU CYS LEU ASP LEU ALA PRO SER GLU THR          
SEQRES  17 D  353  GLY ASN THR PHE VAL SER GLY GLY CYS ASP LYS LYS ALA          
SEQRES  18 D  353  MET VAL TRP ASP MET ARG SER GLY GLN CYS VAL GLN ALA          
SEQRES  19 D  353  PHE GLU THR HIS GLU SER ASP VAL ASN SER VAL ARG TYR          
SEQRES  20 D  353  TYR PRO SER GLY ASP ALA PHE ALA SER GLY SER ASP ASP          
SEQRES  21 D  353  ALA THR CYS ARG LEU TYR ASP LEU ARG ALA ASP ARG GLU          
SEQRES  22 D  353  VAL ALA ILE TYR SER LYS GLU SER ILE ILE PHE GLY ALA          
SEQRES  23 D  353  SER SER VAL ASP PHE SER LEU SER GLY ARG LEU LEU PHE          
SEQRES  24 D  353  ALA GLY TYR ASN ASP TYR THR ILE ASN VAL TRP ASP VAL          
SEQRES  25 D  353  LEU LYS GLY SER ARG VAL SER ILE LEU PHE GLY HIS GLU          
SEQRES  26 D  353  ASN ARG VAL SER THR LEU ARG VAL SER PRO ASP GLY THR          
SEQRES  27 D  353  ALA PHE CYS SER GLY SER TRP ASP HIS THR LEU ARG VAL          
SEQRES  28 D  353  TRP ALA                                                      
FORMUL   5  HOH   *479(H2 O)                                                    
HELIX    1 AA1 SER A   18  GLN A   35  1                                  18    
HELIX    2 AA2 GLY A   59  LEU A   70  1                                  12    
HELIX    3 AA3 ASP A   74  GLY A   89  1                                  16    
HELIX    4 AA4 THR A  112  TRP A  116  5                                   5    
HELIX    5 AA5 GLU A  124  THR A  136  1                                  13    
HELIX    6 AA6 MET A  137  ARG A  142  1                                   6    
HELIX    7 AA7 ALA A  146  PHE A  160  1                                  15    
HELIX    8 AA8 LYS A  163  LYS A  180  1                                  18    
HELIX    9 AA9 ASP A  182  ARG A  201  1                                  20    
HELIX   10 AB1 GLU A  255  ARG A  271  1                                  17    
HELIX   11 AB2 LYS A  275  VAL A  291  1                                  17    
HELIX   12 AB3 GLU A  292  ASP A  294  5                                   3    
HELIX   13 AB4 ASN A  304  ASP A  309  1                                   6    
HELIX   14 AB5 THR A  311  ALA A  318  1                                   8    
HELIX   15 AB6 SER A  323  GLY A  331  1                                   9    
HELIX   16 AB7 GLY A  333  ASP A  340  1                                   8    
HELIX   17 AB8 ASP A  340  GLU A  354  1                                  15    
HELIX   18 AB9 SER A  357  LYS A  370  1                                  14    
HELIX   19 AC1 GLU A  376  LEU A  389  1                                  14    
HELIX   20 AC2 ASP A  400  LYS A  412  1                                  13    
HELIX   21 AC3 PHE A  419  ASP A  433  1                                  15    
HELIX   22 AC4 ASP A  433  ARG A  440  1                                   8    
HELIX   23 AC5 SER A  441  GLN A  449  1                                   9    
HELIX   24 AC6 PRO B   19  GLN B   35  1                                  17    
HELIX   25 AC7 GLY B   59  LEU B   70  1                                  12    
HELIX   26 AC8 ASP B   74  GLY B   89  1                                  16    
HELIX   27 AC9 THR B  112  TRP B  116  5                                   5    
HELIX   28 AD1 GLU B  124  GLN B  138  1                                  15    
HELIX   29 AD2 ALA B  146  PHE B  160  1                                  15    
HELIX   30 AD3 LYS B  163  LYS B  180  1                                  18    
HELIX   31 AD4 ASP B  182  ARG B  201  1                                  20    
HELIX   32 AD5 ASP B  256  ASP B  270  1                                  15    
HELIX   33 AD6 LYS B  275  VAL B  291  1                                  17    
HELIX   34 AD7 GLU B  292  ASP B  294  5                                   3    
HELIX   35 AD8 ASN B  304  ASP B  309  1                                   6    
HELIX   36 AD9 THR B  311  ALA B  318  1                                   8    
HELIX   37 AE1 SER B  323  GLY B  331  1                                   9    
HELIX   38 AE2 GLY B  333  ASP B  340  1                                   8    
HELIX   39 AE3 ASP B  340  GLU B  354  1                                  15    
HELIX   40 AE4 SER B  357  LYS B  370  1                                  14    
HELIX   41 AE5 GLU B  376  LEU B  389  1                                  14    
HELIX   42 AE6 ASP B  400  LYS B  412  1                                  13    
HELIX   43 AE7 PHE B  419  ASP B  433  1                                  15    
HELIX   44 AE8 ASP B  433  ARG B  440  1                                   8    
HELIX   45 AE9 SER B  441  ALA B  450  1                                  10    
HELIX   46 AF1 ASN C    9  HIS C   34  1                                  26    
HELIX   47 AF2 GLU C   37  ALA C   42  1                                   6    
HELIX   48 AF3 GLU C   43  VAL C   45  5                                   3    
HELIX   49 AF4 MET C  142  LYS C  146  5                                   5    
HELIX   50 AF5 GLU D    8  HIS D   34  1                                  27    
HELIX   51 AF6 GLU D   37  ALA D   42  1                                   6    
HELIX   52 AF7 GLU D   43  VAL D   45  5                                   3    
HELIX   53 AF8 MET D  142  LYS D  146  5                                   5    
SHEET    1 AA1 4 ARG A  44  LYS A  47  0                                        
SHEET    2 AA1 4 LYS A  52  SER A  58 -1  O  VAL A  56   N  ARG A  44           
SHEET    3 AA1 4 PHE A 107  PHE A 110 -1  O  TYR A 108   N  PHE A  57           
SHEET    4 AA1 4 PHE A  91  PRO A  93 -1  N  PHE A  92   O  ARG A 109           
SHEET    1 AA2 3 PHE B  57  SER B  58  0                                        
SHEET    2 AA2 3 PHE B 107  PHE B 110 -1  O  TYR B 108   N  PHE B  57           
SHEET    3 AA2 3 PHE B  91  PRO B  93 -1  N  PHE B  92   O  ARG B 109           
SHEET    1 AA3 4 LYS C  54  LYS C  60  0                                        
SHEET    2 AA3 4 THR C 348  ALA C 353 -1  O  VAL C 351   N  ARG C  56           
SHEET    3 AA3 4 PHE C 340  SER C 344 -1  N  PHE C 340   O  TRP C 352           
SHEET    4 AA3 4 VAL C 328  VAL C 333 -1  N  ARG C 332   O  CYS C 341           
SHEET    1 AA4 4 VAL C  66  TRP C  71  0                                        
SHEET    2 AA4 4 ARG C  77  SER C  82 -1  O  SER C  81   N  LEU C  67           
SHEET    3 AA4 4 LYS C  86  ASP C  91 -1  O  TRP C  90   N  ILE C  78           
SHEET    4 AA4 4 LYS C  97  THR C 102 -1  O  GLU C  98   N  VAL C  89           
SHEET    1 AA5 4 ALA C 110  TYR C 113  0                                        
SHEET    2 AA5 4 ALA C 119  GLY C 123 -1  O  ALA C 121   N  ALA C 112           
SHEET    3 AA5 4 LYS C 128  PRO C 133 -1  O  TYR C 132   N  ILE C 120           
SHEET    4 AA5 4 LYS C 147  MET C 151 -1  O  LYS C 147   N  VAL C 131           
SHEET    1 AA6 4 LEU C 156  PHE C 161  0                                        
SHEET    2 AA6 4 GLN C 167  SER C 172 -1  O  LEU C 169   N  SER C 160           
SHEET    3 AA6 4 THR C 176  ASP C 181 -1  O  TRP C 180   N  ILE C 168           
SHEET    4 AA6 4 LEU C 187  HIS C 192 -1  O  PHE C 191   N  CYS C 177           
SHEET    1 AA7 4 VAL C 198  LEU C 203  0                                        
SHEET    2 AA7 4 THR C 211  GLY C 216 -1  O  GLY C 215   N  LEU C 199           
SHEET    3 AA7 4 ALA C 221  ASP C 225 -1  O  TRP C 224   N  PHE C 212           
SHEET    4 AA7 4 CYS C 231  PHE C 235 -1  O  GLN C 233   N  VAL C 223           
SHEET    1 AA8 4 VAL C 242  TYR C 247  0                                        
SHEET    2 AA8 4 ALA C 253  SER C 258 -1  O  ALA C 255   N  ARG C 246           
SHEET    3 AA8 4 CYS C 263  ASP C 267 -1  O  TYR C 266   N  PHE C 254           
SHEET    4 AA8 4 ARG C 272  TYR C 277 -1  O  TYR C 277   N  CYS C 263           
SHEET    1 AA9 4 ALA C 286  PHE C 291  0                                        
SHEET    2 AA9 4 LEU C 297  TYR C 302 -1  O  PHE C 299   N  ASP C 290           
SHEET    3 AA9 4 ILE C 307  ASP C 311 -1  O  TRP C 310   N  LEU C 298           
SHEET    4 AA9 4 ARG C 317  LEU C 321 -1  O  LEU C 321   N  ILE C 307           
SHEET    1 AB1 4 LYS D  54  LYS D  60  0                                        
SHEET    2 AB1 4 THR D 348  ALA D 353 -1  O  VAL D 351   N  ARG D  56           
SHEET    3 AB1 4 PHE D 340  SER D 344 -1  N  PHE D 340   O  TRP D 352           
SHEET    4 AB1 4 VAL D 328  VAL D 333 -1  N  THR D 330   O  GLY D 343           
SHEET    1 AB2 4 VAL D  66  TRP D  71  0                                        
SHEET    2 AB2 4 ARG D  77  SER D  82 -1  O  SER D  81   N  LEU D  67           
SHEET    3 AB2 4 LYS D  86  ASP D  91 -1  O  TRP D  90   N  ILE D  78           
SHEET    4 AB2 4 LYS D  97  THR D 102 -1  O  GLU D  98   N  VAL D  89           
SHEET    1 AB3 4 ALA D 110  TYR D 113  0                                        
SHEET    2 AB3 4 ALA D 119  GLY D 123 -1  O  ALA D 121   N  ALA D 112           
SHEET    3 AB3 4 LYS D 128  PRO D 133 -1  O  TYR D 132   N  ILE D 120           
SHEET    4 AB3 4 LYS D 147  MET D 151 -1  O  LYS D 147   N  VAL D 131           
SHEET    1 AB4 4 LEU D 156  PHE D 161  0                                        
SHEET    2 AB4 4 GLN D 167  SER D 172 -1  O  LEU D 169   N  SER D 160           
SHEET    3 AB4 4 THR D 176  ASP D 181 -1  O  ALA D 178   N  THR D 170           
SHEET    4 AB4 4 GLN D 186  HIS D 192 -1  O  PHE D 191   N  CYS D 177           
SHEET    1 AB5 4 VAL D 198  LEU D 203  0                                        
SHEET    2 AB5 4 THR D 211  GLY D 216 -1  O  GLY D 215   N  LEU D 199           
SHEET    3 AB5 4 ALA D 221  ASP D 225 -1  O  TRP D 224   N  PHE D 212           
SHEET    4 AB5 4 CYS D 231  PHE D 235 -1  O  GLN D 233   N  VAL D 223           
SHEET    1 AB6 4 VAL D 242  TYR D 247  0                                        
SHEET    2 AB6 4 ALA D 253  SER D 258 -1  O  ALA D 255   N  ARG D 246           
SHEET    3 AB6 4 CYS D 263  ASP D 267 -1  O  TYR D 266   N  PHE D 254           
SHEET    4 AB6 4 ARG D 272  TYR D 277 -1  O  TYR D 277   N  CYS D 263           
SHEET    1 AB7 4 ALA D 286  PHE D 291  0                                        
SHEET    2 AB7 4 LEU D 297  TYR D 302 -1  O  PHE D 299   N  ASP D 290           
SHEET    3 AB7 4 ILE D 307  ASP D 311 -1  O  TRP D 310   N  LEU D 298           
SHEET    4 AB7 4 ARG D 317  LEU D 321 -1  O  LEU D 321   N  ILE D 307           
CISPEP   1 ASP A  301    PRO A  302          0         2.19                     
CISPEP   2 ASP B  301    PRO B  302          0         1.37                     
CRYST1   69.323  162.760   95.295  90.00  98.36  90.00 P 1 21 1      4          
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      0.014425  0.000000  0.002120        0.00000                         
SCALE2      0.000000  0.006144  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010606        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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