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Database: PDB
Entry: 5VYK
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HEADER    SIGNALING PROTEIN                       25-MAY-17   5VYK              
TITLE     CRYSTAL STRUCTURE OF THE BRS DOMAIN OF BRAF IN COMPLEX WITH THE CC-SAM
TITLE    2 DOMAIN OF KSR1                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHIMERA PROTEIN OF BRS DOMAIN OF BRAF AND CC-SAM DOMAIN OF 
COMPND   3 KSR1,SERINE/THREONINE-PROTEIN KINASE B-RAF;                          
COMPND   4 CHAIN: A, C;                                                         
COMPND   5 FRAGMENT: UNP Q8IVT5 RESIDUES 27-172, UNP F7FV05 RESIDUES 39-108;    
COMPND   6 SYNONYM: PROTO-ONCOGENE B-RAF,P94,V-RAF MURINE SARCOMA VIRAL ONCOGENE
COMPND   7 HOMOLOG B1;                                                          
COMPND   8 EC: 2.7.11.1;                                                        
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: KSR1, KSR, BRAF, BRAF1, RAFB1;                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    BRAF, KSR1, BRS, CC-SAM, COMPLEX, KINASE, PSEUDOKINASE, SIGNALING.,   
KEYWDS   2 SIGNALING PROTEIN                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.MAISONNEUVE,I.KURINOV,S.A.MARULLO,H.LAVOIE,N.THEVAKUMARAN,M.SAHMI,  
AUTHOR   2 T.JIN,M.THERRIEN,F.SICHERI                                           
REVDAT   3   07-MAR-18 5VYK    1       JRNL                                     
REVDAT   2   28-FEB-18 5VYK    1       JRNL                                     
REVDAT   1   14-FEB-18 5VYK    0                                                
JRNL        AUTH   H.LAVOIE,M.SAHMI,P.MAISONNEUVE,S.A.MARULLO,N.THEVAKUMARAN,   
JRNL        AUTH 2 T.JIN,I.KURINOV,F.SICHERI,M.THERRIEN                         
JRNL        TITL   MEK DRIVES BRAF ACTIVATION THROUGH ALLOSTERIC CONTROL OF KSR 
JRNL        TITL 2 PROTEINS.                                                    
JRNL        REF    NATURE                        V. 554   549 2018              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   29433126                                                     
JRNL        DOI    10.1038/NATURE25478                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.11.1_2575                                   
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.64                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 47163                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.219                           
REMARK   3   R VALUE            (WORKING SET) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.340                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2517                            
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 49.6613 -  4.5837    0.97     2573   146  0.2076 0.2213        
REMARK   3     2  4.5837 -  3.6385    0.98     2528   140  0.1682 0.1644        
REMARK   3     3  3.6385 -  3.1787    0.98     2523   149  0.2021 0.2372        
REMARK   3     4  3.1787 -  2.8881    0.99     2534   133  0.2191 0.2329        
REMARK   3     5  2.8881 -  2.6811    0.99     2539   139  0.2351 0.3263        
REMARK   3     6  2.6811 -  2.5230    0.99     2554   140  0.2310 0.2767        
REMARK   3     7  2.5230 -  2.3967    0.98     2503   148  0.2289 0.2546        
REMARK   3     8  2.3967 -  2.2924    0.99     2485   133  0.2191 0.2214        
REMARK   3     9  2.2924 -  2.2041    0.99     2503   163  0.2131 0.2279        
REMARK   3    10  2.2041 -  2.1280    0.98     2513   125  0.2183 0.2965        
REMARK   3    11  2.1280 -  2.0615    0.98     2515   140  0.2357 0.2677        
REMARK   3    12  2.0615 -  2.0026    0.97     2436   161  0.2910 0.3305        
REMARK   3    13  2.0026 -  1.9499    0.97     2472   147  0.3363 0.3620        
REMARK   3    14  1.9499 -  1.9023    0.97     2520   126  0.3428 0.3444        
REMARK   3    15  1.9023 -  1.8590    0.97     2444   143  0.3826 0.4179        
REMARK   3    16  1.8590 -  1.8195    0.96     2471   132  0.4300 0.4816        
REMARK   3    17  1.8195 -  1.7831    0.94     2361   134  0.4918 0.5608        
REMARK   3    18  1.7831 -  1.7494    0.86     2172   118  0.5311 0.5881        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.330            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.310           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 40.89                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 72.02                          
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      :  0.006           3114                                  
REMARK   3   ANGLE     :  0.750           4226                                  
REMARK   3   CHIRALITY :  0.044            502                                  
REMARK   3   PLANARITY :  0.005            546                                  
REMARK   3   DIHEDRAL  : 17.365           1918                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 33:93 )                            
REMARK   3    ORIGIN FOR THE GROUP (A):   62.952   30.624    7.637              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3137 T22:   0.4636                                     
REMARK   3      T33:   0.2990 T12:  -0.0296                                     
REMARK   3      T13:  -0.0339 T23:   0.0671                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1700 L22:   5.7495                                     
REMARK   3      L33:   7.0748 L12:   0.0625                                     
REMARK   3      L13:   0.3373 L23:  -1.8864                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2984 S12:  -0.4745 S13:  -0.3433                       
REMARK   3      S21:   0.2070 S22:  -0.2008 S23:  -0.1738                       
REMARK   3      S31:   0.3688 S32:  -0.1483 S33:   0.0340                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 94:100 )                           
REMARK   3    ORIGIN FOR THE GROUP (A):   63.493   18.312   28.560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4733 T22:   1.3750                                     
REMARK   3      T33:   0.6256 T12:  -0.3138                                     
REMARK   3      T13:  -0.5254 T23:   1.5483                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7210 L22:   2.5870                                     
REMARK   3      L33:   3.0084 L12:  -0.4351                                     
REMARK   3      L13:  -0.4803 L23:   2.7894                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2439 S12:  -0.3326 S13:  -0.3435                       
REMARK   3      S21:   0.7910 S22:  -0.0064 S23:   0.0100                       
REMARK   3      S31:   1.1568 S32:   0.2460 S33:  -1.1666                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 101:124 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   71.802   24.318   10.792              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5197 T22:   0.6407                                     
REMARK   3      T33:   0.6959 T12:   0.1942                                     
REMARK   3      T13:  -0.2492 T23:   0.2895                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0641 L22:   5.4918                                     
REMARK   3      L33:   7.3239 L12:   0.6100                                     
REMARK   3      L13:   2.1398 L23:  -1.5947                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.7250 S12:  -0.1219 S13:  -1.7398                       
REMARK   3      S21:   0.0496 S22:   0.4051 S23:  -0.0992                       
REMARK   3      S31:   1.9579 S32:   0.7787 S33:   1.5024                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 125:153 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   82.018   27.814   16.262              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5610 T22:   1.4583                                     
REMARK   3      T33:   0.7631 T12:  -0.0182                                     
REMARK   3      T13:  -0.1801 T23:   0.0972                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.0808 L22:   3.3715                                     
REMARK   3      L33:   2.0226 L12:  -1.1557                                     
REMARK   3      L13:   1.6388 L23:  -0.8233                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0897 S12:   0.5479 S13:  -0.3398                       
REMARK   3      S21:   0.1965 S22:   0.0625 S23:  -1.1038                       
REMARK   3      S31:   1.7798 S32:   0.9943 S33:  -0.4564                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 154:171 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   75.273   36.596   13.983              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6902 T22:   1.0054                                     
REMARK   3      T33:   1.2448 T12:  -0.0480                                     
REMARK   3      T13:  -0.2858 T23:   0.0466                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3362 L22:   4.8506                                     
REMARK   3      L33:   4.7815 L12:  -1.5891                                     
REMARK   3      L13:   5.4177 L23:  -1.4044                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7653 S12:  -0.2414 S13:   2.3044                       
REMARK   3      S21:   0.1962 S22:   0.1985 S23:  -0.1702                       
REMARK   3      S31:  -1.0064 S32:   1.0828 S33:   0.3804                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: ( CHAIN C AND RESID 1042:1068 )                        
REMARK   3    ORIGIN FOR THE GROUP (A):   57.750   32.973   -7.654              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6825 T22:   0.5236                                     
REMARK   3      T33:   0.2933 T12:  -0.0402                                     
REMARK   3      T13:   0.0373 T23:  -0.0280                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.5418 L22:   3.9253                                     
REMARK   3      L33:   9.9461 L12:   4.0812                                     
REMARK   3      L13:  -6.2847 L23:  -4.4126                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0188 S12:   0.5758 S13:  -0.1251                       
REMARK   3      S21:  -1.0004 S22:   0.0594 S23:  -0.2994                       
REMARK   3      S31:   0.3633 S32:  -0.1347 S33:  -0.1258                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: ( CHAIN C AND RESID 1069:1105 )                        
REMARK   3    ORIGIN FOR THE GROUP (A):   51.673   37.335   -3.043              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4900 T22:   0.5022                                     
REMARK   3      T33:   0.2776 T12:  -0.0523                                     
REMARK   3      T13:   0.0585 T23:  -0.0198                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.4423 L22:   4.4320                                     
REMARK   3      L33:   8.0289 L12:   2.7343                                     
REMARK   3      L13:  -5.0676 L23:  -1.5447                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4006 S12:   0.1717 S13:   0.2826                       
REMARK   3      S21:  -0.5187 S22:   0.1596 S23:   0.0279                       
REMARK   3      S31:  -0.1207 S32:  -0.8509 S33:  -0.4714                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: ( CHAIN C AND RESID 33:108 )                           
REMARK   3    ORIGIN FOR THE GROUP (A):   66.037   54.542    1.415              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3011 T22:   0.4855                                     
REMARK   3      T33:   0.4453 T12:  -0.0245                                     
REMARK   3      T13:   0.0500 T23:   0.1577                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3215 L22:   5.6764                                     
REMARK   3      L33:   7.4600 L12:   1.3219                                     
REMARK   3      L13:  -1.4599 L23:  -1.6327                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1650 S12:   0.5713 S13:   0.8624                       
REMARK   3      S21:  -0.2281 S22:  -0.2516 S23:  -0.4364                       
REMARK   3      S31:  -0.6393 S32:   0.3671 S33:  -0.1048                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: ( CHAIN C AND RESID 109:171 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   79.825   52.576    7.496              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4218 T22:   1.0199                                     
REMARK   3      T33:   0.8094 T12:  -0.1084                                     
REMARK   3      T13:  -0.0728 T23:   0.0777                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2476 L22:   2.4377                                     
REMARK   3      L33:   7.4627 L12:   0.6805                                     
REMARK   3      L13:  -2.3896 L23:   1.0266                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4826 S12:  -0.7523 S13:  -0.1369                       
REMARK   3      S21:   0.1966 S22:  -0.2767 S23:  -0.5098                       
REMARK   3      S31:   0.1186 S32:   1.0088 S33:  -0.3639                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: ( CHAIN A AND RESID 1042:1068 )                        
REMARK   3    ORIGIN FOR THE GROUP (A):   51.388   50.032   13.295              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5853 T22:   0.5051                                     
REMARK   3      T33:   0.3420 T12:   0.0361                                     
REMARK   3      T13:   0.1741 T23:  -0.0088                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1136 L22:   7.3826                                     
REMARK   3      L33:   3.5012 L12:   0.5744                                     
REMARK   3      L13:  -2.2566 L23:  -3.1466                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0623 S12:  -0.3177 S13:   0.3144                       
REMARK   3      S21:   1.3988 S22:   0.0276 S23:   0.3148                       
REMARK   3      S31:  -0.7810 S32:  -0.2952 S33:  -0.3780                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: ( CHAIN A AND RESID 1069:1075 )                        
REMARK   3    ORIGIN FOR THE GROUP (A):   50.535   58.364   -9.522              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7402 T22:   1.0644                                     
REMARK   3      T33:   0.6654 T12:   0.1361                                     
REMARK   3      T13:   0.1512 T23:   0.3273                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6050 L22:   1.3092                                     
REMARK   3      L33:   7.8358 L12:   1.4437                                     
REMARK   3      L13:  -3.5317 L23:  -3.1949                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3049 S12:   2.0555 S13:   1.0249                       
REMARK   3      S21:  -0.3074 S22:  -1.1541 S23:  -1.1032                       
REMARK   3      S31:  -1.7856 S32:   0.7499 S33:   0.3402                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: ( CHAIN A AND RESID 1076:1104 )                        
REMARK   3    ORIGIN FOR THE GROUP (A):   48.625   43.156    8.968              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5864 T22:   0.5455                                     
REMARK   3      T33:   0.2741 T12:   0.0014                                     
REMARK   3      T13:   0.0585 T23:   0.0187                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4202 L22:   4.6765                                     
REMARK   3      L33:   2.9666 L12:   0.7770                                     
REMARK   3      L13:  -2.0102 L23:  -1.5752                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2097 S12:   0.0568 S13:   0.0774                       
REMARK   3      S21:   0.5254 S22:   0.0464 S23:   0.3154                       
REMARK   3      S31:   0.6681 S32:  -0.5262 S33:  -0.1897                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: (CHAIN A AND (RESID 56 THROUGH 161 OR       
REMARK   3                          (RESID 162 THROUGH 163 AND (NAME N OR       
REMARK   3                          NAME CA OR NAME C OR NAME O OR NAME CB ))   
REMARK   3                          OR RESID 164 THROUGH 171))                  
REMARK   3     SELECTION          : (CHAIN C AND ((RESID 56 AND (NAME N OR      
REMARK   3                          NAME CA OR NAME C OR NAME O OR NAME CB ))   
REMARK   3                          OR RESID 57 THROUGH 161 OR (RESID 162       
REMARK   3                          THROUGH 163 AND (NAME N OR NAME CA OR       
REMARK   3                          NAME C OR NAME O OR NAME CB )) OR RESID     
REMARK   3                          164 THROUGH 171))                           
REMARK   3     ATOM PAIRS NUMBER  : 1040                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5VYK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAY-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000227901.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-APR-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9791                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 47556                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.749                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: SAD                          
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.53                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS PH 7.5, 3.0M SODIUM FORMATE,   
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       89.89800            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       27.16800            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       89.89800            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       27.16800            
REMARK 290   SMTRY3   4  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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6910 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17970 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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     GLY A    24                                                      
REMARK 465     ALA A    25                                                      
REMARK 465     MET A    26                                                      
REMARK 465     GLU A    27                                                      
REMARK 465     GLY A    28                                                      
REMARK 465     GLY A    29                                                      
REMARK 465     ALA A    30                                                      
REMARK 465     GLY A    31                                                      
REMARK 465     ALA A    32                                                      
REMARK 465     GLY A   172                                                      
REMARK 465     GLY A   173                                                      
REMARK 465     SER A   174                                                      
REMARK 465     GLY A   175                                                      
REMARK 465     SER A   176                                                      
REMARK 465     GLY A   177                                                      
REMARK 465     SER A   178                                                      
REMARK 465     GLY A   179                                                      
REMARK 465     SER A   180                                                      
REMARK 465     SER A  1036                                                      
REMARK 465     SER A  1037                                                      
REMARK 465     ALA A  1038                                                      
REMARK 465     ALA A  1039                                                      
REMARK 465     ASP A  1040                                                      
REMARK 465     PRO A  1041                                                      
REMARK 465     ASN A  1105                                                      
REMARK 465     GLY A  1106                                                      
REMARK 465     THR A  1107                                                      
REMARK 465     ASP A  1108                                                      
REMARK 465     PHE A  1109                                                      
REMARK 465     SER A  1110                                                      
REMARK 465     GLY C    24                                                      
REMARK 465     ALA C    25                                                      
REMARK 465     MET C    26                                                      
REMARK 465     GLU C    27                                                      
REMARK 465     GLY C    28                                                      
REMARK 465     GLY C    29                                                      
REMARK 465     ALA C    30                                                      
REMARK 465     GLY C    31                                                      
REMARK 465     ALA C    32                                                      
REMARK 465     GLY C   172                                                      
REMARK 465     GLY C   173                                                      
REMARK 465     SER C   174                                                      
REMARK 465     GLY C   175                                                      
REMARK 465     SER C   176                                                      
REMARK 465     GLY C   177                                                      
REMARK 465     SER C   178                                                      
REMARK 465     GLY C   179                                                      
REMARK 465     SER C   180                                                      
REMARK 465     SER C  1036                                                      
REMARK 465     SER C  1037                                                      
REMARK 465     ALA C  1038                                                      
REMARK 465     ALA C  1039                                                      
REMARK 465     ASP C  1040                                                      
REMARK 465     PRO C  1041                                                      
REMARK 465     GLY C  1106                                                      
REMARK 465     THR C  1107                                                      
REMARK 465     ASP C  1108                                                      
REMARK 465     PHE C  1109                                                      
REMARK 465     SER C  1110                                                      
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     ARG A  36    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A  56    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 102    CG   CD   OE1  OE2                                  
REMARK 470     TYR A 114    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG A 119    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 121    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 124    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 125    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 126    CG1  CG2  CD1                                       
REMARK 470     ARG A 128    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 129    CG   OD1  OD2                                       
REMARK 470     GLU A 140    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 144    CG   CD   CE   NZ                                   
REMARK 470     GLU A 145    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 148    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 149    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 155    CG   OD1  OD2                                       
REMARK 470     GLN A 161    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 169    CG   CD   CE   NZ                                   
REMARK 470     ILE A1043    CG1  CG2  CD1                                       
REMARK 470     GLU A1045    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1055    CG   CD   CE   NZ                                   
REMARK 470     GLU A1101    CG   CD   OE1  OE2                                  
REMARK 470     ARG C  36    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 102    CG   CD   OE1  OE2                                  
REMARK 470     TYR C 114    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG C 119    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 121    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 124    CG   CD   OE1  NE2                                  
REMARK 470     GLU C 125    CG   CD   OE1  OE2                                  
REMARK 470     ILE C 126    CG1  CG2  CD1                                       
REMARK 470     ARG C 128    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP C 129    CG   OD1  OD2                                       
REMARK 470     GLU C 140    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 144    CG   CD   CE   NZ                                   
REMARK 470     GLU C 145    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 148    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 149    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP C 155    CG   OD1  OD2                                       
REMARK 470     GLN C 161    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 169    CG   CD   CE   NZ                                   
REMARK 470     GLU C1045    CG   CD   OE1  OE2                                  
REMARK 470     LYS C1055    CG   CD   CE   NZ                                   
REMARK 470     GLN C1097    CG   CD   OE1  NE2                                  
REMARK 470     GLU C1101    CG   CD   OE1  OE2                                  
REMARK 470     SER C1102    OG                                                  
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   OH   TYR C  1078     O    HOH C   401              2.07            
REMARK 500   OH   TYR A  1078     O    HOH A   401              2.11            
REMARK 500   O    HOH C   437     O    HOH C   439              2.14            
REMARK 500   O3   GOL C   301     O    HOH C   402              2.16            
REMARK 500   O    HOH A   416     O    HOH A   441              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   401     O    HOH C   406     4555     1.91            
REMARK 500   O    HOH A   407     O    HOH C   401     4555     1.96            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 301                 
DBREF  5VYK A   27   172  UNP    Q8IVT5   KSR1_HUMAN      27    172             
DBREF  5VYK A 1036  1110  UNP    P15056   BRAF_HUMAN      36    110             
DBREF  5VYK C   27   172  UNP    Q8IVT5   KSR1_HUMAN      27    172             
DBREF  5VYK C 1036  1110  UNP    P15056   BRAF_HUMAN      36    110             
SEQADV 5VYK GLY A   24  UNP  Q8IVT5              EXPRESSION TAG                 
SEQADV 5VYK ALA A   25  UNP  Q8IVT5              EXPRESSION TAG                 
SEQADV 5VYK MET A   26  UNP  Q8IVT5              EXPRESSION TAG                 
SEQADV 5VYK GLY A  173  UNP  Q8IVT5              LINKER                         
SEQADV 5VYK SER A  174  UNP  Q8IVT5              LINKER                         
SEQADV 5VYK GLY A  175  UNP  Q8IVT5              LINKER                         
SEQADV 5VYK SER A  176  UNP  Q8IVT5              LINKER                         
SEQADV 5VYK GLY A  177  UNP  Q8IVT5              LINKER                         
SEQADV 5VYK SER A  178  UNP  Q8IVT5              LINKER                         
SEQADV 5VYK GLY A  179  UNP  Q8IVT5              LINKER                         
SEQADV 5VYK SER A  180  UNP  Q8IVT5              LINKER                         
SEQADV 5VYK GLY C   24  UNP  Q8IVT5              EXPRESSION TAG                 
SEQADV 5VYK ALA C   25  UNP  Q8IVT5              EXPRESSION TAG                 
SEQADV 5VYK MET C   26  UNP  Q8IVT5              EXPRESSION TAG                 
SEQADV 5VYK GLY C  173  UNP  Q8IVT5              LINKER                         
SEQADV 5VYK SER C  174  UNP  Q8IVT5              LINKER                         
SEQADV 5VYK GLY C  175  UNP  Q8IVT5              LINKER                         
SEQADV 5VYK SER C  176  UNP  Q8IVT5              LINKER                         
SEQADV 5VYK GLY C  177  UNP  Q8IVT5              LINKER                         
SEQADV 5VYK SER C  178  UNP  Q8IVT5              LINKER                         
SEQADV 5VYK GLY C  179  UNP  Q8IVT5              LINKER                         
SEQADV 5VYK SER C  180  UNP  Q8IVT5              LINKER                         
SEQRES   1 A  232  GLY ALA MET GLU GLY GLY ALA GLY ALA ALA ALA SER ARG          
SEQRES   2 A  232  ALA LEU GLN GLN CYS GLY GLN LEU GLN LYS LEU ILE ASP          
SEQRES   3 A  232  ILE SER ILE GLY SER LEU ARG GLY LEU ARG THR LYS CYS          
SEQRES   4 A  232  ALA VAL SER ASN ASP LEU THR GLN GLN GLU ILE ARG THR          
SEQRES   5 A  232  LEU GLU ALA LYS LEU VAL ARG TYR ILE CYS LYS GLN ARG          
SEQRES   6 A  232  GLN CYS LYS LEU SER VAL ALA PRO GLY GLU ARG THR PRO          
SEQRES   7 A  232  GLU LEU ASN SER TYR PRO ARG PHE SER ASP TRP LEU TYR          
SEQRES   8 A  232  THR PHE ASN VAL ARG PRO GLU VAL VAL GLN GLU ILE PRO          
SEQRES   9 A  232  ARG ASP LEU THR LEU ASP ALA LEU LEU GLU MET ASN GLU          
SEQRES  10 A  232  ALA LYS VAL LYS GLU THR LEU ARG ARG CYS GLY ALA SER          
SEQRES  11 A  232  GLY ASP GLU CYS GLY ARG LEU GLN TYR ALA LEU THR CYS          
SEQRES  12 A  232  LEU ARG LYS VAL THR GLY GLY SER GLY SER GLY SER GLY          
SEQRES  13 A  232  SER SER SER ALA ALA ASP PRO ALA ILE PRO GLU GLU VAL          
SEQRES  14 A  232  TRP ASN ILE LYS GLN MET ILE LYS LEU THR GLN GLU HIS          
SEQRES  15 A  232  ILE GLU ALA LEU LEU ASP LYS PHE GLY GLY GLU HIS ASN          
SEQRES  16 A  232  PRO PRO SER ILE TYR LEU GLU ALA TYR GLU GLU TYR THR          
SEQRES  17 A  232  SER LYS LEU ASP ALA LEU GLN GLN ARG GLU GLN GLN LEU          
SEQRES  18 A  232  LEU GLU SER LEU GLY ASN GLY THR ASP PHE SER                  
SEQRES   1 C  232  GLY ALA MET GLU GLY GLY ALA GLY ALA ALA ALA SER ARG          
SEQRES   2 C  232  ALA LEU GLN GLN CYS GLY GLN LEU GLN LYS LEU ILE ASP          
SEQRES   3 C  232  ILE SER ILE GLY SER LEU ARG GLY LEU ARG THR LYS CYS          
SEQRES   4 C  232  ALA VAL SER ASN ASP LEU THR GLN GLN GLU ILE ARG THR          
SEQRES   5 C  232  LEU GLU ALA LYS LEU VAL ARG TYR ILE CYS LYS GLN ARG          
SEQRES   6 C  232  GLN CYS LYS LEU SER VAL ALA PRO GLY GLU ARG THR PRO          
SEQRES   7 C  232  GLU LEU ASN SER TYR PRO ARG PHE SER ASP TRP LEU TYR          
SEQRES   8 C  232  THR PHE ASN VAL ARG PRO GLU VAL VAL GLN GLU ILE PRO          
SEQRES   9 C  232  ARG ASP LEU THR LEU ASP ALA LEU LEU GLU MET ASN GLU          
SEQRES  10 C  232  ALA LYS VAL LYS GLU THR LEU ARG ARG CYS GLY ALA SER          
SEQRES  11 C  232  GLY ASP GLU CYS GLY ARG LEU GLN TYR ALA LEU THR CYS          
SEQRES  12 C  232  LEU ARG LYS VAL THR GLY GLY SER GLY SER GLY SER GLY          
SEQRES  13 C  232  SER SER SER ALA ALA ASP PRO ALA ILE PRO GLU GLU VAL          
SEQRES  14 C  232  TRP ASN ILE LYS GLN MET ILE LYS LEU THR GLN GLU HIS          
SEQRES  15 C  232  ILE GLU ALA LEU LEU ASP LYS PHE GLY GLY GLU HIS ASN          
SEQRES  16 C  232  PRO PRO SER ILE TYR LEU GLU ALA TYR GLU GLU TYR THR          
SEQRES  17 C  232  SER LYS LEU ASP ALA LEU GLN GLN ARG GLU GLN GLN LEU          
SEQRES  18 C  232  LEU GLU SER LEU GLY ASN GLY THR ASP PHE SER                  
HET    GOL  A 301       6                                                       
HET    GOL  C 301       6                                                       
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  GOL    2(C3 H8 O3)                                                  
FORMUL   5  HOH   *99(H2 O)                                                     
HELIX    1 AA1 ALA A   33  CYS A   62  1                                  30    
HELIX    2 AA2 ASN A   66  VAL A   94  1                                  29    
HELIX    3 AA3 THR A  100  SER A  105  1                                   6    
HELIX    4 AA4 ARG A  108  PHE A  116  1                                   9    
HELIX    5 AA5 ARG A  119  GLU A  125  1                                   7    
HELIX    6 AA6 THR A  131  MET A  138  1                                   8    
HELIX    7 AA7 ASN A  139  CYS A  150  1                                  12    
HELIX    8 AA8 SER A  153  THR A  171  1                                  19    
HELIX    9 AA9 ILE A 1043  GLY A 1069  1                                  27    
HELIX   10 AB1 PRO A 1075  GLY A 1104  1                                  30    
HELIX   11 AB2 ALA C   34  CYS C   62  1                                  29    
HELIX   12 AB3 ASN C   66  VAL C   94  1                                  29    
HELIX   13 AB4 THR C  100  SER C  105  1                                   6    
HELIX   14 AB5 ARG C  108  PHE C  116  1                                   9    
HELIX   15 AB6 ARG C  119  GLU C  125  1                                   7    
HELIX   16 AB7 THR C  131  MET C  138  1                                   8    
HELIX   17 AB8 ASN C  139  CYS C  150  1                                  12    
HELIX   18 AB9 SER C  153  THR C  171  1                                  19    
HELIX   19 AC1 ILE C 1043  GLY C 1069  1                                  27    
HELIX   20 AC2 PRO C 1075  ASN C 1105  1                                  31    
CISPEP   1 TYR A  106    PRO A  107          0        -3.16                     
CISPEP   2 TYR C  106    PRO C  107          0        -3.28                     
SITE     1 AC1  7 MET A1053  LEU A1056  THR A1057  TYR A1085                    
SITE     2 AC1  7 LYS A1088  HOH A 403  LEU C  76                               
SITE     1 AC2  8 SER A  54  GLU A  72  LEU A  76  LEU C1056                    
SITE     2 AC2  8 THR C1057  TYR C1085  LYS C1088  HOH C 402                    
CRYST1  179.796   54.336   51.864  90.00 106.68  90.00 C 1 2 1       8          
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      0.005562  0.000000  0.001667        0.00000                         
SCALE2      0.000000  0.018404  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020128        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system