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Database: PDB
Entry: 6M94
LinkDB: 6M94
Original site: 6M94 
HEADER    LIGASE                                  22-AUG-18   6M94              
TITLE     MONOPHOSPHORYLATED PSER33 B-CATENIN PEPTIDE BOUND TO B-TRCP/SKP1      
TITLE    2 COMPLEX                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: F-BOX/WD REPEAT-CONTAINING PROTEIN 1A;                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: E3RSIKAPPAB,EPIDIDYMIS TISSUE PROTEIN LI 2A,F-BOX AND WD    
COMPND   5 REPEATS PROTEIN BETA-TRCP,PIKAPPABALPHA-E3 RECEPTOR SUBUNIT;         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: S-PHASE KINASE-ASSOCIATED PROTEIN 1;                       
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: CYCLIN-A/CDK2-ASSOCIATED PROTEIN P19,P19A,ORGAN OF CORTI    
COMPND  11 PROTEIN 2,OCP-2,ORGAN OF CORTI PROTEIN II,OCP-II,RNA POLYMERASE II   
COMPND  12 ELONGATION FACTOR-LIKE PROTEIN,SIII,TRANSCRIPTION ELONGATION FACTOR B
COMPND  13 POLYPEPTIDE 1-LIKE,P19SKP1;                                          
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 3;                                                           
COMPND  16 MOLECULE: CATENIN BETA-1;                                            
COMPND  17 CHAIN: C;                                                            
COMPND  18 SYNONYM: BETA-CATENIN;                                               
COMPND  19 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: BTRC, BTRCP, FBW1A, FBXW1A;                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: SKP1, EMC19, OCP2, SKP1A, TCEB1L;                              
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 SYNTHETIC: YES;                                                      
SOURCE  17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  18 ORGANISM_COMMON: HUMAN;                                              
SOURCE  19 ORGANISM_TAXID: 9606                                                 
KEYWDS    UBIQUITIN MOLECULAR GLUE ENHANCER, LIGASE                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.R.SIMONETTA,M.C.CLIFTON,R.L.WALTER,G.M.RANIERI,J.J.CARTER           
REVDAT   2   10-APR-19 6M94    1       JRNL                                     
REVDAT   1   03-APR-19 6M94    0                                                
JRNL        AUTH   K.R.SIMONETTA,J.TAYGERLY,K.BOYLE,S.E.BASHAM,C.PADOVANI,      
JRNL        AUTH 2 Y.LOU,T.J.CUMMINS,S.L.YUNG,S.K.VON SOLY,F.KAYSER,J.KURIYAN,  
JRNL        AUTH 3 M.RAPE,M.CARDOZO,M.A.GALLOP,N.F.BENCE,P.A.BARSANTI,A.SAHA    
JRNL        TITL   PROSPECTIVE DISCOVERY OF SMALL MOLECULE ENHANCERS OF AN E3   
JRNL        TITL 2 LIGASE-SUBSTRATE INTERACTION.                                
JRNL        REF    NAT COMMUN                    V.  10  1402 2019              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   30926793                                                     
JRNL        DOI    10.1038/S41467-019-09358-9                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 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) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.26                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.960                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 23426                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.204                           
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.238                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.660                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 858                             
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 44.2699 -  4.9045    0.99     3728   148  0.1713 0.2082        
REMARK   3     2  4.9045 -  3.8936    1.00     3760   152  0.1797 0.2135        
REMARK   3     3  3.8936 -  3.4016    1.00     3790   134  0.2296 0.2789        
REMARK   3     4  3.4016 -  3.0907    1.00     3821   134  0.2618 0.3207        
REMARK   3     5  3.0907 -  2.8692    1.00     3729   160  0.2972 0.2818        
REMARK   3     6  2.8692 -  2.7001    0.99     3740   130  0.3788 0.4194        
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)     : 0.430            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.080           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 92.92                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 118.0                          
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      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 20                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 33 THROUGH 45 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -57.4474   3.1806 -16.5201              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5506 T22:   0.7889                                     
REMARK   3      T33:   1.5733 T12:   0.1810                                     
REMARK   3      T13:   0.3953 T23:  -0.1078                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2190 L22:   0.1219                                     
REMARK   3      L33:   0.4374 L12:   0.0135                                     
REMARK   3      L13:   0.5292 L23:  -0.1568                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3779 S12:  -0.4831 S13:   0.5664                       
REMARK   3      S21:   1.4037 S22:  -0.2937 S23:   1.2563                       
REMARK   3      S31:  -0.5564 S32:   0.1989 S33:  -0.1925                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 46 THROUGH 60 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -50.1094   4.8858  -2.1238              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8014 T22:   1.0743                                     
REMARK   3      T33:   1.0886 T12:   0.1092                                     
REMARK   3      T13:   0.2415 T23:  -0.3463                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4189 L22:   2.7417                                     
REMARK   3      L33:   5.0218 L12:  -3.1596                                     
REMARK   3      L13:  -0.3182 L23:  -1.3228                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.5189 S12:  -1.8471 S13:   0.5412                       
REMARK   3      S21:   1.4891 S22:   0.8297 S23:  -0.6243                       
REMARK   3      S31:  -1.0303 S32:  -0.3711 S33:   0.4941                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 66 THROUGH 78 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -41.3899   1.9366   3.8560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7275 T22:   1.4887                                     
REMARK   3      T33:   1.2029 T12:   0.0418                                     
REMARK   3      T13:   0.1494 T23:  -0.5147                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5221 L22:   1.1430                                     
REMARK   3      L33:   2.5312 L12:  -1.2214                                     
REMARK   3      L13:   1.0304 L23:   0.9145                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.1187 S12:  -1.9191 S13:   0.7080                       
REMARK   3      S21:   0.8726 S22:   0.1120 S23:   1.1569                       
REMARK   3      S31:  -0.5176 S32:   0.5367 S33:   0.8876                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 79 THROUGH 94 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -44.8818  -2.9679  -8.8714              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2973 T22:   0.7218                                     
REMARK   3      T33:   1.0230 T12:  -0.1426                                     
REMARK   3      T13:   0.2336 T23:  -0.2267                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1280 L22:   1.4712                                     
REMARK   3      L33:   2.2415 L12:  -0.9691                                     
REMARK   3      L13:   0.5099 L23:  -0.8203                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4250 S12:  -0.7961 S13:  -0.0439                       
REMARK   3      S21:   0.1465 S22:   0.0425 S23:  -0.0847                       
REMARK   3      S31:  -0.7022 S32:   0.0419 S33:  -0.3312                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 95 THROUGH 109 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -35.7794  -0.6110  -4.0445              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7872 T22:   0.5632                                     
REMARK   3      T33:   0.9760 T12:  -0.4256                                     
REMARK   3      T13:   0.2707 T23:  -0.6978                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4972 L22:   0.3874                                     
REMARK   3      L33:   1.4663 L12:   0.1466                                     
REMARK   3      L13:  -1.4888 L23:   0.3877                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4745 S12:  -1.0927 S13:   0.8082                       
REMARK   3      S21:   0.6478 S22:  -0.7410 S23:   0.6571                       
REMARK   3      S31:  -1.1143 S32:  -0.3006 S33:   0.7074                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 110 THROUGH 121 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -27.6421 -13.9579   0.2276              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1797 T22:   1.1358                                     
REMARK   3      T33:   0.7700 T12:  -0.2459                                     
REMARK   3      T13:  -0.1366 T23:  -0.2269                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.7460 L22:   6.2150                                     
REMARK   3      L33:   1.6804 L12:   2.0631                                     
REMARK   3      L13:  -3.0755 L23:   0.3046                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6226 S12:  -0.6001 S13:  -1.0342                       
REMARK   3      S21:   1.3792 S22:   0.2289 S23:  -1.2023                       
REMARK   3      S31:   0.5651 S32:   0.6750 S33:   0.5310                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 122 THROUGH 139 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -20.9614 -20.6087  -9.7036              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2127 T22:   1.1414                                     
REMARK   3      T33:   1.3136 T12:  -0.2056                                     
REMARK   3      T13:   0.0565 T23:   0.0908                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3753 L22:   2.7631                                     
REMARK   3      L33:   4.9398 L12:   3.1754                                     
REMARK   3      L13:   0.3955 L23:   2.6142                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1667 S12:   1.2216 S13:  -0.8544                       
REMARK   3      S21:  -0.3762 S22:  -0.3946 S23:  -0.9586                       
REMARK   3      S31:   0.4286 S32:   0.2444 S33:   0.0534                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 30 THROUGH 38 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   3.0782  41.7958   4.8201              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1386 T22:   1.2703                                     
REMARK   3      T33:   1.1879 T12:  -0.2994                                     
REMARK   3      T13:   0.0050 T23:  -0.1756                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3043 L22:   3.6407                                     
REMARK   3      L33:   4.8773 L12:   1.3323                                     
REMARK   3      L13:  -1.3451 L23:   1.4290                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.3345 S12:  -1.0447 S13:   0.7316                       
REMARK   3      S21:   0.6836 S22:   0.4839 S23:  -1.5987                       
REMARK   3      S31:   0.1095 S32:   0.0806 S33:  -1.5125                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 138 THROUGH 153 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -39.4749 -12.1863  -9.2443              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3890 T22:   0.8356                                     
REMARK   3      T33:   0.9557 T12:  -0.4661                                     
REMARK   3      T13:   0.1360 T23:  -0.2275                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7861 L22:   2.7780                                     
REMARK   3      L33:   5.4907 L12:  -0.1653                                     
REMARK   3      L13:  -1.7443 L23:  -0.0908                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1682 S12:  -0.3510 S13:  -0.7967                       
REMARK   3      S21:  -0.0816 S22:  -0.0368 S23:   0.8675                       
REMARK   3      S31:   0.7596 S32:   0.6308 S33:  -0.0893                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 154 THROUGH 199 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -24.8462  -5.2128 -11.9206              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4448 T22:   0.9676                                     
REMARK   3      T33:   1.0867 T12:  -0.4132                                     
REMARK   3      T13:  -0.0385 T23:  -0.3216                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9072 L22:   2.1325                                     
REMARK   3      L33:   0.4164 L12:   1.1263                                     
REMARK   3      L13:  -0.6469 L23:  -0.9622                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2828 S12:  -0.1492 S13:   0.3385                       
REMARK   3      S21:  -0.0780 S22:  -0.1913 S23:  -0.7346                       
REMARK   3      S31:  -0.3252 S32:   0.2382 S33:   0.0166                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 200 THROUGH 210 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -10.5922   9.7190 -12.8774              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3961 T22:   0.9592                                     
REMARK   3      T33:   1.3910 T12:  -0.5309                                     
REMARK   3      T13:   0.0476 T23:  -0.1004                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.9355 L22:   7.4475                                     
REMARK   3      L33:   0.2781 L12:  -7.5950                                     
REMARK   3      L13:   0.9117 L23:  -1.0561                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3771 S12:  -0.3944 S13:   0.8905                       
REMARK   3      S21:  -0.6174 S22:  -0.1374 S23:   0.8312                       
REMARK   3      S31:   1.0222 S32:  -0.2641 S33:   0.5509                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 211 THROUGH 217 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -13.9994   5.1458 -21.0390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4082 T22:   1.2613                                     
REMARK   3      T33:   1.8608 T12:  -0.4940                                     
REMARK   3      T13:   0.2147 T23:  -0.0968                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0034 L22:   1.8288                                     
REMARK   3      L33:   6.0180 L12:   1.4355                                     
REMARK   3      L13:   3.1151 L23:  -0.9987                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5842 S12:   0.0023 S13:   1.0364                       
REMARK   3      S21:   0.5265 S22:  -1.6246 S23:  -0.0719                       
REMARK   3      S31:   0.5329 S32:  -0.5720 S33:   0.6695                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 227 THROUGH 252 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.8375   0.4721 -10.5460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4247 T22:   1.1868                                     
REMARK   3      T33:   1.7155 T12:  -0.3633                                     
REMARK   3      T13:   0.2067 T23:  -0.4237                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4836 L22:   1.2747                                     
REMARK   3      L33:   0.6170 L12:   0.8618                                     
REMARK   3      L13:   0.2403 L23:   0.5120                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2051 S12:   0.3444 S13:  -0.7325                       
REMARK   3      S21:   0.4864 S22:   0.5222 S23:  -1.3097                       
REMARK   3      S31:   0.1257 S32:   0.7623 S33:  -0.6825                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 253 THROUGH 333 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   0.5303  33.8774 -13.0035              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2151 T22:   1.2076                                     
REMARK   3      T33:   0.9810 T12:  -0.4530                                     
REMARK   3      T13:   0.0389 T23:  -0.0515                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9349 L22:   3.2592                                     
REMARK   3      L33:   2.7510 L12:  -0.0826                                     
REMARK   3      L13:  -0.5357 L23:  -1.0945                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3576 S12:   0.5859 S13:  -0.1020                       
REMARK   3      S21:  -1.0966 S22:   0.6904 S23:  -0.7997                       
REMARK   3      S31:  -0.1435 S32:   0.0221 S33:  -0.3929                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 334 THROUGH 416 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -13.5698  41.6462  -1.6295              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0058 T22:   1.2570                                     
REMARK   3      T33:   1.0323 T12:  -0.2061                                     
REMARK   3      T13:  -0.0581 T23:   0.2902                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2421 L22:   4.4650                                     
REMARK   3      L33:   2.5976 L12:  -0.0078                                     
REMARK   3      L13:  -0.4660 L23:  -0.2788                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2003 S12:   0.3204 S13:   0.3580                       
REMARK   3      S21:  -0.3675 S22:   0.3140 S23:   0.6249                       
REMARK   3      S31:  -0.5771 S32:  -0.7204 S33:  -0.3974                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 417 THROUGH 439 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -13.8206  34.2914   9.4411              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8998 T22:   1.0061                                     
REMARK   3      T33:   1.2205 T12:  -0.1751                                     
REMARK   3      T13:  -0.0089 T23:   0.1755                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0279 L22:   3.2123                                     
REMARK   3      L33:   3.8676 L12:  -1.4958                                     
REMARK   3      L13:   0.6699 L23:  -0.7961                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0672 S12:  -0.5856 S13:  -0.2149                       
REMARK   3      S21:   0.3930 S22:   0.4479 S23:   0.4110                       
REMARK   3      S31:  -0.1633 S32:  -0.5575 S33:  -0.3003                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 440 THROUGH 548 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.8472  22.5997   4.1690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8184 T22:   0.9221                                     
REMARK   3      T33:   1.2905 T12:  -0.2720                                     
REMARK   3      T13:  -0.1198 T23:  -0.0616                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5481 L22:   4.8794                                     
REMARK   3      L33:   3.6870 L12:   0.4377                                     
REMARK   3      L13:  -1.1310 L23:   0.9332                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2599 S12:   0.2410 S13:  -0.7668                       
REMARK   3      S21:  -0.1144 S22:   0.5802 S23:  -0.5115                       
REMARK   3      S31:   0.4536 S32:   0.0824 S33:  -0.4058                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 12 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -61.0030   2.5671  -9.7330              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5287 T22:   1.4052                                     
REMARK   3      T33:   1.7122 T12:  -0.0760                                     
REMARK   3      T13:   0.2729 T23:  -0.2882                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2292 L22:   1.9512                                     
REMARK   3      L33:   0.6613 L12:   0.5154                                     
REMARK   3      L13:   0.3928 L23:   1.0572                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2609 S12:  -1.0951 S13:   0.5737                       
REMARK   3      S21:  -1.2754 S22:  -0.1552 S23:  -0.5156                       
REMARK   3      S31:  -0.3031 S32:  -1.2793 S33:   0.3921                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 13 THROUGH 23 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -56.1664   9.9637  -7.4263              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.2019 T22:   1.2560                                     
REMARK   3      T33:   1.5086 T12:   0.3508                                     
REMARK   3      T13:   0.3722 T23:  -0.0058                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9359 L22:   4.3753                                     
REMARK   3      L33:   2.1966 L12:  -0.1817                                     
REMARK   3      L13:  -0.8759 L23:  -2.1449                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2907 S12:  -1.2936 S13:   0.5857                       
REMARK   3      S21:   0.6753 S22:   0.4789 S23:   0.7730                       
REMARK   3      S31:  -2.9662 S32:  -0.6387 S33:  -1.0964                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 24 THROUGH 32 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -52.4667   9.5218 -17.2782              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6751 T22:   0.8767                                     
REMARK   3      T33:   1.6831 T12:   0.1628                                     
REMARK   3      T13:   0.5318 T23:  -0.0743                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9726 L22:   2.2042                                     
REMARK   3      L33:   2.0928 L12:   0.3559                                     
REMARK   3      L13:  -1.2272 L23:  -0.5369                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.0576 S12:   1.2516 S13:   0.7671                       
REMARK   3      S21:  -0.3366 S22:  -0.0445 S23:   0.7854                       
REMARK   3      S31:  -1.4401 S32:  -0.5652 S33:  -0.8563                       
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 6M94 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-AUG-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000236270.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-MAY-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CLSI                               
REMARK 200  BEAMLINE                       : 08ID-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
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          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23440                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.264                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 4.512                              
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.3800                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.77                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.88500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.830                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 4000 0.1M BTP PH5.5, VAPOR        
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.63000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       75.26000            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23010 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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     LYS A   218                                                      
REMARK 465     ASN A   219                                                      
REMARK 465     LYS A   220                                                      
REMARK 465     PRO A   221                                                      
REMARK 465     PRO A   222                                                      
REMARK 465     ASP A   223                                                      
REMARK 465     GLY A   224                                                      
REMARK 465     ASN A   225                                                      
REMARK 465     ALA A   226                                                      
REMARK 465     ASP A   549                                                      
REMARK 465     PRO A   550                                                      
REMARK 465     ALA A   551                                                      
REMARK 465     ALA A   552                                                      
REMARK 465     GLN A   553                                                      
REMARK 465     ALA A   554                                                      
REMARK 465     GLU A   555                                                      
REMARK 465     PRO A   556                                                      
REMARK 465     PRO A   557                                                      
REMARK 465     ARG A   558                                                      
REMARK 465     SER A   559                                                      
REMARK 465     PRO A   560                                                      
REMARK 465     SER A   561                                                      
REMARK 465     ARG A   562                                                      
REMARK 465     THR A   563                                                      
REMARK 465     TYR A   564                                                      
REMARK 465     THR A   565                                                      
REMARK 465     TYR A   566                                                      
REMARK 465     ILE A   567                                                      
REMARK 465     SER A   568                                                      
REMARK 465     ARG A   569                                                      
REMARK 465     ASP B    61                                                      
REMARK 465     ASP B    62                                                      
REMARK 465     PRO B    63                                                      
REMARK 465     PRO B    64                                                      
REMARK 465     ASP B    65                                                      
REMARK 465     GLN B   140                                                      
REMARK 465     TRP B   141                                                      
REMARK 465     CYS B   142                                                      
REMARK 465     GLU B   143                                                      
REMARK 465     GLU B   144                                                      
REMARK 465     LYS B   145                                                      
REMARK 465     CYS C    16                                                      
REMARK 465     ASP C    17                                                      
REMARK 465     ARG C    18                                                      
REMARK 465     LYS C    19                                                      
REMARK 465     ALA C    20                                                      
REMARK 465     ALA C    21                                                      
REMARK 465     VAL C    22                                                      
REMARK 465     SER C    23                                                      
REMARK 465     HIS C    24                                                      
REMARK 465     TRP C    25                                                      
REMARK 465     GLN C    26                                                      
REMARK 465     GLN C    27                                                      
REMARK 465     GLN C    28                                                      
REMARK 465     SER C    29                                                      
REMARK 465     ALA C    39                                                      
REMARK 465     THR C    40                                                      
REMARK 465     THR C    41                                                      
REMARK 465     THR C    42                                                      
REMARK 465     ALA C    43                                                      
REMARK 465     PRO C    44                                                      
REMARK 465     SER C    45                                                      
REMARK 465     LEU C    46                                                      
REMARK 465     SER C    47                                                      
REMARK 465     GLY C    48                                                      
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     SER A 138    OG                                                  
REMARK 470     ASN A 159    CG   OD1  ND2                                       
REMARK 470     LYS A 167    CG   CD   CE   NZ                                   
REMARK 470     LYS A 177    CG   CD   CE   NZ                                   
REMARK 470     GLU A 194    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 198    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 209    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 214    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 244    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 247    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 251    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 254    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 263    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 265    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 268    CG   CD   CE   NZ                                   
REMARK 470     LYS A 290    CG   CD   CE   NZ                                   
REMARK 470     LYS A 300    CG   CD   CE   NZ                                   
REMARK 470     ARG A 301    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 317    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 318    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 330    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 338    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 356    CG   OD1  ND2                                       
REMARK 470     ASN A 357    CG   OD1  ND2                                       
REMARK 470     GLU A 470    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 471    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 480    CG   OD1  ND2                                       
REMARK 470     LYS A 481    CG   CD   CE   NZ                                   
REMARK 470     ARG A 504    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PRO B   2    CG   CD                                             
REMARK 470     LYS B   5    CG   CD   CE   NZ                                   
REMARK 470     GLU B  15    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  19    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  22    CG   CD   CE   NZ                                   
REMARK 470     LYS B  28    CG   CD   CE   NZ                                   
REMARK 470     LYS B  50    CG   CD   CE   NZ                                   
REMARK 470     LYS B  60    CG   CD   CE   NZ                                   
REMARK 470     ASP B  66    CG   OD1  OD2                                       
REMARK 470     GLU B  73    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  76    CG   CD   CE   NZ                                   
REMARK 470     LYS B  95    CG   CD   CE   NZ                                   
REMARK 470     LYS B 103    CG   CD   CE   NZ                                   
REMARK 470     LYS B 110    CG   CD   CE   NZ                                   
REMARK 470     GLU B 115    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 119    CG   CD   CE   NZ                                   
REMARK 470     GLU B 130    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 136    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 137    CG   CD   CE   NZ                                   
REMARK 470     TYR C  30    CG   CD1  CD2  CE1  CE2  CZ   OH                    
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 A   488     OD1  ASP C    32              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A 153       59.12   -110.00                                   
REMARK 500    THR A 266      -93.68   -118.85                                   
REMARK 500    LEU A 297       -0.15     68.42                                   
REMARK 500    ASP A 316     -158.47   -125.44                                   
REMARK 500    ARG A 318      -55.12   -133.16                                   
REMARK 500    HIS A 345      -57.47   -150.13                                   
REMARK 500    ASP A 399     -152.47   -146.47                                   
REMARK 500    ASP A 440     -109.62     56.52                                   
REMARK 500    ASP A 479     -148.06   -123.83                                   
REMARK 500    LYS A 481      -38.60   -139.05                                   
REMARK 500    ASP A 528     -148.33   -151.77                                   
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 PO4 A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 602                 
DBREF  6M94 A  139   569  UNP    Q9Y297   FBW1A_HUMAN    175    605             
DBREF  6M94 B    2   145  UNP    P63208   SKP1_HUMAN       2    163             
DBREF  6M94 C   17    48  UNP    P35222   CTNB1_HUMAN     17     48             
SEQADV 6M94 SER A  138  UNP  Q9Y297              EXPRESSION TAG                 
SEQADV 6M94     B       UNP  P63208    ASP    37 DELETION                       
SEQADV 6M94     B       UNP  P63208    ASP    38 DELETION                       
SEQADV 6M94     B       UNP  P63208    GLU    39 DELETION                       
SEQADV 6M94     B       UNP  P63208    GLY    40 DELETION                       
SEQADV 6M94     B       UNP  P63208    ASP    41 DELETION                       
SEQADV 6M94     B       UNP  P63208    ASP    42 DELETION                       
SEQADV 6M94     B       UNP  P63208    PRO    71 DELETION                       
SEQADV 6M94     B       UNP  P63208    PRO    72 DELETION                       
SEQADV 6M94     B       UNP  P63208    GLU    73 DELETION                       
SEQADV 6M94     B       UNP  P63208    ASP    74 DELETION                       
SEQADV 6M94     B       UNP  P63208    ASP    75 DELETION                       
SEQADV 6M94     B       UNP  P63208    GLU    76 DELETION                       
SEQADV 6M94     B       UNP  P63208    ASN    77 DELETION                       
SEQADV 6M94     B       UNP  P63208    LYS    78 DELETION                       
SEQADV 6M94     B       UNP  P63208    GLU    79 DELETION                       
SEQADV 6M94     B       UNP  P63208    LYS    80 DELETION                       
SEQADV 6M94     B       UNP  P63208    ARG    81 DELETION                       
SEQADV 6M94     B       UNP  P63208    THR    82 DELETION                       
SEQADV 6M94 CYS C   16  UNP  P35222              EXPRESSION TAG                 
SEQRES   1 A  432  SER MET LEU GLN ARG ASP PHE ILE THR ALA LEU PRO ALA          
SEQRES   2 A  432  ARG GLY LEU ASP HIS ILE ALA GLU ASN ILE LEU SER TYR          
SEQRES   3 A  432  LEU ASP ALA LYS SER LEU CYS ALA ALA GLU LEU VAL CYS          
SEQRES   4 A  432  LYS GLU TRP TYR ARG VAL THR SER ASP GLY MET LEU TRP          
SEQRES   5 A  432  LYS LYS LEU ILE GLU ARG MET VAL ARG THR ASP SER LEU          
SEQRES   6 A  432  TRP ARG GLY LEU ALA GLU ARG ARG GLY TRP GLY GLN TYR          
SEQRES   7 A  432  LEU PHE LYS ASN LYS PRO PRO ASP GLY ASN ALA PRO PRO          
SEQRES   8 A  432  ASN SER PHE TYR ARG ALA LEU TYR PRO LYS ILE ILE GLN          
SEQRES   9 A  432  ASP ILE GLU THR ILE GLU SER ASN TRP ARG CYS GLY ARG          
SEQRES  10 A  432  HIS SER LEU GLN ARG ILE HIS CYS ARG SER GLU THR SER          
SEQRES  11 A  432  LYS GLY VAL TYR CYS LEU GLN TYR ASP ASP GLN LYS ILE          
SEQRES  12 A  432  VAL SER GLY LEU ARG ASP ASN THR ILE LYS ILE TRP ASP          
SEQRES  13 A  432  LYS ASN THR LEU GLU CYS LYS ARG ILE LEU THR GLY HIS          
SEQRES  14 A  432  THR GLY SER VAL LEU CYS LEU GLN TYR ASP GLU ARG VAL          
SEQRES  15 A  432  ILE ILE THR GLY SER SER ASP SER THR VAL ARG VAL TRP          
SEQRES  16 A  432  ASP VAL ASN THR GLY GLU MET LEU ASN THR LEU ILE HIS          
SEQRES  17 A  432  HIS CYS GLU ALA VAL LEU HIS LEU ARG PHE ASN ASN GLY          
SEQRES  18 A  432  MET MET VAL THR CYS SER LYS ASP ARG SER ILE ALA VAL          
SEQRES  19 A  432  TRP ASP MET ALA SER PRO THR ASP ILE THR LEU ARG ARG          
SEQRES  20 A  432  VAL LEU VAL GLY HIS ARG ALA ALA VAL ASN VAL VAL ASP          
SEQRES  21 A  432  PHE ASP ASP LYS TYR ILE VAL SER ALA SER GLY ASP ARG          
SEQRES  22 A  432  THR ILE LYS VAL TRP ASN THR SER THR CYS GLU PHE VAL          
SEQRES  23 A  432  ARG THR LEU ASN GLY HIS LYS ARG GLY ILE ALA CYS LEU          
SEQRES  24 A  432  GLN TYR ARG ASP ARG LEU VAL VAL SER GLY SER SER ASP          
SEQRES  25 A  432  ASN THR ILE ARG LEU TRP ASP ILE GLU CYS GLY ALA CYS          
SEQRES  26 A  432  LEU ARG VAL LEU GLU GLY HIS GLU GLU LEU VAL ARG CYS          
SEQRES  27 A  432  ILE ARG PHE ASP ASN LYS ARG ILE VAL SER GLY ALA TYR          
SEQRES  28 A  432  ASP GLY LYS ILE LYS VAL TRP ASP LEU VAL ALA ALA LEU          
SEQRES  29 A  432  ASP PRO ARG ALA PRO ALA GLY THR LEU CYS LEU ARG THR          
SEQRES  30 A  432  LEU VAL GLU HIS SER GLY ARG VAL PHE ARG LEU GLN PHE          
SEQRES  31 A  432  ASP GLU PHE GLN ILE VAL SER SER SER HIS ASP ASP THR          
SEQRES  32 A  432  ILE LEU ILE TRP ASP PHE LEU ASN ASP PRO ALA ALA GLN          
SEQRES  33 A  432  ALA GLU PRO PRO ARG SER PRO SER ARG THR TYR THR TYR          
SEQRES  34 A  432  ILE SER ARG                                                  
SEQRES   1 B  144  PRO SER ILE LYS LEU GLN SER SER ASP GLY GLU ILE PHE          
SEQRES   2 B  144  GLU VAL ASP VAL GLU ILE ALA LYS GLN SER VAL THR ILE          
SEQRES   3 B  144  LYS THR MET LEU GLU ASP LEU GLY MET ASP PRO VAL PRO          
SEQRES   4 B  144  LEU PRO ASN VAL ASN ALA ALA ILE LEU LYS LYS VAL ILE          
SEQRES   5 B  144  GLN TRP CYS THR HIS HIS LYS ASP ASP PRO PRO ASP ASP          
SEQRES   6 B  144  ILE PRO VAL TRP ASP GLN GLU PHE LEU LYS VAL ASP GLN          
SEQRES   7 B  144  GLY THR LEU PHE GLU LEU ILE LEU ALA ALA ASN TYR LEU          
SEQRES   8 B  144  ASP ILE LYS GLY LEU LEU ASP VAL THR CYS LYS THR VAL          
SEQRES   9 B  144  ALA ASN MET ILE LYS GLY LYS THR PRO GLU GLU ILE ARG          
SEQRES  10 B  144  LYS THR PHE ASN ILE LYS ASN ASP PHE THR GLU GLU GLU          
SEQRES  11 B  144  GLU ALA GLN VAL ARG LYS GLU ASN GLN TRP CYS GLU GLU          
SEQRES  12 B  144  LYS                                                          
SEQRES   1 C   33  CYS ASP ARG LYS ALA ALA VAL SER HIS TRP GLN GLN GLN          
SEQRES   2 C   33  SER TYR LEU ASP SEP GLY ILE HIS SER GLY ALA THR THR          
SEQRES   3 C   33  THR ALA PRO SER LEU SER GLY                                  
MODRES 6M94 SEP C   33  SER  MODIFIED RESIDUE                                   
HET    SEP  C  33      10                                                       
HET    PO4  A 601       5                                                       
HET    DMS  A 602       4                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   3  SEP    C3 H8 N O6 P                                                 
FORMUL   4  PO4    O4 P 3-                                                      
FORMUL   5  DMS    C2 H6 O S                                                    
HELIX    1 AA1 ASP A  143  ARG A  151  1                                   9    
HELIX    2 AA2 LEU A  153  SER A  162  1                                  10    
HELIX    3 AA3 ASP A  165  LEU A  174  1                                  10    
HELIX    4 AA4 CYS A  176  GLY A  186  1                                  11    
HELIX    5 AA5 MET A  187  ASP A  200  1                                  14    
HELIX    6 AA6 ASP A  200  GLY A  211  1                                  12    
HELIX    7 AA7 TRP A  212  LEU A  216  5                                   5    
HELIX    8 AA8 PRO A  228  GLY A  253  1                                  26    
HELIX    9 AA9 LEU A  497  ASP A  502  1                                   6    
HELIX   10 AB1 VAL B   18  LYS B   22  1                                   5    
HELIX   11 AB2 SER B   24  ASP B   33  1                                  10    
HELIX   12 AB3 ASN B   45  HIS B   59  1                                  15    
HELIX   13 AB4 PRO B   68  LEU B   75  1                                   8    
HELIX   14 AB5 ASP B   78  ASP B   93  1                                  16    
HELIX   15 AB6 ILE B   94  LYS B  110  1                                  17    
HELIX   16 AB7 THR B  113  ASN B  122  1                                  10    
HELIX   17 AB8 THR B  128  GLU B  138  1                                  11    
SHEET    1 AA1 4 SER A 256  HIS A 261  0                                        
SHEET    2 AA1 4 THR A 540  ASP A 545 -1  O  ASP A 545   N  SER A 256           
SHEET    3 AA1 4 GLN A 531  SER A 536 -1  N  ILE A 532   O  TRP A 544           
SHEET    4 AA1 4 VAL A 522  PHE A 527 -1  N  GLN A 526   O  VAL A 533           
SHEET    1 AA2 4 VAL A 270  TYR A 275  0                                        
SHEET    2 AA2 4 LYS A 279  LEU A 284 -1  O  VAL A 281   N  GLN A 274           
SHEET    3 AA2 4 THR A 288  ASP A 293 -1  O  TRP A 292   N  ILE A 280           
SHEET    4 AA2 4 CYS A 299  THR A 304 -1  O  ARG A 301   N  ILE A 291           
SHEET    1 AA3 4 VAL A 310  TYR A 315  0                                        
SHEET    2 AA3 4 VAL A 319  SER A 324 -1  O  GLY A 323   N  CYS A 312           
SHEET    3 AA3 4 THR A 328  ASP A 333 -1  O  ARG A 330   N  THR A 322           
SHEET    4 AA3 4 MET A 339  ILE A 344 -1  O  ASN A 341   N  VAL A 331           
SHEET    1 AA4 4 VAL A 350  ASN A 356  0                                        
SHEET    2 AA4 4 MET A 359  SER A 364 -1  O  VAL A 361   N  ARG A 354           
SHEET    3 AA4 4 ILE A 369  MET A 374 -1  O  TRP A 372   N  MET A 360           
SHEET    4 AA4 4 ILE A 380  LEU A 386 -1  O  THR A 381   N  ASP A 373           
SHEET    1 AA5 4 VAL A 393  PHE A 398  0                                        
SHEET    2 AA5 4 TYR A 402  SER A 407 -1  O  VAL A 404   N  ASP A 397           
SHEET    3 AA5 4 THR A 411  ASN A 416 -1  O  TRP A 415   N  ILE A 403           
SHEET    4 AA5 4 PHE A 422  ASN A 427 -1  O  VAL A 423   N  VAL A 414           
SHEET    1 AA6 4 ILE A 433  ARG A 439  0                                        
SHEET    2 AA6 4 LEU A 442  SER A 447 -1  O  VAL A 444   N  GLN A 437           
SHEET    3 AA6 4 THR A 451  ASP A 456 -1  O  TRP A 455   N  VAL A 443           
SHEET    4 AA6 4 CYS A 462  GLU A 467 -1  O  LEU A 466   N  ILE A 452           
SHEET    1 AA7 4 VAL A 473  PHE A 478  0                                        
SHEET    2 AA7 4 ARG A 482  ALA A 487 -1  O  VAL A 484   N  ARG A 477           
SHEET    3 AA7 4 LYS A 491  ASP A 496 -1  O  LYS A 491   N  ALA A 487           
SHEET    4 AA7 4 CYS A 511  VAL A 516 -1  O  LEU A 515   N  ILE A 492           
SHEET    1 AA8 3 ILE B  13  ASP B  17  0                                        
SHEET    2 AA8 3 SER B   3  GLN B   7 -1  N  ILE B   4   O  VAL B  16           
SHEET    3 AA8 3 VAL B  39  PRO B  40  1  O  VAL B  39   N  GLN B   7           
LINK         C   ASP C  32                 N   SEP C  33     1555   1555  1.33  
LINK         C   SEP C  33                 N   GLY C  34     1555   1555  1.33  
CISPEP   1 ASP B   37    PRO B   38          0         2.00                     
SITE     1 AC1  5 GLN A 437  ARG A 477  PHE A 478  GLN A 526                    
SITE     2 AC1  5 PHE A 527                                                     
SITE     1 AC2  6 ASN A 394  GLY A 408  GLY A 432  SER A 448                    
SITE     2 AC2  6 HIS C  36  SER C  37                                          
CRYST1   82.370   82.370  112.890  90.00  90.00 120.00 P 31          3          
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      0.012140  0.007009  0.000000        0.00000                         
SCALE2      0.000000  0.014018  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008858        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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