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Database: PDB
Entry: 6M92
LinkDB: 6M92
Original site: 6M92 
HEADER    LIGASE                                  22-AUG-18   6M92              
TITLE     MONOPHOSPHORYLATED PSER33 B-CATENIN PEPTIDE, B-TRCP/SKP1, NRX-2663    
TITLE    2 TERNARY 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,S.J.LEE   
REVDAT   3   15-JAN-20 6M92    1       REMARK                                   
REVDAT   2   10-APR-19 6M92    1       JRNL                                     
REVDAT   1   03-APR-19 6M92    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.    2.35 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) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.30                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.960                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 35234                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.221                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.770                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1330                            
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 41.3014 -  4.8858    0.99     3730   149  0.1703 0.1865        
REMARK   3     2  4.8858 -  3.8789    1.00     3780   144  0.1563 0.1804        
REMARK   3     3  3.8789 -  3.3889    1.00     3787   134  0.1923 0.2384        
REMARK   3     4  3.3889 -  3.0791    1.00     3774   142  0.2111 0.2605        
REMARK   3     5  3.0791 -  2.8585    1.00     3769   154  0.2174 0.2861        
REMARK   3     6  2.8585 -  2.6900    1.00     3759   149  0.2204 0.2556        
REMARK   3     7  2.6900 -  2.5553    1.00     3778   146  0.2570 0.3079        
REMARK   3     8  2.5553 -  2.4441    1.00     3779   156  0.2859 0.3471        
REMARK   3     9  2.4441 -  2.3500    1.00     3748   156  0.3158 0.3381        
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)     : 0.340            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.900           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 68.05                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 85.76                          
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  : 10                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 138 THROUGH 252 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  20.7738  -3.1735  10.4869              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0459 T22:   0.6035                                     
REMARK   3      T33:   0.8397 T12:   0.2995                                     
REMARK   3      T13:  -0.0291 T23:   0.0562                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1940 L22:   2.8224                                     
REMARK   3      L33:   0.6270 L12:  -1.1679                                     
REMARK   3      L13:   0.9446 L23:  -0.2373                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1439 S12:   0.0252 S13:   0.1613                       
REMARK   3      S21:   0.0089 S22:  -0.1863 S23:   0.5022                       
REMARK   3      S31:   0.2205 S32:   0.0274 S33:   0.0535                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 253 THROUGH 547 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   5.8315  31.1268   0.7762              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5529 T22:   0.5466                                     
REMARK   3      T33:   0.6103 T12:   0.1935                                     
REMARK   3      T13:  -0.0684 T23:  -0.0481                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9780 L22:   3.2219                                     
REMARK   3      L33:   2.5691 L12:   0.1615                                     
REMARK   3      L13:  -0.4690 L23:  -0.0378                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0426 S12:   0.0741 S13:  -0.3732                       
REMARK   3      S21:   0.2498 S22:   0.1012 S23:  -0.0243                       
REMARK   3      S31:   0.0984 S32:   0.1811 S33:  -0.1524                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 7 )                     
REMARK   3    ORIGIN FOR THE GROUP (A):  61.2551   7.9252   8.1689              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4949 T22:   1.0020                                     
REMARK   3      T33:   1.2298 T12:  -0.0926                                     
REMARK   3      T13:   0.2006 T23:   0.2974                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0332 L22:   2.8501                                     
REMARK   3      L33:   0.6144 L12:   0.3003                                     
REMARK   3      L13:  -0.1442 L23:  -1.3221                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2900 S12:  -0.0991 S13:   0.6559                       
REMARK   3      S21:   0.8727 S22:  -0.0907 S23:  -0.5672                       
REMARK   3      S31:  -1.3744 S32:   0.7407 S33:  -0.0338                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 8 THROUGH 23 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  57.6019   5.4366   5.8598              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4157 T22:   1.1834                                     
REMARK   3      T33:   0.8901 T12:  -0.0512                                     
REMARK   3      T13:   0.2683 T23:   0.4038                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2510 L22:   4.3465                                     
REMARK   3      L33:   3.1800 L12:   0.6011                                     
REMARK   3      L13:   0.2886 L23:  -0.5502                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0555 S12:   0.6532 S13:   0.7966                       
REMARK   3      S21:  -0.4884 S22:  -0.6223 S23:   0.0046                       
REMARK   3      S31:  -1.5532 S32:   0.7488 S33:   0.6696                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 24 THROUGH 68 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  52.2067   5.3611   7.8141              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6180 T22:   0.8863                                     
REMARK   3      T33:   0.9897 T12:   0.0140                                     
REMARK   3      T13:   0.2946 T23:   0.3254                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4774 L22:   2.9747                                     
REMARK   3      L33:   2.5038 L12:   0.4062                                     
REMARK   3      L13:   0.5626 L23:  -0.5208                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0490 S12:   0.7710 S13:   0.9509                       
REMARK   3      S21:  -0.6555 S22:  -0.1910 S23:  -0.7773                       
REMARK   3      S31:  -1.3198 S32:   0.2675 S33:   0.3398                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 69 THROUGH 78 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  42.7010  -0.2331  -6.2777              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5296 T22:   1.1352                                     
REMARK   3      T33:   0.7931 T12:   0.0021                                     
REMARK   3      T13:   0.1134 T23:   0.2807                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6728 L22:   2.1346                                     
REMARK   3      L33:   7.6729 L12:  -0.8547                                     
REMARK   3      L13:   2.5554 L23:  -3.9493                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6113 S12:   1.5238 S13:   0.4515                       
REMARK   3      S21:  -0.0962 S22:   0.2602 S23:   0.2450                       
REMARK   3      S31:  -0.7604 S32:   0.0867 S33:   0.3826                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 79 THROUGH 109 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  40.8826  -2.3498   4.9549              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3945 T22:   0.7052                                     
REMARK   3      T33:   0.6419 T12:   0.2473                                     
REMARK   3      T13:   0.1760 T23:   0.2175                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7697 L22:   0.8624                                     
REMARK   3      L33:   1.8864 L12:   0.1070                                     
REMARK   3      L13:   1.6946 L23:   0.0203                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5563 S12:   0.8220 S13:   0.4399                       
REMARK   3      S21:  -0.3985 S22:  -0.3176 S23:  -0.3453                       
REMARK   3      S31:  -0.2525 S32:   0.5295 S33:  -0.0881                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 110 THROUGH 121 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  27.8648 -15.0843  -1.2524              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4793 T22:   0.8638                                     
REMARK   3      T33:   0.5097 T12:   0.4213                                     
REMARK   3      T13:  -0.2045 T23:   0.0933                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.9376 L22:   6.1242                                     
REMARK   3      L33:   1.0704 L12:  -0.4679                                     
REMARK   3      L13:  -2.3668 L23:  -1.3385                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6523 S12:   0.6767 S13:  -0.3839                       
REMARK   3      S21:  -1.4823 S22:   0.2555 S23:   0.6688                       
REMARK   3      S31:   1.0049 S32:  -0.1410 S33:   0.0631                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 122 THROUGH 139 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  21.7403 -21.4885   8.9313              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2174 T22:   0.6613                                     
REMARK   3      T33:   0.9336 T12:   0.3474                                     
REMARK   3      T13:   0.0005 T23:  -0.1164                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0834 L22:   1.0338                                     
REMARK   3      L33:   2.7231 L12:   2.2439                                     
REMARK   3      L13:  -1.9910 L23:  -1.0881                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4438 S12:   0.3406 S13:  -0.3367                       
REMARK   3      S21:  -0.4010 S22:  -0.4739 S23:   0.2820                       
REMARK   3      S31:  -0.0472 S32:  -0.1296 S33:   0.1117                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 30 THROUGH 39 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.7907  41.8508  -5.4343              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7274 T22:   0.8723                                     
REMARK   3      T33:   0.6809 T12:   0.2385                                     
REMARK   3      T13:  -0.0200 T23:   0.0686                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4742 L22:   4.7177                                     
REMARK   3      L33:   2.1492 L12:  -0.3960                                     
REMARK   3      L13:   1.2131 L23:   2.2493                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1585 S12:   1.4087 S13:   0.3942                       
REMARK   3      S21:  -0.2886 S22:   0.1103 S23:   0.7207                       
REMARK   3      S31:  -0.7993 S32:  -0.5584 S33:  -0.0448                       
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 6M92 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_1000236374.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-SEP-14                          
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   : 35242                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.295                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 4.838                              
REMARK 200  R MERGE                    (I) : 0.04600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.2900                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.41                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.54                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.52600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.920                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
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   (%): 59.83                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.06                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 4000 0.1M BTP PH 5.5, 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       37.03667            
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       74.07333            
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: 4280 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23370 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 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     ASN A   548                                                      
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     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     LYS A 167    CG   CD   CE   NZ                                   
REMARK 470     LYS A 177    CG   CD   CE   NZ                                   
REMARK 470     ARG A 198    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 209    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 244    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     GLU A 265    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 300    CG   CD   CE   NZ                                   
REMARK 470     LYS A 430    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     ASP B  17    CG   OD1  OD2                                       
REMARK 470     GLU B  19    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  28    CG   CD   CE   NZ                                   
REMARK 470     LYS B  50    CG   CD   CE   NZ                                   
REMARK 470     LYS B  51    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 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   OE2  GLU A   470     NZ   LYS A   491              2.15            
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    THR A 266      -79.96   -118.68                                   
REMARK 500    ASN A 287        4.08     88.08                                   
REMARK 500    ASP A 316     -159.20   -130.05                                   
REMARK 500    SER A 327        6.55     80.21                                   
REMARK 500    HIS A 345      -54.87   -163.48                                   
REMARK 500    ASN A 356      137.59   -175.87                                   
REMARK 500    ARG A 367        7.13     83.04                                   
REMARK 500    ASP A 440     -113.16     60.24                                   
REMARK 500    ARG A 464      137.00   -171.96                                   
REMARK 500    ASP A 479     -157.06   -123.13                                   
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 J8V A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 602                 
DBREF  6M92 A  139   569  UNP    Q9Y297   FBW1A_HUMAN    175    605             
DBREF  6M92 B    2   145  UNP    P63208   SKP1_HUMAN       2    163             
DBREF  6M92 C   17    48  UNP    P35222   CTNB1_HUMAN     17     48             
SEQADV 6M92 SER A  138  UNP  Q9Y297              EXPRESSION TAG                 
SEQADV 6M92     B       UNP  P63208    ASP    37 DELETION                       
SEQADV 6M92     B       UNP  P63208    ASP    38 DELETION                       
SEQADV 6M92     B       UNP  P63208    GLU    39 DELETION                       
SEQADV 6M92     B       UNP  P63208    GLY    40 DELETION                       
SEQADV 6M92     B       UNP  P63208    ASP    41 DELETION                       
SEQADV 6M92     B       UNP  P63208    ASP    42 DELETION                       
SEQADV 6M92     B       UNP  P63208    PRO    71 DELETION                       
SEQADV 6M92     B       UNP  P63208    PRO    72 DELETION                       
SEQADV 6M92     B       UNP  P63208    GLU    73 DELETION                       
SEQADV 6M92     B       UNP  P63208    ASP    74 DELETION                       
SEQADV 6M92     B       UNP  P63208    ASP    75 DELETION                       
SEQADV 6M92     B       UNP  P63208    GLU    76 DELETION                       
SEQADV 6M92     B       UNP  P63208    ASN    77 DELETION                       
SEQADV 6M92     B       UNP  P63208    LYS    78 DELETION                       
SEQADV 6M92     B       UNP  P63208    GLU    79 DELETION                       
SEQADV 6M92     B       UNP  P63208    LYS    80 DELETION                       
SEQADV 6M92     B       UNP  P63208    ARG    81 DELETION                       
SEQADV 6M92     B       UNP  P63208    THR    82 DELETION                       
SEQADV 6M92 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 6M92 SEP C   33  SER  MODIFIED RESIDUE                                   
HET    SEP  C  33      10                                                       
HET    J8V  A 601      30                                                       
HET    PO4  A 602       5                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     J8V 3-{[2-OXO-4-PHENOXY-6-(TRIFLUOROMETHYL)-1,2-                     
HETNAM   2 J8V  DIHYDROPYRIDINE-3-CARBONYL]AMINO}BENZOIC ACID                   
HETNAM     PO4 PHOSPHATE ION                                                    
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   3  SEP    C3 H8 N O6 P                                                 
FORMUL   4  J8V    C20 H13 F3 N2 O5                                             
FORMUL   5  PO4    O4 P 3-                                                      
FORMUL   6  HOH   *37(H2 O)                                                     
HELIX    1 AA1 ASP A  143  ARG A  151  1                                   9    
HELIX    2 AA2 LEU A  153  TYR A  163  1                                  11    
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 PRO A  506  THR A  509  5                                   4    
HELIX   11 AB2 VAL B   18  LYS B   22  1                                   5    
HELIX   12 AB3 SER B   24  ASP B   33  1                                  10    
HELIX   13 AB4 ASN B   45  HIS B   59  1                                  15    
HELIX   14 AB5 PRO B   68  LEU B   75  1                                   8    
HELIX   15 AB6 ASP B   78  ASP B   93  1                                  16    
HELIX   16 AB7 ILE B   94  LYS B  110  1                                  17    
HELIX   17 AB8 THR B  113  ASN B  122  1                                  10    
HELIX   18 AB9 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  ILE A 541   N  ILE A 260           
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 ILE A 289  ASP A 293 -1  O  TRP A 292   N  ILE A 280           
SHEET    4 AA2 4 CYS A 299  LEU A 303 -1  O  LEU A 303   N  ILE A 289           
SHEET    1 AA3 4 VAL A 310  TYR A 315  0                                        
SHEET    2 AA3 4 VAL A 319  SER A 324 -1  O  ILE A 321   N  GLN A 314           
SHEET    3 AA3 4 THR A 328  ASP A 333 -1  O  TRP A 332   N  ILE A 320           
SHEET    4 AA3 4 MET A 339  ILE A 344 -1  O  LEU A 340   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 SER A 368  SER A 376 -1  O  TRP A 372   N  MET A 360           
SHEET    4 AA4 4 ASP A 379  VAL A 387 -1  O  ARG A 383   N  VAL A 371           
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 ILE A 412  ASN A 416 -1  O  LYS A 413   N  SER A 405           
SHEET    4 AA5 4 PHE A 422  LEU A 426 -1  O  ARG A 424   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  LEU A 442   N  ARG A 439           
SHEET    3 AA6 4 ILE A 452  ASP A 456 -1  O  TRP A 455   N  VAL A 443           
SHEET    4 AA6 4 CYS A 462  LEU A 466 -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  TRP A 495   N  ILE A 483           
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        -5.62                     
SITE     1 AC1 15 ARG A 330  MET A 339  THR A 342  ASN A 394                    
SITE     2 AC1 15 GLY A 408  ARG A 410  ARG A 431  GLY A 432                    
SITE     3 AC1 15 ILE A 433  ALA A 434  SER A 448  TYR A 488                    
SITE     4 AC1 15 ILE C  35  HIS C  36  SER C  37                               
SITE     1 AC2  6 GLN A 437  ARG A 477  PHE A 478  GLN A 526                    
SITE     2 AC2  6 PHE A 527  HOH A 701                                          
CRYST1   82.590   82.590  111.110  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      0.012108  0.006991  0.000000        0.00000                         
SCALE2      0.000000  0.013981  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system