GenomeNet

Database: PDB
Entry: 6C9J
LinkDB: 6C9J
Original site: 6C9J 
HEADER    TRANSFERASE                             26-JAN-18   6C9J              
TITLE     AMP-ACTIVATED PROTEIN KINASE BOUND TO PHARMACOLOGICAL ACTIVATOR R734  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-1; 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: AMPK SUBUNIT ALPHA-1,ACETYL-COA CARBOXYLASE KINASE,ACACA    
COMPND   5 KINASE,HYDROXYMETHYLGLUTARYL-COA REDUCTASE KINASE,HMGCR KINASE,TAU-  
COMPND   6 PROTEIN KINASE PRKAA1;                                               
COMPND   7 EC: 2.7.11.1,2.7.11.27,2.7.11.31,2.7.11.26;                          
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES;                                                       
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-1;            
COMPND  12 CHAIN: B;                                                            
COMPND  13 SYNONYM: AMPKB;                                                      
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 3;                                                           
COMPND  16 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT GAMMA-1;           
COMPND  17 CHAIN: C;                                                            
COMPND  18 SYNONYM: AMPKG;                                                      
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: PRKAA1, AMPK1;                                                 
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: PRKAB1, AMPK;                                                  
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  17 ORGANISM_COMMON: HUMAN;                                              
SOURCE  18 ORGANISM_TAXID: 9606;                                                
SOURCE  19 GENE: PRKAG1;                                                        
SOURCE  20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    AMPK, ACTIVATOR, TRANSFERASE                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.YAN,X.E.ZHOU,S.NOVICK,S.J.SHAW,Y.LI,J.S.BRUNZELLE,Y.HITOSHI,        
AUTHOR   2 P.R.GRIFFIN,H.E.XU,K.MELCHER                                         
REVDAT   3   30-JAN-19 6C9J    1       JRNL                                     
REVDAT   2   12-DEC-18 6C9J    1       JRNL                                     
REVDAT   1   28-NOV-18 6C9J    0                                                
JRNL        AUTH   Y.YAN,X.E.ZHOU,S.J.NOVICK,S.J.SHAW,Y.LI,J.S.BRUNZELLE,       
JRNL        AUTH 2 Y.HITOSHI,P.R.GRIFFIN,H.E.XU,K.MELCHER                       
JRNL        TITL   STRUCTURES OF AMP-ACTIVATED PROTEIN KINASE BOUND TO NOVEL    
JRNL        TITL 2 PHARMACOLOGICAL ACTIVATORS IN PHOSPHORYLATED,                
JRNL        TITL 3 NON-PHOSPHORYLATED, AND NUCLEOTIDE-FREE STATES.              
JRNL        REF    J. BIOL. CHEM.                V. 294   953 2019              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   30478170                                                     
JRNL        DOI    10.1074/JBC.RA118.004883                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.05 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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.65                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 32702                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.215                           
REMARK   3   R VALUE            (WORKING SET) : 0.214                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.240                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2366                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 49.6525 -  7.8329    0.99     2193   157  0.1846 0.1968        
REMARK   3     2  7.8329 -  6.2211    1.00     2016   179  0.2123 0.2154        
REMARK   3     3  6.2211 -  5.4358    1.00     1999   159  0.2156 0.2091        
REMARK   3     4  5.4358 -  4.9393    1.00     1961   155  0.1902 0.2165        
REMARK   3     5  4.9393 -  4.5855    1.00     1971   152  0.1858 0.1825        
REMARK   3     6  4.5855 -  4.3153    1.00     1940   161  0.1799 0.2130        
REMARK   3     7  4.3153 -  4.0993    1.00     1916   160  0.1914 0.2182        
REMARK   3     8  4.0993 -  3.9210    1.00     1931   164  0.2065 0.2307        
REMARK   3     9  3.9210 -  3.7701    1.00     1940   139  0.2122 0.2203        
REMARK   3    10  3.7701 -  3.6400    1.00     1922   137  0.2401 0.2436        
REMARK   3    11  3.6400 -  3.5262    1.00     1908   153  0.2411 0.2327        
REMARK   3    12  3.5262 -  3.4255    1.00     1912   146  0.2566 0.2705        
REMARK   3    13  3.4255 -  3.3353    0.95     1835   125  0.2756 0.2422        
REMARK   3    14  3.3353 -  3.2539    0.75     1457    94  0.2892 0.3761        
REMARK   3    15  3.2539 -  3.1800    0.66     1265   104  0.3156 0.2955        
REMARK   3    16  3.1800 -  3.1123    0.59     1122    89  0.3266 0.2641        
REMARK   3    17  3.1123 -  3.0501    0.55     1048    92  0.3644 0.3893        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.00                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.300            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.370           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.004           7211                                  
REMARK   3   ANGLE     :  0.782           9796                                  
REMARK   3   CHIRALITY :  0.053           1104                                  
REMARK   3   PLANARITY :  0.006           1218                                  
REMARK   3   DIHEDRAL  :  9.531           4308                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 22                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 11 THROUGH 42 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.4087  26.6555 -32.2436              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5313 T22:   0.4342                                     
REMARK   3      T33:   0.4644 T12:  -0.0018                                     
REMARK   3      T13:  -0.0032 T23:  -0.1105                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4075 L22:   2.6043                                     
REMARK   3      L33:   3.3250 L12:   1.4153                                     
REMARK   3      L13:   1.3679 L23:  -0.0344                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0232 S12:   0.2448 S13:   0.1290                       
REMARK   3      S21:  -0.1052 S22:   0.0877 S23:  -0.0958                       
REMARK   3      S31:  -0.2111 S32:   0.1166 S33:  -0.1109                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 43 THROUGH 72 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -23.1264  36.2116 -30.5525              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6193 T22:   0.5275                                     
REMARK   3      T33:   0.5061 T12:  -0.0339                                     
REMARK   3      T13:   0.0296 T23:  -0.0462                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5482 L22:   0.6874                                     
REMARK   3      L33:   2.3805 L12:  -0.9195                                     
REMARK   3      L13:   1.5376 L23:  -0.1674                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0054 S12:  -0.0829 S13:   0.1498                       
REMARK   3      S21:  -0.0419 S22:   0.0156 S23:   0.1866                       
REMARK   3      S31:  -0.4875 S32:  -0.3542 S33:  -0.0102                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 73 THROUGH 162 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -19.5643  25.0595 -16.4564              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4520 T22:   0.3911                                     
REMARK   3      T33:   0.4120 T12:   0.0315                                     
REMARK   3      T13:  -0.0358 T23:  -0.1145                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5481 L22:   0.7438                                     
REMARK   3      L33:   0.9594 L12:   0.1988                                     
REMARK   3      L13:  -0.3099 L23:  -0.4152                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0125 S12:  -0.0178 S13:   0.0362                       
REMARK   3      S21:   0.0108 S22:  -0.0036 S23:  -0.0426                       
REMARK   3      S31:  -0.1251 S32:  -0.0328 S33:   0.0161                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 163 THROUGH 194 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -38.6937  30.7522 -17.6189              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6593 T22:   0.6276                                     
REMARK   3      T33:   0.5693 T12:   0.0732                                     
REMARK   3      T13:  -0.0442 T23:  -0.0993                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0796 L22:   3.6102                                     
REMARK   3      L33:   1.0679 L12:   0.5547                                     
REMARK   3      L13:  -0.1346 L23:   1.1799                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0356 S12:   0.0594 S13:   0.1688                       
REMARK   3      S21:  -0.1362 S22:  -0.0087 S23:   0.2391                       
REMARK   3      S31:  -0.2442 S32:  -0.2111 S33:   0.0443                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 195 THROUGH 250 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -35.8901  14.8371  -9.0951              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4521 T22:   0.4497                                     
REMARK   3      T33:   0.4318 T12:   0.0454                                     
REMARK   3      T13:  -0.0189 T23:  -0.1090                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8918 L22:   0.8845                                     
REMARK   3      L33:   0.9783 L12:  -0.2652                                     
REMARK   3      L13:   0.2199 L23:  -0.0191                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0050 S12:   0.0212 S13:  -0.1067                       
REMARK   3      S21:  -0.0782 S22:   0.0071 S23:   0.1731                       
REMARK   3      S31:   0.0248 S32:  -0.2524 S33:  -0.0121                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 251 THROUGH 370 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -32.2159  33.0936   5.2525              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7240 T22:   0.6586                                     
REMARK   3      T33:   0.6780 T12:   0.0484                                     
REMARK   3      T13:  -0.0242 T23:  -0.0888                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8216 L22:   0.3734                                     
REMARK   3      L33:   0.5632 L12:  -0.5539                                     
REMARK   3      L13:  -0.6802 L23:   0.4586                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0611 S12:  -0.4401 S13:   0.5292                       
REMARK   3      S21:   0.2204 S22:   0.0995 S23:  -0.0326                       
REMARK   3      S31:  -0.3743 S32:  -0.0883 S33:  -0.1606                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 371 THROUGH 550 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -52.4899  51.5232 -15.9957              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3072 T22:   1.1343                                     
REMARK   3      T33:   1.0946 T12:   0.4285                                     
REMARK   3      T13:  -0.0313 T23:  -0.1665                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3768 L22:   0.3152                                     
REMARK   3      L33:   2.5430 L12:  -0.3042                                     
REMARK   3      L13:   0.3809 L23:   0.0799                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1407 S12:   0.2891 S13:   0.0841                       
REMARK   3      S21:  -0.4095 S22:  -0.0999 S23:   0.0746                       
REMARK   3      S31:  -0.2087 S32:  -0.0308 S33:  -0.0408                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 74 THROUGH 148 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -10.9765  32.2015 -52.1563              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5478 T22:   0.4651                                     
REMARK   3      T33:   0.4566 T12:  -0.1135                                     
REMARK   3      T13:   0.0065 T23:  -0.1013                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6995 L22:   1.9502                                     
REMARK   3      L33:   3.1018 L12:  -0.3451                                     
REMARK   3      L13:  -0.1205 L23:  -0.3043                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0189 S12:  -0.1324 S13:   0.1965                       
REMARK   3      S21:   0.1669 S22:  -0.0626 S23:  -0.0467                       
REMARK   3      S31:  -0.2378 S32:   0.0313 S33:   0.0815                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 149 THROUGH 207 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -30.7559  44.7066 -35.7549              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0083 T22:   0.9866                                     
REMARK   3      T33:   1.0523 T12:   0.0521                                     
REMARK   3      T13:   0.0044 T23:  -0.0548                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0000 L22:   0.0000                                     
REMARK   3      L33:   0.0000 L12:   0.0000                                     
REMARK   3      L13:   0.0000 L23:   0.0000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0478 S12:  -0.0561 S13:   0.3108                       
REMARK   3      S21:   0.0744 S22:   0.0253 S23:   0.2347                       
REMARK   3      S31:  -0.2198 S32:  -0.2286 S33:  -0.0731                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 208 THROUGH 226 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -43.4601  43.2411   4.5662              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1592 T22:   1.1807                                     
REMARK   3      T33:   1.1278 T12:   0.3493                                     
REMARK   3      T13:   0.1220 T23:  -0.1766                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0000 L22:   0.0000                                     
REMARK   3      L33:   0.0000 L12:   0.0000                                     
REMARK   3      L13:   0.0000 L23:   0.0000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2109 S12:  -0.5448 S13:   0.1202                       
REMARK   3      S21:   0.7382 S22:  -0.0158 S23:  -0.3841                       
REMARK   3      S31:   0.3226 S32:   0.1666 S33:  -0.1950                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 227 THROUGH 270 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -44.8359  51.0542  -3.1260              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9340 T22:   0.9144                                     
REMARK   3      T33:   0.8800 T12:   0.3282                                     
REMARK   3      T13:   0.1336 T23:  -0.1499                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3731 L22:   1.9836                                     
REMARK   3      L33:   1.8792 L12:   0.2305                                     
REMARK   3      L13:  -0.1373 L23:   0.2993                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0073 S12:  -0.0735 S13:   0.0206                       
REMARK   3      S21:   0.0437 S22:  -0.0131 S23:   0.0212                       
REMARK   3      S31:  -0.0643 S32:  -0.0500 S33:   0.0059                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 25 THROUGH 48 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -24.1770  59.9191   5.6380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9757 T22:   1.0455                                     
REMARK   3      T33:   1.1737 T12:   0.1135                                     
REMARK   3      T13:   0.1085 T23:  -0.1010                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6336 L22:   0.4562                                     
REMARK   3      L33:   0.0755 L12:   0.8633                                     
REMARK   3      L13:   0.3513 L23:   0.1856                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0021 S12:  -0.2045 S13:   0.1585                       
REMARK   3      S21:   0.1968 S22:  -0.0496 S23:  -0.3844                       
REMARK   3      S31:  -0.2846 S32:   0.3553 S33:   0.0517                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 49 THROUGH 112 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -52.9843  67.7601   9.0558              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8543 T22:   0.7643                                     
REMARK   3      T33:   0.9301 T12:   0.2291                                     
REMARK   3      T13:   0.1918 T23:  -0.0733                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3040 L22:   0.5588                                     
REMARK   3      L33:   2.2343 L12:  -0.3161                                     
REMARK   3      L13:  -0.8234 L23:   0.8250                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0129 S12:   0.2138 S13:  -0.0001                       
REMARK   3      S21:  -0.2352 S22:  -0.0369 S23:  -0.0628                       
REMARK   3      S31:  -0.0926 S32:  -0.0805 S33:   0.0241                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 113 THROUGH 136 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -43.0670  74.6801   3.5170              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1977 T22:   1.2983                                     
REMARK   3      T33:   1.4145 T12:   0.1834                                     
REMARK   3      T13:   0.1640 T23:  -0.1555                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9417 L22:   0.4099                                     
REMARK   3      L33:   0.6775 L12:  -1.4233                                     
REMARK   3      L13:  -1.8297 L23:   0.5270                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0169 S12:  -0.0366 S13:   0.6901                       
REMARK   3      S21:  -0.0086 S22:   0.2096 S23:  -0.5940                       
REMARK   3      S31:  -0.2986 S32:   0.3595 S33:  -0.2266                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 137 THROUGH 155 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -30.3521  70.0802   7.6699              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0745 T22:   1.2542                                     
REMARK   3      T33:   1.4571 T12:   0.1080                                     
REMARK   3      T13:   0.1661 T23:  -0.1780                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8320 L22:   0.3305                                     
REMARK   3      L33:   0.8606 L12:   0.5244                                     
REMARK   3      L13:   0.8462 L23:   0.5333                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0229 S12:  -0.0668 S13:   0.2463                       
REMARK   3      S21:   0.0839 S22:  -0.0050 S23:  -0.3430                       
REMARK   3      S31:  -0.2284 S32:   0.2805 S33:   0.0279                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 156 THROUGH 179 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -29.3069  59.7882   6.4643              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9144 T22:   1.1100                                     
REMARK   3      T33:   1.3293 T12:   0.1053                                     
REMARK   3      T13:   0.2048 T23:  -0.1899                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6727 L22:   2.5088                                     
REMARK   3      L33:   5.6362 L12:  -0.1132                                     
REMARK   3      L13:   2.0919 L23:  -0.8027                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1024 S12:   0.0481 S13:  -0.0237                       
REMARK   3      S21:   0.0867 S22:  -0.1072 S23:  -0.3156                       
REMARK   3      S31:   0.3100 S32:   0.4237 S33:   0.0048                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 180 THROUGH 195 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -13.9994  64.7264  22.9805              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5731 T22:   1.7620                                     
REMARK   3      T33:   1.9939 T12:   0.0952                                     
REMARK   3      T13:   0.1301 T23:  -0.2034                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0000 L22:   0.0000                                     
REMARK   3      L33:   0.0000 L12:   0.0000                                     
REMARK   3      L13:   0.0000 L23:   0.0000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0303 S12:   0.0527 S13:   0.0148                       
REMARK   3      S21:  -0.0461 S22:   0.0294 S23:  -0.2318                       
REMARK   3      S31:   0.0513 S32:   0.1464 S33:   0.0009                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 196 THROUGH 235 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -41.1316  73.0267  30.2780              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8557 T22:   0.9624                                     
REMARK   3      T33:   1.0644 T12:   0.1624                                     
REMARK   3      T13:   0.0700 T23:  -0.1006                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5609 L22:   1.2971                                     
REMARK   3      L33:   0.6387 L12:  -0.3774                                     
REMARK   3      L13:   0.1206 L23:   0.8687                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0422 S12:  -0.2141 S13:   0.1190                       
REMARK   3      S21:   0.2174 S22:  -0.0373 S23:  -0.4611                       
REMARK   3      S31:  -0.1685 S32:   0.4279 S33:  -0.0049                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 236 THROUGH 268 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -50.2855  62.7643  26.2630              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7151 T22:   0.7824                                     
REMARK   3      T33:   0.8518 T12:   0.1981                                     
REMARK   3      T13:   0.0685 T23:  -0.0313                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1407 L22:   1.4410                                     
REMARK   3      L33:   2.4533 L12:   0.0711                                     
REMARK   3      L13:   0.5060 L23:   0.7351                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0728 S12:  -0.1192 S13:  -0.3529                       
REMARK   3      S21:   0.1540 S22:  -0.0151 S23:  -0.1729                       
REMARK   3      S31:   0.3084 S32:   0.1174 S33:  -0.0577                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 269 THROUGH 283 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -32.4282  59.4517  32.5850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5885 T22:   1.7172                                     
REMARK   3      T33:   1.8260 T12:   0.0823                                     
REMARK   3      T13:   0.0917 T23:  -0.2342                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5452 L22:   0.1035                                     
REMARK   3      L33:   1.6117 L12:  -0.2375                                     
REMARK   3      L13:   0.9374 L23:  -0.4084                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1473 S12:  -0.1465 S13:  -0.3371                       
REMARK   3      S21:   0.0749 S22:   0.0282 S23:   0.0005                       
REMARK   3      S31:   0.2025 S32:  -0.2144 S33:  -0.1755                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 284 THROUGH 307 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -28.1189  62.2003  29.1838              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2062 T22:   1.3330                                     
REMARK   3      T33:   1.4721 T12:   0.0535                                     
REMARK   3      T13:   0.0669 T23:  -0.2371                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7118 L22:   0.9555                                     
REMARK   3      L33:   0.8379 L12:  -0.2999                                     
REMARK   3      L13:  -0.3390 L23:  -0.4974                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0070 S12:  -0.1104 S13:  -0.0372                       
REMARK   3      S21:   0.1795 S22:   0.0578 S23:  -0.1305                       
REMARK   3      S31:   0.1805 S32:   0.1754 S33:  -0.0648                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 308 THROUGH 324 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -25.4351  70.3459  21.5030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1809 T22:   1.2919                                     
REMARK   3      T33:   1.4525 T12:   0.0707                                     
REMARK   3      T13:   0.0618 T23:  -0.2460                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9432 L22:   2.9648                                     
REMARK   3      L33:   0.9574 L12:   0.9633                                     
REMARK   3      L13:   1.6024 L23:   0.0498                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0042 S12:   0.4518 S13:   0.0391                       
REMARK   3      S21:  -0.3542 S22:   0.0766 S23:  -0.2693                       
REMARK   3      S31:  -0.1283 S32:   0.0345 S33:  -0.0724                       
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 6C9J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JAN-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000232356.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-NOV-16                          
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               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 9M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32841                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.1                               
REMARK 200  DATA REDUNDANCY                : 34.40                              
REMARK 200  R MERGE                    (I) : 0.80700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.22                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.08970                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4RER                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.39                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.77                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRI-AMMONIUM CITRATE PH7, 12%      
REMARK 280  W/V PEG 3350, VAPOR DIFFUSION, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
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       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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      134.97367            
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      269.94733            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      202.46050            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      337.43417            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       67.48683            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      134.97367            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      269.94733            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      337.43417            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      202.46050            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       67.48683            
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: 13240 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 39930 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.0 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     MET A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     HIS A     5                                                      
REMARK 465     HIS A     6                                                      
REMARK 465     HIS A     7                                                      
REMARK 465     HIS A     8                                                      
REMARK 465     HIS A     9                                                      
REMARK 465     HIS A    10                                                      
REMARK 465     ASP A   282                                                      
REMARK 465     PRO A   283                                                      
REMARK 465     SER A   284                                                      
REMARK 465     TYR A   285                                                      
REMARK 465     SER A   286                                                      
REMARK 465     SER A   287                                                      
REMARK 465     THR A   288                                                      
REMARK 465     MET A   289                                                      
REMARK 465     ILE A   290                                                      
REMARK 465     ASP A   291                                                      
REMARK 465     ASP A   292                                                      
REMARK 465     GLU A   293                                                      
REMARK 465     ALA A   294                                                      
REMARK 465     LEU A   295                                                      
REMARK 465     LYS A   296                                                      
REMARK 465     GLU A   297                                                      
REMARK 465     VAL A   298                                                      
REMARK 465     CYS A   299                                                      
REMARK 465     GLU A   300                                                      
REMARK 465     LYS A   301                                                      
REMARK 465     PHE A   302                                                      
REMARK 465     GLU A   303                                                      
REMARK 465     CYS A   304                                                      
REMARK 465     SER A   305                                                      
REMARK 465     GLU A   306                                                      
REMARK 465     GLU A   307                                                      
REMARK 465     GLU A   308                                                      
REMARK 465     VAL A   309                                                      
REMARK 465     LEU A   310                                                      
REMARK 465     SER A   311                                                      
REMARK 465     CYS A   312                                                      
REMARK 465     LEU A   313                                                      
REMARK 465     TYR A   314                                                      
REMARK 465     ASN A   315                                                      
REMARK 465     ARG A   316                                                      
REMARK 465     ASN A   317                                                      
REMARK 465     HIS A   318                                                      
REMARK 465     GLN A   319                                                      
REMARK 465     ASP A   320                                                      
REMARK 465     PRO A   321                                                      
REMARK 465     LEU A   322                                                      
REMARK 465     ALA A   323                                                      
REMARK 465     VAL A   324                                                      
REMARK 465     ALA A   325                                                      
REMARK 465     TYR A   326                                                      
REMARK 465     HIS A   327                                                      
REMARK 465     LEU A   328                                                      
REMARK 465     ILE A   329                                                      
REMARK 465     ILE A   330                                                      
REMARK 465     ASP A   331                                                      
REMARK 465     ASN A   332                                                      
REMARK 465     ARG A   333                                                      
REMARK 465     ARG A   334                                                      
REMARK 465     ILE A   335                                                      
REMARK 465     MET A   336                                                      
REMARK 465     ASN A   337                                                      
REMARK 465     GLU A   338                                                      
REMARK 465     ALA A   339                                                      
REMARK 465     LYS A   340                                                      
REMARK 465     ASP A   341                                                      
REMARK 465     PHE A   342                                                      
REMARK 465     TYR A   343                                                      
REMARK 465     LEU A   344                                                      
REMARK 465     ALA A   345                                                      
REMARK 465     THR A   346                                                      
REMARK 465     SER A   347                                                      
REMARK 465     PRO A   348                                                      
REMARK 465     PRO A   349                                                      
REMARK 465     ASP A   350                                                      
REMARK 465     SER A   351                                                      
REMARK 465     PHE A   352                                                      
REMARK 465     LEU A   353                                                      
REMARK 465     ASP A   354                                                      
REMARK 465     ASP A   355                                                      
REMARK 465     HIS A   356                                                      
REMARK 465     HIS A   357                                                      
REMARK 465     LEU A   358                                                      
REMARK 465     GLU A   372                                                      
REMARK 465     THR A   373                                                      
REMARK 465     PRO A   374                                                      
REMARK 465     ARG A   375                                                      
REMARK 465     ALA A   376                                                      
REMARK 465     ARG A   377                                                      
REMARK 465     HIS A   378                                                      
REMARK 465     THR A   379                                                      
REMARK 465     LEU A   380                                                      
REMARK 465     ASP A   381                                                      
REMARK 465     GLU A   382                                                      
REMARK 465     LEU A   383                                                      
REMARK 465     ASN A   384                                                      
REMARK 465     PRO A   385                                                      
REMARK 465     GLN A   386                                                      
REMARK 465     LYS A   387                                                      
REMARK 465     SER A   388                                                      
REMARK 465     LYS A   389                                                      
REMARK 465     HIS A   390                                                      
REMARK 465     GLN A   391                                                      
REMARK 465     GLY A   392                                                      
REMARK 465     VAL A   393                                                      
REMARK 465     ARG A   394                                                      
REMARK 465     MET B    67                                                      
REMARK 465     GLU B    68                                                      
REMARK 465     VAL B    69                                                      
REMARK 465     ASN B    70                                                      
REMARK 465     ASP B    71                                                      
REMARK 465     LYS B    72                                                      
REMARK 465     ALA B    73                                                      
REMARK 465     LYS B   171A                                                     
REMARK 465     CYS B   171B                                                     
REMARK 465     SER B   171C                                                     
REMARK 465     ASP B   171D                                                     
REMARK 465     VAL B   171E                                                     
REMARK 465     SER B   171F                                                     
REMARK 465     GLU B   171G                                                     
REMARK 465     LEU B   171H                                                     
REMARK 465     SER B   171I                                                     
REMARK 465     SER B   171J                                                     
REMARK 465     SER B   171K                                                     
REMARK 465     PRO B   171L                                                     
REMARK 465     PRO B   171M                                                     
REMARK 465     GLY B   171N                                                     
REMARK 465     PRO B   171O                                                     
REMARK 465     TYR B   171P                                                     
REMARK 465     HIS B   171Q                                                     
REMARK 465     LYS B   195                                                      
REMARK 465     PRO B   196                                                      
REMARK 465     GLU B   197                                                      
REMARK 465     GLU B   198                                                      
REMARK 465     ARG B   199                                                      
REMARK 465     PHE B   200                                                      
REMARK 465     MET C     0                                                      
REMARK 465     GLU C     1                                                      
REMARK 465     THR C     2                                                      
REMARK 465     VAL C     3                                                      
REMARK 465     ILE C     4                                                      
REMARK 465     SER C     5                                                      
REMARK 465     SER C     6                                                      
REMARK 465     ASP C     7                                                      
REMARK 465     SER C     8                                                      
REMARK 465     SER C     9                                                      
REMARK 465     PRO C    10                                                      
REMARK 465     ALA C    11                                                      
REMARK 465     VAL C    12                                                      
REMARK 465     GLU C    13                                                      
REMARK 465     ASN C    14                                                      
REMARK 465     GLU C    15                                                      
REMARK 465     HIS C    16                                                      
REMARK 465     PRO C    17                                                      
REMARK 465     GLN C    18                                                      
REMARK 465     GLU C    19                                                      
REMARK 465     THR C    20                                                      
REMARK 465     PRO C    21                                                      
REMARK 465     GLU C    22                                                      
REMARK 465     SER C    23                                                      
REMARK 465     ASN C    24                                                      
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   NZ   LYS A    33     OD2  ASP B   108              2.14            
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    HIS A  17       -5.07     75.97                                   
REMARK 500    ARG A 140       -7.34     68.18                                   
REMARK 500    ASP A 159       68.06     61.68                                   
REMARK 500    TPO A 174      102.02   -160.76                                   
REMARK 500    VAL A 429      -60.11   -104.78                                   
REMARK 500    VAL A 442      -61.82   -102.19                                   
REMARK 500    ASN B 110        3.59     86.53                                   
REMARK 500    ASN B 237       -1.76     71.13                                   
REMARK 500    LYS B 258     -118.66     42.36                                   
REMARK 500    LYS C  99      -64.12   -103.55                                   
REMARK 500    LEU C 163      -60.04   -102.37                                   
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 R34 A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue STU A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AMP C 401                 
DBREF  6C9J A   13   471  UNP    Q13131   AAPK1_HUMAN     22    480             
DBREF  6C9J A  526   550  UNP    Q13131   AAPK1_HUMAN    535    559             
DBREF  6C9J B   68   270  UNP    Q9Y478   AAKB1_HUMAN     68    270             
DBREF  6C9J C    0   324  UNP    P54619   AAKG1_HUMAN      1    325             
SEQADV 6C9J MET A    3  UNP  Q13131              EXPRESSION TAG                 
SEQADV 6C9J GLY A    4  UNP  Q13131              EXPRESSION TAG                 
SEQADV 6C9J HIS A    5  UNP  Q13131              EXPRESSION TAG                 
SEQADV 6C9J HIS A    6  UNP  Q13131              EXPRESSION TAG                 
SEQADV 6C9J HIS A    7  UNP  Q13131              EXPRESSION TAG                 
SEQADV 6C9J HIS A    8  UNP  Q13131              EXPRESSION TAG                 
SEQADV 6C9J HIS A    9  UNP  Q13131              EXPRESSION TAG                 
SEQADV 6C9J HIS A   10  UNP  Q13131              EXPRESSION TAG                 
SEQADV 6C9J GLY A   11  UNP  Q13131              EXPRESSION TAG                 
SEQADV 6C9J SER A   12  UNP  Q13131              EXPRESSION TAG                 
SEQADV 6C9J MET B   67  UNP  Q9Y478              EXPRESSION TAG                 
SEQADV 6C9J ASP B  108  UNP  Q9Y478    SER   108 ENGINEERED MUTATION            
SEQRES   1 A  494  MET GLY HIS HIS HIS HIS HIS HIS GLY SER VAL LYS ILE          
SEQRES   2 A  494  GLY HIS TYR ILE LEU GLY ASP THR LEU GLY VAL GLY THR          
SEQRES   3 A  494  PHE GLY LYS VAL LYS VAL GLY LYS HIS GLU LEU THR GLY          
SEQRES   4 A  494  HIS LYS VAL ALA VAL LYS ILE LEU ASN ARG GLN LYS ILE          
SEQRES   5 A  494  ARG SER LEU ASP VAL VAL GLY LYS ILE ARG ARG GLU ILE          
SEQRES   6 A  494  GLN ASN LEU LYS LEU PHE ARG HIS PRO HIS ILE ILE LYS          
SEQRES   7 A  494  LEU TYR GLN VAL ILE SER THR PRO SER ASP ILE PHE MET          
SEQRES   8 A  494  VAL MET GLU TYR VAL SER GLY GLY GLU LEU PHE ASP TYR          
SEQRES   9 A  494  ILE CYS LYS ASN GLY ARG LEU ASP GLU LYS GLU SER ARG          
SEQRES  10 A  494  ARG LEU PHE GLN GLN ILE LEU SER GLY VAL ASP TYR CYS          
SEQRES  11 A  494  HIS ARG HIS MET VAL VAL HIS ARG ASP LEU LYS PRO GLU          
SEQRES  12 A  494  ASN VAL LEU LEU ASP ALA HIS MET ASN ALA LYS ILE ALA          
SEQRES  13 A  494  ASP PHE GLY LEU SER ASN MET MET SER ASP GLY GLU PHE          
SEQRES  14 A  494  LEU ARG TPO SER CYS GLY SER PRO ASN TYR ALA ALA PRO          
SEQRES  15 A  494  GLU VAL ILE SER GLY ARG LEU TYR ALA GLY PRO GLU VAL          
SEQRES  16 A  494  ASP ILE TRP SER SER GLY VAL ILE LEU TYR ALA LEU LEU          
SEQRES  17 A  494  CYS GLY THR LEU PRO PHE ASP ASP ASP HIS VAL PRO THR          
SEQRES  18 A  494  LEU PHE LYS LYS ILE CYS ASP GLY ILE PHE TYR THR PRO          
SEQRES  19 A  494  GLN TYR LEU ASN PRO SER VAL ILE SER LEU LEU LYS HIS          
SEQRES  20 A  494  MET LEU GLN VAL ASP PRO MET LYS ARG ALA THR ILE LYS          
SEQRES  21 A  494  ASP ILE ARG GLU HIS GLU TRP PHE LYS GLN ASP LEU PRO          
SEQRES  22 A  494  LYS TYR LEU PHE PRO GLU ASP PRO SER TYR SER SER THR          
SEQRES  23 A  494  MET ILE ASP ASP GLU ALA LEU LYS GLU VAL CYS GLU LYS          
SEQRES  24 A  494  PHE GLU CYS SER GLU GLU GLU VAL LEU SER CYS LEU TYR          
SEQRES  25 A  494  ASN ARG ASN HIS GLN ASP PRO LEU ALA VAL ALA TYR HIS          
SEQRES  26 A  494  LEU ILE ILE ASP ASN ARG ARG ILE MET ASN GLU ALA LYS          
SEQRES  27 A  494  ASP PHE TYR LEU ALA THR SER PRO PRO ASP SER PHE LEU          
SEQRES  28 A  494  ASP ASP HIS HIS LEU THR ARG PRO HIS PRO GLU ARG VAL          
SEQRES  29 A  494  PRO PHE LEU VAL ALA GLU THR PRO ARG ALA ARG HIS THR          
SEQRES  30 A  494  LEU ASP GLU LEU ASN PRO GLN LYS SER LYS HIS GLN GLY          
SEQRES  31 A  494  VAL ARG LYS ALA LYS TRP HIS LEU GLY ILE ARG SER GLN          
SEQRES  32 A  494  SER ARG PRO ASN ASP ILE MET ALA GLU VAL CYS ARG ALA          
SEQRES  33 A  494  ILE LYS GLN LEU ASP TYR GLU TRP LYS VAL VAL ASN PRO          
SEQRES  34 A  494  TYR TYR LEU ARG VAL ARG ARG LYS ASN PRO VAL THR SER          
SEQRES  35 A  494  THR TYR SER LYS MET SER LEU GLN LEU TYR GLN VAL ASP          
SEQRES  36 A  494  SER ARG THR TYR LEU LEU ASP PHE ARG SER ILE ASP ASP          
SEQRES  37 A  494  GLU LEU THR PRO ARG PRO GLY SER HIS THR ILE GLU PHE          
SEQRES  38 A  494  PHE GLU MET CYS ALA ASN LEU ILE LYS ILE LEU ALA GLN          
SEQRES   1 B  204  MET GLU VAL ASN ASP LYS ALA PRO ALA GLN ALA ARG PRO          
SEQRES   2 B  204  THR VAL PHE ARG TRP THR GLY GLY GLY LYS GLU VAL TYR          
SEQRES   3 B  204  LEU SER GLY SER PHE ASN ASN TRP SER LYS LEU PRO LEU          
SEQRES   4 B  204  THR ARG ASP HIS ASN ASN PHE VAL ALA ILE LEU ASP LEU          
SEQRES   5 B  204  PRO GLU GLY GLU HIS GLN TYR LYS PHE PHE VAL ASP GLY          
SEQRES   6 B  204  GLN TRP THR HIS ASP PRO SER GLU PRO ILE VAL THR SER          
SEQRES   7 B  204  GLN LEU GLY THR VAL ASN ASN ILE ILE GLN VAL LYS LYS          
SEQRES   8 B  204  THR ASP PHE GLU VAL PHE ASP ALA LEU MET VAL ASP SER          
SEQRES   9 B  204  GLN LYS CYS SER ASP VAL SER GLU LEU SER SER SER PRO          
SEQRES  10 B  204  PRO GLY PRO TYR HIS GLN GLU PRO TYR VAL CYS LYS PRO          
SEQRES  11 B  204  GLU GLU ARG PHE ARG ALA PRO PRO ILE LEU PRO PRO HIS          
SEQRES  12 B  204  LEU LEU GLN VAL ILE LEU ASN LYS ASP THR GLY ILE SER          
SEQRES  13 B  204  CYS ASP PRO ALA LEU LEU PRO GLU PRO ASN HIS VAL MET          
SEQRES  14 B  204  LEU ASN HIS LEU TYR ALA LEU SER ILE LYS ASP GLY VAL          
SEQRES  15 B  204  MET VAL LEU SER ALA THR HIS ARG TYR LYS LYS LYS TYR          
SEQRES  16 B  204  VAL THR THR LEU LEU TYR LYS PRO ILE                          
SEQRES   1 C  325  MET GLU THR VAL ILE SER SER ASP SER SER PRO ALA VAL          
SEQRES   2 C  325  GLU ASN GLU HIS PRO GLN GLU THR PRO GLU SER ASN ASN          
SEQRES   3 C  325  SER VAL TYR THR SER PHE MET LYS SER HIS ARG CYS TYR          
SEQRES   4 C  325  ASP LEU ILE PRO THR SER SER LYS LEU VAL VAL PHE ASP          
SEQRES   5 C  325  THR SER LEU GLN VAL LYS LYS ALA PHE PHE ALA LEU VAL          
SEQRES   6 C  325  THR ASN GLY VAL ARG ALA ALA PRO LEU TRP ASP SER LYS          
SEQRES   7 C  325  LYS GLN SER PHE VAL GLY MET LEU THR ILE THR ASP PHE          
SEQRES   8 C  325  ILE ASN ILE LEU HIS ARG TYR TYR LYS SER ALA LEU VAL          
SEQRES   9 C  325  GLN ILE TYR GLU LEU GLU GLU HIS LYS ILE GLU THR TRP          
SEQRES  10 C  325  ARG GLU VAL TYR LEU GLN ASP SER PHE LYS PRO LEU VAL          
SEQRES  11 C  325  CYS ILE SER PRO ASN ALA SER LEU PHE ASP ALA VAL SER          
SEQRES  12 C  325  SER LEU ILE ARG ASN LYS ILE HIS ARG LEU PRO VAL ILE          
SEQRES  13 C  325  ASP PRO GLU SER GLY ASN THR LEU TYR ILE LEU THR HIS          
SEQRES  14 C  325  LYS ARG ILE LEU LYS PHE LEU LYS LEU PHE ILE THR GLU          
SEQRES  15 C  325  PHE PRO LYS PRO GLU PHE MET SER LYS SER LEU GLU GLU          
SEQRES  16 C  325  LEU GLN ILE GLY THR TYR ALA ASN ILE ALA MET VAL ARG          
SEQRES  17 C  325  THR THR THR PRO VAL TYR VAL ALA LEU GLY ILE PHE VAL          
SEQRES  18 C  325  GLN HIS ARG VAL SER ALA LEU PRO VAL VAL ASP GLU LYS          
SEQRES  19 C  325  GLY ARG VAL VAL ASP ILE TYR SER LYS PHE ASP VAL ILE          
SEQRES  20 C  325  ASN LEU ALA ALA GLU LYS THR TYR ASN ASN LEU ASP VAL          
SEQRES  21 C  325  SER VAL THR LYS ALA LEU GLN HIS ARG SER HIS TYR PHE          
SEQRES  22 C  325  GLU GLY VAL LEU LYS CYS TYR LEU HIS GLU THR LEU GLU          
SEQRES  23 C  325  THR ILE ILE ASN ARG LEU VAL GLU ALA GLU VAL HIS ARG          
SEQRES  24 C  325  LEU VAL VAL VAL ASP GLU ASN ASP VAL VAL LYS GLY ILE          
SEQRES  25 C  325  VAL SER LEU SER ASP ILE LEU GLN ALA LEU VAL LEU THR          
MODRES 6C9J TPO A  174  THR  MODIFIED RESIDUE                                   
HET    TPO  A 174      11                                                       
HET    R34  A 601      32                                                       
HET    STU  A 602      35                                                       
HET    AMP  C 401      23                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     R34 5-{[6-CHLORO-5-(1-METHYL-1H-INDOL-5-YL)-1H-                      
HETNAM   2 R34  BENZIMIDAZOL-2-YL]OXY}-N-HYDROXY-2-METHYLBENZAMIDE              
HETNAM     STU STAUROSPORINE                                                    
HETNAM     AMP ADENOSINE MONOPHOSPHATE                                          
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   4  R34    C24 H19 CL N4 O3                                             
FORMUL   5  STU    C28 H26 N4 O3                                                
FORMUL   6  AMP    C10 H14 N5 O7 P                                              
HELIX    1 AA1 ARG A   51  LEU A   57  1                                   7    
HELIX    2 AA2 VAL A   59  LYS A   71  1                                  13    
HELIX    3 AA3 LEU A  103  GLY A  111  1                                   9    
HELIX    4 AA4 ASP A  114  HIS A  135  1                                  22    
HELIX    5 AA5 ASP A  159  SER A  163  5                                   5    
HELIX    6 AA6 SER A  178  ALA A  182  5                                   5    
HELIX    7 AA7 ALA A  183  SER A  188  1                                   6    
HELIX    8 AA8 GLY A  194  GLY A  212  1                                  19    
HELIX    9 AA9 HIS A  220  GLY A  231  1                                  12    
HELIX   10 AB1 ASN A  240  LEU A  251  1                                  12    
HELIX   11 AB2 THR A  260  HIS A  267  1                                   8    
HELIX   12 AB3 HIS A  267  GLN A  272  1                                   6    
HELIX   13 AB4 ARG A  365  ALA A  371  1                                   7    
HELIX   14 AB5 ARG A  407  LEU A  422  1                                  16    
HELIX   15 AB6 SER A  532  GLN A  550  1                                  19    
HELIX   16 AB7 LYS B  156  GLU B  161  1                                   6    
HELIX   17 AB8 GLU B  161  SER B  170  1                                  10    
HELIX   18 AB9 PRO B  207  GLN B  212  5                                   6    
HELIX   19 AC1 ASN B  232  LEU B  236  5                                   5    
HELIX   20 AC2 SER C   26  HIS C   35  1                                  10    
HELIX   21 AC3 ARG C   36  ILE C   41  5                                   6    
HELIX   22 AC4 GLN C   55  GLY C   67  1                                  13    
HELIX   23 AC5 ILE C   87  TYR C   98  1                                  12    
HELIX   24 AC6 ILE C  105  HIS C  111  1                                   7    
HELIX   25 AC7 LYS C  112  GLN C  122  1                                  11    
HELIX   26 AC8 SER C  136  ASN C  147  1                                  12    
HELIX   27 AC9 THR C  167  THR C  180  1                                  14    
HELIX   28 AD1 PRO C  185  LYS C  190  5                                   6    
HELIX   29 AD2 SER C  191  GLN C  196  1                                   6    
HELIX   30 AD3 PRO C  211  ARG C  223  1                                  13    
HELIX   31 AD4 LYS C  242  ILE C  246  1                                   5    
HELIX   32 AD5 ILE C  246  GLU C  251  1                                   6    
HELIX   33 AD6 SER C  260  LEU C  265  1                                   6    
HELIX   34 AD7 GLN C  266  SER C  269  5                                   4    
HELIX   35 AD8 THR C  283  GLU C  295  1                                  13    
HELIX   36 AD9 LEU C  314  LEU C  323  1                                  10    
SHEET    1 AA1 6 LYS A  14  ILE A  15  0                                        
SHEET    2 AA1 6 TYR A  18  VAL A  26 -1  O  TYR A  18   N  ILE A  15           
SHEET    3 AA1 6 LYS A  31  HIS A  37 -1  O  LYS A  36   N  ILE A  19           
SHEET    4 AA1 6 LYS A  43  ASN A  50 -1  O  ILE A  48   N  LYS A  31           
SHEET    5 AA1 6 ASP A  90  GLU A  96 -1  O  MET A  95   N  ALA A  45           
SHEET    6 AA1 6 LEU A  81  SER A  86 -1  N  ILE A  85   O  PHE A  92           
SHEET    1 AA2 3 GLY A 101  GLU A 102  0                                        
SHEET    2 AA2 3 VAL A 147  LEU A 149 -1  O  LEU A 149   N  GLY A 101           
SHEET    3 AA2 3 ALA A 155  ILE A 157 -1  O  LYS A 156   N  LEU A 148           
SHEET    1 AA3 2 VAL A 137  VAL A 138  0                                        
SHEET    2 AA3 2 ASN A 164  MET A 165 -1  O  ASN A 164   N  VAL A 138           
SHEET    1 AA4 7 HIS A 399  LEU A 400  0                                        
SHEET    2 AA4 7 TYR B 240  LYS B 245 -1  O  ALA B 241   N  HIS A 399           
SHEET    3 AA4 7 VAL B 248  TYR B 257 -1  O  SER B 252   N  TYR B 240           
SHEET    4 AA4 7 LYS B 260  PRO B 269 -1  O  LYS B 260   N  TYR B 257           
SHEET    5 AA4 7 SER C  44  ASP C  51  1  O  LEU C  47   N  THR B 263           
SHEET    6 AA4 7 ALA C  70  ASP C  75  1  O  TRP C  74   N  PHE C  50           
SHEET    7 AA4 7 SER C  80  THR C  86 -1  O  VAL C  82   N  LEU C  73           
SHEET    1 AA5 5 ILE A 402  SER A 404  0                                        
SHEET    2 AA5 5 TYR A 461  SER A 467 -1  O  LEU A 463   N  ILE A 402           
SHEET    3 AA5 5 TYR A 446  GLN A 455 -1  N  TYR A 454   O  LEU A 462           
SHEET    4 AA5 5 TYR A 433  LYS A 439 -1  N  LEU A 434   O  LEU A 451           
SHEET    5 AA5 5 GLU A 425  ASN A 430 -1  N  GLU A 425   O  ARG A 437           
SHEET    1 AA6 3 ARG B  78  THR B  85  0                                        
SHEET    2 AA6 3 ASN B 111  LEU B 118 -1  O  LEU B 116   N  THR B  80           
SHEET    3 AA6 3 THR B 106  ARG B 107 -1  N  THR B 106   O  VAL B 113           
SHEET    1 AA7 4 LEU B 103  PRO B 104  0                                        
SHEET    2 AA7 4 VAL B  91  GLY B  95 -1  N  LEU B  93   O  LEU B 103           
SHEET    3 AA7 4 GLY B 121  VAL B 129 -1  O  LYS B 126   N  SER B  94           
SHEET    4 AA7 4 GLN B 132  THR B 134 -1  O  THR B 134   N  PHE B 127           
SHEET    1 AA8 5 LEU B 103  PRO B 104  0                                        
SHEET    2 AA8 5 VAL B  91  GLY B  95 -1  N  LEU B  93   O  LEU B 103           
SHEET    3 AA8 5 GLY B 121  VAL B 129 -1  O  LYS B 126   N  SER B  94           
SHEET    4 AA8 5 VAL B 149  VAL B 155 -1  O  ASN B 151   N  TYR B 125           
SHEET    5 AA8 5 ILE B 141  THR B 143 -1  N  VAL B 142   O  ASN B 150           
SHEET    1 AA9 2 LEU C 152  ILE C 155  0                                        
SHEET    2 AA9 2 THR C 162  LEU C 166 -1  O  LEU C 163   N  VAL C 154           
SHEET    1 AB1 3 VAL C 206  ARG C 207  0                                        
SHEET    2 AB1 3 ALA C 226  VAL C 230  1  O  PRO C 228   N  VAL C 206           
SHEET    3 AB1 3 VAL C 236  SER C 241 -1  O  TYR C 240   N  LEU C 227           
SHEET    1 AB2 3 LYS C 277  CYS C 278  0                                        
SHEET    2 AB2 3 ARG C 298  VAL C 302  1  O  VAL C 302   N  CYS C 278           
SHEET    3 AB2 3 VAL C 308  SER C 313 -1  O  LYS C 309   N  VAL C 301           
LINK         C   ARG A 173                 N   TPO A 174     1555   1555  1.33  
LINK         C   TPO A 174                 N   SER A 175     1555   1555  1.33  
SITE     1 AC1 12 VAL A  13  LEU A  20  LYS A  31  LYS A  33                    
SITE     2 AC1 12 ASN A  50  LYS A  53  ASP A  90  ARG B  83                    
SITE     3 AC1 12 THR B 106  ASP B 108  VAL B 113  ILE B 115                    
SITE     1 AC2 14 LEU A  24  GLY A  25  VAL A  26  GLY A  27                    
SITE     2 AC2 14 ALA A  45  MET A  95  GLU A  96  TYR A  97                    
SITE     3 AC2 14 VAL A  98  GLU A 102  GLU A 145  ASN A 146                    
SITE     4 AC2 14 LEU A 148  ASP A 159                                          
SITE     1 AC3 12 HIS C 150  THR C 199  ILE C 203  ALA C 204                    
SITE     2 AC3 12 VAL C 224  SER C 225  ALA C 226  PRO C 228                    
SITE     3 AC3 12 ILE C 311  SER C 313  SER C 315  ASP C 316                    
CRYST1  123.296  123.296  404.921  90.00  90.00 120.00 P 61 2 2     12          
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      0.008111  0.004683  0.000000        0.00000                         
SCALE2      0.000000  0.009365  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002470        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system