GenomeNet

Database: PDB
Entry: 5TJH
LinkDB: 5TJH
Original site: 5TJH 
HEADER    OXIDOREDUCTASE                          04-OCT-16   5TJH              
TITLE     HUGDH A136M SUBSTITUTION                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UDP-GLUCOSE 6-DEHYDROGENASE;                               
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 FRAGMENT: UNP RESIDUES 1-494;                                        
COMPND   5 SYNONYM: UDPGDH;                                                     
COMPND   6 EC: 1.1.1.22;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: UGDH;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    DEHYDROGENASE, OXIDOREDUCTASE                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.R.BEATTIE,Z.A.WOOD                                                  
REVDAT   4   27-SEP-17 5TJH    1       REMARK                                   
REVDAT   3   25-JAN-17 5TJH    1       JRNL                                     
REVDAT   2   04-JAN-17 5TJH    1       JRNL                                     
REVDAT   1   02-NOV-16 5TJH    0                                                
JRNL        AUTH   N.R.BEATTIE,N.D.KEUL,A.M.SIDLO,Z.A.WOOD                      
JRNL        TITL   ALLOSTERY AND HYSTERESIS ARE COUPLED IN HUMAN UDP-GLUCOSE    
JRNL        TITL 2 DEHYDROGENASE.                                               
JRNL        REF    BIOCHEMISTRY                  V.  56   202 2017              
JRNL        REFN                   ISSN 1520-4995                               
JRNL        PMID   27966912                                                     
JRNL        DOI    10.1021/ACS.BIOCHEM.6B01044                                  
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: ???)                            
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) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.17                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.960                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 206120                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.173                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.203                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 10306                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 37.1795 -  6.3593    0.99     6618   348  0.1434 0.1673        
REMARK   3     2  6.3593 -  5.0516    0.99     6646   350  0.1484 0.1634        
REMARK   3     3  5.0516 -  4.4142    0.99     6592   347  0.1258 0.1444        
REMARK   3     4  4.4142 -  4.0111    0.99     6573   345  0.1350 0.1709        
REMARK   3     5  4.0111 -  3.7239    0.99     6590   347  0.1439 0.1678        
REMARK   3     6  3.7239 -  3.5045    0.99     6599   347  0.1574 0.1851        
REMARK   3     7  3.5045 -  3.3291    0.99     6565   346  0.1772 0.2171        
REMARK   3     8  3.3291 -  3.1843    0.99     6569   346  0.1830 0.2140        
REMARK   3     9  3.1843 -  3.0618    0.99     6579   347  0.1795 0.2018        
REMARK   3    10  3.0618 -  2.9562    0.99     6580   346  0.1782 0.2217        
REMARK   3    11  2.9562 -  2.8638    0.98     6573   346  0.1824 0.2229        
REMARK   3    12  2.8638 -  2.7819    0.98     6523   343  0.1772 0.2228        
REMARK   3    13  2.7819 -  2.7087    0.98     6523   343  0.1737 0.2141        
REMARK   3    14  2.7087 -  2.6427    0.98     6500   343  0.1865 0.2385        
REMARK   3    15  2.6427 -  2.5826    0.98     6585   347  0.1859 0.2314        
REMARK   3    16  2.5826 -  2.5276    0.98     6539   343  0.1816 0.2231        
REMARK   3    17  2.5276 -  2.4771    0.98     6493   343  0.1985 0.2701        
REMARK   3    18  2.4771 -  2.4304    0.98     6499   341  0.1929 0.2566        
REMARK   3    19  2.4304 -  2.3870    0.98     6519   344  0.1963 0.2361        
REMARK   3    20  2.3870 -  2.3465    0.98     6536   344  0.2025 0.2663        
REMARK   3    21  2.3465 -  2.3087    0.97     6444   338  0.2037 0.2382        
REMARK   3    22  2.3087 -  2.2732    0.97     6497   343  0.2187 0.2469        
REMARK   3    23  2.2732 -  2.2397    0.97     6507   342  0.2341 0.2668        
REMARK   3    24  2.2397 -  2.2082    0.97     6470   340  0.2392 0.2889        
REMARK   3    25  2.2082 -  2.1783    0.97     6442   340  0.2528 0.3056        
REMARK   3    26  2.1783 -  2.1501    0.97     6449   339  0.2527 0.2734        
REMARK   3    27  2.1501 -  2.1232    0.97     6509   343  0.2643 0.2692        
REMARK   3    28  2.1232 -  2.0976    0.97     6464   340  0.2762 0.3034        
REMARK   3    29  2.0976 -  2.0732    0.97     6483   341  0.2958 0.3308        
REMARK   3    30  2.0732 -  2.0499    0.96     6348   334  0.3156 0.3452        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.260            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.050           
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      :  0.008          22219                                  
REMARK   3   ANGLE     :  0.893          30083                                  
REMARK   3   CHIRALITY :  0.055           3424                                  
REMARK   3   PLANARITY :  0.007           3862                                  
REMARK   3   DIHEDRAL  : 16.230           8304                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 24                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 87 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -41.7053  29.3368 -20.5319              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6536 T22:   0.8119                                     
REMARK   3      T33:   1.0681 T12:   0.2370                                     
REMARK   3      T13:  -0.2416 T23:  -0.3370                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5124 L22:   3.9505                                     
REMARK   3      L33:   2.9904 L12:  -1.1893                                     
REMARK   3      L13:   1.2458 L23:   0.9624                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0359 S12:   0.0624 S13:  -0.0419                       
REMARK   3      S21:  -0.5423 S22:  -0.7920 S23:   1.7439                       
REMARK   3      S31:  -0.4720 S32:  -1.2098 S33:   0.4088                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 88 THROUGH 276 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -23.4499  26.8463 -13.3340              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4648 T22:   0.3264                                     
REMARK   3      T33:   0.4205 T12:   0.0364                                     
REMARK   3      T13:  -0.0833 T23:   0.0052                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6825 L22:   1.7914                                     
REMARK   3      L33:   4.0470 L12:  -0.1259                                     
REMARK   3      L13:   0.5910 L23:   0.6742                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0404 S12:   0.1210 S13:   0.0263                       
REMARK   3      S21:  -0.3489 S22:  -0.1765 S23:   0.2051                       
REMARK   3      S31:  -0.4942 S32:  -0.2579 S33:   0.1017                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 277 THROUGH 467 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -30.5630  10.6635  11.2547              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4340 T22:   0.2923                                     
REMARK   3      T33:   0.4578 T12:   0.0431                                     
REMARK   3      T13:  -0.0170 T23:   0.0408                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9193 L22:   1.4395                                     
REMARK   3      L33:   4.5079 L12:   1.1516                                     
REMARK   3      L13:  -2.4339 L23:  -1.8907                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0568 S12:   0.0365 S13:  -0.0262                       
REMARK   3      S21:   0.0135 S22:   0.2230 S23:   0.3231                       
REMARK   3      S31:  -0.3405 S32:  -0.4415 S33:  -0.1522                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 212 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   1.8873 -37.4395 -30.0609              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3509 T22:   0.4276                                     
REMARK   3      T33:   0.2785 T12:   0.0019                                     
REMARK   3      T13:   0.0064 T23:  -0.0654                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3498 L22:   1.9947                                     
REMARK   3      L33:   5.1209 L12:   0.4904                                     
REMARK   3      L13:  -0.9944 L23:  -0.6652                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1088 S12:   0.2479 S13:  -0.0400                       
REMARK   3      S21:  -0.1817 S22:   0.1059 S23:   0.0352                       
REMARK   3      S31:   0.4445 S32:  -0.6825 S33:   0.0216                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 213 THROUGH 466 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.1997  -4.6169 -31.4664              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3630 T22:   0.3443                                     
REMARK   3      T33:   0.3377 T12:  -0.0065                                     
REMARK   3      T13:  -0.0478 T23:  -0.0690                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7074 L22:   1.8987                                     
REMARK   3      L33:   1.2067 L12:  -0.9909                                     
REMARK   3      L13:   0.4157 L23:   0.1722                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0767 S12:   0.1539 S13:   0.0022                       
REMARK   3      S21:  -0.3697 S22:  -0.1935 S23:   0.3120                       
REMARK   3      S31:  -0.1669 S32:  -0.2124 S33:   0.1004                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 87 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -29.7373 -25.6532  38.5493              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3419 T22:   0.2520                                     
REMARK   3      T33:   0.3067 T12:  -0.0553                                     
REMARK   3      T13:   0.0796 T23:   0.0106                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5053 L22:   7.4594                                     
REMARK   3      L33:   4.4246 L12:  -0.2330                                     
REMARK   3      L13:   1.2373 L23:   0.0339                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0090 S12:   0.0810 S13:  -0.5067                       
REMARK   3      S21:  -0.0035 S22:   0.1248 S23:   0.2957                       
REMARK   3      S31:   0.5040 S32:  -0.3336 S33:  -0.0967                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 88 THROUGH 135 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -25.8317  -9.8699  27.8111              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3037 T22:   0.2329                                     
REMARK   3      T33:   0.2896 T12:  -0.0016                                     
REMARK   3      T13:   0.0122 T23:  -0.0014                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2669 L22:   2.6740                                     
REMARK   3      L33:   7.9235 L12:  -0.9555                                     
REMARK   3      L13:  -4.4471 L23:   0.9191                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0666 S12:   0.5880 S13:   0.1413                       
REMARK   3      S21:  -0.2483 S22:   0.0306 S23:   0.0729                       
REMARK   3      S31:   0.1250 S32:  -0.4839 S33:  -0.0911                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 136 THROUGH 212 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -18.0133 -13.6203  40.6951              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2797 T22:   0.2833                                     
REMARK   3      T33:   0.1849 T12:  -0.0314                                     
REMARK   3      T13:   0.0567 T23:  -0.0380                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2461 L22:   4.9916                                     
REMARK   3      L33:   2.1098 L12:  -2.3756                                     
REMARK   3      L13:   0.4795 L23:  -0.6966                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0195 S12:  -0.1446 S13:  -0.0507                       
REMARK   3      S21:   0.2229 S22:   0.0939 S23:  -0.1927                       
REMARK   3      S31:   0.0949 S32:   0.1959 S33:  -0.0548                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 213 THROUGH 372 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.0921 -23.9008  13.1312              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2350 T22:   0.2789                                     
REMARK   3      T33:   0.2340 T12:  -0.0213                                     
REMARK   3      T13:   0.0233 T23:  -0.0162                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3194 L22:   1.4522                                     
REMARK   3      L33:   1.7921 L12:  -0.0411                                     
REMARK   3      L13:  -0.0196 L23:   0.6784                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0728 S12:   0.0333 S13:   0.0255                       
REMARK   3      S21:  -0.0062 S22:   0.0460 S23:   0.0340                       
REMARK   3      S31:   0.1397 S32:  -0.0038 S33:   0.0295                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 373 THROUGH 440 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -11.6350 -40.8155   3.4683              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4412 T22:   0.3375                                     
REMARK   3      T33:   0.2789 T12:  -0.1479                                     
REMARK   3      T13:   0.0445 T23:  -0.0272                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7585 L22:   4.2828                                     
REMARK   3      L33:   3.9196 L12:  -0.6721                                     
REMARK   3      L13:  -0.5822 L23:   1.7527                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0525 S12:   0.0783 S13:  -0.1050                       
REMARK   3      S21:   0.1721 S22:  -0.0675 S23:   0.2560                       
REMARK   3      S31:   0.5019 S32:  -0.4659 S33:   0.1140                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 441 THROUGH 467 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   4.9507 -40.7726   6.6817              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3806 T22:   0.3697                                     
REMARK   3      T33:   0.4053 T12:   0.0453                                     
REMARK   3      T13:  -0.0674 T23:  -0.0626                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3562 L22:   2.9484                                     
REMARK   3      L33:   9.1839 L12:   1.8887                                     
REMARK   3      L13:  -0.7793 L23:   4.4325                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1166 S12:  -0.1242 S13:  -0.1551                       
REMARK   3      S21:   0.5657 S22:   0.3938 S23:  -0.7346                       
REMARK   3      S31:   0.6286 S32:   0.7030 S33:  -0.3801                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 2 THROUGH 87 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  37.9332 -24.7559  30.1703              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6809 T22:   1.0510                                     
REMARK   3      T33:   0.5786 T12:  -0.1228                                     
REMARK   3      T13:  -0.2165 T23:   0.1131                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8308 L22:   1.5700                                     
REMARK   3      L33:   5.8848 L12:   0.8479                                     
REMARK   3      L13:   0.7557 L23:  -0.8138                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0238 S12:  -0.8818 S13:   0.0144                       
REMARK   3      S21:   0.5956 S22:  -0.5114 S23:  -0.5168                       
REMARK   3      S31:  -0.9229 S32:   1.6076 S33:   0.2539                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 88 THROUGH 185 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  29.1173 -25.2968  15.6690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3702 T22:   0.5199                                     
REMARK   3      T33:   0.4134 T12:   0.0395                                     
REMARK   3      T13:  -0.1183 T23:  -0.0468                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3338 L22:   1.8550                                     
REMARK   3      L33:   4.2746 L12:   0.4344                                     
REMARK   3      L13:  -0.9100 L23:  -2.5989                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0702 S12:  -0.0280 S13:  -0.2326                       
REMARK   3      S21:   0.2330 S22:  -0.2347 S23:  -0.2207                       
REMARK   3      S31:  -0.3052 S32:   0.5309 S33:   0.2502                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 186 THROUGH 212 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  23.8349 -38.4126  24.9899              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4469 T22:   0.3714                                     
REMARK   3      T33:   0.6079 T12:   0.1431                                     
REMARK   3      T13:   0.0170 T23:   0.1017                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8947 L22:   2.7592                                     
REMARK   3      L33:   5.3933 L12:  -0.6762                                     
REMARK   3      L13:   0.8970 L23:  -2.6401                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3732 S12:  -0.1366 S13:  -1.2805                       
REMARK   3      S21:  -0.1710 S22:  -0.2520 S23:  -0.1751                       
REMARK   3      S31:   0.8833 S32:   0.1852 S33:   0.3173                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 213 THROUGH 321 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   7.1115 -11.1252  22.5602              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2560 T22:   0.3382                                     
REMARK   3      T33:   0.2802 T12:  -0.0409                                     
REMARK   3      T13:   0.0123 T23:  -0.0204                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6004 L22:   1.0824                                     
REMARK   3      L33:   1.4400 L12:   0.0059                                     
REMARK   3      L13:   0.3057 L23:   0.3926                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0304 S12:   0.0193 S13:  -0.0116                       
REMARK   3      S21:  -0.0514 S22:   0.0623 S23:  -0.0633                       
REMARK   3      S31:  -0.0985 S32:   0.2645 S33:  -0.0495                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 322 THROUGH 466 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  14.2772   7.2355  35.9021              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4108 T22:   0.3437                                     
REMARK   3      T33:   0.2959 T12:  -0.1019                                     
REMARK   3      T13:  -0.0865 T23:   0.0041                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9558 L22:   4.1090                                     
REMARK   3      L33:   2.8879 L12:  -0.8494                                     
REMARK   3      L13:  -0.1442 L23:   1.1052                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0309 S12:  -0.0685 S13:   0.0980                       
REMARK   3      S21:   0.4002 S22:  -0.0138 S23:  -0.3152                       
REMARK   3      S31:  -0.1191 S32:   0.2363 S33:   0.0305                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 1 THROUGH 87 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  34.6038  16.0137 -39.5588              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6247 T22:   0.9664                                     
REMARK   3      T33:   0.7432 T12:  -0.2541                                     
REMARK   3      T13:   0.1601 T23:  -0.1673                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5454 L22:   7.3045                                     
REMARK   3      L33:   1.8514 L12:  -2.1820                                     
REMARK   3      L13:  -0.4450 L23:   1.6155                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2062 S12:  -0.0548 S13:   0.5682                       
REMARK   3      S21:  -0.3927 S22:   0.7058 S23:  -1.4577                       
REMARK   3      S31:  -0.2785 S32:   0.9687 S33:  -0.4373                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 88 THROUGH 185 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  19.5508  17.6575 -32.6148              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5111 T22:   0.5525                                     
REMARK   3      T33:   0.3945 T12:  -0.1819                                     
REMARK   3      T13:   0.0441 T23:   0.0077                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8493 L22:   4.6757                                     
REMARK   3      L33:   3.0518 L12:  -0.6929                                     
REMARK   3      L13:  -0.8464 L23:   2.2432                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0652 S12:  -0.0763 S13:   0.1649                       
REMARK   3      S21:  -0.1290 S22:   0.1581 S23:  -0.2272                       
REMARK   3      S31:  -0.3467 S32:   0.5498 S33:  -0.0481                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 186 THROUGH 276 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  16.8854  -3.5346 -32.9573              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2986 T22:   0.3233                                     
REMARK   3      T33:   0.2286 T12:  -0.0737                                     
REMARK   3      T13:   0.0512 T23:  -0.0413                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0883 L22:   2.7039                                     
REMARK   3      L33:   2.1229 L12:   0.2092                                     
REMARK   3      L13:   0.2013 L23:  -0.4231                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0026 S12:   0.1717 S13:   0.0560                       
REMARK   3      S21:  -0.3673 S22:   0.0868 S23:  -0.0672                       
REMARK   3      S31:  -0.1305 S32:   0.1616 S33:  -0.0086                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 277 THROUGH 467 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  30.8003 -10.4240 -11.9750              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3529 T22:   0.6130                                     
REMARK   3      T33:   0.3782 T12:  -0.0521                                     
REMARK   3      T13:   0.0165 T23:  -0.0622                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4191 L22:   1.6264                                     
REMARK   3      L33:   2.2961 L12:  -1.3351                                     
REMARK   3      L13:   1.7637 L23:  -1.4172                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0301 S12:   0.1017 S13:   0.1368                       
REMARK   3      S21:  -0.1004 S22:  -0.2004 S23:  -0.2885                       
REMARK   3      S31:  -0.0105 S32:   0.7120 S33:   0.1727                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 1 THROUGH 87 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):   3.5108  46.8052  26.5673              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8120 T22:   0.4064                                     
REMARK   3      T33:   0.6687 T12:  -0.2204                                     
REMARK   3      T13:  -0.1327 T23:   0.1901                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6453 L22:   5.4917                                     
REMARK   3      L33:   2.4873 L12:  -0.2365                                     
REMARK   3      L13:   1.8514 L23:  -1.4571                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2247 S12:   0.2470 S13:   0.8103                       
REMARK   3      S21:   0.7140 S22:  -0.6427 S23:  -1.1700                       
REMARK   3      S31:  -0.7463 S32:   0.6119 S33:   0.4230                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 88 THROUGH 204 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.8366  32.8208  27.7996              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6840 T22:   0.3046                                     
REMARK   3      T33:   0.3455 T12:  -0.1323                                     
REMARK   3      T13:   0.0114 T23:   0.0036                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7133 L22:   3.4144                                     
REMARK   3      L33:   1.1072 L12:  -1.0792                                     
REMARK   3      L13:   0.6765 L23:  -0.6872                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0417 S12:  -0.0553 S13:   0.1266                       
REMARK   3      S21:   0.2067 S22:  -0.0737 S23:  -0.0814                       
REMARK   3      S31:  -0.2652 S32:   0.0049 S33:   0.0524                       
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 205 THROUGH 372 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.6933  28.7677   0.2907              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4694 T22:   0.2728                                     
REMARK   3      T33:   0.3370 T12:  -0.0644                                     
REMARK   3      T13:  -0.0402 T23:   0.0150                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7378 L22:   0.9455                                     
REMARK   3      L33:   0.6179 L12:   0.3375                                     
REMARK   3      L13:  -0.1427 L23:   0.2437                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0384 S12:   0.0463 S13:  -0.0147                       
REMARK   3      S21:  -0.0603 S22:   0.0530 S23:  -0.0948                       
REMARK   3      S31:  -0.1322 S32:   0.0534 S33:  -0.0110                       
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 373 THROUGH 468 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  10.8808  38.1700 -13.4316              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6543 T22:   0.3240                                     
REMARK   3      T33:   0.4332 T12:  -0.1910                                     
REMARK   3      T13:   0.0245 T23:  -0.0105                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2954 L22:   2.4057                                     
REMARK   3      L33:   3.5256 L12:   0.7000                                     
REMARK   3      L13:   0.2740 L23:  -0.3705                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1308 S12:   0.2057 S13:   0.1973                       
REMARK   3      S21:  -0.3276 S22:   0.3343 S23:   0.0292                       
REMARK   3      S31:  -0.3137 S32:   0.0327 S33:  -0.1935                       
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 5TJH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-OCT-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000224348.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-NOV-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 77                                 
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                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX300-HS                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 206192                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.180                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.3                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.12300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4RJT                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.98                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 3350,0.2M NACL, 0.1M TRIS        
REMARK 280  BUFFER PH 7.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 27360 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 101280 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -191.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     PRO A   383                                                      
REMARK 465     GLY A   384                                                      
REMARK 465     VAL A   385                                                      
REMARK 465     SER A   386                                                      
REMARK 465     GLU A   387                                                      
REMARK 465     ASP A   388                                                      
REMARK 465     SER A   468                                                      
REMARK 465     LYS A   469                                                      
REMARK 465     ARG A   470                                                      
REMARK 465     ILE A   471                                                      
REMARK 465     PRO A   472                                                      
REMARK 465     TYR A   473                                                      
REMARK 465     ALA A   474                                                      
REMARK 465     PRO A   475                                                      
REMARK 465     SER A   476                                                      
REMARK 465     GLY A   477                                                      
REMARK 465     GLU A   478                                                      
REMARK 465     ILE A   479                                                      
REMARK 465     PRO A   480                                                      
REMARK 465     LYS A   481                                                      
REMARK 465     PHE A   482                                                      
REMARK 465     SER A   483                                                      
REMARK 465     LEU A   484                                                      
REMARK 465     GLN A   485                                                      
REMARK 465     ASP A   486                                                      
REMARK 465     PRO A   487                                                      
REMARK 465     PRO A   488                                                      
REMARK 465     ASN A   489                                                      
REMARK 465     LYS A   490                                                      
REMARK 465     LYS A   491                                                      
REMARK 465     PRO A   492                                                      
REMARK 465     LYS A   493                                                      
REMARK 465     VAL A   494                                                      
REMARK 465     PRO B   383                                                      
REMARK 465     GLY B   384                                                      
REMARK 465     VAL B   385                                                      
REMARK 465     SER B   386                                                      
REMARK 465     GLU B   387                                                      
REMARK 465     ASP B   388                                                      
REMARK 465     SER B   467                                                      
REMARK 465     SER B   468                                                      
REMARK 465     LYS B   469                                                      
REMARK 465     ARG B   470                                                      
REMARK 465     ILE B   471                                                      
REMARK 465     PRO B   472                                                      
REMARK 465     TYR B   473                                                      
REMARK 465     ALA B   474                                                      
REMARK 465     PRO B   475                                                      
REMARK 465     SER B   476                                                      
REMARK 465     GLY B   477                                                      
REMARK 465     GLU B   478                                                      
REMARK 465     ILE B   479                                                      
REMARK 465     PRO B   480                                                      
REMARK 465     LYS B   481                                                      
REMARK 465     PHE B   482                                                      
REMARK 465     SER B   483                                                      
REMARK 465     LEU B   484                                                      
REMARK 465     GLN B   485                                                      
REMARK 465     ASP B   486                                                      
REMARK 465     PRO B   487                                                      
REMARK 465     PRO B   488                                                      
REMARK 465     ASN B   489                                                      
REMARK 465     LYS B   490                                                      
REMARK 465     LYS B   491                                                      
REMARK 465     PRO B   492                                                      
REMARK 465     LYS B   493                                                      
REMARK 465     VAL B   494                                                      
REMARK 465     PRO C   383                                                      
REMARK 465     GLY C   384                                                      
REMARK 465     VAL C   385                                                      
REMARK 465     SER C   386                                                      
REMARK 465     GLU C   387                                                      
REMARK 465     SER C   468                                                      
REMARK 465     LYS C   469                                                      
REMARK 465     ARG C   470                                                      
REMARK 465     ILE C   471                                                      
REMARK 465     PRO C   472                                                      
REMARK 465     TYR C   473                                                      
REMARK 465     ALA C   474                                                      
REMARK 465     PRO C   475                                                      
REMARK 465     SER C   476                                                      
REMARK 465     GLY C   477                                                      
REMARK 465     GLU C   478                                                      
REMARK 465     ILE C   479                                                      
REMARK 465     PRO C   480                                                      
REMARK 465     LYS C   481                                                      
REMARK 465     PHE C   482                                                      
REMARK 465     SER C   483                                                      
REMARK 465     LEU C   484                                                      
REMARK 465     GLN C   485                                                      
REMARK 465     ASP C   486                                                      
REMARK 465     PRO C   487                                                      
REMARK 465     PRO C   488                                                      
REMARK 465     ASN C   489                                                      
REMARK 465     LYS C   490                                                      
REMARK 465     LYS C   491                                                      
REMARK 465     PRO C   492                                                      
REMARK 465     LYS C   493                                                      
REMARK 465     VAL C   494                                                      
REMARK 465     MET D     1                                                      
REMARK 465     PRO D   383                                                      
REMARK 465     GLY D   384                                                      
REMARK 465     VAL D   385                                                      
REMARK 465     SER D   386                                                      
REMARK 465     GLU D   387                                                      
REMARK 465     ASP D   388                                                      
REMARK 465     SER D   467                                                      
REMARK 465     SER D   468                                                      
REMARK 465     LYS D   469                                                      
REMARK 465     ARG D   470                                                      
REMARK 465     ILE D   471                                                      
REMARK 465     PRO D   472                                                      
REMARK 465     TYR D   473                                                      
REMARK 465     ALA D   474                                                      
REMARK 465     PRO D   475                                                      
REMARK 465     SER D   476                                                      
REMARK 465     GLY D   477                                                      
REMARK 465     GLU D   478                                                      
REMARK 465     ILE D   479                                                      
REMARK 465     PRO D   480                                                      
REMARK 465     LYS D   481                                                      
REMARK 465     PHE D   482                                                      
REMARK 465     SER D   483                                                      
REMARK 465     LEU D   484                                                      
REMARK 465     GLN D   485                                                      
REMARK 465     ASP D   486                                                      
REMARK 465     PRO D   487                                                      
REMARK 465     PRO D   488                                                      
REMARK 465     ASN D   489                                                      
REMARK 465     LYS D   490                                                      
REMARK 465     LYS D   491                                                      
REMARK 465     PRO D   492                                                      
REMARK 465     LYS D   493                                                      
REMARK 465     VAL D   494                                                      
REMARK 465     PRO E   383                                                      
REMARK 465     GLY E   384                                                      
REMARK 465     VAL E   385                                                      
REMARK 465     SER E   386                                                      
REMARK 465     GLU E   387                                                      
REMARK 465     ASP E   388                                                      
REMARK 465     SER E   468                                                      
REMARK 465     LYS E   469                                                      
REMARK 465     ARG E   470                                                      
REMARK 465     ILE E   471                                                      
REMARK 465     PRO E   472                                                      
REMARK 465     TYR E   473                                                      
REMARK 465     ALA E   474                                                      
REMARK 465     PRO E   475                                                      
REMARK 465     SER E   476                                                      
REMARK 465     GLY E   477                                                      
REMARK 465     GLU E   478                                                      
REMARK 465     ILE E   479                                                      
REMARK 465     PRO E   480                                                      
REMARK 465     LYS E   481                                                      
REMARK 465     PHE E   482                                                      
REMARK 465     SER E   483                                                      
REMARK 465     LEU E   484                                                      
REMARK 465     GLN E   485                                                      
REMARK 465     ASP E   486                                                      
REMARK 465     PRO E   487                                                      
REMARK 465     PRO E   488                                                      
REMARK 465     ASN E   489                                                      
REMARK 465     LYS E   490                                                      
REMARK 465     LYS E   491                                                      
REMARK 465     PRO E   492                                                      
REMARK 465     LYS E   493                                                      
REMARK 465     VAL E   494                                                      
REMARK 465     PRO F   383                                                      
REMARK 465     GLY F   384                                                      
REMARK 465     VAL F   385                                                      
REMARK 465     SER F   386                                                      
REMARK 465     GLU F   387                                                      
REMARK 465     LYS F   469                                                      
REMARK 465     ARG F   470                                                      
REMARK 465     ILE F   471                                                      
REMARK 465     PRO F   472                                                      
REMARK 465     TYR F   473                                                      
REMARK 465     ALA F   474                                                      
REMARK 465     PRO F   475                                                      
REMARK 465     SER F   476                                                      
REMARK 465     GLY F   477                                                      
REMARK 465     GLU F   478                                                      
REMARK 465     ILE F   479                                                      
REMARK 465     PRO F   480                                                      
REMARK 465     LYS F   481                                                      
REMARK 465     PHE F   482                                                      
REMARK 465     SER F   483                                                      
REMARK 465     LEU F   484                                                      
REMARK 465     GLN F   485                                                      
REMARK 465     ASP F   486                                                      
REMARK 465     PRO F   487                                                      
REMARK 465     PRO F   488                                                      
REMARK 465     ASN F   489                                                      
REMARK 465     LYS F   490                                                      
REMARK 465     LYS F   491                                                      
REMARK 465     PRO F   492                                                      
REMARK 465     LYS F   493                                                      
REMARK 465     VAL F   494                                                      
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   O2   POP F   501     O    HOH F   601              2.06            
REMARK 500   O2   POP B   501     O    HOH B   601              2.08            
REMARK 500   OE1  GLU F   242     NH1  ARG F   313              2.16            
REMARK 500   NH1  ARG F   135     OE1  GLU F   138              2.18            
REMARK 500   O    HOH C   646     O    HOH C   777              2.18            
REMARK 500   O3   POP F   501     O    HOH F   602              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS B  64   CB    CYS B  64   SG     -0.119                       
REMARK 500    CYS C  64   CB    CYS C  64   SG     -0.117                       
REMARK 500    CYS F  64   CB    CYS F  64   SG     -0.108                       
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    TYR A  14       -6.28    -59.71                                   
REMARK 500    LYS A  67      -71.73    -95.75                                   
REMARK 500    ARG A 102      -51.53   -138.15                                   
REMARK 500    ARG A 135        5.61     80.29                                   
REMARK 500    ASN A 159       74.54   -150.14                                   
REMARK 500    GLU A 184       35.13    -91.53                                   
REMARK 500    TRP A 202       -8.22   -145.89                                   
REMARK 500    LEU A 322       40.34    -81.53                                   
REMARK 500    GLU A 416       42.12    -80.76                                   
REMARK 500    LYS B  67      -69.93    -94.45                                   
REMARK 500    ARG B 102      -52.10   -138.97                                   
REMARK 500    ARG B 135        5.21     82.41                                   
REMARK 500    ASN B 159       75.45   -150.76                                   
REMARK 500    GLU B 184       35.23    -91.12                                   
REMARK 500    TRP B 202       -7.97   -145.58                                   
REMARK 500    LEU B 322       41.27    -80.50                                   
REMARK 500    GLU B 416       40.59    -80.30                                   
REMARK 500    LYS C  67      -69.87    -96.48                                   
REMARK 500    ARG C 102      -51.41   -139.63                                   
REMARK 500    GLU C 184       34.08    -88.07                                   
REMARK 500    TRP C 202       -6.82   -144.59                                   
REMARK 500    LEU C 293       67.21   -119.37                                   
REMARK 500    LEU C 322       43.40    -80.55                                   
REMARK 500    GLU C 416       40.43    -81.17                                   
REMARK 500    LYS D  67      -69.90    -95.21                                   
REMARK 500    ARG D 102      -51.75   -137.87                                   
REMARK 500    ARG D 135        6.74     81.39                                   
REMARK 500    ASN D 159       76.44   -150.89                                   
REMARK 500    GLU D 184       36.20    -90.77                                   
REMARK 500    TRP D 202       -8.68   -145.65                                   
REMARK 500    CYS D 276      -36.15   -131.40                                   
REMARK 500    LEU D 293       67.02   -119.50                                   
REMARK 500    LEU D 322       43.74    -79.12                                   
REMARK 500    GLU D 416       40.08    -81.97                                   
REMARK 500    LYS E  67      -68.34    -98.73                                   
REMARK 500    ARG E 102      -51.94   -138.26                                   
REMARK 500    ARG E 135        6.55     82.02                                   
REMARK 500    ASN E 159       77.67   -150.89                                   
REMARK 500    GLU E 184       36.82    -91.03                                   
REMARK 500    TRP E 202       -8.27   -146.24                                   
REMARK 500    LEU E 322       42.14    -81.34                                   
REMARK 500    GLU E 416       40.41    -79.50                                   
REMARK 500    LYS F  67      -69.09    -96.57                                   
REMARK 500    ARG F 102      -43.56   -138.43                                   
REMARK 500    ARG F 135        7.59     81.45                                   
REMARK 500    ASN F 159       73.90   -150.69                                   
REMARK 500    GLU F 184       33.92    -90.80                                   
REMARK 500    TRP F 202       -8.17   -145.34                                   
REMARK 500    LEU F 293       65.91   -118.73                                   
REMARK 500    LEU F 322       41.57    -81.81                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      51 RAMACHANDRAN OUTLIERS.                        
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 POP A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue POP B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue UPG C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue POP D 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue POP E 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue POP F 501                 
DBREF  5TJH A    1   494  UNP    O60701   UGDH_HUMAN       1    494             
DBREF  5TJH B    1   494  UNP    O60701   UGDH_HUMAN       1    494             
DBREF  5TJH C    1   494  UNP    O60701   UGDH_HUMAN       1    494             
DBREF  5TJH D    1   494  UNP    O60701   UGDH_HUMAN       1    494             
DBREF  5TJH E    1   494  UNP    O60701   UGDH_HUMAN       1    494             
DBREF  5TJH F    1   494  UNP    O60701   UGDH_HUMAN       1    494             
SEQADV 5TJH MET A  136  UNP  O60701    ALA   136 ENGINEERED MUTATION            
SEQADV 5TJH MET B  136  UNP  O60701    ALA   136 ENGINEERED MUTATION            
SEQADV 5TJH MET C  136  UNP  O60701    ALA   136 ENGINEERED MUTATION            
SEQADV 5TJH MET D  136  UNP  O60701    ALA   136 ENGINEERED MUTATION            
SEQADV 5TJH MET E  136  UNP  O60701    ALA   136 ENGINEERED MUTATION            
SEQADV 5TJH MET F  136  UNP  O60701    ALA   136 ENGINEERED MUTATION            
SEQRES   1 A  494  MET PHE GLU ILE LYS LYS ILE CYS CYS ILE GLY ALA GLY          
SEQRES   2 A  494  TYR VAL GLY GLY PRO THR CYS SER VAL ILE ALA HIS MET          
SEQRES   3 A  494  CYS PRO GLU ILE ARG VAL THR VAL VAL ASP VAL ASN GLU          
SEQRES   4 A  494  SER ARG ILE ASN ALA TRP ASN SER PRO THR LEU PRO ILE          
SEQRES   5 A  494  TYR GLU PRO GLY LEU LYS GLU VAL VAL GLU SER CYS ARG          
SEQRES   6 A  494  GLY LYS ASN LEU PHE PHE SER THR ASN ILE ASP ASP ALA          
SEQRES   7 A  494  ILE LYS GLU ALA ASP LEU VAL PHE ILE SER VAL ASN THR          
SEQRES   8 A  494  PRO THR LYS THR TYR GLY MET GLY LYS GLY ARG ALA ALA          
SEQRES   9 A  494  ASP LEU LYS TYR ILE GLU ALA CYS ALA ARG ARG ILE VAL          
SEQRES  10 A  494  GLN ASN SER ASN GLY TYR LYS ILE VAL THR GLU LYS SER          
SEQRES  11 A  494  THR VAL PRO VAL ARG MET ALA GLU SER ILE ARG ARG ILE          
SEQRES  12 A  494  PHE ASP ALA ASN THR LYS PRO ASN LEU ASN LEU GLN VAL          
SEQRES  13 A  494  LEU SER ASN PRO GLU PHE LEU ALA GLU GLY THR ALA ILE          
SEQRES  14 A  494  LYS ASP LEU LYS ASN PRO ASP ARG VAL LEU ILE GLY GLY          
SEQRES  15 A  494  ASP GLU THR PRO GLU GLY GLN ARG ALA VAL GLN ALA LEU          
SEQRES  16 A  494  CYS ALA VAL TYR GLU HIS TRP VAL PRO ARG GLU LYS ILE          
SEQRES  17 A  494  LEU THR THR ASN THR TRP SER SER GLU LEU SER LYS LEU          
SEQRES  18 A  494  ALA ALA ASN ALA PHE LEU ALA GLN ARG ILE SER SER ILE          
SEQRES  19 A  494  ASN SER ILE SER ALA LEU CYS GLU ALA THR GLY ALA ASP          
SEQRES  20 A  494  VAL GLU GLU VAL ALA THR ALA ILE GLY MET ASP GLN ARG          
SEQRES  21 A  494  ILE GLY ASN LYS PHE LEU LYS ALA SER VAL GLY PHE GLY          
SEQRES  22 A  494  GLY SER CYS PHE GLN LYS ASP VAL LEU ASN LEU VAL TYR          
SEQRES  23 A  494  LEU CYS GLU ALA LEU ASN LEU PRO GLU VAL ALA ARG TYR          
SEQRES  24 A  494  TRP GLN GLN VAL ILE ASP MET ASN ASP TYR GLN ARG ARG          
SEQRES  25 A  494  ARG PHE ALA SER ARG ILE ILE ASP SER LEU PHE ASN THR          
SEQRES  26 A  494  VAL THR ASP LYS LYS ILE ALA ILE LEU GLY PHE ALA PHE          
SEQRES  27 A  494  LYS LYS ASP THR GLY ASP THR ARG GLU SER SER SER ILE          
SEQRES  28 A  494  TYR ILE SER LYS TYR LEU MET ASP GLU GLY ALA HIS LEU          
SEQRES  29 A  494  HIS ILE TYR ASP PRO LYS VAL PRO ARG GLU GLN ILE VAL          
SEQRES  30 A  494  VAL ASP LEU SER HIS PRO GLY VAL SER GLU ASP ASP GLN          
SEQRES  31 A  494  VAL SER ARG LEU VAL THR ILE SER LYS ASP PRO TYR GLU          
SEQRES  32 A  494  ALA CYS ASP GLY ALA HIS ALA VAL VAL ILE CYS THR GLU          
SEQRES  33 A  494  TRP ASP MET PHE LYS GLU LEU ASP TYR GLU ARG ILE HIS          
SEQRES  34 A  494  LYS LYS MET LEU LYS PRO ALA PHE ILE PHE ASP GLY ARG          
SEQRES  35 A  494  ARG VAL LEU ASP GLY LEU HIS ASN GLU LEU GLN THR ILE          
SEQRES  36 A  494  GLY PHE GLN ILE GLU THR ILE GLY LYS LYS VAL SER SER          
SEQRES  37 A  494  LYS ARG ILE PRO TYR ALA PRO SER GLY GLU ILE PRO LYS          
SEQRES  38 A  494  PHE SER LEU GLN ASP PRO PRO ASN LYS LYS PRO LYS VAL          
SEQRES   1 B  494  MET PHE GLU ILE LYS LYS ILE CYS CYS ILE GLY ALA GLY          
SEQRES   2 B  494  TYR VAL GLY GLY PRO THR CYS SER VAL ILE ALA HIS MET          
SEQRES   3 B  494  CYS PRO GLU ILE ARG VAL THR VAL VAL ASP VAL ASN GLU          
SEQRES   4 B  494  SER ARG ILE ASN ALA TRP ASN SER PRO THR LEU PRO ILE          
SEQRES   5 B  494  TYR GLU PRO GLY LEU LYS GLU VAL VAL GLU SER CYS ARG          
SEQRES   6 B  494  GLY LYS ASN LEU PHE PHE SER THR ASN ILE ASP ASP ALA          
SEQRES   7 B  494  ILE LYS GLU ALA ASP LEU VAL PHE ILE SER VAL ASN THR          
SEQRES   8 B  494  PRO THR LYS THR TYR GLY MET GLY LYS GLY ARG ALA ALA          
SEQRES   9 B  494  ASP LEU LYS TYR ILE GLU ALA CYS ALA ARG ARG ILE VAL          
SEQRES  10 B  494  GLN ASN SER ASN GLY TYR LYS ILE VAL THR GLU LYS SER          
SEQRES  11 B  494  THR VAL PRO VAL ARG MET ALA GLU SER ILE ARG ARG ILE          
SEQRES  12 B  494  PHE ASP ALA ASN THR LYS PRO ASN LEU ASN LEU GLN VAL          
SEQRES  13 B  494  LEU SER ASN PRO GLU PHE LEU ALA GLU GLY THR ALA ILE          
SEQRES  14 B  494  LYS ASP LEU LYS ASN PRO ASP ARG VAL LEU ILE GLY GLY          
SEQRES  15 B  494  ASP GLU THR PRO GLU GLY GLN ARG ALA VAL GLN ALA LEU          
SEQRES  16 B  494  CYS ALA VAL TYR GLU HIS TRP VAL PRO ARG GLU LYS ILE          
SEQRES  17 B  494  LEU THR THR ASN THR TRP SER SER GLU LEU SER LYS LEU          
SEQRES  18 B  494  ALA ALA ASN ALA PHE LEU ALA GLN ARG ILE SER SER ILE          
SEQRES  19 B  494  ASN SER ILE SER ALA LEU CYS GLU ALA THR GLY ALA ASP          
SEQRES  20 B  494  VAL GLU GLU VAL ALA THR ALA ILE GLY MET ASP GLN ARG          
SEQRES  21 B  494  ILE GLY ASN LYS PHE LEU LYS ALA SER VAL GLY PHE GLY          
SEQRES  22 B  494  GLY SER CYS PHE GLN LYS ASP VAL LEU ASN LEU VAL TYR          
SEQRES  23 B  494  LEU CYS GLU ALA LEU ASN LEU PRO GLU VAL ALA ARG TYR          
SEQRES  24 B  494  TRP GLN GLN VAL ILE ASP MET ASN ASP TYR GLN ARG ARG          
SEQRES  25 B  494  ARG PHE ALA SER ARG ILE ILE ASP SER LEU PHE ASN THR          
SEQRES  26 B  494  VAL THR ASP LYS LYS ILE ALA ILE LEU GLY PHE ALA PHE          
SEQRES  27 B  494  LYS LYS ASP THR GLY ASP THR ARG GLU SER SER SER ILE          
SEQRES  28 B  494  TYR ILE SER LYS TYR LEU MET ASP GLU GLY ALA HIS LEU          
SEQRES  29 B  494  HIS ILE TYR ASP PRO LYS VAL PRO ARG GLU GLN ILE VAL          
SEQRES  30 B  494  VAL ASP LEU SER HIS PRO GLY VAL SER GLU ASP ASP GLN          
SEQRES  31 B  494  VAL SER ARG LEU VAL THR ILE SER LYS ASP PRO TYR GLU          
SEQRES  32 B  494  ALA CYS ASP GLY ALA HIS ALA VAL VAL ILE CYS THR GLU          
SEQRES  33 B  494  TRP ASP MET PHE LYS GLU LEU ASP TYR GLU ARG ILE HIS          
SEQRES  34 B  494  LYS LYS MET LEU LYS PRO ALA PHE ILE PHE ASP GLY ARG          
SEQRES  35 B  494  ARG VAL LEU ASP GLY LEU HIS ASN GLU LEU GLN THR ILE          
SEQRES  36 B  494  GLY PHE GLN ILE GLU THR ILE GLY LYS LYS VAL SER SER          
SEQRES  37 B  494  LYS ARG ILE PRO TYR ALA PRO SER GLY GLU ILE PRO LYS          
SEQRES  38 B  494  PHE SER LEU GLN ASP PRO PRO ASN LYS LYS PRO LYS VAL          
SEQRES   1 C  494  MET PHE GLU ILE LYS LYS ILE CYS CYS ILE GLY ALA GLY          
SEQRES   2 C  494  TYR VAL GLY GLY PRO THR CYS SER VAL ILE ALA HIS MET          
SEQRES   3 C  494  CYS PRO GLU ILE ARG VAL THR VAL VAL ASP VAL ASN GLU          
SEQRES   4 C  494  SER ARG ILE ASN ALA TRP ASN SER PRO THR LEU PRO ILE          
SEQRES   5 C  494  TYR GLU PRO GLY LEU LYS GLU VAL VAL GLU SER CYS ARG          
SEQRES   6 C  494  GLY LYS ASN LEU PHE PHE SER THR ASN ILE ASP ASP ALA          
SEQRES   7 C  494  ILE LYS GLU ALA ASP LEU VAL PHE ILE SER VAL ASN THR          
SEQRES   8 C  494  PRO THR LYS THR TYR GLY MET GLY LYS GLY ARG ALA ALA          
SEQRES   9 C  494  ASP LEU LYS TYR ILE GLU ALA CYS ALA ARG ARG ILE VAL          
SEQRES  10 C  494  GLN ASN SER ASN GLY TYR LYS ILE VAL THR GLU LYS SER          
SEQRES  11 C  494  THR VAL PRO VAL ARG MET ALA GLU SER ILE ARG ARG ILE          
SEQRES  12 C  494  PHE ASP ALA ASN THR LYS PRO ASN LEU ASN LEU GLN VAL          
SEQRES  13 C  494  LEU SER ASN PRO GLU PHE LEU ALA GLU GLY THR ALA ILE          
SEQRES  14 C  494  LYS ASP LEU LYS ASN PRO ASP ARG VAL LEU ILE GLY GLY          
SEQRES  15 C  494  ASP GLU THR PRO GLU GLY GLN ARG ALA VAL GLN ALA LEU          
SEQRES  16 C  494  CYS ALA VAL TYR GLU HIS TRP VAL PRO ARG GLU LYS ILE          
SEQRES  17 C  494  LEU THR THR ASN THR TRP SER SER GLU LEU SER LYS LEU          
SEQRES  18 C  494  ALA ALA ASN ALA PHE LEU ALA GLN ARG ILE SER SER ILE          
SEQRES  19 C  494  ASN SER ILE SER ALA LEU CYS GLU ALA THR GLY ALA ASP          
SEQRES  20 C  494  VAL GLU GLU VAL ALA THR ALA ILE GLY MET ASP GLN ARG          
SEQRES  21 C  494  ILE GLY ASN LYS PHE LEU LYS ALA SER VAL GLY PHE GLY          
SEQRES  22 C  494  GLY SER CYS PHE GLN LYS ASP VAL LEU ASN LEU VAL TYR          
SEQRES  23 C  494  LEU CYS GLU ALA LEU ASN LEU PRO GLU VAL ALA ARG TYR          
SEQRES  24 C  494  TRP GLN GLN VAL ILE ASP MET ASN ASP TYR GLN ARG ARG          
SEQRES  25 C  494  ARG PHE ALA SER ARG ILE ILE ASP SER LEU PHE ASN THR          
SEQRES  26 C  494  VAL THR ASP LYS LYS ILE ALA ILE LEU GLY PHE ALA PHE          
SEQRES  27 C  494  LYS LYS ASP THR GLY ASP THR ARG GLU SER SER SER ILE          
SEQRES  28 C  494  TYR ILE SER LYS TYR LEU MET ASP GLU GLY ALA HIS LEU          
SEQRES  29 C  494  HIS ILE TYR ASP PRO LYS VAL PRO ARG GLU GLN ILE VAL          
SEQRES  30 C  494  VAL ASP LEU SER HIS PRO GLY VAL SER GLU ASP ASP GLN          
SEQRES  31 C  494  VAL SER ARG LEU VAL THR ILE SER LYS ASP PRO TYR GLU          
SEQRES  32 C  494  ALA CYS ASP GLY ALA HIS ALA VAL VAL ILE CYS THR GLU          
SEQRES  33 C  494  TRP ASP MET PHE LYS GLU LEU ASP TYR GLU ARG ILE HIS          
SEQRES  34 C  494  LYS LYS MET LEU LYS PRO ALA PHE ILE PHE ASP GLY ARG          
SEQRES  35 C  494  ARG VAL LEU ASP GLY LEU HIS ASN GLU LEU GLN THR ILE          
SEQRES  36 C  494  GLY PHE GLN ILE GLU THR ILE GLY LYS LYS VAL SER SER          
SEQRES  37 C  494  LYS ARG ILE PRO TYR ALA PRO SER GLY GLU ILE PRO LYS          
SEQRES  38 C  494  PHE SER LEU GLN ASP PRO PRO ASN LYS LYS PRO LYS VAL          
SEQRES   1 D  494  MET PHE GLU ILE LYS LYS ILE CYS CYS ILE GLY ALA GLY          
SEQRES   2 D  494  TYR VAL GLY GLY PRO THR CYS SER VAL ILE ALA HIS MET          
SEQRES   3 D  494  CYS PRO GLU ILE ARG VAL THR VAL VAL ASP VAL ASN GLU          
SEQRES   4 D  494  SER ARG ILE ASN ALA TRP ASN SER PRO THR LEU PRO ILE          
SEQRES   5 D  494  TYR GLU PRO GLY LEU LYS GLU VAL VAL GLU SER CYS ARG          
SEQRES   6 D  494  GLY LYS ASN LEU PHE PHE SER THR ASN ILE ASP ASP ALA          
SEQRES   7 D  494  ILE LYS GLU ALA ASP LEU VAL PHE ILE SER VAL ASN THR          
SEQRES   8 D  494  PRO THR LYS THR TYR GLY MET GLY LYS GLY ARG ALA ALA          
SEQRES   9 D  494  ASP LEU LYS TYR ILE GLU ALA CYS ALA ARG ARG ILE VAL          
SEQRES  10 D  494  GLN ASN SER ASN GLY TYR LYS ILE VAL THR GLU LYS SER          
SEQRES  11 D  494  THR VAL PRO VAL ARG MET ALA GLU SER ILE ARG ARG ILE          
SEQRES  12 D  494  PHE ASP ALA ASN THR LYS PRO ASN LEU ASN LEU GLN VAL          
SEQRES  13 D  494  LEU SER ASN PRO GLU PHE LEU ALA GLU GLY THR ALA ILE          
SEQRES  14 D  494  LYS ASP LEU LYS ASN PRO ASP ARG VAL LEU ILE GLY GLY          
SEQRES  15 D  494  ASP GLU THR PRO GLU GLY GLN ARG ALA VAL GLN ALA LEU          
SEQRES  16 D  494  CYS ALA VAL TYR GLU HIS TRP VAL PRO ARG GLU LYS ILE          
SEQRES  17 D  494  LEU THR THR ASN THR TRP SER SER GLU LEU SER LYS LEU          
SEQRES  18 D  494  ALA ALA ASN ALA PHE LEU ALA GLN ARG ILE SER SER ILE          
SEQRES  19 D  494  ASN SER ILE SER ALA LEU CYS GLU ALA THR GLY ALA ASP          
SEQRES  20 D  494  VAL GLU GLU VAL ALA THR ALA ILE GLY MET ASP GLN ARG          
SEQRES  21 D  494  ILE GLY ASN LYS PHE LEU LYS ALA SER VAL GLY PHE GLY          
SEQRES  22 D  494  GLY SER CYS PHE GLN LYS ASP VAL LEU ASN LEU VAL TYR          
SEQRES  23 D  494  LEU CYS GLU ALA LEU ASN LEU PRO GLU VAL ALA ARG TYR          
SEQRES  24 D  494  TRP GLN GLN VAL ILE ASP MET ASN ASP TYR GLN ARG ARG          
SEQRES  25 D  494  ARG PHE ALA SER ARG ILE ILE ASP SER LEU PHE ASN THR          
SEQRES  26 D  494  VAL THR ASP LYS LYS ILE ALA ILE LEU GLY PHE ALA PHE          
SEQRES  27 D  494  LYS LYS ASP THR GLY ASP THR ARG GLU SER SER SER ILE          
SEQRES  28 D  494  TYR ILE SER LYS TYR LEU MET ASP GLU GLY ALA HIS LEU          
SEQRES  29 D  494  HIS ILE TYR ASP PRO LYS VAL PRO ARG GLU GLN ILE VAL          
SEQRES  30 D  494  VAL ASP LEU SER HIS PRO GLY VAL SER GLU ASP ASP GLN          
SEQRES  31 D  494  VAL SER ARG LEU VAL THR ILE SER LYS ASP PRO TYR GLU          
SEQRES  32 D  494  ALA CYS ASP GLY ALA HIS ALA VAL VAL ILE CYS THR GLU          
SEQRES  33 D  494  TRP ASP MET PHE LYS GLU LEU ASP TYR GLU ARG ILE HIS          
SEQRES  34 D  494  LYS LYS MET LEU LYS PRO ALA PHE ILE PHE ASP GLY ARG          
SEQRES  35 D  494  ARG VAL LEU ASP GLY LEU HIS ASN GLU LEU GLN THR ILE          
SEQRES  36 D  494  GLY PHE GLN ILE GLU THR ILE GLY LYS LYS VAL SER SER          
SEQRES  37 D  494  LYS ARG ILE PRO TYR ALA PRO SER GLY GLU ILE PRO LYS          
SEQRES  38 D  494  PHE SER LEU GLN ASP PRO PRO ASN LYS LYS PRO LYS VAL          
SEQRES   1 E  494  MET PHE GLU ILE LYS LYS ILE CYS CYS ILE GLY ALA GLY          
SEQRES   2 E  494  TYR VAL GLY GLY PRO THR CYS SER VAL ILE ALA HIS MET          
SEQRES   3 E  494  CYS PRO GLU ILE ARG VAL THR VAL VAL ASP VAL ASN GLU          
SEQRES   4 E  494  SER ARG ILE ASN ALA TRP ASN SER PRO THR LEU PRO ILE          
SEQRES   5 E  494  TYR GLU PRO GLY LEU LYS GLU VAL VAL GLU SER CYS ARG          
SEQRES   6 E  494  GLY LYS ASN LEU PHE PHE SER THR ASN ILE ASP ASP ALA          
SEQRES   7 E  494  ILE LYS GLU ALA ASP LEU VAL PHE ILE SER VAL ASN THR          
SEQRES   8 E  494  PRO THR LYS THR TYR GLY MET GLY LYS GLY ARG ALA ALA          
SEQRES   9 E  494  ASP LEU LYS TYR ILE GLU ALA CYS ALA ARG ARG ILE VAL          
SEQRES  10 E  494  GLN ASN SER ASN GLY TYR LYS ILE VAL THR GLU LYS SER          
SEQRES  11 E  494  THR VAL PRO VAL ARG MET ALA GLU SER ILE ARG ARG ILE          
SEQRES  12 E  494  PHE ASP ALA ASN THR LYS PRO ASN LEU ASN LEU GLN VAL          
SEQRES  13 E  494  LEU SER ASN PRO GLU PHE LEU ALA GLU GLY THR ALA ILE          
SEQRES  14 E  494  LYS ASP LEU LYS ASN PRO ASP ARG VAL LEU ILE GLY GLY          
SEQRES  15 E  494  ASP GLU THR PRO GLU GLY GLN ARG ALA VAL GLN ALA LEU          
SEQRES  16 E  494  CYS ALA VAL TYR GLU HIS TRP VAL PRO ARG GLU LYS ILE          
SEQRES  17 E  494  LEU THR THR ASN THR TRP SER SER GLU LEU SER LYS LEU          
SEQRES  18 E  494  ALA ALA ASN ALA PHE LEU ALA GLN ARG ILE SER SER ILE          
SEQRES  19 E  494  ASN SER ILE SER ALA LEU CYS GLU ALA THR GLY ALA ASP          
SEQRES  20 E  494  VAL GLU GLU VAL ALA THR ALA ILE GLY MET ASP GLN ARG          
SEQRES  21 E  494  ILE GLY ASN LYS PHE LEU LYS ALA SER VAL GLY PHE GLY          
SEQRES  22 E  494  GLY SER CYS PHE GLN LYS ASP VAL LEU ASN LEU VAL TYR          
SEQRES  23 E  494  LEU CYS GLU ALA LEU ASN LEU PRO GLU VAL ALA ARG TYR          
SEQRES  24 E  494  TRP GLN GLN VAL ILE ASP MET ASN ASP TYR GLN ARG ARG          
SEQRES  25 E  494  ARG PHE ALA SER ARG ILE ILE ASP SER LEU PHE ASN THR          
SEQRES  26 E  494  VAL THR ASP LYS LYS ILE ALA ILE LEU GLY PHE ALA PHE          
SEQRES  27 E  494  LYS LYS ASP THR GLY ASP THR ARG GLU SER SER SER ILE          
SEQRES  28 E  494  TYR ILE SER LYS TYR LEU MET ASP GLU GLY ALA HIS LEU          
SEQRES  29 E  494  HIS ILE TYR ASP PRO LYS VAL PRO ARG GLU GLN ILE VAL          
SEQRES  30 E  494  VAL ASP LEU SER HIS PRO GLY VAL SER GLU ASP ASP GLN          
SEQRES  31 E  494  VAL SER ARG LEU VAL THR ILE SER LYS ASP PRO TYR GLU          
SEQRES  32 E  494  ALA CYS ASP GLY ALA HIS ALA VAL VAL ILE CYS THR GLU          
SEQRES  33 E  494  TRP ASP MET PHE LYS GLU LEU ASP TYR GLU ARG ILE HIS          
SEQRES  34 E  494  LYS LYS MET LEU LYS PRO ALA PHE ILE PHE ASP GLY ARG          
SEQRES  35 E  494  ARG VAL LEU ASP GLY LEU HIS ASN GLU LEU GLN THR ILE          
SEQRES  36 E  494  GLY PHE GLN ILE GLU THR ILE GLY LYS LYS VAL SER SER          
SEQRES  37 E  494  LYS ARG ILE PRO TYR ALA PRO SER GLY GLU ILE PRO LYS          
SEQRES  38 E  494  PHE SER LEU GLN ASP PRO PRO ASN LYS LYS PRO LYS VAL          
SEQRES   1 F  494  MET PHE GLU ILE LYS LYS ILE CYS CYS ILE GLY ALA GLY          
SEQRES   2 F  494  TYR VAL GLY GLY PRO THR CYS SER VAL ILE ALA HIS MET          
SEQRES   3 F  494  CYS PRO GLU ILE ARG VAL THR VAL VAL ASP VAL ASN GLU          
SEQRES   4 F  494  SER ARG ILE ASN ALA TRP ASN SER PRO THR LEU PRO ILE          
SEQRES   5 F  494  TYR GLU PRO GLY LEU LYS GLU VAL VAL GLU SER CYS ARG          
SEQRES   6 F  494  GLY LYS ASN LEU PHE PHE SER THR ASN ILE ASP ASP ALA          
SEQRES   7 F  494  ILE LYS GLU ALA ASP LEU VAL PHE ILE SER VAL ASN THR          
SEQRES   8 F  494  PRO THR LYS THR TYR GLY MET GLY LYS GLY ARG ALA ALA          
SEQRES   9 F  494  ASP LEU LYS TYR ILE GLU ALA CYS ALA ARG ARG ILE VAL          
SEQRES  10 F  494  GLN ASN SER ASN GLY TYR LYS ILE VAL THR GLU LYS SER          
SEQRES  11 F  494  THR VAL PRO VAL ARG MET ALA GLU SER ILE ARG ARG ILE          
SEQRES  12 F  494  PHE ASP ALA ASN THR LYS PRO ASN LEU ASN LEU GLN VAL          
SEQRES  13 F  494  LEU SER ASN PRO GLU PHE LEU ALA GLU GLY THR ALA ILE          
SEQRES  14 F  494  LYS ASP LEU LYS ASN PRO ASP ARG VAL LEU ILE GLY GLY          
SEQRES  15 F  494  ASP GLU THR PRO GLU GLY GLN ARG ALA VAL GLN ALA LEU          
SEQRES  16 F  494  CYS ALA VAL TYR GLU HIS TRP VAL PRO ARG GLU LYS ILE          
SEQRES  17 F  494  LEU THR THR ASN THR TRP SER SER GLU LEU SER LYS LEU          
SEQRES  18 F  494  ALA ALA ASN ALA PHE LEU ALA GLN ARG ILE SER SER ILE          
SEQRES  19 F  494  ASN SER ILE SER ALA LEU CYS GLU ALA THR GLY ALA ASP          
SEQRES  20 F  494  VAL GLU GLU VAL ALA THR ALA ILE GLY MET ASP GLN ARG          
SEQRES  21 F  494  ILE GLY ASN LYS PHE LEU LYS ALA SER VAL GLY PHE GLY          
SEQRES  22 F  494  GLY SER CYS PHE GLN LYS ASP VAL LEU ASN LEU VAL TYR          
SEQRES  23 F  494  LEU CYS GLU ALA LEU ASN LEU PRO GLU VAL ALA ARG TYR          
SEQRES  24 F  494  TRP GLN GLN VAL ILE ASP MET ASN ASP TYR GLN ARG ARG          
SEQRES  25 F  494  ARG PHE ALA SER ARG ILE ILE ASP SER LEU PHE ASN THR          
SEQRES  26 F  494  VAL THR ASP LYS LYS ILE ALA ILE LEU GLY PHE ALA PHE          
SEQRES  27 F  494  LYS LYS ASP THR GLY ASP THR ARG GLU SER SER SER ILE          
SEQRES  28 F  494  TYR ILE SER LYS TYR LEU MET ASP GLU GLY ALA HIS LEU          
SEQRES  29 F  494  HIS ILE TYR ASP PRO LYS VAL PRO ARG GLU GLN ILE VAL          
SEQRES  30 F  494  VAL ASP LEU SER HIS PRO GLY VAL SER GLU ASP ASP GLN          
SEQRES  31 F  494  VAL SER ARG LEU VAL THR ILE SER LYS ASP PRO TYR GLU          
SEQRES  32 F  494  ALA CYS ASP GLY ALA HIS ALA VAL VAL ILE CYS THR GLU          
SEQRES  33 F  494  TRP ASP MET PHE LYS GLU LEU ASP TYR GLU ARG ILE HIS          
SEQRES  34 F  494  LYS LYS MET LEU LYS PRO ALA PHE ILE PHE ASP GLY ARG          
SEQRES  35 F  494  ARG VAL LEU ASP GLY LEU HIS ASN GLU LEU GLN THR ILE          
SEQRES  36 F  494  GLY PHE GLN ILE GLU THR ILE GLY LYS LYS VAL SER SER          
SEQRES  37 F  494  LYS ARG ILE PRO TYR ALA PRO SER GLY GLU ILE PRO LYS          
SEQRES  38 F  494  PHE SER LEU GLN ASP PRO PRO ASN LYS LYS PRO LYS VAL          
HET    POP  A 501       9                                                       
HET    POP  B 501       9                                                       
HET     CL  B 502       1                                                       
HET    UPG  C 501      36                                                       
HET    POP  D 501       9                                                       
HET     CL  D 502       1                                                       
HET    POP  E 501       9                                                       
HET    POP  F 501       9                                                       
HETNAM     POP PYROPHOSPHATE 2-                                                 
HETNAM      CL CHLORIDE ION                                                     
HETNAM     UPG URIDINE-5'-DIPHOSPHATE-GLUCOSE                                   
HETSYN     UPG URIDINE-5'-MONOPHOSPHATE GLUCOPYRANOSYL-MONOPHOSPHATE            
HETSYN   2 UPG  ESTER                                                           
FORMUL   7  POP    5(H2 O7 P2 2-)                                               
FORMUL   9   CL    2(CL 1-)                                                     
FORMUL  10  UPG    C15 H24 N2 O17 P2                                            
FORMUL  15  HOH   *802(H2 O)                                                    
HELIX    1 AA1 VAL A   15  CYS A   27  1                                  13    
HELIX    2 AA2 ASN A   38  ASN A   46  1                                   9    
HELIX    3 AA3 GLY A   56  ARG A   65  1                                  10    
HELIX    4 AA4 ASN A   74  ALA A   82  1                                   9    
HELIX    5 AA5 LEU A  106  ASN A  119  1                                  14    
HELIX    6 AA6 ARG A  135  ASN A  147  1                                  13    
HELIX    7 AA7 THR A  167  ASN A  174  1                                   8    
HELIX    8 AA8 THR A  185  GLU A  200  1                                  16    
HELIX    9 AA9 PRO A  204  GLU A  206  5                                   3    
HELIX   10 AB1 ASN A  212  GLY A  245  1                                  34    
HELIX   11 AB2 ASP A  247  MET A  257  1                                  11    
HELIX   12 AB3 CYS A  276  LEU A  291  1                                  16    
HELIX   13 AB4 LEU A  293  LEU A  322  1                                  30    
HELIX   14 AB5 SER A  348  GLU A  360  1                                  13    
HELIX   15 AB6 PRO A  372  SER A  381  1                                  10    
HELIX   16 AB7 GLN A  390  LEU A  394  1                                   5    
HELIX   17 AB8 ASP A  400  ASP A  406  1                                   7    
HELIX   18 AB9 TRP A  417  LEU A  423  5                                   7    
HELIX   19 AC1 ASP A  424  MET A  432  1                                   9    
HELIX   20 AC2 LEU A  448  GLY A  456  1                                   9    
HELIX   21 AC3 VAL B   15  CYS B   27  1                                  13    
HELIX   22 AC4 ASN B   38  ASN B   46  1                                   9    
HELIX   23 AC5 GLY B   56  ARG B   65  1                                  10    
HELIX   24 AC6 ASN B   74  ALA B   82  1                                   9    
HELIX   25 AC7 LEU B  106  ASN B  119  1                                  14    
HELIX   26 AC8 ARG B  135  ASN B  147  1                                  13    
HELIX   27 AC9 THR B  167  ASN B  174  1                                   8    
HELIX   28 AD1 THR B  185  GLU B  200  1                                  16    
HELIX   29 AD2 PRO B  204  GLU B  206  5                                   3    
HELIX   30 AD3 ASN B  212  GLY B  245  1                                  34    
HELIX   31 AD4 ASP B  247  MET B  257  1                                  11    
HELIX   32 AD5 CYS B  276  LEU B  291  1                                  16    
HELIX   33 AD6 LEU B  293  LEU B  322  1                                  30    
HELIX   34 AD7 SER B  348  ASP B  359  1                                  12    
HELIX   35 AD8 PRO B  372  SER B  381  1                                  10    
HELIX   36 AD9 GLN B  390  LEU B  394  1                                   5    
HELIX   37 AE1 ASP B  400  ASP B  406  1                                   7    
HELIX   38 AE2 TRP B  417  LEU B  423  5                                   7    
HELIX   39 AE3 ASP B  424  MET B  432  1                                   9    
HELIX   40 AE4 LEU B  448  GLY B  456  1                                   9    
HELIX   41 AE5 VAL C   15  CYS C   27  1                                  13    
HELIX   42 AE6 ASN C   38  ASN C   46  1                                   9    
HELIX   43 AE7 GLY C   56  ARG C   65  1                                  10    
HELIX   44 AE8 ASN C   74  ALA C   82  1                                   9    
HELIX   45 AE9 LEU C  106  ASN C  119  1                                  14    
HELIX   46 AF1 ARG C  135  ASN C  147  1                                  13    
HELIX   47 AF2 THR C  167  ASN C  174  1                                   8    
HELIX   48 AF3 THR C  185  GLU C  200  1                                  16    
HELIX   49 AF4 PRO C  204  GLU C  206  5                                   3    
HELIX   50 AF5 ASN C  212  GLY C  245  1                                  34    
HELIX   51 AF6 ASP C  247  MET C  257  1                                  11    
HELIX   52 AF7 CYS C  276  LEU C  291  1                                  16    
HELIX   53 AF8 LEU C  293  LEU C  322  1                                  30    
HELIX   54 AF9 SER C  348  ASP C  359  1                                  12    
HELIX   55 AG1 PRO C  372  SER C  381  1                                  10    
HELIX   56 AG2 ASP C  389  LEU C  394  1                                   6    
HELIX   57 AG3 ASP C  400  ASP C  406  1                                   7    
HELIX   58 AG4 TRP C  417  LEU C  423  5                                   7    
HELIX   59 AG5 ASP C  424  MET C  432  1                                   9    
HELIX   60 AG6 LEU C  448  GLY C  456  1                                   9    
HELIX   61 AG7 VAL D   15  CYS D   27  1                                  13    
HELIX   62 AG8 ASN D   38  ASN D   46  1                                   9    
HELIX   63 AG9 GLY D   56  ARG D   65  1                                  10    
HELIX   64 AH1 ASN D   74  ALA D   82  1                                   9    
HELIX   65 AH2 LEU D  106  ASN D  119  1                                  14    
HELIX   66 AH3 ARG D  135  ASN D  147  1                                  13    
HELIX   67 AH4 THR D  167  ASN D  174  1                                   8    
HELIX   68 AH5 THR D  185  GLU D  200  1                                  16    
HELIX   69 AH6 PRO D  204  GLU D  206  5                                   3    
HELIX   70 AH7 ASN D  212  GLY D  245  1                                  34    
HELIX   71 AH8 ASP D  247  MET D  257  1                                  11    
HELIX   72 AH9 CYS D  276  LEU D  291  1                                  16    
HELIX   73 AI1 LEU D  293  LEU D  322  1                                  30    
HELIX   74 AI2 SER D  348  ASP D  359  1                                  12    
HELIX   75 AI3 PRO D  372  SER D  381  1                                  10    
HELIX   76 AI4 GLN D  390  LEU D  394  1                                   5    
HELIX   77 AI5 ASP D  400  ASP D  406  1                                   7    
HELIX   78 AI6 TRP D  417  LEU D  423  5                                   7    
HELIX   79 AI7 ASP D  424  MET D  432  1                                   9    
HELIX   80 AI8 LEU D  448  GLY D  456  1                                   9    
HELIX   81 AI9 VAL E   15  CYS E   27  1                                  13    
HELIX   82 AJ1 ASN E   38  ASN E   46  1                                   9    
HELIX   83 AJ2 GLY E   56  ARG E   65  1                                  10    
HELIX   84 AJ3 ASN E   74  ALA E   82  1                                   9    
HELIX   85 AJ4 LEU E  106  ASN E  119  1                                  14    
HELIX   86 AJ5 ARG E  135  ASN E  147  1                                  13    
HELIX   87 AJ6 THR E  167  ASN E  174  1                                   8    
HELIX   88 AJ7 THR E  185  GLU E  200  1                                  16    
HELIX   89 AJ8 PRO E  204  GLU E  206  5                                   3    
HELIX   90 AJ9 ASN E  212  GLY E  245  1                                  34    
HELIX   91 AK1 ASP E  247  MET E  257  1                                  11    
HELIX   92 AK2 CYS E  276  LEU E  291  1                                  16    
HELIX   93 AK3 LEU E  293  LEU E  322  1                                  30    
HELIX   94 AK4 SER E  348  GLU E  360  1                                  13    
HELIX   95 AK5 PRO E  372  SER E  381  1                                  10    
HELIX   96 AK6 GLN E  390  LEU E  394  1                                   5    
HELIX   97 AK7 ASP E  400  ASP E  406  1                                   7    
HELIX   98 AK8 TRP E  417  LEU E  423  5                                   7    
HELIX   99 AK9 ASP E  424  MET E  432  1                                   9    
HELIX  100 AL1 LEU E  448  GLY E  456  1                                   9    
HELIX  101 AL2 VAL F   15  CYS F   27  1                                  13    
HELIX  102 AL3 ASN F   38  ASN F   46  1                                   9    
HELIX  103 AL4 GLY F   56  ARG F   65  1                                  10    
HELIX  104 AL5 ASN F   74  ALA F   82  1                                   9    
HELIX  105 AL6 LEU F  106  ASN F  119  1                                  14    
HELIX  106 AL7 ARG F  135  ASN F  147  1                                  13    
HELIX  107 AL8 THR F  167  ASN F  174  1                                   8    
HELIX  108 AL9 THR F  185  GLU F  200  1                                  16    
HELIX  109 AM1 PRO F  204  GLU F  206  5                                   3    
HELIX  110 AM2 ASN F  212  GLY F  245  1                                  34    
HELIX  111 AM3 ASP F  247  MET F  257  1                                  11    
HELIX  112 AM4 CYS F  276  LEU F  291  1                                  16    
HELIX  113 AM5 LEU F  293  LEU F  322  1                                  30    
HELIX  114 AM6 SER F  348  GLU F  360  1                                  13    
HELIX  115 AM7 PRO F  372  SER F  381  1                                  10    
HELIX  116 AM8 ASP F  389  LEU F  394  1                                   6    
HELIX  117 AM9 ASP F  400  ASP F  406  1                                   7    
HELIX  118 AN1 TRP F  417  LEU F  423  5                                   7    
HELIX  119 AN2 ASP F  424  MET F  432  1                                   9    
HELIX  120 AN3 LEU F  448  GLY F  456  1                                   9    
SHEET    1 AA1 6 LEU A  69  SER A  72  0                                        
SHEET    2 AA1 6 ARG A  31  VAL A  35  1  N  VAL A  34   O  PHE A  70           
SHEET    3 AA1 6 LYS A   6  ILE A  10  1  N  ILE A   7   O  ARG A  31           
SHEET    4 AA1 6 LEU A  84  ILE A  87  1  O  PHE A  86   N  CYS A   8           
SHEET    5 AA1 6 TYR A 123  GLU A 128  1  O  THR A 127   N  VAL A  85           
SHEET    6 AA1 6 ASN A 153  SER A 158  1  O  GLN A 155   N  VAL A 126           
SHEET    1 AA2 2 VAL A 178  GLY A 181  0                                        
SHEET    2 AA2 2 ILE A 208  THR A 211  1  O  LEU A 209   N  VAL A 178           
SHEET    1 AA3 6 VAL A 395  ILE A 397  0                                        
SHEET    2 AA3 6 HIS A 363  TYR A 367  1  N  LEU A 364   O  THR A 396           
SHEET    3 AA3 6 LYS A 330  LEU A 334  1  N  ILE A 331   O  HIS A 363           
SHEET    4 AA3 6 ALA A 410  ILE A 413  1  O  VAL A 412   N  LEU A 334           
SHEET    5 AA3 6 PHE A 437  ASP A 440  1  O  PHE A 439   N  VAL A 411           
SHEET    6 AA3 6 GLN A 458  THR A 461  1  O  GLU A 460   N  ASP A 440           
SHEET    1 AA4 6 LEU B  69  SER B  72  0                                        
SHEET    2 AA4 6 ARG B  31  VAL B  35  1  N  VAL B  34   O  PHE B  70           
SHEET    3 AA4 6 LYS B   6  ILE B  10  1  N  CYS B   9   O  VAL B  35           
SHEET    4 AA4 6 LEU B  84  ILE B  87  1  O  PHE B  86   N  ILE B  10           
SHEET    5 AA4 6 TYR B 123  GLU B 128  1  O  THR B 127   N  VAL B  85           
SHEET    6 AA4 6 ASN B 153  SER B 158  1  O  GLN B 155   N  VAL B 126           
SHEET    1 AA5 2 VAL B 178  GLY B 181  0                                        
SHEET    2 AA5 2 ILE B 208  THR B 211  1  O  LEU B 209   N  VAL B 178           
SHEET    1 AA6 6 VAL B 395  ILE B 397  0                                        
SHEET    2 AA6 6 HIS B 363  TYR B 367  1  N  LEU B 364   O  THR B 396           
SHEET    3 AA6 6 LYS B 330  LEU B 334  1  N  ILE B 333   O  TYR B 367           
SHEET    4 AA6 6 ALA B 410  ILE B 413  1  O  VAL B 412   N  ALA B 332           
SHEET    5 AA6 6 PHE B 437  ASP B 440  1  O  PHE B 439   N  VAL B 411           
SHEET    6 AA6 6 GLN B 458  THR B 461  1  O  GLU B 460   N  ASP B 440           
SHEET    1 AA7 6 LEU C  69  SER C  72  0                                        
SHEET    2 AA7 6 ARG C  31  VAL C  35  1  N  VAL C  34   O  PHE C  70           
SHEET    3 AA7 6 LYS C   6  ILE C  10  1  N  CYS C   9   O  VAL C  35           
SHEET    4 AA7 6 LEU C  84  ILE C  87  1  O  PHE C  86   N  CYS C   8           
SHEET    5 AA7 6 TYR C 123  GLU C 128  1  O  ILE C 125   N  VAL C  85           
SHEET    6 AA7 6 ASN C 153  SER C 158  1  O  GLN C 155   N  VAL C 126           
SHEET    1 AA8 2 VAL C 178  GLY C 181  0                                        
SHEET    2 AA8 2 ILE C 208  THR C 211  1  O  LEU C 209   N  VAL C 178           
SHEET    1 AA9 6 VAL C 395  ILE C 397  0                                        
SHEET    2 AA9 6 HIS C 363  TYR C 367  1  N  ILE C 366   O  THR C 396           
SHEET    3 AA9 6 LYS C 330  LEU C 334  1  N  ILE C 333   O  HIS C 365           
SHEET    4 AA9 6 ALA C 410  ILE C 413  1  O  VAL C 412   N  LEU C 334           
SHEET    5 AA9 6 PHE C 437  ASP C 440  1  O  PHE C 439   N  VAL C 411           
SHEET    6 AA9 6 GLN C 458  THR C 461  1  O  GLU C 460   N  ASP C 440           
SHEET    1 AB1 6 LEU D  69  SER D  72  0                                        
SHEET    2 AB1 6 ARG D  31  VAL D  35  1  N  VAL D  34   O  PHE D  70           
SHEET    3 AB1 6 LYS D   6  ILE D  10  1  N  ILE D   7   O  ARG D  31           
SHEET    4 AB1 6 LEU D  84  ILE D  87  1  O  PHE D  86   N  CYS D   8           
SHEET    5 AB1 6 TYR D 123  GLU D 128  1  O  THR D 127   N  ILE D  87           
SHEET    6 AB1 6 ASN D 153  SER D 158  1  O  GLN D 155   N  VAL D 126           
SHEET    1 AB2 2 VAL D 178  GLY D 181  0                                        
SHEET    2 AB2 2 ILE D 208  THR D 211  1  O  LEU D 209   N  VAL D 178           
SHEET    1 AB3 6 VAL D 395  ILE D 397  0                                        
SHEET    2 AB3 6 HIS D 363  TYR D 367  1  N  ILE D 366   O  THR D 396           
SHEET    3 AB3 6 LYS D 330  LEU D 334  1  N  ILE D 333   O  TYR D 367           
SHEET    4 AB3 6 ALA D 410  ILE D 413  1  O  VAL D 412   N  ALA D 332           
SHEET    5 AB3 6 PHE D 437  ASP D 440  1  O  PHE D 439   N  VAL D 411           
SHEET    6 AB3 6 GLN D 458  THR D 461  1  O  GLU D 460   N  ASP D 440           
SHEET    1 AB4 6 LEU E  69  SER E  72  0                                        
SHEET    2 AB4 6 ARG E  31  VAL E  35  1  N  VAL E  34   O  PHE E  70           
SHEET    3 AB4 6 LYS E   6  ILE E  10  1  N  CYS E   9   O  VAL E  35           
SHEET    4 AB4 6 LEU E  84  ILE E  87  1  O  LEU E  84   N  CYS E   8           
SHEET    5 AB4 6 TYR E 123  GLU E 128  1  O  THR E 127   N  VAL E  85           
SHEET    6 AB4 6 ASN E 153  SER E 158  1  O  GLN E 155   N  VAL E 126           
SHEET    1 AB5 2 VAL E 178  GLY E 181  0                                        
SHEET    2 AB5 2 ILE E 208  THR E 211  1  O  LEU E 209   N  VAL E 178           
SHEET    1 AB6 6 VAL E 395  ILE E 397  0                                        
SHEET    2 AB6 6 HIS E 363  TYR E 367  1  N  ILE E 366   O  THR E 396           
SHEET    3 AB6 6 LYS E 330  LEU E 334  1  N  ILE E 333   O  HIS E 365           
SHEET    4 AB6 6 ALA E 410  ILE E 413  1  O  VAL E 412   N  LEU E 334           
SHEET    5 AB6 6 PHE E 437  ASP E 440  1  O  PHE E 439   N  VAL E 411           
SHEET    6 AB6 6 GLN E 458  THR E 461  1  O  GLU E 460   N  ASP E 440           
SHEET    1 AB7 6 LEU F  69  SER F  72  0                                        
SHEET    2 AB7 6 ARG F  31  VAL F  35  1  N  VAL F  34   O  PHE F  70           
SHEET    3 AB7 6 LYS F   6  ILE F  10  1  N  CYS F   9   O  VAL F  35           
SHEET    4 AB7 6 LEU F  84  ILE F  87  1  O  PHE F  86   N  CYS F   8           
SHEET    5 AB7 6 GLY F 122  GLU F 128  1  O  THR F 127   N  VAL F  85           
SHEET    6 AB7 6 LEU F 152  SER F 158  1  O  GLN F 155   N  VAL F 126           
SHEET    1 AB8 2 VAL F 178  GLY F 181  0                                        
SHEET    2 AB8 2 ILE F 208  THR F 211  1  O  LEU F 209   N  VAL F 178           
SHEET    1 AB9 6 VAL F 395  ILE F 397  0                                        
SHEET    2 AB9 6 HIS F 363  TYR F 367  1  N  LEU F 364   O  THR F 396           
SHEET    3 AB9 6 LYS F 330  LEU F 334  1  N  ILE F 333   O  TYR F 367           
SHEET    4 AB9 6 ALA F 410  ILE F 413  1  O  VAL F 412   N  LEU F 334           
SHEET    5 AB9 6 PHE F 437  ASP F 440  1  O  PHE F 439   N  VAL F 411           
SHEET    6 AB9 6 GLN F 458  THR F 461  1  O  GLU F 460   N  ILE F 438           
CISPEP   1 LYS A  434    PRO A  435          0        -1.12                     
CISPEP   2 LYS B  434    PRO B  435          0        -0.42                     
CISPEP   3 LYS C  434    PRO C  435          0        -0.02                     
CISPEP   4 LYS D  434    PRO D  435          0        -1.39                     
CISPEP   5 LYS E  434    PRO E  435          0        -1.73                     
CISPEP   6 LYS F  434    PRO F  435          0        -1.84                     
SITE     1 AC1  6 PHE A 272  GLY A 273  PHE A 277  PHE A 338                    
SITE     2 AC1  6 ARG A 442  HOH A 656                                          
SITE     1 AC2  9 GLY B 271  PHE B 272  GLY B 273  PHE B 277                    
SITE     2 AC2  9 PHE B 338  LYS B 339  ARG B 442  HOH B 601                    
SITE     3 AC2  9 HOH B 603                                                     
SITE     1 AC3  1 SER B 316                                                     
SITE     1 AC4 17 PHE C 162  LYS C 220  ASN C 224  ILE C 231                    
SITE     2 AC4 17 PHE C 265  LYS C 267  SER C 269  PHE C 272                    
SITE     3 AC4 17 GLY C 273  CYS C 276  PHE C 277  PHE C 338                    
SITE     4 AC4 17 LYS C 339  ARG C 442  HOH C 621  HOH C 710                    
SITE     5 AC4 17 ARG D 260                                                     
SITE     1 AC5  8 GLY D 271  PHE D 272  GLY D 273  PHE D 277                    
SITE     2 AC5  8 PHE D 338  ARG D 442  HOH D 602  HOH D 678                    
SITE     1 AC6  3 TRP D 417  ASP D 418  MET D 419                               
SITE     1 AC7  6 PHE E 272  GLY E 273  PHE E 338  LYS E 339                    
SITE     2 AC7  6 HOH E 624  HOH E 667                                          
SITE     1 AC8  8 GLY F 271  PHE F 272  GLY F 273  PHE F 277                    
SITE     2 AC8  8 PHE F 338  HOH F 601  HOH F 602  HOH F 701                    
CRYST1   92.350  104.590  107.710  64.82  68.35  73.72 P 1           6          
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      0.010828 -0.003162 -0.003386        0.00000                         
SCALE2      0.000000  0.009960 -0.003855        0.00000                         
SCALE3      0.000000  0.000000  0.010711        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system