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Database: PDB
Entry: 6DAV
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HEADER    OXIDOREDUCTASE                          02-MAY-18   6DAV              
TITLE     CRYSTAL STRUCTURE OF HUMAN DHFR COMPLEXED WITH NADP AND               
TITLE    2 N10FORMYLTETRAHYDROFOLATE                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIHYDROFOLATE REDUCTASE;                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.5.1.3;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: DHFR;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    STRUCTURE-GUIDED DRUG DISCOVERY CONSORTIUM, DIHYDROFOLATE REDUCTASE,  
KEYWDS   2 HDHFR, NADP, OXIDOREDUCTASE                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.J.MAYCLIN,D.M.DRANOW,D.D.LORIMER                                    
REVDAT   1   16-MAY-18 6DAV    0                                                
JRNL        AUTH   S.J.MAYCLIN,D.M.DRANOW,C.WALPOLE,D.D.LORIMER                 
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN DHFR COMPLEXED WITH NADP AND      
JRNL        TITL 2 N10FORMYLTETRAHYDROFOLATE                                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.64                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 50797                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.167                           
REMARK   3   R VALUE            (WORKING SET) : 0.165                           
REMARK   3   FREE R VALUE                     : 0.204                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2028                            
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 36.6426 -  3.7342    0.97     3560   165  0.1359 0.1755        
REMARK   3     2  3.7342 -  2.9643    0.92     3433   151  0.1421 0.1677        
REMARK   3     3  2.9643 -  2.5897    0.92     3402   149  0.1650 0.2030        
REMARK   3     4  2.5897 -  2.3530    0.92     3384   163  0.1736 0.2110        
REMARK   3     5  2.3530 -  2.1844    0.93     3440   148  0.1777 0.2336        
REMARK   3     6  2.1844 -  2.0556    0.94     3480   133  0.1836 0.2519        
REMARK   3     7  2.0556 -  1.9527    0.94     3483   136  0.1785 0.2230        
REMARK   3     8  1.9527 -  1.8677    0.95     3538   137  0.1867 0.2201        
REMARK   3     9  1.8677 -  1.7958    0.95     3545   139  0.1870 0.2425        
REMARK   3    10  1.7958 -  1.7338    0.95     3513   152  0.2065 0.2566        
REMARK   3    11  1.7338 -  1.6796    0.95     3480   133  0.2195 0.3076        
REMARK   3    12  1.6796 -  1.6316    0.94     3550   126  0.2298 0.3251        
REMARK   3    13  1.6316 -  1.5886    0.94     3499   150  0.2553 0.2678        
REMARK   3    14  1.5886 -  1.5499    0.94     3462   146  0.2647 0.2769        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.170            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.200           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 21.34                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.18                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 15                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 28 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.0216  11.1841  22.9352              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1258 T22:   0.1586                                     
REMARK   3      T33:   0.1438 T12:  -0.0217                                     
REMARK   3      T13:   0.0159 T23:   0.0015                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0313 L22:   4.3523                                     
REMARK   3      L33:   2.8644 L12:  -1.7708                                     
REMARK   3      L13:   1.6342 L23:  -0.1325                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1174 S12:   0.0072 S13:   0.0159                       
REMARK   3      S21:   0.0816 S22:   0.1356 S23:   0.1213                       
REMARK   3      S31:   0.0577 S32:   0.2348 S33:   0.0071                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 29 THROUGH 40 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.0391   2.3441  14.4184              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2930 T22:   0.1714                                     
REMARK   3      T33:   0.2681 T12:  -0.0135                                     
REMARK   3      T13:   0.0046 T23:  -0.0447                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2076 L22:   5.8998                                     
REMARK   3      L33:   7.4793 L12:  -1.3074                                     
REMARK   3      L13:   3.0929 L23:  -6.3104                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1076 S12:   0.1857 S13:  -0.5417                       
REMARK   3      S21:  -0.4156 S22:   0.0655 S23:   0.1185                       
REMARK   3      S31:   0.7954 S32:   0.0508 S33:  -0.2156                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 41 THROUGH 76 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   2.2015  12.1973   7.9925              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1744 T22:   0.1595                                     
REMARK   3      T33:   0.1204 T12:  -0.0223                                     
REMARK   3      T13:   0.0274 T23:   0.0019                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6941 L22:   3.4830                                     
REMARK   3      L33:   3.9282 L12:   0.4335                                     
REMARK   3      L13:   1.4598 L23:  -0.0124                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0611 S12:   0.2019 S13:  -0.1422                       
REMARK   3      S21:  -0.2659 S22:   0.0638 S23:  -0.0252                       
REMARK   3      S31:   0.2067 S32:   0.0747 S33:  -0.0107                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 77 THROUGH 88 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   9.9952  22.7829   7.0979              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3129 T22:   0.2922                                     
REMARK   3      T33:   0.2521 T12:  -0.0580                                     
REMARK   3      T13:   0.0018 T23:   0.0711                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.7752 L22:   1.0318                                     
REMARK   3      L33:   2.1487 L12:   1.1864                                     
REMARK   3      L13:  -1.6790 L23:  -1.4886                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0469 S12:   0.1944 S13:   0.4320                       
REMARK   3      S21:  -0.2649 S22:   0.1328 S23:  -0.2795                       
REMARK   3      S31:  -0.2627 S32:   0.6558 S33:  -0.1416                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 89 THROUGH 112 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.4955  22.0998   2.0169              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3228 T22:   0.2486                                     
REMARK   3      T33:   0.2676 T12:  -0.0365                                     
REMARK   3      T13:  -0.0227 T23:   0.0616                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9151 L22:   4.1950                                     
REMARK   3      L33:   2.3802 L12:   2.5671                                     
REMARK   3      L13:   1.6908 L23:   0.8254                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2314 S12:   0.2966 S13:   0.2338                       
REMARK   3      S21:  -0.4681 S22:   0.1766 S23:   0.3865                       
REMARK   3      S31:  -0.0391 S32:  -0.0327 S33:   0.0672                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 113 THROUGH 127 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.0675  20.0995  17.1198              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1426 T22:   0.1617                                     
REMARK   3      T33:   0.2755 T12:  -0.0303                                     
REMARK   3      T13:   0.0120 T23:  -0.0021                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2990 L22:   8.9763                                     
REMARK   3      L33:   9.3996 L12:   1.1702                                     
REMARK   3      L13:   2.7101 L23:   4.4559                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1781 S12:  -0.0195 S13:   0.5632                       
REMARK   3      S21:  -0.2910 S22:   0.0370 S23:   0.7620                       
REMARK   3      S31:  -0.3534 S32:   0.0016 S33:   0.0543                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 128 THROUGH 139 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -11.3962  14.3568  19.0543              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1546 T22:   0.1725                                     
REMARK   3      T33:   0.2942 T12:  -0.0437                                     
REMARK   3      T13:  -0.0147 T23:   0.0353                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.9662 L22:   5.8090                                     
REMARK   3      L33:   7.0423 L12:  -4.1042                                     
REMARK   3      L13:   2.6490 L23:  -1.7803                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0050 S12:   0.2379 S13:   0.5091                       
REMARK   3      S21:  -0.1972 S22:  -0.1440 S23:   0.1161                       
REMARK   3      S31:  -0.2353 S32:   0.0542 S33:   0.1999                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 140 THROUGH 149 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   0.7438  11.8964  30.9502              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2305 T22:   0.3030                                     
REMARK   3      T33:   0.1946 T12:   0.0303                                     
REMARK   3      T13:   0.0097 T23:  -0.0292                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7541 L22:   3.4595                                     
REMARK   3      L33:   4.6001 L12:   1.9571                                     
REMARK   3      L13:  -1.7679 L23:  -3.8910                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1060 S12:  -0.4440 S13:  -0.0861                       
REMARK   3      S21:   0.4776 S22:  -0.0868 S23:  -0.1224                       
REMARK   3      S31:  -0.0698 S32:   0.2091 S33:  -0.0060                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 150 THROUGH 159 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -16.5748  18.4041  25.6760              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1792 T22:   0.2826                                     
REMARK   3      T33:   0.2707 T12:   0.0501                                     
REMARK   3      T13:   0.0338 T23:  -0.0057                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9698 L22:   9.1364                                     
REMARK   3      L33:   8.9239 L12:   3.5634                                     
REMARK   3      L13:   3.4773 L23:   0.6805                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2378 S12:  -0.6842 S13:   0.4238                       
REMARK   3      S21:   0.3012 S22:  -0.0243 S23:   0.4663                       
REMARK   3      S31:  -0.0625 S32:  -0.7595 S33:   0.2074                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 160 THROUGH 187 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -12.1879   4.5729  22.0911              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2153 T22:   0.1804                                     
REMARK   3      T33:   0.2442 T12:  -0.0480                                     
REMARK   3      T13:   0.0101 T23:   0.0378                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6889 L22:   3.9227                                     
REMARK   3      L33:   3.2243 L12:  -3.2045                                     
REMARK   3      L13:   2.7710 L23:  -1.3362                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0364 S12:  -0.2370 S13:  -0.3252                       
REMARK   3      S21:  -0.1698 S22:   0.2075 S23:   0.4141                       
REMARK   3      S31:   0.2096 S32:  -0.2728 S33:  -0.2114                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 28 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -14.5374  29.7770  44.3435              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1422 T22:   0.1377                                     
REMARK   3      T33:   0.1205 T12:   0.0275                                     
REMARK   3      T13:   0.0253 T23:  -0.0057                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7476 L22:   2.5934                                     
REMARK   3      L33:   4.4054 L12:  -0.5686                                     
REMARK   3      L13:   1.9438 L23:   0.1432                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0392 S12:  -0.0876 S13:  -0.0217                       
REMARK   3      S21:  -0.0206 S22:   0.1691 S23:   0.0955                       
REMARK   3      S31:   0.1068 S32:   0.2026 S33:  -0.1156                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 29 THROUGH 60 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -14.0469  17.5778  48.6084              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3152 T22:   0.1894                                     
REMARK   3      T33:   0.2089 T12:   0.0644                                     
REMARK   3      T13:  -0.0434 T23:  -0.0072                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6966 L22:   1.9553                                     
REMARK   3      L33:   2.9943 L12:  -0.1313                                     
REMARK   3      L13:   0.2601 L23:  -1.4198                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0206 S12:  -0.1484 S13:  -0.2070                       
REMARK   3      S21:  -0.0116 S22:   0.1305 S23:   0.0046                       
REMARK   3      S31:   0.7517 S32:   0.2911 S33:  -0.1326                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 61 THROUGH 101 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -20.5325  19.4735  59.0212              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2347 T22:   0.1696                                     
REMARK   3      T33:   0.2069 T12:  -0.0314                                     
REMARK   3      T13:   0.0157 T23:   0.0652                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0022 L22:   3.6543                                     
REMARK   3      L33:   6.6641 L12:   0.1302                                     
REMARK   3      L13:   0.6723 L23:  -0.5207                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0866 S12:  -0.2620 S13:  -0.2573                       
REMARK   3      S21:  -0.0064 S22:   0.1071 S23:   0.3833                       
REMARK   3      S31:   0.2852 S32:  -0.4057 S33:  -0.1715                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 102 THROUGH 118 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.0711  14.6488  59.4735              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3153 T22:   0.2795                                     
REMARK   3      T33:   0.2188 T12:   0.0443                                     
REMARK   3      T13:   0.0027 T23:  -0.0143                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7323 L22:   3.0965                                     
REMARK   3      L33:   3.1682 L12:  -2.2271                                     
REMARK   3      L13:   1.5525 L23:   0.3990                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3514 S12:  -0.0002 S13:  -0.2476                       
REMARK   3      S21:  -0.3216 S22:  -0.1482 S23:   0.2436                       
REMARK   3      S31:   0.9534 S32:   0.3915 S33:  -0.0414                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 119 THROUGH 187 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.9246  29.6898  44.9781              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1689 T22:   0.2361                                     
REMARK   3      T33:   0.1952 T12:  -0.0211                                     
REMARK   3      T13:   0.0141 T23:  -0.0001                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7303 L22:   2.2292                                     
REMARK   3      L33:   4.1667 L12:  -1.5018                                     
REMARK   3      L13:  -0.6333 L23:   0.1828                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0190 S12:  -0.2415 S13:   0.1365                       
REMARK   3      S21:   0.1225 S22:   0.0659 S23:  -0.1992                       
REMARK   3      S31:   0.0544 S32:   0.6693 S33:  -0.0568                       
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 6DAV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAY-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000234256.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-JAN-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CLSI                               
REMARK 200  BEAMLINE                       : 08ID-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979490                           
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50838                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY                : 2.309                              
REMARK 200  R MERGE                    (I) : 0.03100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.4200                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.34                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.110                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: WIZARD 3/4 H10 (296175H10): 100 MM       
REMARK 280  TRIS BASE/ HYDROCHLORIC ACID PH 8.5, 30% (W/V) PEG3350, 30% (V/V)   
REMARK 280  2-PROPANOL, PROTEIN CONC. 28.74 MG/ML, PROTEIN BATCH ID XP819,      
REMARK 280  10 MM NADP, 3.75 MM BSI108214, SEEDED FROM 293949G10,               
REMARK 280  CRYOPROTECTED WITH 20% EG, PUCK IZS6-6, VAPOR DIFFUSION, SITTING    
REMARK 280  DROP, TEMPERATURE 290K                                              
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, 2                                                    
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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     MET B     1                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  45    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  81    CG   CD   CE   NZ                                   
REMARK 470     ARG B  29    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  45    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 151    CG   CD   OE1  OE2                                  
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    ASP A 111      -94.53    -97.84                                   
REMARK 500    ASP B 111      -92.84    -96.69                                   
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 NAP A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue G3V A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAP B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue G3V B 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 204                 
DBREF  6DAV A    1   187  UNP    P00374   DYR_HUMAN        1    187             
DBREF  6DAV B    1   187  UNP    P00374   DYR_HUMAN        1    187             
SEQRES   1 A  187  MET VAL GLY SER LEU ASN CYS ILE VAL ALA VAL SER GLN          
SEQRES   2 A  187  ASN MET GLY ILE GLY LYS ASN GLY ASP LEU PRO TRP PRO          
SEQRES   3 A  187  PRO LEU ARG ASN GLU PHE ARG TYR PHE GLN ARG MET THR          
SEQRES   4 A  187  THR THR SER SER VAL GLU GLY LYS GLN ASN LEU VAL ILE          
SEQRES   5 A  187  MET GLY LYS LYS THR TRP PHE SER ILE PRO GLU LYS ASN          
SEQRES   6 A  187  ARG PRO LEU LYS GLY ARG ILE ASN LEU VAL LEU SER ARG          
SEQRES   7 A  187  GLU LEU LYS GLU PRO PRO GLN GLY ALA HIS PHE LEU SER          
SEQRES   8 A  187  ARG SER LEU ASP ASP ALA LEU LYS LEU THR GLU GLN PRO          
SEQRES   9 A  187  GLU LEU ALA ASN LYS VAL ASP MET VAL TRP ILE VAL GLY          
SEQRES  10 A  187  GLY SER SER VAL TYR LYS GLU ALA MET ASN HIS PRO GLY          
SEQRES  11 A  187  HIS LEU LYS LEU PHE VAL THR ARG ILE MET GLN ASP PHE          
SEQRES  12 A  187  GLU SER ASP THR PHE PHE PRO GLU ILE ASP LEU GLU LYS          
SEQRES  13 A  187  TYR LYS LEU LEU PRO GLU TYR PRO GLY VAL LEU SER ASP          
SEQRES  14 A  187  VAL GLN GLU GLU LYS GLY ILE LYS TYR LYS PHE GLU VAL          
SEQRES  15 A  187  TYR GLU LYS ASN ASP                                          
SEQRES   1 B  187  MET VAL GLY SER LEU ASN CYS ILE VAL ALA VAL SER GLN          
SEQRES   2 B  187  ASN MET GLY ILE GLY LYS ASN GLY ASP LEU PRO TRP PRO          
SEQRES   3 B  187  PRO LEU ARG ASN GLU PHE ARG TYR PHE GLN ARG MET THR          
SEQRES   4 B  187  THR THR SER SER VAL GLU GLY LYS GLN ASN LEU VAL ILE          
SEQRES   5 B  187  MET GLY LYS LYS THR TRP PHE SER ILE PRO GLU LYS ASN          
SEQRES   6 B  187  ARG PRO LEU LYS GLY ARG ILE ASN LEU VAL LEU SER ARG          
SEQRES   7 B  187  GLU LEU LYS GLU PRO PRO GLN GLY ALA HIS PHE LEU SER          
SEQRES   8 B  187  ARG SER LEU ASP ASP ALA LEU LYS LEU THR GLU GLN PRO          
SEQRES   9 B  187  GLU LEU ALA ASN LYS VAL ASP MET VAL TRP ILE VAL GLY          
SEQRES  10 B  187  GLY SER SER VAL TYR LYS GLU ALA MET ASN HIS PRO GLY          
SEQRES  11 B  187  HIS LEU LYS LEU PHE VAL THR ARG ILE MET GLN ASP PHE          
SEQRES  12 B  187  GLU SER ASP THR PHE PHE PRO GLU ILE ASP LEU GLU LYS          
SEQRES  13 B  187  TYR LYS LEU LEU PRO GLU TYR PRO GLY VAL LEU SER ASP          
SEQRES  14 B  187  VAL GLN GLU GLU LYS GLY ILE LYS TYR LYS PHE GLU VAL          
SEQRES  15 B  187  TYR GLU LYS ASN ASP                                          
HET    NAP  A 201      48                                                       
HET    G3V  A 202      34                                                       
HET    EDO  A 203       4                                                       
HET    NAP  B 201      48                                                       
HET    G3V  B 202      34                                                       
HET    EDO  B 203       4                                                       
HET    EDO  B 204       4                                                       
HETNAM     NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE                 
HETNAM     G3V N-(4-{[(2,4-DIAMINOPTERIDIN-6-YL)                                
HETNAM   2 G3V  METHYL](HYDROXYMETHYL)AMINO}BENZENE-1-CARBONYL)-L-              
HETNAM   3 G3V  GLUTAMIC ACID                                                   
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE                       
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  NAP    2(C21 H28 N7 O17 P3)                                         
FORMUL   4  G3V    2(C20 H22 N8 O6)                                             
FORMUL   5  EDO    3(C2 H6 O2)                                                  
FORMUL  10  HOH   *328(H2 O)                                                    
HELIX    1 AA1 LEU A   28  THR A   41  1                                  14    
HELIX    2 AA2 LYS A   55  ILE A   61  1                                   7    
HELIX    3 AA3 PRO A   62  ARG A   66  5                                   5    
HELIX    4 AA4 SER A   93  GLU A  102  1                                  10    
HELIX    5 AA5 GLN A  103  ASN A  108  1                                   6    
HELIX    6 AA6 GLY A  118  ASN A  127  1                                  10    
HELIX    7 AA7 LEU B   28  THR B   41  1                                  14    
HELIX    8 AA8 LYS B   55  PHE B   59  1                                   5    
HELIX    9 AA9 SER B   60  ILE B   61  5                                   2    
HELIX   10 AB1 PRO B   62  ARG B   66  5                                   5    
HELIX   11 AB2 SER B   93  GLU B  102  1                                  10    
HELIX   12 AB3 GLN B  103  ASN B  108  1                                   6    
HELIX   13 AB4 GLY B  118  ASN B  127  1                                  10    
SHEET    1 AA1 8 PHE A  89  SER A  91  0                                        
SHEET    2 AA1 8 ARG A  71  LEU A  76  1  N  VAL A  75   O  PHE A  89           
SHEET    3 AA1 8 GLN A  48  GLY A  54  1  N  VAL A  51   O  ILE A  72           
SHEET    4 AA1 8 VAL A 110  ILE A 115  1  O  TRP A 114   N  LEU A  50           
SHEET    5 AA1 8 LEU A   5  SER A  12  1  N  ASN A   6   O  ILE A 115           
SHEET    6 AA1 8 HIS A 131  ILE A 139  1  O  PHE A 135   N  CYS A   7           
SHEET    7 AA1 8 ILE A 176  ASN A 186 -1  O  LYS A 179   N  ARG A 138           
SHEET    8 AA1 8 LYS A 158  LEU A 159 -1  N  LYS A 158   O  GLU A 184           
SHEET    1 AA2 8 PHE A  89  SER A  91  0                                        
SHEET    2 AA2 8 ARG A  71  LEU A  76  1  N  VAL A  75   O  PHE A  89           
SHEET    3 AA2 8 GLN A  48  GLY A  54  1  N  VAL A  51   O  ILE A  72           
SHEET    4 AA2 8 VAL A 110  ILE A 115  1  O  TRP A 114   N  LEU A  50           
SHEET    5 AA2 8 LEU A   5  SER A  12  1  N  ASN A   6   O  ILE A 115           
SHEET    6 AA2 8 HIS A 131  ILE A 139  1  O  PHE A 135   N  CYS A   7           
SHEET    7 AA2 8 ILE A 176  ASN A 186 -1  O  LYS A 179   N  ARG A 138           
SHEET    8 AA2 8 GLN A 171  GLU A 173 -1  N  GLN A 171   O  TYR A 178           
SHEET    1 AA3 2 GLY A  16  GLY A  18  0                                        
SHEET    2 AA3 2 THR A 147  PHE A 148 -1  O  THR A 147   N  ILE A  17           
SHEET    1 AA4 8 PHE B  89  SER B  91  0                                        
SHEET    2 AA4 8 ARG B  71  LEU B  76  1  N  VAL B  75   O  PHE B  89           
SHEET    3 AA4 8 GLN B  48  GLY B  54  1  N  VAL B  51   O  ILE B  72           
SHEET    4 AA4 8 VAL B 110  ILE B 115  1  O  TRP B 114   N  LEU B  50           
SHEET    5 AA4 8 LEU B   5  VAL B  11  1  N  ASN B   6   O  ILE B 115           
SHEET    6 AA4 8 HIS B 131  ILE B 139  1  O  PHE B 135   N  CYS B   7           
SHEET    7 AA4 8 ILE B 176  ASN B 186 -1  O  LYS B 179   N  ARG B 138           
SHEET    8 AA4 8 LYS B 158  LEU B 159 -1  N  LYS B 158   O  GLU B 184           
SHEET    1 AA5 8 PHE B  89  SER B  91  0                                        
SHEET    2 AA5 8 ARG B  71  LEU B  76  1  N  VAL B  75   O  PHE B  89           
SHEET    3 AA5 8 GLN B  48  GLY B  54  1  N  VAL B  51   O  ILE B  72           
SHEET    4 AA5 8 VAL B 110  ILE B 115  1  O  TRP B 114   N  LEU B  50           
SHEET    5 AA5 8 LEU B   5  VAL B  11  1  N  ASN B   6   O  ILE B 115           
SHEET    6 AA5 8 HIS B 131  ILE B 139  1  O  PHE B 135   N  CYS B   7           
SHEET    7 AA5 8 ILE B 176  ASN B 186 -1  O  LYS B 179   N  ARG B 138           
SHEET    8 AA5 8 GLN B 171  GLU B 173 -1  N  GLN B 171   O  TYR B 178           
SHEET    1 AA6 2 GLY B  16  GLY B  18  0                                        
SHEET    2 AA6 2 THR B 147  PHE B 148 -1  O  THR B 147   N  ILE B  17           
CISPEP   1 ARG A   66    PRO A   67          0        -7.35                     
CISPEP   2 GLY A  117    GLY A  118          0         5.03                     
CISPEP   3 ARG B   66    PRO B   67          0        -7.33                     
CISPEP   4 GLY B  117    GLY B  118          0         4.54                     
SITE     1 AC1 36 VAL A   9  ALA A  10  ILE A  17  GLY A  18                    
SITE     2 AC1 36 GLY A  21  ASP A  22  LEU A  23  GLY A  54                    
SITE     3 AC1 36 LYS A  55  LYS A  56  THR A  57  SER A  60                    
SITE     4 AC1 36 LEU A  76  SER A  77  ARG A  78  GLU A  79                    
SITE     5 AC1 36 ARG A  92  SER A  93  VAL A 116  GLY A 118                    
SITE     6 AC1 36 SER A 119  SER A 120  VAL A 121  TYR A 122                    
SITE     7 AC1 36 GLU A 124  THR A 147  G3V A 202  HOH A 307                    
SITE     8 AC1 36 HOH A 316  HOH A 319  HOH A 325  HOH A 337                    
SITE     9 AC1 36 HOH A 343  HOH A 347  HOH A 357  HOH A 364                    
SITE     1 AC2 19 ILE A   8  VAL A   9  ALA A  10  LEU A  23                    
SITE     2 AC2 19 GLU A  31  PHE A  32  PHE A  35  GLN A  36                    
SITE     3 AC2 19 SER A  60  ILE A  61  ASN A  65  LEU A  68                    
SITE     4 AC2 19 ARG A  71  VAL A 116  THR A 137  NAP A 201                    
SITE     5 AC2 19 HOH A 338  HOH A 346  HOH A 390                               
SITE     1 AC3  6 LEU A 160  VAL A 166  SER A 168  PHE A 180                    
SITE     2 AC3  6 GLU A 181  VAL A 182                                          
SITE     1 AC4 34 VAL B   9  ALA B  10  ILE B  17  GLY B  18                    
SITE     2 AC4 34 GLY B  21  ASP B  22  LEU B  23  GLY B  54                    
SITE     3 AC4 34 LYS B  55  LYS B  56  THR B  57  SER B  60                    
SITE     4 AC4 34 LEU B  76  SER B  77  ARG B  78  GLU B  79                    
SITE     5 AC4 34 ARG B  92  SER B  93  VAL B 116  GLY B 118                    
SITE     6 AC4 34 SER B 119  SER B 120  VAL B 121  TYR B 122                    
SITE     7 AC4 34 GLU B 124  THR B 147  G3V B 202  HOH B 309                    
SITE     8 AC4 34 HOH B 318  HOH B 322  HOH B 328  HOH B 349                    
SITE     9 AC4 34 HOH B 357  HOH B 382                                          
SITE     1 AC5 17 ILE B   8  VAL B   9  ALA B  10  LEU B  23                    
SITE     2 AC5 17 GLU B  31  PHE B  32  PHE B  35  GLN B  36                    
SITE     3 AC5 17 SER B  60  ASN B  65  LEU B  68  ARG B  71                    
SITE     4 AC5 17 VAL B 116  NAP B 201  HOH B 351  HOH B 388                    
SITE     5 AC5 17 HOH B 408                                                     
SITE     1 AC6  5 LEU B 160  VAL B 166  PHE B 180  GLU B 181                    
SITE     2 AC6  5 VAL B 182                                                     
SITE     1 AC7  7 LEU B  80  LYS B  81  GLU B  82  PRO B  83                    
SITE     2 AC7  7 PRO B  84  HOH B 308  HOH B 383                               
CRYST1   37.090   42.740   72.290  91.05 101.88 120.00 P 1           2          
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      0.026961  0.015569  0.007977        0.00000                         
SCALE2      0.000000  0.027018  0.003902        0.00000                         
SCALE3      0.000000  0.000000  0.014282        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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