                         SEQUENCE LISTING

<110>  Centre Nationale de la Recherche Scientifique
       Universit degli Studi di Siena
       Consiglio Nazionale delle Ricerche
       BOTTA, Maurizio
       RADI, Marco
       ANGELI, Lucilla
       FREISZ, Severine
       BEC, Guillaume
       WOLFF, Philippe
       DUMAS, Philippe
       ENNIFAR, Eric
       MAGA, Giovanni
 
<120>  CRYSTAL STRUCTURE OF THE HIV-1 REVERSE TRANSCRIPTASE BOUND TO A 
       NUCLEOTIDE-COMPETITIVE REVERSE TRANSCRIPTASE INHIBITOR AND THE 
       USE THEREOF

<130>  PCT110934

<150>  US 61/288,018
<151>  2009-12-18

<160>  1     

<170>  PatentIn version 3.5

<210>  1
<211>  556
<212>  PRT
<213>  Human immunodeficiency virus type 1

<400>  1

Pro Ile Ser Pro Ile Glu Thr Val Pro Val Lys Leu Lys Pro Gly Met 
1               5                   10                  15      


Asp Gly Pro Lys Val Lys Gln Trp Pro Leu Thr Glu Glu Lys Ile Lys 
            20                  25                  30          


Ala Leu Val Glu Ile Cys Thr Glu Met Glu Lys Glu Gly Lys Ile Ser 
        35                  40                  45              


Lys Ile Gly Pro Glu Asn Pro Tyr Asn Thr Pro Val Phe Ala Ile Lys 
    50                  55                  60                  


Lys Lys Asp Ser Thr Lys Trp Arg Lys Leu Val Asp Phe Arg Glu Leu 
65                  70                  75                  80  


Asn Lys Arg Thr Gln Asp Phe Trp Glu Val Gln Leu Gly Ile Pro His 
                85                  90                  95      


Pro Ala Gly Leu Lys Lys Lys Lys Ser Val Thr Val Leu Asp Val Gly 
            100                 105                 110         


Asp Ala Tyr Phe Ser Val Pro Leu Asp Glu Asp Phe Arg Lys Tyr Thr 
        115                 120                 125             


Ala Phe Thr Ile Pro Ser Ile Asn Asn Glu Thr Pro Gly Ile Arg Tyr 
    130                 135                 140                 


Gln Tyr Asn Val Leu Pro Gln Gly Trp Lys Gly Ser Pro Ala Ile Phe 
145                 150                 155                 160 


Gln Ser Ser Met Thr Lys Ile Leu Glu Pro Phe Lys Lys Gln Asn Pro 
                165                 170                 175     


Asp Ile Val Ile Tyr Gln Tyr Met Asp Asp Leu Tyr Val Gly Ser Asp 
            180                 185                 190         


Leu Glu Ile Gly Gln His Arg Thr Lys Ile Glu Glu Leu Arg Gln His 
        195                 200                 205             


Leu Leu Arg Trp Gly Leu Thr Thr Pro Asp Lys Lys His Gln Lys Glu 
    210                 215                 220                 


Pro Pro Phe Leu Trp Met Gly Tyr Glu Leu His Pro Asp Lys Trp Thr 
225                 230                 235                 240 


Val Gln Pro Ile Val Leu Pro Glu Lys Asp Ser Trp Thr Val Asn Asp 
                245                 250                 255     


Ile Gln Lys Leu Val Gly Lys Leu Asn Trp Ala Ser Gln Ile Tyr Pro 
            260                 265                 270         


Gly Ile Lys Val Arg Gln Leu Ser Lys Leu Leu Arg Gly Thr Lys Ala 
        275                 280                 285             


Leu Thr Glu Val Ile Pro Leu Thr Glu Glu Ala Glu Leu Glu Leu Ala 
    290                 295                 300                 


Glu Asn Arg Glu Ile Leu Lys Glu Pro Val His Gly Val Tyr Tyr Asp 
305                 310                 315                 320 


Pro Ser Lys Asp Leu Ile Ala Glu Ile Gln Lys Gln Gly Gln Gly Gln 
                325                 330                 335     


Trp Thr Tyr Gln Ile Tyr Gln Glu Pro Phe Lys Asn Leu Lys Thr Gly 
            340                 345                 350         


Lys Tyr Ala Arg Met Arg Gly Ala His Thr Asn Asp Val Lys Gln Leu 
        355                 360                 365             


Thr Glu Ala Val Gln Lys Ile Thr Thr Glu Ser Ile Val Ile Trp Gly 
    370                 375                 380                 


Lys Thr Pro Lys Phe Lys Leu Pro Ile Gln Lys Glu Thr Trp Glu Thr 
385                 390                 395                 400 


Trp Trp Thr Glu Tyr Trp Gln Ala Thr Trp Ile Pro Glu Trp Glu Phe 
                405                 410                 415     


Val Asn Thr Pro Pro Leu Val Lys Leu Trp Tyr Gln Leu Glu Lys Glu 
            420                 425                 430         


Pro Ile Val Gly Ala Glu Thr Phe Tyr Val Asp Gly Ala Ala Asn Arg 
        435                 440                 445             


Glu Thr Lys Leu Gly Lys Ala Gly Tyr Val Thr Asn Lys Gly Arg Gln 
    450                 455                 460                 


Lys Val Val Pro Leu Thr Asn Thr Thr Asn Gln Lys Thr Glu Leu Gln 
465                 470                 475                 480 


Ala Ile Tyr Leu Ala Leu Gln Asp Ser Gly Leu Glu Val Asn Ile Val 
                485                 490                 495     


Thr Asp Ser Gln Tyr Ala Leu Gly Ile Ile Gln Ala Gln Pro Asp Lys 
            500                 505                 510         


Ser Glu Ser Glu Leu Val Asn Gln Ile Ile Glu Gln Leu Ile Lys Lys 
        515                 520                 525             


Glu Lys Val Tyr Leu Ala Trp Val Pro Ala His Lys Gly Ile Gly Gly 
    530                 535                 540                 


Asn Glu Gln Val Asp Lys Leu Val Ser Ala Gly Ile 
545                 550                 555     


