INTERFACE RESIDUES IN THE LIGAND

B5     ASP
B6     ALA
B9     LYS
B10    ARG
B13    GLN
B14    LEU
B16    ARG
B17    TRP
B20    SER
B21    GLU
B22    THR
B24    LEU
B25    GLU
B26    PRO
B27    PRO
B28    VAL
B29    VAL
B31    ARG
B33    LYS
B34    THR
B35    LYS
B36    VAL
B37    LYS
B38    PHE
B39    ASP
B42    ALA
B43    VAL
B45    LEU
B46    ALA
B47    ALA
B50    SER
B52    ASP
B55    GLU
B70    ASN
B71    VAL
B72    ASP
B102   PRO
B104   ASN
B105   GLU
B106   GLY
B137   SER
B138   GLU
B173   GLU
B176   ILE
B177   MET
B180   ASP
B184   TRP
B192   ASP
B193   VAL
B195   HIS
B197   LYS
B198   SER
B200   GLY
B201   THR
B202   ALA
B204   HIS
B205   VAL
B208   ALA
B209   LYS
B229   ASP
B231   ASP
B233   TRP
B234   THR
B238   ALA
B241   HIS
B242   TRP
B244   LYS
B261   VAL
B262   ASN
B263   LYS
B264   VAL
B265   GLY
B266   GLN
B270   ASP
B271   VAL
B273   ASP

INTERFACE RESIDUES IN THE RECEPTOR

A21    GLY
A22    CYS
A23    ARG
A24    PRO
A70    THR
A74    ARG
A77    GLU
A167   GLU
A168   LYS
A169   ILE
A177   SER
A178   PRO
A179   ASP
A180   LEU
A181   GLN
A197   ASP
A198   THR
A199   GLY
A200   LEU
A203   ASP
A215   GLY
A216   TRP
A217   GLY
A218   GLU
A222   GLY
A223   VAL
A224   SER
A225   PHE
A230   ASP
A231   VAL
A233   SER
A234   LYS
A235   PHE
A236   LEU
A237   ASN
A238   ARG
A240   ASP
A241   LEU
A242   ASP
A243   LEU
A253   ASP
A255   TYR
A257   PHE
A260   LYS
A261   ARG
A262   GLN
A264   VAL
A279   ALA
A283   MET
A288   THR
A289   LEU
A290   MET
A291   CYS
A292   SER
A293   PHE
A295   ILE
A297   LYS
A299   SER
A300   GLU
A301   LYS
A302   LYS
A303   ALA
A304   LYS
A305   TYR
A306   GLN
A307   TYR
A308   GLY
A309   GLY