#=GF ID   Tetrabrachion
#=GF AC   PF11401.12
#=GF DE   Tetrabrachion
#=GF AU   Pollington J;0000-0002-8158-8998
#=GF AU   Finn RD;0000-0001-8626-2148
#=GF SE   pdb_1fe6
#=GF GA   27.00 27.00;
#=GF TC   114.20 114.20;
#=GF NC   25.90 18.90;
#=GF BM   hmmbuild HMM.ann SEED.ann
#=GF SM   hmmsearch -E 1000 --cpu 4 -Z 75585367 HMM pfamseq
#=GF TP   Family
#=GF RN   [1]
#=GF RM   10966648
#=GF RT   Crystal structure of a naturally occurring parallel right-handed
#=GF RT   coiled coil tetramer. 
#=GF RA   Stetefeld J, Jenny M, Schulthess T, Landwehr R, Engel J,
#=GF RA   Kammerer RA; 
#=GF RL   Nat Struct Biol. 2000;7:772-776.
#=GF DR   INTERPRO; IPR021535;
#=GF DR   SO; 0100021; polypeptide_conserved_region;
#=GF CC   Tetrabrachion forms a parallel right-handed coiled coil
#=GF CC   structure with hydrophobic interactions and salt bridges forming
#=GF CC   a thermostable tetrameric structure. It contains large
#=GF CC   hydrophobic cavities. No function is known for this family of
#=GF CC   proteins [1].
#=GF SQ   1
#=GS A3DN96_STAMF/1238-1286  AC A3DN96.1
A3DN96_STAMF/1238-1286             IINETADDIVYRLTVIIDDRYESLKNLITLRADRLEMIINDNVSTILAS
#=GC seq_cons                      IINETADDIVYRLTVIIDDRYESLKNLITLRADRLEMIINDNVSTILAS
//