loop_ _nef_sequence.index _nef_sequence.chain_code _nef_sequence.sequence_code _nef_sequence.residue_name _nef_sequence.linking _nef_sequence.residue_variant _nef_sequence.cis_peptide # key: chain_code, sequence_code 1 A 13 ALA start . . 2 A 14 TRP middle . . 3 A 15 GLY middle . . 4 A 16 ASN middle . . 5 A 17 VAL middle . . 6 A 18 PHE middle . . 7 A 19 LEU middle . . 8 A 20 CYS middle -HD . 9 A 21 ALA middle . . 10 A 22 THR middle . . 11 A 23 LYS middle . . 12 A 24 ASP middle . . 13 A 24B GLN middle . . 14 A 24C GLN middle . . 15 A 24D TYR middle . . 16 A 25 HIS end -HD1,+HE2 . 17 B 17 CYS single -HD . 18 C 1 GLY cyclic . . 19 C 2 PRO middle . true 20 C 3 ASP middle . . 21 C 4 GLY middle . . 22 C 5 PRO middle . . 23 C 6 ASP cyclic . . 24 D -3 TNSR dummy . . 25 D -2 LL2 dummy . . 26 D -1 LL1 dummy . . 27 D 0 LL dummy . . 28 D 1 ALA . . . 29 D 2 CYS . -HD . 30 D 3 GLY . . . 31 D 4 CYS . -HD . 32 D 5 VAL . . . 33 D 6 CYS . -HD . 34 D 7 PHE . . . 35 D 8 CYS . -HD . 36 D 9 ASN . . . 37 E 1 ASN middle . . 38 E 2 THR middle -HG1,-OG1 . 39 E 3 ALA middle . . 40 E 4 PRO middle . . 41 E 5 ALA middle . . 42 E 6 GLU middle -OE2 . 43 E 7 SER middle . . 44 E 8 GLN middle . . 45 E 9 GLU middle . . 46 E 10 HIS middle . . 47 E 11 HIS middle . . 48 E 12 CYS middle . . 49 E 13 LYS middle . . 50 E 14 ARG middle . . 51 E 15 MOH single -HO . 52 E 16 GLC single -HO1 . 53 F 1 GLY start . . 54 F 2 ILE middle . . 55 F 3 SER middle . . 56 F 4 THR break . . 57 F 11 ASN middle . . 58 F 12 SER end . . 59 G 3 TYR middle . . 60 G 4 GLY middle . . 61 G 5 ALA middle . . stop_ # The first column (index) is a consecutive line number that does not persist # when data are re-exported. It is there only to store the order that the lines # are givn inthe file (which is significant for specifying the sequence). # # Chain A is a linear hexadecapeptide (13-25), disulfide linked to a free cysteine (chain B) # HIS 25 is protonated on NE2 rather than ND1 (and deprotonated on the C terminated carboxyl). # # Chain C is a cyclic hexapeptide, containing a cis-peptide bond at PRO 2. # # Chain D is a nonapeptide, defined with dangling ends (as might for instance be used # for CYANA). It contains two disulfide bonds, 2-6 and 4-8 - the connections are shown # in the _nef_covalent_links loop. Four additional dummy residues have been added at the # N-terminal, three linker residues and a tensor-origin residue ('TNSR'). # Note that there is NO sequential link between chains D and E, even though both have # dangling ends. Interchain links must always be given explictly in the _nef_covalent_links loop. # # Chain E has an amide bond between the backbone N of ASN 1 and the side chain carboxylate # of GLU 6, and a methyl ester cap. # # Chains F and G represent a chimeric protein, where (part of) chain G has been # inserted into chain F while maintaining the original numbering. Each chain is given as a # single block of residues, with the 'break' preceding a chain gap, and the # nef_covalent_links loop to show the additional sequential links.