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.