Fix api return expected results in test 1

tests/fixtures/test_elm.json

@@ -10,13 +10,13 @@
                 "ELME000351",
                 "N-degron",
                 "The N-end rule pathway regulates protein stability by targeting proteins for ubiquitin-dependent proteasomal degradation. Polyubiquitylation of N-end rule substrates depends on their recognition by N-recognins, specific E3 ubiquitin ligases that use their conserved UBR-box and N-box domains to bind specific N-terminal protein motifs, called N-degrons, in their target proteins. N-degrons are defined by a destabilizing N-terminal residue. Type I destabilizing residues can either occur as primary destabilizing residues, which are positively charged amino acids directly recognized by N-recognins, or as secondary and tertiary destabilizing amino acids, which can be conjugated to a primary destabilizing residue. N-degrons containing type I destabilizing residues are specifically bound by the UBR-box of N-recognins. In contrast, type II destabilizing residues, which comprise bulky hydrophobic amino acids, initiate protein degradation by binding to the N-box of N-recognins.",
-                "This class of N-degrons is defined by a positively charged type I primary destabilizing Arg or Lys residue in the N-terminal position, which is recognized by the UBR-box of N-recognins. Functional N-degrons of this class are generated from pre-N-degrons either by excision of the N-terminal Met on nascent proteins or by internal cleavage of a protein (Varshavsky,2011; Tasaki,2007). However, known Met-aminopeptidases catalyzing the N-terminal Met excision were so far found to cleave N-terminal of small amino acids (Varshavsky,2011), and the Arg- or Lys-containing N-degrons identified to date are generated by internal cleavage. It is important to note that the ELM prediction tool will only return internal N-degrons if the sequence of the cleavage product is entered for analysis.Once the active N-degron is generated, the N-terminal Arg or Lys residue binds to the UBR-box of N-recognins. The UBR-box is a highly conserved region whose tertiary structure is stabilized by two zinc fingers, which form a negatively charged binding pocket that rigidly binds the positively charged N-terminal amino acid. It was shown that Arg is favored over Lys as N-terminal residue. Binding also involves a shallow hydrophobic binding pocket that interacts with the side chain of the second residue of the motif. Despite a preference for hydrophobic residues in this second position, any amino acid except Pro is allowed. In addition, the UBR-box forms hydrogen bonds with the free alpha amino group and the backbone of the first three residues (Choi,2010; Tasaki,2012). Hence, the first two residues are the main determits for specific binding to the UBR-box (3NIH; 3NII; 3NIJ; 3NIM). Recent studies showed binding of N-terminal His-containing N-degrons to the UBR-box, indicating a possible role for His as a primary type I destabilizing residue. However, compared to other primary type I interactions, this binding is very weak and naturally occurring N-degrons containing His have not yet been identified (Choi,2010).",
+                "This class of N-degrons is defined by a positively charged type I primary destabilizing Arg or Lys residue in the N-terminal position, which is recognized by the UBR-box of N-recognins. Functional N-degrons of this class are generated from pre-N-degrons either by excision of the N-terminal Met on nascent proteins or by internal cleavage of a protein (Varshavsky,2011; Tasaki,2007). However, known Met-aminopeptidases catalyzing the N-terminal Met excision were so far found to cleave N-terminal of small amino acids (Varshavsky,2011), and the Arg- or Lys-containing N-degrons identified to date are generated by internal cleavage. It is important to note that the ELM prediction tool will only return internal N-degrons if the sequence of the cleavage product is entered for analysis.Once the active N-degron is generated, the N-terminal Arg or Lys residue binds to the UBR-box of N-recognins. The UBR-box is a highly conserved region whose tertiary structure is stabilized by two zinc fingers, which form a negatively charged binding pocket that rigidly binds the positively charged N-terminal amino acid. It was shown that Arg is favored over Lys as N-terminal residue. Binding also involves a shallow hydrophobic binding pocket that interacts with the side chain of the second residue of the motif. Despite a preference for hydrophobic residues in this second position, any amino acid except Pro is allowed. In addition, the UBR-box forms hydrogen bonds with the free alpha amino group and the backbone of the first three residues (Choi,2010; Tasaki,2012). Hence, the first two residues are the main determinants for specific binding to the UBR-box (3NIH; 3NII; 3NIJ; 3NIM). Recent studies showed binding of N-terminal His-containing N-degrons to the UBR-box, indicating a possible role for His as a primary type I destabilizing residue. However, compared to other primary type I interactions, this binding is very weak and naturally occurring N-degrons containing His have not yet been identified (Choi,2010).",
                 "DEG_Nend_Nbox_1   DEG_Nend_UBRbox_1   DEG_Nend_UBRbox_2   DEG_Nend_UBRbox_3   DEG_Nend_UBRbox_4",
                 "^M{0,1}[RK][^P].",
                 "0.0002064",
                 "Eukaryota",
                 "zf-UBR (PF02207)       Putative zinc finger in N-recognin (UBR box)              (Stochiometry: 1 : 1)",
-                "KV",
+                "nan",
                 "1",
                 "3",
                 "False",