Update README.md

README.md

@@ -1,3 +1,27 @@
 ---
 license: mit
+language:
+- en
+tags:
+- biology
+- protein structure
+- token classification
+widget:
+- text: "N-terminal acetylation (Nt-acetylation), carried out by N-terminal acetyltransferases (NATs), is a conserved and primary modification of nascent peptide chains. Naa60 (also named NatF) is a recently identified NAT found only in multicellular eukaryotes. This protein was shown to locate on the Golgi apparatus and mainly catalyze the Nt-acetylation of transmembrane proteins, and it also harbors lysine Nε-acetyltransferase (KAT) activity to catalyze the acetylation of lysine ε-amine. Here, we report the crystal structures of human Naa60 (hNaa60) in complex with Acetyl-Coenzyme A (Ac-CoA) or Coenzyme A (CoA). The hNaa60 protein contains an amphipathic helix following its GNAT domain that may contribute to Golgi localization of hNaa60, and the β7-β8 hairpin adopted different conformations in the hNaa60(1-242) and hNaa60(1-199) crystal structures. Remarkably, we found that the side-chain of Phe 34 can influence the position of the coenzyme, indicating a new regulatory mechanism involving enzyme, co-factor and substrates interactions. Moreover, structural comparison and biochemical studies indicated that Tyr 97 and His 138 are key residues for catalytic reaction and that a non-conserved β3-β4 long loop participates in the regulation of hNaa60 activity."
+model-index:
+- name: BiomedNLP-PubMedBERT-ProteinStructure-NER-v2.1
+  results:
+  - task:
+      name: NER
+      type: token-classification
+    metrics:
+    - name: NER Precision
+      type: precision
+      value: 
+    - name: NER Recall
+      type: recall
+      value: 
+    - name: NER F Score
+      type: f_score
+      value:
 ---