PMC:7094172 / 4823-5755
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2_test
We determined the crystal structure of MERS-CoV N-NTD by molecular replacement (MR) using the structure of HCoV-OC43 N-NTD (PDB ID: 4J3K) as the search model.24 The final structure was refined to R-factor and R-free values of 0.26 and 0.29, respectively, at a resolution of 2.6 Å (Table S1). Each asymmetric unit contained four N-NTD molecules assembled into two identical dimers with an overall RMSD of 0.28 Å between the dimers (Figure S1A,B). The monomers shared a similar structural core preceded by a flexible region (Figure S1D). The core consisted of a five-stranded antiparallel β-sheet sandwiched between loops arranged in a right-handed, fist-shaped structure conserved among the CoVs.25 In our structure, however, the loop connecting strands β2 and β3 protruding out of the core into other CoV N proteins was absent. Unlike the reported structures that have a monomeric conformation, our structure was atypically dimeric.
LitCovid-PMC-OGER-BB
We determined the crystal structure of MERS-CoV N-NTD by molecular replacement (MR) using the structure of HCoV-OC43 N-NTD (PDB ID: 4J3K) as the search model.24 The final structure was refined to R-factor and R-free values of 0.26 and 0.29, respectively, at a resolution of 2.6 Å (Table S1). Each asymmetric unit contained four N-NTD molecules assembled into two identical dimers with an overall RMSD of 0.28 Å between the dimers (Figure S1A,B). The monomers shared a similar structural core preceded by a flexible region (Figure S1D). The core consisted of a five-stranded antiparallel β-sheet sandwiched between loops arranged in a right-handed, fist-shaped structure conserved among the CoVs.25 In our structure, however, the loop connecting strands β2 and β3 protruding out of the core into other CoV N proteins was absent. Unlike the reported structures that have a monomeric conformation, our structure was atypically dimeric.
LitCovid-sentences
We determined the crystal structure of MERS-CoV N-NTD by molecular replacement (MR) using the structure of HCoV-OC43 N-NTD (PDB ID: 4J3K) as the search model.24 The final structure was refined to R-factor and R-free values of 0.26 and 0.29, respectively, at a resolution of 2.6 Å (Table S1). Each asymmetric unit contained four N-NTD molecules assembled into two identical dimers with an overall RMSD of 0.28 Å between the dimers (Figure S1A,B). The monomers shared a similar structural core preceded by a flexible region (Figure S1D). The core consisted of a five-stranded antiparallel β-sheet sandwiched between loops arranged in a right-handed, fist-shaped structure conserved among the CoVs.25 In our structure, however, the loop connecting strands β2 and β3 protruding out of the core into other CoV N proteins was absent. Unlike the reported structures that have a monomeric conformation, our structure was atypically dimeric.
LitCovid-PD-FMA-UBERON
We determined the crystal structure of MERS-CoV N-NTD by molecular replacement (MR) using the structure of HCoV-OC43 N-NTD (PDB ID: 4J3K) as the search model.24 The final structure was refined to R-factor and R-free values of 0.26 and 0.29, respectively, at a resolution of 2.6 Å (Table S1). Each asymmetric unit contained four N-NTD molecules assembled into two identical dimers with an overall RMSD of 0.28 Å between the dimers (Figure S1A,B). The monomers shared a similar structural core preceded by a flexible region (Figure S1D). The core consisted of a five-stranded antiparallel β-sheet sandwiched between loops arranged in a right-handed, fist-shaped structure conserved among the CoVs.25 In our structure, however, the loop connecting strands β2 and β3 protruding out of the core into other CoV N proteins was absent. Unlike the reported structures that have a monomeric conformation, our structure was atypically dimeric.
LitCovid-PD-MONDO
We determined the crystal structure of MERS-CoV N-NTD by molecular replacement (MR) using the structure of HCoV-OC43 N-NTD (PDB ID: 4J3K) as the search model.24 The final structure was refined to R-factor and R-free values of 0.26 and 0.29, respectively, at a resolution of 2.6 Å (Table S1). Each asymmetric unit contained four N-NTD molecules assembled into two identical dimers with an overall RMSD of 0.28 Å between the dimers (Figure S1A,B). The monomers shared a similar structural core preceded by a flexible region (Figure S1D). The core consisted of a five-stranded antiparallel β-sheet sandwiched between loops arranged in a right-handed, fist-shaped structure conserved among the CoVs.25 In our structure, however, the loop connecting strands β2 and β3 protruding out of the core into other CoV N proteins was absent. Unlike the reported structures that have a monomeric conformation, our structure was atypically dimeric.
LitCovid-PubTator
We determined the crystal structure of MERS-CoV N-NTD by molecular replacement (MR) using the structure of HCoV-OC43 N-NTD (PDB ID: 4J3K) as the search model.24 The final structure was refined to R-factor and R-free values of 0.26 and 0.29, respectively, at a resolution of 2.6 Å (Table S1). Each asymmetric unit contained four N-NTD molecules assembled into two identical dimers with an overall RMSD of 0.28 Å between the dimers (Figure S1A,B). The monomers shared a similar structural core preceded by a flexible region (Figure S1D). The core consisted of a five-stranded antiparallel β-sheet sandwiched between loops arranged in a right-handed, fist-shaped structure conserved among the CoVs.25 In our structure, however, the loop connecting strands β2 and β3 protruding out of the core into other CoV N proteins was absent. Unlike the reported structures that have a monomeric conformation, our structure was atypically dimeric.
LitCovid-PD-CLO
We determined the crystal structure of MERS-CoV N-NTD by molecular replacement (MR) using the structure of HCoV-OC43 N-NTD (PDB ID: 4J3K) as the search model.24 The final structure was refined to R-factor and R-free values of 0.26 and 0.29, respectively, at a resolution of 2.6 Å (Table S1). Each asymmetric unit contained four N-NTD molecules assembled into two identical dimers with an overall RMSD of 0.28 Å between the dimers (Figure S1A,B). The monomers shared a similar structural core preceded by a flexible region (Figure S1D). The core consisted of a five-stranded antiparallel β-sheet sandwiched between loops arranged in a right-handed, fist-shaped structure conserved among the CoVs.25 In our structure, however, the loop connecting strands β2 and β3 protruding out of the core into other CoV N proteins was absent. Unlike the reported structures that have a monomeric conformation, our structure was atypically dimeric.
LitCovid-PD-CHEBI
We determined the crystal structure of MERS-CoV N-NTD by molecular replacement (MR) using the structure of HCoV-OC43 N-NTD (PDB ID: 4J3K) as the search model.24 The final structure was refined to R-factor and R-free values of 0.26 and 0.29, respectively, at a resolution of 2.6 Å (Table S1). Each asymmetric unit contained four N-NTD molecules assembled into two identical dimers with an overall RMSD of 0.28 Å between the dimers (Figure S1A,B). The monomers shared a similar structural core preceded by a flexible region (Figure S1D). The core consisted of a five-stranded antiparallel β-sheet sandwiched between loops arranged in a right-handed, fist-shaped structure conserved among the CoVs.25 In our structure, however, the loop connecting strands β2 and β3 protruding out of the core into other CoV N proteins was absent. Unlike the reported structures that have a monomeric conformation, our structure was atypically dimeric.