› 2n44

Solution NMR

EC-NMR Structure of Escherichia coli Maltose-binding protein Determined by Combining Evolutionary Couplings (EC) and Sparse NMR Data. Northeast Structural Genomics Consortium target ER690

Released:
DOI: 10.2210/pdb2n44/pdb
PDB entry 2n44 coloured by chain, ensemble of 20 models, front view.
PDB entry 2n44 coloured by chain, ensemble of 20 models, side view.
PDB entry 2n44 coloured by chain, ensemble of 20 models, top view.
Source organism: Escherichia coli K-12
Primary publication:
Protein structure determination by combining sparse NMR data with evolutionary couplings.
Tang Y, Huang YJ, Hopf TA, Sander C, Marks DS, Montelione GT
OpenAccess logo Nat Methods 12 751-4 (2015)
PMID: 26121406

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142613 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Maltose/maltodextrin-binding periplasmic protein Chain: A
Molecule details ›
Chain: A
Length: 370 amino acids
Theoretical weight: 40.75 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AEX9 (Residues: 27-396; Coverage: 100%)
Gene names: JW3994, b4034, malE
Sequence domains: Bacterial extracellular solute-binding protein

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this NMR entry.
Chemical shift assignment: 45%
Refinement method: torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Principles for Integrative Structural Biology Studies.
Rout et al. (2019)
10 more