2n45

EC-NMR Structure of Escherichia coli Maltose-binding protein Determined by Combining Evolutionary Couplings (EC) and Sparse NMR Data with a second set of RDC data simulated for an alternative alignment tensor. Northeast Structural Genomics Consortium target ER690

Method: SOLUTION NMR Dmax: 70.6 Å Quality: EXCELLENT

1. Protein Identity and Related Structures Protein Identity & Related Structures

Maltose-binding periplasmic protein

Escherichia coli

UniProt P0AEX9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 27–396 Fragment:UNP RESIDUES 27-396 No other associated polymer SOLUTION NMR mmCIF provides none of the parsed experimental conditions Resolution not provided

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

366 other PDB entries and 491 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–370; UniProt 27–396

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 2n45

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2n45
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2n45
Deposition date deposition_date2015-06-17
Structure title titleEC-NMR Structure of Escherichia coli Maltose-binding protein Determined by Combining Evolutionary Couplings (EC) and Sparse NMR Data with a second set of RDC data simulated for an alternative alignment tensor. Northeast Structural Genomics Consortium target ER690
Keywords keywords;EC-NMR, PERIPLASMIC BINDING PROTEIN, Structural Genomics, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG, PSI-Biology, PROTEIN STRUCTURE INITIATIVE ;; PERIPLASMIC BINDING PROTEIN
Experimental Method methodSOLUTION NMR

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier22.59
Radius of gyration Rg (electron density) rg_electron22.25
Forward intensity I(0) i08378630000.00
Molecular weight molecular_weight813990.0 kDa
Excluded volume excluded_volume1030700 ų
Envelope volume envelope_volume89649 ų
Hydration-shell volume shell_volume30663 ų
Envelope diameter envelope_diameter79.9
Shell Rg shell_rg31.83
Envelope Rg envelope_rg23.92
Shape Rg shape_rg22.19
Total Rg total_rg22.55
Total atoms total_atoms114680
Residues n_residues7400
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax70.6
Rg (real space) rg_real22.53
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real8.3790e+09
I(0) uncertainty (real space) i0_real_error1.0990e+08
Rg (reciprocal space) rg_reciprocal22.55
I(0) (reciprocal space) i0_reciprocal8379000000.0000
Solution quality estimate total_estimate0.9094
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.7
Skewness Skewness skewness0.251
Kurtosis Kurtosis kurtosis-0.491
Angular range angular_range— – 0.3500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4724000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.943; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.988

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2n45a_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.94 — Periplasmic binding protein-like II
Superfamily Superfamily superfamilyc.94.1 — Periplasmic binding protein-like II
Family Family familyc.94.1.1 — Phosphate binding protein-like

8. Citations (2)

9. Files and Curves (10)