2ms0

Solution NMR structure pf tRNApro:MLV-Nucleocapsid (1:2) Complex

Method: SOLUTION NMR Dmax: 100.7 Å Quality: GOOD

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

Nucleocapsid protein p10

Murine leukemia virus

UniProt P03355

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–RNA Homooligomer Protein × 2 RNA 1 PDB declaration: trimeric(3) Consistent with all polymer counts Chain A; UniProt 479–534 Chain C; UniProt 479–534 Not recorded tRNApro × 1 ZN ZINC ION × 2 SOLUTION NMR NMR measurement conditions:pH 7.2;311 K;Ionic strength (raw mmCIF value) 10mM Tris, 1mM MgCl2, 10mM NaCl;Pressure ambient NMR sample composition:0.5 mM NC-tRNApro (1:1), 0.5 mM 13C, 15N G-lab tRNA-pro NC-tRNApro (1:1), 0.5 mM 13C, 15N G-lab tRNA-pro NC-tRNApro (1:1), 90% H2O/10% D2O | 90% H2O/10% D2O 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.

44 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name POL_MLVMS
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–56; UniProt 479–534 Author chain C; PDBConstruct 1–56; UniProt 479–534

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 2ms0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2ms0
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2ms0
Deposition date deposition_date2014-07-19
Structure title titleSolution NMR structure pf tRNApro:MLV-Nucleocapsid (1:2) Complex
Keywords keywordsVIRAL PROTEIN-RNA complex, RETROVIRAL PRIMER ANNEALING, NUCLEOCAPSID CHAPERONE, PRIMER BINDING SITE; VIRAL PROTEIN/RNA
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier26.52
Radius of gyration Rg (electron density) rg_electron27.29
Forward intensity I(0) i04272060000.00
Molecular weight molecular_weight357210.0 kDa
Excluded volume excluded_volume367520 ų
Envelope volume envelope_volume207120 ų
Hydration-shell volume shell_volume52034 ų
Envelope diameter envelope_diameter117.4
Shell Rg shell_rg40.19
Envelope Rg envelope_rg32.54
Shape Rg shape_rg27.30
Total Rg total_rg27.55
Total atoms total_atoms40460
Residues n_residues1820
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 dmax100.7
Rg (real space) rg_real26.61
Rg uncertainty (real space) rg_real_error0.88
I(0) (real space) i0_real4.2720e+09
I(0) uncertainty (real space) i0_real_error6.5330e+07
Rg (reciprocal space) rg_reciprocal26.59
I(0) (reciprocal space) i0_reciprocal4272000000.0000
Solution quality estimate total_estimate0.8183
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.5
Skewness Skewness skewness0.438
Kurtosis Kurtosis kurtosis-0.208
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9154000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.649; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.687; Smooth: 1.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)