2b0f

NMR Structure of the Human Rhinovirus 3C Protease (serotype 14) with covalently bound Ace-LEALFQ-ethylpropionate inhibitor

Method: SOLUTION NMR Dmax: 50.7 Å Quality: GOOD

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

Protease 3C

rhinovirus B14

UniProt P03303

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1538–1719 Fragment:Human Rhinovirus serotype 14 3C Protease Ace-LEALFQ-ethylpropionate × 1 SOLUTION NMR NMR measurement conditions:pH 6.5;25 K;Ionic strength (raw mmCIF value) 20mM KH2PO4;Pressure ambient NMR measurement conditions:pH 6.5;25 K;Ionic strength (raw mmCIF value) 20mM KH2PO4;Pressure ambient NMR sample composition:0.75mM HRV14-3C with covalent inhibitor 20mM KH2PO4 15mM DTT 0.5mM EDTA 0.1mM DSS pH 6.5; 90% H2O, 10% D2O | 90% H2O/10% D2O NMR sample composition:0.75mM HRV14-3C with covalent inhibitor 20mM KH2PO4 15mM DTT 0.5mM EDTA 0.1mM DSS pD 6.5; 99.96% D2O | 99.96% 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.

58 other PDB entries and 240 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name POLG_HRV14
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–182; UniProt 1538–1719

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 2b0f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2b0f
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2b0f
Deposition date deposition_date2005-09-13
Structure title titleNMR Structure of the Human Rhinovirus 3C Protease (serotype 14) with covalently bound Ace-LEALFQ-ethylpropionate inhibitor
Keywords keywordsBETA BARREL, HYDROLASE-HYDROLASE INHIBITOR COMPLEX; HYDROLASE/HYDROLASE INHIBITOR
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier15.65
Radius of gyration Rg (electron density) rg_electron15.21
Forward intensity I(0) i02331280000.00
Molecular weight molecular_weight416040.0 kDa
Excluded volume excluded_volume523410 ų
Envelope volume envelope_volume39593 ų
Hydration-shell volume shell_volume19062 ų
Envelope diameter envelope_diameter54.3
Shell Rg shell_rg23.80
Envelope Rg envelope_rg17.02
Shape Rg shape_rg15.19
Total Rg total_rg15.36
Total atoms total_atoms59000
Residues n_residues3740
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 dmax50.7
Rg (real space) rg_real15.51
Rg uncertainty (real space) rg_real_error0.30
I(0) (real space) i0_real2.3310e+09
I(0) uncertainty (real space) i0_real_error2.5520e+07
Rg (reciprocal space) rg_reciprocal15.53
I(0) (reciprocal space) i0_reciprocal2331000000.0000
Solution quality estimate total_estimate0.8674
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.1
Skewness Skewness skewness0.010
Kurtosis Kurtosis kurtosis-0.468
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1313000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.763; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.989

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id2b0fA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id2b0fA02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases

8. Citations (1)

9. Files and Curves (10)