2in2

NMR Structure of the Apo Human Rhinovirus 3C Protease (serotype 14)

Method: SOLUTION NMR Dmax: 49.2 Å Quality: GOOD

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

Picornain 3C

Human rhinovirus 14

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1537–1718 Fragment:Human Rhinovirus 3C Protease No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.5;298 K;Ionic strength (raw mmCIF value) 20 mM;Pressure 1 NMR sample composition:U-13C/15N; 20mM phosphate buffer; 0.5mM EDTA; 15mM DTT; 0.3% NaN3; 90% H2O, 10% D2O | 90% H2O/10% D2O NMR sample composition:U-13C/15N; 20mM phosphate buffer; 0.5mM EDTA; 15mM DTT; NaN3; 99.6% D2O | 99.6% D2O NMR sample composition:U-15N; 20mM phosphate buffer; 0.5mM EDTA; 15mM DTT; 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.

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 1537–1718

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 2in2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2in2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2in2
Deposition date deposition_date2006-10-05
Structure title titleNMR Structure of the Apo Human Rhinovirus 3C Protease (serotype 14)
Keywords keywordsHydrolase, Protease, Beta Barrel, RNA binding, RNA polymerase binding; HYDROLASE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier15.70
Radius of gyration Rg (electron density) rg_electron15.21
Forward intensity I(0) i02205850000.00
Molecular weight molecular_weight399980.0 kDa
Excluded volume excluded_volume501460 ų
Envelope volume envelope_volume40966 ų
Hydration-shell volume shell_volume19442 ų
Envelope diameter envelope_diameter53.4
Shell Rg shell_rg23.99
Envelope Rg envelope_rg17.26
Shape Rg shape_rg15.20
Total Rg total_rg15.37
Total atoms total_atoms56660
Residues n_residues3640
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 dmax49.2
Rg (real space) rg_real15.56
Rg uncertainty (real space) rg_real_error0.28
I(0) (real space) i0_real2.2060e+09
I(0) uncertainty (real space) i0_real_error2.3170e+07
Rg (reciprocal space) rg_reciprocal15.58
I(0) (reciprocal space) i0_reciprocal2206000000.0000
Solution quality estimate total_estimate0.8835
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.4
Skewness Skewness skewness0.020
Kurtosis Kurtosis kurtosis-0.474
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1150000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.835; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2in2a_
Class classb — All beta proteins
Fold Fold foldb.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamilyb.47.1 — Trypsin-like serine proteases
Family Family familyb.47.1.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id2in2A01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id2in2A02
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)