2krk

Solution NMR Structure of 26S protease regulatory subunit 8 from H.sapiens, Northeast Structural Genomics Consortium Target Target HR3102A

Method: SOLUTION NMR Dmax: 40.4 Å Quality: REASONABLE

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

26S protease regulatory subunit 8

Homo sapiens

UniProt P62195

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 320–395 Fragment:sequence database residues 320-395 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.5;298 K;Pressure ambient NMR sample composition:0.82 mM [U-100% 13C; U-100% 15N] HR3102A, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:0.52 mM [U-10% 13C; U-100% 15N] HR3102A, 95% H2O/5% D2O | 95% H2O/5% 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.

127 other PDB entries and 127 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRS8_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 11–86; UniProt 320–395

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 2krk

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2krk
Deposition date deposition_date2009-12-18
Structure title titleSolution NMR Structure of 26S protease regulatory subunit 8 from H.sapiens, Northeast Structural Genomics Consortium Target Target HR3102A
Keywords keywords;Structural Genomics, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG), Target HR3102A, PSI-2, Protein Structure Initiative, Acetylation, ATP-binding, Cytoplasm, Nucleotide-binding, Nucleus, Polymorphism, Proteasome, ATP-dependent degradation, PROTEIN BINDING ;; PROTEIN BINDING
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier14.80
Radius of gyration Rg (electron density) rg_electron14.22
Forward intensity I(0) i0624151000.00
Molecular weight molecular_weight195550.0 kDa
Excluded volume excluded_volume239280 ų
Envelope volume envelope_volume38140 ų
Hydration-shell volume shell_volume16716 ų
Envelope diameter envelope_diameter71.0
Shell Rg shell_rg26.05
Envelope Rg envelope_rg21.54
Shape Rg shape_rg14.25
Total Rg total_rg14.45
Total atoms total_atoms27460
Residues n_residues1720
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 dmax40.4
Rg (real space) rg_real13.86
Rg uncertainty (real space) rg_real_error0.08
I(0) (real space) i0_real5.9480e+08
I(0) uncertainty (real space) i0_real_error5.5540e+06
Rg (reciprocal space) rg_reciprocal14.98
I(0) (reciprocal space) i0_reciprocal624100000.0000
Solution quality estimate total_estimate0.6759
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary15.8
Skewness Skewness skewness0.379
Kurtosis Kurtosis kurtosis-0.211
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha3.5850
Highest regularization parameter α highest_alpha236900.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.005; Oscil: 0.943; Stabil: 0.987; Sysdev: 0.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2krkA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily60

8. Citations (1)

9. Files and Curves (10)