1lwm

Solution Structure of the Sequence-Non-Specific HMGB protein NHP6A

Method: SOLUTION NMR Dmax: 75.1 Å Quality: GOOD

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

NONHISTONE CHROMOSOMAL PROTEIN 6A

Saccharomyces cerevisiae

UniProt P11632

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 1–93 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 5.5;293 K;Ionic strength (raw mmCIF value) 10 mM NaPO4, 100 mM NaCl;Pressure ambient NMR sample composition:1 2mM 15N-labeled NHP6A | 90% H2O, 10% D2O or 100% D2O NMR sample composition:2mM 13C/15N-labeled NHP6A | 90% H2O, 10% D2O or 100% 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NHP6A_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–93; UniProt 1–93

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 1lwm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1lwm
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1lwm
Deposition date deposition_date2002-05-31
Structure title titleSolution Structure of the Sequence-Non-Specific HMGB protein NHP6A
Keywords keywordsHMG-BOX, HMGB, ALPHA HELIX, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier19.66
Radius of gyration Rg (electron density) rg_electron19.55
Forward intensity I(0) i0670310000.00
Molecular weight molecular_weight216210.0 kDa
Excluded volume excluded_volume271010 ų
Envelope volume envelope_volume84491 ų
Hydration-shell volume shell_volume26875 ų
Envelope diameter envelope_diameter83.7
Shell Rg shell_rg33.22
Envelope Rg envelope_rg27.71
Shape Rg shape_rg19.45
Total Rg total_rg20.36
Total atoms total_atoms30780
Residues n_residues1860
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 dmax75.1
Rg (real space) rg_real19.88
Rg uncertainty (real space) rg_real_error1.04
I(0) (real space) i0_real6.7030e+08
I(0) uncertainty (real space) i0_real_error1.0040e+07
Rg (reciprocal space) rg_reciprocal19.85
I(0) (reciprocal space) i0_reciprocal670300000.0000
Solution quality estimate total_estimate0.7812
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary14.8
Skewness Skewness skewness0.426
Kurtosis Kurtosis kurtosis-0.255
Angular range angular_range— – 0.4050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha160500.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.632; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.302; Smooth: 0.954

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1lwma_
Class classa — All alpha proteins
Fold Fold folda.21 — HMG-box
Superfamily Superfamily superfamilya.21.1 — HMG-box
Family Family familya.21.1.1 — HMG-box

CATH v4.4 (1 domains)

Domain ID domain_id1lwmA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology30 — DNA Binding (I), subunit A
Homologous superfamily homologous superfamily10 — High mobility group box domain

8. Citations (1)

9. Files and Curves (10)