1ysm

NMR Structure of N-terminal domain (Residues 1-77) of Siah-Interacting Protein.

Method: SOLUTION NMR Dmax: 56.4 Å Quality: REASONABLE

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

Calcyclin-binding protein

Mus musculus

UniProt Q9CXW3

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 1–77 Fragment:N-Terminal Domain No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7;303 K;Ionic strength (raw mmCIF value) 20 mM NaPi, 50 mM NaCl;Pressure 1 NMR sample composition:1 mM 15N/13C-enriched SIP(1-77), 20 mM NaPi, 50 mM NaCl | 90% H2O/10% D2O NMR sample composition:1 mM 15N-enriched SIP(1-77), 20 mM NaPi, 50 mM NaCl | 90% H2O/10% D2O NMR sample composition:1 mM U-SIP(1-77), 20 mM NaPi, 50 mM NaCl | 90% H2O/10% D2O NMR sample composition:1 mM 13C-enriched SIP(1-77), 20 mM NaPi, 50 mM NaCl | 100% D2O NMR sample composition:1 mM 10% 13C-enriched SIP(1-77), 20 mM NaPi, 50 mM NaCl | 100% D2O NMR sample composition:1 mM U-SIP(1-77), 20 mM NaPi, 50 mM NaCl | 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CYBP_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–77; UniProt 1–77

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 1ysm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1ysm
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1ysm
Deposition date deposition_date2005-02-08
Structure title titleNMR Structure of N-terminal domain (Residues 1-77) of Siah-Interacting Protein.
Keywords keywordshelix-turn-helix, Metal Binding Protein; METAL BINDING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier13.76
Radius of gyration Rg (electron density) rg_electron13.96
Forward intensity I(0) i0236243000.00
Molecular weight molecular_weight129750.0 kDa
Excluded volume excluded_volume163720 ų
Envelope volume envelope_volume24089 ų
Hydration-shell volume shell_volume12394 ų
Envelope diameter envelope_diameter61.7
Shell Rg shell_rg22.49
Envelope Rg envelope_rg18.29
Shape Rg shape_rg13.92
Total Rg total_rg14.33
Total atoms total_atoms18860
Residues n_residues1100
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 dmax56.4
Rg (real space) rg_real13.97
Rg uncertainty (real space) rg_real_error0.66
I(0) (real space) i0_real2.3620e+08
I(0) uncertainty (real space) i0_real_error3.2600e+06
Rg (reciprocal space) rg_reciprocal13.95
I(0) (reciprocal space) i0_reciprocal236200000.0000
Solution quality estimate total_estimate0.7290
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary13.6
Skewness Skewness skewness0.548
Kurtosis Kurtosis kurtosis-0.122
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha35150.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.445; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.145; Smooth: 0.994

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_idd1ysma1
Class classa — All alpha proteins
Fold Fold folda.2 — Long alpha-hairpin
Superfamily Superfamily superfamilya.2.16 — Calcyclin-binding protein-like
Family Family familya.2.16.1 — Siah interacting protein N terminal domain-like

CATH v4.4 (1 domains)

Domain ID domain_id1ysmA01
Class class4 — Few Secondary Structures
Architecture architecture10 — Irregular
Topology topology860 — DNA Excision Repair, Uvrb; Chain A
Homologous superfamily homologous superfamily10 — UVR domain

8. Citations (1)

9. Files and Curves (10)