2cp6

Solution structure of the 2nd CAP-Gly domain in human CLIP-170/restin

Method: SOLUTION NMR Dmax: 84.4 Å Quality: REASONABLE

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

Restin

Homo sapiens

UniProt P30622

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 181–339 Fragment:CAP-Gly domain No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7;298 K;Ionic strength (raw mmCIF value) 120;Pressure ambient NMR sample composition:1mM protein, 20mM d-Tris-HCl, pH7.0, 100mM NaCl, 1mM d-DTT, 0.02% NaN3, 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.

8 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name REST_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 8–166; UniProt 181–339

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 2cp6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2cp6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2cp6
Deposition date deposition_date2005-05-19
Structure title titleSolution structure of the 2nd CAP-Gly domain in human CLIP-170/restin
Keywords keywords;microtubule binding, cytoskeleton associated protein, restin, structural genomics, NPPSFA, National Project on Protein Structural and Functional Analyses, RIKEN Structural Genomics/Proteomics Initiative, RSGI, PROTEIN BINDING ;; PROTEIN BINDING
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier31.50
Radius of gyration Rg (electron density) rg_electron30.81
Forward intensity I(0) i01896950000.00
Molecular weight molecular_weight351840.0 kDa
Excluded volume excluded_volume436730 ų
Envelope volume envelope_volume363860 ų
Hydration-shell volume shell_volume69912 ų
Envelope diameter envelope_diameter174.1
Shell Rg shell_rg47.24
Envelope Rg envelope_rg45.38
Shape Rg shape_rg30.74
Total Rg total_rg31.60
Total atoms total_atoms49740
Residues n_residues3440
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 dmax84.4
Rg (real space) rg_real29.04
Rg uncertainty (real space) rg_real_error0.26
I(0) (real space) i0_real1.8070e+09
I(0) uncertainty (real space) i0_real_error2.3220e+07
Rg (reciprocal space) rg_reciprocal31.92
I(0) (reciprocal space) i0_reciprocal1896000000.0000
Solution quality estimate total_estimate0.6789
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary38.8
Skewness Skewness skewness0.301
Kurtosis Kurtosis kurtosis-0.569
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha1.3790
Highest regularization parameter α highest_alpha881700.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.993; Stabil: 0.980; Sysdev: 0.000; Positv: 1.000; Valcen: 0.912; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2cp6a1
Class classb — All beta proteins
Fold Fold foldb.34 — SH3-like barrel
Superfamily Superfamily superfamilyb.34.10 — Cap-Gly domain
Family Family familyb.34.10.1 — Cap-Gly domain
Domain ID domain_idd2cp6a2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2cp6a3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id2cp6A01
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily190 — CAP Gly-rich-like domain

8. Citations (1)

9. Files and Curves (10)