5day

The structure of NAP1-Related Protein(NRP1) in Arabidopsis

Method: X-RAY DIFFRACTION Dmax: 97.1 Å Quality: GOOD

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

NAP1-related protein 1

Arabidopsis thaliana

UniProt Q9CA59

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 19–225 Chain B; UniProt 19–225 Fragment:UNP RESIDUES 19-225 CA CALCIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.6;289.15 K;25% PEG 400, 0.1 M HEPES pH 7.6, 0.2 M Calcium chloride dihydrate Resolution 2.33 Å R-free 0.269

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 NRP1_ARATH
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–208; UniProt 19–225 Author chain B; PDBConstruct 2–208; UniProt 19–225

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 5day

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5day
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5day
Deposition date deposition_date2015-08-20
Structure title titleThe structure of NAP1-Related Protein(NRP1) in Arabidopsis
Keywords keywordshistone chaperone, NAP1-Related protein, transcriptional activation, CHAPERONE; CHAPERONE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.33
Radius of gyration Rg (electron density) rg_electron26.93
Forward intensity I(0) i024911700.00
Molecular weight molecular_weight40188.0 kDa
Excluded volume excluded_volume50937 ų
Envelope volume envelope_volume67840 ų
Hydration-shell volume shell_volume22409 ų
Envelope diameter envelope_diameter100.0
Shell Rg shell_rg32.60
Envelope Rg envelope_rg26.50
Shape Rg shape_rg26.89
Total Rg total_rg27.77
Total atoms total_atoms2844
Residues n_residues345
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 dmax97.1
Rg (real space) rg_real27.52
Rg uncertainty (real space) rg_real_error1.29
I(0) (real space) i0_real2.4910e+07
I(0) uncertainty (real space) i0_real_error4.4160e+05
Rg (reciprocal space) rg_reciprocal27.46
I(0) (reciprocal space) i0_reciprocal24910000.0000
Solution quality estimate total_estimate0.8499
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.1
Skewness Skewness skewness0.450
Kurtosis Kurtosis kurtosis-0.350
Angular range angular_range— – 0.2900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3455000.0000
Real-space data points n_real_points59
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.754; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.788; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd5daya1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.305 — NAP-like
Superfamily Superfamily superfamilyd.305.1 — NAP-like
Family Family familyd.305.1.0 — automated matches
Domain ID domain_idd5daya2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd5dayb1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.305 — NAP-like
Superfamily Superfamily superfamilyd.305.1 — NAP-like
Family Family familyd.305.1.0 — automated matches
Domain ID domain_idd5dayb2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id5dayA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1120 — Arylsulfatase, C-terminal domain
Homologous superfamily homologous superfamily90 — Nucleosome assembly protein
Domain ID domain_id5dayB02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1120 — Arylsulfatase, C-terminal domain
Homologous superfamily homologous superfamily90 — Nucleosome assembly protein

8. Citations (1)

9. Files and Curves (10)