2rfo

Crystral Structure of the nucleoporin Nic96

Method: X-RAY DIFFRACTION Dmax: 152.1 Å Quality: GOOD

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

Nucleoporin NIC96

Saccharomyces cerevisiae

UniProt P34077

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 189–839 Fragment:UNP residues 189-839 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;3-10% PEG3350, 0.1M BisTris pH6.5, 0.05M lithium sulfate, 3% 1,6-hexandiole, 0.01mM DTE, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.60 Å R-free 0.285
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 189–839 Fragment:UNP residues 189-839 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;3-10% PEG3350, 0.1M BisTris pH6.5, 0.05M lithium sulfate, 3% 1,6-hexandiole, 0.01mM DTE, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.60 Å R-free 0.285

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.

7 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NIC96_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–651; UniProt 189–839 Author chain B; PDBConstruct 1–651; UniProt 189–839

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 2rfo

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2rfo
Deposition date deposition_date2007-10-01
Structure title titleCrystral Structure of the nucleoporin Nic96
Keywords keywords;Alpha-alpha-superhelix, mRNA transport, Nuclear pore complex, Nucleus, Protein transport, Translocation, Transport, STRUCTURAL PROTEIN ;; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier45.19
Radius of gyration Rg (electron density) rg_electron45.46
Forward intensity I(0) i0278109000.00
Molecular weight molecular_weight140410.0 kDa
Excluded volume excluded_volume177580 ų
Envelope volume envelope_volume254350 ų
Hydration-shell volume shell_volume50470 ų
Envelope diameter envelope_diameter162.0
Shell Rg shell_rg44.91
Envelope Rg envelope_rg45.91
Shape Rg shape_rg45.38
Total Rg total_rg45.71
Total atoms total_atoms9896
Residues n_residues1221
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 dmax152.1
Rg (real space) rg_real45.57
Rg uncertainty (real space) rg_real_error1.82
I(0) (real space) i0_real2.7810e+08
I(0) uncertainty (real space) i0_real_error5.7840e+06
Rg (reciprocal space) rg_reciprocal45.20
I(0) (reciprocal space) i0_reciprocal278000000.0000
Solution quality estimate total_estimate0.8491
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary47.8
Skewness Skewness skewness0.512
Kurtosis Kurtosis kurtosis-0.209
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16450000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.868; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.858; Smooth: 0.574

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)