1dz5

The NMR structure of the 38KDa U1A protein-PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein

Method: SOLUTION NMR Dmax: 71.5 Å Quality: GOOD

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

U1 SMALL NUCLEAR RIBONUCLEOPROTEIN A

HOMO SAPIENS

UniProt P09012

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–RNA Homooligomer Protein × 2 RNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain A; UniProt 2–102 Chain B; UniProt 2–102 Fragment:RESIDUES 2-102 Mutation:YES ;PIE, RNA (5'-R(*GP*AP*GP*AP*CP*AP*UP*UP*GP*CP*AP*CP*CP* CP*GP*GP*AP*GP*UP*CP*UP*C)-3') ; × 2 SOLUTION NMR NMR measurement conditions:pH 6;300 K;Ionic strength (raw mmCIF value) 10MM PHOSPHATE BUFFER;Pressure 1 NMR sample composition:10MM PHOSPHATE BUFFER 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.

87 other PDB entries and 145 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RU1A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–101; UniProt 2–102 Author chain B; PDBConstruct 1–101; UniProt 2–102

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 1dz5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1dz5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1dz5
Deposition date deposition_date2000-02-16
Structure title titleThe NMR structure of the 38KDa U1A protein-PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein
Keywords keywordsRIBONUCLEOPROTEIN-RNA COMPLEX, POLYADENYLATION, PROTEIN PROTEIN INTERACTION, RNA PROTEIN INTERACTION; RIBONUCLEOPROTEIN/RNA
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier22.88
Radius of gyration Rg (electron density) rg_electron22.95
Forward intensity I(0) i05126220000.00
Molecular weight molecular_weight484220.0 kDa
Excluded volume excluded_volume555100 ų
Envelope volume envelope_volume95029 ų
Hydration-shell volume shell_volume30836 ų
Envelope diameter envelope_diameter80.0
Shell Rg shell_rg33.23
Envelope Rg envelope_rg25.23
Shape Rg shape_rg22.94
Total Rg total_rg23.13
Total atoms total_atoms61644
Residues n_residues3197
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 dmax71.5
Rg (real space) rg_real22.84
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real5.1260e+09
I(0) uncertainty (real space) i0_real_error6.8890e+07
Rg (reciprocal space) rg_reciprocal22.85
I(0) (reciprocal space) i0_reciprocal5126000000.0000
Solution quality estimate total_estimate0.7529
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary69.3
Skewness Skewness skewness0.202
Kurtosis Kurtosis kurtosis-0.666
Angular range angular_range— – 0.3450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3061000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.958; Stabil: 1.000; Sysdev: 0.307; Positv: 1.000; Valcen: 0.992; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1dz5a_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.58 — Ferredoxin-like
Superfamily Superfamily superfamilyd.58.7 — RNA-binding domain, RBD, aka RNA recognition motif (RRM)
Family Family familyd.58.7.1 — Canonical RBD
Domain ID domain_idd1dz5b_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.58 — Ferredoxin-like
Superfamily Superfamily superfamilyd.58.7 — RNA-binding domain, RBD, aka RNA recognition motif (RRM)
Family Family familyd.58.7.1 — Canonical RBD

CATH v4.4 (2 domains)

Domain ID domain_id1dz5A00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily330 — RRM (RNA recognition motif) domain
Domain ID domain_id1dz5B00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily330 — RRM (RNA recognition motif) domain

8. Citations (1)

9. Files and Curves (10)