1enw

ELONGATION FACTOR TFIIS DOMAIN II

Method: SOLUTION NMR Dmax: 50.9 Å Quality: REASONABLE

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

TRANSCRIPTION ELONGATION FACTOR S-II

Saccharomyces cerevisiae

UniProt P07273

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 131–240 Fragment:DOMAIN II (RESIDUES 131-240) No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.5;270 K;Ionic strength (raw mmCIF value) 50 mM;Pressure ambient NMR sample composition:2 mM TFIIS; 5mM phosphate buffer; 90% H2O, 10% D2O | 90% H2O/10% D2O NMR sample composition:2 mM TFIIS; 5mM phosphate buffer; 99.996% D2O | 99.996% 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.

13 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TFS2_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–114; UniProt 131–240

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 1enw

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1enw
Deposition date deposition_date2000-03-21
Structure title titleELONGATION FACTOR TFIIS DOMAIN II
Keywords keywordshelix-bundle, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier18.99
Radius of gyration Rg (electron density) rg_electron18.63
Forward intensity I(0) i0985926000.00
Molecular weight molecular_weight254190.0 kDa
Excluded volume excluded_volume314610 ų
Envelope volume envelope_volume95751 ų
Hydration-shell volume shell_volume29886 ų
Envelope diameter envelope_diameter93.9
Shell Rg shell_rg34.15
Envelope Rg envelope_rg27.75
Shape Rg shape_rg18.62
Total Rg total_rg19.18
Total atoms total_atoms34850
Residues n_residues2280
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 dmax50.9
Rg (real space) rg_real17.62
Rg uncertainty (real space) rg_real_error0.10
I(0) (real space) i0_real9.3720e+08
I(0) uncertainty (real space) i0_real_error9.1620e+06
Rg (reciprocal space) rg_reciprocal19.27
I(0) (reciprocal space) i0_reciprocal985900000.0000
Solution quality estimate total_estimate0.6820
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary17.7
Skewness Skewness skewness0.379
Kurtosis Kurtosis kurtosis-0.439
Angular range angular_range— – 0.4200 −1
Current regularization parameter α current_alpha2.8420
Highest regularization parameter α highest_alpha809900.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.006; Oscil: 0.968; Stabil: 0.991; Sysdev: 0.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.000

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_idd1enwa_
Class classa — All alpha proteins
Fold Fold folda.5 — RuvA C-terminal domain-like
Superfamily Superfamily superfamilya.5.4 — Elongation factor TFIIS domain 2
Family Family familya.5.4.1 — Elongation factor TFIIS domain 2

CATH v4.4 (1 domains)

Domain ID domain_id1enwA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology472 — Cyclin A; domain 1
Homologous superfamily homologous superfamily30 — Transcription elongation factor S-II, central domain

8. Citations (1)

9. Files and Curves (10)