2ro1

NMR Solution Structures of Human KAP1 PHD finger-bromodomain

Method: SOLUTION NMR Dmax: 58.5 Å Quality: GOOD

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

Transcription intermediary factor 1-beta

Homo sapiens

UniProt Q13263

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 624–812 Fragment:UNP residues 624-812 ZN ZINC ION × 2 SOLUTION NMR NMR measurement conditions:pH 6.5;303 K;Ionic strength (raw mmCIF value) 0.2;Pressure ambient NMR sample composition:0.5mM [U-100% 13C; U-100% 15N] protein, 100% D2O | 100% 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.

9 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TIF1B_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–189; UniProt 624–812

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 2ro1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2ro1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2ro1
Deposition date deposition_date2008-03-04
Structure title titleNMR Solution Structures of Human KAP1 PHD finger-bromodomain
Keywords keywords;KAP, TIF, PHD finger, Bromodomain, SUMO, Acetylation, Alternative splicing, Metal-binding, Nucleus, Phosphoprotein, Repressor, Transcription, Transcription regulation, Zinc, Zinc-finger ;; TRANSCRIPTION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier16.41
Radius of gyration Rg (electron density) rg_electron16.10
Forward intensity I(0) i02665320000.00
Molecular weight molecular_weight422830.0 kDa
Excluded volume excluded_volume522000 ų
Envelope volume envelope_volume57789 ų
Hydration-shell volume shell_volume23325 ų
Envelope diameter envelope_diameter68.7
Shell Rg shell_rg27.42
Envelope Rg envelope_rg20.83
Shape Rg shape_rg16.11
Total Rg total_rg16.21
Total atoms total_atoms58140
Residues n_residues3780
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 dmax58.5
Rg (real space) rg_real16.36
Rg uncertainty (real space) rg_real_error0.47
I(0) (real space) i0_real2.6650e+09
I(0) uncertainty (real space) i0_real_error3.4930e+07
Rg (reciprocal space) rg_reciprocal16.37
I(0) (reciprocal space) i0_reciprocal2665000000.0000
Solution quality estimate total_estimate0.7669
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary21.0
Skewness Skewness skewness0.305
Kurtosis Kurtosis kurtosis-0.087
Angular range angular_range— – 0.4850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1449000.0000
Real-space data points n_real_points79
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.662; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)