2lm0

Solution structure of the AF4-AF9 complex

Method: SOLUTION NMR Dmax: 55.0 Å Quality: REASONABLE

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

AF4/FMR2 family member 1/Protein AF-9 chimera

Homo sapiens

UniProt P42568

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 490–568 Fragment:UNP residues 738-779, UNP residues 490-568 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6;298 K;Ionic strength (raw mmCIF value) 100;Pressure ambient NMR sample composition:9.3 mM Bis-Tris, 15.8 mM MES, 100 mM sodium chloride, 1 mM DTT, 5 % D-99% D2O, 400 uM [U-100% 13C; U-100% 15N] Protein, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:15.8 mM MES, 9.3 mM Bis-Tris, 100 mM sodium chloride, 1 mM DTT, 5 % D-99% D2O, 2 mM [U-100% 13C; U-100% 15N] protein, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:9.3 mM Bis-Tris, 15.8 mM MES, 100 mM sodium chloride, 1 mM DTT, 5 % D-99% D2O, 400 uM [U-100% 13C; U-100% 15N] Protein, 3.5 % (3-acrylamidopropyl)-trimethylammonium chloride, 3.5 % acrylic acid, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:9.3 mM Bis-Tris, 15.8 mM MES, 100 mM sodium chloride, 1 mM DTT, 5 % D-99% D2O, 400 uM [U-100% 13C; U-100% 15N] Protein, 3.5 % (3-acrylamidopropyl)-trimethylammonium chloride, 3.5 % acrylamide, 95% H2O/5% D2O | 95% H2O/5% 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.

24 other PDB entries and 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AF9_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 47–125; UniProt 490–568

AF4/FMR2 family member 1/Protein AF-9 chimera

Homo sapiens

UniProt P51825

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 738–779 Fragment:UNP residues 738-779, UNP residues 490-568 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6;298 K;Ionic strength (raw mmCIF value) 100;Pressure ambient NMR sample composition:9.3 mM Bis-Tris, 15.8 mM MES, 100 mM sodium chloride, 1 mM DTT, 5 % D-99% D2O, 400 uM [U-100% 13C; U-100% 15N] Protein, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:15.8 mM MES, 9.3 mM Bis-Tris, 100 mM sodium chloride, 1 mM DTT, 5 % D-99% D2O, 2 mM [U-100% 13C; U-100% 15N] protein, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:9.3 mM Bis-Tris, 15.8 mM MES, 100 mM sodium chloride, 1 mM DTT, 5 % D-99% D2O, 400 uM [U-100% 13C; U-100% 15N] Protein, 3.5 % (3-acrylamidopropyl)-trimethylammonium chloride, 3.5 % acrylic acid, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:9.3 mM Bis-Tris, 15.8 mM MES, 100 mM sodium chloride, 1 mM DTT, 5 % D-99% D2O, 400 uM [U-100% 13C; U-100% 15N] Protein, 3.5 % (3-acrylamidopropyl)-trimethylammonium chloride, 3.5 % acrylamide, 95% H2O/5% D2O | 95% H2O/5% 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name AFF1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–43; UniProt 738–779

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 2lm0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2lm0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2lm0
Deposition date deposition_date2011-11-18
Structure title titleSolution structure of the AF4-AF9 complex
Keywords keywordsIntrinsically Disordered, NUCLEAR PROTEIN; NUCLEAR PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier19.48
Radius of gyration Rg (electron density) rg_electron19.46
Forward intensity I(0) i0291332000.00
Molecular weight molecular_weight143210.0 kDa
Excluded volume excluded_volume180370 ų
Envelope volume envelope_volume76168 ų
Hydration-shell volume shell_volume25486 ų
Envelope diameter envelope_diameter96.7
Shell Rg shell_rg32.08
Envelope Rg envelope_rg27.90
Shape Rg shape_rg19.42
Total Rg total_rg20.21
Total atoms total_atoms20500
Residues n_residues1250
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 dmax55.0
Rg (real space) rg_real18.20
Rg uncertainty (real space) rg_real_error0.12
I(0) (real space) i0_real2.7820e+08
I(0) uncertainty (real space) i0_real_error2.8820e+06
Rg (reciprocal space) rg_reciprocal19.77
I(0) (reciprocal space) i0_reciprocal291300000.0000
Solution quality estimate total_estimate0.6592
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.4
Skewness Skewness skewness0.503
Kurtosis Kurtosis kurtosis-0.072
Angular range angular_range— – 0.4100 −1
Current regularization parameter α current_alpha2.3320
Highest regularization parameter α highest_alpha1741000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.005; Oscil: 0.873; Stabil: 0.989; Sysdev: 0.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2lm0A01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1270 — Substrate Binding Domain Of Dnak; Chain:A; Domain 2
Homologous superfamily homologous superfamily290

8. Citations (1)

9. Files and Curves (10)