6xnl

GCN4-p1 Peptide Trimer with iodo-phenylalanine residue at position 16 (IPF-F16)

Method: X-RAY DIFFRACTION Dmax: 53.6 Å Quality: REASONABLE

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

GCN4-p1 Peptide with IPF-F16

OrganismNot specified

UniProt P03069

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 homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 249–278 Chain B; UniProt 249–278 Chain C; UniProt 249–278 Mutation:IPF-F16 Non-standard monomer:Yes (specific site not provided by mmCIF) Mutation:N16A NA SODIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;Crystallization drops were prepared by mixing 2 uL of stock peptide solution with 2 uL of mother liquor and allowed to equilibrate at 298 K over a well containing 500 uL of mother liquor. The stock peptide solution (total concentration 1.5 mM) was prepared by mixing 2:1 ratios of the A16 peptide with IPF-F16 in 10 mM potassium phosphate, 100 mM potassium chloride pH 7.0. Resolution 2.20 Å R-free 0.321

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.

162 other PDB entries and 200 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GCN4_YEAST
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–30; UniProt 249–278 Author chain B; PDBConstruct 1–30; UniProt 249–278 Author chain C; PDBConstruct 1–30; UniProt 249–278

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 6xnl

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6xnl
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6xnl
Deposition date deposition_date2020-07-03
Structure title titleGCN4-p1 Peptide Trimer with iodo-phenylalanine residue at position 16 (IPF-F16)
Keywords keywordsCoil-coil, p-methylphenylalanine modified phenylalanine, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.37
Radius of gyration Rg (electron density) rg_electron14.77
Forward intensity I(0) i02344990.00
Molecular weight molecular_weight11035.0 kDa
Excluded volume excluded_volume14017 ų
Envelope volume envelope_volume15933 ų
Hydration-shell volume shell_volume9947 ų
Envelope diameter envelope_diameter53.7
Shell Rg shell_rg19.19
Envelope Rg envelope_rg15.22
Shape Rg shape_rg14.73
Total Rg total_rg15.86
Total atoms total_atoms765
Residues n_residues89
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 dmax53.6
Rg (real space) rg_real15.48
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real2.3450e+06
I(0) uncertainty (real space) i0_real_error2.6590e+04
Rg (reciprocal space) rg_reciprocal15.47
I(0) (reciprocal space) i0_reciprocal2345000.0000
Solution quality estimate total_estimate0.7295
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.6
Skewness Skewness skewness0.546
Kurtosis Kurtosis kurtosis-0.042
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha711000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.541; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.858; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)