1ihq

GLYTM1BZIP: A CHIMERIC PEPTIDE MODEL OF THE N-TERMINUS OF A RAT SHORT ALPHA TROPOMYOSIN WITH THE N-TERMINUS ENCODED BY EXON 1B

Method: SOLUTION NMR Dmax: 43.3 Å Quality: REASONABLE

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

CHIMERIC PEPTIDE GlyTM1bZip: TROPOMYOSIN ALPHA CHAIN, BRAIN-3 and GENERAL CONTROL PROTEIN GCN4

Rattus norvegicus, Saccharomyces cerevisiae

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 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 264–281 Chain B; UniProt 264–281 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.4;281 K;Ionic strength (raw mmCIF value) 0.12 N;Pressure atmospheric NMR sample composition:1-2 mM | 100 mM NaCl, 10 mM phosphate, 10% Deuterium Oxide, pH 6.4 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.

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
Chains and sequence ranges Author chain A; PDBConstruct 21–38; UniProt 264–281 Author chain B; PDBConstruct 21–38; UniProt 264–281

CHIMERIC PEPTIDE GlyTM1bZip: TROPOMYOSIN ALPHA CHAIN, BRAIN-3 and GENERAL CONTROL PROTEIN GCN4

Rattus norvegicus, Saccharomyces cerevisiae

UniProt P18344

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 Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–20 Chain B; UniProt 2–20 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.4;281 K;Ionic strength (raw mmCIF value) 0.12 N;Pressure atmospheric NMR sample composition:1-2 mM | 100 mM NaCl, 10 mM phosphate, 10% Deuterium Oxide, pH 6.4 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 TPMZ_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–20; UniProt 2–20 Author chain B; PDBConstruct 2–20; UniProt 2–20

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 1ihq

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1ihq
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1ihq
Deposition date deposition_date2001-04-19
Structure title titleGLYTM1BZIP: A CHIMERIC PEPTIDE MODEL OF THE N-TERMINUS OF A RAT SHORT ALPHA TROPOMYOSIN WITH THE N-TERMINUS ENCODED BY EXON 1B
Keywords keywords;TROPOMYOSIN, EXON 1B, ACTIN-BINDING, THIN-FILAMENT-REGULATION, NON-MUSCLE, ALPHA-HELIX, COILED-COIL, DIMER, GCN4, CHIMERIC-PEPTIDE-MODEL, TW0-CHAINED, Structural Genomics, PSI, Protein Structure Initiative, Northeast Structural Genomics Consortium, NESG, DE NOVO PROTEIN ;; DE NOVO PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier15.89
Radius of gyration Rg (electron density) rg_electron15.74
Forward intensity I(0) i0119919000.00
Molecular weight molecular_weight86179.0 kDa
Excluded volume excluded_volume106550 ų
Envelope volume envelope_volume25671 ų
Hydration-shell volume shell_volume12459 ų
Envelope diameter envelope_diameter69.3
Shell Rg shell_rg23.45
Envelope Rg envelope_rg19.64
Shape Rg shape_rg15.69
Total Rg total_rg16.21
Total atoms total_atoms12300
Residues n_residues760
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 dmax43.3
Rg (real space) rg_real14.83
Rg uncertainty (real space) rg_real_error0.08
I(0) (real space) i0_real1.1440e+08
I(0) uncertainty (real space) i0_real_error1.0820e+06
Rg (reciprocal space) rg_reciprocal16.17
I(0) (reciprocal space) i0_reciprocal119900000.0000
Solution quality estimate total_estimate0.6728
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary14.8
Skewness Skewness skewness0.437
Kurtosis Kurtosis kurtosis-0.470
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha3.7720
Highest regularization parameter α highest_alpha134200.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.004; Oscil: 0.966; Stabil: 0.984; Sysdev: 0.000; Positv: 1.000; Valcen: 0.901; 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 (2 domains)

Domain ID domain_idd1ihqa_
Class classk — Designed proteins
Fold Fold foldk.31 — Glytm1bzip
Superfamily Superfamily superfamilyk.31.1 — Glytm1bzip
Family Family familyk.31.1.1 — Glytm1bzip
Domain ID domain_idd1ihqb_
Class classk — Designed proteins
Fold Fold foldk.31 — Glytm1bzip
Superfamily Superfamily superfamilyk.31.1 — Glytm1bzip
Family Family familyk.31.1.1 — Glytm1bzip

8. Citations (1)

9. Files and Curves (10)