1fmh

NMR SOLUTION STRUCTURE OF A DESIGNED HETERODIMERIC LEUCINE ZIPPER

Method: SOLUTION NMR Dmax: 47.1 Å Quality: REASONABLE

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

GENERAL CONTROL PROTEIN GCN4

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 249–279 Chain B; UniProt 249–279 Fragment:LEUCINE ZIPPER ACIDIC CHAIN Mutation:R249E M250V K251A D255K K256E E258A E259Q L260A L261E S262A K263E H266Q N269Q R273Q K275E K276H L277E V278C Non-standard monomer:Yes (specific site not provided by mmCIF) Fragment:LEUCINE ZIPPER BASIC CHAIN Mutation:;R249E M250V K251Q Q252A E254K D255K K256R E258Q E259A L261K S262A K263R H266A L267A E268K N269Q E270K A272Q R273A K275R K276H L277K V278C ; Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer SOLUTION NMR NMR measurement conditions:pH 5.65;310 K;Ionic strength (raw mmCIF value) 10 mM;Pressure ambient NMR sample composition:2.1 mM AB zipper; 90% H2O, 10% D2O | 90% H2O/10% 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.

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 2–32; UniProt 249–279 Author chain B; PDBConstruct 2–32; UniProt 249–279

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 1fmh

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1fmh
Deposition date deposition_date2000-08-17
Structure title titleNMR SOLUTION STRUCTURE OF A DESIGNED HETERODIMERIC LEUCINE ZIPPER
Keywords keywordsCOILED COIL, LEUCINE ZIPPER, INTER-HELICAL ION PAIRING, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier13.86
Radius of gyration Rg (electron density) rg_electron14.20
Forward intensity I(0) i0487815000.00
Molecular weight molecular_weight178380.0 kDa
Excluded volume excluded_volume220440 ų
Envelope volume envelope_volume16148 ų
Hydration-shell volume shell_volume9966 ų
Envelope diameter envelope_diameter53.2
Shell Rg shell_rg19.24
Envelope Rg envelope_rg15.54
Shape Rg shape_rg14.14
Total Rg total_rg14.47
Total atoms total_atoms25125
Residues n_residues1550
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 dmax47.1
Rg (real space) rg_real14.11
Rg uncertainty (real space) rg_real_error0.36
I(0) (real space) i0_real4.8780e+08
I(0) uncertainty (real space) i0_real_error5.3230e+06
Rg (reciprocal space) rg_reciprocal14.10
I(0) (reciprocal space) i0_reciprocal487800000.0000
Solution quality estimate total_estimate0.7143
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary11.9
Skewness Skewness skewness0.603
Kurtosis Kurtosis kurtosis-0.317
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha70970.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.624; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.410; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1fmha_
Class classk — Designed proteins
Fold Fold foldk.6 — Designed heterodimeric coiled-coil
Superfamily Superfamily superfamilyk.6.1 — Designed heterodimeric coiled-coil
Family Family familyk.6.1.1 — Designed heterodimeric coiled-coil
Domain ID domain_idd1fmhb_
Class classk — Designed proteins
Fold Fold foldk.6 — Designed heterodimeric coiled-coil
Superfamily Superfamily superfamilyk.6.1 — Designed heterodimeric coiled-coil
Family Family familyk.6.1.1 — Designed heterodimeric coiled-coil

8. Citations (3)

9. Files and Curves (10)