9mni

CGRP Receptor in complex with dC2_050

Method: ELECTRON MICROSCOPY Dmax: 99.9 Å Quality: GOOD

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

Receptor activity-modifying protein 1

Homo sapiens

UniProt O60894

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 27–148 Not recorded Calcitonin gene-related peptide type 1 receptor × 1 (Q16602) De novo designed minibinder - dC2_050 × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.06 Å

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.

25 other PDB entries and 39 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAMP1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain E; PDBConstruct 28–149; UniProt 27–148

Calcitonin gene-related peptide type 1 receptor

Homo sapiens

UniProt Q16602

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain R; UniProt 22–461 Not recorded Receptor activity-modifying protein 1 × 1 (O60894) De novo designed minibinder - dC2_050 × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.06 Å

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 37 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CALRL_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain R; PDBConstruct 32–471; UniProt 22–461

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 9mni

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9mni
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9mni
Deposition date deposition_date2024-12-21
最后修订 last_revision2025-10-22
Structure title titleCGRP Receptor in complex with dC2_050
Keywords keywordsGPCR, de novo protein design, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier30.23
Radius of gyration Rg (electron density) rg_electron29.70
Forward intensity I(0) i039170900.00
Molecular weight molecular_weight50840.0 kDa
Excluded volume excluded_volume64357 ų
Envelope volume envelope_volume88662 ų
Hydration-shell volume shell_volume26906 ų
Envelope diameter envelope_diameter101.0
Shell Rg shell_rg34.60
Envelope Rg envelope_rg29.35
Shape Rg shape_rg29.73
Total Rg total_rg30.17
Total atoms total_atoms3604
Residues n_residues516
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 dmax99.9
Rg (real space) rg_real30.46
Rg uncertainty (real space) rg_real_error0.74
I(0) (real space) i0_real3.9170e+07
I(0) uncertainty (real space) i0_real_error6.2340e+05
Rg (reciprocal space) rg_reciprocal30.37
I(0) (reciprocal space) i0_reciprocal39170000.0000
Solution quality estimate total_estimate0.8512
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary26.9
Skewness Skewness skewness0.453
Kurtosis Kurtosis kurtosis-0.568
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6725000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.811; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.764; Smooth: 0.866

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)