4bq6

Crystal structure of the RGMB-NEO1 complex form 1

Method: X-RAY DIFFRACTION Dmax: 92.9 Å Quality: GOOD

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

NEOGENIN

MUS MUSCULUS

UniProt P97798

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 B; UniProt 883–1133 Fragment:FN-TYPE III DOMAINS 5 AND 6, RESIDUES 883-1133 RGM DOMAIN FAMILY MEMBER B × 1 (Q6NW40) RGM DOMAIN FAMILY MEMBER B × 1 (Q6NW40) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.5;0.1 M TRIS-HCL, PH 8.5 0.2 M SODIUM ACETATE 30% PEG4000 Resolution 2.30 Å R-free 0.267
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 883–1133 Fragment:FN-TYPE III DOMAINS 5 AND 6, RESIDUES 883-1133 RGM DOMAIN FAMILY MEMBER B × 1 (Q6NW40) RGM DOMAIN FAMILY MEMBER B × 1 (Q6NW40) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.5;0.1 M TRIS-HCL, PH 8.5 0.2 M SODIUM ACETATE 30% PEG4000 Resolution 2.30 Å R-free 0.267

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.

8 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NEO1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–254; UniProt 883–1133 Author chain B; PDBConstruct 4–254; UniProt 883–1133

RGM DOMAIN FAMILY MEMBER B

HOMO SAPIENS

UniProt Q6NW40

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 50–168 Chain F; UniProt 169–410 Fragment:ECTODOMAIN, RESIDUES 50-168 Fragment:ECTODOMAIN, RESIDUES 169-410 NEOGENIN × 1 (P97798) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.5;0.1 M TRIS-HCL, PH 8.5 0.2 M SODIUM ACETATE 30% PEG4000 Resolution 2.30 Å R-free 0.267
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 50–168 Chain D; UniProt 169–410 Fragment:ECTODOMAIN, RESIDUES 50-168 Fragment:ECTODOMAIN, RESIDUES 169-410 NEOGENIN × 1 (P97798) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.5;0.1 M TRIS-HCL, PH 8.5 0.2 M SODIUM ACETATE 30% PEG4000 Resolution 2.30 Å R-free 0.267

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.

10 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RGMB_HUMAN
Isoform
PDB entities 2, 3
Chains and sequence ranges Author chain C; PDBConstruct 4–122; UniProt 50–168 Author chain E; PDBConstruct 4–122; UniProt 50–168 Author chain D; PDBConstruct 1–242; UniProt 169–410 Author chain F; PDBConstruct 1–242; UniProt 169–410

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 4bq6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4bq6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4bq6
Deposition date deposition_date2013-05-30
Structure title titleCrystal structure of the RGMB-NEO1 complex form 1
Keywords keywordsCELL ADHESION; CELL ADHESION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.07
Radius of gyration Rg (electron density) rg_electron27.95
Forward intensity I(0) i0109552000.00
Molecular weight molecular_weight82454.0 kDa
Excluded volume excluded_volume103250 ų
Envelope volume envelope_volume131170 ų
Hydration-shell volume shell_volume38514 ų
Envelope diameter envelope_diameter99.5
Shell Rg shell_rg35.75
Envelope Rg envelope_rg28.14
Shape Rg shape_rg27.92
Total Rg total_rg28.82
Total atoms total_atoms5803
Residues n_residues738
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 dmax92.9
Rg (real space) rg_real28.92
Rg uncertainty (real space) rg_real_error0.54
I(0) (real space) i0_real1.0960e+08
I(0) uncertainty (real space) i0_real_error1.5250e+06
Rg (reciprocal space) rg_reciprocal28.99
I(0) (reciprocal space) i0_reciprocal109600000.0000
Solution quality estimate total_estimate0.8967
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.9
Skewness Skewness skewness0.129
Kurtosis Kurtosis kurtosis-0.467
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha19900000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.892; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.978

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id4bq6A01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4bq6A02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4bq6B01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4bq6B02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4bq6D00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1000 — Protein Transport Mog1p; Chain A
Homologous superfamily homologous superfamily10 — Mog1/PsbP, alpha/beta/alpha sandwich
Domain ID domain_id4bq6F00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1000 — Protein Transport Mog1p; Chain A
Homologous superfamily homologous superfamily10 — Mog1/PsbP, alpha/beta/alpha sandwich

8. Citations (1)

9. Files and Curves (10)