4n1d

Nodal/BMP2 chimera NB250

Method: X-RAY DIFFRACTION Dmax: 65.9 Å Quality: GOOD

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

Nodal/BMP2 chimera protein

Homo sapiens

UniProt P12643

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 283–305 Chain A; UniProt 362–396 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.6;288 K;0.2M NaCl, 0.1 M Na acetate pH 4.6, 30% 2-Methyl-2,4-pentanediol, VAPOR DIFFUSION, HANGING DROP, temperature 288K Resolution 1.91 Å R-free 0.204

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.

19 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BMP2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–24; UniProt 283–305 Author chain A; PDBConstruct 82–116; UniProt 362–396

Nodal/BMP2 chimera protein

Homo sapiens

UniProt Q96S42

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 257–313 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.6;288 K;0.2M NaCl, 0.1 M Na acetate pH 4.6, 30% 2-Methyl-2,4-pentanediol, VAPOR DIFFUSION, HANGING DROP, temperature 288K Resolution 1.91 Å R-free 0.204

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 NODAL_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 25–81; UniProt 257–313

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 4n1d

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4n1d
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4n1d
Deposition date deposition_date2013-10-04
Structure title titleNodal/BMP2 chimera NB250
Keywords keywordsCytokine, Signaling Protein; Cytokine, Signaling Protein
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.71
Radius of gyration Rg (electron density) rg_electron18.77
Forward intensity I(0) i02950420.00
Molecular weight molecular_weight12158.0 kDa
Excluded volume excluded_volume15111 ų
Envelope volume envelope_volume19032 ų
Hydration-shell volume shell_volume9584 ų
Envelope diameter envelope_diameter65.1
Shell Rg shell_rg22.57
Envelope Rg envelope_rg19.00
Shape Rg shape_rg18.82
Total Rg total_rg19.29
Total atoms total_atoms852
Residues n_residues105
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 dmax65.9
Rg (real space) rg_real18.96
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real2.9500e+06
I(0) uncertainty (real space) i0_real_error3.9170e+04
Rg (reciprocal space) rg_reciprocal18.93
I(0) (reciprocal space) i0_reciprocal2950000.0000
Solution quality estimate total_estimate0.7906
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.3
Skewness Skewness skewness0.510
Kurtosis Kurtosis kurtosis-0.508
Angular range angular_range— – 0.4250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha285000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.671; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.343; Smooth: 0.917

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd4n1da_
Class classg — Small proteins
Fold Fold foldg.17 — Cystine-knot cytokines
Superfamily Superfamily superfamilyg.17.1 — Cystine-knot cytokines
Family Family familyg.17.1.2 — Transforming growth factor (TGF)-beta

CATH v4.4 (1 domains)

Domain ID domain_id4n1dA00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines

8. Citations (1)

9. Files and Curves (10)