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1j7r

Solution structure and backbone dynamics of the defunct EF-hand domain of Calcium Vector Protein

Method: SOLUTION NMR Dmax: 44.3 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Calcium Vector Protein

Branchiostoma lanceolatum

UniProt P04573

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 1–86 Fragment：N-terminal domain (residues 1-86) No other associated polymer SOLUTION NMR NMR measurement conditions：pH 6.5；298 K；Ionic strength (raw mmCIF value) 100 mM KCL；Pressure ambient NMR sample composition：1.5 mM N-CaVP unlabeled, 20 mM Deuterated Tris buffer, 100 mM KCl | 8% D20 NMR sample composition：1.5 mM N-CaVP uniformly 15N labeled, 20 mM Deuterated Tris buffer, 100 mM KCl | 8% D20 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.

Other PDB Difference from Current Entry 1J7R Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1C7V NMR SOLUTION STRUCTURE OF THE CALCIUM-BOUND C-TERMINAL DOMAIN (W81-S161) OF CALCIUM VECTOR PROTEIN FROM AMPHIOXUS Deposited 2000-03-27 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 81–161（81 aa） Fragment：C-TERMINAL DOMAIN (RESIDUES 81-161)
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；308 K；Ionic strength (raw mmCIF value) 100 mM KCl；Pressure ambient
NMR sample composition Unlabeled | Deuterated Tris buffer (20 mM), 100 mM KCl, pH 6.5, 7% D2O
NMR sample composition Uniformly 15N labeled | Deuterated Tris buffer (20 mM), 100 mM KCl, pH 6.5
Resolution not provided
1C7W NMR SOLUTION STRUCTURE OF THE CALCIUM-BOUND C-TERMINAL DOMAIN (W81-S161) OF CALCIUM VECTOR PROTEIN FROM AMPHIOXUS Deposited 2000-03-27 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 81–161（81 aa） Fragment：C-TERMINAL DOMAIN (RESIDUES 81-161)
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；308 K；Ionic strength (raw mmCIF value) 100 mM KCl；Pressure ambient
NMR sample composition Unlabeled | Deuterated Tris buffer (20 mM), 100 mM KCl, pH 6.5, 7% D2O
NMR sample composition Uniformly 15N labeled | Deuterated Tris buffer (20 mM), 100 mM KCl, pH 6.5
Resolution not provided
1J7Q Solution structure and backbone dynamics of the defunct EF-hand domain of Calcium Vector Protein Deposited 2001-05-18 Parsed fields agree Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–86（86 aa） Fragment：N-terminal domain (residues 1-86)
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 100 mM KCL；Pressure ambient
NMR sample composition 1.5 mM N-CaVP unlabeled, 20 mM Deuterated Tris buffer, 100 mM KCl | 8% D20
NMR sample composition 1.5 mM N-CaVP uniformly 15N labeled, 20 mM Deuterated Tris buffer, 100 mM KCl | 8% D20
Resolution not provided

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CAVP_BRALA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–86； UniProt 1–86

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 1j7r

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1j7r
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1j7r
Deposition date deposition_date2001-05-18
Structure title titleSolution structure and backbone dynamics of the defunct EF-hand domain of Calcium Vector Protein
Keywords keywordsEF-HAND, Calcium Binding Protein, METAL BINDING PROTEIN; METAL BINDING PROTEIN
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier13.23 Å
Radius of gyration Rg (electron density) rg_electron11.98 Å
Forward intensity I(0) i01785370.00
Molecular weight molecular_weight8858.0 kDa
Excluded volume excluded_volume11015 ų
Envelope volume envelope_volume12212 ų
Hydration-shell volume shell_volume8982 ų
Envelope diameter envelope_diameter43.0 Å
Shell Rg shell_rg17.34 Å
Envelope Rg envelope_rg12.43 Å
Shape Rg shape_rg11.96 Å
Total Rg total_rg13.34 Å
Total atoms total_atoms1234
Residues n_residues77
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax44.3 Å
Rg (real space) rg_real13.16 Å
Rg uncertainty (real space) rg_real_error0.27 Å
I(0) (real space) i0_real1.7850e+06
I(0) uncertainty (real space) i0_real_error2.0750e+04
Rg (reciprocal space) rg_reciprocal13.16 Å
I(0) (reciprocal space) i0_reciprocal1785000.0000
Solution quality estimate total_estimate0.7948
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.8 Å
Skewness Skewness skewness0.188
Kurtosis Kurtosis kurtosis-0.214
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha228800.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.776; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1j7ra_
Class classa — All alpha proteins
Fold Fold folda.39 — EF Hand-like
Superfamily Superfamily superfamilya.39.1 — EF-hand
Family Family familya.39.1.5 — Calmodulin-like

CATH v4.4 (1 domains)

Domain ID domain_id1j7rA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
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8. Citations (1)

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9. Files and Curves (10)