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1ttk

NMR solution structure of omega-conotoxin MVIIA, a N-type calcium channel blocker

Method: SOLUTION NMR Dmax: 23.0 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Omega-conotoxin MVIIa

OrganismNot specified

UniProt P05484

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 46–70 Non-standard monomer：Yes (specific site not provided by mmCIF) No other associated polymer SOLUTION NMR NMR measurement conditions：pH 3.5；293 K；Pressure ambient NMR measurement conditions：pH 3.5；280 K；Pressure ambient NMR sample composition：2mM MVIIA, 95% H2O, D2O, DSS | 95% H2O/5% D2O NMR sample composition：2mM MVIIA, 100% D2O | 100% 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.

Other PDB Difference from Current Entry 1TTK Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1DW4 NMR STRUCTURE OF OMEGA-CONOTOXIN MVIIA: CONSTRAINTS ON DISULPHIDE BRIDGES Deposited 2000-01-24 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–25（25 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 3.5；283 K；Ionic strength (raw mmCIF value) 0；Pressure ambient
NMR sample composition 1 | H2O (10% D2O)
NMR sample composition 1 | D2O
Resolution not provided
1DW5 NMR STRUCTURE OF OMEGA-CONOTOXIN MVIIA: NO CONSTRAINTS ON DISULPHIDE BRIDGES Deposited 2000-01-24 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–25（25 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 3.5；283 K；Ionic strength (raw mmCIF value) 0；Pressure AMBIENT
NMR sample composition 1
Resolution not provided
1FEO Solution structure of omega-conotoxin MVIIA with C-terminal Gly Deposited 2000-07-21 Different construct Different mutation/modification Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–25（25 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6；283 K；Pressure ambient
NMR sample composition 2 mM omega-MVIIA-Gly | 93% H2O, 7% D20
NMR sample composition 2 mM omega-MVIIA-Gly U-15N | 93% H2O, 7% D20
Resolution not provided
1MVI N-TYPE CALCIUM CHANNEL BLOCKER, OMEGA-CONOTOXIN MVIIA, NMR, 15 STRUCTURES Deposited 1996-08-02 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–25（25 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 3；293 K
Resolution not provided
1OMG NMR STUDY OF OMEGA-CONOTOXIN MVIIA Deposited 1995-04-26 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–25（25 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1TT3 NMR soulution structure of omega-conotoxin [K10]MVIIA Deposited 2004-06-21 Different mutation/modification Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 46–70（25 aa）
Mutation：R10K Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 3.5；293 K；Pressure ambient
NMR measurement conditions pH 3.5；280 K；Pressure ambient
NMR sample composition 2mM [K10]MVIIA, 95% H2O, 5% D2O, DSS | 95% H2O/5% D2O
NMR sample composition 2mM [K10]MVIIA, 100% D2O, DSS | 100% D2O
Resolution not provided
7MIX Human N-type voltage-gated calcium channel Cav2.2 in the presence of ziconotide at 3.0 Angstrom resolution Deposited 2021-04-18 Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 46–70（25 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 CA CALCIUM ION × 2 Y01 CHOLESTEROL HEMISUCCINATE × 2 CLR CHOLESTEROL × 5 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 2 PT5 [(2R)-1-octadecanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phospho ryl]oxy-propan-2-yl] (8Z)-icosa-5,8,11,14-tetraenoate × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE；blot for 6 seconds before plunging
Resolution 3.00 Å
7VFU Human N-type voltage gated calcium channel CaV2.2-alpha2/delta1-beta1 complex, bound to ziconotide Deposited 2021-09-13 Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric
Chain E 46–70（25 aa）
Not recorded R16 HEXADECANE × 18 Y01 CHOLESTEROL HEMISUCCINATE × 3 PT5 [(2R)-1-octadecanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phospho ryl]oxy-propan-2-yl] (8Z)-icosa-5,8,11,14-tetraenoate × 1 CA CALCIUM ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.00 Å

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

View Construct and Data Evidence
UniProt name CXO7A_CONMA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–25； UniProt 46–70

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 1ttk

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1ttk
Deposition date deposition_date2004-06-22
Structure title titleNMR solution structure of omega-conotoxin MVIIA, a N-type calcium channel blocker
Keywords keywordsfour loop frame work, amidated C-terminal, disulfide rich, TOXIN; TOXIN
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier6.63 Å
Radius of gyration Rg (electron density) rg_electron7.22 Å
Forward intensity I(0) i041143600.00
Molecular weight molecular_weight45054.0 kDa
Excluded volume excluded_volume53310 ų
Envelope volume envelope_volume5117 ų
Hydration-shell volume shell_volume5486 ų
Envelope diameter envelope_diameter27.0 Å
Shell Rg shell_rg13.32 Å
Envelope Rg envelope_rg8.77 Å
Shape Rg shape_rg7.18 Å
Total Rg total_rg7.56 Å
Total atoms total_atoms6035
Residues n_residues425
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 dmax23.0 Å
Rg (real space) rg_real6.59 Å
Rg uncertainty (real space) rg_real_error0.25 Å
I(0) (real space) i0_real4.1140e+07
I(0) uncertainty (real space) i0_real_error4.1860e+05
Rg (reciprocal space) rg_reciprocal6.59 Å
I(0) (reciprocal space) i0_reciprocal41140000.0000
Solution quality estimate total_estimate0.8463
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary22.5 Å
Skewness Skewness skewness0.186
Kurtosis Kurtosis kurtosis-0.182
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4818.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.742; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.785
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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) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1ttka_
Class classg — Small proteins
Fold Fold foldg.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamilyg.3.6 — omega toxin-like
Family Family familyg.3.6.1 — Conotoxin
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8. Citations (2)

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9. Files and Curves (10)