3nla

NMR STRUCTURE OF THE N-TERMINAL DOMAIN WITH A LINKER PORTION OF ANTARCTIC EEL POUT ANTIFREEZE PROTEIN RD3, 40 STRUCTURES

Method: SOLUTION NMR Dmax: 38.0 Å Quality: GOOD

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

ANTIFREEZE PROTEIN RD3 TYPE III

Lycodichthys dearborni

UniProt P35753

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 1–73 Fragment:N-TERMINAL DOMAIN WITH A LINKER PORTION No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.7;277 K 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.

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

View Construct and Data Evidence
UniProt name ANP3_RHIDE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–74; UniProt 1–73

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 3nla

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3nla
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3nla
Deposition date deposition_date1998-02-24
Structure title titleNMR STRUCTURE OF THE N-TERMINAL DOMAIN WITH A LINKER PORTION OF ANTARCTIC EEL POUT ANTIFREEZE PROTEIN RD3, 40 STRUCTURES
Keywords keywordsANTIFREEZE PROTEIN, THERMAL HYSTERESIS PROTEIN, ICE BINDING PROTEIN, ANTIFREEZE; ANTIFREEZE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier11.29
Radius of gyration Rg (electron density) rg_electron11.49
Forward intensity I(0) i01240900000.00
Molecular weight molecular_weight309930.0 kDa
Excluded volume excluded_volume393010 ų
Envelope volume envelope_volume18743 ų
Hydration-shell volume shell_volume11877 ų
Envelope diameter envelope_diameter45.0
Shell Rg shell_rg19.25
Envelope Rg envelope_rg13.66
Shape Rg shape_rg11.47
Total Rg total_rg11.65
Total atoms total_atoms44357
Residues n_residues2920
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 dmax38.0
Rg (real space) rg_real11.19
Rg uncertainty (real space) rg_real_error0.23
I(0) (real space) i0_real1.2410e+09
I(0) uncertainty (real space) i0_real_error1.3420e+07
Rg (reciprocal space) rg_reciprocal11.20
I(0) (reciprocal space) i0_reciprocal1241000000.0000
Solution quality estimate total_estimate0.8652
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary14.9
Skewness Skewness skewness-0.061
Kurtosis Kurtosis kurtosis-0.475
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha76320.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.750; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3nlaa_
Class classb — All beta proteins
Fold Fold foldb.85 — beta-clip
Superfamily Superfamily superfamilyb.85.1 — AFP III-like domain
Family Family familyb.85.1.1 — AFP III-like domain

CATH v4.4 (1 domains)

Domain ID domain_id3nlaA00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology1210 — Type Iii Antifreeze Protein Isoform Hplc 12
Homologous superfamily homologous superfamily10 — Antifreeze-like/N-acetylneuraminic acid synthase C-terminal domain

8. Citations (4)

9. Files and Curves (10)