1c89

NMR STRUCTURE OF INTRAMOLECULAR DIMER ANTIFREEZE PROTEIN RD3, 40 SA STRUCTURES

Method: SOLUTION NMR Dmax: 52.5 Å Quality: GOOD

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

ANTIFREEZE PROTEIN TYPE III

Pachycara brachycephalum

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 1–134 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.7;277 K;Pressure 1 NMR sample composition:90% H2O/10% 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.

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 1–134; UniProt 1–134

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 1c89

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1c89
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1c89
Deposition date deposition_date2000-05-04
Structure title titleNMR STRUCTURE OF INTRAMOLECULAR DIMER ANTIFREEZE PROTEIN RD3, 40 SA STRUCTURES
Keywords keywordsANTIFREEZE, THERMAL HYSTERESIS PROTEIN, ICE BINDING PROTEIN, ANTIFREEZE PROTEIN; ANTIFREEZE PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier15.84
Radius of gyration Rg (electron density) rg_electron16.25
Forward intensity I(0) i04292590000.00
Molecular weight molecular_weight579080.0 kDa
Excluded volume excluded_volume734380 ų
Envelope volume envelope_volume34976 ų
Hydration-shell volume shell_volume16783 ų
Envelope diameter envelope_diameter60.7
Shell Rg shell_rg23.63
Envelope Rg envelope_rg18.09
Shape Rg shape_rg16.23
Total Rg total_rg16.41
Total atoms total_atoms82720
Residues n_residues5360
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 dmax52.5
Rg (real space) rg_real15.92
Rg uncertainty (real space) rg_real_error0.35
I(0) (real space) i0_real4.2930e+09
I(0) uncertainty (real space) i0_real_error4.8520e+07
Rg (reciprocal space) rg_reciprocal15.91
I(0) (reciprocal space) i0_reciprocal4293000000.0000
Solution quality estimate total_estimate0.7734
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.6
Skewness Skewness skewness0.471
Kurtosis Kurtosis kurtosis-0.290
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha554300.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.715; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.909; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1c89a1
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
Domain ID domain_idd1c89a2
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 (2 domains)

Domain ID domain_id1c89A01
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
Domain ID domain_id1c89A02
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 (5)

9. Files and Curves (10)