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1tap

NMR SOLUTION STRUCTURE OF RECOMBINANT TICK ANTICOAGULANT PROTEIN (RTAP), A FACTOR XA INHIBITOR FROM THE TICK ORNITHODOROS MOUBATA

Method: SOLUTION NMR Dmax: 37.1 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

FACTOR XA INHIBITOR

Ornithodoros moubata

UniProt P17726

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 1–60 Not recorded No other associated polymer SOLUTION NMR mmCIF provides none of the parsed experimental conditions 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 1TAP Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1D0D CRYSTAL STRUCTURE OF TICK ANTICOAGULANT PROTEIN COMPLEXED WITH BOVINE PANCREATIC TRYPSIN INHIBITOR Deposited 1999-09-09 Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–60（60 aa）
Not recorded SO4 SULFATE ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；ammonium sulfate, ADA, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
Resolution 1.62 Å R-free 0.211
1KIG BOVINE FACTOR XA Deposited 1997-04-24 Different oligomeric state Different experimental method Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain I 1–60（60 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 3.00 Å
1TCP NMR STRUCTURE DETERMINATION OF TICK ANTICOAGULANT PEPTIDE (TAP) Deposited 1994-10-31 Parsed fields agree Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–60（60 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions 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 TAP_ORNMO
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–60； UniProt 1–60

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 1tap

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1tap
Deposition date deposition_date1994-08-16
Structure title titleNMR SOLUTION STRUCTURE OF RECOMBINANT TICK ANTICOAGULANT PROTEIN (RTAP), A FACTOR XA INHIBITOR FROM THE TICK ORNITHODOROS MOUBATA
Keywords keywordsPROTEINASE INHIBITOR; PROTEINASE INHIBITOR
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier11.28 Å
Radius of gyration Rg (electron density) rg_electron11.02 Å
Forward intensity I(0) i0335548000.00
Molecular weight molecular_weight139270.0 kDa
Excluded volume excluded_volume167080 ų
Envelope volume envelope_volume16765 ų
Hydration-shell volume shell_volume11118 ų
Envelope diameter envelope_diameter40.8 Å
Shell Rg shell_rg18.63 Å
Envelope Rg envelope_rg13.04 Å
Shape Rg shape_rg10.99 Å
Total Rg total_rg11.29 Å
Total atoms total_atoms18140
Residues n_residues1200
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 dmax37.1 Å
Rg (real space) rg_real11.23 Å
Rg uncertainty (real space) rg_real_error0.28 Å
I(0) (real space) i0_real3.3550e+08
I(0) uncertainty (real space) i0_real_error3.4000e+06
Rg (reciprocal space) rg_reciprocal11.23 Å
I(0) (reciprocal space) i0_reciprocal335500000.0000
Solution quality estimate total_estimate0.8985
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary14.1 Å
Skewness Skewness skewness0.154
Kurtosis Kurtosis kurtosis-0.475
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha93080.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.897; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.992
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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_idd1tapa_
Class classg — Small proteins
Fold Fold foldg.8 — BPTI-like
Superfamily Superfamily superfamilyg.8.1 — BPTI-like
Family Family familyg.8.1.2 — Soft tick anticoagulant proteins

CATH v4.4 (1 domains)

Domain ID domain_id1tapA00
Class class4 — Few Secondary Structures
Architecture architecture10 — Irregular
Topology topology410 — Factor Xa Inhibitor
Homologous superfamily homologous superfamily10 — Pancreatic trypsin inhibitor Kunitz domain
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8. Citations (2)

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9. Files and Curves (10)