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1t0v

NMR Solution Structure of the Engineered Lipocalin FluA(R95K) Northeast Structural Genomics Target OR17

Method: SOLUTION NMR Dmax: 74.8 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

BILIN-BINDING PROTEIN

Pieris brassicae

UniProt P09464

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 16–189 Mutation：R95K No other associated polymer SOLUTION NMR NMR measurement conditions：pH 6.4；298 K；Ionic strength (raw mmCIF value) 150 mM NaCl; 10 mM Na-PO4; 50 mM benzamidine; 0.2 mM EDTA；Pressure ambient NMR sample composition：0.7 mM FluA(R95K) U-13C,15N 150 mM NaCl 10 mM Na-PO4 0.2 mM EDTA 50 mM benzamidine pH 6.4 | 90% H2O/10% D2O NMR sample composition：0.7 mM FluA(R95K) U-50% 2H,15N 150 mM NaCl 10 mM Na-PO4 0.2 mM EDTA 50 mM benzamidine pH 6.4 | 90% H2O/10% D2O NMR sample composition：0.7 mM FluA(R95K) U-15N 150 mM NaCl 10 mM Na-PO4 0.2 mM EDTA 50 mM benzamidine pH 6.4 | 90% H2O/10% D2O NMR sample composition：0.7 mM FluA(R95K) 150 mM NaCl 10 mM Na-PO4 0.2 mM EDTA 50 mM benzamidine pH 6.4 | 100% D2O NMR sample composition：0.7 mM FluA(R95K) 150 mM NaCl 10 mM Na-PO4 0.2 mM EDTA 50 mM benzamidine pH 6.4 | 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.

Other PDB Difference from Current Entry 1T0V Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1BBP MOLECULAR STRUCTURE OF THE BILIN BINDING PROTEIN (BBP) FROM PIERIS BRASSICAE AFTER REFINEMENT AT 2.0 ANGSTROMS RESOLUTION. Deposited 1990-09-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 16–188（173 aa）
Chain B 16–188（173 aa）
Chain C 16–188（173 aa）
Chain D 16–188（173 aa）
Not recorded BLV BILIVERDIN IX GAMMA CHROMOPHORE × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å
1KXO ENGINEERED LIPOCALIN DIGA16 : APO-FORM Deposited 2002-02-01 Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 16–189（174 aa）
Mutation：N1D, N21G, E28Q, K31A, N34D, S35H, V36I, E37T, N48R, H60S, I69S, K87S, L88Y, Y90I, K95Q, N97G, Y114F, K116S, Q125M, F127L, K135M No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.6；298 K；0.1-M Hepes, 10% Isopropanole, 19% PEG 4000, pH = 7.8, pH 7.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.80 Å R-free 0.289
1LKE ENGINEERED LIPOCALIN DIGA16 IN COMPLEX WITH DIGOXIGENIN Deposited 2002-04-25 Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 16–189（174 aa）
Mutation：N1D, N21G, E28Q, K31A, N34D, S35H, V36I, E37T, N48R, H60S, I69S, K87S, L88Y, Y90I, K95Q, N97G, Y114F, K116S, Q125M, F127L, K135M DOG DIGOXIGENIN × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；0.1-M HEPES, 10% ISOPROPANOL, 19% PEG 4000, pH 8.00, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.90 Å R-free 0.248
1LNM ANTICALIN DIGA16 IN COMPLEX WITH DIGITOXIGENIN Deposited 2002-05-03 Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 16–189（174 aa）
Mutation：N1D, N21G, E28Q, K31A, N34D, S35H, V36I, E37T, N48R, H60S, I69S, K87S, L88Y, Y90I, K95Q, N97G, Y114F, K116S, Q125M, F127L, K135M DTX DIGITOXIGENIN × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.8；298 K；0.1-M hepes, 10% isopropanol, 19% peg 4000, pH 7.80, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.90 Å R-free 0.245
1N0S ENGINEERED LIPOCALIN FLUA IN COMPLEX WITH FLUORESCEIN Deposited 2002-10-15 Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 16–189（174 aa）
Not recorded FLU 2-(6-HYDROXY-3-OXO-3H-XANTHEN-9-YL)-BENZOIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.1；298 K；2.0 M (NH4)2SO4, 2% (w/v) PEG 400, 10 mM hepes/naoh, pH 8.1, VAPOR DIFFUSION, HANGING DROP, temperature 298 KK
Resolution 2.00 Å R-free 0.243
1N0S ENGINEERED LIPOCALIN FLUA IN COMPLEX WITH FLUORESCEIN Deposited 2002-10-15 Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 16–189（174 aa）
Not recorded FLU 2-(6-HYDROXY-3-OXO-3H-XANTHEN-9-YL)-BENZOIC ACID × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.1；298 K；2.0 M (NH4)2SO4, 2% (w/v) PEG 400, 10 mM hepes/naoh, pH 8.1, VAPOR DIFFUSION, HANGING DROP, temperature 298 KK
Resolution 2.00 Å R-free 0.243

5 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BBP_PIEBR
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–174； UniProt 16–189

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 1t0v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1t0v
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1t0v
Deposition date deposition_date2004-04-13
Structure title titleNMR Solution Structure of the Engineered Lipocalin FluA(R95K) Northeast Structural Genomics Target OR17
Keywords keywords;PIERIS BRASSICAE, LIPOCALIN, ANTICALIN, PROTEIN ENGINEERING, BETA-BARREL, LIGAND BINDING PROTEIN, Structural Genomics, PSI-2, Protein Structure Initiative, Northeast Structural Genomics Consortium, NESG ;; LIGAND 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_guinier17.58 Å
Radius of gyration Rg (electron density) rg_electron17.37 Å
Forward intensity I(0) i02443360000.00
Molecular weight molecular_weight419690.0 kDa
Excluded volume excluded_volume523020 ų
Envelope volume envelope_volume59294 ų
Hydration-shell volume shell_volume22822 ų
Envelope diameter envelope_diameter82.0 Å
Shell Rg shell_rg28.85 Å
Envelope Rg envelope_rg24.20 Å
Shape Rg shape_rg17.35 Å
Total Rg total_rg17.60 Å
Total atoms total_atoms58160
Residues n_residues3680
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 dmax74.8 Å
Rg (real space) rg_real17.57 Å
Rg uncertainty (real space) rg_real_error0.83 Å
I(0) (real space) i0_real2.4430e+09
I(0) uncertainty (real space) i0_real_error3.1470e+07
Rg (reciprocal space) rg_reciprocal17.57 Å
I(0) (reciprocal space) i0_reciprocal2443000000.0000
Solution quality estimate total_estimate0.7231
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.9 Å
Skewness Skewness skewness0.429
Kurtosis Kurtosis kurtosis0.333
Angular range angular_range— – 0.4550 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1106000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.268; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.591; Smooth: 1.000
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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) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1t0va1
Class classb — All beta proteins
Fold Fold foldb.60 — Lipocalins
Superfamily Superfamily superfamilyb.60.1 — Lipocalins
Family Family familyb.60.1.1 — Retinol binding protein-like
Domain ID domain_idd1t0va2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id1t0vA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily20 — Calycin beta-barrel core domain
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8. Citations (1)

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9. Files and Curves (10)