SAXSdb — 6n1l

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

Fibronectin-binding protein BBK32

Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)

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 206–348	Not recorded	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION；pH 6.5；293 K；0.1M MES (pH 6.5), 0.2M ammonium sulfate, 30% PEG-MME 5,000	Resolution 1.72 Å R-free 0.236

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 6N1L	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
4PZ5 Crystal structure of the second and third fibronectin F1 modules in complex with a fragment of BBK32 from Borrelia burgdorferi Deposited 2014-03-28	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 175–189（15 aa） Fragment：BBK32TwL, UNP RESIDUES 175-189	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.9；291 K；1.4 M Na/K phosphate, pH 6.9, VAPOR DIFFUSION, SITTING DROP, temperature 291K	Resolution 1.96 Å R-free 0.199
7MZT Borrelia burgdorferi BBK32-C in complex with an autolytic fragment of human C1r at 4.1A Deposited 2021-05-24	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain I 206–348（143 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.2 M Sodium formate, 27.5% Polyethylene glycol 3,350	Resolution 4.07 Å R-free 0.372

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	O50835_BORBU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 6–148； UniProt 206–348

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	6n1l
Deposition date deposition_date	2018-11-09
Structure title title	The complement inhibitory domain of B. burgdorferi BBK32.
Keywords keywords	C1r-binding, inhibitor, immunomodulator, IMMUNOSUPPRESSANT; IMMUNOSUPPRESSANT
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	19.18 Å
Radius of gyration Rg (electron density) rg_electron	18.56 Å
Forward intensity I(0) i0	4638270.00
Molecular weight molecular_weight	16297.0 kDa
Excluded volume excluded_volume	20801 Å³
Envelope volume envelope_volume	24009 Å³
Hydration-shell volume shell_volume	12374 Å³
Envelope diameter envelope_diameter	73.8 Å
Shell Rg shell_rg	22.58 Å
Envelope Rg envelope_rg	19.31 Å
Shape Rg shape_rg	18.57 Å
Total Rg total_rg	19.28 Å
Total atoms total_atoms	1149
Residues n_residues	141
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	73.7 Å
Rg (real space) rg_real	19.47 Å
Rg uncertainty (real space) rg_real_error	0.82 Å
I(0) (real space) i0_real	4.6380e+06
I(0) uncertainty (real space) i0_real_error	6.5320e+04
Rg (reciprocal space) rg_reciprocal	19.43 Å
I(0) (reciprocal space) i0_reciprocal	4638000.0000
Solution quality estimate total_estimate	0.7198
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	17.4 Å
Skewness Skewness skewness	0.679
Kurtosis Kurtosis kurtosis	0.033
Angular range angular_range	— – 0.4150 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	1237000.0000
Real-space data points n_real_points	73
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.373; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.274; Smooth: 0.960

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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8. Citations (1)

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Unit-cell length a length_a	66.530 Å
Unit-cell length b length_b	66.530 Å
Unit-cell length c length_c	79.508 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	6

Space group space_group	P 65
Space-group number int_tables_number	170
Crystal system crystal_system	hexagonal

Resolution resolution	1.722 Å
Low-resolution limit resolution_low	33.260 Å
R factor r_factor	—
R_work r_work	0.2046
R_free r_free	0.2361

Description description	Fibronectin-binding protein BBK32
Molecular weight formula_weight	16922.3 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1265

The complement inhibitory domain of B. burgdorferi BBK32.

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

Fibronectin-binding protein BBK32

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 water

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
NCBI Class编号 ncbi_taxonomy_id	224326
宿主生物 host_organism	Escherichia coli

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	116

fit	/app/data/saxs_computation/n1/6n1l/6n1l.fit
pddf	/app/data/pr_computation/n1/6n1l/6n1l.pr.out
profile	/app/data/saxs_computation/n1/6n1l/6n1l.dat