SAXSdb — 2hil

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

Fimbrial protein

OrganismNot specified

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Other combination Homooligomer Protein × 18 其他Polymer 18 PDB declaration: octadecameric（18） Consistent with protein copy count	Chain A； UniProt 8–165 Chain B； UniProt 8–165 Chain C； UniProt 8–165 Chain D； UniProt 8–165 Chain E； UniProt 8–165 Chain F； UniProt 8–165 Chain G； UniProt 8–165 Chain H； UniProt 8–165 Chain I； UniProt 8–165 Chain J； UniProt 8–165 Chain K； UniProt 8–165 Chain L； UniProt 8–165 Chain M； UniProt 8–165 Chain N； UniProt 8–165 Chain O； UniProt 8–165 Chain P； UniProt 8–165 Chain Q； UniProt 8–165 Chain R； UniProt 8–165	Non-standard monomer：Yes (specific site not provided by mmCIF)	alpha-D-galactopyranose-(1-3)-2,4-bisacetamido-2,4-dideoxy-beta-D-glucopyranose × 18 OPE PHOSPHORIC ACID MONO-(2-AMINO-ETHYL) ESTER × 18	ELECTRON MICROSCOPY cryo-EM buffer：50 mM CHES；pH 9.5；50 mM CHES cryo-EM vitrification conditions：Cryogen ETHANE；5 ul of sample were applied to grids for 1 minute, blotted for 2.5 seconds then plunge-frozen in liquid ethane using an FEI Vitrobot	Resolution 12.50 Å

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 2HIL	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1AY2 STRUCTURE OF THE FIBER-FORMING PROTEIN PILIN AT 2.6 ANGSTROMS RESOLUTION Deposited 1997-11-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 8–165（158 aa）	Not recorded	PT PLATINUM (II) ION × 2 HTO HEPTANE-1,2,3-TRIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；PROTEIN WAS CRYSTALLIZED FROM 60% PEG400, 50 MM CHESS, PH 8.0, 1% BETA-OCTYL GLUCOSIDE, 0.6% 1,2,3-HEPTANETRIOL.	Resolution 2.60 Å
2HI2 Crystal structure of native Neisseria gonorrhoeae Type IV pilin at 2.3 Angstroms Resolution Deposited 2006-06-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 8–165（158 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	HTO HEPTANE-1,2,3-TRIOL × 1 OPE PHOSPHORIC ACID MONO-(2-AMINO-ETHYL) ESTER × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8；298 K；22% PEG 400 5% HEPTANE TRIOL 50 mM CHES, PH 8.0, VAPOR DIFFUSION, TEMPERATURE 298K	Resolution 2.30 Å R-free 0.282
2PIL Crystallographic Structure of Phosphorylated Pilin from Neisseria: Phosphoserine Sites Modify Type IV Pilus Surface Chemistry Deposited 1998-03-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 8–165（158 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	PT PLATINUM (II) ION × 1 HTO HEPTANE-1,2,3-TRIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；PROTEIN WAS CRYSTALLIZED FROM 60% PEG400, 50 MM CHESS, PH 8.0, 1% BETA-OCTYL GLUCOSIDE, 0.6% 1,2,3-HEPTANETRIOL.	Resolution 2.60 Å
5VXX Cryo-EM reconstruction of Neisseria gonorrhoeae Type IV pilus Deposited 2017-05-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 21 PDB declaration: 21-meric	Chain A 8–165（158 aa） Chain B 8–165（158 aa） Chain C 8–165（158 aa） Chain D 8–165（158 aa） Chain E 8–165（158 aa） Chain F 8–165（158 aa） Chain G 8–165（158 aa） Chain H 8–165（158 aa） Chain I 8–165（158 aa） Chain J 8–165（158 aa） Chain K 8–165（158 aa） Chain L 8–165（158 aa） Chain M 8–165（158 aa） Chain N 8–165（158 aa） Chain O 8–165（158 aa） Chain P 8–165（158 aa） Chain Q 8–165（158 aa） Chain R 8–165（158 aa） Chain S 8–165（158 aa） Chain T 8–165（158 aa） Chain U 8–165（158 aa）	Mutation：P69S, S71T Mutation：P69S, S71T Mutation：P69S, S71T Mutation：P69S, S71T Mutation：P69S, S71T Mutation：P69S, S71T Mutation：P69S, S71T Mutation：P69S, S71T Mutation：P69S, S71T Mutation：P69S, S71T Mutation：P69S, S71T Mutation：P69S, S71T Mutation：P69S, S71T Mutation：P69S, S71T Mutation：P69S, S71T Mutation：P69S, S71T Mutation：P69S, S71T Mutation：P69S, S71T Mutation：P69S, S71T Mutation：P69S, S71T Mutation：P69S, S71T	OPE PHOSPHORIC ACID MONO-(2-AMINO-ETHYL) ESTER × 21	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；PBS buffer cryo-EM vitrification conditions Cryogen ETHANE	Resolution 5.10 Å

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	FMM1_NEIGO
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–158； UniProt 8–165 Author chain B； PDBConstruct 1–158； UniProt 8–165 Author chain C； PDBConstruct 1–158； UniProt 8–165 Author chain D； PDBConstruct 1–158； UniProt 8–165 Author chain E； PDBConstruct 1–158； UniProt 8–165 Author chain F； PDBConstruct 1–158； UniProt 8–165 Author chain G； PDBConstruct 1–158； UniProt 8–165 Author chain H； PDBConstruct 1–158； UniProt 8–165 Author chain I； PDBConstruct 1–158； UniProt 8–165 Author chain J； PDBConstruct 1–158； UniProt 8–165 Author chain K； PDBConstruct 1–158； UniProt 8–165 Author chain L； PDBConstruct 1–158； UniProt 8–165 Author chain M； PDBConstruct 1–158； UniProt 8–165 Author chain N； PDBConstruct 1–158； UniProt 8–165 Author chain O； PDBConstruct 1–158； UniProt 8–165 Author chain P； PDBConstruct 1–158； UniProt 8–165 Author chain Q； PDBConstruct 1–158； UniProt 8–165 Author chain R； PDBConstruct 1–158； UniProt 8–165

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	2hil
Deposition date deposition_date	2006-06-29
Structure title title	Structure of the Neisseria gonorrhoeae Type IV pilus filament from x-ray crystallography and electron cryomicroscopy
Keywords keywords	TYPE IV PILI, virulence factors, DNA binding protein, natural transformation, antigenic variation, CELL ADHESION; CELL ADHESION
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	59.28 Å
Radius of gyration Rg (electron density) rg_electron	61.09 Å
Forward intensity I(0) i0	1476090000.00
Molecular weight molecular_weight	318710.0 kDa
Excluded volume excluded_volume	398470 Å³
Envelope volume envelope_volume	521450 Å³
Hydration-shell volume shell_volume	80566 Å³
Envelope diameter envelope_diameter	263.7 Å
Shell Rg shell_rg	50.93 Å
Envelope Rg envelope_rg	62.57 Å
Shape Rg shape_rg	61.08 Å
Total Rg total_rg	60.87 Å
Total atoms total_atoms	22374
Residues n_residues	2826
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	218.8 Å
Rg (real space) rg_real	60.41 Å
Rg uncertainty (real space) rg_real_error	2.91 Å
I(0) (real space) i0_real	1.4750e+09
I(0) uncertainty (real space) i0_real_error	3.3680e+07
Rg (reciprocal space) rg_reciprocal	58.21 Å
I(0) (reciprocal space) i0_reciprocal	1471000000.0000
Solution quality estimate total_estimate	0.6953
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	42.1 Å
Skewness Skewness skewness	0.758
Kurtosis Kurtosis kurtosis	-0.067
Angular range angular_range	— – 0.1300 Å⁻¹
Current regularization parameter α current_alpha	0.0015
Highest regularization parameter α highest_alpha	1379000000.0000
Real-space data points n_real_points	27
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.266; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.739; Smooth: 0.501

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Fimbrial protein
Molecular weight formula_weight	17210.5 kDa
Source method src_method	nat
Copy count entity_count	18

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R
Atom count atom_count	22374

FTLIELMIVIAIVGILAAVALPAYQDYTARAQVSEAILLAEGQKSAVTEYYLNHGKWPENNTSAGVASSPTDIKGKYVKEVEVKNGVVTATMLSSGVNNEIKGKKLSLWARRENGSVKWFCGQPVTRTDDDTVADAKDGKEIDTKHLPSTCRDNFDAK

Entity 2 Entity 2 branched

Description description	alpha-D-galactopyranose-(1-3)-2,4-bisacetamido-2,4-dideoxy-beta-D-glucopyranose
Molecular weight formula_weight	424.4 kDa
Source method src_method	man
Copy count entity_count	18

Entity 3 Entity 3 non-polymer

Description description	PHOSPHORIC ACID MONO-(2-AMINO-ETHYL) ESTER
Molecular weight formula_weight	141.1 kDa
Source method src_method	syn
Copy count entity_count	18

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	12.500 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

Resolution resolution	12.50 Å
Resolution测定方法 resolution_method	IHRSR
颗粒数 num_particles	25000

fit	/app/data/saxs_computation/hi/2hil/2hil.fit
pddf	/app/data/pr_computation/hi/2hil/2hil.pr.out
profile	/app/data/saxs_computation/hi/2hil/2hil.dat

Structure of the Neisseria gonorrhoeae Type IV pilus filament from x-ray crystallography and electron cryomicroscopy

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

Fimbrial protein

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 branched

Entity 3 Entity 3 non-polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)