SAXSdb — 1n12

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

mature Fimbrial protein PapE

Escherichia coli

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Peptide corresponding to the N-terminal extension of protein PapK × 1 （P42190） water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	Peptide corresponding to the N-terminal extension of protein PapK × 1 （P42190） water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	PAPE_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–127； UniProt 37–173 Author chain C； PDBConstruct 1–127； UniProt 37–173

Peptide corresponding to the N-terminal extension of protein PapK

OrganismNot specified

UniProt P42190

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	mature Fimbrial protein PapE × 1 （P08407） water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	mature Fimbrial protein PapE × 1 （P08407） water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	PAPK_ECOLIX
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–11； UniProt 22–32 Author chain D； PDBConstruct 1–11； UniProt 22–32

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	1n12
Deposition date deposition_date	2002-10-16
Structure title title	Crystal structure of the PapE (N-terminal-deleted) pilus subunit bound to a peptide corresponding to the N-terminal extension of the PapK pilus subunit (residues 1-11) from uropathogenic E. coli
Keywords keywords	;Immunoglobulin-like fold, donor strand complementation, donor strand exchange, chaperone priming, pilus fiber assembly, organelle biogenesis, CHAPERONE ;; CHAPERONE
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

1n12__assembly_2__model_1

Assembly 2 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1n12__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1n12__assembly_2__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	17.10 Å
Rg (electron density)	16.01 Å
Total Rg	17.00 Å
Atom count	1103
Residues	144
Excluded volume	19555 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1n12__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1n12__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	mature Fimbrial protein PapE
Molecular weight formula_weight	14832.0 kDa
Mutation mutation	N-terminal residue 26-36 deleted, contains selenomethionine at methionine positions
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C
Atom count atom_count	2395

VPACTVSNTTVDWQDVEIQTLSQNGNHEKEFTVNMRCPYNLGTMKVTITATNTYNNAILVQNTSNTSSDGLLVYLYNSNAGNIGTAITLGTPFTPGKITGNNADKTISLHAKLGYKGNMQNLIAGPFSATATLVASYS

Source Source

Source organism organism	Escherichia coli
NCBI taxonomy ID ncbi_taxonomy_id	562
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Peptide corresponding to the N-terminal extension of protein PapK
Molecular weight formula_weight	1207.3 kDa
Source method src_method	syn
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,D

SDVAFRGNLLD

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	140

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1n12a_
Class class	b — All beta proteins
Fold Fold fold	b.2 — Common fold of diphtheria toxin/transcription factors/cytochrome f
Superfamily Superfamily superfamily	b.2.3 — Bacterial adhesins
Family Family family	b.2.3.2 — Pilus subunits

Domain ID domain_id	d1n12c_
Class class	b — All beta proteins
Fold Fold fold	b.2 — Common fold of diphtheria toxin/transcription factors/cytochrome f
Superfamily Superfamily superfamily	b.2.3 — Bacterial adhesins
Family Family family	b.2.3.2 — Pilus subunits

CATH v4.4 (2 domains)

Domain ID domain_id	1n12A00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	1090 — Fimbrial-type adhesion domain

Domain ID domain_id	1n12C00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	1090 — Fimbrial-type adhesion domain

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Unit-cell length a length_a	25.254 Å
Unit-cell length b length_b	91.922 Å
Unit-cell length c length_c	51.244 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	99.26 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	1.870 Å
Low-resolution limit resolution_low	26.210 Å
R factor r_factor	0.2080
R_work r_work	0.2080
R_free r_free	0.2490

Crystal structure of the PapE (N-terminal-deleted) pilus subunit bound to a peptide corresponding to the N-terminal extension of the PapK pilus subunit (residues 1-11) from uropathogenic E. coli

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

mature Fimbrial protein PapE

State in the Current Structure

Other States of the Same Protein in the Database

Peptide corresponding to the N-terminal extension of protein PapK

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1n12__assembly_2__model_1

1n12__assembly_2__model_1 | I(q)

1n12__assembly_2__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)

Crystal structure of the PapE (N-terminal-deleted) pilus subunit bound to a peptide corresponding to the N-terminal extension of the PapK pilus subunit (residues 1-11) from uropathogenic E. coli

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

mature Fimbrial protein PapE

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Peptide corresponding to the N-terminal extension of protein PapK

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1n12__assembly_2__model_1

1n12__assembly_2__model_1 | I(q)

1n12__assembly_2__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)