1ei8

STRUCTURAL CONSEQUENCES OF A DISCONTINUITY IN THE REPEATING TRIPEPTIDE SEQUENCE OF A COLLAGEN-LIKE TRIPLE-HELICAL PEPTIDE

Method: X-RAY DIFFRACTION

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

No usable UniProt protein identity is available for this entry.

The relationship tables retain this entry's assembly and composition data, but cross-PDB links for the same protein cannot be established reliably without a unified protein identity.

Assembly Composition of the Current Entry

Assembly	Physical composition	Protein state	蛋白 / DNA / RNA / 其他Polymer	Data consistency
1	Protein homooligomer	Homooligomer	3 / 0 / 0 / 0	Consistent with protein count
2	Protein homooligomer	Homooligomer	3 / 0 / 0 / 0	Consistent with protein count
3	Protein homooligomer	Homooligomer	6 / 0 / 0 / 0	Consistent with protein count

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	1ei8
Deposition date deposition_date	2000-02-24
Structure title title	STRUCTURAL CONSEQUENCES OF A DISCONTINUITY IN THE REPEATING TRIPEPTIDE SEQUENCE OF A COLLAGEN-LIKE TRIPLE-HELICAL PEPTIDE
Keywords keywords	collagen-like peptide, TRIPLE HELIX, CONTRACTILE PROTEIN; CONTRACTILE PROTEIN
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.

1ei8__assembly_1__model_1

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

Download this curve (.dat)

1ei8__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1ei8__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	22.54 Å
Rg (electron density)	23.56 Å
Total Rg	23.70 Å
Atom count	529
Residues	58
Excluded volume	9275 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1ei8__assembly_1__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1ei8__assembly_2__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`1ei8__assembly_3__model_1`	hexameric （6）	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 (2)

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6. Fold Classification (SCOP + CATH) 18 domains

SCOP 2.08 (18 domains)

Domain ID domain_id	d1ei8a1
Class class	k — Designed proteins
Fold Fold fold	k.3 — Collagen-like peptides
Superfamily Superfamily superfamily	k.3.1 — Collagen-like peptides
Family Family family	k.3.1.1 — Collagen-like peptides

Domain ID domain_id	d1ei8a2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1ei8a3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1ei8b1
Class class	k — Designed proteins
Fold Fold fold	k.3 — Collagen-like peptides
Superfamily Superfamily superfamily	k.3.1 — Collagen-like peptides
Family Family family	k.3.1.1 — Collagen-like peptides

Domain ID domain_id	d1ei8b2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1ei8b3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1ei8c1
Class class	k — Designed proteins
Fold Fold fold	k.3 — Collagen-like peptides
Superfamily Superfamily superfamily	k.3.1 — Collagen-like peptides
Family Family family	k.3.1.1 — Collagen-like peptides

Domain ID domain_id	d1ei8c2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1ei8c3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1ei8d1
Class class	k — Designed proteins
Fold Fold fold	k.3 — Collagen-like peptides
Superfamily Superfamily superfamily	k.3.1 — Collagen-like peptides
Family Family family	k.3.1.1 — Collagen-like peptides

Domain ID domain_id	d1ei8d2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1ei8d3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1ei8e1
Class class	k — Designed proteins
Fold Fold fold	k.3 — Collagen-like peptides
Superfamily Superfamily superfamily	k.3.1 — Collagen-like peptides
Family Family family	k.3.1.1 — Collagen-like peptides

Domain ID domain_id	d1ei8e2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1ei8e3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1ei8f1
Class class	k — Designed proteins
Fold Fold fold	k.3 — Collagen-like peptides
Superfamily Superfamily superfamily	k.3.1 — Collagen-like peptides
Family Family family	k.3.1.1 — Collagen-like peptides

Domain ID domain_id	d1ei8f2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1ei8f3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

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Unit-cell length a length_a	14.150 Å
Unit-cell length b length_b	23.770 Å
Unit-cell length c length_c	82.210 Å
Unit-cell angle α angle_alpha	85.86 °
Unit-cell angle β angle_beta	85.54 °
Unit-cell angle γ angle_gamma	84.34 °
Molecules per unit cell Z z_pdb	6

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

Resolution resolution	2.000 Å
Low-resolution limit resolution_low	500.000 Å
R factor r_factor	0.2510
R_work r_work	0.2170
R_free r_free	0.2890

Description description	COLLAGEN-LIKE PEPTIDE (PRO-HYP-GLY)4-PG-(PRO-HYP-GLY)5
Molecular weight formula_weight	2577.7 kDa
Source method src_method	syn
Copy count entity_count	6

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F
Atom count atom_count	1327

STRUCTURAL CONSEQUENCES OF A DISCONTINUITY IN THE REPEATING TRIPEPTIDE SEQUENCE OF A COLLAGEN-LIKE TRIPLE-HELICAL PEPTIDE

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

Assembly Composition of the Current Entry

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1ei8__assembly_1__model_1

1ei8__assembly_1__model_1 | I(q)

1ei8__assembly_1__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 18 domains

SCOP 2.08 (18 domains)

7. Citations (1)

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	249