4i88

R107G HSP16.5

Method: X-RAY DIFFRACTION

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

Small heat shock protein HSP16.5

Methanocaldococcus jannaschii

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 24	water × 24	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	HSPS_METJA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–147； UniProt 1–147 Author chain B； PDBConstruct 1–147； UniProt 1–147 Author chain C； PDBConstruct 1–147； UniProt 1–147 Author chain D； PDBConstruct 1–147； UniProt 1–147 Author chain E； PDBConstruct 1–147； UniProt 1–147 Author chain F； PDBConstruct 1–147； UniProt 1–147 Author chain G； PDBConstruct 1–147； UniProt 1–147 Author chain H； PDBConstruct 1–147； UniProt 1–147

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	4i88
Deposition date deposition_date	2012-12-03
Structure title title	R107G HSP16.5
Keywords keywords	alpha-B domain, 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.

4i88__assembly_1__model_1

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

Download this curve (.dat)

4i88__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

4i88__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	50.30 Å
Rg (electron density)	49.04 Å
Total Rg	49.52 Å
Atom count	20955
Residues	2733
Excluded volume	379000 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`4i88__assembly_1__model_1`	24-meric （24）	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) 16 domains

SCOP 2.08 (8 domains)

Domain ID domain_id	d4i88a_
Class class	b — All beta proteins
Fold Fold fold	b.15 — HSP20-like chaperones
Superfamily Superfamily superfamily	b.15.1 — HSP20-like chaperones
Family Family family	b.15.1.1 — HSP20

Domain ID domain_id	d4i88b_
Class class	b — All beta proteins
Fold Fold fold	b.15 — HSP20-like chaperones
Superfamily Superfamily superfamily	b.15.1 — HSP20-like chaperones
Family Family family	b.15.1.1 — HSP20

Domain ID domain_id	d4i88c_
Class class	b — All beta proteins
Fold Fold fold	b.15 — HSP20-like chaperones
Superfamily Superfamily superfamily	b.15.1 — HSP20-like chaperones
Family Family family	b.15.1.1 — HSP20

Domain ID domain_id	d4i88d_
Class class	b — All beta proteins
Fold Fold fold	b.15 — HSP20-like chaperones
Superfamily Superfamily superfamily	b.15.1 — HSP20-like chaperones
Family Family family	b.15.1.1 — HSP20

Domain ID domain_id	d4i88e_
Class class	b — All beta proteins
Fold Fold fold	b.15 — HSP20-like chaperones
Superfamily Superfamily superfamily	b.15.1 — HSP20-like chaperones
Family Family family	b.15.1.1 — HSP20

Domain ID domain_id	d4i88f_
Class class	b — All beta proteins
Fold Fold fold	b.15 — HSP20-like chaperones
Superfamily Superfamily superfamily	b.15.1 — HSP20-like chaperones
Family Family family	b.15.1.1 — HSP20

Domain ID domain_id	d4i88g_
Class class	b — All beta proteins
Fold Fold fold	b.15 — HSP20-like chaperones
Superfamily Superfamily superfamily	b.15.1 — HSP20-like chaperones
Family Family family	b.15.1.1 — HSP20

Domain ID domain_id	d4i88h_
Class class	b — All beta proteins
Fold Fold fold	b.15 — HSP20-like chaperones
Superfamily Superfamily superfamily	b.15.1 — HSP20-like chaperones
Family Family family	b.15.1.1 — HSP20

CATH v4.4 (8 domains)

Domain ID domain_id	4i88A00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	790 —

Domain ID domain_id	4i88B00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	790 —

Domain ID domain_id	4i88C00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	790 —

Domain ID domain_id	4i88D00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	790 —

Domain ID domain_id	4i88E00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	790 —

Domain ID domain_id	4i88F00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	790 —

Domain ID domain_id	4i88G00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	790 —

Domain ID domain_id	4i88H00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	790 —

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Unit-cell length a length_a	173.600 Å
Unit-cell length b length_b	173.600 Å
Unit-cell length c length_c	103.000 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	72

Space group space_group	H 3
Space-group number int_tables_number	146
Crystal system crystal_system	—

Resolution resolution	2.850 Å
Low-resolution limit resolution_low	48.720 Å
R factor r_factor	0.1977
R_work r_work	0.1947
R_free r_free	0.2543

Description description	Small heat shock protein HSP16.5
Molecular weight formula_weight	16470.0 kDa
Source method src_method	man
Copy count entity_count	8

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H
Atom count atom_count	7025

R107G HSP16.5

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

Small heat shock protein HSP16.5

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

4i88__assembly_1__model_1

4i88__assembly_1__model_1 | I(q)

4i88__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

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

CATH v4.4 (8 domains)

7. Citations (1)

Source organism organism	Methanocaldococcus jannaschii
NCBI taxonomy ID ncbi_taxonomy_id	243232
Host organism host_organism	Escherichia coli

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	40

R107G HSP16.5

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

Small heat shock protein HSP16.5

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

4i88__assembly_1__model_1

4i88__assembly_1__model_1 | I(q)

4i88__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

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

CATH v4.4 (8 domains)

7. Citations (1)