SAXSdb — 8i17

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

Histone H2A type 1-B/E

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 3	Histone H2B type 1-J × 1 （P06899） FACT complex subunit SPT16 × 1 （Q9Y5B9） CHLORIDE ION × 1 water × 3	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 3	Histone H2B type 1-J × 1 （P06899） FACT complex subunit SPT16 × 1 （Q9Y5B9） CHLORIDE ION × 1 water × 3	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 3	Histone H2B type 1-J × 1 （P06899） FACT complex subunit SPT16 × 1 （Q9Y5B9） water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	H2A1B_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–100； UniProt 14–113 Author chain D； PDBConstruct 1–100； UniProt 14–113 Author chain G； PDBConstruct 1–100； UniProt 14–113

Histone H2B type 1-J

Homo sapiens

UniProt P06899

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 3	Histone H2A type 1-B/E × 1 （P04908） FACT complex subunit SPT16 × 1 （Q9Y5B9） CHLORIDE ION × 1 water × 3	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 3	Histone H2A type 1-B/E × 1 （P04908） FACT complex subunit SPT16 × 1 （Q9Y5B9） CHLORIDE ION × 1 water × 3	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 3	Histone H2A type 1-B/E × 1 （P04908） FACT complex subunit SPT16 × 1 （Q9Y5B9） water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	H2B1J_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 2–100； UniProt 28–126 Author chain E； PDBConstruct 2–100； UniProt 28–126 Author chain H； PDBConstruct 2–100； UniProt 28–126

FACT complex subunit SPT16

Homo sapiens

UniProt Q9Y5B9

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 3	Histone H2A type 1-B/E × 1 （P04908） Histone H2B type 1-J × 1 （P06899） CHLORIDE ION × 1 water × 3	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 3	Histone H2A type 1-B/E × 1 （P04908） Histone H2B type 1-J × 1 （P06899） CHLORIDE ION × 1 water × 3	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 3	Histone H2A type 1-B/E × 1 （P04908） Histone H2B type 1-J × 1 （P06899） water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	SP16H_HUMAN
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain C； PDBConstruct 3–42； UniProt 926–965 Author chain F； PDBConstruct 3–42； UniProt 926–965 Author chain I； PDBConstruct 3–42； UniProt 926–965

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	8i17
Deposition date deposition_date	2023-01-12
Structure title title	Structural basis for H2A-H2B recognitions by human Spt16
Keywords keywords	histone chaperone, histone, 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.

8i17__assembly_1__model_1

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

Download this curve (.dat)

8i17__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

8i17__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	18.72 Å
Rg (electron density)	17.31 Å
Total Rg	18.30 Å
Atom count	1475
Residues	190
Excluded volume	26182 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`8i17__assembly_1__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`8i17__assembly_2__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`8i17__assembly_3__model_1`	trimeric （3）	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 (5)

Entity 1 Entity 1 polymer

Description description	Histone H2A type 1-B/E
Molecular weight formula_weight	11014.8 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,D,G
Atom count atom_count	4432

KAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQ

Source Source

Source organism organism	Homo sapiens
Common name common_name	human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli B

Entity 2 Entity 2 polymer

Description description	Histone H2B type 1-J
Molecular weight formula_weight	11253.0 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,E,H

SKKRKRSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK

Source Source

Source organism organism	Homo sapiens
Common name common_name	human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli B

Entity 3 Entity 3 polymer

Description description	FACT complex subunit SPT16
Molecular weight formula_weight	4669.3 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	F,I,C

GPEPEGEGSDAEEGDSESEIEDETFNPSEDDYEEEEEDSDED

Source Source

Source organism organism	Homo sapiens
Common name common_name	human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli B

Entity 4 Entity 4 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	96

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6. Fold Classification (SCOP + CATH) 5 domains

CATH v4.4 (5 domains)

Domain ID domain_id	8i17A01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	20 — Histone, subunit A
Homologous superfamily homologous superfamily	10 — Histone, subunit A

Domain ID domain_id	8i17B01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	20 — Histone, subunit A
Homologous superfamily homologous superfamily	10 — Histone, subunit A

Domain ID domain_id	8i17D01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	20 — Histone, subunit A
Homologous superfamily homologous superfamily	10 — Histone, subunit A

Domain ID domain_id	8i17E01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	20 — Histone, subunit A
Homologous superfamily homologous superfamily	10 — Histone, subunit A

Domain ID domain_id	8i17H01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	20 — Histone, subunit A
Homologous superfamily homologous superfamily	10 — Histone, subunit A

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Unit-cell length a length_a	46.852 Å
Unit-cell length b length_b	49.084 Å
Unit-cell length c length_c	85.195 Å
Unit-cell angle α angle_alpha	85.95 °
Unit-cell angle β angle_beta	74.31 °
Unit-cell angle γ angle_gamma	61.80 °
Molecules per unit cell Z z_pdb	3

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

Resolution resolution	1.980 Å
Low-resolution limit resolution_low	40.191 Å
R factor r_factor	0.1724
R_work r_work	0.1704
R_free r_free	0.2111

Structural basis for H2A-H2B recognitions by human Spt16

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

Histone H2A type 1-B/E

State in the Current Structure

Other States of the Same Protein in the Database

Histone H2B type 1-J

State in the Current Structure

Other States of the Same Protein in the Database

FACT complex subunit SPT16

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

8i17__assembly_1__model_1

8i17__assembly_1__model_1 | I(q)

8i17__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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 5 domains

CATH v4.4 (5 domains)

7. Citations (1)

Structural basis for H2A-H2B recognitions by human Spt16

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

Histone H2A type 1-B/E

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Histone H2B type 1-J

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

FACT complex subunit SPT16

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

8i17__assembly_1__model_1

8i17__assembly_1__model_1 | I(q)

8i17__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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 5 domains

CATH v4.4 (5 domains)

7. Citations (1)