SAXSdb — 2pp4

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

Protein ETO

Homo sapiens

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 119–225	Fragment：TAFH domain, residues 119-225 Mutation：F136Y	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 6.8；293 K；Pressure ambient NMR sample composition：1.1 mM protein, 200 mM phosphate buffer, 95% H2O, 5% D2O \| 95% H2O/5% D2O	Resolution not provided

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 2PP4	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1WQ6 The tetramer structure of the nervy homolgy two (NHR2) domain of AML1-ETO is critical for AML1-ETO'S activity Deposited 2004-09-23	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 335–403（69 aa） Fragment：NHR2 domain Chain B 335–403（69 aa） Fragment：NHR2 domain	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；293 K；100mM Na citrate (pH 5.6), 100mM MgCl2, 30% MPD, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.00 Å R-free 0.270
2DJ8 Solution Structure of zf-MYND Domain of Protein CBFA2TI (Protein MTG8) Deposited 2006-03-31	Different construct Different mutation/modification Different ligand/ion Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 449–450（2 aa） Fragment：zf-MYND	Not recorded	ZN ZINC ION × 2	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 120；Pressure ambient NMR sample composition 0.95mM zf-MYND domain, U-13C, 15N; 20mM d-Tris_HCl (pH 7.0); 100mM NaCl; 1mM d-DTT, 0.02% NaN3; 0.05mM ZnCl2; 1mM IDA; 90% H2O, 10% D20 \| 90% H2O, 10% D20	Resolution not provided
2KNH The Solution structure of the eTAFH domain of AML1-ETO complexed with HEB peptide Deposited 2009-08-25	Different construct Different mutation/modification Different oligomeric state Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 119–216（98 aa） Fragment：eTAFH domain (UNP residues 119-216)	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6；303 K；Ionic strength (raw mmCIF value) 350；Pressure ambient NMR sample composition 25 mM Bis-Tris, 1 mM EDTA, 350 mM sodium chloride, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
2KYG Structure of the AML1-ETO Nervy Domain - PKA(RIIa) complex and its contribution to AML1-ETO activity Deposited 2010-05-25	Different construct Different mutation/modification Different oligomeric state Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 437–467（31 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4；303 K；Ionic strength (raw mmCIF value) 0.0；Pressure ambient NMR sample composition 2 mM [U-99% 13C; U-99% 15N] NHR3, 2 mM [U-99% 13C; U-99% 15N] PKA(RIIa), 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
2OD1 Solution structure of the MYND domain from human AML1-ETO Deposited 2006-12-21	Different construct Different mutation/modification Different ligand/ion Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 510–559（50 aa） Fragment：MYND domain	Not recorded	ZN ZINC ION × 2	SOLUTION NMR NMR measurement conditions pH 6.8；303 K；Pressure 1 NMR sample composition 1-2mM protein, 25mM Bis-Tris, 5mM DTT, 50uM ZnCl2, 95% H20, 5% D2O \| 95% H20, 5% D2O	Resolution not provided
2ODD Solution structure of the MYND domain from AML1-ETO complexed with SMRT, a corepressor Deposited 2006-12-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 510–559（50 aa） Fragment：MYND domain (AML1-ETO, residues 658-707)	Not recorded	ZN ZINC ION × 2	SOLUTION NMR NMR measurement conditions pH 6.8；303 K；Pressure 1 NMR sample composition 2mM SMRT-MYND, 25mM Bis-Tris, pH 6.8, 50uM ZnCl2, 1mM DTT, 95%H2O, 5% D2O \| 95% H2O/5% D2O	Resolution not provided
4JOL Complex structure of AML1-ETO NHR2 domain with HEB fragment Deposited 2013-03-18	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 338–400（63 aa） Fragment：NHR2 domain of AML1-ETO (unp residues 338-400) Chain C 338–400（63 aa） Fragment：NHR2 domain of AML1-ETO (unp residues 338-400)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；0.1 mM Tris, 20% ETHANOL, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.91 Å R-free 0.252
4JOL Complex structure of AML1-ETO NHR2 domain with HEB fragment Deposited 2013-03-18	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 338–400（63 aa） Fragment：NHR2 domain of AML1-ETO (unp residues 338-400) Chain D 338–400（63 aa） Fragment：NHR2 domain of AML1-ETO (unp residues 338-400)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；0.1 mM Tris, 20% ETHANOL, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.91 Å R-free 0.252

7 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	MTG8_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–107； UniProt 119–225

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	2pp4
Deposition date deposition_date	2007-04-27
Structure title title	Solution Structure of ETO-TAFH refined in explicit solvent
Keywords keywords	transcriptional cofactor, Leukemia, 4-helix bundle, TRANSCRIPTION; TRANSCRIPTION
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	15.52 Å
Radius of gyration Rg (electron density) rg_electron	15.03 Å
Forward intensity I(0) i0	749698000.00
Molecular weight molecular_weight	241860.0 kDa
Excluded volume excluded_volume	307450 Å³
Envelope volume envelope_volume	30193 Å³
Hydration-shell volume shell_volume	15344 Å³
Envelope diameter envelope_diameter	55.9 Å
Shell Rg shell_rg	22.57 Å
Envelope Rg envelope_rg	17.26 Å
Shape Rg shape_rg	15.01 Å
Total Rg total_rg	15.23 Å
Total atoms total_atoms	34780
Residues n_residues	2140
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	48.3 Å
Rg (real space) rg_real	15.50 Å
Rg uncertainty (real space) rg_real_error	0.30 Å
I(0) (real space) i0_real	7.4970e+08
I(0) uncertainty (real space) i0_real_error	8.2710e+06
Rg (reciprocal space) rg_reciprocal	15.50 Å
I(0) (reciprocal space) i0_reciprocal	749700000.0000
Solution quality estimate total_estimate	0.8094
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	17.1 Å
Skewness Skewness skewness	0.230
Kurtosis Kurtosis kurtosis	-0.347
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	114000.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.840; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d2pp4a1
Class class	a — All alpha proteins
Fold Fold fold	a.277 — TAFH domain-like
Superfamily Superfamily superfamily	a.277.1 — TAFH domain-like
Family Family family	a.277.1.1 — TAFH domain-like

CATH v4.4 (1 domains)

Domain ID domain_id	2pp4A00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily	1110 — TAFH/NHR1 domain

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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	—

Description description	Protein ETO
Molecular weight formula_weight	12138.0 kDa
Mutation mutation	F136Y
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	34780

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli BL21(DE3)

Solution Structure of ETO-TAFH refined in explicit solvent

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

Protein ETO

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

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/pp/2pp4/2pp4.fit
pddf	/app/data/pr_computation/pp/2pp4/2pp4.pr.out
profile	/app/data/saxs_computation/pp/2pp4/2pp4.dat