SAXSdb — 1eg4

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

BETA-DYSTROGLYCAN

OrganismNot specified

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain P； UniProt 881–895	Not recorded	DYSTROPHIN × 1 （P11532）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；ammonium sulfate, glycerol, DTT, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.00 Å R-free 0.249

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 1EG4	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2MK7 Tetra-O-GalNAc glycosylated mucin sequence from alpha dystroglycan mucin domain Deposited 2014-02-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 419–427（9 aa） Fragment：mucin domain peptide (UNP residues 419-427)	Non-standard monomer：Yes (specific site not provided by mmCIF)	A2G 2-acetamido-2-deoxy-alpha-D-galactopyranose × 4	SOLUTION NMR NMR measurement conditions pH 4.5；288 K；Pressure ambient NMR sample composition 2-10 mM aDG mucin domain peptide, 100% D2O \| 100% D2O NMR sample composition 2-10 mM aDG mucin domain peptide, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
5GGP Crystal structure of N-terminal domain of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase in complex with GlcNAc-beta1,2-Man-peptide Deposited 2016-06-16	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 316–325（10 aa）	Not recorded	NA SODIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；293 K；MES-NaOH, LiCl2, Na acetate, PEG-6000	Resolution 1.60 Å R-free 0.246
5GGP Crystal structure of N-terminal domain of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase in complex with GlcNAc-beta1,2-Man-peptide Deposited 2016-06-16	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 316–325（10 aa）	Not recorded	NA SODIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；293 K；MES-NaOH, LiCl2, Na acetate, PEG-6000	Resolution 1.60 Å R-free 0.246
5LLK Crystal structure of human alpha-dystroglycan Deposited 2016-07-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 52–315（264 aa） Fragment：UNP residues 52-315	Mutation：R168H	EDO 1,2-ETHANEDIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.2；277 K；0.8 M Sodium Citrate	Resolution 1.80 Å R-free 0.195
6JJY Crystal Structure of KIBRA and beta-Dystroglycan Deposited 2019-02-27	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain U 877–895（19 aa）	Not recorded	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；289 K；3.0-4.0M NaCl, 100mM Bis-Tris (pH 6.5)	Resolution 2.30 Å R-free 0.253
8UF4 Crystal structure of wildtype dystroglycan proteolytic domain (juxtamembrane domain) Deposited 2023-10-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 491–653（163 aa） Fragment：residues 491-653 Chain B 654–748（95 aa） Fragment：residues 654-748 Chain C 491–653（163 aa） Fragment：residues 491-653 Chain D 654–748（95 aa） Fragment：residues 654-748	Not recorded	CA CALCIUM ION × 1 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.3；295 K；0.1 M Tris, 0.2 M lithium sulfate, 20% PEG 4000	Resolution 2.43 Å R-free 0.275

5 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	DAG1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain P； PDBConstruct 1–15； UniProt 881–895

DYSTROPHIN

Homo sapiens

UniProt P11532

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 3046–3306	Fragment：WW DOMAIN	BETA-DYSTROGLYCAN × 1 （Q14118）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；ammonium sulfate, glycerol, DTT, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.00 Å R-free 0.249

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 1EG4	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1DXX N-terminal Actin-binding Domain of Human Dystrophin Deposited 2000-01-20	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–246（246 aa） Fragment：ACTIN-BINDING Chain B 1–246（246 aa） Fragment：ACTIN-BINDING	Mutation：YES Mutation：YES	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；1.55M AMMONIUM FORMATE, 0.1M HEPES 7.4, pH 7.40	Resolution 2.60 Å R-free 0.268
1DXX N-terminal Actin-binding Domain of Human Dystrophin Deposited 2000-01-20	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–246（246 aa） Fragment：ACTIN-BINDING Chain D 1–246（246 aa） Fragment：ACTIN-BINDING	Mutation：YES Mutation：YES	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；1.55M AMMONIUM FORMATE, 0.1M HEPES 7.4, pH 7.40	Resolution 2.60 Å R-free 0.268
1EG3 STRUCTURE OF A DYSTROPHIN WW DOMAIN FRAGMENT IN COMPLEX WITH A BETA-DYSTROGLYCAN PEPTIDE Deposited 2000-02-11	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 3046–3306（261 aa） Fragment：WW DOMAIN	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；ammonium sulfate, glycerol, DTT, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 2.00 Å R-free 0.257
3UUN Crystal Structure of N-terminal first spectrin repeat of dystrophin Deposited 2011-11-28	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 338–456（119 aa） Fragment：Spectrin Repeat, UNP residues 338-456	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；294.15 K；0.1M Tris HCl, 2.0M Ammonium sulphate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 294.15K	Resolution 2.30 Å R-free 0.260
3UUN Crystal Structure of N-terminal first spectrin repeat of dystrophin Deposited 2011-11-28	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 338–456（119 aa） Fragment：Spectrin Repeat, UNP residues 338-456	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；294.15 K；0.1M Tris HCl, 2.0M Ammonium sulphate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 294.15K	Resolution 2.30 Å R-free 0.260
3UUN Crystal Structure of N-terminal first spectrin repeat of dystrophin Deposited 2011-11-28	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 338–456（119 aa） Fragment：Spectrin Repeat, UNP residues 338-456 Chain B 338–456（119 aa） Fragment：Spectrin Repeat, UNP residues 338-456	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；294.15 K；0.1M Tris HCl, 2.0M Ammonium sulphate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 294.15K	Resolution 2.30 Å R-free 0.260
9D58 Human Dystrophin tandem calponin homology actin-binding domain crystallized in a closed-state conformation Deposited 2024-08-13	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–246（245 aa） Fragment：actin-binding domain/calponin homology domains 1 and 2	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1 M Bis-Tris pH 6.7, 30% w/v Polyethylene monomethyl ether (MPEG) 5,000	Resolution 1.94 Å R-free 0.262
9D58 Human Dystrophin tandem calponin homology actin-binding domain crystallized in a closed-state conformation Deposited 2024-08-13	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–246（245 aa） Fragment：actin-binding domain/calponin homology domains 1 and 2	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1 M Bis-Tris pH 6.7, 30% w/v Polyethylene monomethyl ether (MPEG) 5,000	Resolution 1.94 Å R-free 0.262
9D58 Human Dystrophin tandem calponin homology actin-binding domain crystallized in a closed-state conformation Deposited 2024-08-13	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 2–246（245 aa） Fragment：actin-binding domain/calponin homology domains 1 and 2	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1 M Bis-Tris pH 6.7, 30% w/v Polyethylene monomethyl ether (MPEG) 5,000	Resolution 1.94 Å R-free 0.262
9D58 Human Dystrophin tandem calponin homology actin-binding domain crystallized in a closed-state conformation Deposited 2024-08-13	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 2–246（245 aa） Fragment：actin-binding domain/calponin homology domains 1 and 2	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1 M Bis-Tris pH 6.7, 30% w/v Polyethylene monomethyl ether (MPEG) 5,000	Resolution 1.94 Å R-free 0.262
9EC1 The Structure of Human Dystrophin Spectrin Repeat 24 Deposited 2024-11-13	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2933–3046（114 aa） Fragment：spectrin repeat 24	Not recorded	SO4 SULFATE ION × 2 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；0.1 M Sodium citrate tribasic dihydrate, pH 5.6, 0.5 M Ammonium sulfate , 1 M Lithium sulfate monohydrate	Resolution 2.14 Å R-free 0.255
9EC1 The Structure of Human Dystrophin Spectrin Repeat 24 Deposited 2024-11-13	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2933–3046（114 aa） Fragment：spectrin repeat 24	Not recorded	SO4 SULFATE ION × 2 CL CHLORIDE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；0.1 M Sodium citrate tribasic dihydrate, pH 5.6, 0.5 M Ammonium sulfate , 1 M Lithium sulfate monohydrate	Resolution 2.14 Å R-free 0.255
9EC1 The Structure of Human Dystrophin Spectrin Repeat 24 Deposited 2024-11-13	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 2933–3046（114 aa） Fragment：spectrin repeat 24	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；0.1 M Sodium citrate tribasic dihydrate, pH 5.6, 0.5 M Ammonium sulfate , 1 M Lithium sulfate monohydrate	Resolution 2.14 Å R-free 0.255
9EC1 The Structure of Human Dystrophin Spectrin Repeat 24 Deposited 2024-11-13	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 2933–3046（114 aa） Fragment：spectrin repeat 24	Not recorded	SO4 SULFATE ION × 1 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；0.1 M Sodium citrate tribasic dihydrate, pH 5.6, 0.5 M Ammonium sulfate , 1 M Lithium sulfate monohydrate	Resolution 2.14 Å R-free 0.255
9EC1 The Structure of Human Dystrophin Spectrin Repeat 24 Deposited 2024-11-13	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain E 2933–3046（114 aa） Fragment：spectrin repeat 24	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；0.1 M Sodium citrate tribasic dihydrate, pH 5.6, 0.5 M Ammonium sulfate , 1 M Lithium sulfate monohydrate	Resolution 2.14 Å R-free 0.255
9EC1 The Structure of Human Dystrophin Spectrin Repeat 24 Deposited 2024-11-13	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 6 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain F 2933–3046（114 aa） Fragment：spectrin repeat 24	Not recorded	SO4 SULFATE ION × 2 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；0.1 M Sodium citrate tribasic dihydrate, pH 5.6, 0.5 M Ammonium sulfate , 1 M Lithium sulfate monohydrate	Resolution 2.14 Å R-free 0.255
9EC1 The Structure of Human Dystrophin Spectrin Repeat 24 Deposited 2024-11-13	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 7 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain G 2933–3046（114 aa） Fragment：spectrin repeat 24	Not recorded	SO4 SULFATE ION × 4 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；0.1 M Sodium citrate tribasic dihydrate, pH 5.6, 0.5 M Ammonium sulfate , 1 M Lithium sulfate monohydrate	Resolution 2.14 Å R-free 0.255
9EC1 The Structure of Human Dystrophin Spectrin Repeat 24 Deposited 2024-11-13	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 8 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain H 2933–3046（114 aa） Fragment：spectrin repeat 24	Not recorded	CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；0.1 M Sodium citrate tribasic dihydrate, pH 5.6, 0.5 M Ammonium sulfate , 1 M Lithium sulfate monohydrate	Resolution 2.14 Å R-free 0.255

5 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	DMD_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain A； PDBConstruct 1–261； UniProt 3046–3306

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	1eg4
Deposition date deposition_date	2000-02-11
Structure title title	STRUCTURE OF A DYSTROPHIN WW DOMAIN FRAGMENT IN COMPLEX WITH A BETA-DYSTROGLYCAN PEPTIDE
Keywords keywords	EF-hand like domain, WW domain, Polyproline type II (PPII) helix, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	20.12 Å
Radius of gyration Rg (electron density) rg_electron	18.95 Å
Forward intensity I(0) i0	17391200.00
Molecular weight molecular_weight	31257.0 kDa
Excluded volume excluded_volume	39081 Å³
Envelope volume envelope_volume	45257 Å³
Hydration-shell volume shell_volume	19978 Å³
Envelope diameter envelope_diameter	70.8 Å
Shell Rg shell_rg	25.35 Å
Envelope Rg envelope_rg	19.30 Å
Shape Rg shape_rg	18.98 Å
Total Rg total_rg	19.76 Å
Total atoms total_atoms	2195
Residues n_residues	273
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	70.7 Å
Rg (real space) rg_real	20.05 Å
Rg uncertainty (real space) rg_real_error	0.51 Å
I(0) (real space) i0_real	1.7390e+07
I(0) uncertainty (real space) i0_real_error	2.2920e+05
Rg (reciprocal space) rg_reciprocal	20.06 Å
I(0) (reciprocal space) i0_reciprocal	17390000.0000
Solution quality estimate total_estimate	0.8530
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	25.2 Å
Skewness Skewness skewness	0.268
Kurtosis Kurtosis kurtosis	-0.181
Angular range angular_range	— – 0.3950 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	4137000.0000
Real-space data points n_real_points	71
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.699; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.992

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	BETA-DYSTROGLYCAN
Molecular weight formula_weight	1746.0 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	P
Atom count atom_count	2478

KNMTPYRSPPPYVPP

Entity 2 Entity 2 polymer

Description description	DYSTROPHIN
Molecular weight formula_weight	29845.2 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A

GPASQHFLSTSVQGPWERAISPNKVPYYINHETQTTCWDHPKMTELYQSLADLNNVRFSAYRTAMKLRRLQKALCLDLLSLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDWMRLEPQSMVWLPVLHRVAAAET

来源 Source

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

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	283

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7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d1eg4a1
Class class	a — All alpha proteins
Fold Fold fold	a.39 — EF Hand-like
Superfamily Superfamily superfamily	a.39.1 — EF-hand
Family Family family	a.39.1.7 — EF-hand modules in multidomain proteins

Domain ID domain_id	d1eg4a2
Class class	a — All alpha proteins
Fold Fold fold	a.39 — EF Hand-like
Superfamily Superfamily superfamily	a.39.1 — EF-hand
Family Family family	a.39.1.7 — EF-hand modules in multidomain proteins

Domain ID domain_id	d1eg4a3
Class class	b — All beta proteins
Fold Fold fold	b.72 — WW domain-like
Superfamily Superfamily superfamily	b.72.1 — WW domain
Family Family family	b.72.1.1 — WW domain

CATH v4.4 (4 domains)

Domain ID domain_id	1eg4A01
Class class	2 — Mainly Beta
Architecture architecture	20 — Single Sheet
Topology topology	70 — Ubiquitin Ligase Nedd4; Chain: W;
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	1eg4A02
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	140 — Helix Hairpins
Homologous superfamily homologous superfamily	70 —

Domain ID domain_id	1eg4A03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	10 — EF-hand

Domain ID domain_id	1eg4A04
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	10 — EF-hand

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8. Citations (1)

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Unit-cell length a length_a	48.680 Å
Unit-cell length b length_b	67.050 Å
Unit-cell length c length_c	83.840 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	4

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.000 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	—
R_work r_work	0.1970
R_free r_free	0.2490

fit	/app/data/saxs_computation/eg/1eg4/1eg4.fit
pddf	/app/data/pr_computation/eg/1eg4/1eg4.pr.out
profile	/app/data/saxs_computation/eg/1eg4/1eg4.dat

STRUCTURE OF A DYSTROPHIN WW DOMAIN FRAGMENT IN COMPLEX WITH A BETA-DYSTROGLYCAN PEPTIDE

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

BETA-DYSTROGLYCAN

State in the Current Structure

Other States of the Same Protein in the Database

DYSTROPHIN

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

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 water

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

CATH v4.4 (4 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)