SAXSdb — 3fb2

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

Spectrin alpha chain, brain spectrin

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 1337–1544	Fragment：Repeats 15 and 16 Non-standard monomer：Yes (specific site not provided by mmCIF)	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：microbatch crystallization under oil；pH 5；277 K；12% PEG 20000, 0.1M magnesium sulfate, 0.1M sodium acetate, pH 5.0, microbatch crystallization under oil, temperature 277K	Resolution 2.30 Å R-free 0.248
2	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain B； UniProt 1337–1544	Fragment：Repeats 15 and 16 Non-standard monomer：Yes (specific site not provided by mmCIF)	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：microbatch crystallization under oil；pH 5；277 K；12% PEG 20000, 0.1M magnesium sulfate, 0.1M sodium acetate, pH 5.0, microbatch crystallization under oil, temperature 277K	Resolution 2.30 Å R-free 0.248

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 3FB2	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2FOT Crystal structure of the complex between calmodulin and alphaII-spectrin Deposited 2006-01-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1172–1211（40 aa） Fragment：Calmodulin binding domain	Mutation：L1211R	CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；298 K；50mM Tris,pH 8.00, 30% PEG 8000, 0.1M ammonium-sulfate, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 2.45 Å R-free 0.269
3F31 Crystal Structure of the N-terminal region of AlphaII-spectrin Tetramerization Domain Deposited 2008-10-30	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 1–147（147 aa） Chain B 1–147（147 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；293 K；PEG8000:PEG1000 (1:2), 4% 1,4-butane-diol, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.30 Å R-free 0.280
3F31 Crystal Structure of the N-terminal region of AlphaII-spectrin Tetramerization Domain Deposited 2008-10-30	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–147（147 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；293 K；PEG8000:PEG1000 (1:2), 4% 1,4-butane-diol, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.30 Å R-free 0.280
3F31 Crystal Structure of the N-terminal region of AlphaII-spectrin Tetramerization Domain Deposited 2008-10-30	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1–147（147 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；293 K；PEG8000:PEG1000 (1:2), 4% 1,4-butane-diol, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.30 Å R-free 0.280
5FW9 Human Spectrin SH3 domain D48G, E7Y, K60Y Deposited 2016-02-12	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 965–1025（61 aa） Fragment：SH3 DOMAIN, RESIDUES 965-1025	Mutation：YES	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.55 Å R-free 0.249
5FWB Human Spectrin SH3 domain D48G, E7F, K60F Deposited 2016-02-12	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 965–1022（58 aa） Fragment：SH3, UNP RESIDUES 965-1025	Mutation：YES	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.50 Å R-free 0.236
5FWC Human Spectrin SH3 domain D48G, E7A, K60A Deposited 2016-02-12	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 965–1022（58 aa） Fragment：SH3, RESIDUES 965-1022	Mutation：YES	EDO 1,2-ETHANEDIOL × 2 NH4 AMMONIUM ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.40 Å R-free 0.238
6ZEH Structure of PP1-spectrin alpha II chimera [PP1(7-304) + linker (G/S)x9 + spectrin alpha II (1025-1039)] bound to Phactr1 (516-580) Deposited 2020-06-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1025–1039（15 aa）	Mutation：N-terminal Vector derived sequence GHMGS	MN MANGANESE (II) ION × 2 PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；20% (w/v) polyethylene glycol 3350, 0.2 M NaI and 0.1 M BIS-Tris propane pH 8.5	Resolution 1.30 Å R-free 0.169
6ZEH Structure of PP1-spectrin alpha II chimera [PP1(7-304) + linker (G/S)x9 + spectrin alpha II (1025-1039)] bound to Phactr1 (516-580) Deposited 2020-06-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1025–1039（15 aa）	Mutation：N-terminal Vector derived sequence GHMGS	MN MANGANESE (II) ION × 2 PO4 PHOSPHATE ION × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；20% (w/v) polyethylene glycol 3350, 0.2 M NaI and 0.1 M BIS-Tris propane pH 8.5	Resolution 1.30 Å R-free 0.169

6 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	SPTA2_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 11–218； UniProt 1337–1544 Author chain B； PDBConstruct 11–218； UniProt 1337–1544

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	3fb2
Deposition date deposition_date	2008-11-18
Structure title title	Crystal structure of the human brain alpha spectrin repeats 15 and 16. Northeast Structural Genomics Consortium target HR5563a.
Keywords keywords	;Spectrin alpha chain, brain spectrin, non-erythroid alpha chain Alpha-II spectrin, fordrin alpha chain, SPTAN1, SPTA2_HUMAN, NESG, HR5563A, Structural Genomics, PSI-2, Protein Structure Initiative, Northeast Structural Genomics Consortium, Actin capping, Actin-binding, Alternative splicing, Calcium, Calmodulin-binding, Cytoplasm, Cytoskeleton, Phosphoprotein, Polymorphism, SH3 domain, 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	33.18 Å
Radius of gyration Rg (electron density) rg_electron	34.36 Å
Forward intensity I(0) i0	38084100.00
Molecular weight molecular_weight	45615.0 kDa
Excluded volume excluded_volume	55691 Å³
Envelope volume envelope_volume	75370 Å³
Hydration-shell volume shell_volume	21910 Å³
Envelope diameter envelope_diameter	139.3 Å
Shell Rg shell_rg	33.48 Å
Envelope Rg envelope_rg	35.63 Å
Shape Rg shape_rg	34.33 Å
Total Rg total_rg	34.38 Å
Total atoms total_atoms	3179
Residues n_residues	380
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	134.0 Å
Rg (real space) rg_real	34.18 Å
Rg uncertainty (real space) rg_real_error	2.61 Å
I(0) (real space) i0_real	3.8080e+07
I(0) uncertainty (real space) i0_real_error	7.5320e+05
Rg (reciprocal space) rg_reciprocal	33.75 Å
I(0) (reciprocal space) i0_reciprocal	38070000.0000
Solution quality estimate total_estimate	0.6715
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	22.3 Å
Skewness Skewness skewness	0.767
Kurtosis Kurtosis kurtosis	0.075
Angular range angular_range	— – 0.2400 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	2826000.0000
Real-space data points n_real_points	49
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.242; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.048; Smooth: 0.952

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id	3fb2A01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	60 —

Domain ID domain_id	3fb2A02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	60 —

Domain ID domain_id	3fb2B01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	60 —

Domain ID domain_id	3fb2B02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	60 —

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8. Citations (1)

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Unit-cell length a length_a	65.610 Å
Unit-cell length b length_b	96.376 Å
Unit-cell length c length_c	111.145 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	8

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

Resolution resolution	2.300 Å
Low-resolution limit resolution_low	36.410 Å
R factor r_factor	0.2190
R_work r_work	0.2190
R_free r_free	0.2480

Description description	Spectrin alpha chain, brain spectrin
Molecular weight formula_weight	25665.8 kDa
Source method src_method	man
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	3459

Crystal structure of the human brain alpha spectrin repeats 15 and 16. Northeast Structural Genomics Consortium target HR5563a.

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

Spectrin alpha chain, brain spectrin

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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 water

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

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

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	280

fit	/app/data/saxs_computation/fb/3fb2/3fb2.fit
pddf	/app/data/pr_computation/fb/3fb2/3fb2.pr.out
profile	/app/data/saxs_computation/fb/3fb2/3fb2.dat