SAXSdb — 7eye

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

G protein/GFP fusion protein,Nuclear pore complex protein Nup155

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	Insufficient information Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 512–750	Not recorded	No other associated polymer	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5；Buffer was freshly made. cryo-EM vitrification conditions：Cryogen ETHANE；Blot for 3 seconds before plunging	Resolution 5.10 Å

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 7EYE	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6ZQO EYFP mutant - F165G Deposited 2020-07-10	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 512–750（239 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；5.7 mg/ml in 20mM Tris 8.0 200 mM NaCl mixed with a 1.44M (NH4)2SO4, 60mM Bicine pH 9.0 reservoir solution.	Resolution 2.20 Å R-free 0.340
7EYQ Cryo-EM (SPA) structure of human Nup155 Longer N-terminus (19-1069) at 5.4 Angstrom resolution Deposited 2021-05-31	Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 512–750（239 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；Buffer was freshly made. cryo-EM vitrification conditions Cryogen ETHANE；Blot for 3 seconds before plunging	Resolution 5.40 Å
7FBS structure of a channel Deposited 2021-07-12	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 512–750（239 aa）	Mutation：I1487Q,F1488Q,M1489Q	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 6OU [(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-yl] (~{Z})-octadec-9-enoate × 11 4Y4 1-[2-[(2R)-2-oxidanyl-3-(propylamino)propoxy]phenyl]-3-phenyl-propan-1-one × 1 9Z9 (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
7XSU Cardiac sodium channel in complex with LqhIII Deposited 2022-05-15	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 512–750（239 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 BMA beta-D-mannopyranose × 1 6OU [(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-yl] (~{Z})-octadec-9-enoate × 6 9Z9 (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 6.1 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
9NTM SPEF1 bound to 14-pf microtubule Deposited 2025-03-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 89 PDB declaration: 89-meric	Chain 1A 512–750（239 aa） Chain 1B 512–750（239 aa） Chain 1C 512–750（239 aa） Chain 1D 512–750（239 aa） Chain 1E 512–750（239 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 42 MG MAGNESIUM ION × 42 GDP GUANOSINE-5'-DIPHOSPHATE × 42 TA1 TAXOL × 42	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 7.10 Å

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

View Construct and Data Evidence

UniProt name	B7UCZ6_9RHAB
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–239； UniProt 512–750

G protein/GFP fusion protein,Nuclear pore complex protein Nup155

Homo sapiens

UniProt O75694

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Insufficient information Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 1–863	Not recorded	No other associated polymer	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5；Buffer was freshly made. cryo-EM vitrification conditions：Cryogen ETHANE；Blot for 3 seconds before plunging	Resolution 5.10 Å

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 7EYE	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
5A9Q Human nuclear pore complex Deposited 2015-07-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 304 PDB declaration: 304-meric	Chain A 1–1391（1391 aa） Chain B 1–1391（1391 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 20MM TRIS, 0.2-0.4% TREHALOSE；pH 7.5；20MM TRIS, 0.2-0.4% TREHALOSE cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；VITRIFICATION 1 -- CRYOGEN- ETHANE-PROPANE MIXTURE, INSTRUMENT- HOMEMADE PLUNGER,	Resolution 23.00 Å
5IJN Composite structure of the inner ring of the human nuclear pore complex (32 copies of Nup205) Deposited 2016-03-02	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 208 PDB declaration: 208-meric	Chain A 1–1391（1391 aa） Chain B 1–1391（1391 aa） Chain E 1–1391（1391 aa） Chain K 1–1391（1391 aa） Chain Q 1–1391（1391 aa） Chain W 1–1391（1391 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 21.40 Å
5IJO Alternative composite structure of the inner ring of the human nuclear pore complex (16 copies of Nup188, 16 copies of Nup205) Deposited 2016-03-02	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 208 PDB declaration: 208-meric	Chain A 1–1391（1391 aa） Chain B 1–1391（1391 aa） Chain E 1–1391（1391 aa） Chain K 1–1391（1391 aa） Chain Q 1–1391（1391 aa） Chain W 1–1391（1391 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 21.40 Å
7EYF Cryo-EM (SPA) structure of human Nup155 C-terminus (864-1337) at 5.3 Angstroms resolution Deposited 2021-05-30	Different construct Different oligomeric state Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 864–1391（528 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；Buffer was freshly made. cryo-EM vitrification conditions Cryogen ETHANE；Blot for 3 seconds before plunging	Resolution 5.30 Å
7EYQ Cryo-EM (SPA) structure of human Nup155 Longer N-terminus (19-1069) at 5.4 Angstrom resolution Deposited 2021-05-31	Different construct Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–1391（1391 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；Buffer was freshly made. cryo-EM vitrification conditions Cryogen ETHANE；Blot for 3 seconds before plunging	Resolution 5.40 Å
7PER Model of the inner ring of the human nuclear pore complex Deposited 2021-08-11	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 192 PDB declaration: 192-meric	Chain E 1–1391（1391 aa） Chain K 1–1391（1391 aa） Chain Q 1–1391（1391 aa） Chain W 1–1391（1391 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE；Cells were grown on holey carbon, Au-mesh supports. Grids were rinsed briefly with PBS and manually blotted before plunging into liquid ethane.	Resolution 35.00 Å
7R1Y cryoEM structure of human Nup155 (residues 19-981) Deposited 2022-02-03	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–1391（1390 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
7R5J Human nuclear pore complex (dilated) Deposited 2022-02-10	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 808 PDB declaration: 808-meric	Chain D0 1–1391（1391 aa） Chain D1 1–1391（1391 aa） Chain D2 1–1391（1391 aa） Chain D3 1–1391（1391 aa） Chain D4 1–1391（1391 aa） Chain D5 1–1391（1391 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 50.00 Å
7R5K Human nuclear pore complex (constricted) Deposited 2022-02-10	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 808 PDB declaration: 808-meric	Chain D0 1–1391（1391 aa） Chain D1 1–1391（1391 aa） Chain D2 1–1391（1391 aa） Chain D3 1–1391（1391 aa） Chain D4 1–1391（1391 aa） Chain D5 1–1391（1391 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 12.00 Å

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

View Construct and Data Evidence

UniProt name	NU155_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 252–1114； UniProt 1–863

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	7eye
Deposition date deposition_date	2021-05-30
Structure title title	Cryo-EM (SPA) structure of Nup155 N-terminus (19-863) at 5.1 Angstrom resolution
Keywords keywords	Human Nucleoporin 155, NUCLEAR PROTEIN; NUCLEAR PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	29.36 Å
Radius of gyration Rg (electron density) rg_electron	28.60 Å
Forward intensity I(0) i0	93464200.00
Molecular weight molecular_weight	77199.0 kDa
Excluded volume excluded_volume	97208 Å³
Envelope volume envelope_volume	126400 Å³
Hydration-shell volume shell_volume	36504 Å³
Envelope diameter envelope_diameter	101.6 Å
Shell Rg shell_rg	36.15 Å
Envelope Rg envelope_rg	28.70 Å
Shape Rg shape_rg	28.61 Å
Total Rg total_rg	29.29 Å
Total atoms total_atoms	5426
Residues n_residues	696
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	91.8 Å
Rg (real space) rg_real	29.29 Å
Rg uncertainty (real space) rg_real_error	0.61 Å
I(0) (real space) i0_real	9.3460e+07
I(0) uncertainty (real space) i0_real_error	1.4970e+06
Rg (reciprocal space) rg_reciprocal	29.32 Å
I(0) (reciprocal space) i0_reciprocal	93470000.0000
Solution quality estimate total_estimate	0.7256
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	35.7 Å
Skewness Skewness skewness	0.230
Kurtosis Kurtosis kurtosis	-0.498
Angular range angular_range	— – 0.2700 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	21950000.0000
Real-space data points n_real_points	55
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.949; Stabil: 1.000; Sysdev: 0.218; Positv: 1.000; Valcen: 0.999; Smooth: 0.928

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Description description	G protein/GFP fusion protein,Nuclear pore complex protein Nup155
Molecular weight formula_weight	122962.1 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	5426

MVSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKNGIKVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSALSKDPNEKRDHMVLLEFVTAAGITLGMDELYKSGLRSRAQASNSMPSSLLGAAMPASTSAAALQEALENAGRLIDRQLQEDRMYPDLSELLMVSAPNNPTVSGMSDMDYPLQGPGLLSVPNLPEISSIRRVPLPPELVEQFGHMQCNCMMGVFPPISRAWLTIDSDIFMWNYEDGGDLAYFDGLSETILAVGLVKPKAGIFQPHVRHLLVLATPVDIVILGLSYANLQTGSGVLNDSLSGGMQLLPDPLYSLPTDNTYLLTITSTDNGRIFLAGKDGCLYEVAYQAEAGWFSQRCRKINHSKSSLSFLVPSLLQFTFSEDDPILQIAIDNSRNILYTRSEKGVIQVYDLGQDGQGMSRVASVSQNAIVSAAGNIARTIDRSVFKPIVQIAVIENSESLDCQLLAVTHAGVRLYFSTCPFRQPLARPNTLTLVHVRLPPGFSASSTVEKPSKVHRALYSKGILLMAASENEDNDILWCVNHDTFPFQKPMMETQMTAGVDGHSWALSAIDELKVDKIITPLNKDHIPITDSPVVVQQHMLPPKKFVLLSAQGSLMFHKLRPVDQLRHLLVSNVGGDGEEIERFFKLHQEDQACATCLILACSTAACDREVSAWATRAFFRYGGEAQMRFPTTLPPPSNVGPILGSPVYSSSPVPSGSPYPNPSFLGTPSHGIQPPAMSTPVCALGNPATQATNMSCVTGPEIVYSGKHNGICIYFSRIMGNIWDASLVVERIFKSGNREITAIESSVPCQLLESVLQELKGLQEFLDRNSQFAGGPLGNPNTTAKVQQRLIGFMRPENGNPQQMQQELQRKFHEAQLSEKISLQAIQQLVRKSYQALALWKLLCEHQFTIIVAELQKELQEQLKITTFKDLVIRDKELTGALIASLINCYIRDNAAVDGISLHLQDIC

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	Homo sapiens

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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	—

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

Resolution resolution	5.10 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	88595

fit	/app/data/saxs_computation/ey/7eye/7eye.fit
pddf	/app/data/pr_computation/ey/7eye/7eye.pr.out
profile	/app/data/saxs_computation/ey/7eye/7eye.dat

Cryo-EM (SPA) structure of Nup155 N-terminus (19-863) at 5.1 Angstrom resolution

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

G protein/GFP fusion protein,Nuclear pore complex protein Nup155

State in the Current Structure

Other States of the Same Protein in the Database

G protein/GFP fusion protein,Nuclear pore complex protein Nup155

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)