SAXSdb — 2ve7

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

KINETOCHORE PROTEIN HEC1, KINETOCHORE PROTEIN SPC25

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 Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 80–286	Fragment：CHIMERA OF NDC80 RESIDUES 80-286 WITH SPC25 RESIDUES 118-224	KINETOCHORE PROTEIN NUF2, KINETOCHORE PROTEIN SPC24 × 1 （Q9BZD4,Q8NBT2） GOL GLYCEROL × 1 IPH PHENOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 7.5；4.5-6.5 PEG 6000, 1.5-2 MPD, 0.1 M NAHEPES PH 7.5, 16 MM TCEP, 15 MM PHENOL	Resolution 2.88 Å R-free 0.261
2	Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 80–286	Fragment：CHIMERA OF NDC80 RESIDUES 80-286 WITH SPC25 RESIDUES 118-224	KINETOCHORE PROTEIN NUF2, KINETOCHORE PROTEIN SPC24 × 1 （Q9BZD4,Q8NBT2） GOL GLYCEROL × 1 IPH PHENOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 7.5；4.5-6.5 PEG 6000, 1.5-2 MPD, 0.1 M NAHEPES PH 7.5, 16 MM TCEP, 15 MM PHENOL	Resolution 2.88 Å R-free 0.261

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 2VE7	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2IGP Crystal Structure of Hec1 CH domain Deposited 2006-09-22	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 81–196（116 aa）	Not recorded	BME BETA-MERCAPTOETHANOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；291 K；0.1 M cacodylate, pH 6.5, 22-30% PEG 8K, 0.2 M (NH4)2SO4, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 1.80 Å R-free 0.231
8G0P Crystal structure of the human Ndc80:Nuf2 loop region Deposited 2023-02-01	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 370–509（140 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；20% (w/v) polyethylene glycol 4000, 0.1 M TRIS pH 8.6, and 0.2 M magnesium chloride	Resolution 2.00 Å R-free 0.297
9N9G Cryo-EM structure of the human Hec1-Nuf2 dimer bound to the paclitaxel-stabilized microtubule Deposited 2025-02-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain 1 1–642（642 aa） Chain N 1–642（642 aa） Chain n 1–642（642 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 4 GDP GUANOSINE-5'-DIPHOSPHATE × 2 TA1 TAXOL × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	KNTC2_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–208； UniProt 80–286 Author chain B； PDBConstruct 2–208； UniProt 80–286

KINETOCHORE PROTEIN HEC1, KINETOCHORE PROTEIN SPC25

HOMO SAPIENS

UniProt Q9HBM1

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 Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 118–224	Fragment：CHIMERA OF NDC80 RESIDUES 80-286 WITH SPC25 RESIDUES 118-224	KINETOCHORE PROTEIN NUF2, KINETOCHORE PROTEIN SPC24 × 1 （Q9BZD4,Q8NBT2） GOL GLYCEROL × 1 IPH PHENOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 7.5；4.5-6.5 PEG 6000, 1.5-2 MPD, 0.1 M NAHEPES PH 7.5, 16 MM TCEP, 15 MM PHENOL	Resolution 2.88 Å R-free 0.261
2	Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 118–224	Fragment：CHIMERA OF NDC80 RESIDUES 80-286 WITH SPC25 RESIDUES 118-224	KINETOCHORE PROTEIN NUF2, KINETOCHORE PROTEIN SPC24 × 1 （Q9BZD4,Q8NBT2） GOL GLYCEROL × 1 IPH PHENOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 7.5；4.5-6.5 PEG 6000, 1.5-2 MPD, 0.1 M NAHEPES PH 7.5, 16 MM TCEP, 15 MM PHENOL	Resolution 2.88 Å R-free 0.261

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 2VE7	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3IZ0 Human Ndc80 Bonsai Decorated Microtubule Deposited 2010-08-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric	Chain C 118–224（107 aa） Chain E 118–224（107 aa）	Not recorded	ZN ZINC ION × 1 MG MAGNESIUM ION × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 TA1 TAXOL × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8；80mM PIPES, 1mM MgCl2, 1mM EGTA, 1mM DTT, 0.05% Nonidet P-40, 20uM taxol cryo-EM vitrification conditions 2ul of 0.25 mg per ml MTs applied to grid for 1 minute 4ul of 0.7 mg per ml Ndc80 bonsai added, 1 minute manually blotted, then another 4ul of Ndc80 applied 1 minute 2ul removed with pipetter Blot for 2 seconds before plunging, 0mm offset；Cryogen ETHANE	Resolution 8.60 Å
8PPR Structure of the human outer kinetochore KMN network complex Deposited 2023-07-08	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain G 1–224（224 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
8Q5H Human KMN network (outer kinetochore) Deposited 2023-08-09	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric	Chain 5 93–224（132 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.50 Å

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	SPC25_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 209–315； UniProt 118–224 Author chain B； PDBConstruct 209–315； UniProt 118–224

KINETOCHORE PROTEIN NUF2, KINETOCHORE PROTEIN SPC24

HOMO SAPIENS

UniProt Q8NBT2

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 Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 122–197	Fragment：CHIMERA OF NUF2 RESIDUES 1-169 WITH SPC24 RESIDUES 122-197 Mutation：YES	KINETOCHORE PROTEIN HEC1, KINETOCHORE PROTEIN SPC25 × 1 （O14777,Q9HBM1） GOL GLYCEROL × 1 IPH PHENOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 7.5；4.5-6.5 PEG 6000, 1.5-2 MPD, 0.1 M NAHEPES PH 7.5, 16 MM TCEP, 15 MM PHENOL	Resolution 2.88 Å R-free 0.261
2	Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain D； UniProt 122–197	Fragment：CHIMERA OF NUF2 RESIDUES 1-169 WITH SPC24 RESIDUES 122-197 Mutation：YES	KINETOCHORE PROTEIN HEC1, KINETOCHORE PROTEIN SPC25 × 1 （O14777,Q9HBM1） GOL GLYCEROL × 1 IPH PHENOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 7.5；4.5-6.5 PEG 6000, 1.5-2 MPD, 0.1 M NAHEPES PH 7.5, 16 MM TCEP, 15 MM PHENOL	Resolution 2.88 Å R-free 0.261

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 2VE7	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
8PPR Structure of the human outer kinetochore KMN network complex Deposited 2023-07-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain F 1–197（197 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
8Q5H Human KMN network (outer kinetochore) Deposited 2023-08-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric	Chain 4 110–197（88 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.50 Å

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	SPC24_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 175–250； UniProt 122–197 Author chain D； PDBConstruct 175–250； UniProt 122–197

KINETOCHORE PROTEIN NUF2, KINETOCHORE PROTEIN SPC24

HOMO SAPIENS

UniProt Q9BZD4

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 Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 1–169	Fragment：CHIMERA OF NUF2 RESIDUES 1-169 WITH SPC24 RESIDUES 122-197 Mutation：YES	KINETOCHORE PROTEIN HEC1, KINETOCHORE PROTEIN SPC25 × 1 （O14777,Q9HBM1） GOL GLYCEROL × 1 IPH PHENOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 7.5；4.5-6.5 PEG 6000, 1.5-2 MPD, 0.1 M NAHEPES PH 7.5, 16 MM TCEP, 15 MM PHENOL	Resolution 2.88 Å R-free 0.261
2	Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain D； UniProt 1–169	Fragment：CHIMERA OF NUF2 RESIDUES 1-169 WITH SPC24 RESIDUES 122-197 Mutation：YES	KINETOCHORE PROTEIN HEC1, KINETOCHORE PROTEIN SPC25 × 1 （O14777,Q9HBM1） GOL GLYCEROL × 1 IPH PHENOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 7.5；4.5-6.5 PEG 6000, 1.5-2 MPD, 0.1 M NAHEPES PH 7.5, 16 MM TCEP, 15 MM PHENOL	Resolution 2.88 Å R-free 0.261

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 2VE7	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
8G0P Crystal structure of the human Ndc80:Nuf2 loop region Deposited 2023-02-01	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 B 252–347（96 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；20% (w/v) polyethylene glycol 4000, 0.1 M TRIS pH 8.6, and 0.2 M magnesium chloride	Resolution 2.00 Å R-free 0.297
9N9G Cryo-EM structure of the human Hec1-Nuf2 dimer bound to the paclitaxel-stabilized microtubule Deposited 2025-02-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain F 1–464（464 aa） Chain f 1–464（464 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 4 GDP GUANOSINE-5'-DIPHOSPHATE × 2 TA1 TAXOL × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	NUF2_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 6–174； UniProt 1–169 Author chain D； PDBConstruct 6–174； UniProt 1–169

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	2ve7
Deposition date deposition_date	2007-10-17
Structure title title	Crystal structure of a bonsai version of the human Ndc80 complex
Keywords keywords	MITOSIS, CENTROMERE, CELL CYCLE, MICROTUBULE, KINETOCHORE, CELL DIVISION, CALPONIN HOMOLOGY; CELL CYCLE
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	65.73 Å
Radius of gyration Rg (electron density) rg_electron	67.72 Å
Forward intensity I(0) i0	192282000.00
Molecular weight molecular_weight	116960.0 kDa
Excluded volume excluded_volume	147420 Å³
Envelope volume envelope_volume	285670 Å³
Hydration-shell volume shell_volume	43187 Å³
Envelope diameter envelope_diameter	236.3 Å
Shell Rg shell_rg	48.57 Å
Envelope Rg envelope_rg	69.07 Å
Shape Rg shape_rg	67.82 Å
Total Rg total_rg	66.62 Å
Total atoms total_atoms	8236
Residues n_residues	1010
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	220.3 Å
Rg (real space) rg_real	67.37 Å
Rg uncertainty (real space) rg_real_error	2.73 Å
I(0) (real space) i0_real	1.9230e+08
I(0) uncertainty (real space) i0_real_error	4.1120e+06
Rg (reciprocal space) rg_reciprocal	64.25 Å
I(0) (reciprocal space) i0_reciprocal	191200000.0000
Solution quality estimate total_estimate	0.6562
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	3
Primary peak position r_peak_primary	36.7 Å
Skewness Skewness skewness	0.478
Kurtosis Kurtosis kurtosis	-0.657
Angular range angular_range	— – 0.1200 Å⁻¹
Current regularization parameter α current_alpha	0.0003
Highest regularization parameter α highest_alpha	6097000.0000
Real-space data points n_real_points	25
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.358; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.266; Smooth: 0.190

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	KINETOCHORE PROTEIN HEC1, KINETOCHORE PROTEIN SPC25
Molecular weight formula_weight	36351.3 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	8258

MIKDPRPLNDKAFIQQCIRQLCEFLTENGYAHNVSMKSLQAPSVKDFLKIFTFLYGFLCPSYELPDTKFEEEVPRIFKDLGYPFALSKSSMYTVGAPHTWPHIVAALVWLIDCIKIHTAMKESSPLFDDGQPWGEETEDGIMHNKLFLDYTIKCYESFMSGADSFDEMNAELQSKLKDLFNVDAFKLESLEAKNRALNEQIARLEQERSTANKANAERLKRLQKSADLYKDRLGLEIRKIYGEKLQFIFTNIDPKNPESPFMFSLHLNEARDYEVSDSAPHLEGLAEFQENVRKTNNFSAFLANVRKAFTATVYQ

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 2 Entity 2 polymer

Description description	KINETOCHORE PROTEIN NUF2, KINETOCHORE PROTEIN SPC24
Molecular weight formula_weight	28993.4 kDa
Mutation mutation	YES
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,D

GPLGSMETLSFPRYNVAEIVIHIRNKILTGADGKNLTKNDLYPNPKPEVLHMIYMRALQIVYGIRLEHFYMMPVNSGVMYPHLMEGFLPFSNLVTHLDSFLPICRVNDFETADILCPKAKRTSRFLSGIINFIHFREACRETYMEFLWQYKSSADKMQQLNAAHQEALMKLERLEKEVDEDTTVTIPSAVYVAQLYHQVSKIEWEYECEPGMVKGIHHGPSVAQPIHLDSTQLSRKFISDYLWSLVDTEW

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 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

Description description	PHENOL
Molecular weight formula_weight	94.1 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	22

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7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id	2ve7A01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	418 — Actin-binding Protein, T-fimbrin; domain 1
Homologous superfamily homologous superfamily	30 — Ncd80 complex, Ncd80 subunit

Domain ID domain_id	2ve7A02
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	250 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	1950 —

Domain ID domain_id	2ve7B01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	418 — Actin-binding Protein, T-fimbrin; domain 1
Homologous superfamily homologous superfamily	30 — Ncd80 complex, Ncd80 subunit

Domain ID domain_id	2ve7C01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	418 — Actin-binding Protein, T-fimbrin; domain 1
Homologous superfamily homologous superfamily	60 — Ncd80 complex, Nuf2 subunit

Domain ID domain_id	2ve7C02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	160 — Double Stranded RNA Binding Domain
Homologous superfamily homologous superfamily	570 — Ncd80 complex, Spc24 subunit

Domain ID domain_id	2ve7D01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	418 — Actin-binding Protein, T-fimbrin; domain 1
Homologous superfamily homologous superfamily	60 — Ncd80 complex, Nuf2 subunit

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8. Citations (1)

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Unit-cell length a length_a	157.653 Å
Unit-cell length b length_b	248.965 Å
Unit-cell length c length_c	58.250 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 2
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	2.880 Å
Low-resolution limit resolution_low	50.000 Å
R factor r_factor	0.2340
R_work r_work	0.2320
R_free r_free	0.2610

fit	/app/data/saxs_computation/ve/2ve7/2ve7.fit
pddf	/app/data/pr_computation/ve/2ve7/2ve7.pr.out
profile	/app/data/saxs_computation/ve/2ve7/2ve7.dat

Crystal structure of a bonsai version of the human Ndc80 complex

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

KINETOCHORE PROTEIN HEC1, KINETOCHORE PROTEIN SPC25

State in the Current Structure

Other States of the Same Protein in the Database

KINETOCHORE PROTEIN HEC1, KINETOCHORE PROTEIN SPC25

State in the Current Structure

Other States of the Same Protein in the Database

KINETOCHORE PROTEIN NUF2, KINETOCHORE PROTEIN SPC24

State in the Current Structure

Other States of the Same Protein in the Database

KINETOCHORE PROTEIN NUF2, KINETOCHORE PROTEIN SPC24

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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)