SAXSdb — 8yue

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

Protein claret segregational

Drosophila melanogaster

UniProt P20480

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 293–680 Chain B； UniProt 293–680	Mutation：Y485K	ADP ADENOSINE-5'-DIPHOSPHATE × 2 PO4 PHOSPHATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；296 K；0.5M NaCl, 50mM NaPi, pH6.8, 7mM DTT, 13% PEG 8000	Resolution 3.15 Å R-free 0.295

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 8YUE	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1CZ7 THE CRYSTAL STRUCTURE OF A MINUS-END DIRECTED MICROTUBULE MOTOR PROTEIN NCD REVEALS VARIABLE DIMER CONFORMATIONS Deposited 1999-09-01	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 295–700（406 aa） Fragment：CONSTRUCT MC5 FROM NCD Chain B 295–700（406 aa） Fragment：CONSTRUCT MC5 FROM NCD	Not recorded	MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.2；292 K；PEG 4000, NACL, MGCL2, K3PO4, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 2.90 Å R-free 0.294
1CZ7 THE CRYSTAL STRUCTURE OF A MINUS-END DIRECTED MICROTUBULE MOTOR PROTEIN NCD REVEALS VARIABLE DIMER CONFORMATIONS Deposited 1999-09-01	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 295–700（406 aa） Fragment：CONSTRUCT MC5 FROM NCD Chain D 295–700（406 aa） Fragment：CONSTRUCT MC5 FROM NCD	Not recorded	MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.2；292 K；PEG 4000, NACL, MGCL2, K3PO4, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 2.90 Å R-free 0.294
1CZ7 THE CRYSTAL STRUCTURE OF A MINUS-END DIRECTED MICROTUBULE MOTOR PROTEIN NCD REVEALS VARIABLE DIMER CONFORMATIONS Deposited 1999-09-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain C 295–700（406 aa） Fragment：CONSTRUCT MC5 FROM NCD Chain D 295–700（406 aa） Fragment：CONSTRUCT MC5 FROM NCD	Not recorded	MG MAGNESIUM ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.2；292 K；PEG 4000, NACL, MGCL2, K3PO4, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 2.90 Å R-free 0.294
1N6M Rotation of the stalk/neck and one head in a new crystal structure of the kinesin motor protein, Ncd Deposited 2002-11-11	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 293–700（408 aa） Fragment：NCD Chain B 293–700（408 aa） Fragment：NCD	Mutation：N600K Mutation：N600K	MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.8；291 K；PEG 8000, NaCl, Sodium Phosphate, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 2.50 Å R-free 0.302
1N6M Rotation of the stalk/neck and one head in a new crystal structure of the kinesin motor protein, Ncd Deposited 2002-11-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 293–700（408 aa） Fragment：NCD Chain B 293–700（408 aa） Fragment：NCD	Mutation：N600K Mutation：N600K	MG MAGNESIUM ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.8；291 K；PEG 8000, NaCl, Sodium Phosphate, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 2.50 Å R-free 0.302
2NCD NCD (NON-CLARET DISJUNCTIONAL) DIMER FROM D. MELANOGASTER Deposited 1999-06-04	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 281–700（420 aa） Fragment：RESIDUES 281-700	Not recorded	SO4 SULFATE ION × 8 ADP ADENOSINE-5'-DIPHOSPHATE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；THE MOTHER LIQUOR CONTAINED PROTEIN AT ABOUT 20 MG/ML, 2 MM ADP, 10 MM MGCL2, 100 MM NACL, 700 MM LI2SO4, 1 MM EGTA, AND 1 MM DTT IN 20 MM HEPES, PH 7.5. THE RESERVOIR WAS 1.4 M LI2SO4, 10 MM MGCL2, 1 MM EGTA, 1 MM DTT IN 20 MM HEPES, PH 7.5., VAPOR DIFFUSION, HANGING DROP	Resolution 2.50 Å R-free 0.270
3L1C Kinesin-14 Protein Ncd, T436S Mutant Deposited 2009-12-11	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 293–674（382 aa） Fragment：residues 293-674 Chain B 293–674（382 aa） Fragment：residues 293-674	Mutation：T436S Mutation：T436S	MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.75 Å R-free 0.292
3U06 Crystal structure of the kinesin-14 NcdG347D Deposited 2011-09-28	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 293–700（408 aa） Fragment：unp residues 293-700 Chain B 293–700（408 aa） Fragment：unp residues 293-700	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 1 GOL GLYCEROL × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；288 K；Bis-Tris propane, Na2SO4, PEG3350, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 288K	Resolution 2.35 Å R-free 0.250
5HLE Structural basis of backwards motion in kinesin-14: minus-end directed nKn664 in the ADP state Deposited 2016-01-14	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 325–348（24 aa） Chain A 664–700（37 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；PEG 3350, Ammonium sulfate, HEPES Benzamidine-HCl, ADP	Resolution 2.90 Å R-free 0.287
5HNW Structural basis of backwards motion in kinesin-14: minus-end directed nKn664 in the AMPPNP state Deposited 2016-01-19	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 × 3 PDB declaration: trimeric	Chain K 325–348（24 aa） Fragment：UNP RESIDUES 325-348, 664-700 Chain K 664–700（37 aa） Fragment：UNP RESIDUES 325-348, 664-700	Not recorded	MG MAGNESIUM ION × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 TA1 TAXOL × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.60 Å
5HNX Structural basis of backwards motion in kinesin-14: minus-end directed nKn664 in the nucleotide-free state Deposited 2016-01-19	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 × 3 PDB declaration: trimeric	Chain K 325–348（24 aa） Fragment：UNP residues 325-348,UNP residues 664-700 Chain K 664–700（37 aa） Fragment：UNP residues 325-348,UNP residues 664-700	Not recorded	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 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.60 Å
5HNY Structural basis of backwards motion in kinesin-14: plus-end directed nKn669 in the AMPPNP state Deposited 2016-01-19	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 × 3 PDB declaration: trimeric	Chain K 325–348（24 aa） Fragment：UNP residues 325-348, UNP residues 664-700 Chain K 669–700（32 aa） Fragment：UNP residues 325-348, UNP residues 664-700	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 1 TA1 TAXOL × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.30 Å
5HNZ Structural basis of backwards motion in kinesin-14: plus-end directed nKn669 in the nucleotide-free state Deposited 2016-01-19	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 × 3 PDB declaration: trimeric	Chain K 325–348（24 aa） Fragment：UNP residues 325-348,UNP residues 664-700 Chain K 669–700（32 aa） Fragment：UNP residues 325-348,UNP residues 664-700	Not recorded	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 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 5.80 Å
5W3D The structure of kinesin-14 wild-type Ncd-ADP dimer Deposited 2017-06-07	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 293–700（408 aa） Chain B 293–700（408 aa）	Not recorded	MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.8；291 K；50 mM sodium phosphate, 7 mM dithiothreitol, 10 mM magnesium chloride, 700 mM sodium chloride, 13% PEG8000 (w/v)	Resolution 2.79 Å R-free 0.280
8YY2 Kinesin-14 in nucleotide-free state bound to 13 PF Microtubule Deposited 2024-04-03	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 × 4 PDB declaration: tetrameric	Chain C 292–700（409 aa） Chain D 292–700（409 aa）	Mutation：E292M, Y485K, N697S Mutation：E292M, Y485K, N697S	GTP GUANOSINE-5'-TRIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8；100 mM PIPES pH 6.8, 1 mM MgCl2, 1 mM EGTA, and 1 mM GTP cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å
8YY3 Kinesin-14 in nucleotide-free state bound to 14 PF Microtubule Deposited 2024-04-03	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 × 4 PDB declaration: tetrameric	Chain C 292–700（409 aa） Chain D 292–700（409 aa）	Mutation：E292M, Y485K, N697S Mutation：E292M, Y485K, N697S	GTP GUANOSINE-5'-TRIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8；100 mM PIPES pH 6.8, 1 mM MgCl2, 1 mM EGTA, and 1 mM GTP cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.24 Å
8YY4 Kinesin-14 with AlF3 bound to 13 PF Microtubule Deposited 2024-04-03	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 × 4 PDB declaration: tetrameric	Chain C 292–700（409 aa） Chain D 292–700（409 aa）	Mutation：E292M, Y485K, N697S Mutation：E292M, Y485K, N697S	GTP GUANOSINE-5'-TRIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ALF TETRAFLUOROALUMINATE ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8；100 mM PIPES pH 6.8, 1 mM MgCl2, 1 mM EGTA, 1 mM GTP, 2 mM ADP, 2 mM AlCl3, and 8 mM NaF cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.02 Å
8YY5 Kinesin-14 with AlF3 bound to 14 PF Microtubule Deposited 2024-04-03	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 × 4 PDB declaration: tetrameric	Chain C 292–700（409 aa） Chain D 292–700（409 aa）	Mutation：E292M, Y485K, N697S Mutation：E292M, Y485K, N697S	GTP GUANOSINE-5'-TRIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ALF TETRAFLUOROALUMINATE ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8；100 mM PIPES pH 6.8, 1 mM MgCl2, 1 mM EGTA, 1 mM GTP, 2 mM ADP, 2 mM AlCl3, and 8 mM NaF cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.99 Å

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

View Construct and Data Evidence

UniProt name	NCD_DROME
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–390； UniProt 293–680 Author chain B； PDBConstruct 3–390； UniProt 293–680

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	8yue
Deposition date deposition_date	2024-03-27
Structure title title	Crystal structure of the kinesin-14 motor protein from Drosophila melanogaster
Keywords keywords	Kinesin-related, Microtubule motor protein, Spindle motor, MOTOR PROTEIN; MOTOR 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	33.03 Å
Radius of gyration Rg (electron density) rg_electron	32.36 Å
Forward intensity I(0) i0	120840000.00
Molecular weight molecular_weight	82907.0 kDa
Excluded volume excluded_volume	101960 Å³
Envelope volume envelope_volume	132860 Å³
Hydration-shell volume shell_volume	35101 Å³
Envelope diameter envelope_diameter	116.2 Å
Shell Rg shell_rg	38.11 Å
Envelope Rg envelope_rg	32.24 Å
Shape Rg shape_rg	32.34 Å
Total Rg total_rg	32.90 Å
Total atoms total_atoms	5793
Residues n_residues	721
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	108.1 Å
Rg (real space) rg_real	33.03 Å
Rg uncertainty (real space) rg_real_error	0.87 Å
I(0) (real space) i0_real	1.2080e+08
I(0) uncertainty (real space) i0_real_error	1.8370e+06
Rg (reciprocal space) rg_reciprocal	33.04 Å
I(0) (reciprocal space) i0_reciprocal	120800000.0000
Solution quality estimate total_estimate	0.8967
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	33.8 Å
Skewness Skewness skewness	0.254
Kurtosis Kurtosis kurtosis	-0.581
Angular range angular_range	— – 0.2400 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	13820000.0000
Real-space data points n_real_points	49
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.920; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.963; Smooth: 0.929

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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	Protein claret segregational
Molecular weight formula_weight	44456.4 kDa
EC 编号 ec_number	3.6.4.-
Mutation mutation	Y485K
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	5793

SMHAALSTEVVHLRQRTEELLRCNEQQAAELETCKEQLFQSNMERKELHNTVMDLRGNIRVFCRIRPPLESEENRMCCTWTYHDESTVELQSIDAQAKSKMGQQIFSFDQVFHPLSSQSDIFEMVSPLIQSALDGYNICIFAYGQTGSGKTYTMDGVPESVGVIPRTVDLLFDSIRGYRNLGWEYEIKATFLEIKNEVLYDLLSNEQKDMEIRMAKNNKNDIYVSNITEETVLDPNHLRHLMHTAKMNRATASTAGNERSSRSHAVTKLELIGRHAEKQEISVGSINLVDLAGSESPKTSTRMTETKNINRSLSELTNVILALLQKQDHIPYRNSKLTHLLMPSLGGNSKTLMFINVSPFQDCFQESVKSLRFAASVNSCKMTKAKRNRY

来源 Source

来源生物 organism	Drosophila melanogaster
通用名 common_name	fruit fly
NCBI Class编号 ncbi_taxonomy_id	7227
宿主生物 host_organism	;Escherichia coli 'BL21-Gold(DE3)pLysS AG' ;

Entity 2 Entity 2 non-polymer

Description description	ADENOSINE-5'-DIPHOSPHATE
Molecular weight formula_weight	427.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	PHOSPHATE ION
Molecular weight formula_weight	95.0 kDa
Source method src_method	syn
Copy count entity_count	4

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8. Citations (1)

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Unit-cell length a length_a	164.506 Å
Unit-cell length b length_b	67.617 Å
Unit-cell length c length_c	94.196 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	96.99 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	3.150 Å
Low-resolution limit resolution_low	46.750 Å
R factor r_factor	0.2532
R_work r_work	0.2510
R_free r_free	0.2947

fit	/app/data/saxs_computation/yu/8yue/8yue.fit
pddf	/app/data/pr_computation/yu/8yue/8yue.pr.out
profile	/app/data/saxs_computation/yu/8yue/8yue.dat

Crystal structure of the kinesin-14 motor protein from Drosophila melanogaster

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

Protein claret segregational

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