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2v1n

SOLUTION STRUCTURE OF THE REGION 51-160 OF HUMAN KIN17 REVEALS A WINGED HELIX FOLD

Method: SOLUTION NMR Dmax: 42.8 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

PROTEIN KIN HOMOLOG

HOMO SAPIENS

UniProt O60870

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 51–160 Fragment：RESIDUES 51-160 No other associated polymer SOLUTION NMR NMR measurement conditions：pH 6；303 K；Ionic strength (raw mmCIF value) 50MM PHOSPHATE , 150MM NACL NMR measurement conditions：pH 6；303 K；Ionic strength (raw mmCIF value) 50MM PHOSPHATE , 150MM NACL NMR sample composition：90%WATER / 10%D2O Resolution not provided

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 2V1N Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2CKK High resolution crystal structure of the human kin17 C-terminal domain containing a kow motif Deposited 2006-04-20 Different construct 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 268–393（126 aa） Fragment：C-TERMINAL DOMAIN, RESIDUES 268-393
Not recorded IOD IODIDE ION × 12 ACT ACETATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.3；290 K；VAPOR DIFFUSION, SITTING DROP 10% ETHYLENE GLYCOL, 27% PEG 6000, 500 MM LICL, 100 MM SODIUM ACETATE PH 6.3 290 K
Resolution 1.45 Å R-free 0.175
7ABH Human pre-Bact-2 spliceosome (SF3b/U2 snRNP portion) Deposited 2020-09-07 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein–RNA Heteromer；Protein × 14 PDB declaration: hexadecameric
Chain 7 1–393（393 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.9
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.50 Å
7ABI Human pre-Bact-2 spliceosome Deposited 2020-09-07 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein–RNA Heteromer；Protein × 52 PDB declaration: 56-meric
Chain 7 1–393（393 aa）
Not recorded GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 IHP INOSITOL HEXAKISPHOSPHATE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.9
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 8.00 Å
8I0P The cryo-EM structure of human pre-Bact complex Deposited 2023-01-11 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein–RNA Heteromer；Protein × 47 PDB declaration: 51-meric
Chain K 1–393（393 aa）
Not recorded GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.9
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å
9COJ SH3-like tandem domain of human KIN protein Deposited 2024-07-16 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 268–393（126 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；298.4 K；Ionic strength (raw mmCIF value) 50 mM NaPi, 100 mM NaCl；Pressure 1
NMR sample composition 500 uM [U-13C; U-15N] SH3-like tandem domain of human KIN protein, 0.5 mM PMSF, 3 mM EDTA, 0.02 % v/v sodium azide, 0.33 mM 98% 2H DSS, 95% H2O/5% D2O | 95% H2O/5% D2O
Resolution not provided

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

View Construct and Data Evidence
UniProt name O60870_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 2–111； UniProt 51–160

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.

SAXS scattering curve SAXS Profile

SAXS profile for 2v1n

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2v1n
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2v1n
Deposition date deposition_date2007-05-27
Structure title titleSOLUTION STRUCTURE OF THE REGION 51-160 OF HUMAN KIN17 REVEALS A WINGED HELIX FOLD
Keywords keywordsKIN17, NUCLEAR PROTEIN, WINGED HELIX MOTIF; NUCLEAR PROTEIN
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier15.96 Å
Radius of gyration Rg (electron density) rg_electron15.76 Å
Forward intensity I(0) i0393601000.00
Molecular weight molecular_weight163770.0 kDa
Excluded volume excluded_volume203870 ų
Envelope volume envelope_volume48170 ų
Hydration-shell volume shell_volume19384 ų
Envelope diameter envelope_diameter79.8 Å
Shell Rg shell_rg27.84 Å
Envelope Rg envelope_rg23.07 Å
Shape Rg shape_rg15.69 Å
Total Rg total_rg16.43 Å
Total atoms total_atoms22848
Residues n_residues1332
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax42.8 Å
Rg (real space) rg_real14.86 Å
Rg uncertainty (real space) rg_real_error0.06 Å
I(0) (real space) i0_real3.7340e+08
I(0) uncertainty (real space) i0_real_error3.1210e+06
Rg (reciprocal space) rg_reciprocal16.11 Å
I(0) (reciprocal space) i0_reciprocal393600000.0000
Solution quality estimate total_estimate0.6822
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary18.4 Å
Skewness Skewness skewness0.287
Kurtosis Kurtosis kurtosis-0.271
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha3.8880
Highest regularization parameter α highest_alpha369200.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.009; Oscil: 0.974; Stabil: 0.983; Sysdev: 0.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2v1nA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily2030 — DNA/RNA-binding protein Kin17, conserved domain
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8. Citations (1)

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9. Files and Curves (10)