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2yu7

Solution structure of the SHP-1 C-terminal SH2 domain complexed with a tyrosine-phosphorylated peptide from NKG2A

Method: SOLUTION NMR Dmax: 52.0 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Tyrosine-protein phosphatase non-receptor type 6

Homo sapiens

UniProt P29350

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 110–214 Fragment：SH2 domain natural killer group 2A × 1 （P26715） SOLUTION NMR NMR measurement conditions：pH 7.4；296 K；Ionic strength (raw mmCIF value) 120mM；Pressure ambient NMR measurement conditions：pH 7.4；298 K；Ionic strength (raw mmCIF value) 120mM；Pressure ambient NMR sample composition：0.89mM SHP1 SH2 domain U-15N,13C; 0.89mM NKG2A peptide; 20mM d-Tris-HCl (pH 7.4); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 90% H2O, 10% D2O | 90% H2O/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 2YU7 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1FPR CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN THE CATALYTIC DOMAIN OF SHP-1 AND AN IN VITRO PEPTIDE SUBSTRATE PY469 DERIVED FROM SHPS-1. Deposited 2000-08-31 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 243–526（284 aa） Fragment：CATALYTIC DOMAIN
Mutation：C455S No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；277 K；ammonium sulfate, pH 8.5, VAPOR DIFFUSION, temperature 277K
Resolution 2.50 Å R-free 0.303
1FPR CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN THE CATALYTIC DOMAIN OF SHP-1 AND AN IN VITRO PEPTIDE SUBSTRATE PY469 DERIVED FROM SHPS-1. Deposited 2000-08-31 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 243–526（284 aa） Fragment：CATALYTIC DOMAIN
Mutation：C455S No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；277 K；ammonium sulfate, pH 8.5, VAPOR DIFFUSION, temperature 277K
Resolution 2.50 Å R-free 0.303
1GWZ CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF THE PROTEIN TYROSINE PHOSPHATASE SHP-1 Deposited 1998-08-22 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 243–541（299 aa） Fragment：CATALYTIC DOMAIN
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；pH 7.5
Resolution 2.50 Å R-free 0.293
1X6C Solution structures of the SH2 domain of human protein-tyrosine phosphatase SHP-1 Deposited 2005-05-17 Different oligomeric state Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 110–214（105 aa） Fragment：SH2 domain
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 120mM；Pressure ambient
NMR sample composition 1mM SH2 domain U-15N, 13C; 20mM d-Tris HCl; 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 10% D2O | 90% H2O/10% D2O
Resolution not provided
2B3O Crystal structure of human tyrosine phosphatase SHP-1 Deposited 2005-09-20 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–532（532 aa） Fragment：SHP-1
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；PEG 800, DTT, HEPES, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 2.80 Å R-free 0.296
2RMX Solution structure of the SHP-1 C-terminal SH2 domain complexed with a tyrosine-phosphorylated peptide from NKG2A Deposited 2007-11-30 Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 110–214（105 aa） Fragment：SH2 domain
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.4；Ionic strength (raw mmCIF value) 120；Pressure ambient
NMR sample composition 0.8mM [U-13C; U-15N] SHP-1 C-terminal SH2 domain; 0.8mM tyrosine-phosphorylated peptide; 20mM [U-2H] TRIS; 100mM sodium chloride; 0.02% sodium azide; 1mM [U-2H] DTT; 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
3PS5 Crystal structure of the full-length Human Protein Tyrosine Phosphatase SHP-1 Deposited 2010-11-30 Different construct 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 1–595（595 aa）
Mutation：C453S SO4 SULFATE ION × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；278 K；2.5 ul of SHP-1 at 3.5 mg/ml in 25mM Tris-HCl, beta-mercaptoethanol, 1mM EDTA mixed with 2.5 ul of 1.8M ammonium sulfate, 0.1M glycine, 0.1M Tris-HCl, with the addition of 0.5 ul 14mM deoxy Big Chap to form the final drop., pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 278K
Resolution 3.10 Å R-free 0.276
3PS5 Crystal structure of the full-length Human Protein Tyrosine Phosphatase SHP-1 Deposited 2010-11-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–595（595 aa）
Mutation：C453S SO4 SULFATE ION × 10 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；278 K；2.5 ul of SHP-1 at 3.5 mg/ml in 25mM Tris-HCl, beta-mercaptoethanol, 1mM EDTA mixed with 2.5 ul of 1.8M ammonium sulfate, 0.1M glycine, 0.1M Tris-HCl, with the addition of 0.5 ul 14mM deoxy Big Chap to form the final drop., pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 278K
Resolution 3.10 Å R-free 0.276
4GRY Crystal structure of SHP1 catalytic domain with SO4 Deposited 2012-08-27 Different construct 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 243–528（286 aa） Fragment：Phosphatase domain UNP Residues 242-528
Mutation：C453S SO4 SULFATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；0.1 M MES pH 6.5, 1.5 M ammonium sulfate, 3% PEG400, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.70 Å R-free 0.231
4GRZ Crystal structure of SHP1 catalytic domain with PO4 Deposited 2012-08-27 Different construct 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 243–528（286 aa） Fragment：Phosphatase domain UNP Residues 242-528
Mutation：C453S PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；0.2 M ammonium phosphate, 12% PEG2000 , pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.37 Å R-free 0.189
4GS0 Crystal structure of SHP1 catalytic domain with JAK1 activation loop peptide Deposited 2012-08-27 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 243–528（286 aa） Fragment：Phosphatase domain (UNP Residues 242-528)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；0.2 M calcium acetate, 13% PEG3350, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.80 Å R-free 0.195
4GS0 Crystal structure of SHP1 catalytic domain with JAK1 activation loop peptide Deposited 2012-08-27 Different construct Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 243–528（286 aa） Fragment：Phosphatase domain (UNP Residues 242-528)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；0.2 M calcium acetate, 13% PEG3350, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.80 Å R-free 0.195
4HJP SHP-1 catalytic domain WPD loop open Deposited 2012-10-13 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 243–528（286 aa） Fragment：Phosphatase domain (UNP Residues 242-528)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；0.1 M HEPES pH 7.5, 1.0 M tri-sodium citrate, 2-4% 1-propanol, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.40 Å R-free 0.186
4HJQ SHP-1 catalytic domain WPD loop closed Deposited 2012-10-13 Different construct 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 243–528（286 aa） Fragment：Phosphatase domain (UNP Residues 242-528)
Mutation：C453S PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；0.1 M HEPES pH7.5, 20 mM MgCl2, 28% sodium polyacrylate 5100 , VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.80 Å R-free 0.202
4HJQ SHP-1 catalytic domain WPD loop closed Deposited 2012-10-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 243–528（286 aa） Fragment：Phosphatase domain (UNP Residues 242-528)
Mutation：C453S PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；0.1 M HEPES pH7.5, 20 mM MgCl2, 28% sodium polyacrylate 5100 , VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.80 Å R-free 0.202
6SM5 MbC/SHP1-C-SH2 complex Deposited 2019-08-21 Different construct Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 100–214（115 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；0.2 M sodium citrate tribasic, 0.1 M bistros propane 8.4 and 20 % PEG 3350
Resolution 2.75 Å R-free 0.276
8YHI The Crystal Structure of SHP1 from Biortus. Deposited 2024-02-28 Different construct 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 243–528（286 aa）
Not recorded SO4 SULFATE ION × 2 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1M Hepes pH7.5, 2% PEG 400, 2.0M (NH4)2SO4
Resolution 1.75 Å R-free 0.227

13 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PTN6_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 8–112； UniProt 110–214

natural killer group 2A

OrganismNot specified

UniProt P26715

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain B； UniProt 33–47 Non-standard monomer：Yes (specific site not provided by mmCIF) Tyrosine-protein phosphatase non-receptor type 6 × 1 （P29350） SOLUTION NMR NMR measurement conditions：pH 7.4；296 K；Ionic strength (raw mmCIF value) 120mM；Pressure ambient NMR measurement conditions：pH 7.4；298 K；Ionic strength (raw mmCIF value) 120mM；Pressure ambient NMR sample composition：0.89mM SHP1 SH2 domain U-15N,13C; 0.89mM NKG2A peptide; 20mM d-Tris-HCl (pH 7.4); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 90% H2O, 10% D2O | 90% H2O/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 2YU7 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2RMX Solution structure of the SHP-1 C-terminal SH2 domain complexed with a tyrosine-phosphorylated peptide from NKG2A Deposited 2007-11-30 Different construct Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–15（15 aa） Fragment：tyrosine phosphorylation site, UNP residues 1-15
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.4；Ionic strength (raw mmCIF value) 120；Pressure ambient
NMR sample composition 0.8mM [U-13C; U-15N] SHP-1 C-terminal SH2 domain; 0.8mM tyrosine-phosphorylated peptide; 20mM [U-2H] TRIS; 100mM sodium chloride; 0.02% sodium azide; 1mM [U-2H] DTT; 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
3BDW Human CD94/NKG2A Deposited 2007-11-15 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 113–232（120 aa） Fragment：Residues UNP 113-232
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.9；298 K；1.0M tri-sodium citrate, 0.1M HEPES, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.50 Å R-free 0.270
3BDW Human CD94/NKG2A Deposited 2007-11-15 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 113–232（120 aa） Fragment：Residues UNP 113-232
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.9；298 K；1.0M tri-sodium citrate, 0.1M HEPES, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.50 Å R-free 0.270
3CDG Human CD94/NKG2A in complex with HLA-E Deposited 2008-02-26 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain K 113–232（120 aa） Fragment：residues in database 113-232
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.9；291 K；Ammonium sulfate, pH 7.9, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 3.40 Å R-free 0.279
3CDG Human CD94/NKG2A in complex with HLA-E Deposited 2008-02-26 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain F 113–232（120 aa） Fragment：residues in database 113-232
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.9；291 K；Ammonium sulfate, pH 7.9, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 3.40 Å R-free 0.279
3CII Structure of NKG2A/CD94 bound to HLA-E Deposited 2008-03-11 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain H 113–232（120 aa） Fragment：Ectodomain
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；291 K；1.8M ammonium sulfate, 0.3-0.7% sucrose, 100 mM Tris (8.0), VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 4.41 Å R-free 0.355
3CII Structure of NKG2A/CD94 bound to HLA-E Deposited 2008-03-11 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain J 113–232（120 aa） Fragment：Ectodomain
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；291 K；1.8M ammonium sulfate, 0.3-0.7% sucrose, 100 mM Tris (8.0), VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 4.41 Å R-free 0.355

4 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NKG2A_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain B； PDBConstruct 1–15； UniProt 33–47

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 2yu7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2yu7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2yu7
Deposition date deposition_date2007-04-05
Structure title titleSolution structure of the SHP-1 C-terminal SH2 domain complexed with a tyrosine-phosphorylated peptide from NKG2A
Keywords keywords;SH2 domain, Protein-peptide complex, Phosphorylated peptide recognition, Phosphotyrosine binding domain, Signal Transduction, Structural Genomics, NPPSFA, National Project on Protein Structural and Functional Analyses, RIKEN Structural Genomics/Proteomics Initiative, RSGI, SIGNALING PROTEIN ;; SIGNALING 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_guinier14.93 Å
Radius of gyration Rg (electron density) rg_electron14.34 Å
Forward intensity I(0) i01206300000.00
Molecular weight molecular_weight287780.0 kDa
Excluded volume excluded_volume356750 ų
Envelope volume envelope_volume39982 ų
Hydration-shell volume shell_volume18530 ų
Envelope diameter envelope_diameter59.9 Å
Shell Rg shell_rg24.43 Å
Envelope Rg envelope_rg18.46 Å
Shape Rg shape_rg14.31 Å
Total Rg total_rg14.60 Å
Total atoms total_atoms39700
Residues n_residues2640
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 dmax52.0 Å
Rg (real space) rg_real14.84 Å
Rg uncertainty (real space) rg_real_error0.31 Å
I(0) (real space) i0_real1.2060e+09
I(0) uncertainty (real space) i0_real_error1.2920e+07
Rg (reciprocal space) rg_reciprocal14.85 Å
I(0) (reciprocal space) i0_reciprocal1206000000.0000
Solution quality estimate total_estimate0.7663
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.8 Å
Skewness Skewness skewness0.190
Kurtosis Kurtosis kurtosis-0.167
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha556000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.654; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.000
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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) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2yu7A00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology505 — SHC Adaptor Protein
Homologous superfamily homologous superfamily10 — SH2 domain
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8. Citations (1)

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9. Files and Curves (10)