SAXSdb — 5abs

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

SH3 DOMAIN-CONTAINING KINASE-BINDING PROTEIN 1

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	Protein homooligomer Homooligomer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain A； UniProt 599–662	Fragment：COILED-COIL DOMAIN, RESIDUES 599-662 Non-standard monomer：Yes (specific site not provided by mmCIF)	ZN ZINC ION × 12	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 7；298 K；0.05M ZN ACETATE, 20% PEG3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K, pH 7	Resolution 1.74 Å R-free 0.283

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 5ABS	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2BZ8 N-terminal Sh3 domain of CIN85 bound to Cbl-b peptide Deposited 2005-08-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–58（58 aa） Fragment：N-TERMINAL SH3 DOMAIN RESIDUES 1-58 Chain B 1–58（58 aa） Fragment：N-TERMINAL SH3 DOMAIN RESIDUES 1-58	Not recorded	NA SODIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；0.8 M NA CITRATE, 0.1 M BIS-TRIS PH 7.5, 0.2 M NACL	Resolution 2.00 Å R-free 0.271
2K6D CIN85 Sh3-C domain in complex with ubiquitin Deposited 2008-07-07	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 × 2 PDB declaration: dimeric	Chain A 267–328（62 aa） Fragment：CIN85 SH3-C domain	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.4；298 K；Ionic strength (raw mmCIF value) 0.150；Pressure ambient NMR sample composition 0.1 mM CIN85, 0.1 mM [U-100% 15N] ubiquitin, 50 mM sodium phosphate, 2 mM DTT, 5 mM DSS, 150 mM sodium chloride, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.1 mM [U-100% 15N] CIN85, 0.1 mM ubiquitiny, 50 mM sodium phosphate, 2 mM DTT, 5 mM DSS, 150 mM sodium chloride, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1.0 mM [U-100% 13C; U-100% 15N] CIN85, 50 mM sodium phosphate, 2 mM DTT, 5 mM DSS, 150 mM sodium chloride, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2K9G Solution structure of the third SH3 domain of the Cin85 adapter protein Deposited 2008-10-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 262–333（72 aa） Fragment：SH3 domain C, UNP residues 262-333	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.4；298 K；Ionic strength (raw mmCIF value) 140；Pressure ambient NMR sample composition 1mM Cin85 SH3-C, 20mM sodium phosphate, 100mM sodium chloride, 1mM DTT, 1mM EDTA, 0.02% sodium azide, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1mM [U-98% 13C; U-98% 15N] Cin85 SH3-C, 20mM sodium phosphate, 100mM sodium chloride, 1mM DTT, 1mM EDTA, 0.02% sodium azide, 100% D2O \| 100% D2O NMR sample composition 1mM [U-99% 15N] Cin85 SH3-C, 20mM sodium phosphate, 100mM sodium chloride, 1mM DTT, 1mM EDTA, 0.02% sodium azide, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1mM [U-99% 13C; U-99% 15N] Cin85 SH3-C, 20mM sodium phosphate, 100mM sodium chloride, 1mM DTT, 1mM EDTA, 0.02% sodium azide, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2N64 NMR Structure of the C-terminal Coiled-Coil Domain of CIN85 Deposited 2015-08-11	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 594–665（72 aa） Fragment：Coiled coil domain residues 594-665 Chain B 594–665（72 aa） Fragment：Coiled coil domain residues 594-665 Chain C 594–665（72 aa） Fragment：Coiled coil domain residues 594-665	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.9；305 K；Pressure ambient NMR sample composition 1-3 mM [U-13C; U-15N; U-2H] CIN85 CC-domain, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 1-3 mM [U-13C; U-15N; U-2H] CIN85 CC-domain, 1-3 mM [U-2H] CIN85 CC-domain, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
2O2O Solution structure of domain B from human CIN85 PROTEIN Deposited 2006-11-30	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 92–168（77 aa） Fragment：CIN85_B	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.3；298 K；Ionic strength (raw mmCIF value) 20mM PO4, 100mM NACL, 1mM EDTA, 2mM DTT, 0.01% NAN3；Pressure AMBIENT NMR sample composition 1MM CIN85_B U-15N PHOSPHATE BUFFER; 1MM CIN85_B U-15N,13C; 20MM PHOSPHATE BUFFER; 1MM CIN85_B U-15N,13C; 20MM PHOSPHATE BUFFER	Resolution not provided
2YDL Crystal structure of SH3C from CIN85 Deposited 2011-03-22	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 270–328（59 aa） Fragment：SH3 C, RESIDUES 270-328	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions 0.1M CITRATE PH 5.5, 2.0 M AMMONIUM SULPHATE	Resolution 2.05 Å R-free 0.252

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	SH3K1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–66； UniProt 599–662

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	5abs
Deposition date deposition_date	2015-08-07
Structure title title	CRYSTAL STRUCTURE OF THE C-TERMINAL COILED-COIL DOMAIN OF CIN85 IN SPACE GROUP P321
Keywords keywords	SIGNALING PROTEIN, CBL-INTERACTING PROTEIN OF 85 KDA, ADAPTER PROTEIN, COILED-COIL DOMAIN, B-CELL ANTIGEN RECEPTOR SIGNALING; SIGNALING 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	25.67 Å
Radius of gyration Rg (electron density) rg_electron	26.62 Å
Forward intensity I(0) i0	1436320.00
Molecular weight molecular_weight	7794.0 kDa
Excluded volume excluded_volume	9407 Å³
Envelope volume envelope_volume	14714 Å³
Hydration-shell volume shell_volume	6365 Å³
Envelope diameter envelope_diameter	92.0 Å
Shell Rg shell_rg	25.71 Å
Envelope Rg envelope_rg	27.01 Å
Shape Rg shape_rg	26.72 Å
Total Rg total_rg	26.19 Å
Total atoms total_atoms	524
Residues n_residues	63
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	96.5 Å
Rg (real space) rg_real	26.42 Å
Rg uncertainty (real space) rg_real_error	1.27 Å
I(0) (real space) i0_real	1.4360e+06
I(0) uncertainty (real space) i0_real_error	2.1290e+04
Rg (reciprocal space) rg_reciprocal	26.19 Å
I(0) (reciprocal space) i0_reciprocal	1436000.0000
Solution quality estimate total_estimate	0.6236
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	10.9 Å
Skewness Skewness skewness	0.611
Kurtosis Kurtosis kurtosis	-0.528
Angular range angular_range	— – 0.3100 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	40910.0000
Real-space data points n_real_points	63
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.055; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.010; 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	SH3 DOMAIN-CONTAINING KINASE-BINDING PROTEIN 1
Molecular weight formula_weight	7885.6 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	554

GHMEPAASSQAAVEELRTQVRELRSIIETMKDQQKREIKQLLSELDEEKKIRLRLQMEVNDIKKAL

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 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	14

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8. Citations (1)

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Unit-cell length a length_a	40.968 Å
Unit-cell length b length_b	40.968 Å
Unit-cell length c length_c	90.036 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	6

Space group space_group	P 3 2 1
Space-group number int_tables_number	150
Crystal system crystal_system	—

Resolution resolution	1.740 Å
Low-resolution limit resolution_low	45.020 Å
R factor r_factor	0.2480
R_work r_work	0.2440
R_free r_free	0.2833

fit	/app/data/saxs_computation/ab/5abs/5abs.fit
pddf	/app/data/pr_computation/ab/5abs/5abs.pr.out
profile	/app/data/saxs_computation/ab/5abs/5abs.dat

CRYSTAL STRUCTURE OF THE C-TERMINAL COILED-COIL DOMAIN OF CIN85 IN SPACE GROUP P321

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

SH3 DOMAIN-CONTAINING KINASE-BINDING PROTEIN 1

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