2lmg

Solution Structure of The C-terminal Domain (537-610) of Human Heat Shock Protein 70

Method: SOLUTION NMR Dmax: 41.6 Å Quality: REASONABLE

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

Heat shock 70 kDa protein 1A/1B

Homo sapiens

UniProt P08107

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 537–610 Fragment:UNP residues 537-610 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.5;298 K;Pressure ambient NMR sample composition:1 mM [U-100% 15N] protein-1, 20 mM sodium phosphate-2, 50 mM sodium chloride-3, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:1 mM [U-100% 13C; U-100% 15N] protein-4, 20 mM sodium phosphate-5, 50 mM sodium chloride-6, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:1 mM [U-100% 13C; U-100% 15N] protein-7, 20 mM sodium phosphate-8, 50 mM sodium chloride-9, 100% D2O | 100% 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.

15 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HSP71_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–75; UniProt 537–610

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 2lmg

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2lmg
Deposition date deposition_date2011-12-01
Structure title titleSolution Structure of The C-terminal Domain (537-610) of Human Heat Shock Protein 70
Keywords keywordsHSP70, Helix, CHAPERONE; CHAPERONE
Experimental Method methodSOLUTION NMR

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier12.40
Radius of gyration Rg (electron density) rg_electron12.32
Forward intensity I(0) i0392864000.00
Molecular weight molecular_weight166190.0 kDa
Excluded volume excluded_volume207510 ų
Envelope volume envelope_volume14730 ų
Hydration-shell volume shell_volume9783 ų
Envelope diameter envelope_diameter46.5
Shell Rg shell_rg18.51
Envelope Rg envelope_rg13.89
Shape Rg shape_rg12.32
Total Rg total_rg12.42
Total atoms total_atoms23340
Residues n_residues1480
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax41.6
Rg (real space) rg_real12.45
Rg uncertainty (real space) rg_real_error0.41
I(0) (real space) i0_real3.9290e+08
I(0) uncertainty (real space) i0_real_error4.6450e+06
Rg (reciprocal space) rg_reciprocal12.44
I(0) (reciprocal space) i0_reciprocal392900000.0000
Solution quality estimate total_estimate0.7439
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary13.7
Skewness Skewness skewness0.417
Kurtosis Kurtosis kurtosis-0.230
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha156100.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.569; Stabil: 0.994; Sysdev: 1.000; Positv: 1.000; Valcen: 0.978; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2lmga_
Class classa — All alpha proteins
Fold Fold folda.8 — immunoglobulin/albumin-binding domain-like
Superfamily Superfamily superfamilya.8.4 — Heat shock protein 70kD (HSP70), C-terminal subdomain
Family Family familya.8.4.1 — Heat shock protein 70kD (HSP70), C-terminal subdomain

CATH v4.4 (1 domains)

Domain ID domain_id2lmgA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1270 — Substrate Binding Domain Of Dnak; Chain:A; Domain 2
Homologous superfamily homologous superfamily10

8. Citations (1)

9. Files and Curves (10)