3csg

Crystal Structure of Monobody YS1(MBP-74)/Maltose Binding Protein Fusion Complex

Method: X-RAY DIFFRACTION Dmax: 79.9 Å Quality: EXCELLENT

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

Maltose-binding protein Monobody YS1 Fusion

Escherichia coli, synthetic

UniProt P0AEX9

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 31–396 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.2;292 K;20% polyethyleneglycol-1000, 0.1 M Na/K phosphate, 0.2 M NaCl, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 1.80 Å R-free 0.235

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.

366 other PDB entries and 491 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–368; UniProt 31–396

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 3csg

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3csg
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3csg
Deposition date deposition_date2008-04-09
Structure title titleCrystal Structure of Monobody YS1(MBP-74)/Maltose Binding Protein Fusion Complex
Keywords keywords;Engineered Binding Protein, Antibody Mimic, Synthetic Protein Interface, Minimalist Protein Interface, DE NOVO PROTEIN, SUGAR BINDING PROTEIN ;; DE NOVO PROTEIN, SUGAR BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.14
Radius of gyration Rg (electron density) rg_electron24.14
Forward intensity I(0) i039206100.00
Molecular weight molecular_weight50213.0 kDa
Excluded volume excluded_volume63516 ų
Envelope volume envelope_volume75380 ų
Hydration-shell volume shell_volume26160 ų
Envelope diameter envelope_diameter83.8
Shell Rg shell_rg31.19
Envelope Rg envelope_rg24.21
Shape Rg shape_rg24.11
Total Rg total_rg25.07
Total atoms total_atoms3554
Residues n_residues458
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 dmax79.9
Rg (real space) rg_real25.08
Rg uncertainty (real space) rg_real_error0.47
I(0) (real space) i0_real3.9210e+07
I(0) uncertainty (real space) i0_real_error5.2080e+05
Rg (reciprocal space) rg_reciprocal25.10
I(0) (reciprocal space) i0_reciprocal39210000.0000
Solution quality estimate total_estimate0.9073
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.9
Skewness Skewness skewness0.231
Kurtosis Kurtosis kurtosis-0.493
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7116000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.934; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id3csgA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II
Domain ID domain_id3csgA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II
Domain ID domain_id3csgA03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (2)

9. Files and Curves (10)