6uz5

Solution structure of KTI55-Kringle 2 complex

Method: SOLUTION NMR Dmax: 63.5 Å Quality: REASONABLE

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

Plasminogen

Homo sapiens

UniProt P00747

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 185–262 Mutation:C11G, E63D, L79Y M protein × 1 (M4I070) SOLUTION NMR NMR measurement conditions:pH 6.7;298 K;Ionic strength (raw mmCIF value) 20;Pressure 1 NMR sample composition:1.0 mM [U-99% 13C; U-99% 15N] KTI55, 1.2 mM Kringle 2, 20 mM [U-2H] Bis-Tris-d19, 2 ug/mL DSS, 2 ug/mL sodium azide, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:1.0 mM [U-99% 13C; U-99% 15N] Kringle 2, 1.2 mM KTI55, 20 mM [U-2H] Bis-Tris-d19, 2 ug/mL DSS, 2 ug/mL sodium azide, 95% H2O/5% D2O | 95% H2O/5% 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.

46 other PDB entries and 76 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PLMN_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 8–85; UniProt 185–262

M protein

Streptococcus pyogenes

UniProt M4I070

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 44–98 Not recorded Plasminogen × 1 (P00747) SOLUTION NMR NMR measurement conditions:pH 6.7;298 K;Ionic strength (raw mmCIF value) 20;Pressure 1 NMR sample composition:1.0 mM [U-99% 13C; U-99% 15N] KTI55, 1.2 mM Kringle 2, 20 mM [U-2H] Bis-Tris-d19, 2 ug/mL DSS, 2 ug/mL sodium azide, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:1.0 mM [U-99% 13C; U-99% 15N] Kringle 2, 1.2 mM KTI55, 20 mM [U-2H] Bis-Tris-d19, 2 ug/mL DSS, 2 ug/mL sodium azide, 95% H2O/5% D2O | 95% H2O/5% 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name M4I070_STRPY
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 3–57; UniProt 44–98

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 6uz5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6uz5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6uz5
Deposition date deposition_date2019-11-14
Structure title titleSolution structure of KTI55-Kringle 2 complex
Keywords keywordsPlasminogen binding peptide, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier17.65
Radius of gyration Rg (electron density) rg_electron17.84
Forward intensity I(0) i01709240000.00
Molecular weight molecular_weight322600.0 kDa
Excluded volume excluded_volume392170 ų
Envelope volume envelope_volume52718 ų
Hydration-shell volume shell_volume20693 ų
Envelope diameter envelope_diameter71.8
Shell Rg shell_rg28.08
Envelope Rg envelope_rg23.43
Shape Rg shape_rg17.76
Total Rg total_rg18.26
Total atoms total_atoms43960
Residues n_residues2740
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 dmax63.5
Rg (real space) rg_real17.78
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real1.7090e+09
I(0) uncertainty (real space) i0_real_error2.2130e+07
Rg (reciprocal space) rg_reciprocal17.77
I(0) (reciprocal space) i0_reciprocal1709000000.0000
Solution quality estimate total_estimate0.7465
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary17.8
Skewness Skewness skewness0.527
Kurtosis Kurtosis kurtosis-0.116
Angular range angular_range— – 0.4500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha696100.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.671; Stabil: 0.995; Sysdev: 1.000; Positv: 1.000; Valcen: 0.702; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd6uz5a1
Class classg — Small proteins
Fold Fold foldg.14 — Kringle-like
Superfamily Superfamily superfamilyg.14.1 — Kringle-like
Family Family familyg.14.1.0 — automated matches
Domain ID domain_idd6uz5a2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

8. Citations (1)

9. Files and Curves (10)