2xny

A fragment of streptococcal M1 protein in complex with human fibrinogen

Method: X-RAY DIFFRACTION Dmax: 194.8 Å Quality: REASONABLE

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

FIBRINOGEN ALPHA CHAIN

OrganismNot specified

UniProt P02671

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 130–216 Fragment:FRAGMENT D, RESIDUES 130-216 FIBRINOGEN BETA CHAIN × 1 (P02675) FIBRINOGEN GAMMA CHAIN × 1 (P02679) X-RAY DIFFRACTION X-ray crystallization conditions:1.3 M AMMONIUM TARTRATE, 0.1 M MES, PH 6.25. Resolution 7.50 Å R-free 0.408
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 130–216 Fragment:FRAGMENT D, RESIDUES 130-216 FIBRINOGEN BETA CHAIN × 1 (P02675) FIBRINOGEN GAMMA CHAIN × 1 (P02679) X-RAY DIFFRACTION X-ray crystallization conditions:1.3 M AMMONIUM TARTRATE, 0.1 M MES, PH 6.25. Resolution 7.50 Å R-free 0.408

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.

36 other PDB entries and 68 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FIBA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–87; UniProt 130–216 Author chain D; PDBConstruct 1–87; UniProt 130–216

FIBRINOGEN BETA CHAIN

OrganismNot specified

UniProt P02675

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 164–491 Fragment:FRAGMENT D, RESIDUES 164-491 FIBRINOGEN ALPHA CHAIN × 1 (P02671) FIBRINOGEN GAMMA CHAIN × 1 (P02679) X-RAY DIFFRACTION X-ray crystallization conditions:1.3 M AMMONIUM TARTRATE, 0.1 M MES, PH 6.25. Resolution 7.50 Å R-free 0.408
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 164–491 Fragment:FRAGMENT D, RESIDUES 164-491 FIBRINOGEN ALPHA CHAIN × 1 (P02671) FIBRINOGEN GAMMA CHAIN × 1 (P02679) X-RAY DIFFRACTION X-ray crystallization conditions:1.3 M AMMONIUM TARTRATE, 0.1 M MES, PH 6.25. Resolution 7.50 Å R-free 0.408

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.

30 other PDB entries and 56 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FIBB_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–328; UniProt 164–491 Author chain E; PDBConstruct 1–328; UniProt 164–491

FIBRINOGEN GAMMA CHAIN

OrganismNot specified

UniProt P02679

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 114–432 Fragment:FRAGMENT D, RESIDUES 114-432 FIBRINOGEN ALPHA CHAIN × 1 (P02671) FIBRINOGEN BETA CHAIN × 1 (P02675) X-RAY DIFFRACTION X-ray crystallization conditions:1.3 M AMMONIUM TARTRATE, 0.1 M MES, PH 6.25. Resolution 7.50 Å R-free 0.408
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 114–432 Fragment:FRAGMENT D, RESIDUES 114-432 FIBRINOGEN ALPHA CHAIN × 1 (P02671) FIBRINOGEN BETA CHAIN × 1 (P02675) X-RAY DIFFRACTION X-ray crystallization conditions:1.3 M AMMONIUM TARTRATE, 0.1 M MES, PH 6.25. Resolution 7.50 Å R-free 0.408

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.

36 other PDB entries and 56 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FIBG_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–319; UniProt 114–432 Author chain F; PDBConstruct 1–319; UniProt 114–432

M PROTEIN

STREPTOCOCCUS PYOGENES

UniProt Q48WD8

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
3 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain M; UniProt 42–135 Chain N; UniProt 42–135 Fragment:N-TERMINAL FRAGMENT, RESIDUES 42-134 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:1.3 M AMMONIUM TARTRATE, 0.1 M MES, PH 6.25. Resolution 7.50 Å R-free 0.408

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.

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

View Construct and Data Evidence
UniProt name Q48WD8_STRP1
Isoform
PDB entities 4
Chains and sequence ranges Author chain M; PDBConstruct 3–96; UniProt 42–135 Author chain N; PDBConstruct 3–96; UniProt 42–135

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 2xny

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2xny
Deposition date deposition_date2010-08-06
Structure title titleA fragment of streptococcal M1 protein in complex with human fibrinogen
Keywords keywordsCELL ADHESION, VIRULENCE FACTOR, STREPTOCOCCAL TOXIC SHOCK SYNDROME; CELL ADHESION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier60.04
Radius of gyration Rg (electron density) rg_electron61.68
Forward intensity I(0) i0378017000.00
Molecular weight molecular_weight155800.0 kDa
Excluded volume excluded_volume192380 ų
Envelope volume envelope_volume291110 ų
Hydration-shell volume shell_volume46569 ų
Envelope diameter envelope_diameter210.1
Shell Rg shell_rg48.17
Envelope Rg envelope_rg59.62
Shape Rg shape_rg61.81
Total Rg total_rg60.86
Total atoms total_atoms10956
Residues n_residues1359
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 dmax194.8
Rg (real space) rg_real61.17
Rg uncertainty (real space) rg_real_error2.12
I(0) (real space) i0_real3.7800e+08
I(0) uncertainty (real space) i0_real_error7.4910e+06
Rg (reciprocal space) rg_reciprocal59.02
I(0) (reciprocal space) i0_reciprocal376700000.0000
Solution quality estimate total_estimate0.6724
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary30.0
Skewness Skewness skewness0.485
Kurtosis Kurtosis kurtosis-0.745
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6798000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.449; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.383; Smooth: 0.006

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)