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9bb6

Backbone Modification in the GA Module of Protein PAB: ACPC residues at positions 5 and 13, beta3 residue at position 9

Method: SOLUTION NMR Dmax: 33.7 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Peptostreptococcal albumin-binding protein

OrganismNot specified

UniProt Q51911

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 219–265 Non-standard monomer：Yes (specific site not provided by mmCIF) No other associated polymer SOLUTION NMR NMR measurement conditions：pH 5.8；283 K；Ionic strength (raw mmCIF value) 1；Pressure 1 NMR sample composition：1 mM GA Module of Protein PAB: ACPC residues at positions 5 and 13, beta3 residue at position 9, 0.2 mM dss, 90% H2O/10% D2O | 90% H2O/10% 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.

Other PDB Difference from Current Entry 9BB6 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1GAB STRUCTURE OF AN ALBUMIN-BINDING DOMAIN, NMR, 20 STRUCTURES Deposited 1996-12-30 Different construct Different mutation/modification Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 213–265（53 aa） Fragment：ALBUMIN-BINDING DOMAIN, RESIDUES 213 - 265
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6；300 K
Resolution not provided
1PRB STRUCTURE OF AN ALBUMIN-BINDING DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE Deposited 1997-01-15 Different construct Different mutation/modification Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 213–265（53 aa） Fragment：ALBUMIN-BINDING DOMAIN, RESIDUES 213 - 265
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6；300 K
Resolution not provided
1TF0 Crystal structure of the GA module complexed with human serum albumin Deposited 2004-05-26 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 B 213–265（53 aa）
Not recorded DKA DECANOIC ACID × 3 CIT CITRIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；291 K；Ammonium sulfate, citrate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 2.70 Å R-free 0.295
2J5Y Crystal structure of the GA module from F.magna Deposited 2006-09-20 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 213–265（53 aa） Fragment：ALBUMIN-BINDING DOMAIN, RESIDUES 213-265
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；22-26% (W/V) PEG 3350, 50 MM POTASSIUM PHOSPHATE PH 7.5, 100 MM AMMONIUM ACETATE
Resolution 1.40 Å R-free 0.199
2J5Y Crystal structure of the GA module from F.magna Deposited 2006-09-20 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 213–265（53 aa） Fragment：ALBUMIN-BINDING DOMAIN, RESIDUES 213-265
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；22-26% (W/V) PEG 3350, 50 MM POTASSIUM PHOSPHATE PH 7.5, 100 MM AMMONIUM ACETATE
Resolution 1.40 Å R-free 0.199
2VDB Structure of human serum albumin with S-naproxen and the GA module Deposited 2007-10-04 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 B 213–265（53 aa） Fragment：RESIDUES 213-265
Not recorded DKA DECANOIC ACID × 6 NPS (2S)-2-(6-methoxynaphthalen-2-yl)propanoic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions 26-32% PEG 3350, 50 MM POTASSIUM PHOSPHATE, 0.1 M AMMONIUM PHOSPHATE/POTASSIUM PHOSPHATE
Resolution 2.52 Å R-free 0.280
9BB1 Backbone Modification in the GA Module of Protein PAB: Wild-type Sequence Deposited 2024-04-05 Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 219–265（47 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.3；300 K；Ionic strength (raw mmCIF value) 1；Pressure 1
NMR sample composition 1 mM GA Module of Protein PAB, 0.2 mM DSS, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
9BB2 Backbone Modification in the GA Module of Protein PAB: beta3-residues at positions 20 and 24 Deposited 2024-04-05 Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 219–265（47 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6；283 K；Ionic strength (raw mmCIF value) 1；Pressure 1
NMR sample composition 1 mM GA Module of Protein PAB: beta3 residues at positions 20 and 24, 0.2 mM DSS, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
9BB3 Backbone Modification in the GA Module of Protein PAB: beta3-residues at positions 22 and 26 Deposited 2024-04-05 Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 219–265（47 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6；300 K；Ionic strength (raw mmCIF value) 1；Pressure 1
NMR sample composition 1 mM GA Module of Protein PAB: beta3 residues at positions 22 and 26, 0.2 mM DSS, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
9BB4 Backbone Modification in the GA Module of Protein PAB: beta3-residues at positions 23 and 26 Deposited 2024-04-05 Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 219–265（47 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.9；283 K；Ionic strength (raw mmCIF value) 1；Pressure 1
NMR sample composition 1 mM GA Module of Protein PAB: beta3 residues at positions 23 and 26, 0.2 mM DSS, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
9BB5 Backbone Modification in the GA Module of Protein PAB: ACPC residues at positions 22 and 26 Deposited 2024-04-05 Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 219–265（47 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.9；283 K；Ionic strength (raw mmCIF value) 1；Pressure 1
NMR sample composition 1 mM GA Module of Protein PAB: ACPC residues at positions 22 and 26, 0.2 mM DSS, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
9BB7 Backbone Modification in the GA Module of Protein PAB: ACPC residues at positions 5 and 39, beta3 residue at position 26 Deposited 2024-04-05 Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 219–265（47 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.6；300 K；Ionic strength (raw mmCIF value) 1；Pressure 1
NMR sample composition 0.88 mM GA Module of Protein PAB: ACPC residues at positions 5 and 39, beta3 residue at position 26, 0.19 mM DSS, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided

11 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PAB_FINMA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–47； UniProt 219–265

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 9bb6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9bb6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9bb6
Deposition date deposition_date2024-04-05
Structure title titleBackbone Modification in the GA Module of Protein PAB: ACPC residues at positions 5 and 13, beta3 residue at position 9
Keywords keywordshelix bundle, designed variant, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier10.05 Å
Radius of gyration Rg (electron density) rg_electron9.94 Å
Forward intensity I(0) i035039800.00
Molecular weight molecular_weight51550.0 kDa
Excluded volume excluded_volume65785 ų
Envelope volume envelope_volume10435 ų
Hydration-shell volume shell_volume8212 ų
Envelope diameter envelope_diameter36.6 Å
Shell Rg shell_rg16.52 Å
Envelope Rg envelope_rg11.61 Å
Shape Rg shape_rg9.89 Å
Total Rg total_rg10.48 Å
Total atoms total_atoms7420
Residues n_residues440
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax33.7 Å
Rg (real space) rg_real9.98 Å
Rg uncertainty (real space) rg_real_error0.28 Å
I(0) (real space) i0_real3.5040e+07
I(0) uncertainty (real space) i0_real_error3.7720e+05
Rg (reciprocal space) rg_reciprocal9.99 Å
I(0) (reciprocal space) i0_reciprocal35040000.0000
Solution quality estimate total_estimate0.7270
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary13.6 Å
Skewness Skewness skewness-0.056
Kurtosis Kurtosis kurtosis-0.222
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha31320.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.496; Stabil: 0.989; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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9. Files and Curves (10)