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1r1b

EPRS SECOND REPEATED ELEMENT, NMR, MINIMIZED AVERAGE STRUCTURE

Method: SOLUTION NMR Dmax: 43.5 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

TRNA SYNTHETASE

Cricetulus griseus

UniProt Q7SIA2

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 1–49 Fragment：RESIDUES 1 - 59 No other associated polymer SOLUTION NMR NMR measurement conditions：pH 7；293 K；Pressure 1 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 1R1B Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1D2D Hamster EprS second repeated element. NMR, 5 structures Deposited 1999-09-23 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–49（49 aa） Fragment：RESIDUES 1-59
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；298 K；Pressure 1
NMR sample composition 1.5 MM EPRS REPEAT U-15N; 20 MM POTASSIUM PHOSPHATE PH 7.0, 5 MM DITHIOTHREITOL, 0.5 MM NAN3;
Resolution not provided

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

View Construct and Data Evidence
UniProt name SYEP_CRIGR
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 3–51； UniProt 1–49

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 1r1b

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1r1b
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1r1b
Deposition date deposition_date1998-12-15
Structure title titleEPRS SECOND REPEATED ELEMENT, NMR, MINIMIZED AVERAGE STRUCTURE
Keywords keywordsTRNA SYNTHETASE (LIGASE), PROTEIN TRANSCRIPTION, LIGASE; LIGASE
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier12.40 Å
Radius of gyration Rg (electron density) rg_electron11.41 Å
Forward intensity I(0) i0878165.00
Molecular weight molecular_weight6278.0 kDa
Excluded volume excluded_volume7990 ų
Envelope volume envelope_volume8738 ų
Hydration-shell volume shell_volume7063 ų
Envelope diameter envelope_diameter43.4 Å
Shell Rg shell_rg16.08 Å
Envelope Rg envelope_rg12.02 Å
Shape Rg shape_rg11.33 Å
Total Rg total_rg12.95 Å
Total atoms total_atoms905
Residues n_residues56
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 dmax43.5 Å
Rg (real space) rg_real12.43 Å
Rg uncertainty (real space) rg_real_error0.38 Å
I(0) (real space) i0_real8.7820e+05
I(0) uncertainty (real space) i0_real_error8.9320e+03
Rg (reciprocal space) rg_reciprocal12.43 Å
I(0) (reciprocal space) i0_reciprocal878200.0000
Solution quality estimate total_estimate0.7685
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary13.8 Å
Skewness Skewness skewness0.417
Kurtosis Kurtosis kurtosis-0.084
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha182700.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.685; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.934; 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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7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1r1ba1
Class classa — All alpha proteins
Fold Fold folda.16 — S15/NS1 RNA-binding domain
Superfamily Superfamily superfamilya.16.1 — S15/NS1 RNA-binding domain
Family Family familya.16.1.3 — a tRNA synthase domain
Domain ID domain_idd1r1ba2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id1r1bA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily10 — S15/NS1, RNA-binding
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8. Citations (1)

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9. Files and Curves (10)