1cop

THREE-DIMENSIONAL DIMER STRUCTURE OF THE LAMBDA-CRO REPRESSOR IN SOLUTION AS DETERMINED BY HETERONUCLEAR MULTIDIMENSIONAL NMR

Method: SOLUTION NMR Dmax: 54.5 Å Quality: GOOD

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

CRO REPRESSOR

Enterobacteria phage lambda

UniProt P03040

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–66 Chain E; UniProt 1–66 Not recorded No other associated polymer SOLUTION NMR mmCIF provides none of the parsed experimental conditions 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.

11 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RCRO_LAMBD
Isoform
PDB entities 1
Chains and sequence ranges Author chain D; PDBConstruct 1–66; UniProt 1–66 Author chain E; PDBConstruct 1–66; UniProt 1–66

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 1cop

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1cop
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1cop
Deposition date deposition_date1995-06-23
Structure title titleTHREE-DIMENSIONAL DIMER STRUCTURE OF THE LAMBDA-CRO REPRESSOR IN SOLUTION AS DETERMINED BY HETERONUCLEAR MULTIDIMENSIONAL NMR
Keywords keywordsGENE REGULATING PROTEIN; GENE REGULATING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier17.73
Radius of gyration Rg (electron density) rg_electron17.31
Forward intensity I(0) i01168030000.00
Molecular weight molecular_weight294740.0 kDa
Excluded volume excluded_volume371930 ų
Envelope volume envelope_volume55872 ų
Hydration-shell volume shell_volume23041 ų
Envelope diameter envelope_diameter63.8
Shell Rg shell_rg26.68
Envelope Rg envelope_rg19.82
Shape Rg shape_rg17.25
Total Rg total_rg17.72
Total atoms total_atoms42080
Residues n_residues2640
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 dmax54.5
Rg (real space) rg_real17.73
Rg uncertainty (real space) rg_real_error0.32
I(0) (real space) i0_real1.1680e+09
I(0) uncertainty (real space) i0_real_error1.4280e+07
Rg (reciprocal space) rg_reciprocal17.73
I(0) (reciprocal space) i0_reciprocal1168000000.0000
Solution quality estimate total_estimate0.8181
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.7
Skewness Skewness skewness0.230
Kurtosis Kurtosis kurtosis-0.724
Angular range angular_range— – 0.4500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha750200.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.888; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1copd_
Class classa — All alpha proteins
Fold Fold folda.35 — lambda repressor-like DNA-binding domains
Superfamily Superfamily superfamilya.35.1 — lambda repressor-like DNA-binding domains
Family Family familya.35.1.2 — Phage repressors
Domain ID domain_idd1cope_
Class classa — All alpha proteins
Fold Fold folda.35 — lambda repressor-like DNA-binding domains
Superfamily Superfamily superfamilya.35.1 — lambda repressor-like DNA-binding domains
Family Family familya.35.1.2 — Phage repressors

CATH v4.4 (2 domains)

Domain ID domain_id1copD00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology240 — CRO Repressor
Homologous superfamily homologous superfamily10 — CRO Repressor
Domain ID domain_id1copE00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology240 — CRO Repressor
Homologous superfamily homologous superfamily10 — CRO Repressor

8. Citations (1)

9. Files and Curves (10)