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1egf

SOLUTION STRUCTURE OF MURINE EPIDERMAL GROWTH FACTOR DETERMINED BY NMR SPECTROSCOPY AND REFINED BY ENERGY MINIMIZATION WITH RESTRAINTS

Method: SOLUTION NMR Dmax: 33.0 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

EPIDERMAL GROWTH FACTOR

Mus musculus

UniProt P01132

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 977–1029 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.

Other PDB Difference from Current Entry 1EGF Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1A3P ROLE OF THE 6-20 DISULFIDE BRIDGE IN THE STRUCTURE AND ACTIVITY OF EPIDERMAL GROWTH FACTOR, NMR, 20 STRUCTURES Deposited 1998-01-22 Different construct Different mutation/modification Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 980–1024（45 aa） Fragment：RESIDUES 4 - 48
Mutation：DEL(1-3, 49-53), C6(AMINO-BUTYRIC ACID), C20 (AMINO-BUTYRIC ACID) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 2.8；300 K；Pressure 1
NMR sample composition H2O
Resolution not provided
1EPG THREE-DIMENSIONAL NUCLEAR MAGNETIC RESONANCE STRUCTURES OF MOUSE EPIDERMAL GROWTH FACTOR IN ACIDIC AND PHYSIOLOGICAL PH SOLUTIONS Deposited 1992-03-24 Parsed fields agree Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 977–1029（53 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1EPH THREE-DIMENSIONAL NUCLEAR MAGNETIC RESONANCE STRUCTURES OF MOUSE EPIDERMAL GROWTH FACTOR IN ACIDIC AND PHYSIOLOGICAL PH SOLUTIONS Deposited 1992-03-24 Parsed fields agree Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 977–1029（53 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1EPI THREE-DIMENSIONAL NUCLEAR MAGNETIC RESONANCE STRUCTURES OF MOUSE EPIDERMAL GROWTH FACTOR IN ACIDIC AND PHYSIOLOGICAL PH SOLUTIONS Deposited 1992-03-24 Parsed fields agree Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 977–1029（53 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1EPJ THREE-DIMENSIONAL NUCLEAR MAGNETIC RESONANCE STRUCTURES OF MOUSE EPIDERMAL GROWTH FACTOR IN ACIDIC AND PHYSIOLOGICAL PH SOLUTIONS Deposited 1992-03-24 Parsed fields agree Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 977–1029（53 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1GK5 Solution Structure the mEGF/TGFalpha44-50 chimeric growth factor Deposited 2001-08-08 Different construct Different oligomeric state Different experimental conditions Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain A 977–1018（42 aa） Fragment：UNP residues 977-1018,UNP residues 83-89
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 3；298 K
Resolution not provided
3EGF SOLUTION STRUCTURE OF MURINE EPIDERMAL GROWTH FACTOR DETERMINED BY NMR SPECTROSCOPY AND REFINED BY ENERGY MINIMIZATION WITH RESTRAINTS Deposited 1992-08-30 Parsed fields agree Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 977–1029（53 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EGF_MOUSE
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–53； UniProt 977–1029

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 1egf

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1egf
Deposition date deposition_date1991-10-01
Structure title titleSOLUTION STRUCTURE OF MURINE EPIDERMAL GROWTH FACTOR DETERMINED BY NMR SPECTROSCOPY AND REFINED BY ENERGY MINIMIZATION WITH RESTRAINTS
Keywords keywordsGROWTH FACTOR; GROWTH FACTOR
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier12.31 Å
Radius of gyration Rg (electron density) rg_electron12.88 Å
Forward intensity I(0) i0164627000.00
Molecular weight molecular_weight96699.0 kDa
Excluded volume excluded_volume116150 ų
Envelope volume envelope_volume18921 ų
Hydration-shell volume shell_volume10618 ų
Envelope diameter envelope_diameter54.0 Å
Shell Rg shell_rg21.06 Å
Envelope Rg envelope_rg17.34 Å
Shape Rg shape_rg12.93 Å
Total Rg total_rg12.96 Å
Total atoms total_atoms6720
Residues n_residues848
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 dmax33.0 Å
Rg (real space) rg_real11.54 Å
Rg uncertainty (real space) rg_real_error0.06 Å
I(0) (real space) i0_real1.5740e+08
I(0) uncertainty (real space) i0_real_error1.2880e+06
Rg (reciprocal space) rg_reciprocal12.54 Å
I(0) (reciprocal space) i0_reciprocal164600000.0000
Solution quality estimate total_estimate0.6732
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary10.4 Å
Skewness Skewness skewness0.384
Kurtosis Kurtosis kurtosis-0.602
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha3.9460
Highest regularization parameter α highest_alpha43650.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.985; Stabil: 0.979; Sysdev: 0.000; Positv: 1.000; Valcen: 0.859; 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) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1egfa_
Class classg — Small proteins
Fold Fold foldg.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamilyg.3.11 — EGF/Laminin
Family Family familyg.3.11.1 — EGF-type module

CATH v4.4 (1 domains)

Domain ID domain_id1egfA00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology25 — Laminin
Homologous superfamily homologous superfamily10 — Laminin
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8. Citations (4)

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9. Files and Curves (10)