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1a7m

LEUKAEMIA INHIBITORY FACTOR CHIMERA (MH35-LIF), NMR, 20 STRUCTURES

Method: SOLUTION NMR Dmax: 67.3 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

LEUKEMIA INHIBITORY FACTOR

Mus musculus

UniProt P09056

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 24–203 Mutation：T107S, Q112H, V113S, A155V, R158K No other associated polymer SOLUTION NMR NMR measurement conditions：pH 4.4；310 K；Ionic strength (raw mmCIF value) 1 mM；Pressure AMBIENT NMR sample composition：H2O 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 1A7M Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1LKI THE CRYSTAL STRUCTURE AND BIOLOGICAL FUNCTION OF LEUKEMIA INHIBITORY FACTOR: IMPLICATIONS FOR RECEPTOR BINDING Deposited 1994-12-12 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 24–203（180 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å

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

View Construct and Data Evidence
UniProt name LIF_MOUSE
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–180； UniProt 24–203

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 1a7m

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1a7m
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1a7m
Deposition date deposition_date1998-03-16
Structure title titleLEUKAEMIA INHIBITORY FACTOR CHIMERA (MH35-LIF), NMR, 20 STRUCTURES
Keywords keywordsCYTOKINE, FOUR HELICAL BUNDLE; CYTOKINE
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier17.10 Å
Radius of gyration Rg (electron density) rg_electron17.01 Å
Forward intensity I(0) i02114250000.00
Molecular weight molecular_weight396120.0 kDa
Excluded volume excluded_volume498520 ų
Envelope volume envelope_volume50586 ų
Hydration-shell volume shell_volume20554 ų
Envelope diameter envelope_diameter75.5 Å
Shell Rg shell_rg27.63 Å
Envelope Rg envelope_rg22.31 Å
Shape Rg shape_rg16.99 Å
Total Rg total_rg17.24 Å
Total atoms total_atoms56060
Residues n_residues3600
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 dmax67.3 Å
Rg (real space) rg_real17.14 Å
Rg uncertainty (real space) rg_real_error0.70 Å
I(0) (real space) i0_real2.1140e+09
I(0) uncertainty (real space) i0_real_error3.1320e+07
Rg (reciprocal space) rg_reciprocal17.14 Å
I(0) (reciprocal space) i0_reciprocal2114000000.0000
Solution quality estimate total_estimate0.7700
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary18.6 Å
Skewness Skewness skewness0.435
Kurtosis Kurtosis kurtosis-0.162
Angular range angular_range— – 0.4650 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1099000.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.471; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.596; Smooth: 0.997
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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_idd1a7ma_
Class classa — All alpha proteins
Fold Fold folda.26 — 4-helical cytokines
Superfamily Superfamily superfamilya.26.1 — 4-helical cytokines
Family Family familya.26.1.1 — Long-chain cytokines

CATH v4.4 (1 domains)

Domain ID domain_id1a7mA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1250 — Growth Hormone; Chain: A;
Homologous superfamily homologous superfamily10 —
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8. Citations (1)

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9. Files and Curves (10)