1m12

NMR solution structure of human Saposin C

Method: SOLUTION NMR Dmax: 37.1 Å Quality: REASONABLE

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

SAPOSIN C

Homo sapiens

UniProt P07602

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 311–390 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.8;298 K;Ionic strength (raw mmCIF value) ~10-20mM NaCl;Pressure ambient NMR sample composition:U-15N | 90% H20, 10% D20 NMR sample composition:U-15N, U-13C | 90% H20, 10% D20 NMR sample composition:U-15N, U-13C | 100% D20 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.

20 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SAP_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–80; UniProt 311–390

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 1m12

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1m12
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1m12
Deposition date deposition_date2002-06-17
Structure title titleNMR solution structure of human Saposin C
Keywords keywordsdisulfide bridges, alpha-helices, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier13.22
Radius of gyration Rg (electron density) rg_electron12.98
Forward intensity I(0) i0484977000.00
Molecular weight molecular_weight188160.0 kDa
Excluded volume excluded_volume236310 ų
Envelope volume envelope_volume23947 ų
Hydration-shell volume shell_volume13132 ų
Envelope diameter envelope_diameter55.9
Shell Rg shell_rg21.27
Envelope Rg envelope_rg16.77
Shape Rg shape_rg12.98
Total Rg total_rg13.15
Total atoms total_atoms26200
Residues n_residues1680
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 dmax37.1
Rg (real space) rg_real12.85
Rg uncertainty (real space) rg_real_error0.05
I(0) (real space) i0_real4.7030e+08
I(0) uncertainty (real space) i0_real_error3.9640e+06
Rg (reciprocal space) rg_reciprocal13.20
I(0) (reciprocal space) i0_reciprocal485000000.0000
Solution quality estimate total_estimate0.7069
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary15.5
Skewness Skewness skewness0.076
Kurtosis Kurtosis kurtosis-0.395
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha6.3510
Highest regularization parameter α highest_alpha103600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.934; Stabil: 0.963; Sysdev: 0.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.518

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1m12a1
Class classa — All alpha proteins
Fold Fold folda.64 — Saposin-like
Superfamily Superfamily superfamilya.64.1 — Saposin
Family Family familya.64.1.1 — NKL-like
Domain ID domain_idd1m12a2
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_id1m12A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology225 — NK-Lysin
Homologous superfamily homologous superfamily10 — Saposin-like

8. Citations (1)

9. Files and Curves (10)