1ssz

Conformational Mapping of Mini-B: An N-terminal/C-terminal Construct of Surfactant Protein B Using 13C-Enhanced Fourier Transform Infrared (FTIR) Spectroscopy

Method: INFRARED SPECTROSCOPY
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Pulmonary surfactant-associated protein B

OrganismNot specified

UniProt P07988

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein monomer Monomer Protein 1 No other associated polymer Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name PSPB_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–34; UniProt 208–278

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id1ssz
Deposition date deposition_date2004-03-24
Structure title titleConformational Mapping of Mini-B: An N-terminal/C-terminal Construct of Surfactant Protein B Using 13C-Enhanced Fourier Transform Infrared (FTIR) Spectroscopy
Keywords keywordsLUNG SURFACTANT PROTEIN, SAPOSIN, SURFACE ACTIVE PROTEIN; SURFACE ACTIVE PROTEIN
Experimental Method methodINFRARED SPECTROSCOPY
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

1ssz__assembly_1__model_5

Assembly 1 · Model 5 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1ssz__assembly_1__model_5 | I(q)

10-2 10-1 104 105 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

1ssz__assembly_1__model_5 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)10.80 Å
Rg (electron density)9.70 Å
Total Rg11.30 Å
Atom count575
Residues34
Excluded volume5020 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1ssz__assembly_1__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 2 1ssz__assembly_1__model_2 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 3 1ssz__assembly_1__model_3 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 4 1ssz__assembly_1__model_4 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 5 1ssz__assembly_1__model_5 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 6 1ssz__assembly_1__model_6 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 7 1ssz__assembly_1__model_7 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 8 1ssz__assembly_1__model_8 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 9 1ssz__assembly_1__model_9 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 10 1ssz__assembly_1__model_10 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (1)

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6. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1ssza_
Class classj — Peptides
Fold Fold foldj.35 — Transmembrane helical fragments
Superfamily Superfamily superfamilyj.35.1 — Transmembrane helical fragments
Family Family familyj.35.1.1 — Transmembrane helical fragments
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7. Citations (1)