SAXSdb — 1qls

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

S100C PROTEIN

SUS SCROFA

UniProt P31950

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 1–99	Not recorded	ANNEXIN I × 2 （P04083） CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION；pH 8.5；20 MG/ML PROTEIN WERE CRYSTALLIZED BY VAPOR DIFFUSION AGAINST 10% PEG 4000, 20% PEG 4000, 10% 2-PROPANOL, 100MM HEPES, PH=8.5, pH 8.50	Resolution 2.30 Å R-free 0.268

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	S111_PIG
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–99； UniProt 1–99

ANNEXIN I

OrganismNot specified

UniProt P04083

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain D； UniProt 1–11	Fragment：N-TERMINAL Non-standard monomer：Yes (specific site not provided by mmCIF)	S100C PROTEIN × 2 （P31950） CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION；pH 8.5；20 MG/ML PROTEIN WERE CRYSTALLIZED BY VAPOR DIFFUSION AGAINST 10% PEG 4000, 20% PEG 4000, 10% 2-PROPANOL, 100MM HEPES, PH=8.5, pH 8.50	Resolution 2.30 Å R-free 0.268

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 1QLS	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1AIN CRYSTAL STRUCTURE OF HUMAN ANNEXIN I AT 2.5 ANGSTROMS RESOLUTION Deposited 1992-06-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 32–345（314 aa）	Not recorded	CA CALCIUM ION × 6	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å
1BO9 NMR SOLUTION STRUCTURE OF DOMAIN 1 OF HUMAN ANNEXIN I Deposited 1998-08-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 41–113（73 aa） Fragment：DOMAIN 1	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；300 K；Pressure 1	Resolution not provided
5VFW An engineered cyclic peptide alleviates symptoms of inflammation in a murine model of inflammatory bowel disease Deposited 2017-04-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–26（25 aa） Fragment：N terminal Annexin I (2-26)	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5；290 K；Ionic strength (raw mmCIF value) 1；Pressure 1 NMR sample composition 0.2 mM Ac 2-26, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
9NP0 Structure of human annexin A1 in complex with 2C1 Fab Deposited 2025-03-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–346（346 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.32 Å

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ANX1_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain D； PDBConstruct 2–12； UniProt 1–11

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_id	1qls
Deposition date deposition_date	1999-09-15
Structure title title	S100C (S100A11),OR CALGIZZARIN, IN COMPLEX WITH ANNEXIN I N-TERMINUS
Keywords keywords	;METAL-BINDING PROTEIN/INHIBITOR, S100 FAMILY, EF-HAND PROTEIN, COMPLEX (LIGAND-ANNEXIN), LIGAND OF ANNEXIN II, CALCIUM/PHOSPHOLIPID BINDING PROTEIN, METAL-BINDING PROTEIN-INHIBITOR complex ;; METAL-BINDING PROTEIN/INHIBITOR
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	15.85 Å
Radius of gyration Rg (electron density) rg_electron	14.64 Å
Forward intensity I(0) i0	2952450.00
Molecular weight molecular_weight	12066.0 kDa
Excluded volume excluded_volume	15129 Å³
Envelope volume envelope_volume	17636 Å³
Hydration-shell volume shell_volume	10829 Å³
Envelope diameter envelope_diameter	53.6 Å
Shell Rg shell_rg	19.49 Å
Envelope Rg envelope_rg	14.91 Å
Shape Rg shape_rg	14.63 Å
Total Rg total_rg	15.71 Å
Total atoms total_atoms	842
Residues n_residues	106
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	59.4 Å
Rg (real space) rg_real	15.81 Å
Rg uncertainty (real space) rg_real_error	0.58 Å
I(0) (real space) i0_real	2.9520e+06
I(0) uncertainty (real space) i0_real_error	4.0090e+04
Rg (reciprocal space) rg_reciprocal	15.82 Å
I(0) (reciprocal space) i0_reciprocal	2952000.0000
Solution quality estimate total_estimate	0.8336
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	20.3 Å
Skewness Skewness skewness	0.203
Kurtosis Kurtosis kurtosis	-0.246
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	219300.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.647; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.890; Smooth: 1.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	S100C PROTEIN
Molecular weight formula_weight	11194.8 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	870

MAKRPTETERCIESLIAIFQKHAGRDGNNTKISKTEFLIFMNTELAAFTQNQKDPGVLDRMMKKLDLDSDGQLDFQEFLNLIGGLAIACHDSFIKSTQK

来源 Source

来源生物 organism	SUS SCROFA
通用名 common_name	PIG
NCBI Class编号 ncbi_taxonomy_id	9823
宿主生物 host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 polymer

Description description	ANNEXIN I
Molecular weight formula_weight	1278.5 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D

XAMVSAFLKQAW

Entity 3 Entity 3 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	23

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1qlsa_
Class class	a — All alpha proteins
Fold Fold fold	a.39 — EF Hand-like
Superfamily Superfamily superfamily	a.39.1 — EF-hand
Family Family family	a.39.1.2 — S100 proteins

CATH v4.4 (1 domains)

Domain ID domain_id	1qlsA00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	10 — EF-hand

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8. Citations (1)

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Unit-cell length a length_a	77.510 Å
Unit-cell length b length_b	77.510 Å
Unit-cell length c length_c	111.610 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	12

Space group space_group	P 61 2 2
Space-group number int_tables_number	178
Crystal system crystal_system	—

Resolution resolution	2.300 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	—
R_work r_work	0.2140
R_free r_free	0.2680

fit	/app/data/saxs_computation/ql/1qls/1qls.fit
pddf	/app/data/pr_computation/ql/1qls/1qls.pr.out
profile	/app/data/saxs_computation/ql/1qls/1qls.dat

S100C (S100A11),OR CALGIZZARIN, IN COMPLEX WITH ANNEXIN I N-TERMINUS

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

S100C PROTEIN

State in the Current Structure

Other States of the Same Protein in the Database

ANNEXIN I

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)