SAXSdb — 1cnp

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

CALCYCLIN (RABBIT, APO)

OrganismNot specified

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 1–90 Chain B； UniProt 1–90	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 1CNP	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1A03 THE THREE-DIMENSIONAL STRUCTURE OF CA2+-BOUND CALCYCLIN: IMPLICATIONS FOR CA2+-SIGNAL TRANSDUCTION BY S100 PROTEINS, NMR, 20 STRUCTURES Deposited 1997-12-08	Different experimental conditions	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–90（90 aa） Chain B 1–90（90 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；300 K；Ionic strength (raw mmCIF value) 50mM TRIS, 20-38mM CACL2 NMR sample composition 95% H2O, 5% D2O	Resolution not provided
1JWD Ca2+-induced Structural Changes in Calcyclin: High-resolution Solution Structure of Ca2+-bound Calcyclin. Deposited 2001-09-04	Different experimental conditions	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–90（90 aa） Chain B 1–90（90 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；300 K；Ionic strength (raw mmCIF value) 30 mM CaCl2；Pressure ambient NMR sample composition 2 mM calcyclin, 50 MM TRIS buffer, 30 mM CaCl2 \| 90% H2O/10% D2O NMR sample composition 2 mM 15N, 13C-enriched calcyclin, 50 mM TRIS-buffer, 0.05% NaN3, 30 mM CaCl2 \| 90% H2O/10% D2O NMR sample composition 1:1 15N,13C-enriched:unlabled calcyclin, 50 mM TRIS-buffer, 0.05% NaN3, 30 mM CaCl2 \| 90% H2O/10% D2O NMR sample composition 15N-enriched calcyclin, 50 mM TRIS-buffer, 0.05% NaN3, 30 mM CaCl2 \| 90% H2O/10% D2O NMR sample composition 10% 13C-enriched calcyclin, 50 mM TRIS-buffer, 0.05% NaN3, 30 mM CaCl2 \| D2O	Resolution not provided
2CNP HIGH RESOLUTION SOLUTION STRUCTURE OF APO RABBIT CALCYCLIN, NMR, 22 STRUCTURES Deposited 1999-01-07	Different experimental conditions	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–90（90 aa） Chain B 1–90（90 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；300 K	Resolution not provided
2JTT Solution structure of calcium loaded S100A6 bound to C-terminal Siah-1 interacting protein Deposited 2007-08-06	Different oligomeric state Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–90（90 aa） Chain B 1–90（90 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；318 K；Ionic strength (raw mmCIF value) 0.08；Pressure ambient NMR sample composition 1 mM [U-100% 13C; U-100% 15N] SIP(189-219), 1 mM S100A6, 0.05 mM [U-2H] TRIS, 0.01 mM Ca2+, 93% H2O/5% D2O/2% d-TFE \| 93% H2O/5% D2O/2% d-TFE NMR sample composition 1 mM [U-100% 15N] SIP(189-219), 1 mM S100A6, 0.05 mM [U-2H] TRIS, 0.01 mM Ca2+, 93% H2O/5% D2O/2% d-TFE \| 93% H2O/5% D2O/2% d-TFE NMR sample composition 1 mM [U-100% 13C] SIP(189-219), 1 mM S100A6, 0.05 mM [U-2H] TRIS, 0.01 mM Ca2+, 98% D2O/2% d-TFE \| 98% D2O/2% d-TFE NMR sample composition 2.3 mM [U-100% 13C] SIP(189-219), 2.3 mM [U-100% 15N] S100A6, 0.05 mM [U-2H] TRIS, 0.01 mM Ca2+, 93% H2O/5% D2O/2% d-TFE \| 93% H2O/5% D2O/2% d-TFE	Resolution not provided

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

View Construct and Data Evidence

UniProt name	S10A6_RABIT
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–90； UniProt 1–90 Author chain B； PDBConstruct 1–90； UniProt 1–90

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	1cnp
Deposition date deposition_date	1995-08-31
Structure title title	THE STRUCTURE OF CALCYCLIN REVEALS A NOVEL HOMODIMERIC FOLD FOR S100 CA2+-BINDING PROTEINS, NMR, 22 STRUCTURES
Keywords keywords	EF-HAND, CALCIUM-BINDING PROTEIN, S-100 PROTEIN; CALCIUM-BINDING PROTEIN
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	16.68 Å
Radius of gyration Rg (electron density) rg_electron	16.40 Å
Forward intensity I(0) i0	2529000000.00
Molecular weight molecular_weight	446630.0 kDa
Excluded volume excluded_volume	567110 Å³
Envelope volume envelope_volume	55550 Å³
Hydration-shell volume shell_volume	23354 Å³
Envelope diameter envelope_diameter	59.0 Å
Shell Rg shell_rg	26.47 Å
Envelope Rg envelope_rg	19.28 Å
Shape Rg shape_rg	16.35 Å
Total Rg total_rg	16.72 Å
Total atoms total_atoms	63712
Residues n_residues	3960
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	53.8 Å
Rg (real space) rg_real	16.56 Å
Rg uncertainty (real space) rg_real_error	0.31 Å
I(0) (real space) i0_real	2.5290e+09
I(0) uncertainty (real space) i0_real_error	3.1860e+07
Rg (reciprocal space) rg_reciprocal	16.58 Å
I(0) (reciprocal space) i0_reciprocal	2529000000.0000
Solution quality estimate total_estimate	0.8930
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	22.4 Å
Skewness Skewness skewness	0.040
Kurtosis Kurtosis kurtosis	-0.539
Angular range angular_range	— – 0.4750 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	845300.0000
Real-space data points n_real_points	78
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.870; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.998

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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) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1cnpa_
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

Domain ID domain_id	d1cnpb_
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 (2 domains)

Domain ID domain_id	1cnpA00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	10 — EF-hand

Domain ID domain_id	1cnpB00
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 (3)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Description description	CALCYCLIN (RABBIT, APO)
Molecular weight formula_weight	10167.7 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	63712

fit	/app/data/saxs_computation/cn/1cnp/1cnp.fit
pddf	/app/data/pr_computation/cn/1cnp/1cnp.pr.out
profile	/app/data/saxs_computation/cn/1cnp/1cnp.dat

THE STRUCTURE OF CALCYCLIN REVEALS A NOVEL HOMODIMERIC FOLD FOR S100 CA2+-BINDING PROTEINS, NMR, 22 STRUCTURES

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

CALCYCLIN (RABBIT, APO)

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

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

8. Citations (3)

9. Files and Curves (10)

Files (7)

Curves (3)