SAXSdb — 1a66

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

CORE NFATC1

Homo sapiens

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–DNA Monomer Protein × 1 DNA 2 PDB declaration: trimeric（3） Consistent with all polymer counts	Chain A； UniProt 414–591	Fragment：DNA BINDING DOMAIN OF NFATC1 Mutation：A1M, L2K, H28R	;DNA (5'-D(CPGPAPGPGPAPAPAPAPTPTPG)-3') ; × 1 ;DNA (5'-D(CPAPAPTPTPTPTPCPCPTPCPG)-3') ; × 1	SOLUTION NMR NMR measurement conditions：pH 6.5；300 K	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 1A66	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1NFA HUMAN TRANSCRIPTION FACTOR NFATC DNA BINDING DOMAIN, NMR, 10 STRUCTURES Deposited 1997-01-18	Different construct Different mutation/modification Different oligomeric state	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 416–591（176 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 416 - 591	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；300 K	Resolution not provided

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

View Construct and Data Evidence

UniProt name	NFAC1_HUMAN
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain A； PDBConstruct 1–178； UniProt 414–591

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	1a66
Deposition date deposition_date	1998-03-06
Structure title title	SOLUTION NMR STRUCTURE OF THE CORE NFATC1/DNA COMPLEX, 18 STRUCTURES
Keywords keywords	;NFATC1/DNA, REL, NFAT/DNA, ARRE2, NFAT, NFATC1, NFATC, NFAT2, BINARY COMPLEX, TRANSCRIPTION FACTOR, ENHANCEOSOME, IL-2, COMPLEX, BINARY, TRANSCRIPTION-DNA COMPLEX ;; TRANSCRIPTION/DNA
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	20.14 Å
Radius of gyration Rg (electron density) rg_electron	19.89 Å
Forward intensity I(0) i0	4762190000.00
Molecular weight molecular_weight	491180.0 kDa
Excluded volume excluded_volume	576050 Å³
Envelope volume envelope_volume	66713 Å³
Hydration-shell volume shell_volume	25233 Å³
Envelope diameter envelope_diameter	76.8 Å
Shell Rg shell_rg	29.43 Å
Envelope Rg envelope_rg	22.62 Å
Shape Rg shape_rg	19.84 Å
Total Rg total_rg	20.11 Å
Total atoms total_atoms	64710
Residues n_residues	3636
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	69.4 Å
Rg (real space) rg_real	20.24 Å
Rg uncertainty (real space) rg_real_error	0.61 Å
I(0) (real space) i0_real	4.7620e+09
I(0) uncertainty (real space) i0_real_error	6.6240e+07
Rg (reciprocal space) rg_reciprocal	20.23 Å
I(0) (reciprocal space) i0_reciprocal	4762000000.0000
Solution quality estimate total_estimate	0.8650
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	20.8 Å
Skewness Skewness skewness	0.493
Kurtosis Kurtosis kurtosis	-0.200
Angular range angular_range	— – 0.3950 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	2170000.0000
Real-space data points n_real_points	71
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.789; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.887; Smooth: 0.991

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	;DNA (5'-D(CPGPAPGPGPAPAPAPAPTPTPG)-3') ;
Molecular weight formula_weight	3735.5 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polydeoxyribonucleotide
Chain IDs strand_id	B
Atom count atom_count	64710

CGAGGAAAATTG

Entity 2 Entity 2 polymer

Description description	;DNA (5'-D(CPAPAPTPTPTPTPCPCPTPCPG)-3') ;
Molecular weight formula_weight	3588.4 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polydeoxyribonucleotide
Chain IDs strand_id	C

CAATTTTCCTCG

Entity 3 Entity 3 polymer

Description description	CORE NFATC1
Molecular weight formula_weight	20004.9 kDa
Mutation mutation	A1M, L2K, H28R
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A

MKDWQLPSHSGPYELRIEVQPKSHHRARYETEGSRGAVKASAGGHPIVQLHGYLENEPLMLQLFIGTADDRLLRPHAFYQVHRITGKTVSTTSHEAILSNTKVLEIPLLPENSMRAVIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHVPQPSGRTLSLQVASNPIECSQRS

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli BL21(DE3)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1a66a_
Class class	b — All beta proteins
Fold Fold fold	b.2 — Common fold of diphtheria toxin/transcription factors/cytochrome f
Superfamily Superfamily superfamily	b.2.5 — p53-like transcription factors
Family Family family	b.2.5.3 — Rel/Dorsal transcription factors, DNA-binding domain

CATH v4.4 (1 domains)

Domain ID domain_id	1a66A00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	340 — Rel homology domain (RHD), DNA-binding domain

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8. Citations (1)

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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	—

fit	/app/data/saxs_computation/a6/1a66/1a66.fit
pddf	/app/data/pr_computation/a6/1a66/1a66.pr.out
profile	/app/data/saxs_computation/a6/1a66/1a66.dat

SOLUTION NMR STRUCTURE OF THE CORE NFATC1/DNA COMPLEX, 18 STRUCTURES

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

CORE NFATC1

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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

来源 Source

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)