SAXSdb — 1nfa

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

HUMAN TRANSCRIPTION FACTOR 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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 416–591	Fragment：DNA-BINDING DOMAIN, RESIDUES 416 - 591	No other associated polymer	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 1NFA	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1A66 SOLUTION NMR STRUCTURE OF THE CORE NFATC1/DNA COMPLEX, 18 STRUCTURES Deposited 1998-03-06	Different construct Different mutation/modification Different oligomeric state	Assembly 1 Protein–DNA Monomer；Protein × 1 PDB declaration: trimeric	Chain A 414–591（178 aa） Fragment：DNA BINDING DOMAIN OF NFATC1	Mutation：A1M, L2K, H28R	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	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–178； UniProt 416–591

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	1nfa
Deposition date deposition_date	1997-01-18
Structure title title	HUMAN TRANSCRIPTION FACTOR NFATC DNA BINDING DOMAIN, NMR, 10 STRUCTURES
Keywords keywords	NFAT, TRANSCRIPTION REGULATION, REL-HOMOLOGY FOLD, ACTIVATES CYTOKINE TRANSCRIPTION; TRANSCRIPTION REGULATION
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	19.53 Å
Radius of gyration Rg (electron density) rg_electron	19.00 Å
Forward intensity I(0) i0	596280000.00
Molecular weight molecular_weight	199580.0 kDa
Excluded volume excluded_volume	248420 Å³
Envelope volume envelope_volume	71834 Å³
Hydration-shell volume shell_volume	25579 Å³
Envelope diameter envelope_diameter	83.3 Å
Shell Rg shell_rg	30.70 Å
Envelope Rg envelope_rg	24.45 Å
Shape Rg shape_rg	18.98 Å
Total Rg total_rg	19.43 Å
Total atoms total_atoms	28270
Residues n_residues	1780
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	77.5 Å
Rg (real space) rg_real	19.65 Å
Rg uncertainty (real space) rg_real_error	0.70 Å
I(0) (real space) i0_real	5.9630e+08
I(0) uncertainty (real space) i0_real_error	8.1840e+06
Rg (reciprocal space) rg_reciprocal	19.63 Å
I(0) (reciprocal space) i0_reciprocal	596300000.0000
Solution quality estimate total_estimate	0.7484
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	20.8 Å
Skewness Skewness skewness	0.583
Kurtosis Kurtosis kurtosis	0.179
Angular range angular_range	— – 0.4050 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	3063000.0000
Real-space data points n_real_points	72
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.400; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.526; Smooth: 0.999

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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) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1nfaa1
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

Domain ID domain_id	d1nfaa2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id	1nfaA00
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	—

Description description	HUMAN TRANSCRIPTION FACTOR NFATC1
Molecular weight formula_weight	19985.9 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	28270

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

HUMAN TRANSCRIPTION FACTOR NFATC DNA BINDING DOMAIN, NMR, 10 STRUCTURES

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

HUMAN TRANSCRIPTION FACTOR 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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/nf/1nfa/1nfa.fit
pddf	/app/data/pr_computation/nf/1nfa/1nfa.pr.out
profile	/app/data/saxs_computation/nf/1nfa/1nfa.dat