SAXSdb — 1f96

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

DYNEIN LIGHT CHAIN 8

Rattus norvegicus

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 1–89 Chain B； UniProt 1–89	Fragment：DLC8 BINDING REGION	PROTEIN (NNOS, NEURONAL NITRIC OXIDE SYNTHASE) × 2	SOLUTION NMR NMR measurement conditions：pH 7；303 K；Ionic strength (raw mmCIF value) 100mM；Pressure ambient NMR sample composition：1.5mM DLC8/nNOS ppetide complex 15N; 100mM phosphate buffer; 10mM DTT; 90%H2O and 10% D2O \| 90%H2O and 10% D2O NMR sample composition：1.5mM DLC8/nNOS ppetide complex 15N,13C; 100mM phosphate buffer; 10mM DTT; 90%H2O and 10% D2O \| 90%H2O and 10% D2O NMR sample composition：1.5mM DLC8/nNOS ppetide complex ; 100mM phosphate buffer; 10mM DTT; 99.9% D2O \| 99.9% D2O	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 1F96	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1F3C REFINED SOLUTION STRUCTURE OF 8KDA DYNEIN LIGHT CHAIN (DLC8) Deposited 2000-06-02	Different construct Different oligomeric state Different experimental conditions	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–89（89 aa） Fragment：8KDA LIGHT CHAIN Chain B 1–89（89 aa） Fragment：8KDA LIGHT CHAIN	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；303 K NMR sample composition 1.5mM DLC8; 100mM phosphate buffer NA; 99.99% D2O \| 99.99% D2O NMR sample composition 1.5mM DLC8 U-15N;100mM phosphate buffer NA; 90% H2O, 10% D2O \| 90% H2O/10% D2O NMR sample composition 1.5mM DLC8 U-15N,13C;100mM phosphate buffer NA; 90% H2O, 10% D2O \| 90% H2O/10% D2O	Resolution not provided
1F95 SOLUTION STRUCTURE OF DYNEIN LIGHT CHAIN 8 (DLC8) AND BIM PEPTIDE COMPLEX Deposited 2000-07-07	Different construct Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–89（89 aa） Fragment：8KDA LIGHT CHAIN Chain B 1–89（89 aa） Fragment：8KDA LIGHT CHAIN	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；303 K；Ionic strength (raw mmCIF value) 100mM；Pressure ambient NMR sample composition 1.5mM DLC8/Bim peptide complex 15N; 100mM phosphate buffer; 10mM DTT; 90% H2O and 10% D2O \| 90% H2O and 10% D2O NMR sample composition 1.5mM DLC8/Bim peptide complex 15N,13C; 100mM phosphate buffer; 10mM DTT; 90% H2O and 10% D2O \| 90% H2O and 10% D2O NMR sample composition 1.5mM DLC8/Bim peptide complex ; 100mM phosphate buffer; 10mM DTT; 99.9% D2O \| 99.9% D2O	Resolution not provided

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	DYL1_RAT
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–89； UniProt 1–89 Author chain B； PDBConstruct 1–89； UniProt 1–89

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	1f96
Deposition date deposition_date	2000-07-07
Structure title title	SOLUTION STRUCTURE OF DYNEIN LIGHT CHAIN 8 (DLC8) AND NNOS PEPTIDE COMPLEX
Keywords keywords	dynein, light chain, DLC8, nNOS, INHIBITOR-OXIDOREDUCTASE COMPLEX; INHIBITOR/OXIDOREDUCTASE
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	17.69 Å
Radius of gyration Rg (electron density) rg_electron	17.20 Å
Forward intensity I(0) i0	3479310000.00
Molecular weight molecular_weight	496110.0 kDa
Excluded volume excluded_volume	618080 Å³
Envelope volume envelope_volume	60105 Å³
Hydration-shell volume shell_volume	23975 Å³
Envelope diameter envelope_diameter	72.3 Å
Shell Rg shell_rg	27.93 Å
Envelope Rg envelope_rg	20.92 Å
Shape Rg shape_rg	17.11 Å
Total Rg total_rg	17.66 Å
Total atoms total_atoms	69260
Residues n_residues	4280
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	62.3 Å
Rg (real space) rg_real	17.62 Å
Rg uncertainty (real space) rg_real_error	0.43 Å
I(0) (real space) i0_real	3.4790e+09
I(0) uncertainty (real space) i0_real_error	4.4520e+07
Rg (reciprocal space) rg_reciprocal	17.63 Å
I(0) (reciprocal space) i0_reciprocal	3479000000.0000
Solution quality estimate total_estimate	0.7730
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	3
Primary peak position r_peak_primary	22.4 Å
Skewness Skewness skewness	0.266
Kurtosis Kurtosis kurtosis	-0.261
Angular range angular_range	— – 0.4500 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	2160000.0000
Real-space data points n_real_points	76
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.695; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.965; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1f96a_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.39 — DLC
Superfamily Superfamily superfamily	d.39.1 — DLC
Family Family family	d.39.1.1 — DLC

Domain ID domain_id	d1f96b_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.39 — DLC
Superfamily Superfamily superfamily	d.39.1 — DLC
Family Family family	d.39.1.1 — DLC

CATH v4.4 (2 domains)

Domain ID domain_id	1f96A00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	740 — Protein Inhibitor Of Neuronal Nitric Oxide Synthase
Homologous superfamily homologous superfamily	10 — Protein Inhibitor Of Neuronal Nitric Oxide Synthase;

Domain ID domain_id	1f96B00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	740 — Protein Inhibitor Of Neuronal Nitric Oxide Synthase
Homologous superfamily homologous superfamily	10 — Protein Inhibitor Of Neuronal Nitric Oxide Synthase;

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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	DYNEIN LIGHT CHAIN 8
Molecular weight formula_weight	10381.9 kDa
Source method src_method	man
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	69260

来源生物 organism	Rattus norvegicus
通用名 common_name	Norway rat
NCBI Class编号 ncbi_taxonomy_id	10116
宿主生物 host_organism	Escherichia coli

SOLUTION STRUCTURE OF DYNEIN LIGHT CHAIN 8 (DLC8) AND NNOS PEPTIDE COMPLEX

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

DYNEIN LIGHT CHAIN 8

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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/f9/1f96/1f96.fit
pddf	/app/data/pr_computation/f9/1f96/1f96.pr.out
profile	/app/data/saxs_computation/f9/1f96/1f96.dat