SAXSdb — 1d8v

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

ANTI-HIV AND ANTI-TUMOR PROTEIN MAP30

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 24–286	Not recorded	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 5.5；313 K；Ionic strength (raw mmCIF value) 10 mM NAPI；Pressure 1 NMR sample composition：~0.7 MM PROTEIN MAP30 (15N/13C) ENRICHED.	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.

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

View Construct and Data Evidence

UniProt name	RIP3_MOMCH
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–263； UniProt 24–286

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	1d8v
Deposition date deposition_date	1999-10-26
Structure title title	THE RESTRAINED AND MINIMIZED AVERAGE NMR STRUCTURE OF MAP30.
Keywords keywords	SINGLE CHAIN, ANTITUMOR PROTEIN; ANTITUMOR 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	20.50 Å
Radius of gyration Rg (electron density) rg_electron	19.22 Å
Forward intensity I(0) i0	14313800.00
Molecular weight molecular_weight	29604.0 kDa
Excluded volume excluded_volume	37628 Å³
Envelope volume envelope_volume	45507 Å³
Hydration-shell volume shell_volume	19808 Å³
Envelope diameter envelope_diameter	69.0 Å
Shell Rg shell_rg	25.64 Å
Envelope Rg envelope_rg	19.80 Å
Shape Rg shape_rg	19.18 Å
Total Rg total_rg	20.31 Å
Total atoms total_atoms	4208
Residues n_residues	263
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	68.7 Å
Rg (real space) rg_real	20.43 Å
Rg uncertainty (real space) rg_real_error	0.45 Å
I(0) (real space) i0_real	1.4310e+07
I(0) uncertainty (real space) i0_real_error	1.8410e+05
Rg (reciprocal space) rg_reciprocal	20.45 Å
I(0) (reciprocal space) i0_reciprocal	14310000.0000
Solution quality estimate total_estimate	0.8746
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	26.5 Å
Skewness Skewness skewness	0.277
Kurtosis Kurtosis kurtosis	-0.241
Angular range angular_range	— – 0.3900 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	3464000.0000
Real-space data points n_real_points	71
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.790; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.994

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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 (1 domains)

Domain ID domain_id	d1d8va_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.165 — Ribosome inactivating proteins (RIP)
Superfamily Superfamily superfamily	d.165.1 — Ribosome inactivating proteins (RIP)
Family Family family	d.165.1.1 — Plant cytotoxins

CATH v4.4 (2 domains)

Domain ID domain_id	1d8vA01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	420 — Ricin (A subunit); domain 1
Homologous superfamily homologous superfamily	10 — Ricin (A subunit), domain 1

Domain ID domain_id	1d8vA02
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	470 — Ricin (A Subunit), domain 2
Homologous superfamily homologous superfamily	10 — Ricin (A Subunit), domain 2

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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	ANTI-HIV AND ANTI-TUMOR PROTEIN MAP30
Molecular weight formula_weight	29630.6 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	4208

fit	/app/data/saxs_computation/d8/1d8v/1d8v.fit
pddf	/app/data/pr_computation/d8/1d8v/1d8v.pr.out
profile	/app/data/saxs_computation/d8/1d8v/1d8v.dat

THE RESTRAINED AND MINIMIZED AVERAGE NMR STRUCTURE OF MAP30.

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

ANTI-HIV AND ANTI-TUMOR PROTEIN MAP30

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) 3 domains

SCOP 2.08 (1 domains)

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)