SAXSdb — 1m8c

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

Ovomucoid

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 130–185	Fragment：RESIDUES 130-185; KAZAL-LIKE 3 (INHIBIT CHYMOTRYPIN, ELASTASE, ETC.) Mutation：P14D	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 2.5；298 K；Ionic strength (raw mmCIF value) no salt added；Pressure ambient NMR sample composition：1 mM \| 90% H2O/10% D2O NMR sample composition：1 mM \| 100% 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 1M8C	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1M8B Solution structure of the C State of turkey ovomucoid at pH 2.5 Deposited 2002-07-24	Parsed fields agree	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 130–185（56 aa） Fragment：RESIDUES 130-185; KAZAL-LIKE 3 (INHIBIT CHYMOTRYPIN, ELASTASE, ETC.)	Mutation：P14D	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 2.5；298 K；Ionic strength (raw mmCIF value) no salt added；Pressure ambient NMR sample composition 1 mM \| 90% H2O/10% D2O NMR sample composition 1 mM \| 100% D2O	Resolution not provided
1PPF X-RAY CRYSTAL STRUCTURE OF THE COMPLEX OF HUMAN LEUKOCYTE ELASTASE (PMN ELASTASE) AND THE THIRD DOMAIN OF THE TURKEY OVOMUCOID INHIBITOR Deposited 1991-10-24	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain I 130–185（56 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.80 Å

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

View Construct and Data Evidence

UniProt name	IOVO_MELGA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–56； UniProt 130–185

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	1m8c
Deposition date deposition_date	2002-07-24
Structure title title	SOLUTION STRUCTURE OF THE T State OF TURKEY OVOMUCOID AT PH 2.5
Keywords keywords	OMTKY3 CONFORMATIONAL TRANSITION T STATE, CIS-TRANS ISOMERIZATION, HYDROLASE INHIBITOR; HYDROLASE INHIBITOR
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	10.54 Å
Radius of gyration Rg (electron density) rg_electron	10.67 Å
Forward intensity I(0) i0	234572000.00
Molecular weight molecular_weight	120420.0 kDa
Excluded volume excluded_volume	146970 Å³
Envelope volume envelope_volume	14571 Å³
Hydration-shell volume shell_volume	9980 Å³
Envelope diameter envelope_diameter	42.7 Å
Shell Rg shell_rg	18.15 Å
Envelope Rg envelope_rg	13.21 Å
Shape Rg shape_rg	10.65 Å
Total Rg total_rg	10.94 Å
Total atoms total_atoms	15100
Residues n_residues	1120
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	38.5 Å
Rg (real space) rg_real	10.47 Å
Rg uncertainty (real space) rg_real_error	0.46 Å
I(0) (real space) i0_real	2.3460e+08
I(0) uncertainty (real space) i0_real_error	2.7000e+06
Rg (reciprocal space) rg_reciprocal	10.48 Å
I(0) (reciprocal space) i0_reciprocal	234600000.0000
Solution quality estimate total_estimate	0.8495
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	3
Primary peak position r_peak_primary	14.1 Å
Skewness Skewness skewness	-0.005
Kurtosis Kurtosis kurtosis	-0.561
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	31480.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.700; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.958; Smooth: 0.983

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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) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1m8ca_
Class class	g — Small proteins
Fold Fold fold	g.68 — Kazal-type serine protease inhibitors
Superfamily Superfamily superfamily	g.68.1 — Kazal-type serine protease inhibitors
Family Family family	g.68.1.1 — Ovomucoid domain III-like

CATH v4.4 (1 domains)

Domain ID domain_id	1m8cA00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	60 — Wheat Germ Agglutinin (Isolectin 2); domain 1
Homologous superfamily homologous superfamily	30 —

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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	Ovomucoid
Molecular weight formula_weight	6044.8 kDa
Mutation mutation	P14D
Source method src_method	syn
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	15100

fit	/app/data/saxs_computation/m8/1m8c/1m8c.fit
pddf	/app/data/pr_computation/m8/1m8c/1m8c.pr.out
profile	/app/data/saxs_computation/m8/1m8c/1m8c.dat

SOLUTION STRUCTURE OF THE T State OF TURKEY OVOMUCOID AT PH 2.5

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

Ovomucoid

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) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)