1d6x

THE STRUCTURE OF THE ANTIMICROBIAL PEPTIDE TRITRPTICIN BOUND TO MICELLES-A DISTINCT MEMBRANE-BOUND PEPTIDE FOLD

Method: SOLUTION NMR D_max: 32.0 Å Quality: GOOD

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

No usable UniProt protein identity is available for this entry.

七张关系表仍保留该条目的 assembly 与组成信息，但缺少统一蛋白身份时，不能可靠建立跨 PDB 的同蛋白Chain接。

Assembly Composition of the Current Entry

Assembly	Oligomeric State	实体与Construct证据	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein monomer Monomer 蛋白 1 / DNA 0 / RNA 0 / 其他Polymer 0 PDB declaration: monomeric	Entity 1：ANTIMICROBIAL PEPTIDE, TRITRPTICIN × 1 缺少 UniProt 身份时不显示参考序列区间	Entity 1Fragment：SYNTHETIC CATHELICIDIN FRAGMENT	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions：pH 4.5；313 K；Ionic strength (raw mmCIF value) 400 mM SDS；Pressure AMBIENTNMR sample composition：3 MM TRITRPTICIN, 400 MM PERDEUTERATED SDSNMR sample composition：3 MM TRITRPTICIN, 400 MM PERDEUTERATED SDS	Resolution not provided

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.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1d6x
Deposition date deposition_date	1999-10-15
Structure title title	THE STRUCTURE OF THE ANTIMICROBIAL PEPTIDE TRITRPTICIN BOUND TO MICELLES-A DISTINCT MEMBRANE-BOUND PEPTIDE FOLD
Keywords keywords	TYPE IV TURN-TYPE III TURN, IMMUNE SYSTEM; IMMUNE SYSTEM
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	8.12 Å
Radius of gyration Rg (electron density) rg_electron	8.04 Å
Forward intensity I(0) i0	14990000.00
Molecular weight molecular_weight	36220.0 kDa
Excluded volume excluded_volume	47077 Å³
Envelope volume envelope_volume	7986 Å³
Hydration-shell volume shell_volume	7055 Å³
Envelope diameter envelope_diameter	32.2 Å
Shell Rg shell_rg	15.15 Å
Envelope Rg envelope_rg	10.41 Å
Shape Rg shape_rg	7.96 Å
Total Rg total_rg	8.90 Å
Total atoms total_atoms	5206
Residues n_residues	247
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	32.0 Å
Rg (real space) rg_real	8.18 Å
Rg uncertainty (real space) rg_real_error	0.56 Å
I(0) (real space) i0_real	1.4990e+07
I(0) uncertainty (real space) i0_real_error	1.7730e+05
Rg (reciprocal space) rg_reciprocal	8.18 Å
I(0) (reciprocal space) i0_reciprocal	14990000.0000
Solution quality estimate total_estimate	0.8013
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	3
Primary peak position r_peak_primary	9.7 Å
Skewness Skewness skewness	0.384
Kurtosis Kurtosis kurtosis	-0.129
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	3603.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.677; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.476; Smooth: 0.911

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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) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1d6xa_
Class class	j — Peptides
Fold Fold fold	j.27 — Membrane-bound antimicrobial peptides
Superfamily Superfamily superfamily	j.27.1 — Membrane-bound antimicrobial peptides
Family Family family	j.27.1.1 — Membrane-bound antimicrobial peptides

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8. Citations (2)

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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	ANTIMICROBIAL PEPTIDE, TRITRPTICIN
Molecular weight formula_weight	1906.3 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	5206

fit	/app/data/saxs_computation/d6/1d6x/1d6x.fit
pddf	/app/data/pr_computation/d6/1d6x/1d6x.pr.out
profile	/app/data/saxs_computation/d6/1d6x/1d6x.dat

THE STRUCTURE OF THE ANTIMICROBIAL PEPTIDE TRITRPTICIN BOUND TO MICELLES-A DISTINCT MEMBRANE-BOUND PEPTIDE FOLD

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

Assembly Composition of the Current Entry

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) 1 domains

SCOP 2.08 (1 domains)

8. Citations (2)

9. Files and Curves (10)

Files (7)

Curves (3)