1djf

NMR STRUCTURE OF A MODEL HYDROPHILIC AMPHIPATHIC HELICAL BASIC PEPTIDE

Method: SOLUTION NMR D_max: 35.8 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：GLN-ALA-PRO-ALA-TYR-LYS-LYS-ALA-ALA-LYS-LYS-LEU-ALA-GLU-SER × 1 缺少 UniProt 身份时不显示参考序列区间	Entity 1Fragment：HUMAN PLATELET FACTOR 4, SEGMENT 56-70 Entity 1Mutation：L59A, I63A, I64A, L68A	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions：pH 6；293 K；Ionic strength (raw mmCIF value) 10mM SODIUM PHOSPHATE；Pressure AMBIENTNMR sample composition：10MM SODIUM PHOSPHATE BUFFER PH 6.0	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	1djf
Deposition date deposition_date	1999-12-03
Structure title title	NMR STRUCTURE OF A MODEL HYDROPHILIC AMPHIPATHIC HELICAL BASIC PEPTIDE
Keywords keywords	HYDROPHILIC AMPHIPATHIC BASIC HELIX PEPTIDE MODEL, DE NOVO PROTEIN; DE NOVO 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	9.61 Å
Radius of gyration Rg (electron density) rg_electron	8.21 Å
Forward intensity I(0) i0	88477.50
Molecular weight molecular_weight	1607.0 kDa
Excluded volume excluded_volume	2068 Å³
Envelope volume envelope_volume	2418 Å³
Hydration-shell volume shell_volume	3170 Å³
Envelope diameter envelope_diameter	31.4 Å
Shell Rg shell_rg	11.72 Å
Envelope Rg envelope_rg	8.82 Å
Shape Rg shape_rg	8.17 Å
Total Rg total_rg	9.90 Å
Total atoms total_atoms	238
Residues n_residues	15
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	35.8 Å
Rg (real space) rg_real	9.78 Å
Rg uncertainty (real space) rg_real_error	0.49 Å
I(0) (real space) i0_real	8.8480e+04
I(0) uncertainty (real space) i0_real_error	9.7660e+02
Rg (reciprocal space) rg_reciprocal	9.77 Å
I(0) (reciprocal space) i0_reciprocal	88480.0000
Solution quality estimate total_estimate	0.7965
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	10.0 Å
Skewness Skewness skewness	0.616
Kurtosis Kurtosis kurtosis	0.007
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	5976.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.692; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.368; Smooth: 0.905

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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	d1djfa_
Class class	k — Designed proteins
Fold Fold fold	k.2 — Amphiphilic (amphipathic) alpha helix
Superfamily Superfamily superfamily	k.2.1 — Amphiphilic (amphipathic) alpha helix
Family Family family	k.2.1.1 — Amphiphilic (amphipathic) alpha helix

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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	GLN-ALA-PRO-ALA-TYR-LYS-LYS-ALA-ALA-LYS-LYS-LEU-ALA-GLU-SER
Molecular weight formula_weight	1607.9 kDa
Mutation mutation	L59A, I63A, I64A, L68A
Source method src_method	syn
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	238

fit	/app/data/saxs_computation/dj/1djf/1djf.fit
pddf	/app/data/pr_computation/dj/1djf/1djf.pr.out
profile	/app/data/saxs_computation/dj/1djf/1djf.dat

NMR STRUCTURE OF A MODEL HYDROPHILIC AMPHIPATHIC HELICAL BASIC PEPTIDE

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 (1)

9. Files and Curves (10)

Files (7)

Curves (3)