1a4t

SOLUTION STRUCTURE OF PHAGE P22 N PEPTIDE-BOX B RNA COMPLEX, NMR, 20 STRUCTURES

Method: SOLUTION NMR D_max: 38.9 Å Quality: GOOD

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

20-MER BASIC PEPTIDE

Enterobacteria phage P22

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–RNA Monomer Protein × 1 RNA 1 PDB declaration: dimeric（2） Consistent with all polymer counts	Chain B； UniProt 14–32	Not recorded	BOXB RNA × 1	SOLUTION NMR NMR measurement conditions：pH 5.7；297 K	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	REGN_BPP22
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–19； UniProt 14–32

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	1a4t
Deposition date deposition_date	1998-02-04
Structure title title	SOLUTION STRUCTURE OF PHAGE P22 N PEPTIDE-BOX B RNA COMPLEX, NMR, 20 STRUCTURES
Keywords keywords	;BACTERIOPHAGE TRANSCRIPTIONAL ANTITERMINATION, PEPTIDE-RNA RECOGNITION, GNRA LOOP, BENT ALPHA-HELICAL PEPTIDE, TRANSCRIPTION REGULATION, TRANSCRIPTION-RNA COMPLEX ;; TRANSCRIPTION/RNA
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	11.05 Å
Radius of gyration Rg (electron density) rg_electron	11.29 Å
Forward intensity I(0) i0	705725000.00
Molecular weight molecular_weight	144760.0 kDa
Excluded volume excluded_volume	148510 Å³
Envelope volume envelope_volume	12351 Å³
Hydration-shell volume shell_volume	8999 Å³
Envelope diameter envelope_diameter	44.0 Å
Shell Rg shell_rg	17.40 Å
Envelope Rg envelope_rg	12.63 Å
Shape Rg shape_rg	11.25 Å
Total Rg total_rg	11.45 Å
Total atoms total_atoms	16720
Residues n_residues	680
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	38.9 Å
Rg (real space) rg_real	11.06 Å
Rg uncertainty (real space) rg_real_error	0.34 Å
I(0) (real space) i0_real	7.0570e+08
I(0) uncertainty (real space) i0_real_error	7.0710e+06
Rg (reciprocal space) rg_reciprocal	11.06 Å
I(0) (reciprocal space) i0_reciprocal	705700000.0000
Solution quality estimate total_estimate	0.8473
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	13.8 Å
Skewness Skewness skewness	0.427
Kurtosis Kurtosis kurtosis	0.102
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	85910.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.713; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.938; Smooth: 0.933

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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) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1a4tb_
Class class	j — Peptides
Fold Fold fold	j.9 — Arg-rich RNA binding peptides
Superfamily Superfamily superfamily	j.9.5 — Box B RNA-binding N peptide
Family Family family	j.9.5.1 — Box B RNA-binding N peptide

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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	BOXB RNA
Molecular weight formula_weight	4830.0 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer type type	polyribonucleotide
Chain IDs strand_id	A
Atom count atom_count	16720

Description description	20-MER BASIC PEPTIDE
Molecular weight formula_weight	2415.8 kDa
Source method src_method	man
Copy count entity_count	1

SOLUTION STRUCTURE OF PHAGE P22 N PEPTIDE-BOX B RNA COMPLEX, NMR, 20 STRUCTURES

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

20-MER BASIC PEPTIDE

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

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Enterobacteria phage P22
NCBI Class编号 ncbi_taxonomy_id	10754

fit	/app/data/saxs_computation/a4/1a4t/1a4t.fit
pddf	/app/data/pr_computation/a4/1a4t/1a4t.pr.out
profile	/app/data/saxs_computation/a4/1a4t/1a4t.dat