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1mnb

BIV TAT PEPTIDE (RESIDUES 68-81), NMR, MINIMIZED AVERAGE STRUCTURE

Method: SOLUTION NMR Dmax: 51.4 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

BIV TAT PEPTIDE

OrganismNot specified

UniProt P19564

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 A； UniProt 68–81 Fragment：RESIDUES 68 - 81 BIV TAR RNA × 1 SOLUTION NMR NMR measurement conditions：pH 6.4；298 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.

Other PDB Difference from Current Entry 1MNB Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1BIV BOVINE IMMUNODEFICIENCY VIRUS TAT-TAR COMPLEX, NMR, 5 STRUCTURES Deposited 1996-06-12 Different construct Different experimental conditions Assembly 1 Protein–RNA Monomer；Protein × 1 PDB declaration: dimeric
Chain B 65–81（17 aa） Fragment：RESIDUES 65 - 81
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.8；298 K
Resolution not provided

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TAT_BIV06
Isoform —
PDB entities 2
Chains and sequence ranges Author chain A； PDBConstruct 1–14； UniProt 68–81

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

SAXS profile for 1mnb

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1mnb
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1mnb
Deposition date deposition_date1996-07-25
Structure title titleBIV TAT PEPTIDE (RESIDUES 68-81), NMR, MINIMIZED AVERAGE STRUCTURE
Keywords keywordsCOMPLEX (REGULATORY PROTEIN-RNA), TRANSCRIPTION REGULATION, Viral protein-RNA COMPLEX; Viral protein/RNA
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier14.91 Å
Radius of gyration Rg (electron density) rg_electron14.18 Å
Forward intensity I(0) i05679510.00
Molecular weight molecular_weight10727.0 kDa
Excluded volume excluded_volume10505 ų
Envelope volume envelope_volume14469 ų
Hydration-shell volume shell_volume9517 ų
Envelope diameter envelope_diameter51.0 Å
Shell Rg shell_rg18.51 Å
Envelope Rg envelope_rg14.50 Å
Shape Rg shape_rg14.08 Å
Total Rg total_rg14.95 Å
Total atoms total_atoms1145
Residues n_residues42
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax51.4 Å
Rg (real space) rg_real14.97 Å
Rg uncertainty (real space) rg_real_error0.33 Å
I(0) (real space) i0_real5.6800e+06
I(0) uncertainty (real space) i0_real_error6.0890e+04
Rg (reciprocal space) rg_reciprocal14.96 Å
I(0) (reciprocal space) i0_reciprocal5680000.0000
Solution quality estimate total_estimate0.8479
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.9 Å
Skewness Skewness skewness0.478
Kurtosis Kurtosis kurtosis-0.069
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha418300.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.736; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.924; Smooth: 0.888
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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_idd1mnba_
Class classj — Peptides
Fold Fold foldj.9 — Arg-rich RNA binding peptides
Superfamily Superfamily superfamilyj.9.4 — TAT peptides
Family Family familyj.9.4.1 — TAT peptides
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8. Citations (1)

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9. Files and Curves (10)