BMRB Entry 4869
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4869
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Allain, F.; Yen, Y.; Masse, J.; Schultze, P.; Dieckmann, T.; Johnson, R.; Feigon, J.. "Solution Structure of the Hmg Protein Nhp6A and its Interaction with DNA Reveals
the Structural Determinants for Non-sequence-specific Binding" EMBO J. 18, 2563-2579 (1999).
PubMed: 10228169
Assembly members:
PROTEIN (NON HISTONE PROTEIN 6 A), polymer, 93 residues, Formula weight is not available
Natural source: Common Name: yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
PROTEIN (NON HISTONE PROTEIN 6 A): MVTPREPKKRTTRKKKDPNA
PKRALSAYMFFANENRDIVR
SENPDITFGQVGKKLGEKWK
ALTPEEKQPYEAKAQADKKR
YESEKELYNATLA
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 548 |
| 13C chemical shifts | 249 |
| 15N chemical shifts | 83 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | nhp6a | 1 |
Entities:
Entity 1, nhp6a 93 residues - Formula weight is not available
| 1 | MET | VAL | THR | PRO | ARG | GLU | PRO | LYS | LYS | ARG | ||||
| 2 | THR | THR | ARG | LYS | LYS | LYS | ASP | PRO | ASN | ALA | ||||
| 3 | PRO | LYS | ARG | ALA | LEU | SER | ALA | TYR | MET | PHE | ||||
| 4 | PHE | ALA | ASN | GLU | ASN | ARG | ASP | ILE | VAL | ARG | ||||
| 5 | SER | GLU | ASN | PRO | ASP | ILE | THR | PHE | GLY | GLN | ||||
| 6 | VAL | GLY | LYS | LYS | LEU | GLY | GLU | LYS | TRP | LYS | ||||
| 7 | ALA | LEU | THR | PRO | GLU | GLU | LYS | GLN | PRO | TYR | ||||
| 8 | GLU | ALA | LYS | ALA | GLN | ALA | ASP | LYS | LYS | ARG | ||||
| 9 | TYR | GLU | SER | GLU | LYS | GLU | LEU | TYR | ASN | ALA | ||||
| 10 | THR | LEU | ALA |
Samples:
sample_1: PROTEIN (NON HISTONE PROTEIN 6 A), [U-13C; U-15N], 1.0 mM
sample_cond_1: pH: 5.5; temperature: 293 K; ionic strength: 100 mM
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 15N and 13C-separated 3D NOESY | not available | not available | not available |
| 3D HNCA | not available | not available | not available |
| 3D HN(CO)CA | not available | not available | not available |
| 3D HN(CO)CACB | not available | not available | not available |
| 3D HCCH-TOCSY | not available | not available | not available |
| 3D 15N-TOCSY | not available | not available | not available |
Software:
DYANA - refinement, structure calculation
FELIX - resonance assignments
XEASY - NOE cross-peaks assignments
XWINNMR - data processing, data acquisitions
NMR spectrometers:
- Bruker DRX 600 MHz
- Bruker DRX 500 MHz
Related Database Links:
| PDB | |
| DBJ | GAA27020 |
| EMBL | CAA33377 CAA89171 CAA94998 CAY87008 |
| GB | AAA34754 AAT93249 AHY78218 EDN61184 EDV11256 |
| REF | NP_015377 |
| SP | P11632 |
| TPG | DAA11475 |
| AlphaFold | P11632 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks