BMRB Entry 4869

Title:
HMG PROTEIN NHP6A FROM SACCHAROMYCES CEREVISIAE
Deposition date:
2000-10-19
Original release date:
2001-11-14
Authors:
Allain, F.; Yen, Y.; Masse, J.; Schultze, P.; Dieckmann, T.; Johnson, R.; Feigon, J.
Citation:

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:

Assembly members:
PROTEIN (NON HISTONE PROTEIN 6 A), polymer, 93 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):

Data sets:
Data typeCount
1H chemical shifts548
13C chemical shifts249
15N chemical shifts83

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1nhp6a1

Entities:

Entity 1, nhp6a 93 residues - Formula weight is not available

1   METVALTHRPROARGGLUPROLYSLYSARG
2   THRTHRARGLYSLYSLYSASPPROASNALA
3   PROLYSARGALALEUSERALATYRMETPHE
4   PHEALAASNGLUASNARGASPILEVALARG
5   SERGLUASNPROASPILETHRPHEGLYGLN
6   VALGLYLYSLYSLEUGLYGLULYSTRPLYS
7   ALALEUTHRPROGLUGLULYSGLNPROTYR
8   GLUALALYSALAGLNALAASPLYSLYSARG
9   TYRGLUSERGLULYSGLULEUTYRASNALA
10   THRLEUALA

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:

NameSampleSample stateSample conditions
15N and 13C-separated 3D NOESYnot availablenot availablenot available
3D HNCAnot availablenot availablenot available
3D HN(CO)CAnot availablenot availablenot available
3D HN(CO)CACBnot availablenot availablenot available
3D HCCH-TOCSYnot availablenot availablenot available
3D 15N-TOCSYnot availablenot availablenot 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