BMRB Entry 5390

Click here to enlarge.

PDB ID: 1lr1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5390
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

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

1H,13C and 15N Chemical Shifts Assignments for the Oligomerization Domain of H-NS

Deposition date:

2002-06-12

Original release date:

2003-02-25

Authors:

Esposito, D.; Petrovic, A.; Harris, R.; Shusuke, O.; Eccleston, J.; Mbabaali, A.; Haq, I.; Higgins, C.; Hinton, J.; Driscoll, P.; Ladbury, J.

Citation:

Citation: Esposito, D.; Petrovic, A.; Harris, R.; Ono, S.; Eccleston, J.; Mbabaali, A.; Haq, I.; Higgins, C.; Hinton, J.; Driscoll, P.; Ladbury, J.. "H-NS Oligomerization Domain Structure Reveals the Mechanism for High Order Self-association of the Intact Protein" J. Mol. Biol. 324, 841-850 (2002).
PubMed: 12460581

Assembly members:

Assembly members:
H-NS, polymer, 61 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
H-NS: GSHMSEALKILNNIRTLRAQ ARESTLETLEEMLEKLEVVV NERREEESAAAAEVEERTRK L

Data sets:

assigned_chemical_shifts
- chemical_shift_set_1

Data type	Count
1H chemical shifts	366
13C chemical shifts	193
15N chemical shifts	62

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	dna-binding protein h-ns, chain A	1
2	dna-binding protein h-ns, chain B	1

Entities:

Entity 1, dna-binding protein h-ns, chain A 61 residues - Formula weight is not available

1

GLY

SER

HIS

MET

SER

GLU

ALA

LEU

LYS

ILE

2

LEU

ASN

ILE

ARG

THR

LEU

ARG

ALA

GLN

3

ALA

ARG

GLU

SER

THR

LEU

GLU

THR

LEU

GLU

4

GLU

MET

LEU

GLU

LYS

LEU

GLU

VAL

5

ASN

GLU

ARG

GLU

SER

ALA

6

ALA

GLU

VAL

GLU

ARG

THR

ARG

LYS

7

LEU

Samples:

sample_1: H-NS, [U-15N], 1.5 mM; NaCl 300 mM; potassium phosphate 20 mM; EDTA 1 mM

sample_2: H-NS, [U-13C; U-15N], 1.5 mM; NaCl 300 mM; potassium phosphate 20 mM; EDTA 1 mM

sample_3: H-NS, [U-13C; U-15N], 1.0 mM; H-NS 1.0 mM; NaCl 300 mM; potassium phosphate 20 mM; EDTA 1 mM

sample_cond_1: pH: 7.0; temperature: 298 K; ionic strength: 300 mM; pressure: 1 atm

Experiments:

Name	Sample	Sample state	Sample conditions
3D 15N-separated NOESY	not available	not available	not available
3D 13C-separated NOESY	not available	not available	not available
3D 13C F1-filtered F3-edited NOESY-HSQC	not available	not available	not available

Software:

AZARA v2.6 - processing

ANSIG v3.3 - data analysis

CNS v1.1 - structure solution, refinement

NMR spectrometers:

Bruker AVANCE 800 MHz

BMRB	18814 4802
PDB	1LR1 1NI8 3NR7
DBJ	BAA36117 BAB35162 BAG76811 BAI25048 BAI30173
EMBL	CAA30530 CAA32549 CAA40507 CAA42565 CAA47322
GB	AAB61148 AAC74319 AAG56094 AAL20669 AAN42850
PIR	AC0650
PRF	1607341A
REF	NP_287482 NP_309766 NP_415753 NP_455749 NP_460710
SP	P09120 P0A1S2 P0A1S3 P0ACF8 P0ACF9
AlphaFold	P09120 P0A1S2 P0A1S3 P0ACF8 P0ACF9