BMRB Entry 18446

Name: Sequence specific 1H, 13C and 15N resonance assignments of an intrinsically unstructured -Crystallin from Hahella chejuensis
Published: 2012-09-14

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18446

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

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Title:

Sequence specific 1H, 13C and 15N resonance assignments of an intrinsically unstructured -Crystallin from Hahella chejuensis

Deposition date:

2012-05-07

Original release date:

2012-09-14

Authors:

Ramanujam, Venkatraman; Patel, Sunita; Srivastava, Atul; Sharma, Yogendra; Chary, Kandala

Citation:

Citation: Ramanujam, Venkatraman; Patel, Sunita; Srivastava, Atul; Sharma, Yogendra; Chary, Kandala. "Backbone 1H, 13C and 15N resonance assignments of an intrinsically unstructured -crystallin from Hahella chejuensis." Biomol. NMR Assignments 7, 221-224 (2013).
PubMed: 22836948

Assembly members:

Assembly members:
Apoform_Hahellin, polymer, 92 residues, 10249.3 Da.

Natural source:

Natural source: Common Name: Hahella chejuensis Taxonomy ID: 158327 Superkingdom: Bacteria Kingdom: not available Genus/species: Hahella chejuensis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Hahella chejuensis Vector: pET21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Apoform_Hahellin: MGEKTVKLYEDTHFKGYSVE LPVGDYNLSSLISRGALNDD LSSARVPSGLRLEVFQHNNF KGVRDFYTSDAAELSRDNDA SSVRVSKMETTN

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	222
15N chemical shifts	71
1H chemical shifts	71

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Apoform of Hahellin	1

Entities:

Entity 1, Apoform of Hahellin 92 residues - 10249.3 Da.

1

MET

GLY

GLU

LYS

THR

VAL

LYS

LEU

TYR

GLU

2

ASP

THR

HIS

PHE

LYS

GLY

TYR

SER

VAL

GLU

3

LEU

PRO

VAL

GLY

ASP

TYR

ASN

LEU

SER

4

LEU

ILE

SER

ARG

GLY

ALA

LEU

ASN

ASP

5

LEU

SER

ALA

ARG

VAL

PRO

SER

GLY

LEU

6

ARG

LEU

GLU

VAL

PHE

GLN

HIS

ASN

PHE

7

LYS

GLY

VAL

ARG

ASP

PHE

TYR

THR

SER

ASP

8

ALA

GLU

LEU

SER

ARG

ASP

ASN

ASP

ALA

9

SER

VAL

ARG

VAL

SER

LYS

MET

GLU

THR

10

THR

ASN

Samples:

sample_1: Apoform Hahellin, [U-100% 13C; U-100% 15N], 0.7 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.05 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - processing

NMR spectrometers:

Bruker Avance 800 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks