BMRB Entry 16338

Click here to enlarge.

PDB ID: 2kjr
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16338
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:

Solution NMR structure of the N-terminal Ubiquitin-like Domain from Tubulin-binding Cofactor B, CG11242, from Drosophila melanogaster. Northeast Structural Genomics Consortium Target FR629A (residues 8-92).

Deposition date:

2009-06-08

Original release date:

2009-07-08

Authors:

Ramelot, Theresa; Cort, John; Shastry, Ritu; Ciccosanti, Colleen; Jiang, Mei; Nair, R; Rost, Burkhard; Swapna, G.V.T.; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael

Citation:

Citation: Ramelot, Theresa; Cort, John; Shastry, Ritu; Ciccosanti, Colleen; Jiang, Mei; Nair, R; Rost, Burkhard; Swapna, G.V.T.; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of the N-terminal Ubiquitin-like Domain from Tubulin-binding Cofactor B, CG11242, from Drosophila melanogaster. Northeast Structural Genomics Consortium Target FR629A (residues 8-92)." .

Assembly members:

Assembly members:
CG11242, polymer, 95 residues, 10300 Da.

Natural source:

Natural source: Common Name: fruit fly Taxonomy ID: 7227 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Drosophila melanogaster

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET14-15C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CG11242: MGHHHHHHSHGKSDFIKVNV SNSHNDAVAFEVKLAKDLTV AQLKTKLEILTGGCAGTMKV QVFKGDTCVSTMDNNDAQLG YYANSDGLRLHVVDS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	373
15N chemical shifts	96
1H chemical shifts	588

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CG11242	1

Entities:

Entity 1, CG11242 95 residues - 10300 Da.

8 non-native residues at N-teriminus (MGHHHHHH)

1

MET

GLY

HIS

SER

HIS

2

GLY

LYS

SER

ASP

PHE

ILE

LYS

VAL

ASN

VAL

3

SER

ASN

SER

HIS

ASN

ASP

ALA

VAL

ALA

PHE

4

GLU

VAL

LYS

LEU

ALA

LYS

ASP

LEU

THR

VAL

5

ALA

GLN

LEU

LYS

THR

LYS

LEU

GLU

ILE

LEU

6

THR

GLY

CYS

ALA

GLY

THR

MET

LYS

VAL

7

GLN

VAL

PHE

LYS

GLY

ASP

THR

CYS

VAL

SER

8

THR

MET

ASP

ASN

ASP

ALA

GLN

LEU

GLY

9

TYR

ALA

ASN

SER

ASP

GLY

LEU

ARG

LEU

10

HIS

VAL

ASP

SER

Samples:

NC_sample: MES 50 ± 2.5 mM; arginine 50 ± 2.5 mM; DTT 10 ± .5 mM; sodium azide 0.02 ± .001 %; entity, [U-100% 13C; U-100% 15N], 1.1 ± .05 mM; DSS 50 ± 2.5 uM; H2O 95%; D2O 5%

NC5_sample: MES 50 ± 2.5 mM; arginine 50 ± 2.5 mM; DTT 10 ± .5 mM; sodium azide 0.02 ± .001 %; entity, [U-5% 13C; U-100% 15N], 1.0 ± .05 mM; DSS 50 ± 2.5 uM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 50 mM; pH: 6.0; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	NC_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	NC_sample	isotropic	sample_conditions_1
3D 1H-15N NOESY	NC_sample	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	NC_sample	isotropic	sample_conditions_1
3D HNCO	NC_sample	isotropic	sample_conditions_1
3D HNCA	NC_sample	isotropic	sample_conditions_1
3D CBCA(CO)NH	NC_sample	isotropic	sample_conditions_1
3D HNCACB	NC_sample	isotropic	sample_conditions_1
3D C(CO)NH	NC_sample	isotropic	sample_conditions_1
3D HBHA(CO)NH	NC_sample	isotropic	sample_conditions_1
3D HCCH-TOCSY	NC_sample	isotropic	sample_conditions_1
3D CCH-TOCSY	NC_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC	NC5_sample	isotropic	sample_conditions_1
2D 1H-15N HSQC	NC5_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	NC_sample	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	NC_sample	isotropic	sample_conditions_1

Software:

NMRPipe v2008, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMR v6.1C, Varian - collection

TOPSPIN v2.1.3, Bruker Biospin - collection

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - data analysis

X-PLOR NIH v2.20, Schwieters, Kuszewski, Tjandra and Clore - structure solution

SPARKY v3.113, Goddard - data analysis

PSVS v1.3, Bhattacharya and Montelione - structure validation

AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

PDBStat v5.1, (PDBStat) R. Tejero, G.T. Montelione - data analysis

NMR spectrometers:

Varian INOVA 500 MHz
Bruker AvanceIII 850 MHz

PDB	2KJR
GB	AAF57546 AAL29037 ACL84771 ACL89668 EDW48612
REF	NP_611425 XP_002034599 XP_002076374