BMRB Entry 6369

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PDB ID: 1xn5
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6369
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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:

1H, 13C 15N chemical shift assignment Bacillus halodurans Protein BH1534: The Northeast Structural Genomics Consortium Target BhR29

Deposition date:

2004-10-27

Original release date:

2008-08-28

Authors:

Liu, Gaohua; Ma, Lichung; Shen, Yang; Acton, Thomas; Atreya, Hanudatta; Xiao, Rong; Montelione, Gaetano; Szyperski, Thomas

Citation:

Citation: Liu, Gaohua; Shen, Yang; Atreya, Hanudatta; Parish, David; Shao, Ying; Sukumaran, Dinesh; Xiao, Rong; Yee, Adelinda; Lemak, Alexander; Bhattacharya, Aneerban; Acton, Thomas; Arrowsmith, Cheryl; Montelione, Gaetano; Szyperski, Thomas. "NMR data collection and analysis protocol for high-throughput protein structure determination" Proc. Natl. Acad. Sci. U.S.A. 102, 10487-10492 (2005).
PubMed: 16027363

Assembly members:

Assembly members:
Protein BH1534, polymer, 138 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Bacillus halodurans Taxonomy ID: 86665 Superkingdom: Bacteria Kingdom: Not applicable Genus/species: Bacillus halodurans

Experimental source:

Experimental source: Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Protein BH1534: MTRLPDIKKEVRFNAPIEKV WEAVSTSEGLAFWFMENDLK AETGHHFHLQSPFGPSPCQV TDVERPIKLSFTWDTDGWSV TFHLKEEENGTIFTIVHSGW KQGDTKVEKAGAESAVVHER MDRGWHDLVNERLRQIVE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts

Data type	Count
1H chemical shifts	988
13C chemical shifts	501
15N chemical shifts	148

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Protein BH1534	1

Entities:

Entity 1, Protein BH1534 138 residues - Formula weight is not available

1

MET

THR

ARG

LEU

PRO

ASP

ILE

LYS

GLU

2

VAL

ARG

PHE

ASN

ALA

PRO

ILE

GLU

LYS

VAL

3

TRP

GLU

ALA

VAL

SER

THR

SER

GLU

GLY

LEU

4

ALA

PHE

TRP

PHE

MET

GLU

ASN

ASP

LEU

LYS

5

ALA

GLU

THR

GLY

HIS

PHE

HIS

LEU

GLN

6

SER

PRO

PHE

GLY

PRO

SER

PRO

CYS

GLN

VAL

7

THR

ASP

VAL

GLU

ARG

PRO

ILE

LYS

LEU

SER

8

PHE

THR

TRP

ASP

THR

ASP

GLY

TRP

SER

VAL

9

THR

PHE

HIS

LEU

LYS

GLU

ASN

GLY

10

THR

ILE

PHE

THR

ILE

VAL

HIS

SER

GLY

TRP

11

LYS

GLN

GLY

ASP

THR

LYS

VAL

GLU

LYS

ALA

12

GLY

ALA

GLU

SER

ALA

VAL

HIS

GLU

ARG

13

MET

ASP

ARG

GLY

TRP

HIS

ASP

LEU

VAL

ASN

14

GLU

ARG

LEU

ARG

GLN

ILE

VAL

GLU

Samples:

sample_1: Protein BH1534, [U-13C; U-15N], 0.8 mM; MES 20 mM; NaCl 100 mM; DTT 10 mM; CaCl2 5 mM; NaN3 0.02%; H2O 95%; D2O 5%

sample_conditions: temperature: 298 K; pH: 6.5; pressure: 1 atm

Experiments:

Name	Sample	Sample state	Sample conditions
GFT (4,3)D HNNCabCa	not available	not available	not available
GFT (4,3)D CabCacONHN	not available	not available	not available
GFT (4,3)D HabCabcoNHN	not available	not available	not available
GFT (4,3)HCCH and simutanously NOESY	not available	not available	not available

Software:

No software information available

NMR spectrometers:

Varian Inova 600 MHz
Varian Inova 750 MHz

PDB	1XN5
DBJ	BAB05253
REF	NP_242400 WP_010897699