BMRB Entry 17276

Name: Unbound TbRI-ED
Published: 2011-10-28

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17276

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Unbound TbRI-ED

Deposition date:

2010-11-02

Original release date:

2011-10-28

Authors:

Zuniga, Jorge; Ilangovan, Udayar; Pardeep, Mahlawat; Hinck, Cynthia; Huang, Tao

Citation:

Citation: Zuniga, Jorge; Ilangovan, Udayar; Mahlawat, Pardeep; Hinck, Cynthia; Huang, Tao; Groppe, Jay; McEwen, Donald; Hinck, Andrew. "The TR-I pre-helix extension is structurally ordered in the unbound form and its flanking prolines are essential for binding." J. Mol. Biol. 412, 601-618 (2011).
PubMed: 21821041

Assembly members:

Assembly members:
TbRI, polymer, 87 residues, 9465.8 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TbRI: GSATALQCFCHLCTKDNFTC VTDGLCFVSVTETTDKVIHN SMCIAEIDLIPRDRPFVCAP SSKTGSVTTTYCCNQDHCNK IELPTTV

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	247
15N chemical shifts	85
1H chemical shifts	529

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unbound Alk5 ectodomain	1

Entities:

Entity 1, unbound Alk5 ectodomain 87 residues - 9465.8 Da.

1

GLY

SER

ALA

THR

ALA

LEU

GLN

CYS

PHE

CYS

2

HIS

LEU

CYS

THR

LYS

ASP

ASN

PHE

THR

CYS

3

VAL

THR

ASP

GLY

LEU

CYS

PHE

VAL

SER

VAL

4

THR

GLU

THR

ASP

LYS

VAL

ILE

HIS

ASN

5

SER

MET

CYS

ILE

ALA

GLU

ILE

ASP

LEU

ILE

6

PRO

ARG

ASP

ARG

PRO

PHE

VAL

CYS

ALA

PRO

7

SER

LYS

THR

GLY

SER

VAL

THR

8

TYR

CYS

ASN

GLN

ASP

HIS

CYS

ASN

LYS

9

ILE

GLU

LEU

PRO

THR

VAL

Samples:

sample_1: TbRI, [U-100% 13C; U-100% 15N], 1 mM; H2O 95%; D2O 5%; Sodium phosphate 25 mM

sample_conditions_1: ionic strength: 0.025 M; pH: 7.2; pressure: 1 atm; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMR spectrometers:

Bruker Avance 600 MHz

PDB	2L5S 2PJY 3KFD
DBJ	BAD91020 BAD91021 BAD91022 BAD91023 BAG10679
EMBL	CAF02096 CAF02097
GB	AAA16073 AAA80265 AAC08998 AAD02042 AAH71181
REF	NP_001033728 NP_001124388 NP_001293139 NP_004603 XP_001112590
SP	P36897 Q5CD18
AlphaFold	P36897 Q5CD18