BMRB Entry 11122

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PDB ID: 2dba
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11122
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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:

The solution structure of the tetratrico peptide repeat of human Smooth muscle cell associated protein-1, isoform 2

Deposition date:

2010-03-31

Original release date:

2011-04-01

Authors:

Tochio, N.; Sasagawa, A.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.

Citation:

Citation: Tochio, N.; Sasagawa, A.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "The solution structure of the tetratrico peptide repeat of human Smooth muscle cell associated protein-1, isoform 2" .

Assembly members:

Assembly members:
TPR, Residues 8-142, polymer, 148 residues, Formula weight is not available

Natural source:

Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: cell free synthesis Host organism: E. coli - cell free Vector: P050302-63

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TPR, Residues 8-142: GSSGSSGMTVSGPGTPEPRP ATPGASSVEQLRKEGNELFK CGDYGGALAAYTQALGLDAT PQDQAVLHRNRAACHLKLED YDKAETEASKAIEKDGGDVK ALYRRSQALEKLGRLDQAVL DLQRCVSLEPKNKVFQEALR NISGPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	585
15N chemical shifts	144
1H chemical shifts	920

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TPR, Residues 8-142	1

Entities:

Entity 1, TPR, Residues 8-142 148 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

MET

THR

VAL

2

SER

GLY

PRO

GLY

THR

PRO

GLU

PRO

ARG

PRO

3

ALA

THR

PRO

GLY

ALA

SER

VAL

GLU

GLN

4

LEU

ARG

LYS

GLU

GLY

ASN

GLU

LEU

PHE

LYS

5

CYS

GLY

ASP

TYR

GLY

ALA

LEU

ALA

6

TYR

THR

GLN

ALA

LEU

GLY

LEU

ASP

ALA

THR

7

PRO

GLN

ASP

GLN

ALA

VAL

LEU

HIS

ARG

ASN

8

ARG

ALA

CYS

HIS

LEU

LYS

LEU

GLU

ASP

9

TYR

ASP

LYS

ALA

GLU

THR

GLU

ALA

SER

LYS

10

ALA

ILE

GLU

LYS

ASP

GLY

ASP

VAL

LYS

11

ALA

LEU

TYR

ARG

SER

GLN

ALA

LEU

GLU

12

LYS

LEU

GLY

ARG

LEU

ASP

GLN

ALA

VAL

LEU

13

ASP

LEU

GLN

ARG

CYS

VAL

SER

LEU

GLU

PRO

14

LYS

ASN

LYS

VAL

PHE

GLN

GLU

ALA

LEU

ARG

15

ASN

ILE

SER

GLY

PRO

SER

GLY

Samples:

sample_1: TPRx3 domain, [U-13C; U-15N], 1.3 mM; d-Tris HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 15N-separated NOESY	sample_1	isotropic	condition_1
3D 13C-separated NOESY	sample_1	isotropic	condition_1

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20031121, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B.A. - data analysis

Kujira v0.932, Kobayashi, N. - data analysis

CYANA v2.0.17, Guntert, P. - structure solution

NMR spectrometers:

Bruker AVANCE 900 MHz

PDB	2DBA
DBJ	BAB20266 BAB20273 BAF84311 BAG54239 BAG57020
EMBL	CAH91170
GB	AAH06214 AAH37992 AAH45635 ABM83879 ABM87199
REF	NP_001034764 NP_001127383 NP_061141 XP_003268606 XP_003807756
SP	Q5RAP0 Q9H3U1
AlphaFold	Q5RAP0 Q9H3U1