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PDB ID: 2g9j
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR7080
MolProbity Validation Chart

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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

Please specify the pdb ID.

Title:

Complex of TM1a(1-14)Zip with TM9a(251-284): a model for the polymerization domain ("overlap region")of tropomyosin

Deposition date:

2006-04-20

Original release date:

2006-10-31

Authors:

Greenfield, Norma; Huang, Yuanpeng; Swapna, G.V.T.; Bhattacharya, Aneerban; Rapp, Brian; Singh, Abhishek; Montelione, Gaetano; Hitchcock-DeGregori, Sarah

Citation:

Citation: Greenfield, Norma; Huang, Yuanpeng; Swapna, G.V.T.; Bhattacharya, Aneerban; Rapp, Brian; Singh, Abhishek; Montelione, Gaetano; Hitchcock-DeGregori, Sarah. "Solution NMR Structure of the Junction between Tropomyosin Molecules: Implications for Actin Binding and Regulation" J. Mol. Biol. 364, 80-96 (2006).
PubMed: 16999976

Assembly members:

Assembly members:
Tropomyosin N-terminal domain, polymer, 33 residues, 3900.7 Da.
Tropomyosin C-terminal domain, polymer, 37 residues, 4170.6 Da.

Natural source:

Natural source: Common Name: Rat Taxonomy ID: 10117 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus Rattus

Experimental source:

Experimental source: Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Tropomyosin N-terminal domain: GMDAIKKKMQMLKLDNYHLE NEVARLKKLVGER
Tropomyosin C-terminal domain: GCGKSIDDLEDELYAQKLKY KAISEELDHALKDMTSI

Data sets:

assigned_chemical_shifts
- chem_shift_list_1

Data type	Count
13C chemical shifts	304
15N chemical shifts	72
1H chemical shifts	524

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	molecule 1, Chain A	1
2	$GlyTm1a(1-14)Zip	.
3	.	yes
4	native	no

Entities:

Entity 1, molecule 1, Chain A 33 residues - 3900.7 Da.

1

GLY

MET

ASP

ALA

ILE

LYS

MET

GLN

2

MET

LEU

LYS

LEU

ASP

ASN

TYR

HIS

LEU

GLU

3

ASN

GLU

VAL

ALA

ARG

LEU

LYS

LEU

VAL

4

GLY

GLU

ARG

Entity ., $GlyTm1a(1-14)Zip

Entity yes, .

Entity no, native

Samples:

Sample_1: Tropomyosin C-terminal domain, [U-95% 15N], 1.0 ± 0.1 mM; Tropomyosin N-terminal domain, [U-95% 15N], 1.0 ± 0.1 mM; NaCl 100 ± 10 mM; Sodium Phosphate 10 ± 1 mM; Deuterium Oxide, [U-2H], 7.5 ± 2.5 %

Sample_2: Tropomyosin C-terminal domain, [U-95% 15N U-95% 13C], 1.0 ± 0.1 mM; Tropomyosin N-terminal domain, unlabeled, 1.0 ± 0.1 mM; NaCl 100 ± 10 mM; Sodium Phosphate 10 ± 1 mM; Deuterium Oxide, [U-2H], 7.5 ± 2.5 %

sample_3: Tropomyosin C-terminal domain, unlabeled, 1.0 ± 0.1 mM; Tropomyosin N-terminal domain, [U-95% 15N; U-95% 13C], 1.0 ± 0.1 mM; NaCl 100 ± 10 mM; Sodium Phosphate 10 ± 1 mM; Deuterium Oxide, [U-2H], 7.5 ± 2.5 %

Sample_4: Tropomyosin C-terminal domain, [U-95% 15N], 1.0 ± 0.1 mM; Tropomyosin N-terminal domain, [U-95% 15N], 1.0 ± 0.1 mM; NaCl 100 ± 10 mM; Sodium Phosphate 10 ± 1 mM; Deuterium Oxide, [U-2H], 99 ± 1 %

Sample_5: Tropomyosin C-terminal domain, unlabeled, 1.0 ± 0.1 mM; Tropomyosin N-terminal domain, [U-95% 15N; U-95% 13C], 1.0 ± 0.1 mM; NaCl 100 ± 10 mM; Sodium Phosphate 10 ± 1 mM; Deuterium Oxide, [U-2H], 7.5 ± 2.5 %

Sample_6: Tropomyosin C-terminal domain, [U-95% 15N; U-95% 13C], 0.5 ± 0.05 mM; Tropomyosin C-terminal domain, unlabeled, 0.5 ± 0.05 mM; Tropomyosin N-terminal domain, unlabeled, 1.0 ± 0.1 mM; NaCl 100 ± 10 mM; Sodium Phosphate 10 ± 1 mM; Deuterium Oxide, [U-2H], 7.5 ± 2.5 %

Sample_7: Tropomyosin C-terminal domain, unlabeled, 1.0 ± 0.1 mM; Tropomyosin N-terminal domain, [U-95% 15N; U-95% 13C], 0.5 ± 0.05 mM; Tropomyosin N-terminal domain, unlabeled, 0.5 ± 0.05 mM; NaCl 100 ± 10 mM; Sodium Phosphate 10 ± 1 mM; Deuterium Oxide, [U-2H], 7.5 ± 2.5 %

conditions_1: ionic strength: 0.14 M; pH*: 6.5; pressure: 1 atm; temperature: 283 K

conditions_2: ionic strength: 0.14 M; pH*: 6.5; pressure: 1 atm; temperature: 283 K

Experiments:

Name	Sample	Sample state	Sample conditions
1H15N_HSQC	not available	not available	not available
1H13C_HSQC	not available	not available	not available
HNCA	not available	not available	not available
HNcoCA	not available	not available	not available
HCCH_COSY	not available	not available	not available
CCH-COSY	not available	not available	not available
HNCO	not available	not available	not available
HAcaNH	not available	not available	not available
HAcacoNH	not available	not available	not available
CBCAcoNH	not available	not available	not available
CBCANH	not available	not available	not available
15N Edited NOESY	not available	not available	not available
13C Edited NOESY	not available	not available	not available
13C X-filtered NOESY	not available	not available	not available
T1 Relaxation	not available	not available	not available
T2 Relaxation	not available	not available	not available
15N1H HNOE	not available	not available	not available
15N Edited TOCSY	not available	not available	not available
HNcoHA	not available	not available	not available

Software:

AutoStruct vCustom, not commercial -

DYANA v1.5, not commercial - Structure Analysis

CYANA v2.1, L. A. Systems - Strucutre determination

VNMR v6.1c, Varian - Data Collection

NMR spectrometers:

Varian ANOVA 600 MHz
Varan Anova 500 MHz
Bruker AVANCE 600 MHz

BMRB	5610
PDB	1C1G 1MV4 2D3E 2G9J 2TMA 2W49 2W4U
DBJ	BAB21978 BAC36973 BAC85248 BAD86590 BAE40499
EMBL	CAA26259 CAA28393 CAA34344 CAA41056 CAA43577
GB	AAA18096 AAA21801 AAA21803 AAA48577 AAA48610
PRF	1105305B
REF	NP_001013608 NP_001018005 NP_001029247 NP_001090952 NP_001099158
SP	P04268 P04692 P09493 P13105 P42639
AlphaFold	P04268 P04692 P09493 P13105 P42639

BMRB Entry 7080