BMRB Entry 11593

Name: Effects of linker length and transient secondary structure elements in the intrinsically disordered RAM region of NICD on Notch signaling
Published: 2016-07-01

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11593

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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:

Effects of linker length and transient secondary structure elements in the intrinsically disordered RAM region of NICD on Notch signaling

Deposition date:

2015-05-21

Original release date:

2016-07-01

Authors:

Sherry, Kathryn; Johnson, Scott; Hatem, Christine; Majumdar, Ananya; Barrick, Doug

Citation:

Citation: Sherry, Kathryn; Johnson, Scott; Hatem, Christine; Majumdar, Ananya; Barrick, Doug. "Effects of Linker Length and Transient Secondary Structure Elements in the Intrinsically Disordered Notch RAM Region on Notch Signaling" J. Mol. Biol. 427, 3587-3597 (2015).
PubMed: 26344835

Assembly members:

Assembly members:
RAM, polymer, 133 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: recombinant technology Host organism: Escherichia coli Vector: pET24b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RAM: MMARKRRRQHGQLWFPEGFK VSEASKKKRREPLGEDSVGL KPLKNASDGALMDDNQNEWG DEDLETKKFRFEEPVVLPDL DDQTDHRQWTQQHLDAADLR MSAMAPTPPQGEVDADCMDV NVRGPDGFTPLLE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	282
15N chemical shifts	97
1H chemical shifts	97

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RAM	1

Entities:

Entity 1, RAM 133 residues - Formula weight is not available

1

MET

ALA

ARG

LYS

ARG

GLN

HIS

2

GLY

GLN

LEU

TRP

PHE

PRO

GLU

GLY

PHE

LYS

3

VAL

SER

GLU

ALA

SER

LYS

ARG

4

GLU

PRO

LEU

GLY

GLU

ASP

SER

VAL

GLY

LEU

5

LYS

PRO

LEU

LYS

ASN

ALA

SER

ASP

GLY

ALA

6

LEU

MET

ASP

ASN

GLN

ASN

GLU

TRP

GLY

7

ASP

GLU

ASP

LEU

GLU

THR

LYS

PHE

ARG

8

PHE

GLU

PRO

VAL

LEU

PRO

ASP

LEU

9

ASP

GLN

THR

ASP

HIS

ARG

GLN

TRP

THR

10

GLN

HIS

LEU

ASP

ALA

ASP

LEU

ARG

11

MET

SER

ALA

MET

ALA

PRO

THR

PRO

GLN

12

GLY

GLU

VAL

ASP

ALA

ASP

CYS

MET

ASP

VAL

13

ASN

VAL

ARG

GLY

PRO

ASP

GLY

PHE

THR

PRO

14

LEU

GLU

Samples:

sample_1: RAM, [U-100% 13C; U-100% 15N], 2 mM; sodium phosphate 25 mM; sodium chloride 50 mM; EDTA 1 mM; TCEP 0.1 mM; H2O 95%; D2O, [U-2H], 5%

sample_conditions_1: ionic strength: 75 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HN(CA)N	sample_1	isotropic	sample_conditions_1
3D HN(COCA)N	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

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

NMR spectrometers:

Varian INOVA 800 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks