BMRB Entry 18185

Name: Backbone 1H and 15N Chemical Shift Assignments of the VHS-UIM domains of STAM2
Published: 2012-04-05

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18185

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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:

Backbone 1H and 15N Chemical Shift Assignments of the VHS-UIM domains of STAM2

Deposition date:

2012-01-06

Original release date:

2012-04-05

Authors:

Walker, Olivier; Lange, Anja; Castaneda, Carlos; Hoeller, Daniela; Lancelin, Jean-Marc; Fushman, David

Citation:

Citation: Lange, Anja; Castaneda, Carlos; Hoeller, Daniela; Lancelin, Jean-Marc; Fushman, David; Walker, Olivier. "Evidence for cooperative and domain-specific binding of the signal transducing adaptor molecule 2 (STAM2) to Lys63-linked diubiquitin." J. Biol. Chem. 287, 18687-18699 (2012).
PubMed: 22493438

Assembly members:

Assembly members:
VHS-UIM_domains_of_STAM2, polymer, 192 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: pETEM-60

Entity Sequences (FASTA):

Entity Sequences (FASTA):
VHS-UIM_domains_of_STAM2: GAMGMPLFTANPFEQDVEKA TNEYNTTEDWSLIMDICDKV GSTPNGAKDCLKAIMKRVNH KVPHVALQALTLLGACVANC GKIFRLGVCSRDFATEVRAV IKNKAHPKVCEKLKSLMVEW SEEFQKDPQFSLISATIKSM KEEGITFPPAGSQTVSAAAK NGTSSNKNKEDEDIAKAIEL SLQEQKQQHTET

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	165
1H chemical shifts	165

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	VHS-UIM	1

Entities:

Entity 1, VHS-UIM 192 residues - Formula weight is not available

1

GLY

ALA

MET

GLY

MET

PRO

LEU

PHE

THR

ALA

2

ASN

PRO

PHE

GLU

GLN

ASP

VAL

GLU

LYS

ALA

3

THR

ASN

GLU

TYR

ASN

THR

GLU

ASP

TRP

4

SER

LEU

ILE

MET

ASP

ILE

CYS

ASP

LYS

VAL

5

GLY

SER

THR

PRO

ASN

GLY

ALA

LYS

ASP

CYS

6

LEU

LYS

ALA

ILE

MET

LYS

ARG

VAL

ASN

HIS

7

LYS

VAL

PRO

HIS

VAL

ALA

LEU

GLN

ALA

LEU

8

THR

LEU

GLY

ALA

CYS

VAL

ALA

ASN

CYS

9

GLY

LYS

ILE

PHE

ARG

LEU

GLY

VAL

CYS

SER

10

ARG

ASP

PHE

ALA

THR

GLU

VAL

ARG

ALA

VAL

11

ILE

LYS

ASN

LYS

ALA

HIS

PRO

LYS

VAL

CYS

12

GLU

LYS

LEU

LYS

SER

LEU

MET

VAL

GLU

TRP

13

SER

GLU

PHE

GLN

LYS

ASP

PRO

GLN

PHE

14

SER

LEU

ILE

SER

ALA

THR

ILE

LYS

SER

MET

15

LYS

GLU

GLY

ILE

THR

PHE

PRO

ALA

16

GLY

SER

GLN

THR

VAL

SER

ALA

LYS

17

ASN

GLY

THR

SER

ASN

LYS

ASN

LYS

GLU

18

ASP

GLU

ASP

ILE

ALA

LYS

ALA

ILE

GLU

LEU

19

SER

LEU

GLN

GLU

GLN

LYS

GLN

HIS

THR

20

GLU

THR

Samples:

sample_1: VHS-UIM domains of STAM2, [U-13C; U-15N], 200-400 uM; sodium phosphate 20 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 20 mM; pH: 6.8; pressure: 1 atm; temperature: 288 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

VNMRJ, Varian - collection

CARA, Keller and Wuthrich - chemical shift assignment

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

NMR spectrometers:

Varian INOVA 600 MHz

BMRB	10264
PDB	1X5B 2L0T
DBJ	BAF84954 BAF85536 BAG72771 BAK62690
EMBL	CAB63735 CAL38297
GB	AAC63963 AAC63964 AAH28740 AAI12605 AAY14712
REF	NP_001069574 NP_001267210 NP_005834 XP_002749486 XP_002926244
SP	O75886
TPG	DAA32691
AlphaFold	O75886