BMRB Entry 15274

Name: NMR chemical shift assignments for Arf-binding domain of Hdm2
Published: 2008-10-28

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15274

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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:

NMR chemical shift assignments for Arf-binding domain of Hdm2

Deposition date:

2007-05-31

Original release date:

2008-10-28

Authors:

Sivakolundu, Sivashankar; Kriwacki, Richard

Citation:

Citation: Sivakolundu, Sivashankar; Nourse, Amanda; Moshiach, Simon; Bothner, Brian; Ashley, Chimere; Satumba, John; Lahti, Jill; Kriwacki, Richard. "Intrinsically Unstructured Domains of Arf and Hdm2 Form Bimolecular Oligomeric Structures In Vitro and In Vivo" J. Mol. Biol. 384, 240-254 (2008).
PubMed: 18809412

Assembly members:

Assembly members:
Hdm2-ABD, polymer, 99 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: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Hdm2-ABD: GSHMSSSSESTGTPSNPDLD AGVSEHSGDWLDQDSVSDQF SVEFEVESLDSEDYSLSEEG QELSDEDDEVYQVTVYQAGE SDTDSFEEDPEISLADYWK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	276
15N chemical shifts	91
1H chemical shifts	91

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Hdm2-ABD	1

Entities:

Entity 1, Hdm2-ABD 99 residues - Formula weight is not available

1

GLY

SER

HIS

MET

SER

GLU

SER

2

THR

GLY

THR

PRO

SER

ASN

PRO

ASP

LEU

ASP

3

ALA

GLY

VAL

SER

GLU

HIS

SER

GLY

ASP

TRP

4

LEU

ASP

GLN

ASP

SER

VAL

SER

ASP

GLN

PHE

5

SER

VAL

GLU

PHE

GLU

VAL

GLU

SER

LEU

ASP

6

SER

GLU

ASP

TYR

SER

LEU

SER

GLU

GLY

7

GLN

GLU

LEU

SER

ASP

GLU

ASP

GLU

VAL

8

TYR

GLN

VAL

THR

VAL

TYR

GLN

ALA

GLY

GLU

9

SER

ASP

THR

ASP

SER

PHE

GLU

ASP

PRO

10

GLU

ILE

SER

LEU

ALA

ASP

TYR

TRP

LYS

Samples:

sample_1: Hdm2-ABD, [U-98% 13C; U-98% 15N], 1 mM; sodium phosphate 10 mM; NaCl 10 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.02 M; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCACO	sample_1	isotropic	sample_conditions_1

Software:

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

FELIX, Accelrys Software Inc. - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 600 MHz
Varian INOVA 600 MHz

DBJ	BAB11975 BAC78209 BAF83030 BAJ17752
EMBL	CAA78055 CAH89564 CAP16704 CAP16705 CAP16729
GB	AAA60568 AAA75514 AAA75516 AAF28866 AAF42995
PRF	1814460A
REF	NP_001009346 NP_001092577 NP_001124685 NP_001138811 NP_001138812
SP	P56950 P56951 Q00987 Q7YRZ8
TPG	DAA29805
AlphaFold	Q00987 P56951 P56950 Q7YRZ8