BMRB Entry 15049

Name: Resonance assignment of the first and second KH (hnRNP-K homology) domains of human poly(C)-binding protein-2 (PCBP2)
Published: 2007-05-09

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15049

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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:

Resonance assignment of the first and second KH (hnRNP-K homology) domains of human poly(C)-binding protein-2 (PCBP2)

Deposition date:

2006-11-21

Original release date:

2007-05-09

Authors:

Du, Zhihua; Fenn, Sebastian; James, Thomas

Citation:

Citation: Du, Zhihua; Fenn, Sebastian; James, Thomas. "Resonance assignment of the first and second KH (hnRNP-K homology) domains of human poly(C)-binding protein-2 (PCBP2)" J. Biomol. NMR 38, 197-197 (2007).
PubMed: 17479348

Assembly members:

Assembly members:
PCBP2_KH1_and_KH2_domains, polymer, 168 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: pet24A

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PCBP2_KH1_and_KH2_domains: MKHHHHHHKNVTLTIRLLMH GKEVGSIIGKKGESVKKMRE ESGARINISEGNCPERIITL AGPTNAIFKAFAMIIGKLEE DISSSMTNSTAASRPPVTLR LVVPASQCGSLIGKGGCKIK EIRESTGAQVQVAGDMLPNS TERAITIAGIPQSIIECVKQ ICVVMLET

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	626
15N chemical shifts	172
1H chemical shifts	1126

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Kh1+Kh2	1

Entities:

Entity 1, Kh1+Kh2 168 residues - Formula weight is not available

residues M2-K10 is a non-native tag

1

MET

LYS

HIS

LYS

ASN

2

VAL

THR

LEU

THR

ILE

ARG

LEU

MET

HIS

3

GLY

LYS

GLU

VAL

GLY

SER

ILE

GLY

LYS

4

LYS

GLY

GLU

SER

VAL

LYS

MET

ARG

GLU

5

GLU

SER

GLY

ALA

ARG

ILE

ASN

ILE

SER

GLU

6

GLY

ASN

CYS

PRO

GLU

ARG

ILE

THR

LEU

7

ALA

GLY

PRO

THR

ASN

ALA

ILE

PHE

LYS

ALA

8

PHE

ALA

MET

ILE

GLY

LYS

LEU

GLU

9

ASP

ILE

SER

MET

THR

ASN

SER

THR

10

ALA

SER

ARG

PRO

VAL

THR

LEU

ARG

11

LEU

VAL

PRO

ALA

SER

GLN

CYS

GLY

SER

12

LEU

ILE

GLY

LYS

GLY

CYS

LYS

ILE

LYS

13

GLU

ILE

ARG

GLU

SER

THR

GLY

ALA

GLN

VAL

14

GLN

VAL

ALA

GLY

ASP

MET

LEU

PRO

ASN

SER

15

THR

GLU

ARG

ALA

ILE

THR

ILE

ALA

GLY

ILE

16

PRO

GLN

SER

ILE

GLU

CYS

VAL

LYS

GLN

17

ILE

CYS

VAL

MET

LEU

GLU

THR

Samples:

sample_1: PCBP2 KH1 and KH2 domains, [U-100% 13C; U-100% 15N], 1 mM; H2O 10%; D2O 90%

sample_conditions_1: ionic strength: 50 mM; pH: 5.4; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Varian INOVA 600 MHz

PDB	2JZX
DBJ	BAE41029 BAG59482
GB	KFP19120 KFQ73073
REF	XP_002721142 XP_004951015 XP_004951016 XP_004951017 XP_004951018