BMRB Entry 26509

Name: Backbone resonance assignments and secondary structure determination for the human PHF6-ePHD1
Published: 2015-04-10

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26509

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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 resonance assignments and secondary structure determination for the human PHF6-ePHD1

Deposition date:

2015-02-14

Original release date:

2015-04-10

Authors:

Bao, Yun; Liu, Zhonghua; Zhang, Jiahai; Wu, Jihui; Shi, Yunyu

Citation:

Citation: Bao, Yun; Liu, Zhonghua; Zhang, Jiahai; Wu, Jihui; Shi, Yunyu. "1H, 13C and 15N resonance assignments and secondary structure of the human PHF6-ePHD1 domain" Biomol. NMR Assign. 10, 1-4 (2016).
PubMed: 26286319

Assembly members:

Assembly members:
PHF6-ePHD1, polymer, 127 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: pGEX-4T-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PHF6-ePHD1: TRQRKCGFCKSNRDKECGQL LISENQKVAAHHKCMLFSSA LVSSHSDNESLGGFSIEDVQ KEIKRGTKLMCSLCHCPGAT IGCDVKTCHRTYHYHCALHD KAQIREKPSQGIYMVYCRKH KKTAHNS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	464
15N chemical shifts	127
1H chemical shifts	726

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PHF6-ePHD1	1

Entities:

Entity 1, PHF6-ePHD1 127 residues - Formula weight is not available

1

THR

ARG

GLN

ARG

LYS

CYS

GLY

PHE

CYS

LYS

2

SER

ASN

ARG

ASP

LYS

GLU

CYS

GLY

GLN

LEU

3

LEU

ILE

SER

GLU

ASN

GLN

LYS

VAL

ALA

4

HIS

LYS

CYS

MET

LEU

PHE

SER

ALA

5

LEU

VAL

SER

HIS

SER

ASP

ASN

GLU

SER

6

LEU

GLY

PHE

SER

ILE

GLU

ASP

VAL

GLN

7

LYS

GLU

ILE

LYS

ARG

GLY

THR

LYS

LEU

MET

8

CYS

SER

LEU

CYS

HIS

CYS

PRO

GLY

ALA

THR

9

ILE

GLY

CYS

ASP

VAL

LYS

THR

CYS

HIS

ARG

10

THR

TYR

HIS

TYR

HIS

CYS

ALA

LEU

HIS

ASP

11

LYS

ALA

GLN

ILE

ARG

GLU

LYS

PRO

SER

GLN

12

GLY

ILE

TYR

MET

VAL

TYR

CYS

ARG

LYS

HIS

13

LYS

THR

ALA

HIS

ASN

SER

Samples:

sample_1: PHF6-ePHD1, [U-13C; U-15N], 0.6 mM; phosphate sodium 20 mM; NaCl 100 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 289 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 HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Zhengrong and Bax - processing

NMR spectrometers:

Bruker DMX 600 MHz

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