BMRB Entry 15100

Name: NMR structure of E.coli YfgJ protein modelled with two Zn+2 bound. Northeast Structural Genomics Consortium Target ER317.
Published: 2007-10-03

Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15100

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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 structure of E.coli YfgJ protein modelled with two Zn+2 bound. Northeast Structural Genomics Consortium Target ER317.

Deposition date:

2007-01-12

Original release date:

2007-10-03

Authors:

Ramelot, Theresa; Cort, John; Yee, Adelinda; Semesi, Anthony; Johnathan, Lukin; Arrowsmith, Cheryl; Kennedy, Michael

Citation:

Citation: Ramelot, Theresa; Cort, John; Yee, Adelinda; Arrowsmith, Cheryl; Kennedy, Michael. "NMR structure of E.coli YfgJ protein modelled with two Zn+2 bound. Northeast Structural Genomics Consortium Target ER317." .

Assembly members:

Assembly members:
YfgJ protein, polymer, 101 residues, 8010.390 Da.
ZN, non-polymer, 65.409 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET

Entity Sequences (FASTA):

Entity Sequences (FASTA):
YfgJ protein: FCLTLRRRYTMGSSHHHHHH SSGLVPRGSHMELHCPQCQH VLDQDNGHARCRSCGEFIEM KALCPDCHQPLQVLKACGAV DYFCQHGHGLISKKRVEFVL A

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
13C chemical shifts	302
15N chemical shifts	71
1H chemical shifts	478

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	YfgJ protein	1
2	1st Zn+2	2
3	2nd Zn+2	2

Entities:

Entity 1, YfgJ protein 101 residues - 8010.390 Da.

30 NON-NATIVE N-TERMINAL RESIDUES (FCLTLRRRYTMGSSHHHHHHSSGLVPRGSH) WERE NOT INCLUDED IN THE STRUCTURE CALCULATION.

1

PHE

CYS

LEU

THR

LEU

ARG

TYR

THR

2

MET

GLY

SER

HIS

3

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

4

MET

GLU

LEU

HIS

CYS

PRO

GLN

CYS

GLN

HIS

5

VAL

LEU

ASP

GLN

ASP

ASN

GLY

HIS

ALA

ARG

6

CYS

ARG

SER

CYS

GLY

GLU

PHE

ILE

GLU

MET

7

LYS

ALA

LEU

CYS

PRO

ASP

CYS

HIS

GLN

PRO

8

LEU

GLN

VAL

LEU

LYS

ALA

CYS

GLY

ALA

VAL

9

ASP

TYR

PHE

CYS

GLN

HIS

GLY

HIS

GLY

LEU

10

ILE

SER

LYS

ARG

VAL

GLU

PHE

VAL

LEU

11

ALA

Entity 2, 1st Zn+2 - Zn - 65.409 Da.

1

ZN

Samples:

sample_1: protein, [U-100% 13C], 1 ± 0.2 mM; TRIS 10 ± 1 mM; sodium chloride 250 ± 5 mM; ZINC ION 10 ± 1 uM; DTT 10 ± 1 mM; sodium azide 0.01 ± 0.001 %

sample_conditions_1: ionic strength: 250 mM; pH: 7.3; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

AutoStruct v2.1.1, Huang, Swapana, Rajan, Ke, Xia, Shukla, Inouye and Montelione - data analysis

X-PLOR NIH v2.15.0, Schwieters, Kuszewski, Tjandra and Clore - structure solution

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

SPARKY v3.1, Goddard - peak picking

NMRPipe vlinux9, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Varian INOVA 600 MHz
Varian INOVA 750 MHz
Varian INOVA 800 MHz

SWS	P76575
PDB	2JNE
DBJ	BAE76728 BAI31784 BAJ44293 BAL39266
EMBL	CAQ32881 CBJ02173 CCP95953 CCQ02273 CDJ72855
GB	AAC75563 ABV17482 ACB03662 ACD09416 ACR64901
REF	NP_417005 WP_001295478 WP_001297332 WP_001301158 WP_001341056
SP	P76575
AlphaFold	P76575