BMRB Entry 15269

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PDB ID: 2jq4
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15269
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Complete resonance assignments and solution structure calcualtion of ATC2521 (NESG ID: AtT6) from Agrobacterium tumeraciens

Deposition date:

2007-05-29

Original release date:

2007-07-05

Authors:

Srisailam, Sampath; Lemak, Alexander; Yee, Adelinda; Karra, Murthy; Lukin, Jonathan; Arrowsmith, Cheryl

Citation:

Citation: Srisailam, Sampath; Lemak, Alexander; Yee, Adelinda; Karra, Murthy; Lukin, Jonathan; Arrowsmith, Cheryl. "Solution Structure of a protein (ATC2521)of unknow function from Agrobacterium tumefaciens" .

Assembly members:

Assembly members:
ATC2521, polymer, 188 residues, 11548.9 Da.

Natural source:

Natural source: Common Name: Agrobacterium tumefaciens Taxonomy ID: 358 Superkingdom: Bacteria Kingdom: not available Genus/species: Agrobacterium tumefaciens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: BL21-CodonPlus(DE3)-RP

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ATC2521: MGSSHHHHHHSSGRENLYFQ GHMNATIREILAKFGQLPTP VDTIADEADLYAAGLSSFAS VQLMLGIEEAFDIEFPDNLL NRKSFASIKAIEDTVKLILD GKEAAMNATIREILAKFGQL PTPVDTIADEADLYAAGLSS FASVQLMLGIEEAFDIEFPD NLLNRKSFASIKAIEDTVKL ILDGKEAA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	335
15N chemical shifts	77
1H chemical shifts	560

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ATC2521	1

Entities:

Entity 1, ATC2521 188 residues - 11548.9 Da.

1

MET

GLY

SER

HIS

2

SER

GLY

ARG

GLU

ASN

LEU

TYR

PHE

GLN

3

GLY

HIS

MET

ASN

ALA

THR

ILE

ARG

GLU

ILE

4

LEU

ALA

LYS

PHE

GLY

GLN

LEU

PRO

THR

PRO

5

VAL

ASP

THR

ILE

ALA

ASP

GLU

ALA

ASP

LEU

6

TYR

ALA

GLY

LEU

SER

PHE

ALA

SER

7

VAL

GLN

LEU

MET

LEU

GLY

ILE

GLU

ALA

8

PHE

ASP

ILE

GLU

PHE

PRO

ASP

ASN

LEU

9

ASN

ARG

LYS

SER

PHE

ALA

SER

ILE

LYS

ALA

10

ILE

GLU

ASP

THR

VAL

LYS

LEU

ILE

LEU

ASP

11

GLY

LYS

GLU

ALA

MET

ASN

ALA

THR

ILE

12

ARG

GLU

ILE

LEU

ALA

LYS

PHE

GLY

GLN

LEU

13

PRO

THR

PRO

VAL

ASP

THR

ILE

ALA

ASP

GLU

14

ALA

ASP

LEU

TYR

ALA

GLY

LEU

SER

15

PHE

ALA

SER

VAL

GLN

LEU

MET

LEU

GLY

ILE

16

GLU

ALA

PHE

ASP

ILE

GLU

PHE

PRO

ASP

17

ASN

LEU

ASN

ARG

LYS

SER

PHE

ALA

SER

18

ILE

LYS

ALA

ILE

GLU

ASP

THR

VAL

LYS

LEU

19

ILE

LEU

ASP

GLY

LYS

GLU

ALA

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 HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	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
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1

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

BMRB Entry 15269

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: