BMRB Entry 15264

Name: Complete backbone 15N, 13C, and 1H resonance assignments for the N-terminal domain of AhpF
Published: 2007-10-29

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15264

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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:

Complete backbone 15N, 13C, and 1H resonance assignments for the N-terminal domain of AhpF

Deposition date:

2007-05-23

Original release date:

2007-10-29

Authors:

Benison, Gregory; Barbar, Elisar; Horita, David

Citation:

Citation: Benison, Gregory; Berkholz, Donald; Barbar, Elisar. "Protein assignments without peak lists using higher-order spectra" J. Magn. Reson. 189, 173-181 (2007).
PubMed: 17919953

Assembly members:

Assembly members:
ahpfn, polymer, 202 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Salmonella typhimurium Taxonomy ID: 602 Superkingdom: Bacteria Kingdom: not available Genus/species: Salmonella typhimurium

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pOXO4

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ahpfn: MLDTNMKTQLRAYLEKLTKP VELIATLDDSAKSAEIKELL AEIAELSDKVTFKEDNTLPV RKPSFLITNPGSQQGPRFAG SPLGHEFTSLVLALLWTGGH PSKEAQSLLEQIRDIDGDFE FETYYSLSCHNCPDVVQALN LMAVLNPRIKHTAIDGGTFQ NEITERNVMGVPAVFVNGKE FGQGRMTLTEIVAKVDTGAE KR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	390
15N chemical shifts	191
1H chemical shifts	191

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ahpfn	1

Entities:

Entity 1, ahpfn 202 residues - Formula weight is not available

1

MET

LEU

ASP

THR

ASN

MET

LYS

THR

GLN

LEU

2

ARG

ALA

TYR

LEU

GLU

LYS

LEU

THR

LYS

PRO

3

VAL

GLU

LEU

ILE

ALA

THR

LEU

ASP

SER

4

ALA

LYS

SER

ALA

GLU

ILE

LYS

GLU

LEU

5

ALA

GLU

ILE

ALA

GLU

LEU

SER

ASP

LYS

VAL

6

THR

PHE

LYS

GLU

ASP

ASN

THR

LEU

PRO

VAL

7

ARG

LYS

PRO

SER

PHE

LEU

ILE

THR

ASN

PRO

8

GLY

SER

GLN

GLY

PRO

ARG

PHE

ALA

GLY

9

SER

PRO

LEU

GLY

HIS

GLU

PHE

THR

SER

LEU

10

VAL

LEU

ALA

LEU

TRP

THR

GLY

HIS

11

PRO

SER

LYS

GLU

ALA

GLN

SER

LEU

GLU

12

GLN

ILE

ARG

ASP

ILE

ASP

GLY

ASP

PHE

GLU

13

PHE

GLU

THR

TYR

SER

LEU

SER

CYS

HIS

14

ASN

CYS

PRO

ASP

VAL

GLN

ALA

LEU

ASN

15

LEU

MET

ALA

VAL

LEU

ASN

PRO

ARG

ILE

LYS

16

HIS

THR

ALA

ILE

ASP

GLY

THR

PHE

GLN

17

ASN

GLU

ILE

THR

GLU

ARG

ASN

VAL

MET

GLY

18

VAL

PRO

ALA

VAL

PHE

VAL

ASN

GLY

LYS

GLU

19

PHE

GLY

GLN

GLY

ARG

MET

THR

LEU

THR

GLU

20

ILE

VAL

ALA

LYS

VAL

ASP

THR

GLY

ALA

GLU

21

LYS

ARG

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

BMRB	16265
PDB	1HYU 1ZYN 1ZYP
DBJ	BAA02486 BAH62352 BAJ35614 BAP06377 GAL49470
EMBL	CAD05085 CAR32166 CAR36509 CAR60178 CBG23683
GB	AAA16432 AAL19560 AAO69861 AAV78017 AAX64546
PIR	AC0577
REF	NP_455185 NP_459601 WP_000886405 WP_000887631 WP_000887632
SP	P19480
AlphaFold	P19480

BMRB Entry 15264

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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