BMRB Entry 6030

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PDB ID: 2a29
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6030
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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:

1H, 13C and 15N resonance assignment of the nucleotide binding domain of KdpB from Escherichia coli

Deposition date:

2003-12-03

Original release date:

2004-07-06

Authors:

Haupt, Melina; Coles, Murray; Truffault, Vincent; Bramkamp, Marc; Altendorf, Karlheinz; Kessler, Horst

Citation:

Citation: Haupt, Melina; Coles, Murray; Truffault, Vincent; Bramkamp, Marc; Altendorf, Karlheinz; Kessler, Horst. "Letter to the Editor: 1H, 13C and 15N resonance assignment of the nucleotide binding domain of KdpB from Escherichia coli" J. Biomol. NMR 29, 437-438 (2004).
PubMed: 15213457

Assembly members:

Assembly members:
potassium transporting ATPase, polymer, 156 residues, 17000 Da.
ANP, non-polymer, 506.196 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
potassium transporting ATPase: MGHHHHHHHHHHSSGHGGRH NRQASEFIPAQGVDEKTLAD AAQLASLADETPEGRSIVIL AKQRFNLRERDVQSLHATFV PFTAQSRMSGINIDNRMIRK GSVDAIRRHVEANGGHFPTD VDQKVDQVARQGATPLVVVE GSRVLGVIALKDIVKG

Data sets:

assigned_chemical_shifts
- KdpBN-ANP_shift

Data type	Count
1H chemical shifts	898
13C chemical shifts	413
15N chemical shifts	144

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	KdpBN	1
2	ANP	2

Entities:

Entity 1, KdpBN 156 residues - 17000 Da.

1

MET

GLY

HIS

2

HIS

SER

GLY

HIS

GLY

ARG

HIS

3

ASN

ARG

GLN

ALA

SER

GLU

PHE

ILE

PRO

ALA

4

GLN

GLY

VAL

ASP

GLU

LYS

THR

LEU

ALA

ASP

5

ALA

GLN

LEU

ALA

SER

LEU

ALA

ASP

GLU

6

THR

PRO

GLU

GLY

ARG

SER

ILE

VAL

ILE

LEU

7

ALA

LYS

GLN

ARG

PHE

ASN

LEU

ARG

GLU

ARG

8

ASP

VAL

GLN

SER

LEU

HIS

ALA

THR

PHE

VAL

9

PRO

PHE

THR

ALA

GLN

SER

ARG

MET

SER

GLY

10

ILE

ASN

ILE

ASP

ASN

ARG

MET

ILE

ARG

LYS

11

GLY

SER

VAL

ASP

ALA

ILE

ARG

HIS

VAL

12

GLU

ALA

ASN

GLY

HIS

PHE

PRO

THR

ASP

13

VAL

ASP

GLN

LYS

VAL

ASP

GLN

VAL

ALA

ARG

14

GLN

GLY

ALA

THR

PRO

LEU

VAL

GLU

15

GLY

SER

ARG

VAL

LEU

GLY

VAL

ILE

ALA

LEU

16

LYS

ASP

ILE

VAL

LYS

GLY

Entity 2, ANP - C10 H17 N6 O12 P3 - 506.196 Da.

1

ANP

Samples:

KdpBN-ANP: Type IA potassium translocating ATPase B chain, [U-13C; U-15N], 1.0 mM; PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER0.5 – 15.0 mM

KdpBN-ANP_cond: pH: 6.0 na; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
CBCA(CO)NH	KdpBN-ANP	not available	KdpBN-ANP_cond
(H)CCH-COSY	KdpBN-ANP	not available	KdpBN-ANP_cond

Software:

No software information available

NMR spectrometers:

Bruker DMX 600 MHz
Bruker DMX 750 MHz
Bruker DMX 900 MHz

BMRB	6029
PDB	1SVJ 1U7Q 2A00 2A29
DBJ	BAA35354 BAB34148 BAG76281 BAI24086 BAI29554
EMBL	CAP75183 CAQ31162 CAQ89912 CAQ97541 CAR02071
GB	AAB96336 AAC73791 AAG55018 AAN79255 AAZ87406
REF	NP_286410 NP_308752 NP_415225 NP_752712 WP_000087925
SP	A1A8W1 A7ZJ80 A7ZXV8 B1IY32 B1LLE1
AlphaFold	A1A8W1 A7ZJ80 A7ZXV8 B1IY32 B1LLE1