BMRB Entry 50085

Name: Collective exchange processes reveal an active site proton cage in bacteriorhodopsin
Published: 2020-01-06

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR50085

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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:

Collective exchange processes reveal an active site proton cage in bacteriorhodopsin

Deposition date:

2019-11-11

Original release date:

2020-01-06

Authors:

Friedrich, Daniel

Citation:

Citation: Friedrich, Daniel; Brunig, Florian; Nieuwkoop, Andrew; Netz, Roland; Hegemann, Peter; Oschkinat, Hartmut. "Collective exchange processes reveal an active site proton cage in bacteriorhodopsin" Commun. Biol. 3, 4-4 (2020).
PubMed: 31925324

Assembly members:

Assembly members:
entity_1, polymer, 248 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Halobacterium salinarum Taxonomy ID: 2242 Superkingdom: Archaea Kingdom: not available Genus/species: Halobacterium salinarum

Experimental source:

Experimental source: Production method: native organism Host organism: Halobacterium salinarum

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: QAQITGRPEWIWLALGTALM GLGTLYFLVKGMGVSDPDAK KFYAITTLVPAIAFTMYLSM LLGYGLTMVPFGGEQNPIYW ARYADWLFTTPLLLLDLALL VDADQGTILALVGADGIMIG TGLVGALTKVYSYRFVWWAI STAAMLYILYVLFFGFTSLA ESMRPEVASTFKVLRNVTVV LWSAYPVVWLIGSEGAGIVP LNIETLLFMVLDVSAKVGFG LILLRSRAIFGEAEAPEPSA GDGAAATS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	2
15N chemical shifts	42
1H chemical shifts	44

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	bacteriorhodopsin	1

Entities:

Entity 1, bacteriorhodopsin 248 residues - Formula weight is not available

1

GLN

ALA

GLN

ILE

THR

GLY

ARG

PRO

GLU

TRP

2

ILE

TRP

LEU

ALA

LEU

GLY

THR

ALA

LEU

MET

3

GLY

LEU

GLY

THR

LEU

TYR

PHE

LEU

VAL

LYS

4

GLY

MET

GLY

VAL

SER

ASP

PRO

ASP

ALA

LYS

5

LYS

PHE

TYR

ALA

ILE

THR

LEU

VAL

PRO

6

ALA

ILE

ALA

PHE

THR

MET

TYR

LEU

SER

MET

7

LEU

GLY

TYR

GLY

LEU

THR

MET

VAL

PRO

8

PHE

GLY

GLU

GLN

ASN

PRO

ILE

TYR

TRP

9

ALA

ARG

TYR

ALA

ASP

TRP

LEU

PHE

THR

10

PRO

LEU

ASP

LEU

ALA

LEU

11

VAL

ASP

ALA

ASP

GLN

GLY

THR

ILE

LEU

ALA

12

LEU

VAL

GLY

ALA

ASP

GLY

ILE

MET

ILE

GLY

13

THR

GLY

LEU

VAL

GLY

ALA

LEU

THR

LYS

VAL

14

TYR

SER

TYR

ARG

PHE

VAL

TRP

ALA

ILE

15

SER

THR

ALA

MET

LEU

TYR

ILE

LEU

TYR

16

VAL

LEU

PHE

GLY

PHE

THR

SER

LEU

ALA

17

GLU

SER

MET

ARG

PRO

GLU

VAL

ALA

SER

THR

18

PHE

LYS

VAL

LEU

ARG

ASN

VAL

THR

VAL

19

LEU

TRP

SER

ALA

TYR

PRO

VAL

TRP

LEU

20

ILE

GLY

SER

GLU

GLY

ALA

GLY

ILE

VAL

PRO

21

LEU

ASN

ILE

GLU

THR

LEU

PHE

MET

VAL

22

LEU

ASP

VAL

SER

ALA

LYS

VAL

GLY

PHE

GLY

23

LEU

ILE

LEU

ARG

SER

ARG

ALA

ILE

PHE

24

GLY

GLU

ALA

GLU

ALA

PRO

GLU

PRO

SER

ALA

25

GLY

ASP

GLY

ALA

THR

SER

Samples:

sample_1: bacteriorhodopsin, DCN, 10 mM

sample_conditions_1: pH: 7.5; temperature: 290 K

Experiments:

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

Software:

CcpNMR, CcpNMR - chemical shift assignment

NMR spectrometers:

Bruker Avance 900 MHz

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