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Found 1 Document (0.301 seconds)

BMRB: 17064

2M3G

13C, and 15N Chemical Shift Assignments for Anabaena sensory rhodopsin 1-229

Authors

Shi, L., Kawamura, I., Jung, K., Brown, L., Ladizhansky, V.

Assembly

ASR

Entity

1. opsin (polymer, Thiol state: all free), 235 monomers, 27219.59 Da Detail

MNLESLLHWI YVAGMTIGAL HFWSLSRNPR GVPQYEYLVA MFIPIWSGLA YMAMAIDQGK VEAAGQIAHY ARYIDWMVTT PLLLLSLSWT AMQFIKKDWT LIGFLMSTQI VVITSGLIAD LSERDWVRYL WYICGVCAFL IILWGIWNPL RAKTRTQSSE LANLYDKLVT YFTVLWIGYP IVWIIGPSGF GWINQTIDTF LFCLLPFFSK VGFSFLDLHG LRNLNDSRQH HHHHH

2. RET (non-polymer, Thiol state: not present), 284.436 Da

Total weight

27504.025 Da

Max. entity weight

27219.59 Da

Source organism

Nostoc sp. PCC 7120 = FACHB-418

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 77.4 %, Completeness: 61.8 %, Completeness (bb): 74.0 % Detail

Polymer type: polypeptide(L)

	Total	¹³C	¹⁵N
All	61.8 % (876 of 1417)	59.8 % (695 of 1162)	71.0 % (181 of 255)
Backbone	74.0 % (678 of 916)	72.7 % (501 of 689)	78.0 % (177 of 227)
Sidechain	48.3 % (348 of 720)	49.7 % (344 of 692)	14.3 % (4 of 28)
Aromatic	10.1 % (21 of 207)	9.3 % (18 of 194)	23.1 % (3 of 13)
Methyl	72.5 % (116 of 160)	72.5 % (116 of 160)

1. opsin

Show sample condition

Sample

Solvent system 100% H2O, Pressure 1 atm, Temperature 273 K, pH 9 (±0.1)

#	Name	Isotope labeling	Concentration
1	opsin	[U-99% 13C; U-99% 15N]	11 (±1.0) mg
2	retinal	natural abundance	110 (±10.0) ug
3	H2O	natural abundance	100 %
4	NaCl	natural abundance	10 mM
5	CHES	natural abundance	25 mM

Release date

2011-01-18

Citation

Conformation of a seven-helical transmembrane photosensor in the lipid environment
Shi, L., Kawamura, I., Jung, K., Brown, L.S., Ladizhansky, V.
Angew. Chem Int Ed Engl. (2011), 50, 1302-1305, PubMed 21290498 , DOI 10.1002/anie.201004422 , Abstract

Related entities 1. opsin, : 1 : 2 : 98 entities Detail

Experiments performed 3 experiments Detail

Chemical shift validation 4 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr17064_3.str
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	None
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

None

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

None

Content subtype: bmr17064_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	845		71.9 (chain: 1, length: 235)
1	Chemical shift references	chemical_shift_reference_1	OK	2		No information

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1

Status: Warning

Sequence coverage of experimental data

Entity_assembly_ID: 1, Chain length: 235, Sequence coverage: 71.9%

--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100
MNLESLLHWIYVAGMTIGALHFWSLSRNPRGVPQYEYLVAMFIPIWSGLAYMAMAIDQGKVEAAGQIAHYARYIDWMVTTPLLLLSLSWTAMQFIKKDWT
     |||||||||||||||                  ||||||||||||||||||||||||||||||||||||||||||||||||||||||        
.....LLHWIYVAGMTIGAL..................VAMFIPIWSGLAYMAMAIDQGKVEAAGQIAHYARYIDWMVTTPLLLLSLSWTAM........
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100

-------110-------120-------130-------140-------150-------160-------170-------180-------190-------200
LIGFLMSTQIVVITSGLIADLSERDWVRYLWYICGVCAFLIILWGIWNPLRAKTRTQSSELANLYDKLVTYFTVLWIGYPIVWIIGPSGFGWINQTIDTF
 ||| ||||||||||||||||||  ||| ||||||||||     ||||       |||||||||||| ||||||||||||||||||||||||||||||||
.IGF.MSTQIVVITSGLIADLSE..WVR.LWYICGVCAF.....GIWN.......TQSSELANLYDK.VTYFTVLWIGYPIVWIIGPSGFGWINQTIDTF
-------110-------120-------130-------140-------150-------160-------170-------180-------190-------200

-------210-------220-------230-----
LFCLLPFFSKVGFSFLDLHGLRNLNDSRQHHHHHH
||||||| |||||| |||||               
LFCLLPF.SKVGFS.LDLHG               
-------210-------220

Total number of assignments
- ¹³C chemical shifts: 668
- ¹⁵N chemical shifts: 177

Completeness of assignments

Entity_assemble_ID: 1

Excluded Atom_ID in statistics

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
8	HIS	CG	129.2
9	TRP	CG	111.9
44	PRO	N	132.2
46	TRP	CE2	139.7
46	TRP	CG	112.0
51	TYR	CZ	157.4
57	ASP	CG	182.0
60	LYS	NZ	33.4
62	GLU	CD	183.6
66	GLN	CD	179.3
69	HIS	CG	128.8
72	ARG	CZ	159.5
72	ARG	NH1	77.3
72	ARG	NH2	69.7
73	TYR	CG	128.6
73	TYR	CZ	158.1
75	ASP	CG	178.7
76	TRP	CE2	139.2
76	TRP	CG	113.7
81	PRO	N	137.6
89	TRP	CG	115.6
109	GLN	CD	175.0
120	ASP	CG	181.1
126	TRP	CG	111.6
131	TRP	CG	111.6
132	TYR	CG	129.1
132	TYR	CZ	158.3
147	TRP	CG	114.2
148	ASN	CG	176.7
163	ASN	CG	176.2
166	ASP	CG	180.1
180	PRO	N	132.2
183	TRP	CD2	129.1
183	TRP	CG	112.2
187	PRO	N	133.4
195	GLN	CD	180.7
198	ASP	CG	177.8
202	PHE	CG	140.4
206	PRO	N	139.3
210	LYS	NZ	177.2
217	ASP	CG	176.1

All atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	1162	636	54.7
¹⁵N chemical shifts	264	168	63.6

Backbone atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	470	334	71.1
¹⁵N chemical shifts	227	164	72.2

Side chain atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	692	302	43.6
¹⁵N chemical shifts	37	4	10.8

Methyl group atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	168	108	64.3

Aromatic group atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	194	7	3.6
¹⁵N chemical shifts	13	2	15.4

Redox state of CYS
Peptide bond of PRO
Tautomeric state of HIS
Rotameric state of ILE , LEU, and VAL
Histogram of normalized assigned chemical shifts
Random coil index and derived parameters (S² and NMR RMSD)
- Chain_ID: 1

Keywords membrane proteins, protein structure, receptor, rhodopsin, Solid state NMR

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Found 1 Document (0.301 seconds)

BMRB: 17064

Sample

Related entities 1. opsin, : 1 : 2 : 98 entities Detail

Experiments performed 3 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Chemical shift validation 4 contents Detail