BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	62.2 % (797 of 1281)	51.3 % (337 of 657)	69.8 % (361 of 517)	92.5 % (99 of 107)
Backbone	87.9 % (566 of 644)	87.7 % (200 of 228)	86.5 % (268 of 310)	92.5 % (98 of 106)
Sidechain	43.1 % (315 of 731)	31.9 % (137 of 429)	58.8 % (177 of 301)	100.0 % (1 of 1)
Aromatic	8.3 % (10 of 120)	16.7 % (10 of 60)	0.0 % (0 of 60)
Methyl	57.6 % (91 of 158)	41.8 % (33 of 79)	73.4 % (58 of 79)

1. entity

MTSLYKKVGM DLIGFGYAAL VTFGSIFGYK RRGGVPSLIA GLFVGCLAGY GAYRVSNDKR DVKVSLFTAF FLATIMGVRF KRSKKIMPAG LVAGLSLMMI LRLVLLLL

Show sample condition

Sample #1

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6.0, Details U-15N-labeled protein

#	Name	Isotope labeling	Concentration
1	TMEM14A	[U-15N]	0.2 mM
2	MES-Bis-TRIS	natural abundance	20 mM
3	LMPG	natural abundance	2 %
4	DSS	natural abundance	0.5 mM
5	H2O	natural abundance	95 %
6	D2O	natural abundance	5 %

Sample #2

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6.0, Details U-15N-2H-labeled protein

#	Name	Isotope labeling	Concentration
7	TMEM14A	[U-15N; U-2H]	0.2 mM
8	MES-Bis-TRIS	natural abundance	20 mM
9	LMPG	natural abundance	2 %
10	DSS	natural abundance	0.5 mM
11	H2O	natural abundance	95 %
12	D2O	natural abundance	5 %

Sample #3

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6.0, Details U-15N-13C-labeled protein

#	Name	Isotope labeling	Concentration
13	TMEM14A	[U-15N; U-13C]	0.2 mM
14	MES-Bis-TRIS	natural abundance	20 mM
15	LMPG	natural abundance	2 %
16	DSS	natural abundance	0.5 mM
17	H2O	natural abundance	95 %
18	D2O	natural abundance	5 %

Sample #4

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6.0, Details U-15N-labeled single-cysteine mutants with paramagnetic spin-label (MTSL)

#	Name	Isotope labeling	Concentration
19	TMEM14A	[U-15N]	0.2 mM
20	MES-Bis-TRIS	natural abundance	20 mM
21	LMPG	natural abundance	2 %
22	DSS	natural abundance	0.5 mM
23	H2O	natural abundance	95 %
24	D2O	natural abundance	5 %

Sample #5

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6.0, Details U-15N-labeled single-cysteine mutants with diamagnetic analog of MTSL

#	Name	Isotope labeling	Concentration
25	TMEM14A	[U-15N]	0.2 mM
26	MES-Bis-TRIS	natural abundance	20 mM
27	LMPG	natural abundance	2 %
28	DSS	natural abundance	0.5 mM
29	H2O	natural abundance	95 %
30	D2O	natural abundance	5 %

Sample #6

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6.0, Details U-15N-labeled cysteine-free mutant protein

#	Name	Isotope labeling	Concentration
31	TMEM14A	[U-15N]	0.2 mM
32	MES-Bis-TRIS	natural abundance	20 mM
33	LMPG	natural abundance	2 %
34	DSS	natural abundance	0.5 mM
35	H2O	natural abundance	95 %
36	D2O	natural abundance	5 %

Sample #7

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6.0, Details U-15N-13C-2H-labeled protein

#	Name	Isotope labeling	Concentration
37	TMEM14A	[U-15N; U-13C; U-2H]	0.2 mM
38	MES-Bis-TRIS	natural abundance	20 mM
39	LMPG	natural abundance	2 %
40	DSS	natural abundance	0.5 mM
41	H2O	natural abundance	95 %
42	D2O	natural abundance	5 %

LACS Plot; CA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	water	protons	4.703 ppm	internal	indirect	0.2514495
¹H	water	protons	4.703 ppm	internal	direct	1.0
¹⁵N	water	protons	4.703 ppm	internal	indirect	0.1013291

Referencing offset: 0.36 ppm, Outliers: 2 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	water	protons	4.703 ppm	internal	indirect	0.2514495
¹H	water	protons	4.703 ppm	internal	direct	1.0
¹⁵N	water	protons	4.703 ppm	internal	indirect	0.1013291

Referencing offset: 0.36 ppm, Outliers: 2 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	water	protons	4.703 ppm	internal	indirect	0.2514495
¹H	water	protons	4.703 ppm	internal	direct	1.0
¹⁵N	water	protons	4.703 ppm	internal	indirect	0.1013291

Referencing offset: 0.06 ppm, Outliers: 1 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	water	protons	4.703 ppm	internal	indirect	0.2514495
¹H	water	protons	4.703 ppm	internal	direct	1.0
¹⁵N	water	protons	4.703 ppm	internal	indirect	0.1013291

Referencing offset: 2.69 ppm, Outliers: 2 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2LOP, Strand ID: A Detail

Release date

2012-05-21

Citation

Facile backbone structure determination of human membrane proteins by NMR spectroscopy
Klammt, C., Maslennikov, I., Bayrhuber, M., Eichmann, C., Vajpai, N., Chiu, E., Blain, K.Y., Esquivies, L., Kwon, J., Balana, B., Pieper, U., Sali, A., Slesinger, P.A., Kwiatkowski, W., Riek, R., Choe, S.
Nat. Methods (2012), 9, 834-839, PubMed 22609626 , DOI 10.1038/nmeth.2033 , Abstract

Related entities 1. TMEM14A, : 1 : 1 : 2 : 29 entities Detail

Interaction partners 1. TMEM14A, : 7 interactors Detail

More details for 7 interactors identified by 5 citations

Experiments performed 7 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker DRX - 700 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6.0, Details U-15N-labeled cysteine-free mutant protein

#	Name	Isotope labeling	Concentration
31	TMEM14A	[U-15N]	0.2 mM
32	MES-Bis-TRIS	natural abundance	20 mM
33	LMPG	natural abundance	2 %
34	DSS	natural abundance	0.5 mM
35	H2O	natural abundance	95 %
36	D2O	natural abundance	5 %

2 2D 1H-15N HSQC

Instrument

Bruker DRX - 700 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6.0, Details U-15N-labeled single-cysteine mutants with paramagnetic spin-label (MTSL)

#	Name	Isotope labeling	Concentration
19	TMEM14A	[U-15N]	0.2 mM
20	MES-Bis-TRIS	natural abundance	20 mM
21	LMPG	natural abundance	2 %
22	DSS	natural abundance	0.5 mM
23	H2O	natural abundance	95 %
24	D2O	natural abundance	5 %

3 2D 1H-15N HSQC

Instrument

Bruker DRX - 700 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6.0, Details U-15N-labeled single-cysteine mutants with diamagnetic analog of MTSL

#	Name	Isotope labeling	Concentration
25	TMEM14A	[U-15N]	0.2 mM
26	MES-Bis-TRIS	natural abundance	20 mM
27	LMPG	natural abundance	2 %
28	DSS	natural abundance	0.5 mM
29	H2O	natural abundance	95 %
30	D2O	natural abundance	5 %

4 3D HNCO

Instrument

Bruker DRX - 700 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6.0, Details U-15N-13C-2H-labeled protein

#	Name	Isotope labeling	Concentration
37	TMEM14A	[U-15N; U-13C; U-2H]	0.2 mM
38	MES-Bis-TRIS	natural abundance	20 mM
39	LMPG	natural abundance	2 %
40	DSS	natural abundance	0.5 mM
41	H2O	natural abundance	95 %
42	D2O	natural abundance	5 %

5 3D HNCACB

Instrument

Bruker DRX - 700 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6.0, Details U-15N-13C-2H-labeled protein

#	Name	Isotope labeling	Concentration
37	TMEM14A	[U-15N; U-13C; U-2H]	0.2 mM
38	MES-Bis-TRIS	natural abundance	20 mM
39	LMPG	natural abundance	2 %
40	DSS	natural abundance	0.5 mM
41	H2O	natural abundance	95 %
42	D2O	natural abundance	5 %

6 3D 13C-15N HSQC-NOESY-HSQC

Instrument

Bruker DRX - 700 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6.0, Details U-15N-13C-labeled protein

#	Name	Isotope labeling	Concentration
13	TMEM14A	[U-15N; U-13C]	0.2 mM
14	MES-Bis-TRIS	natural abundance	20 mM
15	LMPG	natural abundance	2 %
16	DSS	natural abundance	0.5 mM
17	H2O	natural abundance	95 %
18	D2O	natural abundance	5 %

7 3D 1H-15N NOESY

Instrument

Bruker DRX - 700 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6.0, Details U-15N-2H-labeled protein

#	Name	Isotope labeling	Concentration
7	TMEM14A	[U-15N; U-2H]	0.2 mM
8	MES-Bis-TRIS	natural abundance	20 mM
9	LMPG	natural abundance	2 %
10	DSS	natural abundance	0.5 mM
11	H2O	natural abundance	95 %
12	D2O	natural abundance	5 %

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints	combined_18220_2lop.nef
Input source #2: Coordindates	2lop.cif
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

Sequence alignments

Entity_assembly_ID (NMR): A vs Auth_asym_ID (model): A

-----------------10--------20--------30--------40--------50--------60--------70--------80--------90-
MTSLYKKVGMDLIGFGYAALVTFGSIFGYKRRGGVPSLIAGLFVGCLAGYGAYRVSNDKRDVKVSLFTAFFLATIMGVRFKRSKKIMPAGLVAGLSLMMI
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MTSLYKKVGMDLIGFGYAALVTFGSIFGYKRRGGVPSLIAGLFVGCLAGYGAYRVSNDKRDVKVSLFTAFFLATIMGVRFKRSKKIMPAGLVAGLSLMMI
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100

--------
LRLVLLLL
||||||||
LRLVLLLL
--------

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	108	0	0	100.0

Content subtype: combined_18220_2lop.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	759		90.7 (chain: A, length: 108)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	OK	336 (1)	undefined	80.6 (chain: A, length: 108)
2	Distance restraints	DYANA/DIANA_distance_constraints_3	OK	489 (1)	undefined	87.0 (chain: A, length: 108)
3	Distance restraints	DYANA/DIANA_distance_constraints_4	Warning	176 (1)	hbond	55.6 (chain: A, length: 108)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 108, Sequence coverage: 90.7%
- Total number of assignments
  - ¹H chemical shifts: 312
  - ¹³C chemical shifts: 350
  - ¹⁵N chemical shifts: 97
- Completeness of assignments
  - Entity_assemble_ID: A
- Redox state of CYS
- Peptide bond of PRO
- 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: A

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	657	312	47.5
¹³C chemical shifts	517	350	67.7
¹⁵N chemical shifts	114	97	85.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	228	197	86.4
¹³C chemical shifts	216	179	82.9
¹⁵N chemical shifts	106	96	90.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	429	115	26.8
¹³C chemical shifts	301	171	56.8
¹⁵N chemical shifts	8	1	12.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	85	30	35.3
¹³C chemical shifts	85	57	67.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	60	8	13.3
¹³C chemical shifts	60	0	0.0

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: OK
- Experiment type: undefined
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 108, Sequence coverage: 80.6%
- Total number of restraints: 336
- Weight of restraints: 1.0 (336)
- Potential type of restraints: upper-bound-parabolic (336)
- Range of distance target values: 10.5, 29.9 (Å)
- Histogram of distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map
- Saveframe: DYANA/DIANA_distance_constraints_3
  - Status: OK
  - Experiment type: undefined
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 108, Sequence coverage: 87.0%
  - Total number of restraints: 489
  - Weight of restraints: 1.0 (489)
  - Potential type of restraints: lower-bound-parabolic (489)
  - Range of distance target values: 5.9, 28.1 (Å)
  - Histogram of distance target values
  - Distance restraints per residue
    - Chain_ID: A
  - Distance restraints on contact map
  - Saveframe: DYANA/DIANA_distance_constraints_4
    - Status: Warning
    - Experiment type: hbond
    - Sequence coverage of experimental data
      - Entity_assembly_ID: A, Chain length: 108, Sequence coverage: 55.6%
    - Total number of restraints: 176
    - Weight of restraints: 1.0 (176)
    - Potential type of restraints: upper-bound-parabolic (176)
    - Range of distance target values: 1.8, 3.0 (Å)
    - Histogram of distance target values
    - Histogram of discrepancy in distance target values
    - Distance restraints per residue
      - Chain_ID: A
    - Distance restraints on contact map

Keywords Backbone structure, Helical bundle, Homo sapiens, Membrane protein, Paramagnetic relaxation enhancement

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BMRB: 18220

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Sample #2

Sample #3

Sample #4

Sample #5

Sample #6

Sample #7

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. TMEM14A, : 1 : 1 : 2 : 29 entities Detail

Interaction partners 1. TMEM14A, : 7 interactors Detail

Experiments performed 7 experiments Detail

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NMR combined restraints 5 contents Detail