BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	49.5 % (618 of 1248)	46.6 % (299 of 641)	43.7 % (215 of 492)	90.4 % (104 of 115)
Backbone	76.7 % (491 of 640)	79.3 % (176 of 222)	67.5 % (212 of 314)	99.0 % (103 of 104)
Sidechain	30.9 % (218 of 706)	29.4 % (123 of 419)	34.1 % (94 of 276)	9.1 % (1 of 11)
Aromatic	0.0 % (0 of 126)	0.0 % (0 of 63)	0.0 % (0 of 61)	0.0 % (0 of 2)
Methyl	20.6 % (26 of 126)	27.0 % (17 of 63)	14.3 % (9 of 63)

1. entity

MVNLGLSRVD DAVAAKHPGL GEYAACQSHA FMKGVFTFVT GTGMAFGLQM FIQRKFPYPL QWSLLVAVVA GSVVSYGVTR VESEKCNNLW LFLETGQLPK DRSTDQRS

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	TMEM141	[U-15N]	0.2 mM
2	MES-Bis-TRIS	natural abundance	20 mM
3	LMPG	natural abundance	3 %
4	H2O	natural abundance	95 %
5	D2O	natural abundance	5 %

Sample #2

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
6	TMEM141	[U-15N; U-13C]	0.2 mM
7	MES-Bis-TRIS	natural abundance	20 mM
8	LMPG	natural abundance	3 %
9	H2O	natural abundance	95 %
10	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-2H-labeled protein

#	Name	Isotope labeling	Concentration
11	TMEM141	[U-15N; U-13C; U-2H]	0.2 mM
12	MES-Bis-TRIS	natural abundance	20 mM
13	LMPG	natural abundance	3 %
14	H2O	natural abundance	95 %
15	D2O	natural abundance	5 %

Sample #4

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

#	Name	Isotope labeling	Concentration
16	TMEM141	[U-15N]	0.2 mM
17	MES-Bis-TRIS	natural abundance	20 mM
18	LMPG	natural abundance	3 %
19	H2O	natural abundance	95 %
20	D2O	natural abundance	5 %

Sample #5

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

#	Name	Isotope labeling	Concentration
21	TMEM141	[U-15N]	0.2 mM
22	MES-Bis-TRIS	natural abundance	20 mM
23	LMPG	natural abundance	3 %
24	H2O	natural abundance	95 %
25	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: 0.55 ppm, Outliers: 1 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: 0.55 ppm, Outliers: 1 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: 0.26 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2LOR, 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

Entries sharing articles BMRB: 6, Swiss-Prot: 6 entries Detail

  BMRB: 18217 released on 2012-05-21
    Title Backbone structure of human membrane protein HIGD1A
  BMRB: 18218 released on 2012-05-21
    Title Backbone structure of human membrane protein HIGD1B
  BMRB: 18219 released on 2012-05-21
    Title Backbone structure of human membrane protein TMEM14A from NOE data
  BMRB: 18220 released on 2012-05-21
    Title Backbone structure of human membrane protein TMEM14A
  BMRB: 18221 released on 2012-05-21
    Title Backbone structure of human membrane protein FAM14B (Interferon alpha-inducible protein 27-like protein 1)
  BMRB: 18223 released on 2012-05-21
    Title Backbone structure of human membrane protein TMEM14C
  Swiss-Prot: Q96I45 released on 2007-03-06
    Title TM141_HUMAN Entity Transmembrane protein 141
  Swiss-Prot: Q9P298 released on 2005-09-27
    Title HIG1B_HUMAN Entity HIG1 domain family member 1B
  Swiss-Prot: Q9Y241 released on 2005-09-27
    Title HIG1A_HUMAN Entity HIG1 domain family member 1A, mitochondrial
  Swiss-Prot: Q96BM0 released on 2003-01-17
    Title I27L1_HUMAN Entity Interferon alpha-inducible protein 27-like protein 1
  Swiss-Prot: Q9P0S9 released on 2003-01-10
    Title TM14C_HUMAN Entity Transmembrane protein 14C
  Swiss-Prot: Q9Y6G1 released on 2000-12-01
    Title TM14A_HUMAN Entity Transmembrane protein 14A

Related entities 1. TMEM141, : 1 : 2 : 7 entities Detail

Experiments performed 9 experiments Detail

NMR combined restraints 8 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints	combined_18222_2lor.nef
Input source #2: Coordindates	2lor.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-------100
MVNLGLSRVDDAVAAKHPGLGEYAACQSHAFMKGVFTFVTGTGMAFGLQMFIQRKFPYPLQWSLLVAVVAGSVVSYGVTRVESEKCNNLWLFLETGQLPK
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MVNLGLSRVDDAVAAKHPGLGEYAACQSHAFMKGVFTFVTGTGMAFGLQMFIQRKFPYPLQWSLLVAVVAGSVVSYGVTRVESEKCNNLWLFLETGQLPK

--------
DRSTDQRS
||||||||
DRSTDQRS

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_18222_2lor.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	581		100.0 (chain: A, length: 108)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	OK	151 (1)	noe	84.3 (chain: A, length: 108)
2	Distance restraints	DYANA/DIANA_distance_constraints_3	OK	151 (1)	noe	84.3 (chain: A, length: 108)
3	Distance restraints	DYANA/DIANA_distance_constraints_7	OK	162 (1)	undefined	77.8 (chain: A, length: 108)
4	Distance restraints	DYANA/DIANA_distance_constraints_6	OK	279 (1)	undefined	88.0 (chain: A, length: 108)
5	Distance restraints	DYANA/DIANA_distance_constraints_4	OK	120 (1)	hbond	70.4 (chain: A, length: 108)
6	Distance restraints	DYANA/DIANA_distance_constraints_5	OK	120 (1)	hbond	70.4 (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: 100.0%
- Total number of assignments
  - ¹³C chemical shifts: 197
  - ¹H chemical shifts: 281
  - ¹⁵N chemical shifts: 103
- Completeness of assignments
  - Entity_assemble_ID: A
- Redox state of CYS
- Peptide bond of PRO
- 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 (%)
¹³C chemical shifts	492	197	40.0
¹H chemical shifts	641	281	43.8
¹⁵N chemical shifts	120	103	85.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	216	108	50.0
¹H chemical shifts	222	173	77.9
¹⁵N chemical shifts	104	103	99.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	276	89	32.2
¹H chemical shifts	419	108	25.8
¹⁵N chemical shifts	16	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	67	7	10.4
¹H chemical shifts	67	15	22.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	61	0	0.0
¹H chemical shifts	63	0	0.0
¹⁵N chemical shifts	2	0	0.0

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 108, Sequence coverage: 84.3%
- Total number of restraints: 151
- Weight of restraints: 1.0 (151)
- Potential type of restraints: lower-bound-parabolic (151)
- Range of distance target values: 2.0, 3.5 (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: noe
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 108, Sequence coverage: 84.3%
  - Total number of restraints: 151
  - Weight of restraints: 1.0 (151)
  - Potential type of restraints: upper-bound-parabolic (151)
  - Range of distance target values: 4.0, 5.5 (Å)
  - Histogram of distance target values
  - Distance restraints per residue
    - Chain_ID: A
  - Distance restraints on contact map
  - Saveframe: DYANA/DIANA_distance_constraints_7
    - Status: OK
    - Experiment type: undefined
    - Sequence coverage of experimental data
      - Entity_assembly_ID: A, Chain length: 108, Sequence coverage: 77.8%
    - Total number of restraints: 162
    - Weight of restraints: 1.0 (162)
    - Potential type of restraints: upper-bound-parabolic (162)
    - Range of distance target values: 11.7, 27.2 (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
    - Saveframe: DYANA/DIANA_distance_constraints_6
      - Status: OK
      - Experiment type: undefined
      - Sequence coverage of experimental data
        Entity_assembly_ID: A, Chain length: 108, Sequence coverage: 88.0%
        --------10--------20--------30--------40--------50--------60--------70--------80--------90-------100 MVNLGLSRVDDAVAAKHPGLGEYAACQSHAFMKGVFTFVTGTGMAFGLQMFIQRKFPYPLQWSLLVAVVAGSVVSYGVTRVESEKCNNLWLFLETGQLPK ||||||||||| ||| |||||||||| ||||||||||||||| ||||||||||| | |||||||||||||||||| ||||| || | ||||||||| | .VNLGLSRVDDA..AKH.GLGEYAACQS.AFMKGVFTFVTGTGM.FGLQMFIQRKF.Y.LQWSLLVAVVAGSVVSYG.TRVES.KC.N.WLFLETGQL.K -------- DRSTDQRS |||||||| DRSTDQRS
      - Total number of restraints: 279
        Long range restraints, | i - j | >= 5 : 279
      - Weight of restraints: 1.0 (279)
        Long range restraints, | i - j | >= 5 : 1.0 (279)
      - Potential type of restraints: lower-bound-parabolic (279)
        Long range restraints, | i - j | >= 5 : lower-bound-parabolic (279)
      - Range of distance target values: 4.2, 24.8 (Å)
      - Histogram of distance target values
      - Distance restraints per residue
        Chain_ID: A
      - Distance restraints on contact map
        Chain_ID_1: A - Chain_ID_2: A
      - Saveframe: DYANA/DIANA_distance_constraints_4
        Status: OK
        Experiment type: hbond
        Sequence coverage of experimental data
        Entity_assembly_ID: A, Chain length: 108, Sequence coverage: 70.4%
        --------10--------20--------30--------40--------50--------60--------70--------80--------90-------100 MVNLGLSRVDDAVAAKHPGLGEYAACQSHAFMKGVFTFVTGTGMAFGLQMFIQRKFPYPLQWSLLVAVVAGSVVSYGVTRVESEKCNNLWLFLETGQLPK |||||||||| ||||||||||||||||||||| |||||||||||| ||||||||||||||||||||||||||||||||| .....LSRVDDAVAA....LGEYAACQSHAFMKGVFTFVT..GMAFGLQMFIQR.......WSLLVAVVAGSVVSYGVTRVESEKCNNLWLFLE --------10--------20--------30--------40--------50--------60--------70--------80--------90---- -------- DRSTDQRS
        Total number of restraints: 120
        Total hydrogen bond restraints: 120
        O...H-x: 60
        O...h-N: 60
        Weight of restraints: 1.0 (120)
        Total hydrogen bond restraints: 1.0 (120)
        O...H-x: 1.0 (60)
        O...h-N: 1.0 (60)
        Potential type of restraints: lower-bound-parabolic (120)
        Total hydrogen bond restraints: lower-bound-parabolic (120)
        O...H-x: lower-bound-parabolic (60)
        O...h-N: lower-bound-parabolic (60)
        Range of distance target values: 1.8, 2.7 (Å)
        Histogram of distance target values
        Distance restraints per residue
        Chain_ID: A
        Distance restraints on contact map
        Chain_ID_1: A - Chain_ID_2: A
        Saveframe: DYANA/DIANA_distance_constraints_5
        Status: OK
        Experiment type: hbond
        Sequence coverage of experimental data
        Entity_assembly_ID: A, Chain length: 108, Sequence coverage: 70.4%
        --------10--------20--------30--------40--------50--------60--------70--------80--------90-------100 MVNLGLSRVDDAVAAKHPGLGEYAACQSHAFMKGVFTFVTGTGMAFGLQMFIQRKFPYPLQWSLLVAVVAGSVVSYGVTRVESEKCNNLWLFLETGQLPK |||||||||| ||||||||||||||||||||| |||||||||||| ||||||||||||||||||||||||||||||||| .....LSRVDDAVAA....LGEYAACQSHAFMKGVFTFVT..GMAFGLQMFIQR.......WSLLVAVVAGSVVSYGVTRVESEKCNNLWLFLE --------10--------20--------30--------40--------50--------60--------70--------80--------90---- -------- DRSTDQRS
        Total number of restraints: 120
        Total hydrogen bond restraints: 120
        O...H-x: 60
        O...h-N: 60
        Weight of restraints: 1.0 (120)
        Total hydrogen bond restraints: 1.0 (120)
        O...H-x: 1.0 (60)
        O...h-N: 1.0 (60)
        Potential type of restraints: upper-bound-parabolic (120)
        Total hydrogen bond restraints: upper-bound-parabolic (120)
        O...H-x: upper-bound-parabolic (60)
        O...h-N: upper-bound-parabolic (60)
        Range of distance target values: 2.0, 3.0 (Å)
        Histogram of distance target values
        Distance restraints per residue
        Chain_ID: A
        Distance restraints on contact map
        Chain_ID_1: A - Chain_ID_2: A

Keywords Backbone structure, Helical bundle, Homo sapiens, Membrane protein

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Found 1 Document (0.964 seconds)

BMRB: 18222

Sample #1

Sample #2

Sample #3

Sample #4

Sample #5

Chemical shift reference

Chemical shift reference

Chemical shift reference

Entries sharing articles BMRB: 6, Swiss-Prot: 6 entries Detail

Related entities 1. TMEM141, : 1 : 2 : 7 entities Detail

Experiments performed 9 experiments Detail

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NMR combined restraints 8 contents Detail