BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	81.7 % (924 of 1131)	79.0 % (464 of 587)	82.4 % (366 of 444)	94.0 % (94 of 100)
Backbone	96.6 % (566 of 586)	97.5 % (196 of 201)	95.2 % (276 of 290)	98.9 % (94 of 95)
Sidechain	70.5 % (449 of 637)	69.4 % (268 of 386)	73.6 % (181 of 246)	0.0 % (0 of 5)
Aromatic	16.7 % (12 of 72)	33.3 % (12 of 36)	0.0 % (0 of 34)	0.0 % (0 of 2)
Methyl	94.1 % (111 of 118)	96.6 % (57 of 59)	91.5 % (54 of 59)

1. entity

MSANRRWWVP PDDEDCVSEK LLRKTRESPL VPIGLGGCLV VAAYRIYRLR SRGSTKMSIH LIHTRVAAQA CAVGAIMLGA VYTMYSDYVK RMAQDAGEK

Show sample condition

Sample #1

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6.0, Details Combinatorial residue-selective 15N,13C1-labeled protein

#	Name	Isotope labeling	Concentration
1	HIGD1B	[U-15N; U13C1]	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-labeled protein

#	Name	Isotope labeling	Concentration
7	HIGD1B	[U-15N]	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	HIGD1B	[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-13C-2H-labeled protein

#	Name	Isotope labeling	Concentration
19	HIGD1B	[U-15N; U-13C; U-2H]	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-13C-labeled protein with d27-LMPG

#	Name	Isotope labeling	Concentration
25	HIGD1B	[U-15N; U-13C]	?0.2 mM
26	MES-Bis-TRIS	natural abundance	20 mM
27	d27-LMPG	95%-2H in alkyl chain	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 single cysteine mutants for paramagnetic MTSL labeling

#	Name	Isotope labeling	Concentration
31	HIGD1B	[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 single cysteine mutants for labeling with diamagnetic MTSL analog

#	Name	Isotope labeling	Concentration
37	HIGD1B	[U-15N]	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 %

Sample #8

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 6.0, Details U-15N-2H-labeled protein with back-exchanged amides (expressed and prepared in H2O)

#	Name	Isotope labeling	Concentration
43	HIGD1B	[U-15N; U-2H]	0.2 mM
44	MES-Bis-TRIS	natural abundance	20 mM
45	LMPG	natural abundance	2 %
46	DSS	natural abundance	0.5 mM
47	H2O	natural abundance	95 %
48	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: 3.18 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: 3.18 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: 0.04 ppm, Outliers: 2 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: 2.83 ppm, Outliers: 2 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2LON, 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: 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: 18222 released on 2012-05-21
    Title Backbone structure of human membrane protein TMEM141
  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. HIGD1B, : 1 : 2 : 26 entities Detail

Interaction partners 1. HIGD1B, : 1 interactors Detail

More details for 1 interactors identified by 1 citations

Experiments performed 13 experiments Detail

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints	combined_18218_2lon.nef
Input source #2: Coordindates	2lon.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---------
MSANRRWWVPPDDEDCVSEKLLRKTRESPLVPIGLGGCLVVAAYRIYRLRSRGSTKMSIHLIHTRVAAQACAVGAIMLGAVYTMYSDYVKRMAQDAGEK
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MSANRRWWVPPDDEDCVSEKLLRKTRESPLVPIGLGGCLVVAAYRIYRLRSRGSTKMSIHLIHTRVAAQACAVGAIMLGAVYTMYSDYVKRMAQDAGEK

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	99	0	0	100.0

Content subtype: combined_18218_2lon.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	885		100.0 (chain: A, length: 99)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	OK	407 (1)	undefined	94.9 (chain: A, length: 99)
2	Distance restraints	DYANA/DIANA_distance_constraints_3	OK	285 (1)	undefined	87.9 (chain: A, length: 99)
3	Distance restraints	DYANA/DIANA_distance_constraints_4	Warning	168 (1)	hbond	54.5 (chain: A, length: 99)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 99, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 440
  - ¹³C chemical shifts: 351
  - ¹⁵N chemical shifts: 94
- 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	587	440	75.0
¹³C chemical shifts	444	351	79.1
¹⁵N chemical shifts	110	94	85.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	201	196	97.5
¹³C chemical shifts	198	183	92.4
¹⁵N chemical shifts	95	94	98.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	386	244	63.2
¹³C chemical shifts	246	168	68.3
¹⁵N chemical shifts	15	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	64	59	92.2
¹³C chemical shifts	64	48	75.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	36	12	33.3
¹³C chemical shifts	34	0	0.0
¹⁵N chemical shifts	2	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: 99, Sequence coverage: 94.9%
- Total number of restraints: 407
- Weight of restraints: 1.0 (407)
- Potential type of restraints: lower-bound-parabolic (407)
- Range of distance target values: 4.8, 25.0 (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: 99, Sequence coverage: 87.9%
  - Total number of restraints: 285
  - Weight of restraints: 1.0 (285)
  - Potential type of restraints: upper-bound-parabolic (285)
  - Range of distance target values: 10.0, 29.1 (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: 99, Sequence coverage: 54.5%
    - Total number of restraints: 168
    - Weight of restraints: 1.0 (168)
    - Potential type of restraints: upper-bound-parabolic (168)
    - 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: 18218

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Sample #8

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

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

Related entities 1. HIGD1B, : 1 : 2 : 26 entities Detail

Interaction partners 1. HIGD1B, : 1 interactors Detail

Experiments performed 13 experiments Detail

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NMR combined restraints 5 contents Detail