BMRBj - BMREntryMaster

Found 1 Document (0.888 seconds)

BMRB: 19637

2MHL

NMR solution Structure of the E.coli Outer Membrane Protein W

Authors

Horst, R., Stanczak, P., Wuthrich, K.

Assembly

Outer Membrane Protein X from E. coli

Entity

1. Outer Membrane Protein X from E. coli (polymer, Thiol state: not present), 192 monomers, 20983.23 Da Detail

MHEAGEFFMR AGSATVRPTE GAGGTLGSLG GFSVTNNTQL GLTFTYMATD NIGVELLAAT PFRHKIGTRA TGDIATVHHL PPTLMAQWYF GDASSKFRPY VGAGINYTTF FDNGFNDHGK EAGLSDLSLK DSWGAAGQVG VDYLINRDWL VNMSVWYMDI DTTANYKLGG AQQHDSVRLD PWVFMFSAGY RF

Formula weight

20983.23 Da

Source organism

Escherichia coli

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 91.7 %, Completeness: 43.3 %, Completeness (bb): 75.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	43.3 % (933 of 2156)	23.7 % (260 of 1096)	57.8 % (494 of 855)	87.3 % (179 of 205)
Backbone	75.1 % (856 of 1140)	50.2 % (202 of 402)	86.8 % (479 of 552)	94.1 % (175 of 186)
Sidechain	18.8 % (223 of 1184)	8.4 % (58 of 694)	34.2 % (161 of 471)	21.1 % (4 of 19)
Aromatic	4.0 % (11 of 278)	5.8 % (8 of 139)	0.0 % (0 of 134)	60.0 % (3 of 5)
Methyl	19.7 % (39 of 198)	12.1 % (12 of 99)	27.3 % (27 of 99)

1. Outer Membrane Protein W

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 bar, Temperature 308 K, pH 6.8

#	Name	Isotope labeling	Concentration
1	Outer Membrane Protein W	[U-13C; U-15N; U-2H]	1.2 mM
2	H2O	natural abundance	90 %
3	D2O	natural abundance	10 %
4	Sodium Chloride	natural abundance	10 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291
³¹P	DSS	methyl protons	na	indirect	0.4048086

Referencing offset: 1.09 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291
³¹P	DSS	methyl protons	na	indirect	0.4048086

Referencing offset: 1.09 ppm, Outliers: 1 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291
³¹P	DSS	methyl protons	na	indirect	0.4048086

Referencing offset: 0.7 ppm, Outliers: 3 Detail

Protein Blocks Logo

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

Release date

2014-08-03

Citation

NMR polypeptide backbone conformation of the E. coli outer membrane protein W
Horst, R., Stanczak, P., Wuthrich, K.
Structure (2014), 22, 1204-1209, PubMed 25017731 , DOI 10.1016/j.str.2014.05.016 , Abstract

Related entities 1. Outer Membrane Protein X from E. coli, : 1 : 4 : 15 entities Detail

Interaction partners 1. Outer Membrane Protein X from E. coli, : 4 interactors Detail

More details for 4 interactors identified by 3 citations

Experiments performed 2 experiments Detail

NMR combined restraints 3 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints	combined_19637_2mhl.nef
Input source #2: Coordindates	2mhl.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
MHEAGEFFMRAGSATVRPTEGAGGTLGSLGGFSVTNNTQLGLTFTYMATDNIGVELLAATPFRHKIGTRATGDIATVHHLPPTLMAQWYFGDASSKFRPY
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MHEAGEFFMRAGSATVRPTEGAGGTLGSLGGFSVTNNTQLGLTFTYMATDNIGVELLAATPFRHKIGTRATGDIATVHHLPPTLMAQWYFGDASSKFRPY

-------110-------120-------130-------140-------150-------160-------170-------180-------190--
VGAGINYTTFFDNGFNDHGKEAGLSDLSLKDSWGAAGQVGVDYLINRDWLVNMSVWYMDIDTTANYKLGGAQQHDSVRLDPWVFMFSAGYRF
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
VGAGINYTTFFDNGFNDHGKEAGLSDLSLKDSWGAAGQVGVDYLINRDWLVNMSVWYMDIDTTANYKLGGAQQHDSVRLDPWVFMFSAGYRF

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	192	0	0	100.0

Content subtype: combined_19637_2mhl.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	824		90.6 (chain: A, length: 192)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	OK	224 (1)	noe	87.0 (chain: A, length: 192)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 192, Sequence coverage: 90.6%
- Total number of assignments
  - ¹H chemical shifts: 177
  - ¹³C chemical shifts: 470
  - ¹⁵N chemical shifts: 177
- Completeness of assignments
  - Entity_assemble_ID: A
- 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	1096	177	16.1
¹³C chemical shifts	855	470	55.0
¹⁵N chemical shifts	213	177	83.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	402	174	43.3
¹³C chemical shifts	384	326	84.9
¹⁵N chemical shifts	186	174	93.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	694	3	0.4
¹³C chemical shifts	471	144	30.6
¹⁵N chemical shifts	27	3	11.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	106	0	0.0
¹³C chemical shifts	106	18	17.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	139	3	2.2
¹³C chemical shifts	134	0	0.0
¹⁵N chemical shifts	5	3	60.0

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 192, Sequence coverage: 87.0%
- Total number of restraints: 224
- Weight of restraints: 1.0 (224)
- Potential type of restraints: upper-bound-parabolic (224)
- Range of distance target values: 3.22, 7.5 (Å)
- Histogram of distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map

Keywords beta barrel, integral membrane protein, outer membrane protein

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Found 1 Document (0.888 seconds)

BMRB: 19637

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Outer Membrane Protein X from E. coli, : 1 : 4 : 15 entities Detail

Interaction partners 1. Outer Membrane Protein X from E. coli, : 4 interactors Detail

Experiments performed 2 experiments Detail

Instrument

Sample

Instrument

Sample

NMR combined restraints 3 contents Detail