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BMRB: 25788

2N70

Two-fold symmetric structure of the 18-60 construct of S31N M2 from Influenza A in lipid bilayers

Authors

Andreas, L.B., Reese, M., Eddy, M.T., Gelev, V., Ni, Q., Miller, E.A., Emsley, L., Pintacuda, G., Chou, J.J., Griffin, R.G.

Assembly

Influenza-A M2

Entity

1. Influenza-A M2 (polymer, Thiol state: not present), 43 monomers, 5028.851 × 4 Da Detail

RSNDSSDPLV VAANIIGILH LILWILDRLF FKSIYRFFEH GLK

Total weight

20115.404 Da

Max. entity weight

5028.851 Da

Source organism

Influenza A virus (A/udorn/1972(H3N2))

Exptl. method

NMR

Refine. method

DGSA-distance geometry simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 72.1 %, Completeness: 43.4 %, Completeness (bb): 58.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	43.4 % (235 of 542)	19.7 % (55 of 279)	67.9 % (148 of 218)	71.1 % (32 of 45)
Backbone	58.2 % (149 of 256)	34.5 % (30 of 87)	70.1 % (89 of 127)	71.4 % (30 of 42)
Sidechain	35.2 % (115 of 327)	13.0 % (25 of 192)	66.7 % (88 of 132)	66.7 % (2 of 3)
Aromatic	19.1 % (13 of 68)	2.9 % (1 of 34)	33.3 % (11 of 33)	100.0 % (1 of 1)
Methyl	56.3 % (36 of 64)	18.8 % (6 of 32)	93.8 % (30 of 32)

1. matrix protein 2

RSNDSSDPLV VAANIIGILH LILWILDRLF FKSIYRFFEH GLK

Show sample condition

Sample #1

#	Name	Isotope labeling	Type	Concentration
1	sodium phosphate	natural abundance	buffer	40 (±1.0) mM
2	glutamic acid	natural abundance		30 (±1.0) mM
3	sodium azide	natural abundance		3 (±1.0) mM
4	1,2-diphytanoyl-sn-glycero-3-phosphocholine	natural abundance		50 % w/w
5	matrix protein 2	[U-13C,15N]	protein	50 % w/w
6	H2O	natural abundance	solvent	100 %

Sample #2

Solvent system H2O, Temperature 298 (±5) K, pH 7.8, Details Per liter, 3 g 13C glucose and 1 g 15N ammonium chloride (CIL), with another 0.5 to 1 g 13C glucose added at induction. Cells were grown in 700 mL of media, with 300 mL of media used to dissolve the amino acids. When the OD600 reached 0.7, the reserved 300 mL of media was added, along with amino acids at natural isotopic abundance:23,24 150 mg isoleucine, 150 mg leucine, 50 mg phenylalanine, and 100 mg tyrosine (Sigma-Aldrich). Expression of protein was induced with 150 M IPTG at 18 C as before. The final OD600 reached 3.5 to 4.6, after 18 hours of expression at 18 C, and yielded up to 15 mg of pure protein.

#	Name	Isotope labeling	Type	Concentration
7	sodium phosphate	natural abundance	buffer	40 (±1.0) mM
8	glutamic acid	natural abundance		30 (±1.0) mM
9	sodium azide	natural abundance		3 (±1.0) mM
10	1,2-diphytanoyl-sn-glycero-3-phosphocholine	natural abundance		50 % w/w
11	matrix protein 2	U-13C,15N-[12C,14N-ILFY]	protein	50 % w/w
12	H2O	natural abundance	solvent	100 %

Sample #3

Solvent system H2O, Temperature 298 (±5) K, pH 7.8, Details Preparation was identical to U-13C-15N M2 except that specifically isotopically labeled glucose was used. The labeling pattern resulting from [1,6-13C]-glucose is the same as from [1-13C]-glucose25 (Omicron Biochemicals) except that the [1,6-13C]-glucose results in double the labeling level per site.

#	Name	Isotope labeling	Type	Concentration
19	sodium phosphate	natural abundance	buffer	40 (±1.0) mM
20	glutamic acid	natural abundance		30 (±1.0) mM
21	sodium azide	natural abundance		3 (±1.0) mM
22	1,2-diphytanoyl-sn-glycero-3-phosphocholine	natural abundance		50 % w/w
23	matrix protein 2	[1,6-13C2]-Glucose	protein	50 % w/w
24	H2O	natural abundance	solvent	100 %

Sample #4

Solvent system H2O, Temperature 298 (±5) K, pH 7.8, Details An overnight culture in 50 mL of 90 % 2H M9, 10 % SOC media was grown from a fresh transformation in BL21-DE3 until an OD600 of 2 to 3. Cells were then pelleted by centrifugation and transferred to 1L of 2H M9 media containing 3 g 2H-13C glucose, 1 g 15N ammonium chloride, salts, and Centrum in 1 L of 99.8 % 2H D2O. The doubling time was 2 hours. At an OD600 of 0.65 to 0.75, ILV precursors were added: 75 mg alpha-keto-butyric acid,26 sodium salt 4-13C 99 %, 3,3,4,4-2H4, 98 % (CIL), and 350 mg of 2-(13C,2H2)methyl-4-(2H3)-acetolactate prepared as described previously. Cells were harvested after 24 to 36 hours, and yielded up to 5 mg of pure protein. This labeling pattern re-sults in methyl groups with isolated 13C1H spin pairs in an otherwise 2H, 12C background at nearby sites. The protein was purified and refolded in 1H buffers, resulting in complete exchange to 1H at exchangeable sites such as the backbone amides.

#	Name	Isotope labeling	Type	Concentration
25	sodium phosphate	natural abundance	buffer	40 (±1.0) mM
26	glutamic acid	natural abundance		30 (±1.0) mM
27	sodium azide	natural abundance		3 (±1.0) mM
28	1,2-diphytanoyl-sn-glycero-3-phosphocholine	aliphatic chain [U-2H]		50 % w/w
29	matrix protein 2	U-13C,15N,2H-[12C,13C2H21H 1-Ile, 12C,13Ca,13C',13C2H21H 2-Leu, 12C,13C2H21H 2-Val]	protein	50 % w/w
30	H2O	natural abundance	solvent	100 %

Protein Blocks Logo

Calculated from 20 models in PDB: 2N70, Strand ID: A, B, C, D Detail

Release date

2016-02-23

Citation

Structure and Mechanism of the Influenza A M218-60 Dimer of Dimers
Andreas, L.B., Reese, M., Eddy, M.T., Gelev, V., Ni, Q., Miller, E.A., Emsley, L., Pintacuda, G., Chou, J.J., Griffin, R.G.
J. Am. Chem. Soc. (2015), 137, 14877-14886, PubMed 26218479 , DOI 10.1021/jacs.5b04802 , Abstract

Related entities 1. Influenza-A M2, : 1 : 1 : 1 : 93 entities Detail

Experiments performed 11 experiments Detail

1 2D ZF-TEDOR

Instrument

Bruker Avance - 800 MHz

Sample

State anisotropic, Solvent system H2O, Temperature 298 (±5) K, pH 7.8, Details Per liter, 3 g 13C glucose and 1 g 15N ammonium chloride (CIL), with another 0.5 to 1 g 13C glucose added at induction (150 M IPTG, 18 C) at an OD600 of 0.7 to 0.9. The final OD600 reached 3.5 to 4, after 18 hours of expression at 18 C, 15mg of pure protein.

#	Name	Isotope labeling	Type	Concentration
1	sodium phosphate	natural abundance	buffer	40 (±1.0) mM
2	glutamic acid	natural abundance		30 (±1.0) mM
3	sodium azide	natural abundance		3 (±1.0) mM
4	1,2-diphytanoyl-sn-glycero-3-phosphocholine	natural abundance		50 % w/w
5	matrix protein 2	[U-13C,15N]	protein	50 % w/w
6	H2O	natural abundance	solvent	100 %

2 3D ZF-TEDOR-RFDR

Instrument

Bruker Avance - 800 MHz

Sample

State anisotropic, Solvent system H2O, Temperature 298 (±5) K, pH 7.8, Details Per liter, 3 g 13C glucose and 1 g 15N ammonium chloride (CIL), with another 0.5 to 1 g 13C glucose added at induction (150 M IPTG, 18 C) at an OD600 of 0.7 to 0.9. The final OD600 reached 3.5 to 4, after 18 hours of expression at 18 C, 15mg of pure protein.

#	Name	Isotope labeling	Type	Concentration
1	sodium phosphate	natural abundance	buffer	40 (±1.0) mM
2	glutamic acid	natural abundance		30 (±1.0) mM
3	sodium azide	natural abundance		3 (±1.0) mM
4	1,2-diphytanoyl-sn-glycero-3-phosphocholine	natural abundance		50 % w/w
5	matrix protein 2	[U-13C,15N]	protein	50 % w/w
6	H2O	natural abundance	solvent	100 %

3 2D HN

Instrument

Bruker Avance - 800 MHz

Sample

State anisotropic, Solvent system H2O, Temperature 298 (±5) K, pH 7.8, Details Per liter, 3 g 13C glucose and 1 g 15N ammonium chloride (CIL), with another 0.5 to 1 g 13C glucose added at induction (150 M IPTG, 18 C) at an OD600 of 0.7 to 0.9. The final OD600 reached 3.5 to 4, after 18 hours of expression at 18 C, 15mg of pure protein.

#	Name	Isotope labeling	Type	Concentration
1	sodium phosphate	natural abundance	buffer	40 (±1.0) mM
2	glutamic acid	natural abundance		30 (±1.0) mM
3	sodium azide	natural abundance		3 (±1.0) mM
4	1,2-diphytanoyl-sn-glycero-3-phosphocholine	natural abundance		50 % w/w
5	matrix protein 2	[U-13C,15N]	protein	50 % w/w
6	H2O	natural abundance	solvent	100 %

4 3D (H) CaNH

Instrument

Bruker Avance - 800 MHz

Sample

State anisotropic, Solvent system H2O, Temperature 298 (±5) K, pH 7.8, Details Per liter, 3 g 13C glucose and 1 g 15N ammonium chloride (CIL), with another 0.5 to 1 g 13C glucose added at induction. Cells were grown in 700 mL of media, with 300 mL of media used to dissolve the amino acids. When the OD600 reached 0.7, the reserved 300 mL of media was added, along with amino acids at natural isotopic abundance:23,24 150 mg isoleucine, 150 mg leucine, 50 mg phenylalanine, and 100 mg tyrosine (Sigma-Aldrich). Expression of protein was induced with 150 M IPTG at 18 C as before. The final OD600 reached 3.5 to 4.6, after 18 hours of expression at 18 C, and yielded up to 15 mg of pure protein.

#	Name	Isotope labeling	Type	Concentration
7	sodium phosphate	natural abundance	buffer	40 (±1.0) mM
8	glutamic acid	natural abundance		30 (±1.0) mM
9	sodium azide	natural abundance		3 (±1.0) mM
10	1,2-diphytanoyl-sn-glycero-3-phosphocholine	natural abundance		50 % w/w
11	matrix protein 2	U-13C,15N-[12C,14N-ILFY]	protein	50 % w/w
12	H2O	natural abundance	solvent	100 %

5 2D PAR

Instrument

Bruker Avance - 800 MHz

Sample

State anisotropic, Solvent system H2O, Temperature 298 (±5) K, pH 7.8, Details Per liter, 3 g 13C glucose and 1 g 15N ammonium chloride (CIL), with another 0.5 to 1 g 13C glucose added at induction (150 M IPTG, 18 C) at an OD600 of 0.7 to 0.9. The final OD600 reached 3.5 to 4, after 18 hours of expression at 18 C, 15mg of pure protein.

#	Name	Isotope labeling	Type	Concentration
1	sodium phosphate	natural abundance	buffer	40 (±1.0) mM
2	glutamic acid	natural abundance		30 (±1.0) mM
3	sodium azide	natural abundance		3 (±1.0) mM
4	1,2-diphytanoyl-sn-glycero-3-phosphocholine	natural abundance		50 % w/w
5	matrix protein 2	[U-13C,15N]	protein	50 % w/w
6	H2O	natural abundance	solvent	100 %

6 2D PDSD

Instrument

Bruker Avance - 800 MHz

Sample

State anisotropic, Solvent system H2O, Temperature 298 (±5) K, pH 7.8, Details Per liter, 3 g 13C glucose and 1 g 15N ammonium chloride (CIL), with another 0.5 to 1 g 13C glucose added at induction (150 M IPTG, 18 C) at an OD600 of 0.7 to 0.9. The final OD600 reached 3.5 to 4, after 18 hours of expression at 18 C, 15mg of pure protein.

#	Name	Isotope labeling	Type	Concentration
1	sodium phosphate	natural abundance	buffer	40 (±1.0) mM
2	glutamic acid	natural abundance		30 (±1.0) mM
3	sodium azide	natural abundance		3 (±1.0) mM
4	1,2-diphytanoyl-sn-glycero-3-phosphocholine	natural abundance		50 % w/w
5	matrix protein 2	[U-13C,15N]	protein	50 % w/w
6	H2O	natural abundance	solvent	100 %

7 2D ZF-TEDOR

Instrument

Bruker Avance - 800 MHz

Sample

State anisotropic, Solvent system H2O, Temperature 298 (±5) K, pH 7.8, Details Preparation was identical to U-13C-15N M2 except that specifically isotopically labeled glucose was used. The labeling pattern resulting from [1,6-13C]-glucose is the same as from [1-13C]-glucose25 (Omicron Biochemicals) except that the [1,6-13C]-glucose results in double the labeling level per site.

#	Name	Isotope labeling	Type	Concentration
19	sodium phosphate	natural abundance	buffer	40 (±1.0) mM
20	glutamic acid	natural abundance		30 (±1.0) mM
21	sodium azide	natural abundance		3 (±1.0) mM
22	1,2-diphytanoyl-sn-glycero-3-phosphocholine	natural abundance		50 % w/w
23	matrix protein 2	[1,6-13C2]-Glucose	protein	50 % w/w
24	H2O	natural abundance	solvent	100 %

8 2D RFDR

Instrument

Bruker Avance - 800 MHz

Sample

#	Name	Isotope labeling	Type	Concentration
19	sodium phosphate	natural abundance	buffer	40 (±1.0) mM
20	glutamic acid	natural abundance		30 (±1.0) mM
21	sodium azide	natural abundance		3 (±1.0) mM
22	1,2-diphytanoyl-sn-glycero-3-phosphocholine	natural abundance		50 % w/w
23	matrix protein 2	[1,6-13C2]-Glucose	protein	50 % w/w
24	H2O	natural abundance	solvent	100 %

9 3D 1H-1H RFDR

Instrument

Bruker Avance - 800 MHz

Sample

State anisotropic, Solvent system H2O, Temperature 298 (±5) K, pH 7.8, Details Per liter, 3 g 13C glucose and 1 g 15N ammonium chloride (CIL), with another 0.5 to 1 g 13C glucose added at induction. Cells were grown in 700 mL of media, with 300 mL of media used to dissolve the amino acids. When the OD600 reached 0.7, the reserved 300 mL of media was added, along with amino acids at natural isotopic abundance:23,24 150 mg isoleucine, 150 mg leucine, 50 mg phenylalanine, and 100 mg tyrosine (Sigma-Aldrich). Expression of protein was induced with 150 M IPTG at 18 C as before. The final OD600 reached 3.5 to 4.6, after 18 hours of expression at 18 C, and yielded up to 15 mg of pure protein.

#	Name	Isotope labeling	Type	Concentration
7	sodium phosphate	natural abundance	buffer	40 (±1.0) mM
8	glutamic acid	natural abundance		30 (±1.0) mM
9	sodium azide	natural abundance		3 (±1.0) mM
10	1,2-diphytanoyl-sn-glycero-3-phosphocholine	natural abundance		50 % w/w
11	matrix protein 2	U-13C,15N-[12C,14N-ILFY]	protein	50 % w/w
12	H2O	natural abundance	solvent	100 %

10 4D HCHHCH

Instrument

Bruker Avance - 800 MHz

Sample

State anisotropic, Solvent system H2O, Temperature 298 (±5) K, pH 7.8, Details Per liter, 3 g 13C glucose and 1 g 15N ammonium chloride (CIL), with another 0.5 to 1 g 13C glucose added at induction. Cells were grown in 700 mL of media, with 300 mL of media used to dissolve the amino acids. When the OD600 reached 0.7, the reserved 300 mL of media was added, along with amino acids at natural isotopic abundance:23,24 150 mg isoleucine, 150 mg leucine, 50 mg phenylalanine, and 100 mg tyrosine (Sigma-Aldrich). Expression of protein was induced with 150 M IPTG at 18 C as before. The final OD600 reached 3.5 to 4.6, after 18 hours of expression at 18 C, and yielded up to 15 mg of pure protein.

#	Name	Isotope labeling	Type	Concentration
7	sodium phosphate	natural abundance	buffer	40 (±1.0) mM
8	glutamic acid	natural abundance		30 (±1.0) mM
9	sodium azide	natural abundance		3 (±1.0) mM
10	1,2-diphytanoyl-sn-glycero-3-phosphocholine	natural abundance		50 % w/w
11	matrix protein 2	U-13C,15N-[12C,14N-ILFY]	protein	50 % w/w
12	H2O	natural abundance	solvent	100 %

11 2D C-H

Instrument

Bruker Avance - 800 MHz

Sample

State anisotropic, Solvent system H2O, Temperature 298 (±5) K, pH 7.8, Details An overnight culture in 50 mL of 90 % 2H M9, 10 % SOC media was grown from a fresh transformation in BL21-DE3 until an OD600 of 2 to 3. Cells were then pelleted by centrifugation and transferred to 1L of 2H M9 media containing 3 g 2H-13C glucose, 1 g 15N ammonium chloride, salts, and Centrum in 1 L of 99.8 % 2H D2O. The doubling time was 2 hours. At an OD600 of 0.65 to 0.75, ILV precursors were added: 75 mg alpha-keto-butyric acid,26 sodium salt 4-13C 99 %, 3,3,4,4-2H4, 98 % (CIL), and 350 mg of 2-(13C,2H2)methyl-4-(2H3)-acetolactate prepared as described previously. Cells were harvested after 24 to 36 hours, and yielded up to 5 mg of pure protein. This labeling pattern re-sults in methyl groups with isolated 13C1H spin pairs in an otherwise 2H, 12C background at nearby sites. The protein was purified and refolded in 1H buffers, resulting in complete exchange to 1H at exchangeable sites such as the backbone amides.

#	Name	Isotope labeling	Type	Concentration
25	sodium phosphate	natural abundance	buffer	40 (±1.0) mM
26	glutamic acid	natural abundance		30 (±1.0) mM
27	sodium azide	natural abundance		3 (±1.0) mM
28	1,2-diphytanoyl-sn-glycero-3-phosphocholine	aliphatic chain [U-2H]		50 % w/w
29	matrix protein 2	U-13C,15N,2H-[12C,13C2H21H 1-Ile, 12C,13Ca,13C',13C2H21H 2-Leu, 12C,13C2H21H 2-Val]	protein	50 % w/w
30	H2O	natural abundance	solvent	100 %

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_25788_2n70.nef
Input source #2: Coordindates	2n70.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

--120-----130-------140-------150-------160
RSNDSSDPLVVAANIIGILHLILWILDRLFFKSIYRFFEHGLK
|||||||||||||||||||||||||||||||||||||||||||
RSNDSSDPLVVAANIIGILHLILWILDRLFFKSIYRFFEHGLK
--------10--------20--------30--------40---

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

--220-----230-------240-------250-------260
RSNDSSDPLVVAANIIGILHLILWILDRLFFKSIYRFFEHGLK
|||||||||||||||||||||||||||||||||||||||||||
RSNDSSDPLVVAANIIGILHLILWILDRLFFKSIYRFFEHGLK
--------10--------20--------30--------40---

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

--320-----330-------340-------350-------360
RSNDSSDPLVVAANIIGILHLILWILDRLFFKSIYRFFEHGLK
|||||||||||||||||||||||||||||||||||||||||||
RSNDSSDPLVVAANIIGILHLILWILDRLFFKSIYRFFEHGLK
--------10--------20--------30--------40---

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

--420-----430-------440-------450-------460
RSNDSSDPLVVAANIIGILHLILWILDRLFFKSIYRFFEHGLK
|||||||||||||||||||||||||||||||||||||||||||
RSNDSSDPLVVAANIIGILHLILWILDRLFFKSIYRFFEHGLK
--------10--------20--------30--------40---

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Sequence coverage (%)
A	A	43	100.0
B	B	43	100.0
C	C	43	100.0
D	D	43	100.0

Content subtype: combined_25788_2n70.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	231		67.4 (chain: A, length: 43)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	1151 (1)	undefined	60.5 (chain: A, length: 43), 51.2 (chain: B, length: 43), 44.2 (chain: C, length: 43), 37.2 (chain: D, length: 43)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	184 (184)	.	67.4 (chain: A, length: 43), 67.4 (chain: B, length: 43), 48.8 (chain: C, length: 43), 48.8 (chain: D, length: 43)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1

Status: Warning

Sequence coverage of experimental data

Entity_assembly_ID: A, Chain length: 43, Sequence coverage: 67.4%

--120-----130-------140-------150-------160
RSNDSSDPLVVAANIIGILHLILWILDRLFFKSIYRFFEHGLK
      |||||||||||||||||||||||||||||        
......DPLVVAANIIGILHLILWILDRLFFKSIY        
--120-----130-------140-------150--

Total number of assignments
- ¹H chemical shifts: 47
- ¹³C chemical shifts: 149
- ¹⁵N chemical shifts: 35

Completeness of assignments

Entity_assemble_ID: A

Excluded Atom_ID in statistics

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
124	ASP	CG	179.075
125	PRO	N	135.18
131	ASN	CG	177.469
137	HIS	HE2	14.889
137	HIS	CG	136.279
137	HIS	ND1	251.069
137	HIS	NE2	173.47
141	TRP	CD2	129.327
141	TRP	CE2	138.728
141	TRP	CG	111.799
144	ASP	CG	180.189
145	ARG	CZ	159.631
149	LYS	NZ	32.214

All atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	279	46	16.5
¹³C chemical shifts	218	141	64.7
¹⁵N chemical shifts	48	31	64.6

Backbone atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	87	27	31.0
¹³C chemical shifts	86	56	65.1
¹⁵N chemical shifts	42	28	66.7

Side chain atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	192	19	9.9
¹³C chemical shifts	132	85	64.4
¹⁵N chemical shifts	6	3	50.0

Methyl group atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	32	3	9.4
¹³C chemical shifts	32	30	93.8

Aromatic group atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	34	1	2.9
¹³C chemical shifts	33	11	33.3
¹⁵N chemical shifts	1	1	100.0

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: A

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: OK
- Experiment type: undefined
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 43, Sequence coverage: 60.5%
  - Entity_assembly_ID: B, Chain length: 43, Sequence coverage: 51.2%
  - Entity_assembly_ID: C, Chain length: 43, Sequence coverage: 44.2%
  - Entity_assembly_ID: D, Chain length: 43, Sequence coverage: 37.2%
- Total number of restraints: 1151
- Weight of restraints: 1.0 (1151)
- Potential type of restraints: square-well-parabolic (1151)
- Range of distance target values: 2.1, 5.9 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
  - Chain_ID: B
  - Chain_ID: C
  - Chain_ID: D
- Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 43, Sequence coverage: 67.4%
  - Entity_assembly_ID: B, Chain length: 43, Sequence coverage: 67.4%
  - Entity_assembly_ID: C, Chain length: 43, Sequence coverage: 48.8%
  - Entity_assembly_ID: D, Chain length: 43, Sequence coverage: 48.8%
- Total number of restraints: 184
- Total number of restraints per polymer type: 184
- Weight of restraints: 1.0 (184)
- Potential type of restraints: square-well-parabolic (184)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A
  - Chain_ID: B

Keywords Influenza, M2, S31N

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Found 1 Document (0.693 seconds)

BMRB: 25788

Sample #1

Sample #2

Sample #3

Sample #4

Related entities 1. Influenza-A M2, : 1 : 1 : 1 : 93 entities Detail

Experiments performed 11 experiments Detail

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NMR combined restraints 4 contents Detail