BMRBj - BMREntryMaster

Found 1 Document (1.434 seconds)

BMRB: 7208

2KPF

1H, 13C, 15N Chemical shift assignment for Glycophorine A in bicelles and micelles

Authors

Mineev, K.S., Bocharov, E.V., Maslennikov, I.V., Goncharuk, M.V., Arseniev, A.S.

Assembly

GpATM

Entity

1. GpATM (polymer, Thiol state: not present), 38 monomers, 4235.048 × 2 Da Detail

RVQLAHHFSE PEITLIIFGV MAGVIGTILL ISYGIRRL

Total weight

8470.096 Da

Max. entity weight

4235.048 Da

Source organism

Homo sapiens

Exptl. method

NMR

Data set

assigned_chemical_shifts, coupling_constants, heteronucl_T1_relaxation, heteronucl_T2_relaxation

Chem. Shift Complete1

Sequence coverage: 97.4 %, Completeness: 82.0 %, Completeness (bb): 81.0 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	82.0 % (373 of 455)	92.7 % (215 of 232)	67.0 % (124 of 185)	89.5 % (34 of 38)
Backbone	81.0 % (183 of 226)	93.7 % (74 of 79)	68.2 % (75 of 110)	91.9 % (34 of 37)
Sidechain	84.8 % (223 of 263)	92.2 % (141 of 153)	75.2 % (82 of 109)	0.0 % (0 of 1)
Aromatic	44.4 % (16 of 36)	83.3 % (15 of 18)	5.6 % (1 of 18)
Methyl	92.6 % (63 of 68)	97.1 % (33 of 34)	88.2 % (30 of 34)

1. GpATM

RVQLAHHFSE PEITLIIFGV MAGVIGTILL ISYGIRRL

Show sample condition

Sample

Temperature 313 (±1) K, pH 5.4 (±0.1)

#	Name	Isotope labeling	Type	Concentration
9	GpATM	[U-15N; U-13C]	protein	2.0 (±0.2) mM
10	DMPC	[U-2H]	lipid	16.0 (±1.0) mM
11	DHPC	[U-2H]	lipid	64.0 (±1.0) mM

Chem. Shift Complete2

Sequence coverage: 100.0 %, Completeness: 86.0 %, Completeness (bb): 88.9 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	86.0 % (783 of 910)	93.3 % (433 of 464)	75.4 % (279 of 370)	93.4 % (71 of 76)
Backbone	88.9 % (402 of 452)	95.6 % (151 of 158)	82.3 % (181 of 220)	94.6 % (70 of 74)
Sidechain	85.2 % (448 of 526)	92.2 % (282 of 306)	75.7 % (165 of 218)	50.0 % (1 of 2)
Aromatic	41.7 % (30 of 72)	72.2 % (26 of 36)	11.1 % (4 of 36)
Methyl	91.2 % (124 of 136)	95.6 % (65 of 68)	86.8 % (59 of 68)

1. GpATM

RVQLAHHFSE PEITLIIFGV MAGVIGTILL ISYGIRRL

Show sample condition

Sample

Temperature 313 (±1) K, pH 5.4 (±0.1)

#	Name	Isotope labeling	Type	Concentration
9	GpATM	[U-15N; U-13C]	protein	2.0 (±0.2) mM
10	DMPC	[U-2H]	lipid	16.0 (±1.0) mM
11	DHPC	[U-2H]	lipid	64.0 (±1.0) mM

Heteronucl. T₁

64 T₁ values in 2 lists
Coherence Sz, Field strength (¹H) 600 MHz, Temperature 313 (±1) K, pH 5.4 (±0.1) Detail

Heteronucl. T₂

64 T₂ values in 2 lists
Coherence S(+,-), Field strength (¹H) 600 MHz, Temperature 313 (±1) K, pH 5.4 (±0.1) Detail

Heteronucl. T₁/T₂

64 T₁/T₂ values in 2 lists
Field strength (¹H) 600 MHz, Temperature 313 (±1) K, pH 5.4 (±0.1) Detail

Coupling constant

84 J values in 2 lists
Temperature 313 (±1) K, pH 5.4 (±0.1) Detail

Release date

2007-01-08

Citation

Structure and dynamics of glycophorin A TM segment in micelles and bicelles
Mineev, K.S., Bocharov, E.V., Maslennikov, I.V., Goncharuk, M.V., Arseniev, A.S.

Related entities 1. GpATM, : 1 : 2 : 3 : 14 entities Detail

Interaction partners 1. GpATM, : 3 interactors Detail

More details for 3 interactors identified by 3 citations

Chemical shift validation 4 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts, Heteronucl T1 relaxation data, Heteronucl T2 relaxation data	bmr7208_3.str
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

Content subtype: bmr7208_3.str

#	Content subtype	Saveframe	Status	# of rows	Sequence coverage (%)
1	Assigned chemical shifts	shifts_mic	Warning	437	97.4 (chain: 1, length: 38)
2	Assigned chemical shifts	shifts_bic	Warning	469	100.0 (chain: 1, length: 38)
1	Chemical shift references	chemical_shift_referencing	OK	3	No information

Assigned chemical shifts

Saveframe: shifts_mic
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 38, Sequence coverage: 97.4%
- Total number of assignments
  - ¹H chemical shifts: 287
  - ¹³C chemical shifts: 117
  - ¹⁵N chemical shifts: 33
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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: 1
Saveframe: shifts_bic
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 38, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 280
  - ¹³C chemical shifts: 151
  - ¹⁵N chemical shifts: 38
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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: 1

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
7	HIS	HD1	7.059
14	THR	HG1	4.591
27	THR	HG1	4.914
32	SER	HG	4.625
37	ARG	HH21	7.334
37	ARG	HH22	7.334

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	232	215	92.7
¹³C chemical shifts	185	117	63.2
¹⁵N chemical shifts	41	33	80.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	79	74	93.7
¹³C chemical shifts	76	37	48.7
¹⁵N chemical shifts	37	33	89.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	153	141	92.2
¹³C chemical shifts	109	80	73.4
¹⁵N chemical shifts	4	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	35	33	94.3
¹³C chemical shifts	35	28	80.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	18	15	83.3
¹³C chemical shifts	18	1	5.6

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
14	THR	HG1	4.62
27	THR	HG1	4.94
32	SER	HG	4.635
36	ARG	HH11	6.82
36	ARG	HH12	6.82
37	ARG	HH11	6.679
37	ARG	HH12	6.679

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	232	209	90.1
¹³C chemical shifts	185	151	81.6
¹⁵N chemical shifts	41	38	92.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	79	76	96.2
¹³C chemical shifts	76	72	94.7
¹⁵N chemical shifts	37	35	94.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	153	133	86.9
¹³C chemical shifts	109	79	72.5
¹⁵N chemical shifts	4	3	75.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	35	32	91.4
¹³C chemical shifts	35	30	85.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	18	4	22.2
¹³C chemical shifts	18	0	0.0

Keywords assignment, dimer, glycophorin, membrane mimetics, structure

Search

Query history

Resources

Search for primary databases

Search for subsidiary databases

Display

Hits per page

Statistics

Query Changes will take effect after "OK" button is selected.

Maximum hits

Default conjunction operator

Omni-box

Search filter

Sequence search (BLAST)

E-value

Query sequence coverage

Miscellaneous

The number of previewed publications

Completeness of assigned chemical shift

Sequence chart about top aligned regions

Sequence chart about interacting regions

Hit context with highlight

Link destinations for BMRB, PDB and EMDB

Found 1 Document (1.434 seconds)

BMRB: 7208

Sample

Sample

Related entities 1. GpATM, : 1 : 2 : 3 : 14 entities Detail

Interaction partners 1. GpATM, : 3 interactors Detail

Chemical shift validation 4 contents Detail