BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	84.4 % (635 of 752)	97.7 % (382 of 391)	64.9 % (187 of 288)	90.4 % (66 of 73)
Backbone	76.8 % (298 of 388)	95.5 % (128 of 134)	59.5 % (113 of 190)	89.1 % (57 of 64)
Sidechain	93.2 % (395 of 424)	98.8 % (254 of 257)	83.5 % (132 of 158)	100.0 % (9 of 9)
Aromatic	50.0 % (26 of 52)	96.2 % (25 of 26)	0.0 % (0 of 25)	100.0 % (1 of 1)
Methyl	100.0 % (70 of 70)	100.0 % (35 of 35)	100.0 % (35 of 35)

1. MuB-NTD

GPMNISDIRA GLRTLVENEE TTFKQIALES GLSTGTISSF INDKYNGDNE RVSQTLQRWL EKYHA

Show sample condition

Sample #1

Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 298 K, pH 7.5

#	Name	Isotope labeling	Concentration
1	MuB-NTD	natural abundance	500 uM
2	sodium phosphate	natural abundance	20 mM
3	sodium chloride	natural abundance	100 mM

Sample #2

Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 298 K, pH 7.5

#	Name	Isotope labeling	Concentration
4	MuB-NTD	[U-98% 15N]	500 uM
5	sodium phosphate	natural abundance	20 mM
6	sodium chloride	natural abundance	100 mM

Protein Blocks Logo

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

Release date

2015-06-28

Related entities 1. N terminal domain of the MuB AAA+ ATPase, : 2 : 9 entities Detail

Experiments performed 6 experiments Detail

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_25037_2mqk.nef
Input source #2: Coordindates	2mqk.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

-0--------10--------20--------30--------40--------50--------60---
GPMNISDIRAGLRTLVENEETTFKQIALESGLSTGTISSFINDKYNGDNERVSQTLQRWLEKYHA
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
GPMNISDIRAGLRTLVENEETTFKQIALESGLSTGTISSFINDKYNGDNERVSQTLQRWLEKYHA
--------10--------20--------30--------40--------50--------60-----

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	65	0	0	100.0

Content subtype: combined_25037_2mqk.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	633		100.0 (chain: A, length: 65)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	OK	1912 (1)	noe	96.9 (chain: A, length: 65)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_3	OK	92 (92)	.	86.2 (chain: A, length: 65)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 65, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 382
  - ¹³C chemical shifts: 183
  - ¹⁵N chemical shifts: 68
- Completeness of assignments
  - Entity_assemble_ID: A
- 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

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
28	SER	HG	4.553

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	391	381	97.4
¹³C chemical shifts	288	183	63.5
¹⁵N chemical shifts	77	68	88.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	134	127	94.8
¹³C chemical shifts	130	51	39.2
¹⁵N chemical shifts	64	57	89.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	257	254	98.8
¹³C chemical shifts	158	132	83.5
¹⁵N chemical shifts	13	11	84.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	36	36	100.0
¹³C chemical shifts	36	36	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	26	25	96.2
¹³C chemical shifts	25	0	0.0
¹⁵N chemical shifts	1	1	100.0

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 65, Sequence coverage: 96.9%
- Total number of restraints: 1909
- Weight of restraints: 1.0 (1909)
- Potential type of restraints: upper-bound-parabolic (1909)
- Range of distance target values: 2.43, 5.5 (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

Dihedral angle restraints

Saveframe: DYANA/DIANA_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 65, Sequence coverage: 86.2%
- Total number of restraints: 92
- Total number of restraints per polymer type: 92
- Weight of restraints: 1.0 (92)
- Potential type of restraints: square-well-parabolic (92)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords protein

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 (0.573 seconds)

BMRB: 25037

Sample #1

Sample #2

Related entities 1. N terminal domain of the MuB AAA+ ATPase, : 2 : 9 entities Detail

Experiments performed 6 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 4 contents Detail