BMRBj - BMREntryMaster

	Total	¹H	¹³C
All	75.1 % (837 of 1115)	81.6 % (519 of 636)	66.4 % (318 of 479)
Backbone	72.8 % (389 of 534)	88.9 % (192 of 216)	61.9 % (197 of 318)
Sidechain	78.5 % (536 of 683)	77.9 % (327 of 420)	79.5 % (209 of 263)
Aromatic	43.6 % (24 of 55)	57.1 % (16 of 28)	29.6 % (8 of 27)
Methyl	94.4 % (136 of 144)	94.4 % (68 of 72)	94.4 % (68 of 72)

1. entity 1

ALTTISPHDA QELIARGAKL IDIRDADEYL REHIPEADLA PLSVLEQSGL PAKLRHEQII FHCQAGKRTS NNADKLAAIA APAEIFLLED GIDGWKKAGL PVAVNKSQ

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Sample

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 303 K, pH 7, Details 1 mM [U-99% 13C; U-99% 15N] S-nitrosylated rhodanese domain, 95% H2O/5% D2O

#	Name	Isotope labeling	Type	Concentration
1	S-nitrosylated rhodanese domain	[U-99% 13C; U-99% 15N]		1 mM

LACS Plot; CA

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

Referencing offset: 0.47 ppm, Outliers: 1 Detail

LACS Plot; CB

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

Referencing offset: 0.47 ppm, Outliers: 1 Detail

LACS Plot; HA

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

Referencing offset: 0.02 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 5LAO, Strand ID: A Detail

Release date

2016-08-14

Citation

S-Nitrosylation Induces Structural and Dynamical Changes in a Rhodanese Family Protein
Eichmann, C., Tzitzilonis, C., Nakamura, T., Kwiatkowski, W., Maslennikov, I., Choe, S., Lipton, S.A., Riek, R.
J. Mol. Biol. (2016), 428, 3737-3751, PubMed 27473602 , DOI 10.1016/j.jmb.2016.07.010 , Abstract

Related entities 1. Inner membrane protein YgaP, : 1 : 5 : 5 : 63 entities Detail

Interaction partners 1. Inner membrane protein YgaP, : 1 interactors Detail

More details for 1 interactors identified by 1 citations

Experiments performed 6 experiments Detail

NMR combined restraints 3 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints	combined_34010_5lao.nef
Input source #2: Coordindates	5lao.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
ALTTISPHDAQELIARGAKLIDIRDADEYLREHIPEADLAPLSVLEQSGLPAKLRHEQIIFHCQAGKRTSNNADKLAAIAAPAEIFLLEDGIDGWKKAGL
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
ALTTISPHDAQELIARGAKLIDIRDADEYLREHIPEADLAPLSVLEQSGLPAKLRHEQIIFHCQAGKRTSNNADKLAAIAAPAEIFLLEDGIDGWKKAGL

--------
PVAVNKSQ
||||||||
PVAVNKSQ

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	108	0	0	100.0

Content subtype: combined_34010_5lao.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	826		94.4 (chain: A, length: 108)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	Warning	2480 (1)	noe	95.4 (chain: A, length: 108)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 108, Sequence coverage: 94.4%
- Total number of assignments
  - ¹H chemical shifts: 516
  - ¹³C chemical shifts: 310
- 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	636	515	81.0
¹³C chemical shifts	479	310	64.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	216	194	89.8
¹³C chemical shifts	216	99	45.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	420	321	76.4
¹³C chemical shifts	263	211	80.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	72	69	95.8
¹³C chemical shifts	72	70	97.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	28	16	57.1
¹³C chemical shifts	27	8	29.6

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 108, Sequence coverage: 95.4%
- Total number of restraints: 2480
- Weight of restraints: 1.0 (2480)
- Potential type of restraints: upper-bound-parabolic (2480)
- Range of distance target values: 2.07, 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

Keywords PROTEIN, S-nitrosylated rhodanese domain of YgaP, membrane protein

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Found 1 Document (0.714 seconds)

BMRB: 34010

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Inner membrane protein YgaP, : 1 : 5 : 5 : 63 entities Detail

Interaction partners 1. Inner membrane protein YgaP, : 1 interactors Detail

Experiments performed 6 experiments Detail

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NMR combined restraints 3 contents Detail