BMRBj - BMREntryMaster

	Total	¹H
All	6.7 % (54 of 809)	6.7 % (54 of 809)
Backbone	6.3 % (17 of 270)	6.3 % (17 of 270)
Sidechain	6.9 % (37 of 539)	6.9 % (37 of 539)
Aromatic	0.0 % (0 of 78)	0.0 % (0 of 78)
Methyl	7.5 % (4 of 53)	7.5 % (4 of 53)

1. entity 1

MGSSHHHHHH SSGLVPRGSH MEWYFGKLGR KDAERQLLSF GNPRGTFLIR ESETTKGAYS LSIRDWDDMK GDHVKHYKIR KLDNGGYYIT TRAQFETLQQ LVQHYSERAA GLCCRLVVPC HK

2. entity 2

EPQXQPGENL

Show sample condition

Sample

Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 298 K, pH 6.50

#	Name	Isotope labeling	Type	Concentration
1	entity_1	[U-99% 13C; U-99% 15N]		0.93 mM
2	entity_2	natural abundance		1.2 mM

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Calculated from 27 models in PDB: 2MRK, Strand ID: A, B Detail

Release date

2015-07-12

Citation

Dynamically coupled residues within the SH2 domain of FYN are key to unlock its activity
Huculeci, R., Cilia, E., Buts, L., Houben, K., van Nuland, N., Lenaerts, T.
Not known

Related entities 1. Fyn SH2 domain in complex with the natural inhibitory phosphotyrosine peptide, entity 1, : 3 : 97 entities Detail

Experiments performed 2 experiments Detail

NMR combined restraints 3 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints	combined_25082_2mrk.nef
Input source #2: Coordindates	2mrk.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	True (see coodinates for details)
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)

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
2:3:GLN:C	2:4:PTR:N	unknown	unknown	n/a
2:4:PTR:C	2:5:GLN:N	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
B	4	PTR	O-PHOSPHOTYROSINE	Assigned chemical shifts, Distance restraints, Coordinates

Sequence alignments

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

-150-----160-------170-------180-------190-------200-------210-------220-------230-------240--------
WYFGKLGRKDAERQLLSFGNPRGTFLIRESETTKGAYSLSIRDWDDMKGDHVKHYKIRKLDNGGYYITTRAQFETLQQLVQHYSERAAGLCCRLVVPCHK
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
WYFGKLGRKDAERQLLSFGNPRGTFLIRESETTKGAYSLSIRDWDDMKGDHVKHYKIRKLDNGGYYITTRAQFETLQQLVQHYSERAAGLCCRLVVPCHK
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100

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

--------10
EPQXQPGENL
||||||||||
EPQXQPGENL

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	100	0	0	100.0
B	B	10	0	0	100.0

Content subtype: combined_25082_2mrk.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	2		No information
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	53		100.0 (chain: B, length: 10)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	2996 (1)	noe	100.0 (chain: A, length: 100), 100.0 (chain: B, length: 10)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: B, Chain length: 10, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 53
- Completeness of assignments
  - Entity_assemble_ID: B
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: B

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	66	52	78.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	19	15	78.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	47	37	78.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	2	2	100.0

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

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 100, Sequence coverage: 100.0%
  - Entity_assembly_ID: B, Chain length: 10, Sequence coverage: 100.0%
- Total number of restraints: 2988
- Weight of restraints: 1.0 (2988)
- Potential type of restraints: square-well-parabolic (2988)
- Range of distance target values: 2.03, 3.99 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
  - Chain_ID: B
- Distance restraints on contact map

Keywords Fyn kinase, SH2 domain, Src kinase, phosphorylated peptide

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Found 1 Document (1.049 seconds)

BMRB: 25082

Sample

Related entities 1. Fyn SH2 domain in complex with the natural inhibitory phosphotyrosine peptide, entity 1, : 3 : 97 entities Detail

Experiments performed 2 experiments Detail

Instrument

Sample

Instrument

Sample

NMR combined restraints 3 contents Detail