BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	93.5 % (1042 of 1115)	93.8 % (547 of 583)	93.3 % (405 of 434)	91.8 % (90 of 98)
Backbone	92.2 % (533 of 578)	90.2 % (184 of 204)	94.0 % (266 of 283)	91.2 % (83 of 91)
Sidechain	95.0 % (591 of 622)	95.8 % (363 of 379)	93.6 % (221 of 236)	100.0 % (7 of 7)
Aromatic	85.5 % (53 of 62)	100.0 % (31 of 31)	69.0 % (20 of 29)	100.0 % (2 of 2)
Methyl	99.0 % (103 of 104)	100.0 % (52 of 52)	98.1 % (51 of 52)

1. entity 1

GSMKYLNVLA KALYDNVAES PDELSFRKGD IMTVLERDTQ GLDGWWLCSL HGRQGIVPGN RLKILVGMYD KKPAGSGGSG SGLTDELAPP KPPLPEGEV

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.5, Details 25 mM sodium phosphate, 1 M TCEP, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	entity_1	[U-13C; U-15N]	0.45 mM
2	TCEP	natural abundance	1 M
3	sodium phosphate	natural abundance	25 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: -0.07 ppm, Outliers: 2 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: -0.07 ppm, Outliers: 2 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: 2 Detail

LACS Plot; CO

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: 0.46 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 40 models in PDB: 5O2Q, Strand ID: A Detail

Release date

2017-09-12

Citation

Structural characterization of CAS SH3 domain selectivity and regulation reveals new CAS interaction partners
Gemperle, J., Hexnerova, R., Lepsik, M., Tesina, P., Dibus, M., Novotny, M., Brabek, J., Veverka, V., Rosel, D.
Sci. Rep. (2017), 7, 8057-8057, PubMed 28808245 , DOI 10.1038/s41598-017-08303-4 , Abstract

Entries sharing articles BMRB: 2 entries Detail

  BMRB: 34141 released on 2017-09-12
    Title p130Cas SH3 domain
  BMRB: 34142 released on 2017-09-12
    Title p130Cas SH3 domain PTP-PEST peptide chimera

Related entities 1. Breast cancer anti-estrogen resistance 1,Vinculin, : 19 entities Detail

Experiments performed 5 experiments Detail

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_34143_5o2q.nef
Input source #2: Coordindates	5o2q.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---------
GSMKYLNVLAKALYDNVAESPDELSFRKGDIMTVLERDTQGLDGWWLCSLHGRQGIVPGNRLKILVGMYDKKPAGSGGSGSGLTDELAPPKPPLPEGEV
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
GSMKYLNVLAKALYDNVAESPDELSFRKGDIMTVLERDTQGLDGWWLCSLHGRQGIVPGNRLKILVGMYDKKPAGSGGSGSGLTDELAPPKPPLPEGEV

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	99	0	0	100.0

Content subtype: combined_34143_5o2q.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	1021		90.9 (chain: A, length: 99)
1	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	3295 (1)	noe	89.9 (chain: A, length: 99)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_2	OK	88 (88)	.	64.6 (chain: A, length: 99)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 99, Sequence coverage: 90.9%
- Total number of assignments
  - ¹H chemical shifts: 540
  - ¹³C chemical shifts: 395
  - ¹⁵N chemical shifts: 86
- Completeness of assignments
  - Entity_assemble_ID: A
- Redox state of CYS
- 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

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
48	CYS	HG	1.705

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	583	539	92.5
¹³C chemical shifts	434	395	91.0
¹⁵N chemical shifts	102	86	84.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	204	178	87.3
¹³C chemical shifts	198	177	89.4
¹⁵N chemical shifts	91	78	85.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	379	361	95.3
¹³C chemical shifts	236	218	92.4
¹⁵N chemical shifts	11	8	72.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	55	54	98.2
¹³C chemical shifts	55	52	94.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	31	31	100.0
¹³C chemical shifts	29	20	69.0
¹⁵N chemical shifts	2	2	100.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_3
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 99, Sequence coverage: 89.9%
- Total number of restraints: 3295
- Weight of restraints: 1.0 (3295)
- Potential type of restraints: square-well-parabolic (3295)
- Range of distance target values: 1.17, 2.75 (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: CNS/XPLOR_dihedral_2
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 99, Sequence coverage: 64.6%
- Total number of restraints: 88
- Total number of restraints per polymer type: 88
- Weight of restraints: 1.0 (88)
- Potential type of restraints: square-well-parabolic (88)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords SH3 domain, STRUCTURE FROM CYANA 3.97, p130Cas

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BMRB: 34143

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Entries sharing articles BMRB: 2 entries Detail

Related entities 1. Breast cancer anti-estrogen resistance 1,Vinculin, : 19 entities Detail

Experiments performed 5 experiments Detail

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NMR combined restraints 4 contents Detail