BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	91.7 % (867 of 945)	91.9 % (451 of 491)	91.1 % (336 of 369)	94.1 % (80 of 85)
Backbone	94.8 % (455 of 480)	90.5 % (152 of 168)	97.9 % (229 of 234)	94.9 % (74 of 78)
Sidechain	89.9 % (483 of 537)	92.6 % (299 of 323)	86.0 % (178 of 207)	85.7 % (6 of 7)
Aromatic	56.9 % (41 of 72)	75.0 % (27 of 36)	35.3 % (12 of 34)	100.0 % (2 of 2)
Methyl	95.7 % (90 of 94)	100.0 % (47 of 47)	91.5 % (43 of 47)

1. entity 1

GSMKYLNVLA KALYDNVAES PDELSFRKGD IMTVLERDTQ GLDGWWLCSL HGRQGIVPGN RLKILVGMYD KKPAGEFIVT D

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: -0.03 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: -0.03 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: 1 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: 0.51 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 40 models in PDB: 5O2M, 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: 34142 released on 2017-09-12
    Title p130Cas SH3 domain PTP-PEST peptide chimera
  BMRB: 34143 released on 2017-09-12
    Title p130Cas SH3 domain Vinculin peptide chimera

Related entities 1. Breast cancer anti-estrogen resistance 1, : 1 : 6 : 47 entities Detail

Interaction partners 1. Breast cancer anti-estrogen resistance 1, : 17 interactors Detail

More details for 17 interactors identified by 10 citations

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_34141_5o2m.nef
Input source #2: Coordindates	5o2m.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-
GSMKYLNVLAKALYDNVAESPDELSFRKGDIMTVLERDTQGLDGWWLCSLHGRQGIVPGNRLKILVGMYDKKPAGEFIVTD
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
GSMKYLNVLAKALYDNVAESPDELSFRKGDIMTVLERDTQGLDGWWLCSLHGRQGIVPGNRLKILVGMYDKKPAGEFIVTD

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	81	0	0	100.0

Content subtype: combined_34141_5o2m.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	867		97.5 (chain: A, length: 81)
1	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	1579 (1)	noe	87.7 (chain: A, length: 81)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_2	OK	100 (100)	.	80.2 (chain: A, length: 81)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 81, Sequence coverage: 97.5%
- Total number of assignments
  - ¹³C chemical shifts: 336
  - ¹H chemical shifts: 451
  - ¹⁵N chemical shifts: 80
- 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 (%)
¹³C chemical shifts	369	336	91.1
¹H chemical shifts	491	451	91.9
¹⁵N chemical shifts	89	80	89.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	162	158	97.5
¹H chemical shifts	168	156	92.9
¹⁵N chemical shifts	78	74	94.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	207	178	86.0
¹H chemical shifts	323	295	91.3
¹⁵N chemical shifts	11	6	54.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	50	45	90.0
¹H chemical shifts	50	49	98.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	34	12	35.3
¹H chemical shifts	36	27	75.0
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: 81, Sequence coverage: 87.7%
- Total number of restraints: 1579
- Weight of restraints: 1.0 (1579)
- Potential type of restraints: square-well-parabolic (1579)
- Range of distance target values: 1.36, 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: 81, Sequence coverage: 80.2%
- Total number of restraints: 100
- Total number of restraints per polymer type: 100
- Weight of restraints: 1.0 (100)
- Potential type of restraints: square-well-parabolic (100)
- 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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Found 1 Document (3.365 seconds)

BMRB: 34141

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, : 1 : 6 : 47 entities Detail

Interaction partners 1. Breast cancer anti-estrogen resistance 1, : 17 interactors Detail

Experiments performed 5 experiments Detail

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NMR combined restraints 4 contents Detail