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Found 1 Document (0.636 seconds)

BMRB: 15020

2IFS

Structure of the N-WASP EVH1 domain in complex with an extended WIP peptide

Authors

Volkman, B.F., Peterson, F.C., Deng, Q.

Assembly

exWIP-EVH1

Entity

1. exWIP-EVH1 (polymer, Thiol state: all free), 169 monomers, 19296.73 Da Detail

GSESRFYFHP ISDLPPPEPY VQTTKSYPSK LARNESRGGL VPRGSGGSLF SFLGKKCVTM SSAVVQLYAA DRNCMWSKKC SGVACLVKDN PQRSYFLRIF DIKDGKLLWE QELYNNFVYN SPRGYFHTFA GDTCQVALNF ANEEEAKKFR KAVTDLLGRR QRKSEKRRD

Formula weight

19296.73 Da

Source organism

Homo sapiens , Rattus norvegicus

Exptl. method

solution NMR

Refine. method

AUTOMATED METHODS WERE USED FOR BACKBONE CHEMICAL SHIFT ASSIGNMENT AND ITERATIVE NOE REFINEMENT.

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 85.2 %, Completeness: 76.0 %, Completeness (bb): 79.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	76.0 % (1535 of 2019)	75.3 % (800 of 1063)	76.0 % (593 of 780)	80.7 % (142 of 176)
Backbone	79.2 % (789 of 996)	78.0 % (266 of 341)	79.8 % (395 of 495)	80.0 % (128 of 160)
Sidechain	74.0 % (873 of 1180)	74.0 % (534 of 722)	73.5 % (325 of 442)	87.5 % (14 of 16)
Aromatic	70.9 % (146 of 206)	87.4 % (90 of 103)	53.5 % (54 of 101)	100.0 % (2 of 2)
Methyl	88.6 % (124 of 140)	87.1 % (61 of 70)	90.0 % (63 of 70)

1. WIP-EVH1 polypeptide

GSESRFYFHP ISDLPPPEPY VQTTKSYPSK LARNESRGGL VPRGSGGSLF SFLGKKCVTM SSAVVQLYAA DRNCMWSKKC SGVACLVKDN PQRSYFLRIF DIKDGKLLWE QELYNNFVYN SPRGYFHTFA GDTCQVALNF ANEEEAKKFR KAVTDLLGRR QRKSEKRRD

Show sample condition

Sample

Solvent system 90% H2O, 10% D2O, Pressure 1 atm, Temperature 303 K, pH 7.0, Details 1.0 mM U-15N/13C protein, 20 mM sodium phosphate, 1 mM Dithiothreitol, 90% H2O, 10% D2O

#	Name	Isotope labeling	Concentration
1	WIP-EVH1 polypeptide	[U-99% 13C; U-99% 15N]	1.0 mM
2	sodium phosphate	none	20 mM
3	Dithiothreitol	none	1 mM
4	H2O	none	90 mM
5	D2O	none	10 mM

LACS Plot; CA

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

Referencing offset: -0.33 ppm, Outliers: 2 Detail

LACS Plot; CB

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

Referencing offset: -0.33 ppm, Outliers: 2 Detail

LACS Plot; HA

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

Referencing offset: 0.18 ppm, Outliers: 2 Detail

Protein Blocks Logo

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

Release date

2007-05-03

Citation

Multiple WASP-interacting protein recognition motifs are required for a functional interaction with N-WASP
Peterson, F.C., Deng, Q., Zettl, M., Prehoda, K.E., Lim, W.A., Way, M., Volkman, B.F.
J. Biol. Chem. (2007), 282, 8446-8453, PubMed 17229736 , DOI 10.1074/jbc.M609902200 , Abstract

Related entities 1. exWIP-EVH1, : 1 : 1 entities Detail

Experiments performed 3 experiments Detail

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_15020_2ifs.nef
Input source #2: Coordindates	2ifs.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

-450-----460-------470-------480-------520-------530-------540-------550-------560-------570-------5
GSESRFYFHPISDLPPPEPYVQTTKSYPSKLARNESRGGLVPRGSGGSLFSFLGKKCVTMSSAVVQLYAADRNCMWSKKCSGVACLVKDNPQRSYFLRIF
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
GSESRFYFHPISDLPPPEPYVQTTKSYPSKLARNESRGGLVPRGSGGSLFSFLGKKCVTMSSAVVQLYAADRNCMWSKKCSGVACLVKDNPQRSYFLRIF
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100

80-------590-------600-------610-------620-------630-------640-------
DIKDGKLLWEQELYNNFVYNSPRGYFHTFAGDTCQVALNFANEEEAKKFRKAVTDLLGRRQRKSEKRRD
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
DIKDGKLLWEQELYNNFVYNSPRGYFHTFAGDTCQVALNFANEEEAKKFRKAVTDLLGRRQRKSEKRRD
-------110-------120-------130-------140-------150-------160---------

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	169	0	0	100.0

Content subtype: combined_15020_2ifs.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1507		82.2 (chain: A, length: 169)
1	Distance restraints	DYANA/DIANA_distance_constraints_3	Warning	3259 (1)	noe	77.5 (chain: A, length: 169)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_2	OK	190 (190)	.	74.0 (chain: A, length: 169)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 169, Sequence coverage: 82.2%
- Total number of assignments
  - ¹³C chemical shifts: 578
  - ¹H chemical shifts: 790
  - ¹⁵N chemical shifts: 139
- 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)
597	TYR	HH	12.754
605	HIS	NE2	163.313
606	THR	HG1	5.78

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	780	578	74.1
¹H chemical shifts	1063	788	74.1
¹⁵N chemical shifts	190	138	72.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	338	259	76.6
¹H chemical shifts	341	261	76.5
¹⁵N chemical shifts	160	123	76.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	442	319	72.2
¹H chemical shifts	722	527	73.0
¹⁵N chemical shifts	30	15	50.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	72	64	88.9
¹H chemical shifts	72	64	88.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	101	51	50.5
¹H chemical shifts	103	89	86.4
¹⁵N chemical shifts	2	2	100.0

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_3
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 169, Sequence coverage: 77.5%
- Total number of restraints: 3250
- Weight of restraints: 1.0 (3250)
- Potential type of restraints: upper-bound-parabolic (3250)
- Range of distance target values: 2.69, 11.2 (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_2
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 169, Sequence coverage: 74.0%
- Total number of restraints: 190
- Total number of restraints per polymer type: 190
- Weight of restraints: 1.0 (190)
- Potential type of restraints: square-well-parabolic (190)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords NMR, Polyproline, protein-protein complex, verprolin, Wiskott-Aldrich syndrome

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Found 1 Document (0.636 seconds)

BMRB: 15020

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. exWIP-EVH1, : 1 : 1 entities Detail

Experiments performed 3 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 4 contents Detail