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Found 1 Document (3.664 seconds)

BMRB: 17016

2KZ7

solution structure of the CARMIL CAH3a/b domain bound to capping protein (CP_

Authors

Zwolak, A., Nico, T.

Assembly

CARMIL CAH3a/b domain bound to capping protein

Entity

1. CPalpha subunit (polymer, Thiol state: all free), 286 monomers, 32923.33 Da Detail

MADFEDRVSD EEKVRIAAKF ITHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNMD QFTPVKIEGY DDQVLITEHG DLGNSRFLDP RNQISFKFDH LRKEASDPQP EDVDGGLKSW RESCDSALRA YVKDHYSNGF CTVYAKTIDG QQTIIACIES HQFQPKNFWN GRWRSEWKFT ITPPSAQVVA VLKIQVHYYE DGNVQLVSHK DVQDSVTVSN EVQTAKEFIK IIESAENEYQ TAISENYQTM SDTTFKALRR QLPVTRTKID WNKILSYKIG KEMQNA

2. CPbeta subunit (polymer, Thiol state: all free), 277 monomers, 31193.95 Da Detail

MSDQQLDCAL DLMRRLPPQQ IEKNLSDLID LVPSLCEDLL SSVDQPLKIA RDKVVGKDYL LCDYNRDGDS YRSPWSNKYD PPLEDGAMPS ARLRKLEVEA NNAFDQYRDL YFEGGVSSVY LWDLDHGFAG VILIKKAGDG SKKIKGCWDS IHVVEVQEKS SGRTAHYKLT STVMLWLQTN KTGSGTMNLG GSLTRQMEKD ETVSDSSPHI ANIGRLVEDM ENKIRSTLNE IYFGKTKDIV NGLRSVQTFA DKSKQEALKN DLVEALKRKQ QCIQPDN

3. CARMIL CAH3a b domain (polymer, Thiol state: all free), 81 monomers, 9100.210 Da Detail

GAMGSWSVRQ EKRSSGLISE LPSEEGRRLE HFTKLRPKRN KKQQPTQAAV CTISILPQDG EQNGLMGRVD EGVDEFFTKK V

Total weight

73217.484 Da

Max. entity weight

32923.33 Da

Source organism

Gallus gallus , Mus musculus

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 85.9 %, Completeness: 42.0 %, Completeness (bb): 70.3 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	42.0 % (3180 of 7576)	24.9 % (988 of 3966)	57.9 % (1686 of 2910)	72.3 % (506 of 700)
Backbone	70.3 % (2684 of 3816)	47.2 % (615 of 1302)	82.7 % (1566 of 1894)	81.1 % (503 of 620)
Sidechain	22.4 % (976 of 4366)	13.9 % (371 of 2664)	37.2 % (603 of 1622)	2.5 % (2 of 80)
Aromatic	3.2 % (18 of 554)	5.8 % (16 of 277)	0.7 % (2 of 267)	0.0 % (0 of 10)
Methyl	25.4 % (165 of 650)	24.9 % (81 of 325)	25.8 % (84 of 325)

1. CPalpha subunit

2. CPbeta subunit

3. CARMIL CAH3a b domain

GAMGSWSVRQ EKRSSGLISE LPSEEGRRLE HFTKLRPKRN KKQQPTQAAV CTISILPQDG EQNGLMGRVD EGVDEFFTKK V

Show sample condition

Sample #1

Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 305 K, pH 6.5

#	Name	Isotope labeling	Concentration
1	CPalpha subunit	[U-99% 15N; U-80% 2H]	0.35 mM
2	CPbeta subunit	[U-99% 15N; U-80% 2H]	0.35 mM
3	CARMIL CAH3a/b domain	[U-2H]	0.39 mM
4	H2O	natural abundance	93 %
5	D2O	natural abundance	7 %

Sample #2

Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 305 K, pH 6.5

#	Name	Isotope labeling	Concentration
6	CARMIL CAH3a/b domain	[U-99% 15N; U-80% 2H]	0.35 mM
7	CPalpha subunit	[U-2H]	0.39 mM
8	CPbeta subunit	[U-2H]	0.39 mM
9	H2O	natural abundance	93 %
10	D2O	natural abundance	7 %

Sample #3

Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 305 K, pH 6.5

#	Name	Isotope labeling	Concentration
11	CPalpha subunit	[U-99% 15N; U-80% 2H]	0.35 mM
12	CPbeta subunit	[U-99% 15N; U-80% 2H]	0.35 mM
13	CARMIL CAH3a/b domain	[U-2H; spin labeled at 1 or 5 postions]	0.39 mM
14	H2O	natural abundance	93 %
15	D2O	natural abundance	7 %

LACS Plot; CA

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	acetate	methyl carbon	0.0 ppm	external	direct	1.0

Referencing offset: 0.51 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	acetate	methyl carbon	0.0 ppm	external	direct	1.0

Referencing offset: 0.51 ppm, Outliers: 1 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
¹³C	acetate	methyl carbon	0.0 ppm	external	direct	1.0

Referencing offset: 0.19 ppm, Outliers: 1 Detail

Release date

2010-08-11

Citation

Molecular basis for barbed end uncapping by CARMIL homology domain 3 of mouse CARMIL-1
Zwolak, A., Uruno, T., Piszczek, G., Hammer, J.A., Tjandra, N.
J. Biol. Chem. (2010), 285, 29014-29026, PubMed 20630878 , DOI 10.1074/jbc.M110.134221 , Abstract

Related entities 1. CPalpha subunit, : 3 : 83 entities Detail

Related entities 2. CPbeta subunit, : 45 entities Detail

Related entities 3. CARMIL CAH3a b domain, : 1 : 2 : 5 entities Detail

Experiments performed 3 experiments Detail

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints	combined_17016_2kz7.nef
Input source #2: Coordindates	2kz7.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	Error

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
MADFEDRVSDEEKVRIAAKFITHAPPGEFNEVFNDVRLLLNNDNLLREGAAHAFAQYNMDQFTPVKIEGYDDQVLITEHGDLGNGRFLDPRNKISFKFDH
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MADFEDRVSDEEKVRIAAKFITHAPPGEFNEVFNDVRLLLNNDNLLREGAAHAFAQYNMDQFTPVKIEGYDDQVLITEHGDLGNGRFLDPRNKISFKFDH

-------110-------120-------130-------140-------150-------160-------170-------180-------190-------200
LRKEASDPQPEDTESALKQWRDACDSALRAYVKDHYPNGFCTVYGKSIDGQQTIIACIESHQFQPKNFWNGRWRSEWKFTITPPTAQVAAVLKIQVHYYE
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LRKEASDPQPEDTESALKQWRDACDSALRAYVKDHYPNGFCTVYGKSIDGQQTIIACIESHQFQPKNFWNGRWRSEWKFTITPPTAQVAAVLKIQVHYYE

-------210-------220-------230-------240-------250-------260-------270-------280------
DGNVQLVSHKDIQDSVQVSSDVQTAKEFIKIIENAENEYQTAISENYQTMSDTTFKALRRQLPVTRTKIDWNKILSYKIGKEMQNA
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
DGNVQLVSHKDIQDSVQVSSDVQTAKEFIKIIENAENEYQTAISENYQTMSDTTFKALRRQLPVTRTKIDWNKILSYKIGKEMQNA

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

-------310-------320-------330-------340-------350-------360-------370-------380-------390-------400
MSDQQLDCALDLMRRLPPQQIEKNLSDLIDLVPSLCEDLLSSVDQPLKIARDKVVGKDYLLCDYNRDGDSYRSPWSNKYDPPLEDGAMPSARLRKLEVEA
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MSDQQLDCALDLMRRLPPQQIEKNLSDLIDLVPSLCEDLLSSVDQPLKIARDKVVGKDYLLCDYNRDGDSYRSPWSNKYDPPLEDGAMPSARLRKLEVEA
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100

-------410-------420-------430-------440-------450-------460-------470-------480-------490-------500
NNAFDQYRDLYFEGGVSSVYLWDLDHGFAGVILIKKAGDGSKKIKGCWDSIHVVEVQEKSSGRTAHYKLTSTVMLWLQTNKTGSGTMNLGGSLTRQMEKD
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
NNAFDQYRDLYFEGGVSSVYLWDLDHGFAGVILIKKAGDGSKKIKGCWDSIHVVEVQEKSSGRTAHYKLTSTVMLWLQTNKTGSGTMNLGGSLTRQMEKD
-------110-------120-------130-------140-------150-------160-------170-------180-------190-------200

-------510-------520-------530-------540-------550-------560-------570-------
ETVSDSSPHIANIGRLVEDMENKIRSTLNEIYFGKTKDIVNGLRSIDAIPDNQKYKQLQRELSQVLTQRQIYIQPDN
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
ETVSDSSPHIANIGRLVEDMENKIRSTLNEIYFGKTKDIVNGLRSIDAIPDNQKYKQLQRELSQVLTQRQIYIQPDN
-------210-------220-------230-------240-------250-------260-------270-------

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

--600-----610-------620-------630-------640-------650-------660-------670-------680--
GAMGSWGCVRQEKRSSGLISELPSEEGRRLEHFTKLRPKRNKKQQPTQAAVCTISILPQDGEQNGLMGRVDEGVDEFFTKKVTGC
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
GAMGSWGCVRQEKRSSGLISELPSEEGRRLEHFTKLRPKRNKKQQPTQAAVCTISILPQDGEQNGLMGRVDEGVDEFFTKKVTGC
--------10--------20--------30--------40--------50--------60--------70--------80-----

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Sequence coverage (%)
A	A	286	100.0
B	B	277	100.0
C	C	85	100.0

Content subtype: combined_17016_2kz7.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	chemical_shifts	Error	2452		76.9 (chain: A, length: 286), 68.2 (chain: B, length: 277), 88.2 (chain: C, length: 85)
1	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	18 (1)	pre	6.3 (chain: A, length: 286)
2	Distance restraints	CNS/XPLOR_distance_constraints_4	OK	20 (1)	pre	5.6 (chain: A, length: 286), 1.4 (chain: B, length: 277)
3	Distance restraints	CNS/XPLOR_distance_constraints_5	OK	63 (1)	pre	12.6 (chain: A, length: 286), 8.7 (chain: B, length: 277)

Assigned chemical shifts

Saveframe: chemical_shifts
- Status: Error
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 286, Sequence coverage: 76.9%
  - Entity_assembly_ID: B, Chain length: 277, Sequence coverage: 68.2%
  - Entity_assembly_ID: C, Chain length: 85, Sequence coverage: 88.2%
- Total number of assignments
  - ¹H chemical shifts: 474
  - ¹³C chemical shifts: 1504
  - ¹⁵N chemical shifts: 474
- Completeness of assignments
- Redox state of CYS
- Peptide bond of PRO
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: A
  - Chain_ID: B
  - Chain_ID: C

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_3
- Status: OK
- Experiment type: pre
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 286, Sequence coverage: 6.3%
- Total number of restraints: 18
- Weight of restraints: 1.0 (18)
- Potential type of restraints: square-well-parabolic (18)
- Range of distance target values: 11.5, 17.5 (Å)
- Histogram of distance target values
- Distance restraints per residue
  - Chain_ID: A
  - Chain_ID: B
    None
  - Chain_ID: C
- Distance restraints on contact map
- Saveframe: CNS/XPLOR_distance_constraints_4
  - Status: OK
  - Experiment type: pre
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 286, Sequence coverage: 5.6%
    - Entity_assembly_ID: B, Chain length: 277, Sequence coverage: 1.4%
  - Total number of restraints: 20
  - Weight of restraints: 1.0 (20)
  - Potential type of restraints: square-well-parabolic (20)
  - Range of distance target values: 5.5, 23.0 (Å)
  - Histogram of distance target values
  - Distance restraints per residue
    - Chain_ID: A
    - Chain_ID: B
    - Chain_ID: C
  - Distance restraints on contact map
  - Saveframe: CNS/XPLOR_distance_constraints_5
    - Status: OK
    - Experiment type: pre
    - Sequence coverage of experimental data
      - Entity_assembly_ID: A, Chain length: 286, Sequence coverage: 12.6%
      - Entity_assembly_ID: B, Chain length: 277, Sequence coverage: 8.7%
    - Total number of restraints: 63
    - Weight of restraints: 1.0 (63)
    - Potential type of restraints: square-well-parabolic (63)
    - Range of distance target values: 7.5, 18.5 (Å)
    - Histogram of distance target values
    - Distance restraints per residue
      - Chain_ID: A
      - Chain_ID: B
      - Chain_ID: C
    - Distance restraints on contact map

Keywords NMR, Paramagnetic relaxation enhancement, protein-protein complex, TROSY

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Found 1 Document (3.664 seconds)

BMRB: 17016

Sample #1

Sample #2

Sample #3

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. CPalpha subunit, : 3 : 83 entities Detail

Related entities 2. CPbeta subunit, : 45 entities Detail

Related entities 3. CARMIL CAH3a b domain, : 1 : 2 : 5 entities Detail

Interaction partners 1. CPalpha subunit, : 15 interactors Detail

Interaction partners 2. CPbeta subunit, : 2 interactors Detail

Interaction partners 3. CARMIL CAH3a b domain, : 1 interactors Detail

Experiments performed 3 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 5 contents Detail