BMRBj - BMREntryMaster

Found 1 Document (1.254 seconds)

BMRB: 4107

2L15

Acid Denatured Cold Shock Protein A (CspA)

Authors

Alexandrescu, A.T., Rathgeb-Szabo, K.

Assembly

CspA

Entity

1. CspA (polymer), 70 monomers, 7403.187 Da Detail

MSGKMTGIVK WFNADKGFGF ITPDDGSKDV FVHFSAIQND GYKSLDEGQK VSFTIESGAK GPAAGNVTSL

Formula weight

7403.187 Da

Source organism

Escherichia coli

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 97.1 %, Completeness: 53.2 %, Completeness (bb): 78.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	53.2 % (416 of 782)	55.2 % (222 of 402)	41.8 % (128 of 306)	89.2 % (66 of 74)
Backbone	78.1 % (325 of 416)	89.2 % (132 of 148)	63.5 % (127 of 200)	97.1 % (66 of 68)
Sidechain	34.7 % (148 of 426)	35.4 % (90 of 254)	34.9 % (58 of 166)	0.0 % (0 of 6)
Aromatic	0.0 % (0 of 84)	0.0 % (0 of 42)	0.0 % (0 of 41)	0.0 % (0 of 1)
Methyl	46.8 % (29 of 62)	74.2 % (23 of 31)	19.4 % (6 of 31)

1. Cold shock protein A

MSGKMTGIVK WFNADKGFGF ITPDDGSKDV FVHFSAIQND GYKSLDEGQK VSFTIESGAK GPAAGNVTSL

Show sample condition

Sample #1

Temperature 293 (±1) K, pH 2.0 (±0.2)

#	Name	Isotope labeling	Type	Concentration
1	Cold shock protein A	[U-15N]		1 mM

Sample #2

Temperature 293 (±1) K, pH 2.0 (±0.2)

#	Name	Isotope labeling	Type	Concentration
2	Cold shock protein A	[U-15N;U-13C]		2 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl	external	indirect	0.2514495
¹H	DSS	methyl	internal	direct	0.0
¹⁵N	DSS	methyl	external	indirect	0.1013291

Referencing offset: -0.05 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl	external	indirect	0.2514495
¹H	DSS	methyl	internal	direct	0.0
¹⁵N	DSS	methyl	external	indirect	0.1013291

Referencing offset: -0.05 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl	external	indirect	0.2514495
¹H	DSS	methyl	internal	direct	0.0
¹⁵N	DSS	methyl	external	indirect	0.1013291

Referencing offset: 0.09 ppm, Outliers: 1 Detail

Release date

1998-03-03

Citation 1

NMR assignments for acid-denatured cold shock protein A
Alexandrescu, A.T., Rathgeb-Szabo, K.
J. Biomol. NMR (1998), 11, 461-462, PubMed 9691289 , Abstract

Show more 1 citaion

Citation 2

1H, 13C and 15N chemical shift referencing in biomolecular NMR
Wishart, D.S., Bigam, C.G., Yao, J., Abildgaard, F., Dyson, H.J., Oldfield, E., Markley, J.L., Sykes, B.D.
J. Biomol. NMR (1995), 6, 135-140, PubMed 8589602 , DOI: , Abstract

Hide non-primary 1 citaion

Related entities 1. CspA, : 1 : 2 : 3 : 203 entities Detail

Interaction partners 1. CspA, : 11 interactors Detail

More details for 11 interactors identified by 4 citations

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4107_3.str
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

Content subtype: bmr4107_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	chemical_shift_assignment_one	Warning	460		97.1 (chain: 1, length: 70)
1	Chemical shift references	chemical_shift_reference_one	Warning	3		No information

Assigned chemical shifts

Saveframe: chemical_shift_assignment_one
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 70, Sequence coverage: 97.1%
- Total number of assignments
  - ¹³C chemical shifts: 124
  - ¹H chemical shifts: 270
  - ¹⁵N chemical shifts: 66
- Completeness of assignments
  - Entity_assemble_ID: 1
- Peptide bond of PRO
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	306	124	40.5
¹H chemical shifts	402	222	55.2
¹⁵N chemical shifts	74	66	89.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	140	67	47.9
¹H chemical shifts	148	133	89.9
¹⁵N chemical shifts	68	66	97.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	166	57	34.3
¹H chemical shifts	254	89	35.0
¹⁵N chemical shifts	6	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	33	5	15.2
¹H chemical shifts	33	24	72.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	41	0	0.0
¹H chemical shifts	42	0	0.0
¹⁵N chemical shifts	1	0	0.0

Keywords aggregation, CspA, fibril formation, protein folding

Search

Query history

Resources

Search for primary databases

Search for subsidiary databases

Display

Hits per page

Statistics

Query Changes will take effect after "OK" button is selected.

Maximum hits

Default conjunction operator

Omni-box

Search filter

Sequence search (BLAST)

E-value

Query sequence coverage

Miscellaneous

The number of previewed publications

Completeness of assigned chemical shift

Sequence chart about top aligned regions

Sequence chart about interacting regions

Hit context with highlight

Link destinations for BMRB, PDB and EMDB

Found 1 Document (1.254 seconds)

BMRB: 4107

Sample #1

Sample #2

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. CspA, : 1 : 2 : 3 : 203 entities Detail

Interaction partners 1. CspA, : 11 interactors Detail

Chemical shift validation 3 contents Detail