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Found 1 Document (1.479 seconds)

BMRB: 4388

4N9I

Backbone NMR Assignments of a High Molecular Weight Protein (47kD), Cyclic AMP Receptor Protein (apo-CRP)

Authors

Won, H., Yamazaki, T., Lee, T., Jee, J., Yoon, M., Park, S., Otomo, T., Aiba, H., Kyogoku, Y., Lee, B.

Assembly

Cyclic AMP Receptor Protein dimer

Entity

1. Cyclic AMP Receptor Protein dimer (polymer), 209 monomers, 23508.95 × 2 Da Detail

VLGKPQTDPT LEWFLSHCHI HKYPSKSTLI HQGEKAETLY YIVKGSVAVL IKDEEGKEMI LSYLNQGDFI GELGLFEEGQ ERSAWVRAKT ACEVAEISYK KFRQLIQVNP DILMRLSAQM ARRLQVTSEK VGNLAFLDVT GRIAQTLLNL AKQPDAMTHP DGMQIKITRQ EIGQIVGCSR ETVGRILKML EDQNLISAHG KTIVVYGTR

Total weight

47017.9 Da

Max. entity weight

23508.95 Da

Source organism

Escherichia coli

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 97.6 %, Completeness: 44.4 %, Completeness (bb): 80.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	44.4 % (1099 of 2475)	23.3 % (300 of 1290)	62.9 % (604 of 961)	87.1 % (195 of 224)
Backbone	80.5 % (1000 of 1242)	51.6 % (221 of 428)	95.7 % (585 of 611)	95.6 % (194 of 203)
Sidechain	20.2 % (288 of 1426)	9.3 % (80 of 862)	38.1 % (207 of 543)	4.8 % (1 of 21)
Aromatic	0.0 % (0 of 146)	0.0 % (0 of 73)	0.0 % (0 of 71)	0.0 % (0 of 2)
Methyl	15.2 % (40 of 264)	12.9 % (17 of 132)	17.4 % (23 of 132)

1. Cyclic AMP Receptor Protein

Show sample condition

Sample

Temperature 313 (±0.5) K

#	Name	Isotope labeling	Type	Concentration
1	Cyclic AMP Receptor Protein	[U-90% 2H; U-95% 13C; U-95% 15N]		0.6 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
²H	DSS	methyl protons	null	indirect	0.1535061
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: 0.25 ppm, Outliers: 1 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
²H	DSS	methyl protons	null	indirect	0.1535061
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: 0.25 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
²H	DSS	methyl protons	null	indirect	0.1535061
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: 0.04 ppm, Outliers: 1 Detail

Release date

2000-03-19

Citation 1

Letter to the Editor: Backbone NMR assignments of a high molecular weight protein (47 kDa), cyclic AMP receptor protein (apo-CRP)
Won, H., Yamazaki, T., Lee, T., Jee, J., Yoon, M., Park, S., Otomo, T., Aiba, H., Kyogoku, Y., Lee, B.
J. Biomol. NMR (2000), 16, 79-80

Show more 1 citaion

Citation 2

NMRPipe: a multidimensional spectral processing system based on UNIX pipes
Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., Bax, A.
J. Biomol. NMR (1995), 6, 277-293, PubMed 8520220 , Abstract

Hide non-primary 1 citaion

Related entities 1. Cyclic AMP Receptor Protein dimer, : 1 : 29 : 3 : 18 : 89 entities Detail

Experiments performed 7 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4388_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: bmr4388_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	shift_set_1	Warning	961		97.1 (chain: 1, length: 209)
1	Chemical shift references	chemical_shift_reference	OK	4		No information

Assigned chemical shifts

Saveframe: shift_set_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 209, Sequence coverage: 97.1%
- Total number of assignments
  - ¹³C chemical shifts: 579
  - ¹H chemical shifts: 191
  - ¹⁵N chemical shifts: 191
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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: 1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	961	579	60.2
¹H chemical shifts	1290	191	14.8
¹⁵N chemical shifts	235	191	81.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	418	393	94.0
¹H chemical shifts	428	191	44.6
¹⁵N chemical shifts	203	191	94.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	543	186	34.3
¹H chemical shifts	862	0	0.0
¹⁵N chemical shifts	32	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	138	13	9.4
¹H chemical shifts	138	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	71	0	0.0
¹H chemical shifts	73	0	0.0
¹⁵N chemical shifts	2	0	0.0

Keywords apo-CRP, backbone NMR assignments

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Found 1 Document (1.479 seconds)

BMRB: 4388

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Cyclic AMP Receptor Protein dimer, : 1 : 29 : 3 : 18 : 89 entities Detail

Experiments performed 7 experiments Detail

Instrument

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Chemical shift validation 3 contents Detail