BMRBj - BMREntryMaster

Found 1 Document (1.335 seconds)

BMRB: 5514

1GFL

Backbone HN, N, Ca and Cb assignment of the GFPuv mutant, an 54 kDa protein

Authors

Georgescu, J., Rehm, T., Wiehler, J., Steipe, B., Holak, T.A.

Assembly

GFPuv

Entity

1. GFPuv (polymer, Thiol state: all free), 239 monomers, 26822.83 × 2 Da Detail

MGKGEELFTG VVPILVELDG DVNGHKFSVS GEGEGDATYG KLTLKFICTT GKLPVPWPTL VTTFSYGVQC FSRYPDHMKR HDFFKSAMPE GYVQERTISF KDDGNYKTRA EVKFEGDTLV NRIELKGIDF KEDGNILGHK LEYNYNSHNV YITADKQKNG IKANFKIRHN IEDGSVQLAD HYQQNTPIGD GPVLLPDNHY LSTQSALSKD PNEKRDHMVL LEFVTAAGIT HGMDELYKG

Total weight

53645.66 Da

Max. entity weight

26822.83 Da

Source organism

Aequorea victoria

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 89.1 %, Completeness: 43.0 %, Completeness (bb): 76.0 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	43.0 % (1198 of 2788)	29.9 % (433 of 1448)	52.8 % (575 of 1090)	76.0 % (190 of 250)
Backbone	76.0 % (1075 of 1414)	68.5 % (337 of 492)	79.2 % (549 of 693)	82.5 % (189 of 229)
Sidechain	17.1 % (271 of 1589)	10.0 % (96 of 956)	28.4 % (174 of 612)	4.8 % (1 of 21)
Aromatic	3.8 % (10 of 260)	3.8 % (5 of 130)	3.9 % (5 of 129)	0.0 % (0 of 1)
Methyl	9.7 % (23 of 238)	7.6 % (9 of 119)	11.8 % (14 of 119)

1. green fluorescent protein uv

Show sample condition

Sample #1

Temperature 310 (±0.5) K, pH 7.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	green fluorescent protein uv	[U-15N]		0.8 ~ 1.5 mM

Sample #2

Temperature 310 (±0.5) K, pH 7.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
2	green fluorescent protein uv	[U-15N; U-13C; U-70% 2H]		0.8 ~ 1.5 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹H	DSS	methyl protons	internal	direct	1.0
¹³C	TMS	methyl protons	external	indirect	0.0
¹⁵N	ammonia	nitrogen	internal	indirect	0.0

Referencing offset: 3.71 ppm, Outliers: 2 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹H	DSS	methyl protons	internal	direct	1.0
¹³C	TMS	methyl protons	external	indirect	0.0
¹⁵N	ammonia	nitrogen	internal	indirect	0.0

Referencing offset: 3.71 ppm, Outliers: 2 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹H	DSS	methyl protons	internal	direct	1.0
¹³C	TMS	methyl protons	external	indirect	0.0
¹⁵N	ammonia	nitrogen	internal	indirect	0.0

Referencing offset: -0.1 ppm, Outliers: 1 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹H	DSS	methyl protons	internal	direct	1.0
¹³C	TMS	methyl protons	external	indirect	0.0
¹⁵N	ammonia	nitrogen	internal	indirect	0.0

Referencing offset: 5.41 ppm, Outliers: 2 Detail

Release date

2003-02-17

Citation

Letter to the editor: Backbone HN, N, Ca and Cb assignment of the GFPuv mutant
Georgescu, J., Rehm, T., Wiehler, J., Steipe, B., Holak, T.A.
J. Biomol. NMR (2003), 25, 161-162

Related entities 1. GFPuv, : 1 : 1 : 104 entities Detail

Interaction partners 1. GFPuv, : 1 interactors Detail

More details for 1 interactors identified by 1 citations

Experiments performed 6 experiments Detail

1 1H-15N NOESY HSQC

Instrument

#1 Model Bruker DRX (600 MHz)

#2 Model Bruker DMX (750 MHz)

Sample #1

Temperature 310 (±0.5) K, pH 7.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	green fluorescent protein uv	[U-15N]		0.8 ~ 1.5 mM

Sample #2

Temperature 310 (±0.5) K, pH 7.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
2	green fluorescent protein uv	[U-15N; U-13C; U-70% 2H]		0.8 ~ 1.5 mM

2 2D-TOCSY

Instrument

#1 Model Bruker DRX (600 MHz)

#2 Model Bruker DMX (750 MHz)

Sample #1

Temperature 310 (±0.5) K, pH 7.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	green fluorescent protein uv	[U-15N]		0.8 ~ 1.5 mM

Sample #2

Temperature 310 (±0.5) K, pH 7.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
2	green fluorescent protein uv	[U-15N; U-13C; U-70% 2H]		0.8 ~ 1.5 mM

3 2D NOESY in D2O

Instrument

#1 Model Bruker DRX (600 MHz)

#2 Model Bruker DMX (750 MHz)

Sample #1

Temperature 310 (±0.5) K, pH 7.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	green fluorescent protein uv	[U-15N]		0.8 ~ 1.5 mM

Sample #2

Temperature 310 (±0.5) K, pH 7.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
2	green fluorescent protein uv	[U-15N; U-13C; U-70% 2H]		0.8 ~ 1.5 mM

4 HNCA

Instrument

#1 Model Bruker DRX (600 MHz)

#2 Model Bruker DMX (750 MHz)

Sample #1

Temperature 310 (±0.5) K, pH 7.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	green fluorescent protein uv	[U-15N]		0.8 ~ 1.5 mM

Sample #2

Temperature 310 (±0.5) K, pH 7.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
2	green fluorescent protein uv	[U-15N; U-13C; U-70% 2H]		0.8 ~ 1.5 mM

5 HNCO

Instrument

#1 Model Bruker DRX (600 MHz)

#2 Model Bruker DMX (750 MHz)

Sample #1

Temperature 310 (±0.5) K, pH 7.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	green fluorescent protein uv	[U-15N]		0.8 ~ 1.5 mM

Sample #2

Temperature 310 (±0.5) K, pH 7.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
2	green fluorescent protein uv	[U-15N; U-13C; U-70% 2H]		0.8 ~ 1.5 mM

6 CBCACONH

Instrument

#1 Model Bruker DRX (600 MHz)

#2 Model Bruker DMX (750 MHz)

Sample #1

Temperature 310 (±0.5) K, pH 7.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	green fluorescent protein uv	[U-15N]		0.8 ~ 1.5 mM

Sample #2

Temperature 310 (±0.5) K, pH 7.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
2	green fluorescent protein uv	[U-15N; U-13C; U-70% 2H]		0.8 ~ 1.5 mM

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr5514_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: bmr5514_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	shift_set_1	Warning	1039		87.4 (chain: 1, length: 239)
1	Chemical shift references	chemical_shift_reference	OK	1		No information

Assigned chemical shifts

Saveframe: shift_set_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 239, Sequence coverage: 87.4%
- Total number of assignments
  - ¹³C chemical shifts: 536
  - ¹H chemical shifts: 319
  - ¹⁵N chemical shifts: 184
- 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	1090	536	49.2
¹H chemical shifts	1448	319	22.0
¹⁵N chemical shifts	257	184	71.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	478	393	82.2
¹H chemical shifts	492	319	64.8
¹⁵N chemical shifts	229	184	80.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	612	143	23.4
¹H chemical shifts	956	0	0.0
¹⁵N chemical shifts	28	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	124	9	7.3
¹H chemical shifts	124	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	129	0	0.0
¹H chemical shifts	130	0	0.0
¹⁵N chemical shifts	1	0	0.0

Keywords green fluorescent protein, deuteration, chromophore

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Found 1 Document (1.335 seconds)

BMRB: 5514

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Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. GFPuv, : 1 : 1 : 104 entities Detail

Interaction partners 1. GFPuv, : 1 interactors Detail

Experiments performed 6 experiments Detail

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Chemical shift validation 3 contents Detail