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BMRB: 17429

2L8V

Solution NMR structure of the phycobilisome linker polypeptide domain of CpcC (20-153) from Thermosynechococcus elongatus, Northeast Structural Genomics Consortium Target TeR219A

Authors

Ramelot, T.A., Yang, Y., Cort, J.R., Lee, D., Ciccosanti, C., Hamilton, K., Acton, T.B., Xiao, R., Everett, J.K., Montelione, G.T., Kennedy, M.A.

Assembly

CpcC

Entity

1. CpcC (polymer, Thiol state: not present), 143 monomers, 16883.60 Da Detail

MPVELRANWS EEDLETVIRA VYRQVLGNDY VMASERLVSA ESLLRNGKIT VREFVRAVAK SELYKEKFLY GNFQTRVIEL NYKHLLGRAP YDESEVIFHL DLYENEGFDA DIDSYIDSPE YTNSFGDWVV PYYRGLEHHH HHH

Formula weight

16883.6 Da

Source organism

Thermosynechococcus elongatus

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 88.1 %, Completeness: 78.7 %, Completeness (bb): 80.0 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	78.7 % (1347 of 1711)	79.0 % (698 of 884)	78.7 % (533 of 677)	77.3 % (116 of 150)
Backbone	80.0 % (680 of 850)	81.3 % (235 of 289)	79.9 % (337 of 422)	77.7 % (108 of 139)
Sidechain	78.2 % (780 of 997)	77.8 % (463 of 595)	79.0 % (309 of 391)	72.7 % (8 of 11)
Aromatic	65.2 % (133 of 204)	66.7 % (68 of 102)	63.0 % (63 of 100)	100.0 % (2 of 2)
Methyl	96.2 % (150 of 156)	96.2 % (75 of 78)	96.2 % (75 of 78)

1. CpcC

MPVELRANWS EEDLETVIRA VYRQVLGNDY VMASERLVSA ESLLRNGKIT VREFVRAVAK SELYKEKFLY GNFQTRVIEL NYKHLLGRAP YDESEVIFHL DLYENEGFDA DIDSYIDSPE YTNSFGDWVV PYYRGLEHHH HHH

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 (±1) K, pH 7.5 (±0.1)

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N]	1.3 (±0.1) mM
2	Tris-HCl	natural abundance	10 (±1.0) mM
3	sodium chloride	natural abundance	100 (±5.0) mM
4	calcium chloride	natural abundance	5 (±0.25) mM
5	sodium azide	natural abundance	0.02 (±0.001) %
6	DTT	natural abundance	5 (±0.5) mM

Sample #2

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 (±1) K, pH 7.5 (±0.1)

#	Name	Isotope labeling	Concentration
7	protein	[U-5% 13C; U-100% 15N]	1.3 (±0.1) mM
8	Tris-HCl	natural abundance	10 (±1.0) mM
9	sodium chloride	natural abundance	100 (±5.0) mM
10	calcium chloride	natural abundance	5 (±0.25) mM
11	DTT	natural abundance	5 (±0.5) mM
12	sodium azide	natural abundance	0.02 (±0.001) %

Sample #3

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 (±1) K, pH 7.5 (±0.1)

#	Name	Isotope labeling	Concentration
13	protein	[U-100% 13C; U-100% 15N]	1.3 (±0.1) mM
14	Tris-HCl	natural abundance	10 (±1.0) mM
15	sodium chloride	natural abundance	100 (±5.0) mM
16	calcium chloride	natural abundance	5 (±0.25) mM
17	sodium azide	natural abundance	0.02 (±0.001) %
18	DTT	natural abundance	10 (±0.5) 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: -0.48 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
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: -0.48 ppm, Outliers: 1 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: 4 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: -0.66 ppm, Outliers: 4 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2L8V, Strand ID: A Detail

Release date

2011-02-10

Citation

Solution NMR structure of the phycobilisome linker polypeptide domain of CpcC (20-153) from Thermosynechococcus elongatus, Northeast Structural Genomics Consortium Target TeR219A
Ramelot, T.A., Yang, Y., Cort, J.R., Lee, D., Ciccosanti, C., Hamilton, K., Acton, T.B., Xiao, R., Everett, J.K., Montelione, G.T., Kennedy, M.A.
Not known

Related entities 1. CpcC, : 1 : 2 : 113 entities Detail

Experiments performed 23 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker Avance III - 850 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 (±1) K, pH 7.5 (±0.1)

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N]	1.3 (±0.1) mM
2	Tris-HCl	natural abundance	10 (±1.0) mM
3	sodium chloride	natural abundance	100 (±5.0) mM
4	calcium chloride	natural abundance	5 (±0.25) mM
5	sodium azide	natural abundance	0.02 (±0.001) %
6	DTT	natural abundance	5 (±0.5) mM

2 2D 1H-13C HSQC aliphatic

Instrument

Bruker Avance III - 850 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 (±1) K, pH 7.5 (±0.1)

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N]	1.3 (±0.1) mM
2	Tris-HCl	natural abundance	10 (±1.0) mM
3	sodium chloride	natural abundance	100 (±5.0) mM
4	calcium chloride	natural abundance	5 (±0.25) mM
5	sodium azide	natural abundance	0.02 (±0.001) %
6	DTT	natural abundance	5 (±0.5) mM

3 2D 1H-13C HSQC aromatic

Instrument

Bruker Avance III - 850 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 (±1) K, pH 7.5 (±0.1)

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N]	1.3 (±0.1) mM
2	Tris-HCl	natural abundance	10 (±1.0) mM
3	sodium chloride	natural abundance	100 (±5.0) mM
4	calcium chloride	natural abundance	5 (±0.25) mM
5	sodium azide	natural abundance	0.02 (±0.001) %
6	DTT	natural abundance	5 (±0.5) mM

4 2D 1H-15N HSQC

Instrument

Bruker Avance III - 850 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 (±1) K, pH 7.5 (±0.1)

#	Name	Isotope labeling	Concentration
13	protein	[U-100% 13C; U-100% 15N]	1.3 (±0.1) mM
14	Tris-HCl	natural abundance	10 (±1.0) mM
15	sodium chloride	natural abundance	100 (±5.0) mM
16	calcium chloride	natural abundance	5 (±0.25) mM
17	sodium azide	natural abundance	0.02 (±0.001) %
18	DTT	natural abundance	10 (±0.5) mM

5 2D 1H-13C HSQC-CT

Instrument

Bruker Avance III - 850 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 (±1) K, pH 7.5 (±0.1)

#	Name	Isotope labeling	Concentration
7	protein	[U-5% 13C; U-100% 15N]	1.3 (±0.1) mM
8	Tris-HCl	natural abundance	10 (±1.0) mM
9	sodium chloride	natural abundance	100 (±5.0) mM
10	calcium chloride	natural abundance	5 (±0.25) mM
11	DTT	natural abundance	5 (±0.5) mM
12	sodium azide	natural abundance	0.02 (±0.001) %

6 3D 1H-15N NOESY

Instrument

Bruker Avance III - 850 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 (±1) K, pH 7.5 (±0.1)

#	Name	Isotope labeling	Concentration
7	protein	[U-5% 13C; U-100% 15N]	1.3 (±0.1) mM
8	Tris-HCl	natural abundance	10 (±1.0) mM
9	sodium chloride	natural abundance	100 (±5.0) mM
10	calcium chloride	natural abundance	5 (±0.25) mM
11	DTT	natural abundance	5 (±0.5) mM
12	sodium azide	natural abundance	0.02 (±0.001) %

7 3D 1H-13C NOESY-aliph

Instrument

Bruker Avance III - 850 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 (±1) K, pH 7.5 (±0.1)

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N]	1.3 (±0.1) mM
2	Tris-HCl	natural abundance	10 (±1.0) mM
3	sodium chloride	natural abundance	100 (±5.0) mM
4	calcium chloride	natural abundance	5 (±0.25) mM
5	sodium azide	natural abundance	0.02 (±0.001) %
6	DTT	natural abundance	5 (±0.5) mM

8 3D HNCO

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 (±1) K, pH 7.5 (±0.1)

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N]	1.3 (±0.1) mM
2	Tris-HCl	natural abundance	10 (±1.0) mM
3	sodium chloride	natural abundance	100 (±5.0) mM
4	calcium chloride	natural abundance	5 (±0.25) mM
5	sodium azide	natural abundance	0.02 (±0.001) %
6	DTT	natural abundance	5 (±0.5) mM

9 3D HNCACB

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 (±1) K, pH 7.5 (±0.1)

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N]	1.3 (±0.1) mM
2	Tris-HCl	natural abundance	10 (±1.0) mM
3	sodium chloride	natural abundance	100 (±5.0) mM
4	calcium chloride	natural abundance	5 (±0.25) mM
5	sodium azide	natural abundance	0.02 (±0.001) %
6	DTT	natural abundance	5 (±0.5) mM

10 3D CBCA(CO)NH

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 (±1) K, pH 7.5 (±0.1)

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N]	1.3 (±0.1) mM
2	Tris-HCl	natural abundance	10 (±1.0) mM
3	sodium chloride	natural abundance	100 (±5.0) mM
4	calcium chloride	natural abundance	5 (±0.25) mM
5	sodium azide	natural abundance	0.02 (±0.001) %
6	DTT	natural abundance	5 (±0.5) mM

11 3D HN(CO)CA

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 (±1) K, pH 7.5 (±0.1)

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N]	1.3 (±0.1) mM
2	Tris-HCl	natural abundance	10 (±1.0) mM
3	sodium chloride	natural abundance	100 (±5.0) mM
4	calcium chloride	natural abundance	5 (±0.25) mM
5	sodium azide	natural abundance	0.02 (±0.001) %
6	DTT	natural abundance	5 (±0.5) mM

12 3D HBHA(CO)NH

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 (±1) K, pH 7.5 (±0.1)

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N]	1.3 (±0.1) mM
2	Tris-HCl	natural abundance	10 (±1.0) mM
3	sodium chloride	natural abundance	100 (±5.0) mM
4	calcium chloride	natural abundance	5 (±0.25) mM
5	sodium azide	natural abundance	0.02 (±0.001) %
6	DTT	natural abundance	5 (±0.5) mM

13 3D H(CCO)NH

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 (±1) K, pH 7.5 (±0.1)

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N]	1.3 (±0.1) mM
2	Tris-HCl	natural abundance	10 (±1.0) mM
3	sodium chloride	natural abundance	100 (±5.0) mM
4	calcium chloride	natural abundance	5 (±0.25) mM
5	sodium azide	natural abundance	0.02 (±0.001) %
6	DTT	natural abundance	5 (±0.5) mM

14 3D C(CCO)NH

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 (±1) K, pH 7.5 (±0.1)

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N]	1.3 (±0.1) mM
2	Tris-HCl	natural abundance	10 (±1.0) mM
3	sodium chloride	natural abundance	100 (±5.0) mM
4	calcium chloride	natural abundance	5 (±0.25) mM
5	sodium azide	natural abundance	0.02 (±0.001) %
6	DTT	natural abundance	5 (±0.5) mM

15 3D HCCH-COSY

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 (±1) K, pH 7.5 (±0.1)

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N]	1.3 (±0.1) mM
2	Tris-HCl	natural abundance	10 (±1.0) mM
3	sodium chloride	natural abundance	100 (±5.0) mM
4	calcium chloride	natural abundance	5 (±0.25) mM
5	sodium azide	natural abundance	0.02 (±0.001) %
6	DTT	natural abundance	5 (±0.5) mM

16 3D HCCH-TOCSY

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 (±1) K, pH 7.5 (±0.1)

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N]	1.3 (±0.1) mM
2	Tris-HCl	natural abundance	10 (±1.0) mM
3	sodium chloride	natural abundance	100 (±5.0) mM
4	calcium chloride	natural abundance	5 (±0.25) mM
5	sodium azide	natural abundance	0.02 (±0.001) %
6	DTT	natural abundance	5 (±0.5) mM

17 3D CCH-TOCSY

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 (±1) K, pH 7.5 (±0.1)

#	Name	Isotope labeling	Concentration
13	protein	[U-100% 13C; U-100% 15N]	1.3 (±0.1) mM
14	Tris-HCl	natural abundance	10 (±1.0) mM
15	sodium chloride	natural abundance	100 (±5.0) mM
16	calcium chloride	natural abundance	5 (±0.25) mM
17	sodium azide	natural abundance	0.02 (±0.001) %
18	DTT	natural abundance	10 (±0.5) mM

18 4D CC-NOESY

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 298 (±1) K, pH 7.5 (±0.1)

#	Name	Isotope labeling	Concentration
13	protein	[U-100% 13C; U-100% 15N]	1.3 (±0.1) mM
14	Tris-HCl	natural abundance	10 (±1.0) mM
15	sodium chloride	natural abundance	100 (±5.0) mM
16	calcium chloride	natural abundance	5 (±0.25) mM
17	sodium azide	natural abundance	0.02 (±0.001) %
18	DTT	natural abundance	10 (±0.5) mM

19 3D 1H-13C NOESY-aromatic

Instrument

Bruker Avance III - 850 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 (±1) K, pH 7.5 (±0.1)

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N]	1.3 (±0.1) mM
2	Tris-HCl	natural abundance	10 (±1.0) mM
3	sodium chloride	natural abundance	100 (±5.0) mM
4	calcium chloride	natural abundance	5 (±0.25) mM
5	sodium azide	natural abundance	0.02 (±0.001) %
6	DTT	natural abundance	5 (±0.5) mM

20 2D 1H-15N HSQC His

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 (±1) K, pH 7.5 (±0.1)

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N]	1.3 (±0.1) mM
2	Tris-HCl	natural abundance	10 (±1.0) mM
3	sodium chloride	natural abundance	100 (±5.0) mM
4	calcium chloride	natural abundance	5 (±0.25) mM
5	sodium azide	natural abundance	0.02 (±0.001) %
6	DTT	natural abundance	5 (±0.5) mM

21 2D 1H-15N HSQC 150ppm

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 (±1) K, pH 7.5 (±0.1)

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N]	1.3 (±0.1) mM
2	Tris-HCl	natural abundance	10 (±1.0) mM
3	sodium chloride	natural abundance	100 (±5.0) mM
4	calcium chloride	natural abundance	5 (±0.25) mM
5	sodium azide	natural abundance	0.02 (±0.001) %
6	DTT	natural abundance	5 (±0.5) mM

22 2D 1H-15N HSQC NH2 only

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 (±1) K, pH 7.5 (±0.1)

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N]	1.3 (±0.1) mM
2	Tris-HCl	natural abundance	10 (±1.0) mM
3	sodium chloride	natural abundance	100 (±5.0) mM
4	calcium chloride	natural abundance	5 (±0.25) mM
5	sodium azide	natural abundance	0.02 (±0.001) %
6	DTT	natural abundance	5 (±0.5) mM

23 3D HNCA

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 (±1) K, pH 7.5 (±0.1)

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N]	1.3 (±0.1) mM
2	Tris-HCl	natural abundance	10 (±1.0) mM
3	sodium chloride	natural abundance	100 (±5.0) mM
4	calcium chloride	natural abundance	5 (±0.25) mM
5	sodium azide	natural abundance	0.02 (±0.001) %
6	DTT	natural abundance	5 (±0.5) mM

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_17429_2l8v.nef
Input source #2: Coordindates	2l8v.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

--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100
MPVELRANWSEEDLETVIRAVYRQVLGNDYVMASERLVSAESLLRNGKITVREFVRAVAKSELYKEKFLYGNFQTRVIELNYKHLLGRAPYDESEVIFHL
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MPVELRANWSEEDLETVIRAVYRQVLGNDYVMASERLVSAESLLRNGKITVREFVRAVAKSELYKEKFLYGNFQTRVIELNYKHLLGRAPYDESEVIFHL

-------110-------120-------130-------140---
DLYENEGFDADIDSYIDSPEYTNSFGDWVVPYYRGLEHHHHHH
|||||||||||||||||||||||||||||||||||||||||||
DLYENEGFDADIDSYIDSPEYTNSFGDWVVPYYRGLEHHHHHH

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	143	0	0	100.0

Content subtype: combined_17429_2l8v.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1318		83.2 (chain: A, length: 143)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	1721 (1)	noe	83.2 (chain: A, length: 143)
2	Distance restraints	CNS/XPLOR_distance_constraints_4	OK	96 (1)	hbond	53.8 (chain: A, length: 143)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	194 (194)	.	76.2 (chain: A, length: 143)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 143, Sequence coverage: 83.2%
- Total number of assignments
  - ¹H chemical shifts: 683
  - ¹³C chemical shifts: 522
  - ¹⁵N chemical shifts: 113
- Completeness of assignments
  - Entity_assemble_ID: A
- 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)
8	ASN	CG	178.5
46	ASN	CG	177.2
50	THR	HG1	5.77
61	SER	HG	6.34
81	ASN	CG	177.2
105	ASN	CG	176.5
114	SER	HG	5.79
123	ASN	CG	176.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	884	680	76.9
¹³C chemical shifts	677	517	76.4
¹⁵N chemical shifts	160	113	70.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	289	227	78.5
¹³C chemical shifts	286	216	75.5
¹⁵N chemical shifts	139	104	74.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	595	453	76.1
¹³C chemical shifts	391	301	77.0
¹⁵N chemical shifts	21	9	42.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	80	74	92.5
¹³C chemical shifts	80	74	92.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	102	63	61.8
¹³C chemical shifts	100	59	59.0
¹⁵N chemical shifts	2	2	100.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 143, Sequence coverage: 83.2%
- Total number of restraints: 1720
- Weight of restraints: 1.0 (1720)
- Potential type of restraints: square-well-parabolic (1720)
- Range of distance target values: 2.34, 4.0 (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
- Saveframe: CNS/XPLOR_distance_constraints_4
  - Status: OK
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 143, Sequence coverage: 53.8%
  - Total number of restraints: 96
  - Weight of restraints: 1.0 (96)
  - Potential type of restraints: square-well-parabolic (96)
  - Range of distance target values: 2.0, 3.0 (Å)
  - Histogram of distance target values
  - Distance restraints per residue
    - Chain_ID: A
  - Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 143, Sequence coverage: 76.2%
- Total number of restraints: 194
- Total number of restraints per polymer type: 194
- Weight of restraints: 1.0 (194)
- Potential type of restraints: square-well-parabolic (194)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords NESG, NMR structure, phycobilisome linker polypeptide

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Found 1 Document (0.934 seconds)

BMRB: 17429

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Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. CpcC, : 1 : 2 : 113 entities Detail

Experiments performed 23 experiments Detail

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