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BMRB: 17381

2L7Y

Backbone 1H, 13C, and 15N Chemical Shift Assignments for a putative surface protein

Authors

Assembly

putative surface protein

Entity

1. putative surface protein (polymer, Thiol state: not present), 97 monomers, 10871.69 Da Detail

SPKTILGIEV SQEPKKDYLV GDSLDLSEGR FAVAYSNDTM EEHSFTDEGV EISGYDAQKT GRQTLTLHYQ GHEVSFDVLV SPKAALNDEL EHHHHHH

Formula weight

10871.69 Da

Source organism

Streptococcus pneumoniae

Exptl. method

Refine. method

DGSA-distance geometry simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 91.8 %, Completeness: 66.1 %, Completeness (bb): 74.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	66.1 % (720 of 1090)	72.1 % (404 of 560)	53.7 % (231 of 430)	85.0 % (85 of 100)
Backbone	74.8 % (431 of 576)	89.9 % (178 of 198)	59.2 % (168 of 284)	90.4 % (85 of 94)
Sidechain	61.1 % (369 of 604)	62.4 % (226 of 362)	60.6 % (143 of 236)	0.0 % (0 of 6)
Aromatic	0.0 % (0 of 98)	0.0 % (0 of 49)	0.0 % (0 of 49)
Methyl	69.4 % (68 of 98)	75.5 % (37 of 49)	63.3 % (31 of 49)

1. putative surface protein

SPKTILGIEV SQEPKKDYLV GDSLDLSEGR FAVAYSNDTM EEHSFTDEGV EISGYDAQKT GRQTLTLHYQ GHEVSFDVLV SPKAALNDEL EHHHHHH

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	putative surface protein	[U-99% 13C; U-99% 15N]		0.7 mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

LACS Plot; CA

Referencing offset: 0.0 ppm, Outliers: 2 Detail

LACS Plot; CB

Referencing offset: 0.0 ppm, Outliers: 2 Detail

LACS Plot; HA

Referencing offset: -0.06 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2L7Y, Strand ID: A Detail

Release date

2012-02-28

Citation

1H and 15N Assigned Chemical Shifts for a putative surface protein
Wang, T.
Not known

Related entities 1. putative surface protein, : 1 : 2 entities Detail

Experiments performed 8 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker DMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	putative surface protein	[U-99% 13C; U-99% 15N]		0.7 mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

2 3D 1H-13C NOESY

Instrument

Bruker DMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	putative surface protein	[U-99% 13C; U-99% 15N]		0.7 mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

3 3D CBCA(CO)NH

Instrument

Bruker DMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	putative surface protein	[U-99% 13C; U-99% 15N]		0.7 mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

4 3D C(CO)NH

Instrument

Bruker DMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	putative surface protein	[U-99% 13C; U-99% 15N]		0.7 mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

5 3D HNCACB

Instrument

Bruker DMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	putative surface protein	[U-99% 13C; U-99% 15N]		0.7 mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

6 3D HBHA(CO)NH

Instrument

Bruker DMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	putative surface protein	[U-99% 13C; U-99% 15N]		0.7 mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

7 3D H(CCO)NH

Instrument

Bruker DMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	putative surface protein	[U-99% 13C; U-99% 15N]		0.7 mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

8 3D 1H-15N NOESY

Instrument

Bruker DMX - 500 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	putative surface protein	[U-99% 13C; U-99% 15N]		0.7 mM
2	H2O	natural abundance		90 %
3	D2O	natural abundance		10 %

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_17381_2l7y.nef
Input source #2: Coordindates	2l7y.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

0--------10--------20--------30--------40--------50--------60--------70--------80--------90-------
MSPKTILGIEVSQEPKKDYLVGDSLDLSEGRFAVAYSNDTMEEHSFTDEGVEISGYDAQKTGRQTLTLHYQGHEVSFDVLVSPKAALNDELEHHHHHH
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MSPKTILGIEVSQEPKKDYLVGDSLDLSEGRFAVAYSNDTMEEHSFTDEGVEISGYDAQKTGRQTLTLHYQGHEVSFDVLVSPKAALNDELEHHHHHH
--------10--------20--------30--------40--------50--------60--------70--------80--------90--------

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	98	0	0	100.0

Content subtype: combined_17381_2l7y.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	721		89.8 (chain: A, length: 98)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	1301 (1)	noe	89.8 (chain: A, length: 98)
2	Distance restraints	CNS/XPLOR_distance_constraints_3	Warning	38 (1)	hbond	23.5 (chain: A, length: 98)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_4	OK	90 (90)	.	70.4 (chain: A, length: 98)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 98, Sequence coverage: 89.8%
- Total number of assignments
  - ¹H chemical shifts: 409
  - ¹³C chemical shifts: 228
  - ¹⁵N chemical shifts: 84
- Completeness of assignments
  - Entity_assemble_ID: A
- Peptide bond of PRO
- 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

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 98, Sequence coverage: 89.8%
- Total number of restraints: 1300
- Weight of restraints: 1.0 (1300)
- Potential type of restraints: square-well-parabolic (1300)
- Range of distance target values: 2.4, 4.15 (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_3
  - Status: Warning
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 98, Sequence coverage: 23.5%
  - Total number of restraints: 38
  - Weight of restraints: 1.0 (38)
  - Potential type of restraints: square-well-parabolic (38)
  - Range of distance target values: 2.0, 3.4 (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_4
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 98, Sequence coverage: 70.4%
- Total number of restraints: 90
- Total number of restraints per polymer type: 90
- Weight of restraints: 1.0 (90)
- Potential type of restraints: square-well-parabolic (90)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A