BMRBj - BMREntryMaster

Found 1 Document (0.69 seconds)

BMRB: 15206

2JOW

Differences in the electrostatic surfaces of the type III secretion needle proteins

Authors

Wang, Y., Ouellette, A.N., Egan, C.W., De Guzman, R.N.

Assembly

Needle Monomer

Entity

1. Needle Monomer (polymer, Thiol state: not present), 83 monomers, 9263.157 Da Detail

MATPWSGYLD DVSAKFDTGV DNLQTQVTEA LDKLAAKPSD PALLAAYQSK LSEYNLYRNA QSNTVKVFKD IDAAILEHHH HHH

Formula weight

9263.157 Da

Source organism

Salmonella enterica subsp. enterica serovar Typhimurium

Exptl. method

solution NMR

Refine. method

simulated annealing, molecular dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 96.4 %, Completeness: 79.8 %, Completeness (bb): 90.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	79.8 % (755 of 946)	79.3 % (384 of 484)	80.2 % (299 of 373)	80.9 % (72 of 89)
Backbone	90.2 % (444 of 492)	90.9 % (150 of 165)	90.3 % (223 of 247)	88.7 % (71 of 80)
Sidechain	72.0 % (385 of 535)	73.4 % (234 of 319)	72.5 % (150 of 207)	11.1 % (1 of 9)
Aromatic	2.3 % (2 of 88)	2.3 % (1 of 44)	0.0 % (0 of 43)	100.0 % (1 of 1)
Methyl	96.9 % (93 of 96)	97.9 % (47 of 48)	95.8 % (46 of 48)

1. needle monomer

MATPWSGYLD DVSAKFDTGV DNLQTQVTEA LDKLAAKPSD PALLAAYQSK LSEYNLYRNA QSNTVKVFKD IDAAILEHHH HHH

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0

#	Name	Isotope labeling	Type	Concentration
1	entity	natural abundance		0.8 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	protons	external	indirect	0.2514495
¹H	DSS	protons	external	indirect	1.0
¹⁵N	DSS	protons	external	indirect	0.1013291

Referencing offset: -0.11 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	protons	external	indirect	0.2514495
¹H	DSS	protons	external	indirect	1.0
¹⁵N	DSS	protons	external	indirect	0.1013291

Referencing offset: -0.11 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	protons	external	indirect	0.2514495
¹H	DSS	protons	external	indirect	1.0
¹⁵N	DSS	protons	external	indirect	0.1013291

Referencing offset: 0.09 ppm, Outliers: 2 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	protons	external	indirect	0.2514495
¹H	DSS	protons	external	indirect	1.0
¹⁵N	DSS	protons	external	indirect	0.1013291

Referencing offset: 0.21 ppm, Outliers: 1 Detail

Protein Blocks Logo

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

Release date

2007-10-23

Citation

Differences in the electrostatic surfaces of the type III secretion needle proteins PrgI, BsaL, and MxiH
Wang, Y., Ouellette, A.N., Egana, C.W., Rathinavelana, T., Ima, W., De Guzman, R.N.
J. Mol. Biol. (2007), 371, 1304-1314, PubMed 17617421 , DOI 10.1016/j.jmb.2007.06.034 , Abstract

Related entities 1. Needle Monomer, : 1 : 46 entities Detail

Interaction partners 1. Needle Monomer, : 3 interactors Detail

More details for 3 interactors identified by 1 citations

Experiments performed 8 experiments Detail

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_15206_2jow.nef
Input source #2: Coordindates	2jow.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---
MATPWSGYLDDVSAKFDTGVDNLQTQVTEALDKLAAKPSDPALLAAYQSKLSEYNLYRNAQSNTVKVFKDIDAAILEHHHHHH
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MATPWSGYLDDVSAKFDTGVDNLQTQVTEALDKLAAKPSDPALLAAYQSKLSEYNLYRNAQSNTVKVFKDIDAAILEHHHHHH

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	83	0	0	100.0

Content subtype: combined_15206_2jow.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	751		96.4 (chain: A, length: 83)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	Warning	1676 (1)	noe	94.0 (chain: A, length: 83)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_3	OK	101 (101)	.	92.8 (chain: A, length: 83)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 83, Sequence coverage: 96.4%
- Total number of assignments
  - ¹H chemical shifts: 383
  - ¹³C chemical shifts: 297
  - ¹⁵N chemical shifts: 71
- 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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	484	383	79.1
¹³C chemical shifts	373	297	79.6
¹⁵N chemical shifts	90	71	78.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	165	149	90.3
¹³C chemical shifts	166	147	88.6
¹⁵N chemical shifts	80	70	87.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	319	234	73.4
¹³C chemical shifts	207	150	72.5
¹⁵N chemical shifts	10	1	10.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	49	47	95.9
¹³C chemical shifts	49	46	93.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	44	1	2.3
¹³C chemical shifts	43	0	0.0
¹⁵N chemical shifts	1	1	100.0

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 83, Sequence coverage: 94.0%
- Total number of restraints: 1668
- Weight of restraints: 1.0 (1668)
- Potential type of restraints: upper-bound-parabolic (1668)
- Range of distance target values: 2.7, 5.5 (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

Dihedral angle restraints

Saveframe: DYANA/DIANA_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 83, Sequence coverage: 92.8%
- Total number of restraints: 101
- Total number of restraints per polymer type: 101
- Weight of restraints: 1.0 (101)
- Potential type of restraints: square-well-parabolic (101)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords needle protein

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Found 1 Document (0.69 seconds)

BMRB: 15206

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Needle Monomer, : 1 : 46 entities Detail

Interaction partners 1. Needle Monomer, : 3 interactors Detail

Experiments performed 8 experiments Detail

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NMR combined restraints 4 contents Detail