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Found 1 Document (0.475 seconds)

BMRB: 25032

2MQG

Solution structure of a bacterial immunoglobulin-like domain form a surface protein of Leptospira

Authors

Mei, S.

Assembly

bacterial immunoglobulin-like domain form a surface protein of Leptospira

Entity

1. bacterial immunoglobulin-like domain form a surface protein of Leptospira (polymer, Thiol state: not present), 102 monomers, 10421.30 Da Detail

ENIDITVSAA TLSSISISPI NTNINTTVSK QFFAVGTYSD GTKADLTSSV TWSSSNQSQA KVSNASETKG LVTGIASGNP TIIATYGSVS GNTILTVNKT DT

Formula weight

10421.3 Da

Source organism

Leptospira interrogans serovar Pomona

Exptl. method

solution NMR

Refine. method

distance geometry

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 68.3 %, Completeness (bb): 80.3 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	68.3 % (732 of 1071)	78.0 % (419 of 537)	48.7 % (205 of 421)	95.6 % (108 of 113)
Backbone	80.3 % (488 of 608)	92.3 % (193 of 209)	66.2 % (198 of 299)	97.0 % (97 of 100)
Sidechain	60.6 % (338 of 558)	69.2 % (227 of 328)	46.1 % (100 of 217)	84.6 % (11 of 13)
Aromatic	4.2 % (2 of 48)	4.2 % (1 of 24)	0.0 % (0 of 23)	100.0 % (1 of 1)
Methyl	37.7 % (52 of 138)	60.9 % (42 of 69)	14.5 % (10 of 69)

1. entity

ENIDITVSAA TLSSISISPI NTNINTTVSK QFFAVGTYSD GTKADLTSSV TWSSSNQSQA KVSNASETKG LVTGIASGNP TIIATYGSVS GNTILTVNKT DT

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	H2O	natural abundance		90 %
2	D2O	natural abundance		10 %

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	DSS	methyl protons	internal	direct	0.2514495
¹⁵N	DSS	methyl protons	internal	direct	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
¹H	DSS	methyl protons	internal	direct	1.0
¹³C	DSS	methyl protons	internal	direct	0.2514495
¹⁵N	DSS	methyl protons	internal	direct	0.1013291

Referencing offset: -0.25 ppm, Outliers: 1 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	DSS	methyl protons	internal	direct	0.2514495
¹⁵N	DSS	methyl protons	internal	direct	0.1013291

Referencing offset: -0.12 ppm, Outliers: 2 Detail

Protein Blocks Logo

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

Release date

2014-07-13

Citation

Solution structure of a bacterial immunoglobulin-like domain form a surface protein of Leptospira
Mei, S.
Not known

Related entities 1. bacterial immunoglobulin-like domain form a surface protein of Leptospira, : 1 : 1 : 2 entities Detail

Experiments performed 1 experiments Detail

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_25032_2mqg.nef
Input source #2: Coordindates	2mqg.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
ENIDITVSAATLSSISISPINTNINTTVSKQFFAVGTYSDGTKADLTSSVTWSSSNQSQAKVSNASETKGLVTGIASGNPTIIATYGSVSGNTILTVNKT
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
ENIDITVSAATLSSISISPINTNINTTVSKQFFAVGTYSDGTKADLTSSVTWSSSNQSQAKVSNASETKGLVTGIASGNPTIIATYGSVSGNTILTVNKT

--
DT
||
DT

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	102	0	0	100.0

Content subtype: combined_25032_2mqg.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	712		100.0 (chain: A, length: 102)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	593 (1)	noe	96.1 (chain: A, length: 102)
2	Distance restraints	CNS/XPLOR_distance_constraints_3	Warning	40 (1)	hbond	19.6 (chain: A, length: 102)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_4	OK	123 (123)	.	88.2 (chain: A, length: 102)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 102, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 411
  - ¹³C chemical shifts: 193
  - ¹⁵N chemical shifts: 108
- Completeness of assignments
  - Entity_assemble_ID: A
- Peptide bond of PRO
- 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	537	410	76.4
¹³C chemical shifts	421	193	45.8
¹⁵N chemical shifts	113	108	95.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	209	191	91.4
¹³C chemical shifts	204	100	49.0
¹⁵N chemical shifts	100	97	97.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	328	219	66.8
¹³C chemical shifts	217	93	42.9
¹⁵N chemical shifts	13	11	84.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	69	38	55.1
¹³C chemical shifts	69	8	11.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	24	1	4.2
¹³C chemical shifts	23	0	0.0
¹⁵N chemical shifts	1	1	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: 102, Sequence coverage: 96.1%
- Total number of restraints: 593
- Weight of restraints: 1.0 (593)
- Potential type of restraints: square-well-parabolic (593)
- Range of distance target values: 2.65, 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: 102, Sequence coverage: 19.6%
  - Total number of restraints: 40
  - Weight of restraints: 1.0 (40)
  - Potential type of restraints: square-well-parabolic (40)
  - 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: 102, Sequence coverage: 88.2%
- Total number of restraints: 123
- Total number of restraints per polymer type: 123
- Weight of restraints: 1.0 (123)
- Potential type of restraints: square-well-parabolic (123)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords Bacterial immunoglobulin-like (Big) domain

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Found 1 Document (0.475 seconds)

BMRB: 25032

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. bacterial immunoglobulin-like domain form a surface protein of Leptospira, : 1 : 1 : 2 entities Detail

Experiments performed 1 experiments Detail

Instrument

Sample

NMR combined restraints 5 contents Detail