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BMRB: 25210

4UZM

Shotgun proteolysis: A practical application

Authors

Allen, M.D., Bycroft, M., Freund, S.M.V., Christ, D.

Assembly

PUTATIVE MEMBRANE PROTEIN IGAA HOMOLOG

Entity

1. PUTATIVE MEMBRANE PROTEIN IGAA HOMOLOG (polymer, Thiol state: not present), 120 monomers, 13425.85 Da Detail

MAFADAQTRK LTPEERSAVE NYLESLTQVL QVPGPTGASA APISLALNAE SNNVMMLTHA ITRYGISTDD PNKWRYYLDS VEVHLPPFWE QYINDENTVE LIHTDSLPLV ISLNGHTLQE

Formula weight

13425.85 Da

Source organism

Escherichia coli

Exptl. method

Refine. method

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 99.2 %, Completeness: 96.9 %, Completeness (bb): 98.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	96.9 % (1331 of 1373)	98.2 % (692 of 705)	97.0 % (525 of 541)	89.8 % (114 of 127)
Backbone	98.4 % (693 of 704)	98.3 % (232 of 236)	98.3 % (350 of 356)	99.1 % (111 of 112)
Sidechain	95.8 % (752 of 785)	98.1 % (460 of 469)	96.0 % (289 of 301)	20.0 % (3 of 15)
Aromatic	94.0 % (94 of 100)	100.0 % (50 of 50)	91.7 % (44 of 48)	0.0 % (0 of 2)
Methyl	98.7 % (150 of 152)	97.4 % (74 of 76)	100.0 % (76 of 76)

1. PUTATIVE MEMBRANE PROTEIN IGAA HOMOLOG

MAFADAQTRK LTPEERSAVE NYLESLTQVL QVPGPTGASA APISLALNAE SNNVMMLTHA ITRYGISTDD PNKWRYYLDS VEVHLPPFWE QYINDENTVE LIHTDSLPLV ISLNGHTLQE

Show sample condition

Sample

Solvent system 95% water/5% D2O, Pressure 1 atm, Temperature 293.000 K, pH 6.500, Details 1.5 mmol/l

#	Name	Isotope labeling	Type	Concentration
1	PUTATIVE MEMBRANE PROTEIN IGAA HOMOLOG	[U-13C; U-15N]		1.5 mM
2	potassium phosphate	natural abundance		20 mM
3	NaCl	natural abundance		100 mM

LACS Plot; CA

Referencing offset: -0.04 ppm, Outliers: 1 Detail

LACS Plot; CB

Referencing offset: -0.04 ppm, Outliers: 1 Detail

LACS Plot; HA

Referencing offset: -0.04 ppm, Outliers: 2 Detail

LACS Plot; CO

Referencing offset: 0.15 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 4UZM, Strand ID: A Detail

Release date

2014-09-14

Related entities 1. PUTATIVE MEMBRANE PROTEIN IGAA HOMOLOG, : 1 : 3 : 11 entities Detail

Interaction partners 1. PUTATIVE MEMBRANE PROTEIN IGAA HOMOLOG, : 1 interactors Detail

More details for 1 interactors identified by 1 citations

Experiments performed 10 experiments Detail

1 1H-15N HSQC

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 95% water/5% D2O, Pressure 1 atm, Temperature 293.000 K, pH 6.500, Details 1.5 mmol/l

#	Name	Isotope labeling	Type	Concentration
1	PUTATIVE MEMBRANE PROTEIN IGAA HOMOLOG	[U-13C; U-15N]		1.5 mM
2	potassium phosphate	natural abundance		20 mM
3	NaCl	natural abundance		100 mM

2 1H-13C HSQC

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 95% water/5% D2O, Pressure 1 atm, Temperature 293.000 K, pH 6.500, Details 1.5 mmol/l

#	Name	Isotope labeling	Type	Concentration
1	PUTATIVE MEMBRANE PROTEIN IGAA HOMOLOG	[U-13C; U-15N]		1.5 mM
2	potassium phosphate	natural abundance		20 mM
3	NaCl	natural abundance		100 mM

3 HNCACB

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 95% water/5% D2O, Pressure 1 atm, Temperature 293.000 K, pH 6.500, Details 1.5 mmol/l

#	Name	Isotope labeling	Type	Concentration
1	PUTATIVE MEMBRANE PROTEIN IGAA HOMOLOG	[U-13C; U-15N]		1.5 mM
2	potassium phosphate	natural abundance		20 mM
3	NaCl	natural abundance		100 mM

4 CBCA(CO)NH

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 95% water/5% D2O, Pressure 1 atm, Temperature 293.000 K, pH 6.500, Details 1.5 mmol/l

#	Name	Isotope labeling	Type	Concentration
1	PUTATIVE MEMBRANE PROTEIN IGAA HOMOLOG	[U-13C; U-15N]		1.5 mM
2	potassium phosphate	natural abundance		20 mM
3	NaCl	natural abundance		100 mM

5 HNCO

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 95% water/5% D2O, Pressure 1 atm, Temperature 293.000 K, pH 6.500, Details 1.5 mmol/l

#	Name	Isotope labeling	Type	Concentration
1	PUTATIVE MEMBRANE PROTEIN IGAA HOMOLOG	[U-13C; U-15N]		1.5 mM
2	potassium phosphate	natural abundance		20 mM
3	NaCl	natural abundance		100 mM

6 HN(CA)CO

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 95% water/5% D2O, Pressure 1 atm, Temperature 293.000 K, pH 6.500, Details 1.5 mmol/l

#	Name	Isotope labeling	Type	Concentration
1	PUTATIVE MEMBRANE PROTEIN IGAA HOMOLOG	[U-13C; U-15N]		1.5 mM
2	potassium phosphate	natural abundance		20 mM
3	NaCl	natural abundance		100 mM

7 HNHB

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 95% water/5% D2O, Pressure 1 atm, Temperature 293.000 K, pH 6.500, Details 1.5 mmol/l

#	Name	Isotope labeling	Type	Concentration
1	PUTATIVE MEMBRANE PROTEIN IGAA HOMOLOG	[U-13C; U-15N]		1.5 mM
2	potassium phosphate	natural abundance		20 mM
3	NaCl	natural abundance		100 mM

8 1H-NOESY

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 95% water/5% D2O, Pressure 1 atm, Temperature 293.000 K, pH 6.500, Details 1.5 mmol/l

#	Name	Isotope labeling	Type	Concentration
1	PUTATIVE MEMBRANE PROTEIN IGAA HOMOLOG	[U-13C; U-15N]		1.5 mM
2	potassium phosphate	natural abundance		20 mM
3	NaCl	natural abundance		100 mM

9 1H-DQF-COSY

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 95% water/5% D2O, Pressure 1 atm, Temperature 293.000 K, pH 6.500, Details 1.5 mmol/l

#	Name	Isotope labeling	Type	Concentration
1	PUTATIVE MEMBRANE PROTEIN IGAA HOMOLOG	[U-13C; U-15N]		1.5 mM
2	potassium phosphate	natural abundance		20 mM
3	NaCl	natural abundance		100 mM

10 1H-TOCSY

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 95% water/5% D2O, Pressure 1 atm, Temperature 293.000 K, pH 6.500, Details 1.5 mmol/l

#	Name	Isotope labeling	Type	Concentration
1	PUTATIVE MEMBRANE PROTEIN IGAA HOMOLOG	[U-13C; U-15N]		1.5 mM
2	potassium phosphate	natural abundance		20 mM
3	NaCl	natural abundance		100 mM

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_25210_4uzm.nef
Input source #2: Coordindates	4uzm.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

----40--------50--------60--------70--------80--------90-------100-------110-------120-------130----
MAFADAQTRKLTPEERSAVENYLESLTQVLQVPGPTGASAAPISLALNAESNNVMMLTHAITRYGISTDDPNKWRYYLDSVEVHLPPFWEQYINDENTVE
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MAFADAQTRKLTPEERSAVENYLESLTQVLQVPGPTGASAAPISLALNAESNNVMMLTHAITRYGISTDDPNKWRYYLDSVEVHLPPFWEQYINDENTVE
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100

---140-------150----
LIHTDSLPLVISLNGHTLQE
||||||||||||||||||||
LIHTDSLPLVISLNGHTLQE
-------110-------120

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	120	0	0	100.0

Content subtype: combined_25210_4uzm.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list	Warning	1340		99.2 (chain: A, length: 120)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	3863 (1)	noe	99.2 (chain: A, length: 120)
2	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	88 (1)	hbond	48.3 (chain: A, length: 120)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_4	OK	224 (224)	.	90.0 (chain: A, length: 120)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list

Status: Warning

Sequence coverage of experimental data

Entity_assembly_ID: A, Chain length: 120, Sequence coverage: 99.2%

----40--------50--------60--------70--------80--------90-------100-------110-------120-------130----
MAFADAQTRKLTPEERSAVENYLESLTQVLQVPGPTGASAAPISLALNAESNNVMMLTHAITRYGISTDDPNKWRYYLDSVEVHLPPFWEQYINDENTVE
 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
.AFADAQTRKLTPEERSAVENYLESLTQVLQVPGPTGASAAPISLALNAESNNVMMLTHAITRYGISTDDPNKWRYYLDSVEVHLPPFWEQYINDENTVE

---140-------150----
LIHTDSLPLVISLNGHTLQE
||||||||||||||||||||
LIHTDSLPLVISLNGHTLQE

Total number of assignments
- ¹H chemical shifts: 705
- ¹³C chemical shifts: 524
- ¹⁵N chemical shifts: 111

Completeness of assignments

Entity_assemble_ID: A

Excluded Atom_ID in statistics

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
93	HIS	HE2	7.193
96	THR	HG1	5.418
97	ARG	HH11	6.157
97	ARG	HH12	6.157
97	ARG	HH21	6.157
97	ARG	HH22	6.157
109	ARG	HH11	6.812
109	ARG	HH12	6.812
109	ARG	HH21	6.812
109	ARG	HH22	6.812
138	THR	HG1	5.732
140	SER	HG	5.645

All atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	705	692	98.2
¹³C chemical shifts	541	524	96.9
¹⁵N chemical shifts	131	111	84.7

Backbone atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	236	233	98.7
¹³C chemical shifts	240	236	98.3
¹⁵N chemical shifts	112	111	99.1

Side chain atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	469	459	97.9
¹³C chemical shifts	301	288	95.7
¹⁵N chemical shifts	19	0	0.0

Methyl group atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	79	74	93.7
¹³C chemical shifts	79	78	98.7

Aromatic group atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	50	50	100.0
¹³C chemical shifts	48	44	91.7
¹⁵N chemical shifts	2	0	0.0

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

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 120, Sequence coverage: 99.2%
- Total number of restraints: 3841
- Weight of restraints: 1.0 (3841)
- Potential type of restraints: square-well-parabolic (3841)
- Range of distance target values: 2.3, 3.9 (Å)
- Histogram of distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map
- Saveframe: CNS/XPLOR_distance_constraints_3
  - Status: OK
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 120, Sequence coverage: 48.3%
  - Total number of restraints: 88
  - Weight of restraints: 1.0 (88)
  - Potential type of restraints: square-well-parabolic (88)
  - Range of distance target values: 1.95, 2.9 (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: 120, Sequence coverage: 90.0%
- Total number of restraints: 224
- Total number of restraints per polymer type: 224
- Weight of restraints: 1.0 (224)
- Potential type of restraints: square-well-parabolic (224)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords STRUCTURAL PROTEIN