BMRBj - BMREntryMaster

Found 1 Document (2.787 seconds)

BMRB: 30082

5JTN

The structure of chaperone SecB in complex with unstructured proPhoA binding site c

Authors

Huang, C., Saio, T., Rossi, P., Kalodimos, C.G.

Assembly

Protein-export protein SecB, Alkaline phosphatase (E.C.3.1.3.1)

Entity

1. Protein-export protein SecB (polymer), 155 monomers, 17277.16 × 4 Da Detail

MSEQNNTEMT FQIQRIYTKD ISFEAPNAPH VFQKDWQPEV KLDLDTASSQ LADDVYEVVL RVTVTASLGE ETAFLCEVQQ GGIFSIAGIE GTQMAHCLGA YCPNILFPYA RECITSMVSR GTFPQLNLAP VNFDALFMNY LQQQAGEGTE EHQDA

2. Alkaline phosphatase (polymer, Thiol state: not present), 55 monomers, 5726.277 × 2 Da Detail

GGFFKGIDAL PLTGQYTHYA LNKKTGKPDY VTDSAASATA WSTGVKTYNG ALGVD

Total weight

80561.195 Da

Max. entity weight

17277.16 Da

Source organism

Escherichia coli O157:H7 , Escherichia coli K-12

Exptl. method

solution NMR

Refine. method

molecular dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete1

Sequence coverage: 77.6 %, Completeness: 49.4 %, Completeness (bb): 63.0 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	49.4 % (1172 of 2371)	37.9 % (461 of 1215)	60.8 % (565 of 929)	64.3 % (146 of 227)
Backbone	63.0 % (782 of 1242)	47.9 % (205 of 428)	70.6 % (433 of 613)	71.6 % (144 of 201)
Sidechain	39.9 % (527 of 1322)	32.5 % (256 of 787)	52.8 % (269 of 509)	7.7 % (2 of 26)
Aromatic	40.1 % (89 of 222)	43.2 % (48 of 111)	36.7 % (40 of 109)	50.0 % (1 of 2)
Methyl	73.5 % (169 of 230)	73.9 % (85 of 115)	73.0 % (84 of 115)

1. Protein-export protein SecB

MSEQNNTEMT FQIQRIYTKD ISFEAPNAPH VFQKDWQPEV KLDLDTASSQ LADDVYEVVL RVTVTASLGE ETAFLCEVQQ GGIFSIAGIE GTQMAHCLGA YCPNILFPYA RECITSMVSR GTFPQLNLAP VNFDALFMNY LQQQAGEGTE EHQDA

2. Alkaline phosphatase

GGFFKGIDAL PLTGQYTHYA LNKKTGKPDY VTDSAASATA WSTGVKTYNG ALGVD

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 301 K, pH 7, Details 300 uM [U-100% 13C; U-100% 15N] E.coli Chaperone SecB, 300 uM [U-100% 13C; U-100% 15N] E.coli Alkaline Phosphatase (PhoA) binding site c, 150 mM potassium chloride, 50 mM sodium phosphate, 50 mM potassium phosphate, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	E.coli Alkaline Phosphatase (PhoA) binding site c	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli Chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 mM
4	potassium phosphate	natural abundance	50 mM
5	sodium phosphate	natural abundance	50 mM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

Chem. Shift Complete2

Sequence coverage: 75.2 %, Completeness: 50.8 %, Completeness (bb): 63.6 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	50.8 % (2411 of 4742)	40.0 % (973 of 2430)	61.5 % (1142 of 1858)	65.2 % (296 of 454)
Backbone	63.6 % (1579 of 2484)	49.2 % (421 of 856)	70.9 % (869 of 1226)	71.9 % (289 of 402)
Sidechain	42.0 % (1111 of 2644)	35.1 % (552 of 1574)	54.2 % (552 of 1018)	13.5 % (7 of 52)
Aromatic	39.4 % (175 of 444)	42.3 % (94 of 222)	36.2 % (79 of 218)	50.0 % (2 of 4)
Methyl	73.3 % (337 of 460)	73.9 % (170 of 230)	72.6 % (167 of 230)

1. Protein-export protein SecB

MSEQNNTEMT FQIQRIYTKD ISFEAPNAPH VFQKDWQPEV KLDLDTASSQ LADDVYEVVL RVTVTASLGE ETAFLCEVQQ GGIFSIAGIE GTQMAHCLGA YCPNILFPYA RECITSMVSR GTFPQLNLAP VNFDALFMNY LQQQAGEGTE EHQDA

2. Alkaline phosphatase

GGFFKGIDAL PLTGQYTHYA LNKKTGKPDY VTDSAASATA WSTGVKTYNG ALGVD

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	E.coli Alkaline Phosphatase (PhoA) binding site c	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli Chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 mM
4	potassium phosphate	natural abundance	50 mM
5	sodium phosphate	natural abundance	50 mM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

Chem. Shift Complete3

Sequence coverage: 75.2 %, Completeness: 52.3 %, Completeness (bb): 64.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	52.3 % (3723 of 7113)	42.2 % (1540 of 3645)	62.1 % (1732 of 2787)	66.2 % (451 of 681)
Backbone	64.2 % (2393 of 3726)	50.9 % (653 of 1284)	70.9 % (1304 of 1839)	72.3 % (436 of 603)
Sidechain	44.1 % (1749 of 3966)	37.6 % (887 of 2361)	55.5 % (847 of 1527)	19.2 % (15 of 78)
Aromatic	37.8 % (252 of 666)	39.9 % (133 of 333)	35.5 % (116 of 327)	50.0 % (3 of 6)
Methyl	73.5 % (507 of 690)	73.9 % (255 of 345)	73.0 % (252 of 345)

1. Protein-export protein SecB

MSEQNNTEMT FQIQRIYTKD ISFEAPNAPH VFQKDWQPEV KLDLDTASSQ LADDVYEVVL RVTVTASLGE ETAFLCEVQQ GGIFSIAGIE GTQMAHCLGA YCPNILFPYA RECITSMVSR GTFPQLNLAP VNFDALFMNY LQQQAGEGTE EHQDA

2. Alkaline phosphatase

GGFFKGIDAL PLTGQYTHYA LNKKTGKPDY VTDSAASATA WSTGVKTYNG ALGVD

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	E.coli Alkaline Phosphatase (PhoA) binding site c	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli Chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 mM
4	potassium phosphate	natural abundance	50 mM
5	sodium phosphate	natural abundance	50 mM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

Chem. Shift Complete4

Sequence coverage: 75.7 %, Completeness: 51.8 %, Completeness (bb): 64.0 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	51.8 % (4916 of 9484)	41.3 % (2007 of 4860)	62.1 % (2307 of 3716)	66.3 % (602 of 908)
Backbone	64.0 % (3181 of 4968)	50.1 % (857 of 1712)	71.0 % (1742 of 2452)	72.4 % (582 of 804)
Sidechain	43.4 % (2294 of 5288)	36.5 % (1150 of 3148)	55.2 % (1124 of 2036)	19.2 % (20 of 104)
Aromatic	37.3 % (331 of 888)	39.2 % (174 of 444)	35.1 % (153 of 436)	50.0 % (4 of 8)
Methyl	72.5 % (667 of 920)	72.8 % (335 of 460)	72.2 % (332 of 460)

1. Protein-export protein SecB

MSEQNNTEMT FQIQRIYTKD ISFEAPNAPH VFQKDWQPEV KLDLDTASSQ LADDVYEVVL RVTVTASLGE ETAFLCEVQQ GGIFSIAGIE GTQMAHCLGA YCPNILFPYA RECITSMVSR GTFPQLNLAP VNFDALFMNY LQQQAGEGTE EHQDA

2. Alkaline phosphatase

GGFFKGIDAL PLTGQYTHYA LNKKTGKPDY VTDSAASATA WSTGVKTYNG ALGVD

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	E.coli Alkaline Phosphatase (PhoA) binding site c	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli Chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 mM
4	potassium phosphate	natural abundance	50 mM
5	sodium phosphate	natural abundance	50 mM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

Chem. Shift Complete5

Sequence coverage: 57.6 %, Completeness: 48.5 %, Completeness (bb): 60.0 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	48.5 % (5752 of 11855)	39.7 % (2414 of 6075)	56.5 % (2625 of 4645)	62.8 % (713 of 1135)
Backbone	60.0 % (3725 of 6210)	49.4 % (1058 of 2140)	64.6 % (1979 of 3065)	68.5 % (688 of 1005)
Sidechain	40.5 % (2679 of 6610)	34.5 % (1356 of 3935)	51.0 % (1298 of 2545)	19.2 % (25 of 130)
Aromatic	33.3 % (370 of 1110)	35.3 % (196 of 555)	31.0 % (169 of 545)	50.0 % (5 of 10)
Methyl	65.9 % (758 of 1150)	65.9 % (379 of 575)	65.9 % (379 of 575)

1. Protein-export protein SecB

MSEQNNTEMT FQIQRIYTKD ISFEAPNAPH VFQKDWQPEV KLDLDTASSQ LADDVYEVVL RVTVTASLGE ETAFLCEVQQ GGIFSIAGIE GTQMAHCLGA YCPNILFPYA RECITSMVSR GTFPQLNLAP VNFDALFMNY LQQQAGEGTE EHQDA

2. Alkaline phosphatase

GGFFKGIDAL PLTGQYTHYA LNKKTGKPDY VTDSAASATA WSTGVKTYNG ALGVD

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	E.coli Alkaline Phosphatase (PhoA) binding site c	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli Chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 mM
4	potassium phosphate	natural abundance	50 mM
5	sodium phosphate	natural abundance	50 mM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

Chem. Shift Complete6

Sequence coverage: 63.8 %, Completeness: 47.4 %, Completeness (bb): 57.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	47.4 % (6737 of 14226)	40.0 % (2914 of 7290)	53.5 % (2981 of 5574)	61.8 % (842 of 1362)
Backbone	57.8 % (4308 of 7452)	49.6 % (1273 of 2568)	60.5 % (2225 of 3678)	67.2 % (810 of 1206)
Sidechain	40.0 % (3173 of 7932)	34.8 % (1641 of 4722)	49.1 % (1500 of 3054)	20.5 % (32 of 156)
Aromatic	33.3 % (444 of 1332)	35.9 % (239 of 666)	30.3 % (198 of 654)	58.3 % (7 of 12)
Methyl	62.8 % (867 of 1380)	62.9 % (434 of 690)	62.8 % (433 of 690)

1. Protein-export protein SecB

MSEQNNTEMT FQIQRIYTKD ISFEAPNAPH VFQKDWQPEV KLDLDTASSQ LADDVYEVVL RVTVTASLGE ETAFLCEVQQ GGIFSIAGIE GTQMAHCLGA YCPNILFPYA RECITSMVSR GTFPQLNLAP VNFDALFMNY LQQQAGEGTE EHQDA

2. Alkaline phosphatase

GGFFKGIDAL PLTGQYTHYA LNKKTGKPDY VTDSAASATA WSTGVKTYNG ALGVD

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	E.coli Alkaline Phosphatase (PhoA) binding site c	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli Chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 mM
4	potassium phosphate	natural abundance	50 mM
5	sodium phosphate	natural abundance	50 mM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

LACS Plot; CA

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

Referencing offset: 0.03 ppm, Outliers: 1 Detail

LACS Plot; CB

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

Referencing offset: 0.03 ppm, Outliers: 1 Detail

LACS Plot; HA

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

Referencing offset: 0.1 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 5JTN, Strand ID: A, B, C, D, E, F Detail

Release date

2016-08-17

Citation

Structural basis for the antifolding activity of a molecular chaperone
Huang, C., Saio, T., Rossi, P., Kalodimos, C.G.
Nature (2016), 537, 202-206, PubMed 27501151 , DOI 10.1038/nature18965 , Abstract

Entries sharing articles BMRB: 6 entries Detail

  BMRB: 30080 released on 2016-08-17
    Title The structure of chaperone SecB in complex with unstructured proPhoA
  BMRB: 30081 released on 2016-08-17
    Title The structure of chaperone SecB in complex with unstructured PhoA binding site a
  BMRB: 30083 released on 2016-08-17
    Title The structure of chaperone SecB in complex with unstructured proPhoA binding site d
  BMRB: 30084 released on 2016-08-17
    Title The structure of chaperone SecB in complex with unstructured proPhoA binding site e
  BMRB: 30085 released on 2016-08-17
    Title The structure of chaperone SecB in complex with unstructured MBP binding site d
  BMRB: 30086 released on 2016-08-17
    Title The structure of chaperone SecB in complex with unstructured MBP binding site e

Related entities 1. Protein-export protein SecB, : 2 : 3 : 97 entities Detail

Related entities 2. Alkaline phosphatase, : 1 : 39 : 2 : 9 : 20 entities Detail

Interaction partners 2. Alkaline phosphatase, : 8 interactors Detail

More details for 8 interactors identified by 5 citations

Experiments performed 5 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker AvanceIII - 700 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 301 K, pH 7, Details 300 uM [U-100% 13C; U-100% 15N] E.coli Chaperone SecB, 300 uM [U-100% 13C; U-100% 15N] E.coli Alkaline Phosphatase (PhoA) binding site c, 150 mM potassium chloride, 50 mM sodium phosphate, 50 mM potassium phosphate, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	E.coli Alkaline Phosphatase (PhoA) binding site c	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli Chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 mM
4	potassium phosphate	natural abundance	50 mM
5	sodium phosphate	natural abundance	50 mM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

2 2D 1H-13C HSQC aliphatic

Instrument

Bruker AvanceIII - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
1	E.coli Alkaline Phosphatase (PhoA) binding site c	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli Chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 mM
4	potassium phosphate	natural abundance	50 mM
5	sodium phosphate	natural abundance	50 mM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

3 2D 1H-13C HSQC aromatic

Instrument

Varian INOVA - 900 MHz

Sample

#	Name	Isotope labeling	Concentration
1	E.coli Alkaline Phosphatase (PhoA) binding site c	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli Chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 mM
4	potassium phosphate	natural abundance	50 mM
5	sodium phosphate	natural abundance	50 mM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

4 3D 1H-13C NOESY aliphatic

Instrument

Varian INOVA - 900 MHz

Sample

#	Name	Isotope labeling	Concentration
1	E.coli Alkaline Phosphatase (PhoA) binding site c	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli Chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 mM
4	potassium phosphate	natural abundance	50 mM
5	sodium phosphate	natural abundance	50 mM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

5 3D 1H-13C NOESY aromatic

Instrument

Varian INOVA - 900 MHz

Sample

#	Name	Isotope labeling	Concentration
1	E.coli Alkaline Phosphatase (PhoA) binding site c	[U-100% 13C; U-100% 15N]	300 uM
2	E.coli Chaperone SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 mM
4	potassium phosphate	natural abundance	50 mM
5	sodium phosphate	natural abundance	50 mM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

NMR combined restraints 9 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_30082_5jtn.nef
Input source #2: Coordindates	5jtn.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
MSEQNNTEMTFQIQRIYTKDISFEAPNAPHVFQKDWQPEVKLDLDTASSQLADDVYEVVLRVTVTASLGEETAFLCEVQQGGIFSIAGIEGTQMAHCLGA
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MSEQNNTEMTFQIQRIYTKDISFEAPNAPHVFQKDWQPEVKLDLDTASSQLADDVYEVVLRVTVTASLGEETAFLCEVQQGGIFSIAGIEGTQMAHCLGA

-------110-------120-------130-------140-------150-----
YCPNILFPYARECITSMVSRGTFPQLNLAPVNFDALFMNYLQQQAGEGTEEHQDA
|||||||||||||||||||||||||||||||||||||||||||||||||||||||
YCPNILFPYARECITSMVSRGTFPQLNLAPVNFDALFMNYLQQQAGEGTEEHQDA

Entity_assembly_ID (NMR): B vs Auth_asym_ID (model): B

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

-------110-------120-------130-------140-------150-----
YCPNILFPYARECITSMVSRGTFPQLNLAPVNFDALFMNYLQQQAGEGTEEHQDA
|||||||||||||||||||||||||||||||||||||||||||||||||||||||
YCPNILFPYARECITSMVSRGTFPQLNLAPVNFDALFMNYLQQQAGEGTEEHQDA

Entity_assembly_ID (NMR): C vs Auth_asym_ID (model): C

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

-------110-------120-------130-------140-------150-----
YCPNILFPYARECITSMVSRGTFPQLNLAPVNFDALFMNYLQQQAGEGTEEHQDA
|||||||||||||||||||||||||||||||||||||||||||||||||||||||
YCPNILFPYARECITSMVSRGTFPQLNLAPVNFDALFMNYLQQQAGEGTEEHQDA

Entity_assembly_ID (NMR): D vs Auth_asym_ID (model): D

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

-------110-------120-------130-------140-------150-----
YCPNILFPYARECITSMVSRGTFPQLNLAPVNFDALFMNYLQQQAGEGTEEHQDA
|||||||||||||||||||||||||||||||||||||||||||||||||||||||
YCPNILFPYARECITSMVSRGTFPQLNLAPVNFDALFMNYLQQQAGEGTEEHQDA

Entity_assembly_ID (NMR): E vs Auth_asym_ID (model): E

-------100-------110-------120-------130-------140-----
GGFFKGIDALPLTGQYTHYALNKKTGKPDYVTDSAASATAWSTGVKTYNGALGVD
|||||||||||||||||||||||||||||||||||||||||||||||||||||||
GGFFKGIDALPLTGQYTHYALNKKTGKPDYVTDSAASATAWSTGVKTYNGALGVD
--------10--------20--------30--------40--------50-----

Entity_assembly_ID (NMR): F vs Auth_asym_ID (model): F

-------100-------110-------120-------130-------140-----
GGFFKGIDALPLTGQYTHYALNKKTGKPDYVTDSAASATAWSTGVKTYNGALGVD
|||||||||||||||||||||||||||||||||||||||||||||||||||||||
GGFFKGIDALPLTGQYTHYALNKKTGKPDYVTDSAASATAWSTGVKTYNGALGVD
--------10--------20--------30--------40--------50-----

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Sequence coverage (%)
A	A	155	100.0
B	B	155	100.0
C	C	155	100.0
D	D	155	100.0
E	E	55	100.0
F	F	55	100.0

Content subtype: combined_30082_5jtn.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	891		94.8 (chain: A, length: 155)
2	Assigned chemical shifts	assigned_chemical_shifts_2	Warning	886		94.8 (chain: B, length: 155)
3	Assigned chemical shifts	assigned_chemical_shifts_3	Warning	886		94.8 (chain: C, length: 155)
4	Assigned chemical shifts	assigned_chemical_shifts_4	Warning	891		94.8 (chain: D, length: 155)
5	Assigned chemical shifts	assigned_chemical_shifts_5	Warning	329		98.2 (chain: E, length: 55)
6	Assigned chemical shifts	assigned_chemical_shifts_6	Warning	329		98.2 (chain: F, length: 55)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	1608 (1)	noe	78.1 (chain: A, length: 155), 77.4 (chain: B, length: 155), 77.4 (chain: C, length: 155), 77.4 (chain: D, length: 155)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	996 (996)	.	87.1 (chain: A, length: 155), 85.8 (chain: B, length: 155), 86.5 (chain: C, length: 155), 87.1 (chain: D, length: 155)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 155, Sequence coverage: 94.8%
- Total number of assignments
  - ¹H chemical shifts: 251
  - ¹³C chemical shifts: 506
  - ¹⁵N chemical shifts: 134
- Completeness of assignments
  - Entity_assemble_ID: A
- Redox state of CYS
- 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
Saveframe: assigned_chemical_shifts_2
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: B, Chain length: 155, Sequence coverage: 94.8%
- Total number of assignments
  - ¹H chemical shifts: 250
  - ¹³C chemical shifts: 503
  - ¹⁵N chemical shifts: 133
- Completeness of assignments
  - Entity_assemble_ID: B
- Redox state of CYS
- 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: B
Saveframe: assigned_chemical_shifts_3
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: C, Chain length: 155, Sequence coverage: 94.8%
- Total number of assignments
  - ¹H chemical shifts: 250
  - ¹³C chemical shifts: 503
  - ¹⁵N chemical shifts: 133
- Completeness of assignments
  - Entity_assemble_ID: C
- Redox state of CYS
- 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: C
Saveframe: assigned_chemical_shifts_4
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: D, Chain length: 155, Sequence coverage: 94.8%
- Total number of assignments
  - ¹H chemical shifts: 251
  - ¹³C chemical shifts: 506
  - ¹⁵N chemical shifts: 134
- Completeness of assignments
  - Entity_assemble_ID: D
- Redox state of CYS
- 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: D
Saveframe: assigned_chemical_shifts_5
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: E, Chain length: 55, Sequence coverage: 98.2%
- Total number of assignments
  - ¹H chemical shifts: 147
  - ¹³C chemical shifts: 129
  - ¹⁵N chemical shifts: 53
- Completeness of assignments
  - Entity_assemble_ID: E
- 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: E
Saveframe: assigned_chemical_shifts_6
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: F, Chain length: 55, Sequence coverage: 98.2%
- Total number of assignments
  - ¹H chemical shifts: 147
  - ¹³C chemical shifts: 129
  - ¹⁵N chemical shifts: 53
- Completeness of assignments
  - Entity_assemble_ID: F
- 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: F

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	914	251	27.5
¹³C chemical shifts	691	506	73.2
¹⁵N chemical shifts	174	134	77.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	312	133	42.6
¹³C chemical shifts	310	276	89.0
¹⁵N chemical shifts	148	133	89.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	602	118	19.6
¹³C chemical shifts	381	230	60.4
¹⁵N chemical shifts	26	1	3.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	90	79	87.8
¹³C chemical shifts	90	79	87.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	77	39	50.6
¹³C chemical shifts	76	37	48.7
¹⁵N chemical shifts	1	1	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	914	250	27.4
¹³C chemical shifts	691	503	72.8
¹⁵N chemical shifts	174	133	76.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	312	132	42.3
¹³C chemical shifts	310	275	88.7
¹⁵N chemical shifts	148	132	89.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	602	118	19.6
¹³C chemical shifts	381	228	59.8
¹⁵N chemical shifts	26	1	3.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	90	79	87.8
¹³C chemical shifts	90	79	87.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	77	39	50.6
¹³C chemical shifts	76	37	48.7
¹⁵N chemical shifts	1	1	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	914	250	27.4
¹³C chemical shifts	691	503	72.8
¹⁵N chemical shifts	174	133	76.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	312	132	42.3
¹³C chemical shifts	310	275	88.7
¹⁵N chemical shifts	148	132	89.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	602	118	19.6
¹³C chemical shifts	381	228	59.8
¹⁵N chemical shifts	26	1	3.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	90	79	87.8
¹³C chemical shifts	90	79	87.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	77	39	50.6
¹³C chemical shifts	76	37	48.7
¹⁵N chemical shifts	1	1	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	914	251	27.5
¹³C chemical shifts	691	506	73.2
¹⁵N chemical shifts	174	134	77.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	312	133	42.6
¹³C chemical shifts	310	276	89.0
¹⁵N chemical shifts	148	133	89.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	602	118	19.6
¹³C chemical shifts	381	230	60.4
¹⁵N chemical shifts	26	1	3.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	90	79	87.8
¹³C chemical shifts	90	79	87.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	77	39	50.6
¹³C chemical shifts	76	37	48.7
¹⁵N chemical shifts	1	1	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	301	146	48.5
¹³C chemical shifts	238	129	54.2
¹⁵N chemical shifts	57	53	93.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	116	85	73.3
¹³C chemical shifts	110	45	40.9
¹⁵N chemical shifts	53	52	98.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	185	61	33.0
¹³C chemical shifts	128	84	65.6
¹⁵N chemical shifts	4	1	25.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	30	24	80.0
¹³C chemical shifts	30	26	86.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	34	16	47.1
¹³C chemical shifts	33	15	45.5
¹⁵N chemical shifts	1	1	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	301	146	48.5
¹³C chemical shifts	238	129	54.2
¹⁵N chemical shifts	57	53	93.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	116	85	73.3
¹³C chemical shifts	110	45	40.9
¹⁵N chemical shifts	53	52	98.1

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 155, Sequence coverage: 78.1%
  - Entity_assembly_ID: B, Chain length: 155, Sequence coverage: 77.4%
  - Entity_assembly_ID: C, Chain length: 155, Sequence coverage: 77.4%
  - Entity_assembly_ID: D, Chain length: 155, Sequence coverage: 77.4%
- Total number of restraints: 1608
- Weight of restraints: 1.0 (1608)
- Potential type of restraints: square-well-parabolic (1608)
- Range of distance target values: 1.93, 3.52 (Å)
- Histogram of distance target values
- Distance restraints per residue
  - Chain_ID: A
  - Chain_ID: B
  - Chain_ID: C
  - Chain_ID: D
  - Chain_ID: E
    None
  - Chain_ID: F
    None
- 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: 155, Sequence coverage: 87.1%
  - Entity_assembly_ID: B, Chain length: 155, Sequence coverage: 85.8%
  - Entity_assembly_ID: C, Chain length: 155, Sequence coverage: 86.5%
  - Entity_assembly_ID: D, Chain length: 155, Sequence coverage: 87.1%
- Total number of restraints: 996
- Total number of restraints per polymer type: 996
- Weight of restraints: 1.0 (996)
- Potential type of restraints: square-well-parabolic (996)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A
  - Chain_ID: B
  - Chain_ID: C
  - Chain_ID: D

Keywords Molecular Chaperone

Search

Query history

Resources

Search for primary databases

Search for subsidiary databases

Display

Hits per page

Statistics

Query Changes will take effect after "OK" button is selected.

Maximum hits

Default conjunction operator

Omni-box

Search filter

Sequence search (BLAST)

E-value

Query sequence coverage

Miscellaneous

The number of previewed publications

Completeness of assigned chemical shift

Sequence chart about top aligned regions

Sequence chart about interacting regions

Hit context with highlight

Link destinations for BMRB, PDB and EMDB

Found 1 Document (2.787 seconds)

BMRB: 30082

Sample

Sample

Sample

Sample

Sample

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Entries sharing articles BMRB: 6 entries Detail

Related entities 1. Protein-export protein SecB, : 2 : 3 : 97 entities Detail

Related entities 2. Alkaline phosphatase, : 1 : 39 : 2 : 9 : 20 entities Detail

Interaction partners 2. Alkaline phosphatase, : 8 interactors Detail

Experiments performed 5 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 9 contents Detail