BMRBj - BMREntryMaster

Found 1 Document (3.122 seconds)

BMRB: 30081

5JTM

The structure of chaperone SecB in complex with unstructured PhoA binding site a

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), 25 monomers, 2740.303 × 4 Da Detail

MKQSTIALAL LPLLFTPVTK ARTPE

Total weight

80069.85 Da

Max. entity weight

17277.16 Da

Source organism

Escherichia coli 55989 , Escherichia coli K-12

Exptl. method

solution NMR

Refine. method

molecular dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete1

Sequence coverage: 86.1 %, Completeness: 56.6 %, Completeness (bb): 73.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	56.6 % (1175 of 2076)	43.4 % (464 of 1070)	69.0 % (561 of 813)	77.7 % (150 of 193)
Backbone	73.8 % (782 of 1060)	55.7 % (200 of 359)	82.3 % (437 of 531)	85.3 % (145 of 170)
Sidechain	44.8 % (532 of 1187)	37.1 % (264 of 711)	58.1 % (263 of 453)	21.7 % (5 of 23)
Aromatic	53.0 % (87 of 164)	56.1 % (46 of 82)	49.4 % (40 of 81)	100.0 % (1 of 1)
Methyl	75.9 % (161 of 212)	76.4 % (81 of 106)	75.5 % (80 of 106)

1. Protein-export protein SecB

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

2. Alkaline phosphatase

MKQSTIALAL LPLLFTPVTK ARTPE

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] SecB, 300 uM [U-100% 13C; U-100% 15N] PhoA binding site a, 150 uM potassium chloride, 50 uM sodium phosphate, 50 uM potassium phosphate, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	PhoA binding site a	[U-100% 13C; U-100% 15N]	300 uM
2	SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 uM
4	potassium phosphate	natural abundance	50 uM
5	sodium phosphate	natural abundance	50 uM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

Chem. Shift Complete2

Sequence coverage: 86.1 %, Completeness: 56.5 %, Completeness (bb): 73.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	56.5 % (2345 of 4152)	43.6 % (932 of 2140)	68.7 % (1117 of 1626)	76.7 % (296 of 386)
Backbone	73.1 % (1550 of 2120)	56.1 % (403 of 718)	81.2 % (862 of 1062)	83.8 % (285 of 340)
Sidechain	44.5 % (1056 of 2374)	36.8 % (524 of 1422)	57.6 % (522 of 906)	21.7 % (10 of 46)
Aromatic	53.4 % (175 of 328)	58.5 % (96 of 164)	47.5 % (77 of 162)	100.0 % (2 of 2)
Methyl	74.1 % (314 of 424)	74.5 % (158 of 212)	73.6 % (156 of 212)

1. Protein-export protein SecB

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

2. Alkaline phosphatase

MKQSTIALAL LPLLFTPVTK ARTPE

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	PhoA binding site a	[U-100% 13C; U-100% 15N]	300 uM
2	SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 uM
4	potassium phosphate	natural abundance	50 uM
5	sodium phosphate	natural abundance	50 uM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

Chem. Shift Complete3

Sequence coverage: 87.8 %, Completeness: 56.5 %, Completeness (bb): 73.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	56.5 % (3516 of 6228)	43.4 % (1392 of 3210)	68.8 % (1677 of 2439)	77.2 % (447 of 579)
Backbone	73.2 % (2327 of 3180)	56.5 % (609 of 1077)	80.9 % (1289 of 1593)	84.1 % (429 of 510)
Sidechain	44.4 % (1580 of 3561)	36.4 % (777 of 2133)	57.9 % (787 of 1359)	23.2 % (16 of 69)
Aromatic	53.7 % (264 of 492)	58.1 % (143 of 246)	48.6 % (118 of 243)	100.0 % (3 of 3)
Methyl	74.5 % (474 of 636)	74.8 % (238 of 318)	74.2 % (236 of 318)

1. Protein-export protein SecB

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

2. Alkaline phosphatase

MKQSTIALAL LPLLFTPVTK ARTPE

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	PhoA binding site a	[U-100% 13C; U-100% 15N]	300 uM
2	SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 uM
4	potassium phosphate	natural abundance	50 uM
5	sodium phosphate	natural abundance	50 uM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

Chem. Shift Complete4

Sequence coverage: 88.3 %, Completeness: 56.6 %, Completeness (bb): 73.6 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	56.6 % (4697 of 8304)	43.2 % (1848 of 4280)	69.2 % (2249 of 3252)	77.7 % (600 of 772)
Backbone	73.6 % (3120 of 4240)	56.8 % (816 of 1436)	81.5 % (1731 of 2124)	84.3 % (573 of 680)
Sidechain	44.5 % (2112 of 4748)	36.1 % (1027 of 2844)	58.5 % (1060 of 1812)	27.2 % (25 of 92)
Aromatic	52.6 % (345 of 656)	56.1 % (184 of 328)	48.5 % (157 of 324)	100.0 % (4 of 4)
Methyl	74.4 % (631 of 848)	74.8 % (317 of 424)	74.1 % (314 of 424)

1. Protein-export protein SecB

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

2. Alkaline phosphatase

MKQSTIALAL LPLLFTPVTK ARTPE

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	PhoA binding site a	[U-100% 13C; U-100% 15N]	300 uM
2	SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 uM
4	potassium phosphate	natural abundance	50 uM
5	sodium phosphate	natural abundance	50 uM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

Chem. Shift Complete5

Sequence coverage: 48.3 %, Completeness: 51.8 %, Completeness (bb): 67.0 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	51.8 % (5381 of 10380)	40.4 % (2161 of 5350)	62.4 % (2535 of 4065)	71.0 % (685 of 965)
Backbone	67.0 % (3549 of 5300)	53.6 % (963 of 1795)	72.8 % (1933 of 2655)	76.8 % (653 of 850)
Sidechain	41.1 % (2437 of 5935)	33.6 % (1193 of 3555)	53.6 % (1214 of 2265)	26.1 % (30 of 115)
Aromatic	43.8 % (359 of 820)	46.6 % (191 of 410)	40.5 % (164 of 405)	80.0 % (4 of 5)
Methyl	67.9 % (720 of 1060)	68.1 % (361 of 530)	67.7 % (359 of 530)

1. Protein-export protein SecB

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

2. Alkaline phosphatase

MKQSTIALAL LPLLFTPVTK ARTPE

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	PhoA binding site a	[U-100% 13C; U-100% 15N]	300 uM
2	SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 uM
4	potassium phosphate	natural abundance	50 uM
5	sodium phosphate	natural abundance	50 uM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

Chem. Shift Complete6

Sequence coverage: 50.0 %, Completeness: 48.7 %, Completeness (bb): 62.6 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	48.7 % (6063 of 12456)	38.5 % (2473 of 6420)	57.9 % (2823 of 4878)	66.2 % (767 of 1158)
Backbone	62.6 % (3981 of 6360)	51.4 % (1108 of 2154)	67.2 % (2141 of 3186)	71.8 % (732 of 1020)
Sidechain	38.8 % (2761 of 7122)	31.9 % (1361 of 4266)	50.3 % (1367 of 2718)	23.9 % (33 of 138)
Aromatic	38.9 % (383 of 984)	41.5 % (204 of 492)	36.0 % (175 of 486)	66.7 % (4 of 6)
Methyl	62.7 % (797 of 1272)	62.7 % (399 of 636)	62.6 % (398 of 636)

1. Protein-export protein SecB

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

2. Alkaline phosphatase

MKQSTIALAL LPLLFTPVTK ARTPE

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	PhoA binding site a	[U-100% 13C; U-100% 15N]	300 uM
2	SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 uM
4	potassium phosphate	natural abundance	50 uM
5	sodium phosphate	natural abundance	50 uM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

Chem. Shift Complete7

Sequence coverage: 49.4 %, Completeness: 46.4 %, Completeness (bb): 59.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	46.4 % (6744 of 14532)	37.6 % (2817 of 7490)	54.2 % (3083 of 5691)	62.5 % (844 of 1351)
Backbone	59.1 % (4385 of 7420)	50.1 % (1258 of 2513)	62.4 % (2319 of 3717)	67.9 % (808 of 1190)
Sidechain	37.3 % (3103 of 8309)	31.2 % (1555 of 4977)	47.7 % (1514 of 3171)	21.1 % (34 of 161)
Aromatic	36.2 % (416 of 1148)	39.2 % (225 of 574)	33.0 % (187 of 567)	57.1 % (4 of 7)
Methyl	60.2 % (894 of 1484)	60.9 % (452 of 742)	59.6 % (442 of 742)

1. Protein-export protein SecB

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

2. Alkaline phosphatase

MKQSTIALAL LPLLFTPVTK ARTPE

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	PhoA binding site a	[U-100% 13C; U-100% 15N]	300 uM
2	SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 uM
4	potassium phosphate	natural abundance	50 uM
5	sodium phosphate	natural abundance	50 uM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

Chem. Shift Complete8

Sequence coverage: 50.0 %, Completeness: 44.4 %, Completeness (bb): 56.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	44.4 % (7370 of 16608)	36.4 % (3118 of 8560)	51.2 % (3329 of 6504)	59.8 % (923 of 1544)
Backbone	56.4 % (4780 of 8480)	48.6 % (1396 of 2872)	58.8 % (2498 of 4248)	65.1 % (886 of 1360)
Sidechain	35.7 % (3394 of 9496)	30.2 % (1717 of 5688)	45.3 % (1642 of 3624)	19.0 % (35 of 184)
Aromatic	33.5 % (439 of 1312)	36.4 % (239 of 656)	30.2 % (196 of 648)	50.0 % (4 of 8)
Methyl	56.5 % (959 of 1696)	57.3 % (486 of 848)	55.8 % (473 of 848)

1. Protein-export protein SecB

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

2. Alkaline phosphatase

MKQSTIALAL LPLLFTPVTK ARTPE

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	PhoA binding site a	[U-100% 13C; U-100% 15N]	300 uM
2	SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 uM
4	potassium phosphate	natural abundance	50 uM
5	sodium phosphate	natural abundance	50 uM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

Protein Blocks Logo

Calculated from 20 models in PDB: 5JTM, Strand ID: A, B, C, D, E, F, G, H 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: 30082 released on 2016-08-17
    Title The structure of chaperone SecB in complex with unstructured proPhoA binding site c
  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, : 1 : 8 : 3 : 1 : 99 entities Detail

Related entities 2. Alkaline phosphatase, : 1 : 1 entities Detail

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] SecB, 300 uM [U-100% 13C; U-100% 15N] PhoA binding site a, 150 uM potassium chloride, 50 uM sodium phosphate, 50 uM potassium phosphate, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	PhoA binding site a	[U-100% 13C; U-100% 15N]	300 uM
2	SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 uM
4	potassium phosphate	natural abundance	50 uM
5	sodium phosphate	natural abundance	50 uM
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	PhoA binding site a	[U-100% 13C; U-100% 15N]	300 uM
2	SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 uM
4	potassium phosphate	natural abundance	50 uM
5	sodium phosphate	natural abundance	50 uM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

3 2D 1H-13C HSQC aromatic

Instrument

Bruker AvanceIII - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
1	PhoA binding site a	[U-100% 13C; U-100% 15N]	300 uM
2	SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 uM
4	potassium phosphate	natural abundance	50 uM
5	sodium phosphate	natural abundance	50 uM
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	PhoA binding site a	[U-100% 13C; U-100% 15N]	300 uM
2	SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 uM
4	potassium phosphate	natural abundance	50 uM
5	sodium phosphate	natural abundance	50 uM
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	PhoA binding site a	[U-100% 13C; U-100% 15N]	300 uM
2	SecB	[U-100% 13C; U-100% 15N]	300 uM
3	potassium chloride	natural abundance	150 uM
4	potassium phosphate	natural abundance	50 uM
5	sodium phosphate	natural abundance	50 uM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

NMR combined restraints 11 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_30081_5jtm.nef
Input source #2: Coordindates	5jtm.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

--------10--------20-----
MKQSTIALALLPLLFTPVTKARTPE
|||||||||||||||||||||||||
MKQSTIALALLPLLFTPVTKARTPE

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

--------10--------20-----
MKQSTIALALLPLLFTPVTKARTPE
|||||||||||||||||||||||||
MKQSTIALALLPLLFTPVTKARTPE

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

--------10--------20-----
MKQSTIALALLPLLFTPVTKARTPE
|||||||||||||||||||||||||
MKQSTIALALLPLLFTPVTKARTPE

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

--------10--------20-----
MKQSTIALALLPLLFTPVTKARTPE
|||||||||||||||||||||||||
MKQSTIALALLPLLFTPVTKARTPE

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	25	100.0
F	F	25	100.0
G	G	25	100.0
H	H	25	100.0

Content subtype: combined_30081_5jtm.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	186		96.0 (chain: E, length: 25)
6	Assigned chemical shifts	assigned_chemical_shifts_6	Warning	186		96.0 (chain: F, length: 25)
7	Assigned chemical shifts	assigned_chemical_shifts_7	Warning	186		96.0 (chain: G, length: 25)
8	Assigned chemical shifts	assigned_chemical_shifts_8	Warning	186		96.0 (chain: H, length: 25)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	1639 (1)	noe	77.4 (chain: A, length: 155), 77.4 (chain: B, length: 155), 77.4 (chain: C, length: 155), 77.4 (chain: D, length: 155), 32.0 (chain: E, length: 25), 32.0 (chain: F, length: 25), 32.0 (chain: G, length: 25), 32.0 (chain: H, length: 25)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	1004 (1004)	.	85.8 (chain: A, length: 155), 87.1 (chain: B, length: 155), 86.5 (chain: C, length: 155), 88.4 (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: 25, Sequence coverage: 96.0%
- Total number of assignments
  - ¹H chemical shifts: 86
  - ¹³C chemical shifts: 79
  - ¹⁵N chemical shifts: 21
- 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: 25, Sequence coverage: 96.0%
- Total number of assignments
  - ¹H chemical shifts: 86
  - ¹³C chemical shifts: 79
  - ¹⁵N chemical shifts: 21
- 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
Saveframe: assigned_chemical_shifts_7
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: G, Chain length: 25, Sequence coverage: 96.0%
- Total number of assignments
  - ¹H chemical shifts: 86
  - ¹³C chemical shifts: 79
  - ¹⁵N chemical shifts: 21
- Completeness of assignments
  - Entity_assemble_ID: G
- 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: G
Saveframe: assigned_chemical_shifts_8
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: H, Chain length: 25, Sequence coverage: 96.0%
- Total number of assignments
  - ¹H chemical shifts: 86
  - ¹³C chemical shifts: 79
  - ¹⁵N chemical shifts: 21
- Completeness of assignments
  - Entity_assemble_ID: H
- 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: H

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	156	85	54.5
¹³C chemical shifts	122	79	64.8
¹⁵N chemical shifts	24	21	87.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	47	37	78.7
¹³C chemical shifts	50	19	38.0
¹⁵N chemical shifts	22	21	95.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	109	48	44.0
¹³C chemical shifts	72	60	83.3
¹⁵N chemical shifts	2	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	22	20	90.9
¹³C chemical shifts	22	19	86.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	5	5	100.0
¹³C chemical shifts	5	5	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	156	85	54.5
¹³C chemical shifts	122	79	64.8
¹⁵N chemical shifts	24	21	87.5

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: 77.4%
  - 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%
  - Entity_assembly_ID: E, Chain length: 25, Sequence coverage: 32.0%
  - Entity_assembly_ID: F, Chain length: 25, Sequence coverage: 32.0%
  - Entity_assembly_ID: G, Chain length: 25, Sequence coverage: 32.0%
  - Entity_assembly_ID: H, Chain length: 25, Sequence coverage: 32.0%
- Total number of restraints: 1639
- Weight of restraints: 1.0 (1639)
- Potential type of restraints: square-well-parabolic (1639)
- Range of distance target values: 1.9, 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
  - Chain_ID: F
  - Chain_ID: G
  - Chain_ID: H
- 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: 85.8%
  - Entity_assembly_ID: B, Chain length: 155, Sequence coverage: 87.1%
  - Entity_assembly_ID: C, Chain length: 155, Sequence coverage: 86.5%
  - Entity_assembly_ID: D, Chain length: 155, Sequence coverage: 88.4%
- Total number of restraints: 1004
- Total number of restraints per polymer type: 1004
- Weight of restraints: 1.0 (1004)
- Potential type of restraints: square-well-parabolic (1004)
- 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 (3.122 seconds)

BMRB: 30081

Sample

Sample

Sample

Sample

Sample

Sample

Sample

Sample

Entries sharing articles BMRB: 6 entries Detail

Related entities 1. Protein-export protein SecB, : 1 : 8 : 3 : 1 : 99 entities Detail

Related entities 2. Alkaline phosphatase, : 1 : 1 entities Detail

Experiments performed 5 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 11 contents Detail