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BMRB: 30080

5JTL

The structure of chaperone SecB in complex with unstructured proPhoA

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), 471 monomers, 49437.97 Da Detail

MKQSTIALAL LPLLFTPVTK ARTPEMPVLE NRAAQGDITA PGGARRLTGD QTAALRDSLS DKPAKNIILL IGDGMGDSEI TAARNYAEGA GGFFKGIDAL PLTGQYTHYA LNKKTGKPDY VTDSAASATA WSTGVKTYNG ALGVDIHEKD HPTILEMAKA AGLATGNVST AELQDATPAA LVAHVTSRKC YGPSATSEKC PGNALEKGGK GSITEQLLNA RADVTLGGGA KTFAETATAG EWQGKTLREQ AQARGYQLVS DAASLNSVTE ANQQKPLLGL FADGNMPVRW LGPKATYHGN IDKPAVTCTP NPQRNDSVPT LAQMTDKAIE LLSKNEKGFF LQVEGASIDK QDHAANPCGQ IGETVDLDEA VQRALEFAKK EGNTLVIVTA DHAHASQIVA PDTKAPGLTQ ALNTKDGAVM VMSYGNSEED SQEHTGSQLR IAAYGPHAAN VVGLTDQTDL FYTMKAALGL K

Total weight

118546.61 Da

Max. entity weight

49437.97 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: 49.0 %, Completeness: 32.4 %, Completeness (bb): 40.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	32.4 % (2237 of 6896)	27.3 % (969 of 3546)	36.7 % (986 of 2686)	42.5 % (282 of 664)
Backbone	40.7 % (1505 of 3696)	35.5 % (453 of 1276)	42.5 % (775 of 1824)	46.5 % (277 of 596)
Sidechain	26.1 % (983 of 3772)	22.8 % (517 of 2270)	32.1 % (461 of 1434)	7.4 % (5 of 68)
Aromatic	23.8 % (97 of 408)	26.0 % (53 of 204)	21.5 % (43 of 200)	25.0 % (1 of 4)
Methyl	37.9 % (277 of 730)	37.3 % (136 of 365)	38.6 % (141 of 365)

1. Protein-export protein SecB

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

2. Alkaline phosphatase

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), 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)	[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: 53.4 %, Completeness: 34.4 %, Completeness (bb): 42.3 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	34.4 % (4748 of 13792)	29.6 % (2101 of 7092)	38.4 % (2062 of 5372)	44.1 % (585 of 1328)
Backbone	42.3 % (3128 of 7392)	37.1 % (948 of 2552)	44.1 % (1609 of 3648)	47.9 % (571 of 1192)
Sidechain	28.6 % (2155 of 7544)	25.4 % (1155 of 4540)	34.4 % (986 of 2868)	10.3 % (14 of 136)
Aromatic	25.0 % (204 of 816)	28.9 % (118 of 408)	21.0 % (84 of 400)	25.0 % (2 of 8)
Methyl	40.7 % (594 of 1460)	40.3 % (294 of 730)	41.1 % (300 of 730)

1. Protein-export protein SecB

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

2. Alkaline phosphatase

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	E. Coli Alkaline Phosphatase (PhoA)	[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: 45.8 %, Completeness: 33.8 %, Completeness (bb): 41.0 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	33.8 % (6986 of 20688)	28.9 % (3079 of 10638)	37.9 % (3054 of 8058)	42.8 % (853 of 1992)
Backbone	41.0 % (4548 of 11088)	35.7 % (1368 of 3828)	43.0 % (2354 of 5472)	46.2 % (826 of 1788)
Sidechain	28.3 % (3207 of 11316)	25.1 % (1711 of 6810)	34.1 % (1469 of 4302)	13.2 % (27 of 204)
Aromatic	27.4 % (335 of 1224)	31.0 % (190 of 612)	23.7 % (142 of 600)	25.0 % (3 of 12)
Methyl	39.6 % (867 of 2190)	39.1 % (428 of 1095)	40.1 % (439 of 1095)

1. Protein-export protein SecB

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

2. Alkaline phosphatase

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	E. Coli Alkaline Phosphatase (PhoA)	[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: 51.6 %, Completeness: 34.4 %, Completeness (bb): 41.6 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	34.4 % (9486 of 27584)	29.7 % (4216 of 14184)	38.3 % (4115 of 10744)	43.5 % (1155 of 2656)
Backbone	41.6 % (6147 of 14784)	36.5 % (1864 of 5104)	43.4 % (3165 of 7296)	46.9 % (1118 of 2384)
Sidechain	29.0 % (4370 of 15088)	25.9 % (2352 of 9080)	34.5 % (1981 of 5736)	13.6 % (37 of 272)
Aromatic	29.1 % (475 of 1632)	33.0 % (269 of 816)	25.2 % (202 of 800)	25.0 % (4 of 16)
Methyl	40.2 % (1173 of 2920)	39.9 % (583 of 1460)	40.4 % (590 of 1460)

1. Protein-export protein SecB

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

2. Alkaline phosphatase

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	E. Coli Alkaline Phosphatase (PhoA)	[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: 79.1 %, Completeness: 36.2 %, Completeness (bb): 45.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	36.2 % (12472 of 34480)	30.6 % (5423 of 17730)	40.4 % (5429 of 13430)	48.8 % (1620 of 3320)
Backbone	45.2 % (8357 of 18480)	39.7 % (2532 of 6380)	46.6 % (4254 of 9120)	52.7 % (1571 of 2980)
Sidechain	29.5 % (5568 of 18860)	25.5 % (2893 of 11350)	36.6 % (2626 of 7170)	14.4 % (49 of 340)
Aromatic	28.0 % (571 of 2040)	32.0 % (326 of 1020)	23.9 % (239 of 1000)	30.0 % (6 of 20)
Methyl	40.8 % (1489 of 3650)	39.7 % (724 of 1825)	41.9 % (765 of 1825)

1. Protein-export protein SecB

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

2. Alkaline phosphatase

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	E. Coli Alkaline Phosphatase (PhoA)	[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: -0.01 ppm, Outliers: 2 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: -0.01 ppm, Outliers: 2 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: 0.07 ppm, Outliers: 1 Detail

LACS Plot; CO

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: 0.16 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 5JTL, Strand ID: A, B, C, D, E 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: 30081 released on 2016-08-17
    Title The structure of chaperone SecB in complex with unstructured PhoA binding site a
  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 : 16 entities Detail

Experiments performed 6 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), 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)	[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)	[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

Bruker AvanceIII - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
1	E. Coli Alkaline Phosphatase (PhoA)	[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)	[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-15N NOESY

Instrument

Varian INOVA - 900 MHz

Sample

#	Name	Isotope labeling	Concentration
1	E. Coli Alkaline Phosphatase (PhoA)	[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 %

6 3D 1H-13C NOESY aromatic

Instrument

Varian INOVA - 900 MHz

Sample

#	Name	Isotope labeling	Concentration
1	E. Coli Alkaline Phosphatase (PhoA)	[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 8 contents Detail

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	471	100.0

#	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	2046		91.5 (chain: E, length: 471)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	1597 (1)	noe	78.1 (chain: A, length: 155), 78.1 (chain: B, length: 155), 78.1 (chain: C, length: 155), 78.1 (chain: D, length: 155)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	998 (998)	.	87.1 (chain: A, length: 155), 87.1 (chain: B, length: 155), 85.2 (chain: C, length: 155), 87.7 (chain: D, length: 155)

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	2632	660	25.1
¹³C chemical shifts	1995	993	49.8
¹⁵N chemical shifts	508	392	77.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	964	466	48.3
¹³C chemical shifts	942	485	51.5
¹⁵N chemical shifts	448	390	87.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	1668	194	11.6
¹³C chemical shifts	1053	508	48.2
¹⁵N chemical shifts	60	2	3.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	289	92	31.8
¹³C chemical shifts	289	140	48.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	127	35	27.6
¹³C chemical shifts	124	20	16.1
¹⁵N chemical shifts	3	2	66.7

Keywords molecular Chaperone

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_30080_5jtl.nef
Input source #2: Coordindates	5jtl.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

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Found 1 Document (6.186 seconds)

BMRB: 30080

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Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

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 : 16 entities Detail

Experiments performed 6 experiments Detail

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Sample

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NMR combined restraints 8 contents Detail