BMRBj - BMREntryMaster

Found 1 Document (2.962 seconds)

BMRB: 30084

5JTP

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

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), 22 monomers, 2398.771 × 4 Da Detail

NVVGLTDQTD LFYTMKAALG LK

Total weight

78703.73 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: 88.1 %, Completeness: 56.8 %, Completeness (bb): 73.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	56.8 % (1152 of 2028)	42.7 % (445 of 1042)	70.6 % (559 of 792)	76.3 % (148 of 194)
Backbone	73.8 % (773 of 1048)	56.1 % (201 of 358)	82.7 % (430 of 520)	83.5 % (142 of 170)
Sidechain	44.9 % (515 of 1146)	35.7 % (244 of 684)	60.5 % (265 of 438)	25.0 % (6 of 24)
Aromatic	47.1 % (81 of 172)	50.0 % (43 of 86)	43.5 % (37 of 85)	100.0 % (1 of 1)
Methyl	79.4 % (162 of 204)	78.4 % (80 of 102)	80.4 % (82 of 102)

1. Protein-export protein SecB

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

2. Alkaline phosphatase

NVVGLTDQTD LFYTMKAALG LK

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 e, 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 e	[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: 85.9 %, Completeness: 55.9 %, Completeness (bb): 72.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	55.9 % (2266 of 4056)	41.4 % (863 of 2084)	69.9 % (1108 of 1584)	76.0 % (295 of 388)
Backbone	72.8 % (1525 of 2096)	54.5 % (390 of 716)	82.0 % (853 of 1040)	82.9 % (282 of 340)
Sidechain	44.0 % (1008 of 2292)	34.6 % (473 of 1368)	59.6 % (522 of 876)	27.1 % (13 of 48)
Aromatic	47.1 % (162 of 344)	48.8 % (84 of 172)	44.7 % (76 of 170)	100.0 % (2 of 2)
Methyl	78.4 % (320 of 408)	77.9 % (159 of 204)	78.9 % (161 of 204)

1. Protein-export protein SecB

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

2. Alkaline phosphatase

NVVGLTDQTD LFYTMKAALG LK

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	E. Coli Alkaline Phosphatase (PhoA) binding site e	[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: 88.1 %, Completeness: 55.9 %, Completeness (bb): 73.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	55.9 % (3402 of 6084)	41.3 % (1290 of 3126)	70.1 % (1665 of 2376)	76.8 % (447 of 582)
Backbone	73.2 % (2301 of 3144)	54.8 % (589 of 1074)	82.3 % (1284 of 1560)	83.9 % (428 of 510)
Sidechain	43.7 % (1504 of 3438)	34.2 % (701 of 2052)	59.7 % (784 of 1314)	26.4 % (19 of 72)
Aromatic	48.3 % (249 of 516)	50.4 % (130 of 258)	45.5 % (116 of 255)	100.0 % (3 of 3)
Methyl	76.8 % (470 of 612)	76.5 % (234 of 306)	77.1 % (236 of 306)

1. Protein-export protein SecB

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

2. Alkaline phosphatase

NVVGLTDQTD LFYTMKAALG LK

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	E. Coli Alkaline Phosphatase (PhoA) binding site e	[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: 88.1 %, Completeness: 55.4 %, Completeness (bb): 72.9 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	55.4 % (4490 of 8112)	40.3 % (1679 of 4168)	69.9 % (2216 of 3168)	76.7 % (595 of 776)
Backbone	72.9 % (3055 of 4192)	53.8 % (770 of 1432)	82.4 % (1714 of 2080)	84.0 % (571 of 680)
Sidechain	43.1 % (1975 of 4584)	33.3 % (910 of 2736)	59.4 % (1041 of 1752)	25.0 % (24 of 96)
Aromatic	47.7 % (328 of 688)	49.7 % (171 of 344)	45.0 % (153 of 340)	100.0 % (4 of 4)
Methyl	76.3 % (623 of 816)	76.2 % (311 of 408)	76.5 % (312 of 408)

1. Protein-export protein SecB

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

2. Alkaline phosphatase

NVVGLTDQTD LFYTMKAALG LK

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	E. Coli Alkaline Phosphatase (PhoA) binding site e	[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: 54.2 %, Completeness: 51.5 %, Completeness (bb): 67.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	51.5 % (5224 of 10140)	38.7 % (2018 of 5210)	63.6 % (2518 of 3960)	70.9 % (688 of 970)
Backbone	67.8 % (3551 of 5240)	52.2 % (934 of 1790)	75.3 % (1957 of 2600)	77.6 % (660 of 850)
Sidechain	40.0 % (2292 of 5730)	31.7 % (1085 of 3420)	53.8 % (1179 of 2190)	23.3 % (28 of 120)
Aromatic	40.5 % (348 of 860)	43.3 % (186 of 430)	37.2 % (158 of 425)	80.0 % (4 of 5)
Methyl	68.8 % (702 of 1020)	68.8 % (351 of 510)	68.8 % (351 of 510)

1. Protein-export protein SecB

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

2. Alkaline phosphatase

NVVGLTDQTD LFYTMKAALG LK

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	E. Coli Alkaline Phosphatase (PhoA) binding site e	[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: 35.0 %, Completeness: 47.0 %, Completeness (bb): 61.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	47.0 % (5722 of 12168)	36.0 % (2251 of 6252)	57.3 % (2721 of 4752)	64.4 % (750 of 1164)
Backbone	61.7 % (3879 of 6288)	48.6 % (1045 of 2148)	67.7 % (2113 of 3120)	70.7 % (721 of 1020)
Sidechain	36.6 % (2515 of 6876)	29.4 % (1207 of 4104)	48.7 % (1279 of 2628)	20.1 % (29 of 144)
Aromatic	34.2 % (353 of 1032)	37.0 % (191 of 516)	31.0 % (158 of 510)	66.7 % (4 of 6)
Methyl	62.7 % (767 of 1224)	62.6 % (383 of 612)	62.7 % (384 of 612)

1. Protein-export protein SecB

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

2. Alkaline phosphatase

NVVGLTDQTD LFYTMKAALG LK

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	E. Coli Alkaline Phosphatase (PhoA) binding site e	[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 Complete7

Sequence coverage: 46.9 %, Completeness: 45.1 %, Completeness (bb): 58.9 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	45.1 % (6404 of 14196)	35.3 % (2574 of 7294)	54.2 % (3003 of 5544)	60.9 % (827 of 1358)
Backbone	58.9 % (4322 of 7336)	47.8 % (1197 of 2506)	64.0 % (2329 of 3640)	66.9 % (796 of 1190)
Sidechain	35.2 % (2827 of 8022)	28.8 % (1378 of 4788)	46.2 % (1418 of 3066)	18.5 % (31 of 168)
Aromatic	30.9 % (372 of 1204)	33.7 % (203 of 602)	27.7 % (165 of 595)	57.1 % (4 of 7)
Methyl	60.4 % (862 of 1428)	60.4 % (431 of 714)	60.4 % (431 of 714)

1. Protein-export protein SecB

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

2. Alkaline phosphatase

NVVGLTDQTD LFYTMKAALG LK

Show sample condition

Sample

#	Name	Isotope labeling	Concentration
1	E. Coli Alkaline Phosphatase (PhoA) binding site e	[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 Complete8

Sequence coverage: 48.0 %, Completeness: 43.8 %, Completeness (bb): 56.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	43.8 % (7103 of 16224)	34.9 % (2912 of 8336)	51.8 % (3285 of 6336)	58.4 % (906 of 1552)
Backbone	56.7 % (4750 of 8384)	46.9 % (1343 of 2864)	60.9 % (2534 of 4160)	64.2 % (873 of 1360)
Sidechain	34.5 % (3165 of 9168)	28.7 % (1570 of 5472)	44.6 % (1562 of 3504)	17.2 % (33 of 192)
Aromatic	29.6 % (407 of 1376)	33.4 % (230 of 688)	25.4 % (173 of 680)	50.0 % (4 of 8)
Methyl	58.2 % (950 of 1632)	58.3 % (476 of 816)	58.1 % (474 of 816)

1. Protein-export protein SecB

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

2. Alkaline phosphatase

NVVGLTDQTD LFYTMKAALG LK

Show sample condition

Sample

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

Protein Blocks Logo

Calculated from 20 models in PDB: 5JTP, 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

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

Related entities 2. Alkaline phosphatase, : 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] E.coli Chaperone SecB, 300 uM [U-100% 13C; U-100% 15N] E. Coli Alkaline Phosphatase (PhoA) binding site e, 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 e	[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 e	[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) binding site e	[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 e	[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 e	[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 11 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_30084_5jtp.nef
Input source #2: Coordindates	5jtp.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

450-----460-------470-
NVVGLTDQTDLFYTMKAALGLK
||||||||||||||||||||||
NVVGLTDQTDLFYTMKAALGLK
--------10--------20--

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

450-----460-------470-
NVVGLTDQTDLFYTMKAALGLK
||||||||||||||||||||||
NVVGLTDQTDLFYTMKAALGLK
--------10--------20--

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

450-----460-------470-
NVVGLTDQTDLFYTMKAALGLK
||||||||||||||||||||||
NVVGLTDQTDLFYTMKAALGLK
--------10--------20--

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

450-----460-------470-
NVVGLTDQTDLFYTMKAALGLK
||||||||||||||||||||||
NVVGLTDQTDLFYTMKAALGLK
--------10--------20--

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	22	100.0
F	F	22	100.0
G	G	22	100.0
H	H	22	100.0

Content subtype: combined_30084_5jtp.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	183		100.0 (chain: E, length: 22)
6	Assigned chemical shifts	assigned_chemical_shifts_6	Warning	183		100.0 (chain: F, length: 22)
7	Assigned chemical shifts	assigned_chemical_shifts_7	Warning	183		100.0 (chain: G, length: 22)
8	Assigned chemical shifts	assigned_chemical_shifts_8	Warning	183		100.0 (chain: H, length: 22)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	1581 (1)	noe	77.4 (chain: A, length: 155), 77.4 (chain: B, length: 155), 77.4 (chain: C, length: 155), 78.1 (chain: D, length: 155)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	1012 (1012)	.	87.1 (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: 22, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 78
  - ¹³C chemical shifts: 83
  - ¹⁵N chemical shifts: 22
- Completeness of assignments
  - Entity_assemble_ID: E
- 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: 22, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 78
  - ¹³C chemical shifts: 83
  - ¹⁵N chemical shifts: 22
- Completeness of assignments
  - Entity_assemble_ID: F
- 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: 22, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 78
  - ¹³C chemical shifts: 83
  - ¹⁵N chemical shifts: 22
- Completeness of assignments
  - Entity_assemble_ID: G
- 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: 22, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 78
  - ¹³C chemical shifts: 83
  - ¹⁵N chemical shifts: 22
- Completeness of assignments
  - Entity_assemble_ID: H
- 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	128	77	60.2
¹³C chemical shifts	101	83	82.2
¹⁵N chemical shifts	24	22	91.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	46	40	87.0
¹³C chemical shifts	44	39	88.6
¹⁵N chemical shifts	22	22	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	82	37	45.1
¹³C chemical shifts	57	44	77.2
¹⁵N chemical shifts	2	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	18	17	94.4
¹³C chemical shifts	18	17	94.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	9	5	55.6
¹³C chemical shifts	9	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	128	77	60.2
¹³C chemical shifts	101	83	82.2
¹⁵N chemical shifts	24	22	91.7

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: 78.1%
- Total number of restraints: 1581
- Weight of restraints: 1.0 (1581)
- Potential type of restraints: square-well-parabolic (1581)
- Range of distance target values: 1.88, 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
  - Chain_ID: G
    None
  - Chain_ID: H
    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: 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: 1012
- Total number of restraints per polymer type: 1012
- Weight of restraints: 1.0 (1012)
- Potential type of restraints: square-well-parabolic (1012)
- 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

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Found 1 Document (2.962 seconds)

BMRB: 30084

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

Related entities 2. Alkaline phosphatase, : 1 entities Detail

Experiments performed 5 experiments Detail

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NMR combined restraints 11 contents Detail