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Found 1 Document (1.313 seconds)

BMRB: 4001

1QLK

1H, 13C, and 15N resonance assignments for reduced apo-S100beta

Authors

Amburgey, J.C., Abildgaard, F., Starich, M.R., Shah, S., Hilt, D.C., Weber, D.J.

Assembly

apo-S100beta

Entity

1. apo-S100beta (polymer), 92 monomers, 10743.93 Da Detail

MSELEKAMVA LIDVFHQYSG REGDKHKLKK SELKELINNE LSHFLEEIKE QEVVDKVMET LDEDGDGECD FQEFMAFVSM VTTACHEFFE HE

Formula weight

10743.93 Da

Source organism

Rattus norvegicus

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete1

Sequence coverage: 88.0 %, Completeness: 73.2 %, Completeness (bb): 85.9 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	73.2 % (799 of 1091)	71.1 % (403 of 567)	73.1 % (312 of 427)	86.6 % (84 of 97)
Backbone	85.9 % (474 of 552)	84.0 % (158 of 188)	87.1 % (237 of 272)	85.9 % (79 of 92)
Sidechain	64.1 % (402 of 627)	64.6 % (245 of 379)	62.6 % (152 of 243)	100.0 % (5 of 5)
Aromatic	0.0 % (0 of 98)	0.0 % (0 of 49)	0.0 % (0 of 49)
Methyl	69.8 % (60 of 86)	69.8 % (30 of 43)	69.8 % (30 of 43)

1. S100beta

MSELEKAMVA LIDVFHQYSG REGDKHKLKK SELKELINNE LSHFLEEIKE QEVVDKVMET LDEDGDGECD FQEFMAFVSM VTTACHEFFE HE

Show sample condition

Sample

Temperature 310 K, pH 6.5

#	Name	Concentration
1	S100beta	3.0 ~ 6.0 mM
2	EDTA	0.34 ~ 0.34 mM
3	beta-mercaptoethanol	2.0 ~ 10.0 mM
4	d11-Tris-HCl	6.0 ~ 10.0 mM
5	NaCl	17.0 ~ 20.0 mM
6	H2O	90 %
7	D2O	10 %

Chem. Shift Complete2

Sequence coverage: 35.9 %, Completeness: 50.1 %, Completeness (bb): 57.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	50.1 % (1093 of 2182)	49.3 % (559 of 1134)	49.3 % (421 of 854)	58.2 % (113 of 194)
Backbone	57.5 % (635 of 1104)	57.7 % (217 of 376)	57.2 % (311 of 544)	58.2 % (107 of 184)
Sidechain	44.8 % (562 of 1254)	45.1 % (342 of 758)	44.0 % (214 of 486)	60.0 % (6 of 10)
Aromatic	9.7 % (19 of 196)	11.2 % (11 of 98)	8.2 % (8 of 98)
Methyl	55.2 % (95 of 172)	57.0 % (49 of 86)	53.5 % (46 of 86)

1. S100beta

MSELEKAMVA LIDVFHQYSG REGDKHKLKK SELKELINNE LSHFLEEIKE QEVVDKVMET LDEDGDGECD FQEFMAFVSM VTTACHEFFE HE

Show sample condition

Sample

Temperature 310 K, pH 6.5

#	Name	Concentration
1	S100beta	3.0 ~ 6.0 mM
2	EDTA	0.34 ~ 0.34 mM
3	beta-mercaptoethanol	2.0 ~ 10.0 mM
4	d11-Tris-HCl	6.0 ~ 10.0 mM
5	NaCl	17.0 ~ 20.0 mM
6	H2O	90 %
7	D2O	10 %

Chem. Shift Complete3

Sequence coverage: 23.9 %, Completeness: 39.7 %, Completeness (bb): 45.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	39.7 % (1299 of 3273)	38.8 % (660 of 1701)	39.3 % (504 of 1281)	46.4 % (135 of 291)
Backbone	45.7 % (757 of 1656)	45.9 % (259 of 564)	45.2 % (369 of 816)	46.7 % (129 of 276)
Sidechain	35.4 % (665 of 1881)	35.3 % (401 of 1137)	35.4 % (258 of 729)	40.0 % (6 of 15)
Aromatic	6.5 % (19 of 294)	7.5 % (11 of 147)	5.4 % (8 of 147)
Methyl	49.2 % (127 of 258)	51.2 % (66 of 129)	47.3 % (61 of 129)

1. S100beta

MSELEKAMVA LIDVFHQYSG REGDKHKLKK SELKELINNE LSHFLEEIKE QEVVDKVMET LDEDGDGECD FQEFMAFVSM VTTACHEFFE HE

Show sample condition

Sample

Temperature 310 K, pH 6.5

#	Name	Concentration
1	S100beta	3.0 ~ 6.0 mM
2	EDTA	0.34 ~ 0.34 mM
3	beta-mercaptoethanol	2.0 ~ 10.0 mM
4	d11-Tris-HCl	6.0 ~ 10.0 mM
5	NaCl	17.0 ~ 20.0 mM
6	H2O	90 %
7	D2O	10 %

Chem. Shift Complete4

Sequence coverage: 20.7 %, Completeness: 34.2 %, Completeness (bb): 39.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	34.2 % (1491 of 4364)	33.4 % (758 of 2268)	33.9 % (579 of 1708)	39.7 % (154 of 388)
Backbone	39.2 % (865 of 2208)	39.2 % (295 of 752)	38.8 % (422 of 1088)	40.2 % (148 of 368)
Sidechain	30.5 % (766 of 2508)	30.5 % (463 of 1516)	30.6 % (297 of 972)	30.0 % (6 of 20)
Aromatic	4.8 % (19 of 392)	5.6 % (11 of 196)	4.1 % (8 of 196)
Methyl	42.7 % (147 of 344)	44.2 % (76 of 172)	41.3 % (71 of 172)

1. S100beta

MSELEKAMVA LIDVFHQYSG REGDKHKLKK SELKELINNE LSHFLEEIKE QEVVDKVMET LDEDGDGECD FQEFMAFVSM VTTACHEFFE HE

Show sample condition

Sample

Temperature 310 K, pH 6.5

#	Name	Concentration
1	S100beta	3.0 ~ 6.0 mM
2	EDTA	0.34 ~ 0.34 mM
3	beta-mercaptoethanol	2.0 ~ 10.0 mM
4	d11-Tris-HCl	6.0 ~ 10.0 mM
5	NaCl	17.0 ~ 20.0 mM
6	H2O	90 %
7	D2O	10 %

Chem. Shift Complete5

Sequence coverage: 29.3 %, Completeness: 31.7 %, Completeness (bb): 36.3 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	31.7 % (1731 of 5455)	30.9 % (875 of 2835)	31.7 % (677 of 2135)	36.9 % (179 of 485)
Backbone	36.3 % (1001 of 2760)	35.9 % (337 of 940)	36.1 % (491 of 1360)	37.6 % (173 of 460)
Sidechain	28.5 % (894 of 3135)	28.4 % (538 of 1895)	28.8 % (350 of 1215)	24.0 % (6 of 25)
Aromatic	3.9 % (19 of 490)	4.5 % (11 of 245)	3.3 % (8 of 245)
Methyl	39.5 % (170 of 430)	40.0 % (86 of 215)	39.1 % (84 of 215)

1. S100beta

MSELEKAMVA LIDVFHQYSG REGDKHKLKK SELKELINNE LSHFLEEIKE QEVVDKVMET LDEDGDGECD FQEFMAFVSM VTTACHEFFE HE

Show sample condition

Sample

Temperature 310 K, pH 6.5

#	Name	Concentration
1	S100beta	3.0 ~ 6.0 mM
2	EDTA	0.34 ~ 0.34 mM
3	beta-mercaptoethanol	2.0 ~ 10.0 mM
4	d11-Tris-HCl	6.0 ~ 10.0 mM
5	NaCl	17.0 ~ 20.0 mM
6	H2O	90 %
7	D2O	10 %

Chem. Shift Complete6

Sequence coverage: 35.9 %, Completeness: 30.5 %, Completeness (bb): 35.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	30.5 % (1997 of 6546)	29.4 % (1000 of 3402)	30.6 % (785 of 2562)	36.4 % (212 of 582)
Backbone	35.4 % (1173 of 3312)	34.7 % (391 of 1128)	35.3 % (576 of 1632)	37.3 % (206 of 552)
Sidechain	27.1 % (1018 of 3762)	26.8 % (609 of 2274)	27.6 % (403 of 1458)	20.0 % (6 of 30)
Aromatic	3.2 % (19 of 588)	3.7 % (11 of 294)	2.7 % (8 of 294)
Methyl	37.2 % (192 of 516)	37.6 % (97 of 258)	36.8 % (95 of 258)

1. S100beta

MSELEKAMVA LIDVFHQYSG REGDKHKLKK SELKELINNE LSHFLEEIKE QEVVDKVMET LDEDGDGECD FQEFMAFVSM VTTACHEFFE HE

Show sample condition

Sample

Temperature 310 K, pH 6.5

#	Name	Concentration
1	S100beta	3.0 ~ 6.0 mM
2	EDTA	0.34 ~ 0.34 mM
3	beta-mercaptoethanol	2.0 ~ 10.0 mM
4	d11-Tris-HCl	6.0 ~ 10.0 mM
5	NaCl	17.0 ~ 20.0 mM
6	H2O	90 %
7	D2O	10 %

Chem. Shift Complete7

Sequence coverage: 33.7 %, Completeness: 29.3 %, Completeness (bb): 34.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	29.3 % (2238 of 7637)	28.3 % (1125 of 3969)	29.2 % (873 of 2989)	35.3 % (240 of 679)
Backbone	34.5 % (1332 of 3864)	34.1 % (449 of 1316)	34.1 % (650 of 1904)	36.2 % (233 of 644)
Sidechain	25.7 % (1126 of 4389)	25.5 % (677 of 2653)	25.9 % (441 of 1701)	22.9 % (8 of 35)
Aromatic	3.9 % (27 of 686)	4.4 % (15 of 343)	3.5 % (12 of 343)
Methyl	33.6 % (202 of 602)	34.2 % (103 of 301)	32.9 % (99 of 301)

1. S100beta

MSELEKAMVA LIDVFHQYSG REGDKHKLKK SELKELINNE LSHFLEEIKE QEVVDKVMET LDEDGDGECD FQEFMAFVSM VTTACHEFFE HE

Show sample condition

Sample

Temperature 310 K, pH 6.5

#	Name	Concentration
1	S100beta	3.0 ~ 6.0 mM
2	EDTA	0.34 ~ 0.34 mM
3	beta-mercaptoethanol	2.0 ~ 10.0 mM
4	d11-Tris-HCl	6.0 ~ 10.0 mM
5	NaCl	17.0 ~ 20.0 mM
6	H2O	90 %
7	D2O	10 %

Release date

1996-01-28

Citation 1

1H, 13C and 15N NMR Assignments and Solution Secondary Structure of Rat Apo-S100beta
Amburgey, J.C., Abildgaard, F., Starich, M.R., Shah, S., Hilt, D.C., Weber, D.J.
J. Biomol. NMR (1995), 6, 171-179, DOI 10.1007/bf00211781

Show more 1 citaion

Citation 2

Practical introduction to theory and implementation of multinuclear, multidimensional nuclear magnetic resonance experiments
Edison, A.S., Abildgaard, F., Westler, W.M., Mooberry, E.S., Markley, J.L.
Methods. Enzymol. (1994), 239, 3-79, PubMed 7830587 , DOI: , Abstract

Hide non-primary 1 citaion

Entries sharing articles BMRB: 1 entries Detail

BMRB: 6785 released on 2005-12-19
Title Backbone resonance assignments for the Fv fragment of the catalytic antibody 6D9 complexed with a transition state analogue

Related entities 1. apo-S100beta, : 1 : 7 : 2 : 1 : 262 entities Detail

Interaction partners 1. apo-S100beta, : 3 interactors Detail

More details for 3 interactors identified by 3 citations

Experiments performed 1 experiments Detail

Chemical shift validation 9 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4001_3.str
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

Content subtype: bmr4001_3.str

#	Content subtype	Saveframe	Status	# of rows	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_set_one	Warning	827	81.5 (chain: 1, length: 92)
2	Assigned chemical shifts	chemical_shift_assignment_set_two	Warning	115	9.8 (chain: 1, length: 92)
3	Assigned chemical shifts	chemical_shift_assignment_set_three	Warning	116	9.8 (chain: 1, length: 92)
4	Assigned chemical shifts	chemical_shift_assignment_set_four	Warning	35	2.2 (chain: 1, length: 92)
5	Assigned chemical shifts	chemical_shift_assignment_set_five	Warning	64	6.5 (chain: 1, length: 92)
6	Assigned chemical shifts	chemical_shift_assignment_set_six	Warning	64	6.5 (chain: 1, length: 92)
7	Assigned chemical shifts	chemical_shift_assignment_set_seven	Warning	56	5.4 (chain: 1, length: 92)
1	Chemical shift references	chemical_shift_reference_one	OK	3	No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_set_one
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 92, Sequence coverage: 81.5%
- Total number of assignments
  - ¹H chemical shifts: 455
  - ¹³C chemical shifts: 294
  - ¹⁵N chemical shifts: 78
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- 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: 1
Saveframe: chemical_shift_assignment_set_two
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 92, Sequence coverage: 9.8%
- Total number of assignments
  - ¹H chemical shifts: 67
  - ¹³C chemical shifts: 40
  - ¹⁵N chemical shifts: 8
- Completeness of assignments
- 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: 1
Saveframe: chemical_shift_assignment_set_three
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 92, Sequence coverage: 9.8%
- Total number of assignments
  - ¹H chemical shifts: 67
  - ¹³C chemical shifts: 40
  - ¹⁵N chemical shifts: 9
- Completeness of assignments
- 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: 1
Saveframe: chemical_shift_assignment_set_four
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 92, Sequence coverage: 2.2%
- Total number of assignments
  - ¹H chemical shifts: 21
  - ¹³C chemical shifts: 12
  - ¹⁵N chemical shifts: 2
- Completeness of assignments
- 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: 1
Saveframe: chemical_shift_assignment_set_five
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 92, Sequence coverage: 6.5%
- Total number of assignments
  - ¹H chemical shifts: 35
  - ¹³C chemical shifts: 23
  - ¹⁵N chemical shifts: 6
- Completeness of assignments
- 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: 1
Saveframe: chemical_shift_assignment_set_six
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 92, Sequence coverage: 6.5%
- Total number of assignments
  - ¹H chemical shifts: 35
  - ¹³C chemical shifts: 23
  - ¹⁵N chemical shifts: 6
- Completeness of assignments
- 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: 1
Saveframe: chemical_shift_assignment_set_seven
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 92, Sequence coverage: 5.4%
- Total number of assignments
  - ¹H chemical shifts: 31
  - ¹³C chemical shifts: 20
  - ¹⁵N chemical shifts: 5
- Completeness of assignments
- 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: 1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	567	393	69.3
¹³C chemical shifts	427	294	68.9
¹⁵N chemical shifts	98	78	79.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	188	152	80.9
¹³C chemical shifts	184	148	80.4
¹⁵N chemical shifts	92	73	79.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	379	241	63.6
¹³C chemical shifts	243	146	60.1
¹⁵N chemical shifts	6	5	83.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	48	31	64.6
¹³C chemical shifts	48	30	62.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	49	0	0.0
¹³C chemical shifts	49	0	0.0

Keywords EF-hands, S100beta, S100 proteins, secondary structure

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Found 1 Document (1.313 seconds)

BMRB: 4001

Sample

Sample

Sample

Sample

Sample

Sample

Sample

Entries sharing articles BMRB: 1 entries Detail

Related entities 1. apo-S100beta, : 1 : 7 : 2 : 1 : 262 entities Detail

Interaction partners 1. apo-S100beta, : 3 interactors Detail

Experiments performed 1 experiments Detail

Sample

Chemical shift validation 9 contents Detail