BMRBj - BMREntryMaster

Found 1 Document (0.783 seconds)

BMRB: 51867

8RVT

human Insulin Fibrils

Authors

Suladze, S., Sankar, R., Reif, B.

Assembly

Human Insulin Fibrils

Entity

1. Human Insulin Fibrils, entity 1 (polymer, Thiol state: all disulfide bound), 21 monomers, 2383.696 Da Detail

GIVEQCCTSI CSLYQLENYC N

2. Human Insulin Fibrils, entity 2 (polymer, Thiol state: all disulfide bound), 30 monomers, 3429.919 Da Detail

FVNQHLCGSH LVEALYLVCG ERGFFYTPKT

Total weight

5813.615 Da

Max. entity weight

3429.919 Da

Entity Connection

disulfide 3 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS7:SG	2:CYS7:SG
2	disulfide	sing	1:CYS20:SG	2:CYS19:SG
3	disulfide	sing	1:CYS6:SG	1:CYS11:SG

Source organism

Homo sapiens

Exptl. method

solid-state NMR

Data set

assigned_chemical_shifts

Chemical Shifts 1

¹³C: 80, ¹⁵N: 20 assignments Detail

ID	Entity ID	Seq ID	Comp ID	Atom ID	Atom type	Val
1	1	1	GLY	C	C	169.264
2	1	1	GLY	CA	C	43.595
3	1	1	GLY	N	N	106.821
4	1	2	ILE	C	C	174.508
5	1	2	ILE	CA	C	60.024
6	1	2	ILE	CB	C	41.480
7	1	2	ILE	CG1	C	28.264
8	1	2	ILE	CG2	C	16.958
9	1	2	ILE	CD1	C	14.338
10	1	2	ILE	N	N	118.949
11	1	3	VAL	C	C	174.025
12	1	3	VAL	CA	C	60.997
13	1	3	VAL	CB	C	34.967
14	1	3	VAL	CG1	C	20.383
15	1	3	VAL	N	N	127.751
16	1	4	GLU	C	C	174.140
17	1	4	GLU	CA	C	53.838
18	1	4	GLU	CB	C	29.470
19	1	4	GLU	CG	C	34.957
20	1	4	GLU	N	N	124.717
21	1	5	GLN	C	C	174.309
22	1	5	GLN	CA	C	53.887
23	1	5	GLN	CB	C	27.335
24	1	5	GLN	CG	C	33.864
25	1	5	GLN	CD	C	178.524
26	1	5	GLN	N	N	124.741
27	1	6	CYS	C	C	170.763
28	1	6	CYS	CA	C	56.679
29	1	6	CYS	CB	C	50.506
30	1	6	CYS	N	N	119.055
31	1	7	CYS	C	C	174.433
32	1	7	CYS	CA	C	53.849
33	1	7	CYS	CB	C	44.311
34	1	7	CYS	N	N	122.581
35	1	8	THR	C	C	171.940
36	1	8	THR	CA	C	61.793
37	1	8	THR	CB	C	66.894
38	1	8	THR	CG2	C	23.700
39	1	8	THR	N	N	128.223
40	1	9	SER	C	C	171.236
41	1	9	SER	CA	C	57.288
42	1	9	SER	CB	C	72.009
43	1	9	SER	N	N	110.335
44	1	10	ILE	C	C	175.486
45	1	10	ILE	CA	C	60.995
46	1	10	ILE	CB	C	39.700
47	1	10	ILE	CG1	C	27.599
48	1	10	ILE	CG2	C	17.067
49	1	10	ILE	CD1	C	12.116
50	1	10	ILE	N	N	119.859
51	1	11	CYS	C	C	170.712
52	1	11	CYS	CA	C	53.861
53	1	11	CYS	CB	C	47.676
54	1	11	CYS	N	N	126.647
55	1	12	SER	C	C	175.112
56	1	12	SER	CA	C	54.045
57	1	12	SER	CB	C	65.686
58	1	12	SER	N	N	113.280
59	1	13	LEU	C	C	176.669
60	1	13	LEU	CA	C	56.832
61	1	13	LEU	CB	C	40.787
62	1	13	LEU	CG	C	27.112
63	1	13	LEU	CD1	C	24.972
64	1	13	LEU	CD2	C	22.115
65	1	13	LEU	N	N	116.116
66	1	14	TYR	C	C	176.960
67	1	14	TYR	CA	C	56.401
68	1	14	TYR	CB	C	40.429
69	1	14	TYR	CD1	C	133.868
70	1	14	TYR	N	N	116.322
71	1	15	GLN	C	C	175.180
72	1	15	GLN	CA	C	53.931
73	1	15	GLN	CB	C	29.455
74	1	15	GLN	CG	C	32.857
75	1	15	GLN	CD	C	175.254
76	1	15	GLN	N	N	115.624
77	1	16	LEU	C	C	175.128
78	1	16	LEU	CA	C	54.176
79	1	16	LEU	CB	C	38.646
80	1	16	LEU	CG	C	26.624
81	1	16	LEU	CD1	C	25.438
82	1	16	LEU	N	N	115.623
83	1	17	GLU	C	C	176.678
84	1	17	GLU	CA	C	53.962
85	1	17	GLU	CB	C	29.485
86	1	17	GLU	N	N	115.056
87	1	18	ASN	C	C	172.918
88	1	18	ASN	CA	C	51.445
89	1	18	ASN	CB	C	41.635
90	1	18	ASN	N	N	122.502
91	1	19	TYR	C	C	173.078
92	1	19	TYR	CA	C	56.001
93	1	19	TYR	CB	C	41.609
94	1	19	TYR	CD1	C	131.448
95	1	19	TYR	CE1	C	116.956
96	1	19	TYR	N	N	126.219
97	1	20	CYS	C	C	175.908
98	1	20	CYS	CA	C	53.220
99	1	20	CYS	CB	C	44.674
100	1	20	CYS	N	N	118.016

Chemical Shifts 2

¹³C: 101, ¹⁵N: 20 assignments Detail

ID	Entity ID	Seq ID	Comp ID	Atom ID	Atom type	Val
101	2	1	PHE	C	C	170.554
102	2	1	PHE	CA	C	55.237
103	2	1	PHE	CB	C	37.055
104	2	1	PHE	CD1	C	132.290
105	2	1	PHE	CE2	C	135.049
106	2	1	PHE	CZ	C	134.304
107	2	2	VAL	C	C	173.081
108	2	2	VAL	CA	C	61.209
109	2	2	VAL	CB	C	35.459
110	2	2	VAL	CG1	C	20.860
111	2	2	VAL	CG2	C	19.026
112	2	2	VAL	N	N	119.537
113	2	3	ASN	C	C	174.948
114	2	3	ASN	CA	C	51.296
115	2	3	ASN	CB	C	41.123
116	2	3	ASN	CG	C	174.756
117	2	3	ASN	N	N	125.694
118	2	4	GLN	C	C	175.198
119	2	4	GLN	CA	C	53.392
120	2	4	GLN	CB	C	31.580
121	2	4	GLN	CG	C	33.061
122	2	4	GLN	CD	C	177.581
123	2	4	GLN	N	N	122.443
124	2	5	HIS	C	C	174.022
125	2	5	HIS	CA	C	54.127
126	2	5	HIS	CB	C	30.050
127	2	5	HIS	CG	C	130.207
128	2	5	HIS	CD2	C	121.159
129	2	5	HIS	CE1	C	129.854
130	2	5	HIS	N	N	112.405
131	2	6	LEU	C	C	178.769
132	2	6	LEU	CA	C	54.651
133	2	6	LEU	CB	C	39.472
134	2	6	LEU	CG	C	24.173
135	2	6	LEU	CD1	C	27.058
136	2	6	LEU	CD2	C	25.894
137	2	6	LEU	N	N	120.540
138	2	7	CYS	C	C	174.476
139	2	7	CYS	CA	C	59.721
140	2	7	CYS	CB	C	42.905
141	2	7	CYS	N	N	117.225
142	2	8	GLY	C	C	171.902
143	2	8	GLY	CA	C	46.180
144	2	8	GLY	N	N	103.946
145	2	9	SER	C	C	173.386
146	2	9	SER	CA	C	56.277
147	2	9	SER	CB	C	63.904
148	2	9	SER	N	N	107.928
149	2	10	HIS	C	C	175.939
150	2	10	HIS	CA	C	56.157
151	2	10	HIS	CB	C	24.120
152	2	10	HIS	CG	C	131.999
153	2	10	HIS	CD2	C	129.867
154	2	10	HIS	CE1	C	120.138
155	2	10	HIS	N	N	113.879
156	2	11	LEU	C	C	176.738
157	2	11	LEU	CA	C	60.196
158	2	11	LEU	CB	C	43.230
159	2	11	LEU	CG	C	29.144
160	2	11	LEU	CD1	C	25.672
161	2	11	LEU	CD2	C	26.689
162	2	11	LEU	N	N	123.139
163	2	12	VAL	C	C	176.108
164	2	12	VAL	CA	C	59.271
165	2	12	VAL	CB	C	36.024
166	2	12	VAL	CG1	C	22.800
167	2	12	VAL	CG2	C	20.675
168	2	12	VAL	N	N	114.091
169	2	13	GLU	C	C	174.772
170	2	13	GLU	CA	C	58.958
171	2	13	GLU	CB	C	27.447
172	2	13	GLU	CG	C	36.037
173	2	13	GLU	CD	C	181.105
174	2	13	GLU	N	N	126.588
175	2	14	ALA	C	C	172.209
176	2	14	ALA	CA	C	50.793
177	2	14	ALA	CB	C	21.228
178	2	14	ALA	N	N	122.561
179	2	15	LEU	C	C	172.631
180	2	15	LEU	CA	C	54.043
181	2	15	LEU	CB	C	44.450
182	2	15	LEU	CG	C	29.138
183	2	15	LEU	CD1	C	24.886
184	2	15	LEU	CD2	C	23.063
185	2	15	LEU	N	N	127.716
186	2	16	TYR	C	C	173.430
187	2	16	TYR	CA	C	55.982
188	2	16	TYR	CB	C	40.997
189	2	16	TYR	CG	C	132.884
190	2	16	TYR	CD1	C	130.916
191	2	16	TYR	CE1	C	117.462
192	2	16	TYR	N	N	123.352
193	2	17	LEU	C	C	174.436
194	2	17	LEU	CA	C	55.213
195	2	17	LEU	CB	C	42.241
196	2	17	LEU	CG	C	30.282
197	2	17	LEU	CD1	C	23.821
198	2	17	LEU	CD2	C	26.719
199	2	17	LEU	N	N	124.733
200	2	18	VAL	C	C	174.245
201	2	18	VAL	CA	C	61.821
202	2	18	VAL	CB	C	34.226
203	2	18	VAL	CG1	C	20.852
204	2	18	VAL	N	N	124.637
205	2	19	CYS	C	C	174.189
206	2	19	CYS	CA	C	52.059
207	2	19	CYS	CB	C	42.709
208	2	19	CYS	N	N	127.169
209	2	20	GLY	C	C	173.494
210	2	20	GLY	CA	C	45.383
211	2	20	GLY	N	N	112.221
212	2	21	GLU	C	C	177.847
213	2	21	GLU	CA	C	54.251
214	2	21	GLU	CB	C	27.014
215	2	21	GLU	CD	C	179.297
216	2	21	GLU	N	N	120.516
217	2	22	ARG	CA	C	57.982
218	2	22	ARG	CB	C	29.439
219	2	22	ARG	CG	C	28.172
220	2	22	ARG	CD	C	43.364
221	2	22	ARG	CZ	C	159.146

Release date

2023-03-02

Citation

Atomic resolution structure of full-length human insulin fibrils
Suladze, S., Sarkar, R., Rodina, N., Bokvist, K., Krewinkel, M., Scheps, D., Nagel, N., Bardiaux, B., Reif, B.
Proc. Natl. Acad. Sci. U. S. A. (2024), 121, e2401458121-e2401458121, PubMed 38809711 , DOI 10.1073/pnas.2401458121 , Abstract

Related entities 1. Human Insulin Fibrils, entity 1, : 1 : 111 : 13 : 7 : 90 entities Detail

Related entities 2. Human Insulin Fibrils, entity 2, : 1 : 109 : 4 : 18 : 86 entities Detail

Interaction partners 1. Human Insulin Fibrils, entity 1, : 1 : 1 interactors Detail

More details for 2 interactors identified by 2 citations

Interaction partners 2. Human Insulin Fibrils, entity 2, : 6 : 1 interactors Detail

More details for 7 interactors identified by 7 citations

Experiments performed 5 experiments Detail

#	Name	Isotope labeling	Type	Concentration
1	Human insulin, Chain A	[U-100% 15N]		92.5 mM
2	Human insulin, Chain B	[U-100% 15N]		92.5 mM

#	Name	Isotope labeling	Type	Concentration
1	Human insulin, Chain A	[U-100% 15N]		92.5 mM
2	Human insulin, Chain B	[U-100% 15N]		92.5 mM

#	Name	Isotope labeling	Type	Concentration
1	Human insulin, Chain A	[U-100% 15N]		92.5 mM
2	Human insulin, Chain B	[U-100% 15N]		92.5 mM

#	Name	Isotope labeling	Type	Concentration
1	Human insulin, Chain A	[U-100% 15N]		92.5 mM
2	Human insulin, Chain B	[U-100% 15N]		92.5 mM

#	Name	Isotope labeling	Type	Concentration
1	Human insulin, Chain A	[U-100% 15N]		92.5 mM
2	Human insulin, Chain B	[U-100% 15N]		92.5 mM

Chemical shift validation 5 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr51867_3.str
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	True (see coordinates for details)
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Error

Disulfide bonds

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:7:CYS:SG	2:7:CYS:SG	oxidized, CA 53.849, CB 44.311 ppm	unknown	n/a
1:20:CYS:SG	2:19:CYS:SG	oxidized, CA 53.22, CB 44.674 ppm	unknown	n/a
1:6:CYS:SG	1:11:CYS:SG	oxidized, CA 56.679, CB 50.506 ppm	oxidized, CA 53.861, CB 47.676 ppm	n/a

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

None

Content subtype: bmr51867_3.str

#	Content subtype	Saveframe	Status	# of rows	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	100	95.2 (chain: 1, length: 21)
2	Assigned chemical shifts	assigned_chemical_shifts_2	Warning	121	73.3 (chain: 2, length: 30)
1	Chemical shift references	chem_shift_reference_1	OK	2	No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 21, Sequence coverage: 95.2%
- Total number of assignments
  - ¹³C chemical shifts: 80
  - ¹⁵N chemical shifts: 20
- 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: assigned_chemical_shifts_2
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 2, Chain length: 30, Sequence coverage: 73.3%
- Total number of assignments
  - ¹³C chemical shifts: 101
  - ¹⁵N chemical shifts: 20
- Completeness of assignments
  - Entity_assemble_ID: 2
- Redox state of CYS
- 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: 2

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
5	GLN	CD	178.524
15	GLN	CD	175.254

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	89	78	87.6
¹⁵N chemical shifts	25	20	80.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	42	40	95.2
¹⁵N chemical shifts	21	20	95.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	47	38	80.9
¹⁵N chemical shifts	4	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	11	9	81.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	8	3	37.5

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
3	ASN	CG	174.756
4	GLN	CD	177.581
5	HIS	CG	130.207
10	HIS	CG	131.999
13	GLU	CD	181.105
16	TYR	CG	132.884
21	GLU	CD	179.297
22	ARG	CZ	159.146

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	144	93	64.6
¹⁵N chemical shifts	31	20	64.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	60	43	71.7
¹⁵N chemical shifts	29	20	69.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	84	50	59.5
¹⁵N chemical shifts	2	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	17	14	82.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	27	9	33.3

Keywords Human insulin, fibrils, solid-state nmr, amyloid

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Found 1 Document (0.783 seconds)

BMRB: 51867

Related entities 1. Human Insulin Fibrils, entity 1, : 1 : 111 : 13 : 7 : 90 entities Detail

Related entities 2. Human Insulin Fibrils, entity 2, : 1 : 109 : 4 : 18 : 86 entities Detail

Interaction partners 1. Human Insulin Fibrils, entity 1, : 1 : 1 interactors Detail

Interaction partners 2. Human Insulin Fibrils, entity 2, : 6 : 1 interactors Detail

Experiments performed 5 experiments Detail

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Chemical shift validation 5 contents Detail