7NEP: Actin, alpha skeletal muscle

Homology model of the in situ actomyosin complex from the A-band of mouse psoas muscle sarcomere in the rigor state. Determined by electron microscopy at 10.2 Å resolution. Released 7 Apr 2021.

Method: Electron microscopy
Resolution: 10.2 Å
Organism: Mus musculus
Chains: 21
Atoms: 57,453
Mol. weight: 825.75 kDa
Released: 7 Apr 2021

Explore 7NEP in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7NEP contains 336 α-helices and 280 β-strands across 21 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 21 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	10-13	4	1
β-strand	18-23	6	1
β-strand	24	1	2
β-strand	26	1	2
β-strand	31-34	4	1
β-strand	37-40	4	3
α-helix	43-44	2
β-strand	55-56	2	3
α-helix	57-62	6
β-strand	67-70	4	3
β-strand	73-74	2	4
β-strand	77-78	2	4
α-helix	81-90	10
α-helix	91-96	6
α-helix	100-102	3
β-strand	105-109	5	1
α-helix	115-127	13
β-strand	133-138	6	1
α-helix	139-146	8
β-strand	152-157	6	5
β-strand	162-167	6	5
β-strand	178-180	3	5
α-helix	184-195	12
α-helix	196-198	3
α-helix	205-215	11
α-helix	225-231	7
α-helix	232-234	3
β-strand	240-243	4	6
β-strand	249-252	4	6
α-helix	255-261	7
α-helix	266-268	3
α-helix	276-286	11
α-helix	292-296	5
β-strand	299-302	4	5
α-helix	311-322	12
β-strand	331-332	2	5
α-helix	340-348	9
α-helix	353-356	4
β-strand	359-360	2	1
α-helix	361-367	7
α-helix	369-374	6

Chain B: 21 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	10-13	4	7
β-strand	18-23	6	7
β-strand	31-34	4	7
β-strand	37-39	3	8
α-helix	43-44	2
β-strand	55-56	2	8
α-helix	57-62	6
β-strand	68-70	3	8
β-strand	73-74	2	9
β-strand	77-78	2	9
α-helix	81-90	10
α-helix	91-96	6
α-helix	100-102	3
β-strand	105-109	5	7
α-helix	115-127	13
β-strand	133-138	6	7
α-helix	139-146	8
β-strand	152-157	6	10
β-strand	162-167	6	10
β-strand	178-180	3	10
α-helix	184-195	12
α-helix	196-198	3
α-helix	205-215	11
α-helix	225-231	7
α-helix	232-234	3
β-strand	240-243	4	11
β-strand	249-252	4	11
α-helix	255-261	7
α-helix	266-268	3
α-helix	276-286	11
α-helix	292-296	5
β-strand	299-302	4	10
α-helix	311-322	12
β-strand	331-332	2	10
α-helix	340-348	9
α-helix	353-356	4
β-strand	359-360	2	7
α-helix	361-367	7
α-helix	369-374	6

Chains C, D, E, F, G, H, I, J and K: 20 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	10-13	4	12
β-strand	18-23	6	12
β-strand	31-34	4	12
β-strand	37-40	4	13
α-helix	43-44	2
β-strand	55-56	2	13
α-helix	58-62	5
β-strand	67-70	4	13
β-strand	73-74	2	14
β-strand	77-78	2	14
α-helix	81-89	9
α-helix	90-96	7
α-helix	100-102	3
β-strand	105-109	5	12
α-helix	115-127	13
β-strand	133-138	6	12
α-helix	139-147	9
β-strand	152-157	6	15
β-strand	162-167	6	15
β-strand	178-180	3	15
α-helix	184-195	12
α-helix	196-198	3
α-helix	205-217	13
α-helix	225-231	7
β-strand	240-243	4	16
β-strand	249-252	4	16
α-helix	255-261	7
α-helix	276-286	11
α-helix	292-297	6
β-strand	299-302	4	15
α-helix	311-322	12
β-strand	331-332	2	15
α-helix	337-339	3
α-helix	340-350	11
α-helix	353-356	4
β-strand	359-360	2	12
α-helix	361-367	7
α-helix	371-375	5

Chain L: 36 helices, 30 β-strands

Element	Residues	Length	Sheet
β-strand	37-41	5	57
β-strand	47-56	10	57
β-strand	59-64	6	57
β-strand	70-73	4	57
α-helix	74-76	3
β-strand	78-79	2	57
α-helix	80-82	3
β-strand	90	1	58
α-helix	91-93	3
α-helix	99-111	13
β-strand	116-119	4	58
β-strand	122-126	5	58
α-helix	137-143	7
α-helix	155-169	15
β-strand	173-177	5	58
α-helix	185-199	15
α-helix	222-234	13
β-strand	235-236	2	59
β-strand	244-245	2	59
β-strand	247-255	9	58
β-strand	261-271	11	58
α-helix	273-276	4
β-strand	286	1	59
α-helix	287-295	9
α-helix	298-304	7
α-helix	330-341	12
α-helix	346-361	16
α-helix	362-364	3
β-strand	368	1	60
β-strand	377	1	60
α-helix	381-390	10
α-helix	395-403	9
β-strand	406-409	4	61
β-strand	412-415	4	61
α-helix	420-447	28
β-strand	458-464	7	58
α-helix	476-506	31
α-helix	518-527	10
α-helix	533-541	9
α-helix	548-558	11
α-helix	560-562	3
β-strand	566-567	2	62
β-strand	580-584	5	62
β-strand	587-591	5	62
α-helix	596-600	5
β-strand	601	1	63
α-helix	606-612	7
α-helix	618-623	6
β-strand	645	1	64
β-strand	648	1	64
β-strand	650	1	63
α-helix	651-667	17
β-strand	670-677	8	58
α-helix	690-699	10
α-helix	702-711	10
β-strand	715-718	4	65
α-helix	719-726	8
α-helix	727-729	3
α-helix	743-752	10
β-strand	760-762	3	65
β-strand	766-769	4	65
α-helix	773-800	28
α-helix	804-806	3
α-helix	813-828	16
α-helix	832-840	9
α-helix	841-843	3

Chain M: 36 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	37-41	5	71
β-strand	47-56	10	71
β-strand	59-64	6	71
β-strand	70-73	4	71
α-helix	74-76	3
β-strand	78-79	2	71
α-helix	80-82	3
β-strand	90	1	72
α-helix	91-93	3
α-helix	99-111	13
β-strand	116-119	4	72
β-strand	122-126	5	72
α-helix	137-143	7
α-helix	155-169	15
β-strand	173-177	5	72
α-helix	185-199	15
α-helix	222-234	13
β-strand	235-236	2	73
β-strand	244-245	2	73
β-strand	247-255	9	72
β-strand	261-271	11	72
α-helix	274-277	4
β-strand	286	1	73
α-helix	287-295	9
α-helix	298-304	7
α-helix	330-341	12
α-helix	346-361	16
α-helix	362-364	3
β-strand	368	1	74
β-strand	377	1	74
α-helix	381-390	10
α-helix	395-403	9
β-strand	406-409	4	75
β-strand	412-415	4	75
α-helix	420-449	30
β-strand	458-464	7	72
α-helix	476-506	31
α-helix	518-527	10
α-helix	533-542	10
α-helix	548-558	11
α-helix	560-562	3
β-strand	566-567	2	76
β-strand	580-584	5	76
β-strand	587-591	5	76
α-helix	596-600	5
β-strand	601	1	77
α-helix	606-612	7
α-helix	618-623	6
α-helix	630-632	3
β-strand	650	1	77
α-helix	651-667	17
β-strand	670-677	8	72
α-helix	690-699	10
α-helix	702-711	10
β-strand	715-718	4	78
α-helix	719-726	8
α-helix	727-729	3
α-helix	743-752	10
β-strand	760-762	3	78
β-strand	766-769	4	78
α-helix	773-796	24
α-helix	811-828	18
α-helix	832-840	9
α-helix	841-843	3

Chains N and O: 10 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	43-56	14
β-strand	63-65	3	66
α-helix	66-68	3
α-helix	69-75	7
α-helix	82-86	5
β-strand	101-103	3	66
α-helix	104-112	9
α-helix	115-117	3
α-helix	123-130	8
β-strand	140-141	2	67
α-helix	143-152	10
α-helix	159-164	6
β-strand	171	1	68
β-strand	175	1	68
β-strand	176-177	2	67
α-helix	178-185	8

Chains P and Q: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	30-260	231

Chains R and S: 9 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	24-37	14
β-strand	45	1	69
α-helix	47-55	9
α-helix	64-69	6
β-strand	78	1	69
α-helix	80-86	7
α-helix	90-92	3
α-helix	97-105	9
β-strand	115-116	2	70
α-helix	117-125	9
α-helix	133-140	8
β-strand	145	1	70
β-strand	150-151	2	70
α-helix	153-161	9

2 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin, alpha skeletal muscle	A, B, C, D, E, F, G, H, I, J, K	protein	374	Mus musculus	P68134 (AlphaFold model)
Tropomyosin alpha-1 chain	P, Q, T, U	protein	251	Mus musculus	P58771 (AlphaFold model)
Myosin-4	L, M	protein	813	Mus musculus	Q5SX39 (AlphaFold model)
Myosin light chain 1/3, skeletal muscle isoform	N, O	protein	148	Mus musculus	P05977 (AlphaFold model)
Myosin regulatory light chain 2, skeletal muscle isoform	R, S	protein	144	Mus musculus	P97457

Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J, K), FASTA

>7NEP_1 Actin, alpha skeletal muscle (chains A, B, C, D, E, F, G, H, I, J, K)
EDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSK
RGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQ
IMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLA
GRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYE
LPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSG
GTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQE
YDEAGPSIVHRKCF

Sequence of entity 2 (P, Q, T, U), FASTA

>7NEP_2 Tropomyosin alpha-1 chain (chains P, Q, T, U)
LKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEK
LELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVI
ESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKC
AELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLE
KSIDDLEDELY

Sequence of entity 3 (L, M), FASTA

>7NEP_3 Myosin-4 (chains L, M)
FDAKSSVFVVDAKESYVKATVQSREGGKVTAKTEGGATVTVKDDQVFSMNPPKYDKIEDM
AMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEA
PPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGDKKKEEAT
SGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLL
EKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAYVSQGEITVPSIDDQEE
LMATDTAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLT
SLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNSVGALAKSMYEKMFLWMVTRINQQLD
TKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIDW
EFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKP
AKGKAEAHFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSGGQAAE
AEGGGGKKGGKKKGSSFQTVSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHE
LVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFIDSKKASEKLLG
SIDIDHTQYKFGHTKVFFKAGLLGTLEEMRDEKLAQLITRTQAVCRGYLMRVEFKKMMER
RESIFCIQYNVRAFMNVKHWPWMKLYFKIKPLL

Sequence of entity 4 (N, O), FASTA

>7NEP_4 Myosin light chain 1/3, skeletal muscle isoform (chains N, O)
EFSKEQQEDFKEAFLLFDRTGECKITLSQVGDVLRALGTNPTNAEVKKVLGNPSNEEMNA
KKIEFEQFLPMMQAISNNKDQGGYEDFVEGLRVFDKEGNGTVMGAELRHVLATLGEKMKE
EEVEALLAGQEDSNGCINYEAFVKHIMS

Sequence of entity 5 (R, S), FASTA

>7NEP_5 Myosin regulatory light chain 2, skeletal muscle isoform (chains R, S)
MFDQTQIQEFKEAFTVIDQNRDGIIDKEDLRDTFAAMGRLNVKNEELDAMMKEASGPINF
TVFLTMFGEKLKGADPEDVITGAFKVLDPEGKGTIKKQFLEELLTTQCDRFSQEEIKNMW
AAFPPDVGGNVDYKNICYVITHGD

Primary citation

The molecular basis for sarcomere organization in vertebrate skeletal muscle. Wang, Z., Grange, M., Wagner, T. et al. Cell (2021) 184:2135. DOI 10.1016/j.cell.2021.02.047 · PubMed

Other PDB entries of the same protein (UniProt P68134 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4B1U 2.0 Å, Structure of the Phactr1 RPEL domain and RPEL motif directed assemblies with G-actin…
6KLL 3.0 Å, F-actin of cardiac thin filament in low-calcium state
6KLN 3.4 Å, F-actin of cardiac thin filament in high-calcium state
7QIM 4.5 Å, In situ structure of nebulin bound to actin filament in skeletal sarcomere
7QIN 6.6 Å, In situ structure of actomyosin complex in skeletal sarcomere
7AQK 9.0 Å, Model of the actin filament Arp2/3 complex branch junction in cells

Browse structure collections

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