1MVW: Skeletal muscle myosin II

Molecular models of averaged rigor crossbridges from tomograms of insect flight muscle. Determined by electron microscopy at 70.0 Å resolution. Released 20 Nov 2002.

Method: Electron microscopy
Resolution: 70.0 Å
Organisms: Gallus gallus, Oryctolagus cuniculus
Chains: 32
Atoms: 94,966
Mol. weight: 1358.59 kDa
Released: 20 Nov 2002

Explore 1MVW in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1MVW contains 712 α-helices and 521 β-strands across 32 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.

Chains 1, 8, 9 and Z: 26 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	109
β-strand	16-21	6	109
β-strand	25	1	105
β-strand	29-32	4	109
β-strand	35-38	4	110
α-helix	47-49	3
β-strand	53-54	2	110
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	110
β-strand	71-72	2	111
β-strand	75-76	2	111
α-helix	79-88	10
α-helix	89-94	6
α-helix	98-100	3
β-strand	103-107	5	109
α-helix	113-122	10
α-helix	123-127	5
β-strand	131-136	6	109
α-helix	137-144	8
β-strand	150-155	6	112
β-strand	160-166	7	112
β-strand	169-170	2	112
α-helix	172-174	3
β-strand	176-178	3	112
α-helix	182-194	13
α-helix	203-216	14
α-helix	224-232	9
β-strand	238-241	4	113
β-strand	247-250	4	113
α-helix	253-256	4
α-helix	259-262	4
α-helix	264-267	4
α-helix	274-282	9
α-helix	290-294	5
β-strand	297-300	4	112
α-helix	302-305	4
α-helix	309-318	10
α-helix	326-327	2
β-strand	329-330	2	112
α-helix	335-337	3
α-helix	338-348	11
α-helix	353-355	3
β-strand	357-358	2	109
α-helix	359-365	7
α-helix	368-371	4

Chains 2 and X: 26 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	114
β-strand	16-21	6	114
β-strand	22	1	115
β-strand	24	1	115
β-strand	29-32	4	114
β-strand	35-38	4	116
β-strand	47	1	91
α-helix	48-49	2
β-strand	53-54	2	116
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	116
β-strand	71-72	2	117
β-strand	75-76	2	117
α-helix	79-88	10
α-helix	89-94	6
α-helix	98-100	3
β-strand	103-107	5	114
α-helix	113-122	10
α-helix	123-127	5
β-strand	131-136	6	114
α-helix	137-144	8
β-strand	150-155	6	118
β-strand	160-166	7	118
β-strand	169-170	2	118
α-helix	172-174	3
β-strand	176-178	3	118
α-helix	182-194	13
α-helix	203-216	14
α-helix	224-232	9
β-strand	238-241	4	119
β-strand	247-250	4	119
α-helix	253-256	4
α-helix	259-262	4
α-helix	264-267	4
α-helix	274-282	9
α-helix	290-294	5
β-strand	297-300	4	118
α-helix	302-305	4
α-helix	309-318	10
α-helix	326-327	2
β-strand	329-330	2	118
α-helix	335-337	3
α-helix	338-348	11
α-helix	353-355	3
β-strand	357-358	2	114
α-helix	359-365	7
α-helix	368-371	4

Chains 3, 4, 5, 6, 7 and Y: 26 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	120
β-strand	16-21	6	120
β-strand	22	1	121
β-strand	24	1	121
β-strand	29-32	4	120
β-strand	35-38	4	122
α-helix	47-49	3
β-strand	53-54	2	122
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	122
β-strand	71-72	2	123
β-strand	75-76	2	123
α-helix	79-88	10
α-helix	89-94	6
α-helix	98-100	3
β-strand	103-107	5	120
α-helix	113-122	10
α-helix	123-127	5
β-strand	131-136	6	120
α-helix	137-144	8
β-strand	150-155	6	124
β-strand	160-166	7	124
β-strand	169-170	2	124
α-helix	172-174	3
β-strand	176-178	3	124
α-helix	182-194	13
α-helix	203-216	14
α-helix	224-232	9
β-strand	238-241	4	125
β-strand	247-250	4	125
α-helix	253-256	4
α-helix	259-262	4
α-helix	264-267	4
α-helix	274-282	9
α-helix	290-294	5
β-strand	297-300	4	124
α-helix	302-305	4
α-helix	309-318	10
α-helix	326-327	2
β-strand	329-330	2	124
α-helix	335-337	3
α-helix	338-348	11
α-helix	353-355	3
β-strand	357-358	2	120
α-helix	359-365	7
α-helix	368-371	4

Chains A, J, M and P: 39 helices, 32 β-strands

Element	Residues	Length	Sheet
α-helix	14-17	4
α-helix	25-28	4
β-strand	37-41	5	1
β-strand	47-51	5	1
β-strand	52-55	4	2
β-strand	59-62	4	2
β-strand	70-73	4	2
α-helix	74-76	3
β-strand	77-78	2	1
β-strand	90	1	3
α-helix	91-93	3
α-helix	99-108	10
β-strand	116-118	3	3
β-strand	123-126	4	3
α-helix	133-135	3
α-helix	139-142	4
α-helix	155-165	11
α-helix	166-170	5
β-strand	173-179	7	3
α-helix	185-199	15
α-helix	221-233	13
β-strand	234-235	2	4
β-strand	243-244	2	4
β-strand	247-254	8	3
β-strand	260-262	3	3
β-strand	265-268	4	3
α-helix	272-275	4
β-strand	285	1	4
α-helix	286-291	6
α-helix	297-303	7
α-helix	309-311	3
α-helix	313-315	3
α-helix	327-340	14
α-helix	345-361	17
β-strand	366-368	3	5
α-helix	369	1
β-strand	375-377	3	5
α-helix	382-390	9
α-helix	394-402	9
β-strand	405	1	6
β-strand	414	1	6
α-helix	419-448	30
β-strand	457-465	9	3
β-strand	473	1	7
α-helix	475-505	31
α-helix	517-527	11
α-helix	532-539	8
α-helix	547-558	12
β-strand	559	1	9
β-strand	562	1	9
β-strand	565-566	2	7
β-strand	579-582	4	7
β-strand	587-590	4	7
α-helix	595-600	6
α-helix	605-612	8
α-helix	617-627	11
β-strand	632	1	10
α-helix	640-643	4
α-helix	651-665	15
β-strand	668-675	8	3
α-helix	688-698	11
α-helix	700-707	8
β-strand	714-716	3	11
α-helix	717-724	8
α-helix	725-727	3
α-helix	731-738	8
α-helix	742-747	6
β-strand	758-761	4	11
β-strand	764-767	4	11
α-helix	771-826	56
α-helix	830-838	9

Chains B, E, H, K, N and Q: 10 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	21-34	14
β-strand	41-42	2	17
α-helix	44-54	11
α-helix	61-68	8
β-strand	75-76	2	17
α-helix	77-87	11
α-helix	94-104	11
α-helix	110-113	4
α-helix	114-122	9
α-helix	130-137	8
α-helix	142-146	5
α-helix	152-158	7

Chains C, F, I, L, O and R: 9 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	9-17	9
α-helix	27-36	10
α-helix	43-51	9
α-helix	65-75	11
α-helix	76-81	6
α-helix	84-94	11
β-strand	101-103	3	23
α-helix	104-113	10
α-helix	120-127	8
β-strand	128	1	23
β-strand	131	1	23
β-strand	136-138	3	23
α-helix	139-146	8

Chain D: 39 helices, 33 β-strands

Element	Residues	Length	Sheet
α-helix	14-17	4
α-helix	25-28	4
β-strand	37-41	5	29
β-strand	47-51	5	29
β-strand	52-55	4	30
β-strand	59-62	4	30
β-strand	70-73	4	30
α-helix	74-76	3
β-strand	77-78	2	29
β-strand	90	1	31
α-helix	91-93	3
α-helix	99-108	10
β-strand	116-118	3	31
β-strand	123-126	4	31
α-helix	133-135	3
α-helix	139-142	4
α-helix	155-165	11
α-helix	166-170	5
β-strand	173-179	7	31
α-helix	185-199	15
α-helix	221-233	13
β-strand	234-235	2	32
β-strand	243-244	2	32
β-strand	247-254	8	31
β-strand	260-262	3	31
β-strand	265-268	4	31
α-helix	272-275	4
β-strand	285	1	32
α-helix	286-291	6
α-helix	297-303	7
α-helix	309-311	3
α-helix	313-315	3
α-helix	327-340	14
α-helix	345-361	17
β-strand	366-368	3	33
α-helix	369	1
β-strand	375-377	3	33
α-helix	382-390	9
α-helix	394-402	9
β-strand	405	1	34
β-strand	414	1	34
α-helix	419-448	30
β-strand	457-465	9	31
β-strand	473	1	35
α-helix	475-505	31
β-strand	508	1	36
α-helix	517-527	11
α-helix	532-539	8
α-helix	547-558	12
β-strand	559	1	38
β-strand	562	1	38
β-strand	565-566	2	35
β-strand	579-582	4	35
β-strand	587-590	4	35
α-helix	595-600	6
α-helix	605-612	8
α-helix	617-627	11
β-strand	632	1	39
α-helix	640-643	4
α-helix	651-665	15
β-strand	668-675	8	31
α-helix	688-698	11
α-helix	700-707	8
β-strand	714-716	3	36
α-helix	717-724	8
α-helix	725-727	3
α-helix	731-738	8
α-helix	742-747	6
β-strand	758-761	4	36
β-strand	764-767	4	36
α-helix	771-826	56
α-helix	830-838	9

Chain G: 39 helices, 32 β-strands

Element	Residues	Length	Sheet
α-helix	14-17	4
α-helix	25-28	4
β-strand	37-41	5	59
β-strand	47-51	5	59
β-strand	52-55	4	60
β-strand	59-62	4	60
β-strand	70-73	4	60
α-helix	74-76	3
β-strand	77-78	2	59
β-strand	90	1	61
α-helix	91-93	3
α-helix	99-108	10
β-strand	116-119	4	61
β-strand	122-126	5	61
α-helix	133-135	3
α-helix	139-142	4
α-helix	155-165	11
α-helix	166-170	5
β-strand	173-179	7	61
α-helix	185-199	15
α-helix	221-233	13
β-strand	234-235	2	62
β-strand	243-244	2	62
β-strand	247-254	8	61
β-strand	260-262	3	61
β-strand	265-268	4	61
α-helix	272-275	4
β-strand	285	1	62
α-helix	286-291	6
α-helix	297-303	7
α-helix	309-311	3
α-helix	313-315	3
α-helix	327-340	14
α-helix	345-361	17
β-strand	366-368	3	63
α-helix	369	1
β-strand	375-377	3	63
α-helix	382-390	9
α-helix	394-402	9
β-strand	405	1	64
β-strand	414	1	64
α-helix	419-448	30
β-strand	457-465	9	61
β-strand	473	1	65
α-helix	475-506	32
α-helix	517-527	11
α-helix	532-539	8
α-helix	547-558	12
β-strand	559	1	67
β-strand	562	1	67
β-strand	565-566	2	65
β-strand	579-582	4	65
β-strand	587-590	4	65
α-helix	595-600	6
α-helix	605-612	8
α-helix	617-627	11
β-strand	632	1	68
α-helix	640-643	4
α-helix	651-665	15
β-strand	668-675	8	61
α-helix	688-698	11
α-helix	700-707	8
β-strand	714-716	3	69
α-helix	717-724	8
α-helix	725-727	3
α-helix	731-738	8
α-helix	742-747	6
β-strand	758-761	4	69
β-strand	764-767	4	69
α-helix	771-826	56
α-helix	830-838	9

1 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
Skeletal muscle myosin II	A, D, G, J, M, P	protein	840	Gallus gallus	P13538 (AlphaFold model)
Skeletal muscle myosin II regulatory; light chain	B, E, H, K, N, Q	protein	145	Gallus gallus	P02609 (AlphaFold model)
Skeletal muscle myosin II essential; light chain	C, F, I, L, O, R	protein	147	Gallus gallus	P02605 (AlphaFold model)
Rabbit skeletal muscle actin	1, 2, 3, 4, 5, 6, 7, 8, 9, V, W, X, Y, Z	protein	375	Oryctolagus cuniculus	P68135 (AlphaFold model)

Sequence of entity 1 (A, D, G, J, M, P), FASTA

>1MVW_1 SKELETAL MUSCLE MYOSIN II (chains A, D, G, J, M, P)
DAEMAAFGEAAPYLRKSEKERIEAQNKPFDAKSSVFVVHPKQSFVKGTIQSKEGGKVTVK
TEGGETLTVKEDQVFSMNPPKYDKIEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFC
VTVNPYKWLPVYNPKVVLAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGA
GKTVNTKRVIQYFATIAASGEKKKEEQSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNS
SRFGKFIRIHFGATGKLASADIETYLLEKSRVTFQLPAERSYHIFYQIMSNKKPELIDML
LITTNPYDYHYVSEGEITVPSIDDQEELMATDSAIDILGFSADEKTAIYKLTGAVMHYGN
LKFKQKQREEQAEPDGTEVADKAAYLMGLNSAELLKALCYPRVGVGNEAVTKGETVSEVH
NSVGALAKAVYEKMFLWMVIRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFT
NEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFP
KATDTSFKNKLYDEHLGKSNNFQKPKPAKGKAEAHFSLVHYAGTVDYNISGWLEKNKDPL
NETVIGLYQKSSVKTLALLFATYGGEAEGGGGKKGGKKKGSSFQTVSALFRENLNKLMAN
LRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRVLYADFKQR
YRVLNASAIPEGQFMDSKKASEKLLGGGDVDHTQYAFGHTKVFFKAGLLGLLEEMRDDKL
AEIITATQARCRGFLMRVEYRAMVERRESIFCIQYNVRSFMNVKHWPWMKLFFKIKPLLK

Sequence of entity 2 (B, E, H, K, N, Q), FASTA

>1MVW_2 SKELETAL MUSCLE MYOSIN II REGULATORY; LIGHT CHAIN (chains B, E, H, K, N, Q)
FDETEIEDFKEAFTVIDQNADGIIDKDDLRETFAAMGRLNVKNEELDAMIKEASGPINFT
VFLTMFGEKLKGADPEDVIMGAFKVLDPDGKGSIKKSFLEELLTTGGGRFTPEEIKNMWA
AFPPDVAGNVDYKNICYVITHGEDA

Sequence of entity 3 (C, F, I, L, O, R), FASTA

>1MVW_3 SKELETAL MUSCLE MYOSIN II ESSENTIAL; LIGHT CHAIN (chains C, F, I, L, O, R)
SKAAADDFKEAFLLFDRTGDAKITASQVGDIARALGQNPTNAEINKILGNPSKEEMNAAA
ITFEEFLPMLQAAANNKDQGTFEDFVEGLRVFDKEGNGTVMGAELRHVLATLGEKMTEEE
VEELMKGQEDSNGCINYEAFVKHIMSV

Sequence of entity 4 (1, 2, 3, 4, 5, 6, 7, 8, 9, V, W, X, Y, Z), FASTA

>1MVW_4 RABBIT SKELETAL MUSCLE ACTIN (chains 1, 2, 3, 4, 5, 6, 7, 8, 9, V, W, X, Y, Z)
DEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS
KRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMT
QIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDL
AGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSY
ELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMS
GGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQ
EYDEAGPSIVHRKCF

Primary citation

Molecular Modeling of Averaged Rigor Crossbridges from Tomograms of Insect Flight Muscle. Chen, L.F., Winkler, H., Reedy, M.K. et al. J Struct Biol (2002) 138:92-104. DOI 10.1016/S1047-8477(02)00013-8 · PubMed

Other PDB entries of the same protein (UniProt P13538 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2MYS 2.8 Å, Myosin subfragment-1, alpha carbon coordinates only for the two light chains
1M8Q 70.0 Å, Molecular Models of Averaged Rigor Crossbridges from Tomograms of Insect Flight Muscle
1O18 70.0 Å, Molecular models of averaged rigor crossbridges from tomograms of insect flight muscle
1O19 70.0 Å, Molecular models of averaged rigor crossbridges from tomograms of insect flight muscle
1O1A 70.0 Å, Molecular models of averaged rigor crossbridges from tomograms of insect flight muscle
1O1B 70.0 Å, Molecular models of averaged rigor crossbridges from tomograms of insect flight muscle
1O1C 70.0 Å, Molecular models of averaged rigor crossbridges from tomograms of insect flight muscle
1O1D 70.0 Å, Molecular models of averaged rigor crossbridges from tomograms of insect flight muscle
1O1E 70.0 Å, Molecular models of averaged rigor crossbridges from tomograms of insect flight muscle
1O1F 70.0 Å, Molecular models of averaged rigor crossbridges from tomograms of insect flight muscle
1O1G 70.0 Å, Molecular models of averaged rigor crossbridges from tomograms of insect flight muscle
2W4A Isometrically contracting insect asynchronous flight muscle

Browse structure collections

About this viewer

MolViewer shows 1MVW directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.