4v93

Fitted coordinates for Lumbricus terrestris hemoglobin cryo-EM complex (EMD-2627)

Method: ELECTRON MICROSCOPY

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1. Protein Identity and Related Structures Protein Identity & Related Structures

EXTRACELLULAR GLOBIN-3

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 180	HEMOGLOBIN CHAIN D1 × 12 （O61233） EXTRACELLULAR GLOBIN-4 × 24 （P13579） EXTRACELLULAR GLOBIN-2 × 36 （P02218） HEMOGLOBIN CHAIN D1 × 24 （O61233） EXTRACELLULAR GLOBIN-4 × 12 （P13579） HEMOGLOBIN LINKER CHAIN L1 × 12 （Q9GV76） EXTRACELLULAR HEMOGLOBIN LINKER L2 SUBUNIT × 12 （Q2I743） EXTRACELLULAR HEMOGLOBIN LINKER L3 SUBUNIT × 12 （Q2I742）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	GLB3_LUMTE
Isoform	—
PDB entities	1, 7
Chains and sequence ranges	Author chain A0； PDBConstruct 1–149； UniProt 20–168 Author chain A5； PDBConstruct 1–149； UniProt 20–168 Author chain AC； PDBConstruct 1–149； UniProt 20–168 Author chain AH； PDBConstruct 1–149； UniProt 20–168 Author chain AM； PDBConstruct 1–149； UniProt 20–168 Author chain AR； PDBConstruct 1–149； UniProt 20–168 Author chain AW； PDBConstruct 1–149； UniProt 20–168 Author chain Ab； PDBConstruct 1–149； UniProt 20–168 Author chain Ag； PDBConstruct 1–149； UniProt 20–168 Author chain Al； PDBConstruct 1–149； UniProt 20–168 Author chain Aq； PDBConstruct 1–149； UniProt 20–168 Author chain Av； PDBConstruct 1–149； UniProt 20–168 Author chain B4； PDBConstruct 1–170； UniProt 1–170 Author chain BB； PDBConstruct 1–170； UniProt 1–170 Author chain BG； PDBConstruct 1–170； UniProt 1–170 Author chain BL； PDBConstruct 1–170； UniProt 1–170 Author chain BQ； PDBConstruct 1–170； UniProt 1–170 Author chain BV； PDBConstruct 1–170； UniProt 1–170 Author chain Ba； PDBConstruct 1–170； UniProt 1–170 Author chain Bf； PDBConstruct 1–170； UniProt 1–170 Author chain Bk； PDBConstruct 1–170； UniProt 1–170 Author chain Bp； PDBConstruct 1–170； UniProt 1–170 Author chain Bu； PDBConstruct 1–170； UniProt 1–170 Author chain Bz； PDBConstruct 1–170； UniProt 1–170 Author chain C3； PDBConstruct 1–170； UniProt 1–170 Author chain CA； PDBConstruct 1–170； UniProt 1–170 Author chain CF； PDBConstruct 1–170； UniProt 1–170 Author chain CK； PDBConstruct 1–170； UniProt 1–170 Author chain CP； PDBConstruct 1–170； UniProt 1–170 Author chain CU； PDBConstruct 1–170； UniProt 1–170 Author chain CZ； PDBConstruct 1–170； UniProt 1–170 Author chain Ce； PDBConstruct 1–170； UniProt 1–170 Author chain Cj； PDBConstruct 1–170； UniProt 1–170 Author chain Co； PDBConstruct 1–170； UniProt 1–170 Author chain Ct； PDBConstruct 1–170； UniProt 1–170 Author chain Cy； PDBConstruct 1–170； UniProt 1–170

HEMOGLOBIN CHAIN D1

OrganismNot specified

UniProt O61233

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 180	EXTRACELLULAR GLOBIN-3 × 12 （P11069） EXTRACELLULAR GLOBIN-4 × 24 （P13579） EXTRACELLULAR GLOBIN-2 × 36 （P02218） EXTRACELLULAR GLOBIN-4 × 12 （P13579） EXTRACELLULAR GLOBIN-3 × 24 （P11069） HEMOGLOBIN LINKER CHAIN L1 × 12 （Q9GV76） EXTRACELLULAR HEMOGLOBIN LINKER L2 SUBUNIT × 12 （Q2I743） EXTRACELLULAR HEMOGLOBIN LINKER L3 SUBUNIT × 12 （Q2I742）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	O61233_LUMTE
Isoform	—
PDB entities	2, 5
Chains and sequence ranges	Author chain A1； PDBConstruct 1–140； UniProt 19–158 Author chain A6； PDBConstruct 1–140； UniProt 19–158 Author chain AD； PDBConstruct 1–140； UniProt 19–158 Author chain AI； PDBConstruct 1–140； UniProt 19–158 Author chain AN； PDBConstruct 1–140； UniProt 19–158 Author chain AS； PDBConstruct 1–140； UniProt 19–158 Author chain AX； PDBConstruct 1–140； UniProt 19–158 Author chain Ac； PDBConstruct 1–140； UniProt 19–158 Author chain Ah； PDBConstruct 1–140； UniProt 19–158 Author chain Am； PDBConstruct 1–140； UniProt 19–158 Author chain Ar； PDBConstruct 1–140； UniProt 19–158 Author chain Aw； PDBConstruct 1–140； UniProt 19–158 Author chain B0； PDBConstruct 1–158； UniProt 1–158 Author chain B5； PDBConstruct 1–158； UniProt 1–158 Author chain BC； PDBConstruct 1–158； UniProt 1–158 Author chain BH； PDBConstruct 1–158； UniProt 1–158 Author chain BM； PDBConstruct 1–158； UniProt 1–158 Author chain BR； PDBConstruct 1–158； UniProt 1–158 Author chain BW； PDBConstruct 1–158； UniProt 1–158 Author chain Bb； PDBConstruct 1–158； UniProt 1–158 Author chain Bg； PDBConstruct 1–158； UniProt 1–158 Author chain Bl； PDBConstruct 1–158； UniProt 1–158 Author chain Bq； PDBConstruct 1–158； UniProt 1–158 Author chain Bv； PDBConstruct 1–158； UniProt 1–158 Author chain C4； PDBConstruct 1–158； UniProt 1–158 Author chain CB； PDBConstruct 1–158； UniProt 1–158 Author chain CG； PDBConstruct 1–158； UniProt 1–158 Author chain CL； PDBConstruct 1–158； UniProt 1–158 Author chain CQ； PDBConstruct 1–158； UniProt 1–158 Author chain CV； PDBConstruct 1–158； UniProt 1–158 Author chain Ca； PDBConstruct 1–158； UniProt 1–158 Author chain Cf； PDBConstruct 1–158； UniProt 1–158 Author chain Ck； PDBConstruct 1–158； UniProt 1–158 Author chain Cp； PDBConstruct 1–158； UniProt 1–158 Author chain Cu； PDBConstruct 1–158； UniProt 1–158 Author chain Cz； PDBConstruct 1–158； UniProt 1–158

EXTRACELLULAR GLOBIN-4

OrganismNot specified

UniProt P13579

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 180	EXTRACELLULAR GLOBIN-3 × 12 （P11069） HEMOGLOBIN CHAIN D1 × 12 （O61233） EXTRACELLULAR GLOBIN-2 × 36 （P02218） HEMOGLOBIN CHAIN D1 × 24 （O61233） EXTRACELLULAR GLOBIN-3 × 24 （P11069） HEMOGLOBIN LINKER CHAIN L1 × 12 （Q9GV76） EXTRACELLULAR HEMOGLOBIN LINKER L2 SUBUNIT × 12 （Q2I743） EXTRACELLULAR HEMOGLOBIN LINKER L3 SUBUNIT × 12 （Q2I742）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	GLB4_LUMTE
Isoform	—
PDB entities	3, 6
Chains and sequence ranges	Author chain A2； PDBConstruct 1–147； UniProt 5–151 Author chain A3； PDBConstruct 1–147； UniProt 5–151 Author chain A7； PDBConstruct 1–147； UniProt 5–151 Author chain AA； PDBConstruct 1–147； UniProt 5–151 Author chain AE； PDBConstruct 1–147； UniProt 5–151 Author chain AF； PDBConstruct 1–147； UniProt 5–151 Author chain AJ； PDBConstruct 1–147； UniProt 5–151 Author chain AK； PDBConstruct 1–147； UniProt 5–151 Author chain AO； PDBConstruct 1–147； UniProt 5–151 Author chain AP； PDBConstruct 1–147； UniProt 5–151 Author chain AT； PDBConstruct 1–147； UniProt 5–151 Author chain AU； PDBConstruct 1–147； UniProt 5–151 Author chain AY； PDBConstruct 1–147； UniProt 5–151 Author chain AZ； PDBConstruct 1–147； UniProt 5–151 Author chain Ad； PDBConstruct 1–147； UniProt 5–151 Author chain Ae； PDBConstruct 1–147； UniProt 5–151 Author chain Ai； PDBConstruct 1–147； UniProt 5–151 Author chain Aj； PDBConstruct 1–147； UniProt 5–151 Author chain An； PDBConstruct 1–147； UniProt 5–151 Author chain Ao； PDBConstruct 1–147； UniProt 5–151 Author chain As； PDBConstruct 1–147； UniProt 5–151 Author chain At； PDBConstruct 1–147； UniProt 5–151 Author chain Ax； PDBConstruct 1–147； UniProt 5–151 Author chain Ay； PDBConstruct 1–147； UniProt 5–151 Author chain B1； PDBConstruct 1–151； UniProt 1–151 Author chain B6； PDBConstruct 1–151； UniProt 1–151 Author chain BD； PDBConstruct 1–151； UniProt 1–151 Author chain BI； PDBConstruct 1–151； UniProt 1–151 Author chain BN； PDBConstruct 1–151； UniProt 1–151 Author chain BS； PDBConstruct 1–151； UniProt 1–151 Author chain BX； PDBConstruct 1–151； UniProt 1–151 Author chain Bc； PDBConstruct 1–151； UniProt 1–151 Author chain Bh； PDBConstruct 1–151； UniProt 1–151 Author chain Bm； PDBConstruct 1–151； UniProt 1–151 Author chain Br； PDBConstruct 1–151； UniProt 1–151 Author chain Bw； PDBConstruct 1–151； UniProt 1–151

EXTRACELLULAR GLOBIN-2

OrganismNot specified

UniProt P02218

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 180	EXTRACELLULAR GLOBIN-3 × 12 （P11069） HEMOGLOBIN CHAIN D1 × 12 （O61233） EXTRACELLULAR GLOBIN-4 × 24 （P13579） HEMOGLOBIN CHAIN D1 × 24 （O61233） EXTRACELLULAR GLOBIN-4 × 12 （P13579） EXTRACELLULAR GLOBIN-3 × 24 （P11069） HEMOGLOBIN LINKER CHAIN L1 × 12 （Q9GV76） EXTRACELLULAR HEMOGLOBIN LINKER L2 SUBUNIT × 12 （Q2I743） EXTRACELLULAR HEMOGLOBIN LINKER L3 SUBUNIT × 12 （Q2I742）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	GLB2_LUMTE
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain A4； PDBConstruct 1–145； UniProt 1–145 Author chain AB； PDBConstruct 1–145； UniProt 1–145 Author chain AG； PDBConstruct 1–145； UniProt 1–145 Author chain AL； PDBConstruct 1–145； UniProt 1–145 Author chain AQ； PDBConstruct 1–145； UniProt 1–145 Author chain AV； PDBConstruct 1–145； UniProt 1–145 Author chain Aa； PDBConstruct 1–145； UniProt 1–145 Author chain Af； PDBConstruct 1–145； UniProt 1–145 Author chain Ak； PDBConstruct 1–145； UniProt 1–145 Author chain Ap； PDBConstruct 1–145； UniProt 1–145 Author chain Au； PDBConstruct 1–145； UniProt 1–145 Author chain Az； PDBConstruct 1–145； UniProt 1–145 Author chain B2； PDBConstruct 1–145； UniProt 1–145 Author chain B3； PDBConstruct 1–145； UniProt 1–145 Author chain B7； PDBConstruct 1–145； UniProt 1–145 Author chain BA； PDBConstruct 1–145； UniProt 1–145 Author chain BE； PDBConstruct 1–145； UniProt 1–145 Author chain BF； PDBConstruct 1–145； UniProt 1–145 Author chain BJ； PDBConstruct 1–145； UniProt 1–145 Author chain BK； PDBConstruct 1–145； UniProt 1–145 Author chain BO； PDBConstruct 1–145； UniProt 1–145 Author chain BP； PDBConstruct 1–145； UniProt 1–145 Author chain BT； PDBConstruct 1–145； UniProt 1–145 Author chain BU； PDBConstruct 1–145； UniProt 1–145 Author chain BY； PDBConstruct 1–145； UniProt 1–145 Author chain BZ； PDBConstruct 1–145； UniProt 1–145 Author chain Bd； PDBConstruct 1–145； UniProt 1–145 Author chain Be； PDBConstruct 1–145； UniProt 1–145 Author chain Bi； PDBConstruct 1–145； UniProt 1–145 Author chain Bj； PDBConstruct 1–145； UniProt 1–145 Author chain Bn； PDBConstruct 1–145； UniProt 1–145 Author chain Bo； PDBConstruct 1–145； UniProt 1–145 Author chain Bs； PDBConstruct 1–145； UniProt 1–145 Author chain Bt； PDBConstruct 1–145； UniProt 1–145 Author chain Bx； PDBConstruct 1–145； UniProt 1–145 Author chain By； PDBConstruct 1–145； UniProt 1–145

HEMOGLOBIN LINKER CHAIN L1

OrganismNot specified

UniProt Q9GV76

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 180	EXTRACELLULAR GLOBIN-3 × 12 （P11069） HEMOGLOBIN CHAIN D1 × 12 （O61233） EXTRACELLULAR GLOBIN-4 × 24 （P13579） EXTRACELLULAR GLOBIN-2 × 36 （P02218） HEMOGLOBIN CHAIN D1 × 24 （O61233） EXTRACELLULAR GLOBIN-4 × 12 （P13579） EXTRACELLULAR GLOBIN-3 × 24 （P11069） EXTRACELLULAR HEMOGLOBIN LINKER L2 SUBUNIT × 12 （Q2I743） EXTRACELLULAR HEMOGLOBIN LINKER L3 SUBUNIT × 12 （Q2I742）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q9GV76_LUMTE
Isoform	—
PDB entities	8
Chains and sequence ranges	Author chain C0； PDBConstruct 1–240； UniProt 1–240 Author chain C5； PDBConstruct 1–240； UniProt 1–240 Author chain CC； PDBConstruct 1–240； UniProt 1–240 Author chain CH； PDBConstruct 1–240； UniProt 1–240 Author chain CM； PDBConstruct 1–240； UniProt 1–240 Author chain CR； PDBConstruct 1–240； UniProt 1–240 Author chain CW； PDBConstruct 1–240； UniProt 1–240 Author chain Cb； PDBConstruct 1–240； UniProt 1–240 Author chain Cg； PDBConstruct 1–240； UniProt 1–240 Author chain Cl； PDBConstruct 1–240； UniProt 1–240 Author chain Cq； PDBConstruct 1–240； UniProt 1–240 Author chain Cv； PDBConstruct 1–240； UniProt 1–240

EXTRACELLULAR HEMOGLOBIN LINKER L2 SUBUNIT

OrganismNot specified

UniProt Q2I743

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 180	EXTRACELLULAR GLOBIN-3 × 12 （P11069） HEMOGLOBIN CHAIN D1 × 12 （O61233） EXTRACELLULAR GLOBIN-4 × 24 （P13579） EXTRACELLULAR GLOBIN-2 × 36 （P02218） HEMOGLOBIN CHAIN D1 × 24 （O61233） EXTRACELLULAR GLOBIN-4 × 12 （P13579） EXTRACELLULAR GLOBIN-3 × 24 （P11069） HEMOGLOBIN LINKER CHAIN L1 × 12 （Q9GV76） EXTRACELLULAR HEMOGLOBIN LINKER L3 SUBUNIT × 12 （Q2I742）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q2I743_LUMTE
Isoform	—
PDB entities	9
Chains and sequence ranges	Author chain C1； PDBConstruct 1–288； UniProt 1–288 Author chain C6； PDBConstruct 1–288； UniProt 1–288 Author chain CD； PDBConstruct 1–288； UniProt 1–288 Author chain CI； PDBConstruct 1–288； UniProt 1–288 Author chain CN； PDBConstruct 1–288； UniProt 1–288 Author chain CS； PDBConstruct 1–288； UniProt 1–288 Author chain CX； PDBConstruct 1–288； UniProt 1–288 Author chain Cc； PDBConstruct 1–288； UniProt 1–288 Author chain Ch； PDBConstruct 1–288； UniProt 1–288 Author chain Cm； PDBConstruct 1–288； UniProt 1–288 Author chain Cr； PDBConstruct 1–288； UniProt 1–288 Author chain Cw； PDBConstruct 1–288； UniProt 1–288

EXTRACELLULAR HEMOGLOBIN LINKER L3 SUBUNIT

OrganismNot specified

UniProt Q2I742

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 180	EXTRACELLULAR GLOBIN-3 × 12 （P11069） HEMOGLOBIN CHAIN D1 × 12 （O61233） EXTRACELLULAR GLOBIN-4 × 24 （P13579） EXTRACELLULAR GLOBIN-2 × 36 （P02218） HEMOGLOBIN CHAIN D1 × 24 （O61233） EXTRACELLULAR GLOBIN-4 × 12 （P13579） EXTRACELLULAR GLOBIN-3 × 24 （P11069） HEMOGLOBIN LINKER CHAIN L1 × 12 （Q9GV76） EXTRACELLULAR HEMOGLOBIN LINKER L2 SUBUNIT × 12 （Q2I743）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q2I742_LUMTE
Isoform	—
PDB entities	10
Chains and sequence ranges	Author chain C2； PDBConstruct 1–240； UniProt 1–240 Author chain C7； PDBConstruct 1–240； UniProt 1–240 Author chain CE； PDBConstruct 1–240； UniProt 1–240 Author chain CJ； PDBConstruct 1–240； UniProt 1–240 Author chain CO； PDBConstruct 1–240； UniProt 1–240 Author chain CT； PDBConstruct 1–240； UniProt 1–240 Author chain CY； PDBConstruct 1–240； UniProt 1–240 Author chain Cd； PDBConstruct 1–240； UniProt 1–240 Author chain Ci； PDBConstruct 1–240； UniProt 1–240 Author chain Cn； PDBConstruct 1–240； UniProt 1–240 Author chain Cs； PDBConstruct 1–240； UniProt 1–240 Author chain Cx； PDBConstruct 1–240； UniProt 1–240

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	4v93
Deposition date deposition_date	2014-04-16
Structure title title	Fitted coordinates for Lumbricus terrestris hemoglobin cryo-EM complex (EMD-2627)
Keywords keywords	TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

4v93__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

4v93__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

4v93__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	0.00 Å
Rg (electron density)	114.70 Å
Total Rg	114.70 Å
Atom count	231000
Residues	28740
Excluded volume	4071400 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`4v93__assembly_1__model_1`	180-meric （180）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (10)

Entity 1 Entity 1 polymer

Description description	EXTRACELLULAR GLOBIN-3
Molecular weight formula_weight	16902.4 kDa
Source method src_method	nat
Copy count entity_count	12

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A0,A5,AC,AH,AM,AR,AW,Ab,Ag,Al,Aq,Av
Atom count atom_count	231000

HEHCCSEEDHRIVQKQWDILWRDTESSKIKIGFGRLLLTKLAKDIPEVNDLFKRVDIEHAEGPKFSAHALRILNGLDLAINLLDDPPALDAALDHLAHQHEVREGVQKAHFKKFGEILATGLPQVLDDYDALAWKSCLKGILTKISSRL

Entity 2 Entity 2 polymer

Description description	HEMOGLOBIN CHAIN D1
Molecular weight formula_weight	15988.3 kDa
Source method src_method	nat
Copy count entity_count	12

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A1,A6,AD,AI,AN,AS,AX,Ac,Ah,Am,Ar,Aw

ECLVTESLKVKLQWASAFGHAHERVAFGLELWRDIIDDHPEIKAPFSRVRGDNIYSPEFGAHSQRVLSGLDITISMLDTPDMLAAQLAHLKVQHVERNLKPEFFDIFLKHLLHVLGDRLGTHFDFGAWHDCVDQIIDGIK

Entity 3 Entity 3 polymer

Description description	EXTRACELLULAR GLOBIN-4
Molecular weight formula_weight	17136.6 kDa
Source method src_method	nat
Copy count entity_count	24

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A2,A3,A7,AA,AE,AF,AJ,AK,AO,AP,AT,AU,AY,AZ,Ad,Ae,Ai,Aj,An,Ao,As,At,Ax,Ay

DCCSYEDRREIRHIWDDVWSSSFTDRRVAIVRAVFDDLFKHYPTSKALFERVKIDEPESGEFKSHLVRVANGLKLLINLLDDTLVLQSHLGHLADQHIQRKGVTKEYFRGIGEAFARVLPQVLSCFNVDAWNRCFHRLVARIAKDLP

Entity 4 Entity 4 polymer

Description description	EXTRACELLULAR GLOBIN-2
Molecular weight formula_weight	16268.2 kDa
Source method src_method	nat
Copy count entity_count	36

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A4,AB,AG,AL,AQ,AV,Aa,Af,Ak,Ap,Au,Az,B2,B3,B7,BA,BE,BF,BJ,BK,BO,BP,BT,BU,BY,BZ,Bd,Be,Bi,Bj,Bn,Bo,Bs,Bt,Bx,By

KKQCGVLEGLKVKSEWGRAYGSGHDREAFSQAIWRATFAQVPESRSLFKRVHGDDTSHPAFIAHADRVLGGLDIAISTLDQPATLKEELDHLQVQHEGRKIPDNYFDAFKTAILHVVAAQLGRCYDREAWDACIDHIEDGIKGHH

Entity 5 Entity 5 polymer

Description description	HEMOGLOBIN CHAIN D1
Molecular weight formula_weight	17948.7 kDa
Source method src_method	nat
Copy count entity_count	24

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B0,B5,BC,BH,BM,BR,BW,Bb,Bg,Bl,Bq,Bv,C4,CB,CG,CL,CQ,CV,Ca,Cf,Ck,Cp,Cu,Cz

MKVFVAVFLLAFATYVSAECLVTESLKVKLQWASAFGHAHERVAFGLELWRDIIDDHPEIKAPFSRVRGDNIYSPEFGAHSQRVLSGLDITISMLDTPDMLAAQLAHLKVQHVERNLKPEFFDIFLKHLLHVLGDRLGTHFDFGAWHDCVDQIIDGIK

Entity 6 Entity 6 polymer

Description description	EXTRACELLULAR GLOBIN-4
Molecular weight formula_weight	17567.0 kDa
Source method src_method	nat
Copy count entity_count	12

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B1,B6,BD,BI,BN,BS,BX,Bc,Bh,Bm,Br,Bw

ADDEDCCSYEDRREIRHIWDDVWSSSFTDRRVAIVRAVFDDLFKHYPTSKALFERVKIDEPESGEFKSHLVRVANGLKLLINLLDDTLVLQSHLGHLADQHIQRKGVTKEYFRGIGEAFARVLPQVLSCFNVDAWNRCFHRLVARIAKDLP

Entity 7 Entity 7 polymer

Description description	EXTRACELLULAR GLOBIN-3
Molecular weight formula_weight	19126.1 kDa
Source method src_method	nat
Copy count entity_count	24

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B4,BB,BG,BL,BQ,BV,Ba,Bf,Bk,Bp,Bu,Bz,C3,CA,CF,CK,CP,CU,CZ,Ce,Cj,Co,Ct,Cy

MLRQLLVLVGLAVVCLADEHEHCCSEEDHRIVQKQWDILWRDTESSKIKIGFGRLLLTKLAKDIPEVNDLFKRVDIEHAEGPKFSAHALRILNGLDLAINLLDDPPALDAALDHLAHQHEVREGVQKAHFKKFGEILATGLPQVLDDYDALAWKSCLKGILTKISSRLNA

Entity 8 Entity 8 polymer

Description description	HEMOGLOBIN LINKER CHAIN L1
Molecular weight formula_weight	27460.7 kDa
Source method src_method	nat
Copy count entity_count	12

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C0,C5,CC,CH,CM,CR,CW,Cb,Cg,Cl,Cq,Cv

MWYVLGLMLVGLAAGASDPYQERRFQYLVKNQNLHIDYLAKKLHDIEEEYNKLTHDVDKKTIRQLKARISNLEEHHCDEHESECRGDVPECIHDLLFCDGEKDCRDGSDEDPETCSLNITHVGSSYTGLATWTSCEDLNPDHAIVTITAAHRKSFFPNRVWLRATLSYELDEHDHTVSTTQLRGFYNFGKRELLLAPLKGQSEGYGVICDFNLGDDDHADCKIVVPSSLFVCAHFNAQRY

Entity 9 Entity 9 polymer

Description description	EXTRACELLULAR HEMOGLOBIN LINKER L2 SUBUNIT
Molecular weight formula_weight	32075.5 kDa
Source method src_method	nat
Copy count entity_count	12

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C1,C6,CD,CI,CN,CS,CX,Cc,Ch,Cm,Cr,Cw

MLRLLLLSALSGLILADHHQPSGGGGGSYGGGGGGGGPFGRLFSDQLDPRLGANAFLIIRLDRIIEKLRTKLDEAEKIDPEHFVSEIDARVTKIEGTHCEKRTFQCGGNEQECISDLLVCDGHKDCHNAHDEDPDVCDTSVVKAGNVFSGTSTWHGCLAREDHVTRITITASKRRKFFTARIWLRALVESELERHGENVTSSFNAKGYYNFASRRLILLPTDDHDDHLAVVCSFNRGDNERAECHRVTEATLHQCADLFVTLEEHDDHDDHDDDHHDDHGKHHGGKHH

Entity 10 Entity 10 polymer

Description description	EXTRACELLULAR HEMOGLOBIN LINKER L3 SUBUNIT
Molecular weight formula_weight	26877.9 kDa
Source method src_method	nat
Copy count entity_count	12

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C2,C7,CE,CJ,CO,CT,CY,Cd,Ci,Cn,Cs,Cx

MKSLGLLLAALAVVVTLASADSPPAQSHDEIIDKLIERTNKITTSISHVESLLDDRLDPKRIRKAGSLRHRVEELEDPSCDEHEHQCGGDDPQCISKLFVCDGHNDCRNGEDEKDCTLPTKAGDKFIGDVCFDHCTKRRPEHMTLAFESSSIAAFFTPIADLHVHIEIESETDEDESEVSMPADGEYSFADHRLTIHPPEEDGLGLVGEFDGYNFDRFVGHIVHELSEEVCAEFIFHRKK

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	8.100 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

Resolution resolution	8.10 Å
Resolution测定Method resolution_method	—
颗粒数 num_particles	4500

Fitted coordinates for Lumbricus terrestris hemoglobin cryo-EM complex (EMD-2627)

1. Protein Identity and Related Structures Protein Identity & Related Structures

EXTRACELLULAR GLOBIN-3

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

HEMOGLOBIN CHAIN D1

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

EXTRACELLULAR GLOBIN-4

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

EXTRACELLULAR GLOBIN-2

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

HEMOGLOBIN LINKER CHAIN L1

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

EXTRACELLULAR HEMOGLOBIN LINKER L2 SUBUNIT

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

EXTRACELLULAR HEMOGLOBIN LINKER L3 SUBUNIT

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

4v93__assembly_1__model_1

4v93__assembly_1__model_1 | I(q)

4v93__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (10)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 polymer

Polymer Polymer

Entity 5 Entity 5 polymer

Polymer Polymer

Entity 6 Entity 6 polymer