1NR4: Thymus and activation-regulated chemokine

High resolution crystal structures of thymus and activation-regulated chemokine. Determined by X-ray diffraction at 1.72 Å resolution. Released 5 Aug 2003.

Method: X-ray diffraction
Resolution: 1.72 Å
Chains: 8
Atoms: 4,882
Mol. weight: 65.35 kDa
Released: 5 Aug 2003

Explore 1NR4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1NR4 contains 20 α-helices and 38 β-strands across 8 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: 3 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	6	1	1
β-strand	9-11	3	2
α-helix	21-23	3
β-strand	24-29	6	3
α-helix	30-31	2
β-strand	39-43	5	3
β-strand	48-51	4	3
α-helix	56-67	12

Chain B: 2 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	9-11	3	2
β-strand	13	1	1
α-helix	21-23	3
β-strand	24-29	6	4
β-strand	39-43	5	4
β-strand	48-51	4	4
α-helix	56-69	14

Chain C: 3 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	6	1	5
β-strand	9-13	5	6
α-helix	21-23	3
β-strand	24-29	6	7
α-helix	30-31	2
β-strand	39-43	5	7
β-strand	48-51	4	7
α-helix	56-67	12

Chain D: 2 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	8-11	4	6
β-strand	13	1	5
α-helix	21-23	3
β-strand	24-29	6	8
β-strand	39-43	5	8
β-strand	48-51	4	8
α-helix	56-68	13

Chain E: 3 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	6	1	9
β-strand	9-11	3	10
α-helix	21-23	3
β-strand	24-29	6	11
α-helix	30-31	2
β-strand	39-43	5	11
β-strand	48-51	4	11
α-helix	56-69	14

Chain F: 3 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	9-11	3	10
β-strand	13	1	9
α-helix	21-23	3
β-strand	24-29	6	12
α-helix	38	1
β-strand	39-43	5	12
β-strand	48-51	4	12
α-helix	56-69	14

Chain G: 2 helices, 4 β-strands

Element	Residues	Length	Sheet
β-strand	9-11	3	13
α-helix	21-23	3
β-strand	24-29	6	14
β-strand	39-43	5	14
β-strand	48-51	4	14
α-helix	56-67	12

Chain H: 2 helices, 4 β-strands

Element	Residues	Length	Sheet
β-strand	9-11	3	13
α-helix	21-23	3
β-strand	24-29	6	15
β-strand	39-43	5	15
β-strand	48-51	4	15
α-helix	56-69	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Thymus and activation-regulated chemokine	A, B, C, D, E, F, G, H	protein	71		Q92583 (AlphaFold model)

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

>1NR4_1 Thymus and activation-regulated chemokine (chains A, B, C, D, E, F, G, H)
ARGTNVGRECCLEYFKGAIPLRKLKTWYQTSEDCSRDAIVFVTVQGRAICSDPNNKRVKN
AVKYLQSLERS

Primary citation

Structures of thymus and activation-regulated chemokine (TARC). Asojo, O.A., Boulegue, C., Hoover, D.M. et al. Acta Crystallogr D Biol Crystallogr (2003) 59:1165-1173. DOI 10.1107/S0907444903009454 · PubMed

Other PDB entries of the same protein (UniProt Q92583 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7S4N 1.65 Å, Crystal structure of the tick evasin EVA-P974 complexed to human chemokine CCL17
5WK3 1.9 Å, Crystal structure of the complex between CCL17 and M116 FAB
7SCV 2.01 Å, Crystal Structure of the Tick Evasin EVA-AAM1001 Complexed to Human Chemokine CCL17
8FJ2 2.07 Å, Crystal Structure of the Tick Evasin EVA-AAM1001(C8) Complexed to Human Chemokine CCL17
8SKK 2.1 Å, Crystal Structure of the Tick Evasin EVA-AAM1001(L39P) Complexed to Human Chemokine CCL17
1NR2 2.18 Å, High resolution crystal structures of thymus and activation-regulated chemokine

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