PDB-1xk4: Crystal structure of human calprotectin(S100A8/S100A9)

ID or keywords:

Entry

Database: PDB / ID: 1xk4

Title

Crystal structure of human calprotectin(S100A8/S100A9)

Components

Calgranulin A
Calgranulin BCalgranulin

Keywords

METAL BINDING PROTEIN / S100 family /

heterotetramer

Function / homology

Function and homology information

S100A9 complex / regulation of integrin biosynthetic process / sequestering of zinc ion /

calprotectin complex / neutrophil aggregation / positive regulation of peptide secretion / regulation of respiratory burst involved in inflammatory response / modulation of process of another organism /

autocrine signaling /

Toll-like receptor 4 binding ...

S100A9 complex / regulation of integrin biosynthetic process / sequestering of zinc ion /

calprotectin complex / neutrophil aggregation / positive regulation of peptide secretion / regulation of respiratory burst involved in inflammatory response / modulation of process of another organism /

autocrine signaling /

Toll-like receptor 4 binding / chronic inflammatory response / peptidyl-cysteine S-trans-nitrosylation / Metal sequestration by antimicrobial proteins / leukocyte migration involved in inflammatory response / peptide secretion / Regulation of TLR by endogenous ligand /

RAGE receptor binding / astrocyte development / MyD88 deficiency (TLR2/4) /

arachidonic acid binding / intermediate filament cytoskeleton / IRAK4 deficiency (TLR2/4) / MyD88:MAL(TIRAP) cascade initiated on plasma membrane / response to zinc ion /

regulation of toll-like receptor signaling pathway / regulation of cytoskeleton organization / peptidyl-cysteine S-nitrosylation /

antioxidant activity / RHO GTPases Activate NADPH Oxidases / endothelial cell migration / defense response to fungus / positive regulation of intrinsic apoptotic signaling pathway /

neutrophil chemotaxis /

autophagy / positive regulation of neuron projection development / positive regulation of inflammatory response / activation of cysteine-type endopeptidase activity involved in apoptotic process / calcium-dependent protein binding / antimicrobial humoral immune response mediated by antimicrobial peptide / cell-cell signaling / positive regulation of NF-kappaB transcription factor activity / ER-Phagosome pathway / positive regulation of cell growth /

microtubule binding / secretory granule lumen / collagen-containing extracellular matrix / response to ethanol / response to lipopolysaccharide /

cytoskeleton / defense response to bacterium /

inflammatory response /

innate immune response / apoptotic process /

calcium ion binding / Neutrophil degranulation /

extracellular space / extracellular exosome / zinc ion binding / extracellular region /

nucleus /

plasma membrane /

cytosol /

cytoplasm
Similarity search - Function

Biological species

Homo sapiens (human)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 1.8 Å

Authors

Korndoerfer, I.P. / Brueckner, F. / Skerra, A.

Citation

Journal: J.Mol.Biol. / Year: 2007
Title: The crystal structure of the human (S100A8/S100A9)2 heterotetramer, calprotectin, illustrates how conformational changes of interacting alpha-helices can determine specific association of two EF-hand proteins
Authors: Korndoerfer, I.P. / Brueckner, F. / Skerra, A.

History

Deposition	Sep 26, 2004	Deposition site: RCSB / Processing site: PDBJ
Revision 1.0	Oct 18, 2005	Provider: repository / Type: Initial release
Revision 1.1	Apr 30, 2008	Group: Version format compliance
Revision 1.2	Jul 13, 2011	Group: Advisory / Version format compliance
Revision 1.3	Feb 25, 2015	Group: Database references
Revision 1.4	Oct 25, 2023	Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim / struct_ref_seq_dif / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_seq_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	1xk4.cif.gz	272.7 KB	Display	PDBx/mmCIF format
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PDBx/mmJSON format	1xk4.json.gz		Tree view	PDBx/mmJSON format
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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/xk/1xk4 ftp://data.pdbj.org/pub/pdb/validation_reports/xk/1xk4	HTTPS FTP

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Related structure data

Related structure data	1irjS 1mr8S S: Starting model for refinement
Similar structure data	4l56-d 4rx1-d 3e7d-2 2o9o-d 6lbk-1 6nfo-1 4o68-d 6yry-d 4lkv-3 4ggf-2 Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Similarity search - Function & homologyF&H Search Similarity search - FunctionF&H Search Similarity search - HomologyF&H Search

Related structure data

1irjS

1mr8S

S: Starting model for refinement

Similar structure data

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#193 - Jan 2016 Siderocalin similarity (1) #143 - Nov 2011 Toll-like Receptors similarity (4) #83 - Nov 2006 Fibrin similarity (4) #134 - Feb 2011 Integrin similarity (4) #209 - May 2017 Tissue Transglutaminase and Celiac Disease similarity (4) #245 - May 2020 Spliceosomes similarity (1) #129 - Sep 2010 Isocitrate Dehydrogenase similarity (1) #154 - Oct 2012 Citric Acid Cycle similarity (1) #191 - Nov 2015 Glutamate-gated Chloride Receptors similarity (1) #215 - Nov 2017 Aspartate Transcarbamoylase similarity (1) #258 - Jun 2021 Glucocorticoid Receptor and Dexamethasone similarity (1) #89 - May 2007 Aconitase and Iron Regulatory Protein 1 similarity (1)

PDB pages

PDBj /

wwPDB /

NCBI

Related items in Molecule of the Month

#193 - Jan 2016
Siderocalin
similarity (1)
#143 - Nov 2011
Toll-like Receptors
similarity (4)
#83 - Nov 2006
Fibrin
similarity (4)
#134 - Feb 2011
Integrin
similarity (4)
#209 - May 2017
Tissue Transglutaminase and Celiac Disease
similarity (4)
#245 - May 2020
Spliceosomes
similarity (1)
#129 - Sep 2010
Isocitrate Dehydrogenase
similarity (1)
#154 - Oct 2012
Citric Acid Cycle
similarity (1)
#191 - Nov 2015
Glutamate-gated Chloride Receptors
similarity (1)
#215 - Nov 2017
Aspartate Transcarbamoylase
similarity (1)
#258 - Jun 2021
Glucocorticoid Receptor and Dexamethasone
similarity (1)
#89 - May 2007
Aconitase and Iron Regulatory Protein 1
similarity (1)

Deposited unit

A: Calgranulin A

B: Calgranulin A

C: Calgranulin B

D: Calgranulin B

E: Calgranulin A

F: Calgranulin A

G: Calgranulin B

H: Calgranulin B

I: Calgranulin A

J: Calgranulin A

K: Calgranulin B

L: Calgranulin B

hetero molecules

145 kDa, 12 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: Calgranulin A

B: Calgranulin A

C: Calgranulin B

D: Calgranulin B

hetero molecules

defined by author&software
48.3 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

E: Calgranulin A

F: Calgranulin A

G: Calgranulin B

H: Calgranulin B

hetero molecules

defined by author&software
48.5 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

3

I: Calgranulin A

J: Calgranulin A

K: Calgranulin B

L: Calgranulin B

hetero molecules

defined by author&software
48.3 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	48.509, 78.697, 177.411
Angle α, β, γ (deg.)	90.00, 94.94, 90.00
Int Tables number	4
Space group name H-M	P12₁1

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Dom-ID	Component-ID	Ens-ID	Beg auth comp-ID	Beg label comp-ID	End auth comp-ID	End label comp-ID	Refine code	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	1	MET	MET	MET	MET	1	A	A	1	1
2	1	1	MET	MET	MET	MET	1	B	B	1	1
3	1	1	MET	MET	MET	MET	1	E	E	1	1
4	1	1	MET	MET	MET	MET	1	F	F	1	1
5	1	1	MET	MET	MET	MET	1	I	I	1	1
6	1	1	MET	MET	MET	MET	1	J	J	1	1
7	2	1	LEU	LEU	LEU	LEU	4	A	A	2	2
8	2	1	LEU	LEU	LEU	LEU	4	B	B	2	2
9	2	1	LEU	LEU	LEU	LEU	4	E	E	2	2
10	2	1	LEU	LEU	LEU	LEU	4	F	F	2	2
11	2	1	LEU	LEU	LEU	LEU	4	I	I	2	2
12	2	1	LEU	LEU	LEU	LEU	4	J	J	2	2
13	3	1	THR	THR	THR	THR	5	A	A	3	3
14	3	1	THR	THR	THR	THR	5	B	B	3	3
15	3	1	THR	THR	THR	THR	5	E	E	3	3
16	3	1	THR	THR	THR	THR	5	F	F	3	3
17	3	1	THR	THR	THR	THR	5	I	I	3	3
18	3	1	THR	THR	THR	THR	5	J	J	3	3
19	4	1	GLU	GLU	GLU	GLU	4	A	A	4	4
20	4	1	GLU	GLU	GLU	GLU	4	B	B	4	4
21	4	1	GLU	GLU	GLU	GLU	4	E	E	4	4
22	4	1	GLU	GLU	GLU	GLU	4	F	F	4	4
23	4	1	GLU	GLU	GLU	GLU	4	I	I	4	4
24	4	1	GLU	GLU	GLU	GLU	4	J	J	4	4
25	5	1	LEU	LEU	GLU	GLU	5	A	A	5 - 6	5 - 6
26	5	1	LEU	LEU	GLU	GLU	5	B	B	5 - 6	5 - 6
27	5	1	LEU	LEU	GLU	GLU	5	E	E	5 - 6	5 - 6
28	5	1	LEU	LEU	GLU	GLU	5	F	F	5 - 6	5 - 6
29	5	1	LEU	LEU	GLU	GLU	5	I	I	5 - 6	5 - 6
30	5	1	LEU	LEU	GLU	GLU	5	J	J	5 - 6	5 - 6
31	6	1	LYS	LYS	LYS	LYS	1	A	A	7	7
32	6	1	LYS	LYS	LYS	LYS	1	B	B	7	7
33	6	1	LYS	LYS	LYS	LYS	1	E	E	7	7
34	6	1	LYS	LYS	LYS	LYS	1	F	F	7	7
35	6	1	LYS	LYS	LYS	LYS	1	I	I	7	7
36	6	1	LYS	LYS	LYS	LYS	1	J	J	7	7
37	7	1	ALA	ALA	ALA	ALA	5	A	A	8	8
38	7	1	ALA	ALA	ALA	ALA	5	B	B	8	8
39	7	1	ALA	ALA	ALA	ALA	5	E	E	8	8
40	7	1	ALA	ALA	ALA	ALA	5	F	F	8	8
41	7	1	ALA	ALA	ALA	ALA	5	I	I	8	8
42	7	1	ALA	ALA	ALA	ALA	5	J	J	8	8
43	8	1	LEU	LEU	LEU	LEU	4	A	A	9	9
44	8	1	LEU	LEU	LEU	LEU	4	B	B	9	9
45	8	1	LEU	LEU	LEU	LEU	4	E	E	9	9
46	8	1	LEU	LEU	LEU	LEU	4	F	F	9	9
47	8	1	LEU	LEU	LEU	LEU	4	I	I	9	9
48	8	1	LEU	LEU	LEU	LEU	4	J	J	9	9
49	9	1	ASN	ASN	ILE	ILE	5	A	A	10 - 13	10 - 13
50	9	1	ASN	ASN	ILE	ILE	5	B	B	10 - 13	10 - 13
51	9	1	ASN	ASN	ILE	ILE	5	E	E	10 - 13	10 - 13
52	9	1	ASN	ASN	ILE	ILE	5	F	F	10 - 13	10 - 13
53	9	1	ASN	ASN	ILE	ILE	5	I	I	10 - 13	10 - 13
54	9	1	ASN	ASN	ILE	ILE	5	J	J	10 - 13	10 - 13
55	10	1	VAL	VAL	HIS	HIS	5	A	A	15 - 17	15 - 17
56	10	1	VAL	VAL	HIS	HIS	5	B	B	15 - 17	15 - 17
57	10	1	VAL	VAL	HIS	HIS	5	E	E	15 - 17	15 - 17
58	10	1	VAL	VAL	HIS	HIS	5	F	F	15 - 17	15 - 17
59	10	1	VAL	VAL	HIS	HIS	5	I	I	15 - 17	15 - 17
60	10	1	VAL	VAL	HIS	HIS	5	J	J	15 - 17	15 - 17
61	11	1	LYS	LYS	LYS	LYS	1	A	A	18	18
62	11	1	LYS	LYS	LYS	LYS	1	B	B	18	18
63	11	1	LYS	LYS	LYS	LYS	1	E	E	18	18
64	11	1	LYS	LYS	LYS	LYS	1	F	F	18	18
65	11	1	LYS	LYS	LYS	LYS	1	I	I	18	18
66	11	1	LYS	LYS	LYS	LYS	1	J	J	18	18
67	12	1	TYR	TYR	SER	SER	5	A	A	19 - 20	19 - 20
68	12	1	TYR	TYR	SER	SER	5	B	B	19 - 20	19 - 20
69	12	1	TYR	TYR	SER	SER	5	E	E	19 - 20	19 - 20
70	12	1	TYR	TYR	SER	SER	5	F	F	19 - 20	19 - 20
71	12	1	TYR	TYR	SER	SER	5	I	I	19 - 20	19 - 20
72	12	1	TYR	TYR	SER	SER	5	J	J	19 - 20	19 - 20
73	13	1	GLY	GLY	TYR	TYR	5	A	A	24 - 30	24 - 30
74	13	1	GLY	GLY	TYR	TYR	5	B	B	24 - 30	24 - 30
75	13	1	GLY	GLY	TYR	TYR	5	E	E	24 - 30	24 - 30
76	13	1	GLY	GLY	TYR	TYR	5	F	F	24 - 30	24 - 30
77	13	1	GLY	GLY	TYR	TYR	5	I	I	24 - 30	24 - 30
78	13	1	GLY	GLY	TYR	TYR	5	J	J	24 - 30	24 - 30
79	14	1	ASP	ASP	LEU	LEU	5	A	A	33 - 34	33 - 34
80	14	1	ASP	ASP	LEU	LEU	5	B	B	33 - 34	33 - 34
81	14	1	ASP	ASP	LEU	LEU	5	E	E	33 - 34	33 - 34
82	14	1	ASP	ASP	LEU	LEU	5	F	F	33 - 34	33 - 34
83	14	1	ASP	ASP	LEU	LEU	5	I	I	33 - 34	33 - 34
84	14	1	ASP	ASP	LEU	LEU	5	J	J	33 - 34	33 - 34
85	15	1	LYS	LYS	LYS	LYS	1	A	A	35 - 36	35 - 36
86	15	1	LYS	LYS	LYS	LYS	1	B	B	35 - 36	35 - 36
87	15	1	LYS	LYS	LYS	LYS	1	E	E	35 - 36	35 - 36
88	15	1	LYS	LYS	LYS	LYS	1	F	F	35 - 36	35 - 36
89	15	1	LYS	LYS	LYS	LYS	1	I	I	35 - 36	35 - 36
90	15	1	LYS	LYS	LYS	LYS	1	J	J	35 - 36	35 - 36
91	16	1	LEU	LEU	LEU	LEU	5	A	A	37 - 38	37 - 38
92	16	1	LEU	LEU	LEU	LEU	5	B	B	37 - 38	37 - 38
93	16	1	LEU	LEU	LEU	LEU	5	E	E	37 - 38	37 - 38
94	16	1	LEU	LEU	LEU	LEU	5	F	F	37 - 38	37 - 38
95	16	1	LEU	LEU	LEU	LEU	5	I	I	37 - 38	37 - 38
96	16	1	LEU	LEU	LEU	LEU	5	J	J	37 - 38	37 - 38
97	17	1	GLN	GLN	GLN	GLN	4	A	A	44	44
98	17	1	GLN	GLN	GLN	GLN	4	B	B	44	44
99	17	1	GLN	GLN	GLN	GLN	4	E	E	44	44
100	17	1	GLN	GLN	GLN	GLN	4	F	F	44	44
101	17	1	GLN	GLN	GLN	GLN	4	I	I	44	44
102	17	1	GLN	GLN	GLN	GLN	4	J	J	44	44
103	18	1	TYR	TYR	ILE	ILE	5	A	A	45 - 46	45 - 46
104	18	1	TYR	TYR	ILE	ILE	5	B	B	45 - 46	45 - 46
105	18	1	TYR	TYR	ILE	ILE	5	E	E	45 - 46	45 - 46
106	18	1	TYR	TYR	ILE	ILE	5	F	F	45 - 46	45 - 46
107	18	1	TYR	TYR	ILE	ILE	5	I	I	45 - 46	45 - 46
108	18	1	TYR	TYR	ILE	ILE	5	J	J	45 - 46	45 - 46
109	19	1	ARG	ARG	LYS	LYS	1	A	A	47 - 49	47 - 49
110	19	1	ARG	ARG	LYS	LYS	1	B	B	47 - 49	47 - 49
111	19	1	ARG	ARG	LYS	LYS	1	E	E	47 - 49	47 - 49
112	19	1	ARG	ARG	LYS	LYS	1	F	F	47 - 49	47 - 49
113	19	1	ARG	ARG	LYS	LYS	1	I	I	47 - 49	47 - 49
114	19	1	ARG	ARG	LYS	LYS	1	J	J	47 - 49	47 - 49
115	20	1	GLY	GLY	PHE	PHE	5	A	A	50 - 55	50 - 55
116	20	1	GLY	GLY	PHE	PHE	5	B	B	50 - 55	50 - 55
117	20	1	GLY	GLY	PHE	PHE	5	E	E	50 - 55	50 - 55
118	20	1	GLY	GLY	PHE	PHE	5	F	F	50 - 55	50 - 55
119	20	1	GLY	GLY	PHE	PHE	5	I	I	50 - 55	50 - 55
120	20	1	GLY	GLY	PHE	PHE	5	J	J	50 - 55	50 - 55
121	21	1	LYS	LYS	GLU	GLU	1	A	A	56 - 57	56 - 57
122	21	1	LYS	LYS	GLU	GLU	1	B	B	56 - 57	56 - 57
123	21	1	LYS	LYS	GLU	GLU	1	E	E	56 - 57	56 - 57
124	21	1	LYS	LYS	GLU	GLU	1	F	F	56 - 57	56 - 57
125	21	1	LYS	LYS	GLU	GLU	1	I	I	56 - 57	56 - 57
126	21	1	LYS	LYS	GLU	GLU	1	J	J	56 - 57	56 - 57
127	22	1	LEU	LEU	PHE	PHE	5	A	A	58 - 68	58 - 68
128	22	1	LEU	LEU	PHE	PHE	5	B	B	58 - 68	58 - 68
129	22	1	LEU	LEU	PHE	PHE	5	E	E	58 - 68	58 - 68
130	22	1	LEU	LEU	PHE	PHE	5	F	F	58 - 68	58 - 68
131	22	1	LEU	LEU	PHE	PHE	5	I	I	58 - 68	58 - 68
132	22	1	LEU	LEU	PHE	PHE	5	J	J	58 - 68	58 - 68
133	23	1	GLN	GLN	GLN	GLN	1	A	A	69	69
134	23	1	GLN	GLN	GLN	GLN	1	B	B	69	69
135	23	1	GLN	GLN	GLN	GLN	1	E	E	69	69
136	23	1	GLN	GLN	GLN	GLN	1	F	F	69	69
137	23	1	GLN	GLN	GLN	GLN	1	I	I	69	69
138	23	1	GLN	GLN	GLN	GLN	1	J	J	69	69
139	24	1	GLU	GLU	ILE	ILE	5	A	A	70 - 76	70 - 76
140	24	1	GLU	GLU	ILE	ILE	5	B	B	70 - 76	70 - 76
141	24	1	GLU	GLU	ILE	ILE	5	E	E	70 - 76	70 - 76
142	24	1	GLU	GLU	ILE	ILE	5	F	F	70 - 76	70 - 76
143	24	1	GLU	GLU	ILE	ILE	5	I	I	70 - 76	70 - 76
144	24	1	GLU	GLU	ILE	ILE	5	J	J	70 - 76	70 - 76
145	25	1	MET	MET	HIS	HIS	5	A	A	78 - 83	78 - 83
146	25	1	MET	MET	HIS	HIS	5	B	B	78 - 83	78 - 83
147	25	1	MET	MET	HIS	HIS	5	E	E	78 - 83	78 - 83
148	25	1	MET	MET	HIS	HIS	5	F	F	78 - 83	78 - 83
149	25	1	MET	MET	HIS	HIS	5	I	I	78 - 83	78 - 83
150	25	1	MET	MET	HIS	HIS	5	J	J	78 - 83	78 - 83
151	26	1	LYS	LYS	HIS	HIS	1	A	A	84 - 87	84 - 87
152	26	1	LYS	LYS	GLU	GLU	1	B	B	84 - 88	84 - 88
153	26	1	LYS	LYS	GLU	GLU	1	E	E	84 - 88	84 - 88
154	26	1	LYS	LYS	HIS	HIS	1	F	F	84 - 87	84 - 87
155	26	1	LYS	LYS	HIS	HIS	1	I	I	84 - 87	84 - 87
156	26	1	LYS	LYS	GLU	GLU	1	J	J	84 - 88	84 - 88
157	27	1	ILE	ILE	ILE	ILE	5	A	A	22	22
158	27	1	ILE	ILE	ILE	ILE	5	B	B	22	22
159	27	1	ILE	ILE	ILE	ILE	5	E	E	22	22
160	27	1	ILE	ILE	ILE	ILE	5	F	F	22	22
161	27	1	ILE	ILE	ILE	ILE	5	I	I	22	22
162	27	1	ILE	ILE	ILE	ILE	5	J	J	22	22
163	28	1	GLU	GLU	GLU	GLU	1	A	A	39	39
164	28	1	GLU	GLU	GLU	GLU	1	B	B	39	39
165	28	1	GLU	GLU	GLU	GLU	1	E	E	39	39
166	28	1	GLU	GLU	GLU	GLU	1	F	F	39	39
167	28	1	GLU	GLU	GLU	GLU	1	I	I	39	39
168	28	1	GLU	GLU	GLU	GLU	1	J	J	39	39
169	29	1	THR	THR	GLU	GLU	5	A	A	40 - 41	40 - 41
170	29	1	THR	THR	GLU	GLU	5	B	B	40 - 41	40 - 41
171	29	1	THR	THR	GLU	GLU	5	E	E	40 - 41	40 - 41
172	29	1	THR	THR	GLU	GLU	5	F	F	40 - 41	40 - 41
173	29	1	THR	THR	GLU	GLU	5	I	I	40 - 41	40 - 41
174	29	1	THR	THR	GLU	GLU	5	J	J	40 - 41	40 - 41
175	30	1	LYS	LYS	LYS	LYS	4	A	A	77	77
176	30	1	LYS	LYS	LYS	LYS	4	B	B	77	77
177	30	1	LYS	LYS	LYS	LYS	4	E	E	77	77
178	30	1	LYS	LYS	LYS	LYS	4	F	F	77	77
179	30	1	LYS	LYS	LYS	LYS	4	I	I	77	77
180	30	1	LYS	LYS	LYS	LYS	4	J	J	77	77
181	31	1	SER	SER	SER	SER	4	A	A	42	42
182	31	1	SER	SER	SER	SER	4	B	B	42	42
183	31	1	SER	SER	SER	SER	4	E	E	42	42
184	31	1	SER	SER	SER	SER	4	F	F	42	42
185	31	1	SER	SER	SER	SER	4	I	I	42	42
186	31	1	SER	SER	SER	SER	4	J	J	42	42
187	32	1	PRO	PRO	PRO	PRO	5	A	A	43	43
188	32	1	PRO	PRO	PRO	PRO	5	B	B	43	43
189	32	1	PRO	PRO	PRO	PRO	5	E	E	43	43
190	32	1	PRO	PRO	PRO	PRO	5	F	F	43	43
191	32	1	PRO	PRO	PRO	PRO	5	I	I	43	43
192	32	1	PRO	PRO	PRO	PRO	5	J	J	43	43
193	33	1	CA	CA	CA	CA	4	A	M - N	1501 - 1502
194	33	1	CA	CA	CA	CA	4	B	P - Q	2501 - 2502
195	33	1	CA	CA	CA	CA	4	E	W - X	1511 - 1512
196	33	1	CA	CA	CA	CA	4	F	Y - Z	2511 - 2512
197	33	1	CA	CA	CA	CA	4	I	GA - HA	1521 - 1522
198	33	1	CA	CA	CA	CA	4	J	IA - JA	2521 - 2522
1	1	2	LYS	LYS	MET	MET	1	C	C	4 - 5	3 - 4
2	1	2	LYS	LYS	MET	MET	1	D	D	4 - 5	3 - 4
3	1	2	LYS	LYS	MET	MET	1	G	G	4 - 5	3 - 4
4	1	2	LYS	LYS	MET	MET	1	H	H	4 - 5	3 - 4
5	1	2	LYS	LYS	MET	MET	1	K	K	4 - 5	3 - 4
6	1	2	LYS	LYS	MET	MET	1	L	L	4 - 5	3 - 4
7	2	2	SER	SER	GLN	GLN	4	C	C	6 - 7	5 - 6
8	2	2	SER	SER	GLN	GLN	4	D	D	6 - 7	5 - 6
9	2	2	SER	SER	GLN	GLN	4	G	G	6 - 7	5 - 6
10	2	2	SER	SER	GLN	GLN	4	H	H	6 - 7	5 - 6
11	2	2	SER	SER	GLN	GLN	4	K	K	6 - 7	5 - 6
12	2	2	SER	SER	GLN	GLN	4	L	L	6 - 7	5 - 6
13	3	2	LEU	LEU	GLU	GLU	5	C	C	8 - 9	7 - 8
14	3	2	LEU	LEU	GLU	GLU	5	D	D	8 - 9	7 - 8
15	3	2	LEU	LEU	GLU	GLU	5	G	G	8 - 9	7 - 8
16	3	2	LEU	LEU	GLU	GLU	5	H	H	8 - 9	7 - 8
17	3	2	LEU	LEU	GLU	GLU	5	K	K	8 - 9	7 - 8
18	3	2	LEU	LEU	GLU	GLU	5	L	L	8 - 9	7 - 8
19	4	2	ASN	ASN	ILE	ILE	5	C	C	11 - 16	10 - 15
20	4	2	ASN	ASN	ILE	ILE	5	D	D	11 - 16	10 - 15
21	4	2	ASN	ASN	ILE	ILE	5	G	G	11 - 16	10 - 15
22	4	2	ASN	ASN	ILE	ILE	5	H	H	11 - 16	10 - 15
23	4	2	ASN	ASN	ILE	ILE	5	K	K	11 - 16	10 - 15
24	4	2	ASN	ASN	ILE	ILE	5	L	L	11 - 16	10 - 15
25	5	2	THR	THR	PHE	PHE	5	C	C	18 - 19	17 - 18
26	5	2	THR	THR	PHE	PHE	5	D	D	18 - 19	17 - 18
27	5	2	THR	THR	PHE	PHE	5	G	G	18 - 19	17 - 18
28	5	2	THR	THR	PHE	PHE	5	H	H	18 - 19	17 - 18
29	5	2	THR	THR	PHE	PHE	5	K	K	18 - 19	17 - 18
30	5	2	THR	THR	PHE	PHE	5	L	L	18 - 19	17 - 18
31	6	2	HIS	HIS	HIS	HIS	4	C	C	20	19
32	6	2	HIS	HIS	HIS	HIS	4	D	D	20	19
33	6	2	HIS	HIS	HIS	HIS	4	G	G	20	19
34	6	2	HIS	HIS	HIS	HIS	4	H	H	20	19
35	6	2	HIS	HIS	HIS	HIS	4	K	K	20	19
36	6	2	HIS	HIS	HIS	HIS	4	L	L	20	19
37	7	2	TYR	TYR	VAL	VAL	5	C	C	22 - 24	21 - 23
38	7	2	TYR	TYR	VAL	VAL	5	D	D	22 - 24	21 - 23
39	7	2	TYR	TYR	VAL	VAL	5	G	G	22 - 24	21 - 23
40	7	2	TYR	TYR	VAL	VAL	5	H	H	22 - 24	21 - 23
41	7	2	TYR	TYR	VAL	VAL	5	K	K	22 - 24	21 - 23
42	7	2	TYR	TYR	VAL	VAL	5	L	L	22 - 24	21 - 23
43	8	2	GLY	GLY	HIS	HIS	4	C	C	27 - 28	26 - 27
44	8	2	GLY	GLY	HIS	HIS	4	D	D	27 - 28	26 - 27
45	8	2	GLY	GLY	HIS	HIS	4	G	G	27 - 28	26 - 27
46	8	2	GLY	GLY	HIS	HIS	4	H	H	27 - 28	26 - 27
47	8	2	GLY	GLY	HIS	HIS	4	K	K	27 - 28	26 - 27
48	8	2	GLY	GLY	HIS	HIS	4	L	L	27 - 28	26 - 27
49	9	2	PRO	PRO	PRO	PRO	5	C	C	29	28
50	9	2	PRO	PRO	PRO	PRO	5	D	D	29	28
51	9	2	PRO	PRO	PRO	PRO	5	G	G	29	28
52	9	2	PRO	PRO	PRO	PRO	5	H	H	29	28
53	9	2	PRO	PRO	PRO	PRO	5	K	K	29	28
54	9	2	PRO	PRO	PRO	PRO	5	L	L	29	28
55	10	2	ASP	ASP	ASP	ASP	4	C	C	30	29
56	10	2	ASP	ASP	ASP	ASP	4	D	D	30	29
57	10	2	ASP	ASP	ASP	ASP	4	G	G	30	29
58	10	2	ASP	ASP	ASP	ASP	4	H	H	30	29
59	10	2	ASP	ASP	ASP	ASP	4	K	K	30	29
60	10	2	ASP	ASP	ASP	ASP	4	L	L	30	29
61	11	2	THR	THR	ASN	ASN	5	C	C	31 - 33	30 - 32
62	11	2	THR	THR	ASN	ASN	5	D	D	31 - 33	30 - 32
63	11	2	THR	THR	ASN	ASN	5	G	G	31 - 33	30 - 32
64	11	2	THR	THR	ASN	ASN	5	H	H	31 - 33	30 - 32
65	11	2	THR	THR	ASN	ASN	5	K	K	31 - 33	30 - 32
66	11	2	THR	THR	ASN	ASN	5	L	L	31 - 33	30 - 32
67	12	2	GLN	GLN	GLN	GLN	1	C	C	34	33
68	12	2	GLN	GLN	GLN	GLN	1	D	D	34	33
69	12	2	GLN	GLN	GLN	GLN	1	G	G	34	33
70	12	2	GLN	GLN	GLN	GLN	1	H	H	34	33
71	12	2	GLN	GLN	GLN	GLN	1	K	K	34	33
72	12	2	GLN	GLN	GLN	GLN	1	L	L	34	33
73	13	2	GLY	GLY	PHE	PHE	5	C	C	35 - 37	34 - 36
74	13	2	GLY	GLY	PHE	PHE	5	D	D	35 - 37	34 - 36
75	13	2	GLY	GLY	PHE	PHE	5	G	G	35 - 37	34 - 36
76	13	2	GLY	GLY	PHE	PHE	5	H	H	35 - 37	34 - 36
77	13	2	GLY	GLY	PHE	PHE	5	K	K	35 - 37	34 - 36
78	13	2	GLY	GLY	PHE	PHE	5	L	L	35 - 37	34 - 36
79	14	2	LYS	LYS	GLU	GLU	1	C	C	38 - 39	37 - 38
80	14	2	LYS	LYS	GLU	GLU	1	D	D	38 - 39	37 - 38
81	14	2	LYS	LYS	GLU	GLU	1	G	G	38 - 39	37 - 38
82	14	2	LYS	LYS	GLU	GLU	1	H	H	38 - 39	37 - 38
83	14	2	LYS	LYS	GLU	GLU	1	K	K	38 - 39	37 - 38
84	14	2	LYS	LYS	GLU	GLU	1	L	L	38 - 39	37 - 38
85	15	2	LEU	LEU	ARG	ARG	5	C	C	40 - 42	39 - 41
86	15	2	LEU	LEU	ARG	ARG	5	D	D	40 - 42	39 - 41
87	15	2	LEU	LEU	ARG	ARG	5	G	G	40 - 42	39 - 41
88	15	2	LEU	LEU	ARG	ARG	5	H	H	40 - 42	39 - 41
89	15	2	LEU	LEU	ARG	ARG	5	K	K	40 - 42	39 - 41
90	15	2	LEU	LEU	ARG	ARG	5	L	L	40 - 42	39 - 41
91	16	2	GLN	GLN	GLN	GLN	4	C	C	46	45
92	16	2	GLN	GLN	GLN	GLN	4	D	D	46	45
93	16	2	GLN	GLN	GLN	GLN	4	G	G	46	45
94	16	2	GLN	GLN	GLN	GLN	4	H	H	46	45
95	16	2	GLN	GLN	GLN	GLN	4	K	K	46	45
96	16	2	GLN	GLN	GLN	GLN	4	L	L	46	45
97	17	2	ASN	ASN	LEU	LEU	5	C	C	47 - 49	46 - 48
98	17	2	ASN	ASN	LEU	LEU	5	D	D	47 - 49	46 - 48
99	17	2	ASN	ASN	LEU	LEU	5	G	G	47 - 49	46 - 48
100	17	2	ASN	ASN	LEU	LEU	5	H	H	47 - 49	46 - 48
101	17	2	ASN	ASN	LEU	LEU	5	K	K	47 - 49	46 - 48
102	17	2	ASN	ASN	LEU	LEU	5	L	L	47 - 49	46 - 48
103	18	2	HIS	HIS	HIS	HIS	4	C	C	61	60
104	18	2	HIS	HIS	HIS	HIS	4	D	D	61	60
105	18	2	HIS	HIS	HIS	HIS	4	G	G	61	60
106	18	2	HIS	HIS	HIS	HIS	4	H	H	61	60
107	18	2	HIS	HIS	HIS	HIS	4	K	K	61	60
108	18	2	HIS	HIS	HIS	HIS	4	L	L	61	60
109	19	2	ILE	ILE	MET	MET	5	C	C	62 - 63	61 - 62
110	19	2	ILE	ILE	MET	MET	5	D	D	62 - 63	61 - 62
111	19	2	ILE	ILE	MET	MET	5	G	G	62 - 63	61 - 62
112	19	2	ILE	ILE	MET	MET	5	H	H	62 - 63	61 - 62
113	19	2	ILE	ILE	MET	MET	5	K	K	62 - 63	61 - 62
114	19	2	ILE	ILE	MET	MET	5	L	L	62 - 63	61 - 62
115	20	2	THR	THR	THR	THR	4	C	C	68	67
116	20	2	THR	THR	THR	THR	4	D	D	68	67
117	20	2	THR	THR	THR	THR	4	G	G	68	67
118	20	2	THR	THR	THR	THR	4	H	H	68	67
119	20	2	THR	THR	THR	THR	4	K	K	68	67
120	20	2	THR	THR	THR	THR	4	L	L	68	67
121	21	2	ASN	ASN	ASP	ASP	5	C	C	69 - 71	68 - 70
122	21	2	ASN	ASN	ASP	ASP	5	D	D	69 - 71	68 - 70
123	21	2	ASN	ASN	ASP	ASP	5	G	G	69 - 71	68 - 70
124	21	2	ASN	ASN	ASP	ASP	5	H	H	69 - 71	68 - 70
125	21	2	ASN	ASN	ASP	ASP	5	K	K	69 - 71	68 - 70
126	21	2	ASN	ASN	ASP	ASP	5	L	L	69 - 71	68 - 70
127	22	2	LEU	LEU	ALA	ALA	5	C	C	74 - 84	73 - 83
128	22	2	LEU	LEU	ALA	ALA	5	D	D	74 - 84	73 - 83
129	22	2	LEU	LEU	ALA	ALA	5	G	G	74 - 84	73 - 83
130	22	2	LEU	LEU	ALA	ALA	5	H	H	74 - 84	73 - 83
131	22	2	LEU	LEU	ALA	ALA	5	K	K	74 - 84	73 - 83
132	22	2	LEU	LEU	ALA	ALA	5	L	L	74 - 84	73 - 83
133	23	2	LEU	LEU	THR	THR	5	C	C	86 - 87	85 - 86
134	23	2	LEU	LEU	THR	THR	5	D	D	86 - 87	85 - 86
135	23	2	LEU	LEU	THR	THR	5	G	G	86 - 87	85 - 86
136	23	2	LEU	LEU	THR	THR	5	H	H	86 - 87	85 - 86
137	23	2	LEU	LEU	THR	THR	5	K	K	86 - 87	85 - 86
138	23	2	LEU	LEU	THR	THR	5	L	L	86 - 87	85 - 86
139	24	2	TRP	TRP	GLU	GLU	2	C	C	88 - 92	87 - 91
140	24	2	TRP	TRP	HIS	HIS	2	D	D	88 - 95	87 - 94
141	24	2	TRP	TRP	HIS	HIS	2	G	G	88 - 95	87 - 94
142	24	2	TRP	TRP	GLU	GLU	2	H	H	88 - 92	87 - 91
143	24	2	TRP	TRP	HIS	HIS	2	K	K	88 - 95	87 - 94
144	24	2	TRP	TRP	HIS	HIS	2	L	L	88 - 95	87 - 94
145	25	2	GLN	GLN	GLN	GLN	4	C	C	21	20
146	25	2	GLN	GLN	GLN	GLN	4	D	D	21	20
147	25	2	GLN	GLN	GLN	GLN	4	G	G	21	20
148	25	2	GLN	GLN	GLN	GLN	4	H	H	21	20
149	25	2	GLN	GLN	GLN	GLN	4	K	K	21	20
150	25	2	GLN	GLN	GLN	GLN	4	L	L	21	20
151	26	2	LYS	LYS	LYS	LYS	4	C	C	25	24
152	26	2	LYS	LYS	LYS	LYS	4	D	D	25	24
153	26	2	LYS	LYS	LYS	LYS	4	G	G	25	24
154	26	2	LYS	LYS	LYS	LYS	4	H	H	25	24
155	26	2	LYS	LYS	LYS	LYS	4	K	K	25	24
156	26	2	LYS	LYS	LYS	LYS	4	L	L	25	24
157	27	2	CA	CA	CA	CA	4	C	S - T	3501 - 3502
158	27	2	CA	CA	CA	CA	4	D	U - V	4501 - 4502
159	27	2	CA	CA	CA	CA	4	G	CA - DA	3511 - 3512
160	27	2	CA	CA	CA	CA	4	H	EA - FA	4511 - 4512
161	27	2	CA	CA	CA	CA	4	K	LA - MA	3521 - 3522
162	27	2	CA	CA	CA	CA	4	L	NA - OA	4521 - 4522
163	28	2	LYS	LYS	LYS	LYS	1	C	C	43	42
164	28	2	LYS	LYS	LYS	LYS	1	D	D	43	42
165	28	2	LYS	LYS	LYS	LYS	1	G	G	43	42
166	28	2	LYS	LYS	LYS	LYS	1	H	H	43	42
167	28	2	LYS	LYS	LYS	LYS	1	K	K	43	42
168	28	2	LYS	LYS	LYS	LYS	1	L	L	43	42
169	29	2	ASP	ASP	LEU	LEU	5	C	C	44 - 45	43 - 44
170	29	2	ASP	ASP	LEU	LEU	5	D	D	44 - 45	43 - 44
171	29	2	ASP	ASP	LEU	LEU	5	G	G	44 - 45	43 - 44
172	29	2	ASP	ASP	LEU	LEU	5	H	H	44 - 45	43 - 44
173	29	2	ASP	ASP	LEU	LEU	5	K	K	44 - 45	43 - 44
174	29	2	ASP	ASP	LEU	LEU	5	L	L	44 - 45	43 - 44
175	30	2	LYS	LYS	LYS	LYS	1	C	C	50 - 51	49 - 50
176	30	2	LYS	LYS	LYS	LYS	1	D	D	50 - 51	49 - 50
177	30	2	LYS	LYS	LYS	LYS	1	G	G	50 - 51	49 - 50
178	30	2	LYS	LYS	LYS	LYS	1	H	H	50 - 51	49 - 50
179	30	2	LYS	LYS	LYS	LYS	1	K	K	50 - 51	49 - 50
180	30	2	LYS	LYS	LYS	LYS	1	L	L	50 - 51	49 - 50
181	31	2	GLU	GLU	ASN	ASN	5	C	C	52 - 53	51 - 52
182	31	2	GLU	GLU	ASN	ASN	5	D	D	52 - 53	51 - 52
183	31	2	GLU	GLU	ASN	ASN	5	G	G	52 - 53	51 - 52
184	31	2	GLU	GLU	ASN	ASN	5	H	H	52 - 53	51 - 52
185	31	2	GLU	GLU	ASN	ASN	5	K	K	52 - 53	51 - 52
186	31	2	GLU	GLU	ASN	ASN	5	L	L	52 - 53	51 - 52
187	32	2	LYS	LYS	ASN	ASN	1	C	C	54 - 55	53 - 54
188	32	2	LYS	LYS	ASN	ASN	1	D	D	54 - 55	53 - 54
189	32	2	LYS	LYS	ASN	ASN	1	G	G	54 - 55	53 - 54
190	32	2	LYS	LYS	ASN	ASN	1	H	H	54 - 55	53 - 54
191	32	2	LYS	LYS	ASN	ASN	1	K	K	54 - 55	53 - 54
192	32	2	LYS	LYS	ASN	ASN	1	L	L	54 - 55	53 - 54
193	33	2	GLU	GLU	LYS	LYS	1	C	C	56 - 57	55 - 56
194	33	2	GLU	GLU	LYS	LYS	1	D	D	56 - 57	55 - 56
195	33	2	GLU	GLU	LYS	LYS	1	G	G	56 - 57	55 - 56
196	33	2	GLU	GLU	LYS	LYS	1	H	H	56 - 57	55 - 56
197	33	2	GLU	GLU	LYS	LYS	1	K	K	56 - 57	55 - 56
198	33	2	GLU	GLU	LYS	LYS	1	L	L	56 - 57	55 - 56
199	34	2	VAL	VAL	GLU	GLU	5	C	C	58 - 60	57 - 59
200	34	2	VAL	VAL	GLU	GLU	5	D	D	58 - 60	57 - 59
201	34	2	VAL	VAL	GLU	GLU	5	G	G	58 - 60	57 - 59
202	34	2	VAL	VAL	GLU	GLU	5	H	H	58 - 60	57 - 59
203	34	2	VAL	VAL	GLU	GLU	5	K	K	58 - 60	57 - 59
204	34	2	VAL	VAL	GLU	GLU	5	L	L	58 - 60	57 - 59
205	35	2	GLU	GLU	GLU	GLU	1	C	C	64	63
206	35	2	GLU	GLU	GLU	GLU	1	D	D	64	63
207	35	2	GLU	GLU	GLU	GLU	1	G	G	64	63
208	35	2	GLU	GLU	GLU	GLU	1	H	H	64	63
209	35	2	GLU	GLU	GLU	GLU	1	K	K	64	63
210	35	2	GLU	GLU	GLU	GLU	1	L	L	64	63
211	36	2	ASP	ASP	ASP	ASP	5	C	C	65 - 67	64 - 66
212	36	2	ASP	ASP	ASP	ASP	5	D	D	65 - 67	64 - 66
213	36	2	ASP	ASP	ASP	ASP	5	G	G	65 - 67	64 - 66
214	36	2	ASP	ASP	ASP	ASP	5	H	H	65 - 67	64 - 66
215	36	2	ASP	ASP	ASP	ASP	5	K	K	65 - 67	64 - 66
216	36	2	ASP	ASP	ASP	ASP	5	L	L	65 - 67	64 - 66
217	37	2	LYS	LYS	LYS	LYS	1	C	C	72	71
218	37	2	LYS	LYS	LYS	LYS	1	D	D	72	71
219	37	2	LYS	LYS	LYS	LYS	1	G	G	72	71
220	37	2	LYS	LYS	LYS	LYS	1	H	H	72	71
221	37	2	LYS	LYS	LYS	LYS	1	K	K	72	71
222	37	2	LYS	LYS	LYS	LYS	1	L	L	72	71
223	38	2	ARG	ARG	ARG	ARG	1	C	C	85	84
224	38	2	ARG	ARG	ARG	ARG	1	D	D	85	84
225	38	2	ARG	ARG	ARG	ARG	1	G	G	85	84
226	38	2	ARG	ARG	ARG	ARG	1	H	H	85	84
227	38	2	ARG	ARG	ARG	ARG	1	K	K	85	84
228	38	2	ARG	ARG	ARG	ARG	1	L	L	85	84
229	39	2	LEU	LEU	LEU	LEU	5	C	C	26	25
230	39	2	LEU	LEU	LEU	LEU	5	D	D	26	25
231	39	2	LEU	LEU	LEU	LEU	5	G	G	26	25
232	39	2	LEU	LEU	LEU	LEU	5	H	H	26	25
233	39	2	LEU	LEU	LEU	LEU	5	K	K	26	25
234	39	2	LEU	LEU	LEU	LEU	5	L	L	26	25

NCS ensembles :

ID
1
2

Details

The biological assembly is a tetramer composed of A,B,C,D or E,F,G,H or I,J,K,L.

-
Protein , 2 types, 12 molecules ABEFIJCDGHKL

#1: Protein	Calgranulin A / S100 calcium-binding protein a8 / s100a8 / migration inhibitory factor-related protein 8 / MRP-8 / ...S100 calcium-binding protein a8 / s100a8 / migration inhibitory factor-related protein 8 / MRP-8 / P8 / cystic fibrosis antigen / cfag / leukocyte L1 complex light chain / calprotectin L1L Mass: 10837.463 Da / Num. of mol.: 6 / Mutation: C42S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: S100A8 / Plasmid: PET-36B(+)-MRP8C42S / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P05109
#2: Protein	Calgranulin B / Calgranulin / S100 calcium-binding protein A9 / S100A9 / migration inhibitory factor-related protein 14 / MRP-14 ...S100 calcium-binding protein A9 / S100A9 / migration inhibitory factor-related protein 14 / MRP-14 / P14 / leucocyte L1 complex heavy chain / calprotectin L1H subunit Mass: 13116.759 Da / Num. of mol.: 6 / Mutation: C3S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: S100A9 / Plasmid: PET-36B(+)-MRP14C3S / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P06702

#1: Protein

Calgranulin A / S100 calcium-binding protein a8 / s100a8 / migration inhibitory factor-related protein 8 / MRP-8 / ...

Mass: 10837.463 Da / Num. of mol.: 6 / Mutation: C42S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Homo sapiens (human) / Gene: S100A8 / Plasmid: PET-36B(+)-MRP8C42S / Species (production host): Escherichia coli / Production host:

Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P05109

#2: Protein

Calgranulin B /

Calgranulin / S100 calcium-binding protein A9 / S100A9 / migration inhibitory factor-related protein 14 / MRP-14 ...

Mass: 13116.759 Da / Num. of mol.: 6 / Mutation: C3S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Homo sapiens (human) / Gene: S100A9 / Plasmid: PET-36B(+)-MRP14C3S / Species (production host): Escherichia coli / Production host:

Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P06702

-
Non-polymers , 4 types, 1088 molecules

#3: Chemical	... ChemComp-CA / CALCIUM ION Mass: 40.078 Da / Num. of mol.: 24 / Source method: obtained synthetically / Formula: Ca
#4: Chemical	ChemComp-CL / CHLORIDE ION / Chloride Mass: 35.453 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Cl
#5: Chemical	ChemComp-FLC / CITRATE ANION / Citric acid Mass: 189.100 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₆H₅O₇
#6: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 1059 / Source method: isolated from a natural source / Formula: H₂O

-
Experiment

Experiment	Method: X-RAY DIFFRACTION / Number of used crystals: 2

-
Sample preparation

Crystal	Density Matthews: 2.4 Å³/Da / Density % sol: 47.3 %
Crystal grow	Temperature: 285 K / Method: vapor diffusion, hanging drop / pH: 4.2 Details: 32% MPD, 0.1M Citrate (pH= 4.2), 20mM Tris (pH= 8.0), 2mM CaCl2, VAPOR DIFFUSION, HANGING DROP, temperature 285K

-
Data collection

Diffraction

ID	Mean temperature (K)	Crystal-ID
1	100	1
2	100	1

Diffraction source

Source	Site	Beamline	ID	Wavelength (Å)
SYNCHROTRON	SLS	X06SA	1	0.9796
SYNCHROTRON	BESSY	14.2	2	0.92

Detector

Type	ID	Detector	Date
MARRESEARCH	1	CCD	Nov 15, 2003
MARRESEARCH	2	IMAGE PLATE	Jul 28, 2004

Radiation

Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray

Radiation wavelength

ID	Wavelength (Å)	Relative weight
1	0.9796	1
2	0.92	1

Reflection

Resolution: 1.8→30 Å / Num. all: 102635 / Num. obs: 99507 / % possible obs: 81.03 % / Observed criterion σ(F): 6 / Observed criterion σ(I): 6 / Redundancy: 6.2 % / R_merge(I) obs: 0.119 / Net I/σ(I): 3.8005

Reflection shell

Resolution: 1.8→1.9 Å / Redundancy: 6.1 % / R_merge(I) obs: 0.48 / Mean I/σ(I) obs: 1.44 / Num. unique all: 12460 / % possible all: 69.88

-
Processing

Software

Name	Version	Classification
REFMAC	5.2.0005	refinement
MOSFLM		data reduction
CCP4	(SCALA)	data scaling
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 1MR8 and 1IRJ

1mr8

1irj

Resolution: 1.8→30 Å / Cor.coef. F_o:F_c: 0.965 / Cor.coef. F_o:F_c free: 0.942 / SU B: 4.525 / SU ML: 0.076 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): -3 / ESU R: 0.132 / ESU R Free: 0.13 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.20475	5004	5 %	RANDOM
R_work	0.15781	-	-	-
obs	0.1602	94798	81.02 %	-
all	-	99802	-	-

Solvent computation

Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK

Displacement parameters

B_iso mean: 27.208 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	2.25 Å²	0 Å²	-1.05 Å²
2-	-	-1.59 Å²	0 Å²
3-	-	-	-0.84 Å²

Refinement step

Cycle: LAST / Resolution: 1.8→30 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	8880	0	41	1059	9980

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.012	0.022	9050
X-RAY DIFFRACTION	r_bond_other_d
X-RAY DIFFRACTION	r_angle_refined_deg	1.458	1.945	12133
X-RAY DIFFRACTION	r_angle_other_deg
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	5.481	5	1060
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	35.494	25.459	458
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	16.05	15	1827
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	14.033	15	30
X-RAY DIFFRACTION	r_chiral_restr	0.115	0.2	1337
X-RAY DIFFRACTION	r_gen_planes_refined	0.007	0.02	6620
X-RAY DIFFRACTION	r_gen_planes_other
X-RAY DIFFRACTION	r_nbd_refined	0.225	0.3	4878
X-RAY DIFFRACTION	r_nbd_other
X-RAY DIFFRACTION	r_nbtor_refined	0.315	0.5	6299
X-RAY DIFFRACTION	r_nbtor_other
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.255	0.5	1270
X-RAY DIFFRACTION	r_xyhbond_nbd_other
X-RAY DIFFRACTION	r_metal_ion_refined	0.118	0.5	92
X-RAY DIFFRACTION	r_metal_ion_other
X-RAY DIFFRACTION	r_symmetry_vdw_refined	0.372	0.3	133
X-RAY DIFFRACTION	r_symmetry_vdw_other
X-RAY DIFFRACTION	r_symmetry_hbond_refined	0.254	0.5	79
X-RAY DIFFRACTION	r_symmetry_hbond_other
X-RAY DIFFRACTION	r_mcbond_it	2.05	2	5495
X-RAY DIFFRACTION	r_mcbond_other
X-RAY DIFFRACTION	r_mcangle_it	2.93	3	8598
X-RAY DIFFRACTION	r_scbond_it	2.494	2	3970
X-RAY DIFFRACTION	r_scangle_it	3.808	3	3535
X-RAY DIFFRACTION	r_rigid_bond_restr
X-RAY DIFFRACTION	r_sphericity_free
X-RAY DIFFRACTION	r_sphericity_bonded

Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-ID	Dom-ID	Auth asym-ID	Number	Type	Rms dev position (Å)	Weight position
1	1	A	143	tight positional	0.06	0.05
1	2	B	143	tight positional	0.05	0.05
1	3	E	143	tight positional	0.05	0.05
1	4	F	143	tight positional	0.05	0.05
1	5	I	143	tight positional	0.04	0.05
1	6	J	143	tight positional	0.04	0.05
2	1	C	155	tight positional	0.05	0.05
2	2	D	155	tight positional	0.06	0.05
2	3	G	155	tight positional	0.05	0.05
2	4	H	155	tight positional	0.05	0.05
2	5	K	155	tight positional	0.04	0.05
2	6	L	155	tight positional	0.04	0.05
1	1	A	291	medium positional	0.17	0.5
1	2	B	291	medium positional	0.34	0.5
1	3	E	291	medium positional	0.17	0.5
1	4	F	291	medium positional	0.14	0.5
1	5	I	291	medium positional	0.15	0.5
1	6	J	291	medium positional	0.21	0.5
2	1	C	337	medium positional	0.25	0.5
2	2	D	337	medium positional	0.41	0.5
2	3	G	337	medium positional	0.36	0.5
2	4	H	337	medium positional	0.28	0.5
2	5	K	337	medium positional	0.21	0.5
2	6	L	337	medium positional	0.2	0.5
1	1	A	235	loose positional	0.3	5
1	2	B	235	loose positional	0.32	5
1	3	E	235	loose positional	0.36	5
1	4	F	235	loose positional	0.31	5
1	5	I	235	loose positional	0.3	5
1	6	J	235	loose positional	0.26	5
2	1	C	227	loose positional	0.39	5
2	2	D	227	loose positional	0.49	5
2	3	G	227	loose positional	0.71	5
2	4	H	227	loose positional	0.4	5
2	5	K	227	loose positional	0.33	5
2	6	L	227	loose positional	0.28	5
1	1	A	143	tight thermal	0.19	0.5
1	2	B	143	tight thermal	0.17	0.5
1	3	E	143	tight thermal	0.19	0.5
1	4	F	143	tight thermal	0.16	0.5
1	5	I	143	tight thermal	0.16	0.5
1	6	J	143	tight thermal	0.15	0.5
2	1	C	155	tight thermal	0.17	0.5
2	2	D	155	tight thermal	0.17	0.5
2	3	G	155	tight thermal	0.14	0.5
2	4	H	155	tight thermal	0.17	0.5
2	5	K	155	tight thermal	0.14	0.5
2	6	L	155	tight thermal	0.15	0.5
1	1	A	291	medium thermal	1.32	2
1	2	B	291	medium thermal	1.17	2
1	3	E	291	medium thermal	1.59	2
1	4	F	291	medium thermal	1.02	2
1	5	I	291	medium thermal	1.04	2
1	6	J	291	medium thermal	1.15	2
2	1	C	337	medium thermal	1.42	2
2	2	D	337	medium thermal	1.16	2
2	3	G	337	medium thermal	1.45	2
2	4	H	337	medium thermal	1.2	2
2	5	K	337	medium thermal	1.12	2
2	6	L	337	medium thermal	1.05	2
1	1	A	235	loose thermal	2.53	10
1	2	B	235	loose thermal	1.82	10
1	3	E	235	loose thermal	2.27	10
1	4	F	235	loose thermal	2.22	10
1	5	I	235	loose thermal	1.72	10
1	6	J	235	loose thermal	1.62	10
2	1	C	227	loose thermal	2.08	10
2	2	D	227	loose thermal	1.83	10
2	3	G	227	loose thermal	2.16	10
2	4	H	227	loose thermal	1.69	10
2	5	K	227	loose thermal	1.7	10
2	6	L	227	loose thermal	1.47	10

LS refinement shell

Resolution: 1.8→1.847 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.249	303	-
R_work	0.186	5982	-
obs	-	8987	69.93 %

Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

ID	L11 (°²)	L12 (°²)	L13 (°²)	L22 (°²)	L23 (°²)	L33 (°²)	S11 (Å °)	S12 (Å °)	S13 (Å °)	S21 (Å °)	S22 (Å °)	S23 (Å °)	S31 (Å °)	S32 (Å °)	S33 (Å °)	T11 (Å²)	T12 (Å²)	T13 (Å²)	T22 (Å²)	T23 (Å²)	T33 (Å²)	Origin x (Å)	Origin y (Å)	Origin z (Å)
1	0.4744	-0.1014	0.2522	0.7398	-0.483	0.7398	-0.0089	-0.0756	0.0141	0.0238	0.0015	0.0204	-0.0022	-0.0661	0.0074	-0.0123	-0.0028	-0.0276	-0.0097	-0.0163	-0.0198	18.163	53.693	171.001
2	1.0111	-0.1816	0.5938	0.681	-0.3566	1.0489	0.0742	-0.0115	-0.0524	-0.0885	-0.0175	-0.0328	0.0855	-0.0389	-0.0567	-0.001	-0.0206	-0.0447	-0.0323	-0.0087	-0.0198	22.327	30.634	164.474
3	0.6413	-0.1396	0.154	1.5373	0.2387	0.8089	-0.0086	0.033	0.0198	-0.1224	0.0006	-0.0651	0.0847	0.0584	0.008	0.0083	0.0083	-0.0171	-0.0259	0.0184	-0.055	21.445	53.033	150.841
4	0.249	-0.3373	0.373	1.1205	0.2628	1.8116	-0.0125	0.0105	0.064	0.0036	-0.0033	-0.1695	-0.0697	0.1642	0.0158	-0.049	-0.0301	-0.0684	-0.0196	0.0119	0.0131	37.499	37.011	176.595
5	0.7129	-0.0705	-0.5303	0.73	-0.2957	1.7569	0.035	-0.0115	0.007	0.0576	-0.0203	-0.0362	-0.1482	-0.0418	-0.0147	0.0648	0.0139	0.0426	-0.0456	-0.0178	-0.0885	10.81	63.816	103.482
6	0.3352	0.0549	-0.0909	0.9527	-0.5775	1.4472	-0.0058	0.0448	-0.0042	-0.0359	0.0028	0.1141	0.0322	-0.1642	0.003	0.0322	-0.008	0.0319	-0.0077	-0.017	-0.0608	4.487	40.725	99.101
7	0.5999	0.1942	-0.0058	1.3224	-0.0095	1.6565	0.0252	0.0573	-0.063	-0.0109	0.0058	-0.1805	0.0747	0.1046	-0.031	0.0338	0.0162	0.0703	-0.0418	-0.0065	-0.098	20.762	57.295	86.961
8	1.0294	0.2033	-0.1027	1.6289	0.2284	1.1329	-0.051	-0.0076	-0.0084	0.0879	0.0155	-0.0962	-0.0602	0.0819	0.0355	0.0441	-0.0071	0.0221	-0.0489	0.0211	-0.1128	14.751	41.341	116.766
9	0.4515	-0.1316	0.2484	0.7651	-0.4386	1.199	0.0504	-0.0199	-0.0251	-0.0895	0.003	0.0153	0.1062	-0.1165	-0.0534	0.0156	-0.0096	-0.0026	-0.01	-0.0067	-0.0722	3.869	-4.176	134.302
10	0.1444	-0.2296	0.1683	0.7712	-0.4472	1.1571	0.0005	-0.0293	0.0002	0.0114	0.0106	-0.0163	-0.1071	-0.0913	-0.0111	0.0127	0.0077	0.0017	-0.0007	-0.0047	-0.0644	4.539	19.791	138.556
11	0.5337	0.0134	0.1736	1.4903	0.0401	0.9635	-0.0172	-0.0655	0.004	0.0123	-0.0466	-0.1938	0.0037	0.0154	0.0638	-0.0259	0	-0.0384	-0.0356	0.0267	-0.0582	17.387	-0.794	149.048
12	0.6393	-0.1212	0.1221	1.6866	-0.1241	1.0155	-0.0205	0.0818	0.0343	-0.1617	-0.0389	-0.1686	0.0801	0.0461	0.0594	0.0277	0.0207	0.0614	-0.0346	0.0234	-0.1121	11.785	16.471	119.914

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	X-RAY DIFFRACTION	1	A	A	1 - 87	1 - 87
2	X-RAY DIFFRACTION	2	B	B	1 - 88	1 - 88
3	X-RAY DIFFRACTION	3	C	C	4 - 92	3 - 91
4	X-RAY DIFFRACTION	4	D	D	4 - 92	3 - 91
5	X-RAY DIFFRACTION	5	E	E	1 - 88	1 - 88
6	X-RAY DIFFRACTION	6	F	F	1 - 87	1 - 87
7	X-RAY DIFFRACTION	7	G	G	4 - 92	3 - 91
8	X-RAY DIFFRACTION	8	H	H	4 - 92	3 - 91
9	X-RAY DIFFRACTION	9	I	I	1 - 87	1 - 87
10	X-RAY DIFFRACTION	10	J	J	1 - 88	1 - 88
11	X-RAY DIFFRACTION	11	K	K	4 - 92	3 - 91
12	X-RAY DIFFRACTION	12	L	L	4 - 92	3 - 91

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