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

Basic information

• Entry: Database: PDB / ID: 1xk4
• Title: Crystal structure of human calprotectin(S100A8/S100A9)

Components

• Calgranulin A
• Calgranulin B

• Keywords: METAL BINDING PROTEIN / S100 family / heterotetramer

Function / homology

Function:

S100A8 complex / S100A9 complex / neutrophil aggregation / calprotectin complex / positive regulation of peptide secretion / modulation of process of another organism / regulation of respiratory burst involved in inflammatory response / autocrine signaling / chronic inflammatory response / peptidyl-cysteine S-trans-nitrosylation / Toll-like receptor 4 binding / peptidyl-cysteine S-nitrosylation / Metal sequestration by antimicrobial proteins / RAGE receptor binding / peptide secretion / leukocyte migration involved in inflammatory response / Regulation of TLR by endogenous ligand / astrocyte development / intermediate filament cytoskeleton / MyD88 deficiency (TLR2/4) / arachidonate binding / IRAK4 deficiency (TLR2/4) / MyD88:MAL(TIRAP) cascade initiated on plasma membrane / regulation of toll-like receptor signaling pathway / response to zinc ion / regulation of cytoskeleton organization / antioxidant activity / RHO GTPases Activate NADPH Oxidases / defense response to fungus / endothelial cell migration / positive regulation of intrinsic apoptotic signaling pathway / neutrophil chemotaxis / positive regulation of neuron projection development / autophagy / positive regulation of inflammatory response / antimicrobial humoral immune response mediated by antimicrobial peptide / calcium-dependent protein binding / positive regulation of NF-kappaB transcription factor activity / cell-cell signaling / ER-Phagosome pathway / positive regulation of cell growth / microtubule binding / : / secretory granule lumen / response to lipopolysaccharide / response to ethanol / cytoskeleton / defense response to bacterium / inflammatory response / innate immune response / apoptotic process / calcium ion binding / Neutrophil degranulation / extracellular space / extracellular exosome / extracellular region / zinc ion binding / nucleus / plasma membrane / cytosol / cytoplasm

Domain/homology:

S-100/ICaBP type calcium binding protein signature. / S100/Calcium binding protein 7/8-like, conserved site / S100/CaBP-9k-type, calcium binding, subdomain / S-100/ICaBP type calcium binding domain / S-100/ICaBP type calcium binding domain / EF-hand / Recoverin; domain 1 / EF-hand, calcium binding motif / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain. / EF-hand calcium-binding domain profile. / EF-hand domain / EF-hand domain pair / Orthogonal Bundle / Mainly Alpha

Component:

CITRATE ANION / Protein S100-A8 / Protein S100-A9

• 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 / Derived calculations / Refinement description Category: 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 / _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

Assembly

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

Summary:

• 145 kDa, 12 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	145,018	41
Polymers	143,725	12
Non-polymers	1,293	29
Water	19,078	1059

1

A: Calgranulin A

B: Calgranulin A

C: Calgranulin B

D: Calgranulin B

hetero molecules

Summary:

• defined by author&software
• 48.3 kDa, 4 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	48,300	14
Polymers	47,908	4
Non-polymers	392	10
Water	72	4

Symmetry operations:

Type	Name	Symmetry operation	Number
identity operation	1_555	x,y,z	1

Calculated values:

Buried area	8960 Å2
ΔGint	-181 kcal/mol
Surface area	17250 Å2
Method	PISA

2

E: Calgranulin A

F: Calgranulin A

G: Calgranulin B

H: Calgranulin B

hetero molecules

Summary:

• defined by author&software
• 48.5 kDa, 4 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	48,454	14
Polymers	47,908	4
Non-polymers	545	10
Water	72	4

Symmetry operations:

Type	Name	Symmetry operation	Number
identity operation	1_555	x,y,z	1

Calculated values:

Buried area	9080 Å2
ΔGint	-158 kcal/mol
Surface area	17310 Å2
Method	PISA

3

I: Calgranulin A

J: Calgranulin A

K: Calgranulin B

L: Calgranulin B

hetero molecules

Summary:

• defined by author&software
• 48.3 kDa, 4 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	48,265	13
Polymers	47,908	4
Non-polymers	356	9
Water	72	4

Symmetry operations:

Type	Name	Symmetry operation	Number
identity operation	1_555	x,y,z	1

Calculated values:

Buried area	9110 Å2
ΔGint	-172 kcal/mol
Surface area	17390 Å2
Method	PISA

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:

ID	Ens-ID	Details
1	1	A
2	1	B
3	1	E
4	1	F
5	1	I
6	1	J
7	1	A
8	1	B
9	1	E
10	1	F
11	1	I
12	1	J
13	1	A
14	1	B
15	1	E
16	1	F
17	1	I
18	1	J
19	1	A
20	1	B
21	1	E
22	1	F
23	1	I
24	1	J
25	1	A
26	1	B
27	1	E
28	1	F
29	1	I
30	1	J
31	1	A
32	1	B
33	1	E
34	1	F
35	1	I
36	1	J
37	1	A
38	1	B
39	1	E
40	1	F
41	1	I
42	1	J
43	1	A
44	1	B
45	1	E
46	1	F
47	1	I
48	1	J
49	1	A
50	1	B
51	1	E
52	1	F
53	1	I
54	1	J
55	1	A
56	1	B
57	1	E
58	1	F
59	1	I
60	1	J
61	1	A
62	1	B
63	1	E
64	1	F
65	1	I
66	1	J
67	1	A
68	1	B
69	1	E
70	1	F
71	1	I
72	1	J
73	1	A
74	1	B
75	1	E
76	1	F
77	1	I
78	1	J
79	1	A
80	1	B
81	1	E
82	1	F
83	1	I
84	1	J
85	1	A
86	1	B
87	1	E
88	1	F
89	1	I
90	1	J
91	1	A
92	1	B
93	1	E
94	1	F
95	1	I
96	1	J
97	1	A
98	1	B
99	1	E
100	1	F
101	1	I
102	1	J
103	1	A
104	1	B
105	1	E
106	1	F
107	1	I
108	1	J
109	1	A
110	1	B
111	1	E
112	1	F
113	1	I
114	1	J
115	1	A
116	1	B
117	1	E
118	1	F
119	1	I
120	1	J
121	1	A
122	1	B
123	1	E
124	1	F
125	1	I
126	1	J
127	1	A
128	1	B
129	1	E
130	1	F
131	1	I
132	1	J
133	1	A
134	1	B
135	1	E
136	1	F
137	1	I
138	1	J
139	1	A
140	1	B
141	1	E
142	1	F
143	1	I
144	1	J
145	1	A
146	1	B
147	1	E
148	1	F
149	1	I
150	1	J
151	1	A
152	1	B
153	1	E
154	1	F
155	1	I
156	1	J
157	1	A
158	1	B
159	1	E
160	1	F
161	1	I
162	1	J
163	1	A
164	1	B
165	1	E
166	1	F
167	1	I
168	1	J
169	1	A
170	1	B
171	1	E
172	1	F
173	1	I
174	1	J
175	1	A
176	1	B
177	1	E
178	1	F
179	1	I
180	1	J
181	1	A
182	1	B
183	1	E
184	1	F
185	1	I
186	1	J
187	1	A
188	1	B
189	1	E
190	1	F
191	1	I
192	1	J
193	1	A
194	1	B
195	1	E
196	1	F
197	1	I
198	1	J
1	2	C
2	2	D
3	2	G
4	2	H
5	2	K
6	2	L
7	2	C
8	2	D
9	2	G
10	2	H
11	2	K
12	2	L
13	2	C
14	2	D
15	2	G
16	2	H
17	2	K
18	2	L
19	2	C
20	2	D
21	2	G
22	2	H
23	2	K
24	2	L
25	2	C
26	2	D
27	2	G
28	2	H
29	2	K
30	2	L
31	2	C
32	2	D
33	2	G
34	2	H
35	2	K
36	2	L
37	2	C
38	2	D
39	2	G
40	2	H
41	2	K
42	2	L
43	2	C
44	2	D
45	2	G
46	2	H
47	2	K
48	2	L
49	2	C
50	2	D
51	2	G
52	2	H
53	2	K
54	2	L
55	2	C
56	2	D
57	2	G
58	2	H
59	2	K
60	2	L
61	2	C
62	2	D
63	2	G
64	2	H
65	2	K
66	2	L
67	2	C
68	2	D
69	2	G
70	2	H
71	2	K
72	2	L
73	2	C
74	2	D
75	2	G
76	2	H
77	2	K
78	2	L
79	2	C
80	2	D
81	2	G
82	2	H
83	2	K
84	2	L
85	2	C
86	2	D
87	2	G
88	2	H
89	2	K
90	2	L
91	2	C
92	2	D
93	2	G
94	2	H
95	2	K
96	2	L
97	2	C
98	2	D
99	2	G
100	2	H
101	2	K
102	2	L
103	2	C
104	2	D
105	2	G
106	2	H
107	2	K
108	2	L
109	2	C
110	2	D
111	2	G
112	2	H
113	2	K
114	2	L
115	2	C
116	2	D
117	2	G
118	2	H
119	2	K
120	2	L
121	2	C
122	2	D
123	2	G
124	2	H
125	2	K
126	2	L
127	2	C
128	2	D
129	2	G
130	2	H
131	2	K
132	2	L
133	2	C
134	2	D
135	2	G
136	2	H
137	2	K
138	2	L
139	2	C
140	2	D
141	2	G
142	2	H
143	2	K
144	2	L
145	2	C
146	2	D
147	2	G
148	2	H
149	2	K
150	2	L
151	2	C
152	2	D
153	2	G
154	2	H
155	2	K
156	2	L
157	2	C
158	2	D
159	2	G
160	2	H
161	2	K
162	2	L
163	2	C
164	2	D
165	2	G
166	2	H
167	2	K
168	2	L
169	2	C
170	2	D
171	2	G
172	2	H
173	2	K
174	2	L
175	2	C
176	2	D
177	2	G
178	2	H
179	2	K
180	2	L
181	2	C
182	2	D
183	2	G
184	2	H
185	2	K
186	2	L
187	2	C
188	2	D
189	2	G
190	2	H
191	2	K
192	2	L
193	2	C
194	2	D
195	2	G
196	2	H
197	2	K
198	2	L
199	2	C
200	2	D
201	2	G
202	2	H
203	2	K
204	2	L
205	2	C
206	2	D
207	2	G
208	2	H
209	2	K
210	2	L
211	2	C
212	2	D
213	2	G
214	2	H
215	2	K
216	2	L
217	2	C
218	2	D
219	2	G
220	2	H
221	2	K
222	2	L
223	2	C
224	2	D
225	2	G
226	2	H
227	2	K
228	2	L
229	2	C
230	2	D
231	2	G
232	2	H
233	2	K
234	2	L

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.

Components

Protein , 2 types, 12 molecules A B E F I J C D G H K L

#1: Protein

A B E F I J
Calgranulin A / 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

Details:

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

C D G H K L
Calgranulin B / S100 calcium-binding protein A9 / S100A9 / migration inhibitory factor-related protein 14 / MRP-14 / P14 / leucocyte L1 complex heavy chain / calprotectin L1H subunit

Details:

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

A-1501 A-1502 B-2501 B-2502 C-3501 C-3502 D-4501 D-4502 E-1511 E-1512 F-2511 F-2512 G-3511 G-3512 H-4511 H-4512 I-1521 I-1522 J-2521 J-2522 ...
ChemComp-CA / CALCIUM ION

Details:

Mass: 40.078 Da / Num. of mol.: 24 / Source method: obtained synthetically / Formula: Ca

#4: Chemical

A-2004 B-2005 F-2006 J-2007
ChemComp-CL / CHLORIDE ION

Details:

Mass: 35.453 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Cl

#5: Chemical

F-2008 ChemComp-FLC / CITRATE ANION

Details:

Mass: 189.100 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₆H₅O₇

#6: Water

ChemComp-HOH / water

Details:

Mass: 18.015 Da / Num. of mol.: 1059 / Source method: isolated from a natural source / Formula: H₂O

Experimental details

Experiment

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

Sample preparation

• Crystal: Density Matthews: 2.4 ų/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

	Rfactor	Num. reflection	% reflection	Selection details
Rfree	0.20475	5004	5 %	RANDOM
Rwork	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 Ų

	Baniso -1	Baniso -2	Baniso -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

	Rfactor	Num. reflection	% reflection
Rfree	0.249	303	-
Rwork	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