PDB-2bb6: Structure of Cobalamin-complexed Bovine Transcobalamin in Monocli...

Basic information

• Entry: Database: PDB / ID: 2bb6
• Title: Structure of Cobalamin-complexed Bovine Transcobalamin in Monoclinic Crystal Form
• Components: Transcobalamin II
• Keywords: TRANSPORT PROTEIN / alpha_6 - alpha_6 barrel

Function / homology

Function:

Transport of RCbl within the body / cobalt ion transport / cobalamin transport / cobalamin binding / extracellular space / metal ion binding

Domain/homology:

Ferric Hydroxamate Uptake Protein; Chain A, domain 1 - #30 / Cobalamin (vitamin B12)-binding protein / Eukaryotic cobalamin-binding protein / Eukaryotic cobalamin-binding proteins signature. / Ferric Hydroxamate Uptake Protein; Chain A, domain 1 / Glycosyltransferase - #20 / Glycosyltransferase / Alpha/alpha barrel / Beta Complex / Mainly Beta / Mainly Alpha

Component:

COBALAMIN / Transcobalamin-2

• Biological species: Bos taurus (cattle)
• Method: X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å
• Authors: Wuerges, J. / Garau, G. / Geremia, S. / Fedosov, S.N. / Petersen, T.E. / Randaccio, L.
• Citation: Journal: Proc.Natl.Acad.Sci.Usa / Year: 2006; Title: Structural basis for mammalian vitamin B12 transport by transcobalamin.; Authors: Wuerges, J. / Garau, G. / Geremia, S. / Fedosov, S.N. / Petersen, T.E. / Randaccio, L.

History

Deposition	Oct 17, 2005	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Apr 4, 2006	Provider: repository / Type: Initial release
Revision 1.1	May 1, 2008	Group: Version format compliance
Revision 1.2	Jul 13, 2011	Group: Version format compliance
Revision 1.3	Oct 24, 2012	Group: Non-polymer description
Revision 1.4	Oct 11, 2017	Group: Refinement description / Category: software
Revision 1.5	Apr 3, 2024	Group: Data collection / Database references / Derived calculations / Refinement description Category: chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_conn / struct_ncs_dom_lim / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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.end_auth_comp_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

• Remark 650: HELIX DETERMINATION METHOD: AUTHOR PROVIDED
• Remark 700: SHEET DETERMINATION METHOD: AUTHOR PROVIDED.

Assembly

Deposited unit

A: Transcobalamin II

B: Transcobalamin II

C: Transcobalamin II

D: Transcobalamin II

A: COBALAMIN

B: COBALAMIN

C: COBALAMIN

D: COBALAMIN

hetero molecules

Summary:

• 191 kDa, 4 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	190,724	12
Polymers	185,261	4
Non-polymers	5,463	8
Water	13,763	764

1

A: Transcobalamin II

hetero molecules

Summary:

• defined by author
• 47.7 kDa, 1 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	47,681	3
Polymers	46,315	1
Non-polymers	1,366	2
Water	18	1

Symmetry operations:

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

2

B: Transcobalamin II

hetero molecules

Summary:

• defined by author
• 47.7 kDa, 1 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	47,681	3
Polymers	46,315	1
Non-polymers	1,366	2
Water	18	1

Symmetry operations:

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

3

C: Transcobalamin II

hetero molecules

Summary:

• defined by author
• 47.7 kDa, 1 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	47,681	3
Polymers	46,315	1
Non-polymers	1,366	2
Water	18	1

Symmetry operations:

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

4

D: Transcobalamin II

hetero molecules

Summary:

• defined by author
• 47.7 kDa, 1 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	47,681	3
Polymers	46,315	1
Non-polymers	1,366	2
Water	18	1

Symmetry operations:

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

Unit cell

Length a, b, c (Å)	95.826, 100.664, 99.143
Angle α, β, γ (deg.)	90.00, 97.16, 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	A
4	1	B
5	1	A
6	1	B
7	1	A
8	1	B
9	1	A
10	1	B
11	1	A
12	1	B
13	1	A
14	1	B
15	1	A
16	1	B
17	1	A
18	1	B
19	1	A
20	1	B
21	1	A
22	1	B
23	1	A
24	1	B
25	1	A
26	1	B
27	1	A
28	1	B
29	1	A
30	1	B
31	1	A
32	1	B
33	1	A
34	1	B
35	1	A
36	1	B
37	1	A
38	1	B
39	1	A
40	1	B
41	1	A
42	1	B
43	1	A
44	1	B
45	1	A
46	1	B
47	1	A
48	1	B
49	1	A
50	1	B
51	1	A
52	1	B
53	1	A
54	1	B
55	1	A
56	1	B
57	1	A
58	1	B
59	1	A
60	1	B
1	2	C
2	2	D
3	2	C
4	2	D
5	2	C
6	2	D
7	2	C
8	2	D
9	2	C
10	2	D
11	2	C
12	2	D
13	2	C
14	2	D
15	2	C
16	2	D
17	2	C
18	2	D
19	2	C
20	2	D
21	2	C
22	2	D
23	2	C
24	2	D
25	2	C
26	2	D
27	2	C
28	2	D
29	2	C
30	2	D
31	2	C
32	2	D
33	2	C
34	2	D
35	2	C
36	2	D
37	2	C
38	2	D
39	2	C
40	2	D
41	2	C
42	2	D
43	2	C
44	2	D
45	2	C
46	2	D
47	2	C
48	2	D
49	2	C
50	2	D
51	2	C
52	2	D
53	2	C
54	2	D
55	2	C
56	2	D
57	2	C
58	2	D
59	2	C
60	2	D
1	3	A
2	3	C
3	3	A
4	3	C
5	3	A
6	3	C
7	3	A
8	3	C
9	3	A
10	3	C
11	3	A
12	3	C
13	3	A
14	3	C
15	3	A
16	3	C
17	3	A
18	3	C
19	3	A
20	3	C
21	3	A
22	3	C
23	3	A
24	3	C
25	3	A
26	3	C
27	3	A
28	3	C
29	3	A
30	3	C
31	3	A
32	3	C
33	3	A
34	3	C
35	3	A
36	3	C
37	3	A
38	3	C
39	3	A
40	3	C
41	3	A
42	3	C
43	3	A
44	3	C
45	3	A
46	3	C
47	3	A
48	3	C
49	3	A
50	3	C
51	3	A
52	3	C
53	3	A
54	3	C
55	3	A
56	3	C
57	3	A
58	3	C
59	3	A
60	3	C
61	3	A
62	3	C
63	3	A
64	3	C
65	3	A
66	3	C
67	3	A
68	3	C
69	3	A
70	3	C
71	3	A
72	3	C
1	4	A
2	4	D
3	4	A
4	4	D
5	4	A
6	4	D
7	4	A
8	4	D
9	4	A
10	4	D
11	4	A
12	4	D
13	4	A
14	4	D
15	4	A
16	4	D
17	4	A
18	4	D
19	4	A
20	4	D
21	4	A
22	4	D
23	4	A
24	4	D
25	4	A
26	4	D
27	4	A
28	4	D
29	4	A
30	4	D
31	4	A
32	4	D
33	4	A
34	4	D
35	4	A
36	4	D
37	4	A
38	4	D
39	4	A
40	4	D
41	4	A
42	4	D
43	4	A
44	4	D
45	4	A
46	4	D
47	4	A
48	4	D
49	4	A
50	4	D
51	4	A
52	4	D
53	4	A
54	4	D
55	4	A
56	4	D
57	4	A
58	4	D
59	4	A
60	4	D
61	4	A
62	4	D
63	4	A
64	4	D
65	4	A
66	4	D
67	4	A
68	4	D
69	4	A
70	4	D
71	4	A
72	4	D
73	4	A
74	4	D
75	4	A
76	4	D
1	5	B
2	5	C
3	5	B
4	5	C
5	5	B
6	5	C
7	5	B
8	5	C
9	5	B
10	5	C
11	5	B
12	5	C
13	5	B
14	5	C
15	5	B
16	5	C
17	5	B
18	5	C
19	5	B
20	5	C
21	5	B
22	5	C
23	5	B
24	5	C
25	5	B
26	5	C
27	5	B
28	5	C
29	5	B
30	5	C
31	5	B
32	5	C
33	5	B
34	5	C
35	5	B
36	5	C
37	5	B
38	5	C
39	5	B
40	5	C
41	5	B
42	5	C
43	5	B
44	5	C
45	5	B
46	5	C
47	5	B
48	5	C
49	5	B
50	5	C
51	5	B
52	5	C
53	5	B
54	5	C
55	5	B
56	5	C
57	5	B
58	5	C
59	5	B
60	5	C
61	5	B
62	5	C
63	5	B
64	5	C
65	5	B
66	5	C
67	5	B
68	5	C
69	5	B
70	5	C
71	5	B
72	5	C
1	6	B
2	6	D
3	6	B
4	6	D
5	6	B
6	6	D
7	6	B
8	6	D
9	6	B
10	6	D
11	6	B
12	6	D
13	6	B
14	6	D
15	6	B
16	6	D
17	6	B
18	6	D
19	6	B
20	6	D
21	6	B
22	6	D
23	6	B
24	6	D
25	6	B
26	6	D
27	6	B
28	6	D
29	6	B
30	6	D
31	6	B
32	6	D
33	6	B
34	6	D
35	6	B
36	6	D
37	6	B
38	6	D
39	6	B
40	6	D
41	6	B
42	6	D
43	6	B
44	6	D
45	6	B
46	6	D
47	6	B
48	6	D
49	6	B
50	6	D
51	6	B
52	6	D
53	6	B
54	6	D
55	6	B
56	6	D
57	6	B
58	6	D
59	6	B
60	6	D
61	6	B
62	6	D
63	6	B
64	6	D
65	6	B
66	6	D
67	6	B
68	6	D
69	6	B
70	6	D
71	6	B
72	6	D
73	6	B
74	6	D
75	6	B
76	6	D

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	ASN	ASN	THR	THR	1	A	A	1 - 6	1 - 6
2	1	1	ASN	ASN	THR	THR	1	B	B	1 - 6	1 - 6
3	2	1	GLU	GLU	GLU	GLU	2	A	A	7	7
4	2	1	GLU	GLU	GLU	GLU	2	B	B	7	7
5	3	1	VAL	VAL	GLN	GLN	1	A	A	8 - 63	8 - 63
6	3	1	VAL	VAL	GLN	GLN	1	B	B	8 - 63	8 - 63
7	4	1	ARG	ARG	ALA	ALA	6	A	A	68 - 80	68 - 80
8	4	1	ARG	ARG	ALA	ALA	6	B	B	68 - 80	68 - 80
9	5	1	LYS	LYS	LYS	LYS	1	A	A	81 - 114	81 - 114
10	5	1	LYS	LYS	LYS	LYS	1	B	B	81 - 114	81 - 114
11	6	1	ARG	ARG	ARG	ARG	2	A	A	115	115
12	6	1	ARG	ARG	ARG	ARG	2	B	B	115	115
13	7	1	PHE	PHE	LYS	LYS	1	A	A	116 - 121	116 - 121
14	7	1	PHE	PHE	LYS	LYS	1	B	B	116 - 121	116 - 121
15	8	1	HIS	HIS	GLN	GLN	4	A	A	126 - 129	126 - 129
16	8	1	HIS	HIS	GLN	GLN	4	B	B	126 - 129	126 - 129
17	9	1	GLY	GLY	GLU	GLU	1	A	A	130 - 166	130 - 166
18	9	1	GLY	GLY	GLU	GLU	1	B	B	130 - 166	130 - 166
19	10	1	HIS	HIS	ASP	ASP	5	A	A	167 - 174	167 - 174
20	10	1	HIS	HIS	ASP	ASP	5	B	B	167 - 174	167 - 174
21	11	1	HIS	HIS	GLN	GLN	1	A	A	175 - 200	175 - 200
22	11	1	HIS	HIS	GLN	GLN	1	B	B	175 - 200	175 - 200
23	12	1	ARG	ARG	ARG	ARG	2	A	A	201	201
24	12	1	ARG	ARG	ARG	ARG	2	B	B	201	201
25	13	1	ASN	ASN	MET	MET	1	A	A	202 - 239	202 - 239
26	13	1	ASN	ASN	MET	MET	1	B	B	202 - 239	202 - 239
27	14	1	GLY	GLY	PRO	PRO	4	A	A	240 - 244	240 - 244
28	14	1	GLY	GLY	PRO	PRO	4	B	B	240 - 244	240 - 244
29	15	1	SER	SER	VAL	VAL	1	A	A	245 - 246	245 - 246
30	15	1	SER	SER	VAL	VAL	1	B	B	245 - 246	245 - 246
31	16	1	GLU	GLU	GLU	GLU	2	A	A	247	247
32	16	1	GLU	GLU	GLU	GLU	2	B	B	247	247
33	17	1	LEU	LEU	GLN	GLN	1	A	A	248 - 264	248 - 264
34	17	1	LEU	LEU	GLN	GLN	1	B	B	248 - 264	248 - 264
35	18	1	HIS	HIS	LYS	LYS	2	A	A	265 - 266	265 - 266
36	18	1	HIS	HIS	LYS	LYS	2	B	B	265 - 266	265 - 266
37	19	1	THR	THR	PRO	PRO	1	A	A	267 - 303	267 - 303
38	19	1	THR	THR	PRO	PRO	1	B	B	267 - 303	267 - 303
39	20	1	ALA	ALA	GLN	GLN	6	A	A	304 - 310	304 - 310
40	20	1	ALA	ALA	GLN	GLN	6	B	B	304 - 310	304 - 310
41	21	1	ALA	ALA	VAL	VAL	4	A	A	311 - 313	311 - 313
42	21	1	ALA	ALA	VAL	VAL	4	B	B	311 - 313	311 - 313
43	22	1	PRO	PRO	PHE	PHE	1	A	A	314 - 355	314 - 355
44	22	1	PRO	PRO	PHE	PHE	1	B	B	314 - 355	314 - 355
45	23	1	LYS	LYS	LYS	LYS	2	A	A	375	375
46	23	1	LYS	LYS	LYS	LYS	2	B	B	375	375
47	24	1	ALA	ALA	TRP	TRP	1	A	A	376 - 414	376 - 414
48	24	1	ALA	ALA	TRP	TRP	1	B	B	376 - 414	376 - 414
49	25	1	GLN	GLN	GLN	GLN	2	A	A	64	64
50	25	1	GLN	GLN	GLN	GLN	2	B	B	64	64
51	26	1	SER	SER	LEU	LEU	1	A	A	65 - 67	65 - 67
52	26	1	SER	SER	LEU	LEU	1	B	B	65 - 67	65 - 67
53	27	1	ARG	ARG	ARG	ARG	3	A	A	122	122
54	27	1	ARG	ARG	ARG	ARG	3	B	B	122	122
55	28	1	ALA	ALA	GLY	GLY	1	A	A	123 - 125	123 - 125
56	28	1	ALA	ALA	GLY	GLY	1	B	B	123 - 125	123 - 125
57	29	1	ARG	ARG	ARG	ARG	2	A	A	356 - 358	356 - 358
58	29	1	ARG	ARG	ARG	ARG	2	B	B	356 - 358	356 - 358
59	30	1	THR	THR	ARG	ARG	1	A	A	359 - 374	359 - 374
60	30	1	THR	THR	ARG	ARG	1	B	B	359 - 374	359 - 374
1	1	2	ASN	ASN	THR	THR	1	C	C	1 - 6	1 - 6
2	1	2	ASN	ASN	THR	THR	1	D	D	1 - 6	1 - 6
3	2	2	GLU	GLU	GLU	GLU	2	C	C	7	7
4	2	2	GLU	GLU	GLU	GLU	2	D	D	7	7
5	3	2	VAL	VAL	THR	THR	1	C	C	8 - 11	8 - 11
6	3	2	VAL	VAL	THR	THR	1	D	D	8 - 11	8 - 11
7	4	2	ARG	ARG	ALA	ALA	6	C	C	68 - 80	68 - 80
8	4	2	ARG	ARG	ALA	ALA	6	D	D	68 - 80	68 - 80
9	5	2	LYS	LYS	LYS	LYS	1	C	C	81 - 114	81 - 114
10	5	2	LYS	LYS	LYS	LYS	1	D	D	81 - 114	81 - 114
11	6	2	ARG	ARG	ARG	ARG	2	C	C	115	115
12	6	2	ARG	ARG	ARG	ARG	2	D	D	115	115
13	7	2	PHE	PHE	LYS	LYS	1	C	C	116 - 121	116 - 121
14	7	2	PHE	PHE	LYS	LYS	1	D	D	116 - 121	116 - 121
15	8	2	HIS	HIS	GLN	GLN	4	C	C	126 - 129	126 - 129
16	8	2	HIS	HIS	GLN	GLN	4	D	D	126 - 129	126 - 129
17	9	2	GLY	GLY	GLU	GLU	1	C	C	130 - 166	130 - 166
18	9	2	GLY	GLY	GLU	GLU	1	D	D	130 - 166	130 - 166
19	10	2	HIS	HIS	HIS	HIS	4	C	C	167	167
20	10	2	HIS	HIS	HIS	HIS	4	D	D	167	167
21	11	2	LYS	LYS	PRO	PRO	6	C	C	168 - 169	168 - 169
22	11	2	LYS	LYS	PRO	PRO	6	D	D	168 - 169	168 - 169
23	12	2	HIS	HIS	ASP	ASP	4	C	C	170 - 174	170 - 174
24	12	2	HIS	HIS	ASP	ASP	4	D	D	170 - 174	170 - 174
25	13	2	HIS	HIS	GLN	GLN	1	C	C	175 - 200	175 - 200
26	13	2	HIS	HIS	GLN	GLN	1	D	D	175 - 200	175 - 200
27	14	2	ARG	ARG	ARG	ARG	2	C	C	201	201
28	14	2	ARG	ARG	ARG	ARG	2	D	D	201	201
29	15	2	ASN	ASN	MET	MET	1	C	C	202 - 239	202 - 239
30	15	2	ASN	ASN	MET	MET	1	D	D	202 - 239	202 - 239
31	16	2	GLY	GLY	PRO	PRO	2	C	C	240 - 244	240 - 244
32	16	2	GLY	GLY	PRO	PRO	2	D	D	240 - 244	240 - 244
33	17	2	SER	SER	VAL	VAL	1	C	C	245 - 246	245 - 246
34	17	2	SER	SER	VAL	VAL	1	D	D	245 - 246	245 - 246
35	18	2	GLU	GLU	GLU	GLU	2	C	C	247	247
36	18	2	GLU	GLU	GLU	GLU	2	D	D	247	247
37	19	2	LEU	LEU	HIS	HIS	1	C	C	248 - 265	248 - 265
38	19	2	LEU	LEU	HIS	HIS	1	D	D	248 - 265	248 - 265
39	20	2	LYS	LYS	LYS	LYS	2	C	C	266	266
40	20	2	LYS	LYS	LYS	LYS	2	D	D	266	266
41	21	2	THR	THR	PRO	PRO	1	C	C	267 - 303	267 - 303
42	21	2	THR	THR	PRO	PRO	1	D	D	267 - 303	267 - 303
43	22	2	VAL	VAL	VAL	VAL	6	C	C	313	313
44	22	2	VAL	VAL	VAL	VAL	6	D	D	313	313
45	23	2	PRO	PRO	PRO	PRO	4	C	C	314	314
46	23	2	PRO	PRO	PRO	PRO	4	D	D	314	314
47	24	2	LYS	LYS	ARG	ARG	1	C	C	315 - 374	315 - 374
48	24	2	LYS	LYS	ARG	ARG	1	D	D	315 - 374	315 - 374
49	25	2	LYS	LYS	LYS	LYS	2	C	C	375	375
50	25	2	LYS	LYS	LYS	LYS	2	D	D	375	375
51	26	2	ALA	ALA	TRP	TRP	1	C	C	376 - 414	376 - 414
52	26	2	ALA	ALA	TRP	TRP	1	D	D	376 - 414	376 - 414
53	27	2	LEU	LEU	LEU	LEU	3	C	C	12	12
54	27	2	LEU	LEU	LEU	LEU	3	D	D	12	12
55	28	2	VAL	VAL	LEU	LEU	1	C	C	13 - 67	13 - 67
56	28	2	VAL	VAL	LEU	LEU	1	D	D	13 - 67	13 - 67
57	29	2	ARG	ARG	ARG	ARG	2	C	C	122	122
58	29	2	ARG	ARG	ARG	ARG	2	D	D	122	122
59	30	2	ALA	ALA	GLY	GLY	1	C	C	123 - 125	123 - 125
60	30	2	ALA	ALA	GLY	GLY	1	D	D	123 - 125	123 - 125
1	1	3	ASN	ASN	ILE	ILE	1	A	A	1 - 5	1 - 5
2	1	3	ASN	ASN	ILE	ILE	1	C	C	1 - 5	1 - 5
3	2	3	THR	THR	GLU	GLU	2	A	A	6 - 7	6 - 7
4	2	3	THR	THR	GLU	GLU	2	C	C	6 - 7	6 - 7
5	3	3	VAL	VAL	SER	SER	1	A	A	8 - 28	8 - 28
6	3	3	VAL	VAL	SER	SER	1	C	C	8 - 28	8 - 28
7	4	3	GLN	GLN	GLN	GLN	2	A	A	29 - 31	29 - 31
8	4	3	GLN	GLN	GLN	GLN	2	C	C	29 - 31	29 - 31
9	5	3	LEU	LEU	GLY	GLY	1	A	A	32 - 39	32 - 39
10	5	3	LEU	LEU	GLY	GLY	1	C	C	32 - 39	32 - 39
11	6	3	LEU	LEU	LEU	LEU	2	A	A	40	40
12	6	3	LEU	LEU	LEU	LEU	2	C	C	40	40
13	7	3	ARG	ARG	LYS	LYS	1	A	A	41 - 59	41 - 59
14	7	3	ARG	ARG	LYS	LYS	1	C	C	41 - 59	41 - 59
15	8	3	LEU	LEU	LEU	LEU	2	A	A	60 - 67	60 - 67
16	8	3	LEU	LEU	LEU	LEU	2	C	C	60 - 67	60 - 67
17	9	3	ARG	ARG	ALA	ALA	6	A	A	68 - 80	68 - 80
18	9	3	ARG	ARG	ALA	ALA	6	C	C	68 - 80	68 - 80
19	10	3	LYS	LYS	GLY	GLY	1	A	A	81 - 103	81 - 103
20	10	3	LYS	LYS	GLY	GLY	1	C	C	81 - 103	81 - 103
21	11	3	ARG	ARG	LYS	LYS	2	A	A	104 - 105	104 - 105
22	11	3	ARG	ARG	LYS	LYS	2	C	C	104 - 105	104 - 105
23	12	3	GLY	GLY	LYS	LYS	1	A	A	106 - 114	106 - 114
24	12	3	GLY	GLY	LYS	LYS	1	C	C	106 - 114	106 - 114
25	13	3	ARG	ARG	ARG	ARG	2	A	A	115	115
26	13	3	ARG	ARG	ARG	ARG	2	C	C	115	115
27	14	3	PHE	PHE	LYS	LYS	1	A	A	116 - 121	116 - 121
28	14	3	PHE	PHE	LYS	LYS	1	C	C	116 - 121	116 - 121
29	15	3	ARG	ARG	ARG	ARG	3	A	A	122	122
30	15	3	ARG	ARG	ARG	ARG	3	C	C	122	122
31	16	3	ALA	ALA	GLY	GLY	1	A	A	123 - 125	123 - 125
32	16	3	ALA	ALA	GLY	GLY	1	C	C	123 - 125	123 - 125
33	17	3	HIS	HIS	GLN	GLN	6	A	A	126 - 129	126 - 129
34	17	3	HIS	HIS	GLN	GLN	6	C	C	126 - 129	126 - 129
35	18	3	GLY	GLY	GLU	GLU	1	A	A	130 - 166	130 - 166
36	18	3	GLY	GLY	GLU	GLU	1	C	C	130 - 166	130 - 166
37	19	3	HIS	HIS	HIS	HIS	6	A	A	167 - 170	167 - 170
38	19	3	HIS	HIS	HIS	HIS	6	C	C	167 - 170	167 - 170
39	20	3	LEU	LEU	ASP	ASP	5	A	A	171 - 174	171 - 174
40	20	3	LEU	LEU	ASP	ASP	5	C	C	171 - 174	171 - 174
41	21	3	HIS	HIS	GLN	GLN	1	A	A	175 - 200	175 - 200
42	21	3	HIS	HIS	GLN	GLN	1	C	C	175 - 200	175 - 200
43	22	3	ARG	ARG	ARG	ARG	2	A	A	201	201
44	22	3	ARG	ARG	ARG	ARG	2	C	C	201	201
45	23	3	ASN	ASN	MET	MET	1	A	A	202 - 239	202 - 239
46	23	3	ASN	ASN	MET	MET	1	C	C	202 - 239	202 - 239
47	24	3	GLY	GLY	PRO	PRO	6	A	A	240 - 244	240 - 244
48	24	3	GLY	GLY	PRO	PRO	6	C	C	240 - 244	240 - 244
49	25	3	SER	SER	VAL	VAL	1	A	A	245 - 246	245 - 246
50	25	3	SER	SER	VAL	VAL	1	C	C	245 - 246	245 - 246
51	26	3	GLU	GLU	GLU	GLU	2	A	A	247	247
52	26	3	GLU	GLU	GLU	GLU	2	C	C	247	247
53	27	3	LEU	LEU	HIS	HIS	1	A	A	248 - 265	248 - 265
54	27	3	LEU	LEU	HIS	HIS	1	C	C	248 - 265	248 - 265
55	28	3	LYS	LYS	LYS	LYS	2	A	A	266	266
56	28	3	LYS	LYS	LYS	LYS	2	C	C	266	266
57	29	3	THR	THR	PRO	PRO	1	A	A	267 - 303	267 - 303
58	29	3	THR	THR	PRO	PRO	1	C	C	267 - 303	267 - 303
59	30	3	PRO	PRO	PRO	PRO	4	A	A	314	314
60	30	3	PRO	PRO	PRO	PRO	4	C	C	314	314
61	31	3	LYS	LYS	LYS	LYS	1	A	A	315 - 347	315 - 347
62	31	3	LYS	LYS	LYS	LYS	1	C	C	315 - 347	315 - 347
63	32	3	ASN	ASN	ARG	ARG	2	A	A	348 - 358	348 - 358
64	32	3	ASN	ASN	ARG	ARG	2	C	C	348 - 358	348 - 358
65	33	3	THR	THR	ARG	ARG	1	A	A	359 - 374	359 - 374
66	33	3	THR	THR	ARG	ARG	1	C	C	359 - 374	359 - 374
67	34	3	LYS	LYS	LYS	LYS	2	A	A	375	375
68	34	3	LYS	LYS	LYS	LYS	2	C	C	375	375
69	35	3	ALA	ALA	VAL	VAL	1	A	A	376 - 412	376 - 412
70	35	3	ALA	ALA	VAL	VAL	1	C	C	376 - 412	376 - 412
71	36	3	GLY	GLY	TRP	TRP	4	A	A	413 - 414	413 - 414
72	36	3	GLY	GLY	TRP	TRP	4	C	C	413 - 414	413 - 414
1	1	4	ASN	ASN	ILE	ILE	1	A	A	1 - 5	1 - 5
2	1	4	ASN	ASN	ILE	ILE	1	D	D	1 - 5	1 - 5
3	2	4	THR	THR	GLU	GLU	2	A	A	6 - 7	6 - 7
4	2	4	THR	THR	GLU	GLU	2	D	D	6 - 7	6 - 7
5	3	4	VAL	VAL	THR	THR	1	A	A	8 - 11	8 - 11
6	3	4	VAL	VAL	THR	THR	1	D	D	8 - 11	8 - 11
7	4	4	GLN	GLN	GLN	GLN	2	A	A	29 - 31	29 - 31
8	4	4	GLN	GLN	GLN	GLN	2	D	D	29 - 31	29 - 31
9	5	4	LEU	LEU	GLY	GLY	1	A	A	32 - 39	32 - 39
10	5	4	LEU	LEU	GLY	GLY	1	D	D	32 - 39	32 - 39
11	6	4	LEU	LEU	LEU	LEU	2	A	A	40	40
12	6	4	LEU	LEU	LEU	LEU	2	D	D	40	40
13	7	4	ARG	ARG	LYS	LYS	1	A	A	41 - 59	41 - 59
14	7	4	ARG	ARG	LYS	LYS	1	D	D	41 - 59	41 - 59
15	8	4	LEU	LEU	LEU	LEU	2	A	A	60 - 67	60 - 67
16	8	4	LEU	LEU	LEU	LEU	2	D	D	60 - 67	60 - 67
17	9	4	ARG	ARG	ALA	ALA	6	A	A	68 - 80	68 - 80
18	9	4	ARG	ARG	ALA	ALA	6	D	D	68 - 80	68 - 80
19	10	4	LYS	LYS	GLY	GLY	1	A	A	81 - 103	81 - 103
20	10	4	LYS	LYS	GLY	GLY	1	D	D	81 - 103	81 - 103
21	11	4	ARG	ARG	LYS	LYS	2	A	A	104 - 105	104 - 105
22	11	4	ARG	ARG	LYS	LYS	2	D	D	104 - 105	104 - 105
23	12	4	GLY	GLY	LYS	LYS	1	A	A	106 - 114	106 - 114
24	12	4	GLY	GLY	LYS	LYS	1	D	D	106 - 114	106 - 114
25	13	4	ARG	ARG	ARG	ARG	2	A	A	115	115
26	13	4	ARG	ARG	ARG	ARG	2	D	D	115	115
27	14	4	PHE	PHE	LYS	LYS	1	A	A	116 - 121	116 - 121
28	14	4	PHE	PHE	LYS	LYS	1	D	D	116 - 121	116 - 121
29	15	4	ARG	ARG	ARG	ARG	3	A	A	122	122
30	15	4	ARG	ARG	ARG	ARG	3	D	D	122	122
31	16	4	ALA	ALA	GLY	GLY	1	A	A	123 - 125	123 - 125
32	16	4	ALA	ALA	GLY	GLY	1	D	D	123 - 125	123 - 125
33	17	4	HIS	HIS	GLN	GLN	6	A	A	126 - 129	126 - 129
34	17	4	HIS	HIS	GLN	GLN	6	D	D	126 - 129	126 - 129
35	18	4	GLY	GLY	GLU	GLU	1	A	A	130 - 166	130 - 166
36	18	4	GLY	GLY	GLU	GLU	1	D	D	130 - 166	130 - 166
37	19	4	HIS	HIS	HIS	HIS	6	A	A	167 - 170	167 - 170
38	19	4	HIS	HIS	HIS	HIS	6	D	D	167 - 170	167 - 170
39	20	4	LEU	LEU	ASP	ASP	5	A	A	171 - 174	171 - 174
40	20	4	LEU	LEU	ASP	ASP	5	D	D	171 - 174	171 - 174
41	21	4	HIS	HIS	GLN	GLN	1	A	A	175 - 200	175 - 200
42	21	4	HIS	HIS	GLN	GLN	1	D	D	175 - 200	175 - 200
43	22	4	ARG	ARG	ARG	ARG	2	A	A	201	201
44	22	4	ARG	ARG	ARG	ARG	2	D	D	201	201
45	23	4	ASN	ASN	MET	MET	1	A	A	202 - 239	202 - 239
46	23	4	ASN	ASN	MET	MET	1	D	D	202 - 239	202 - 239
47	24	4	GLY	GLY	PRO	PRO	6	A	A	240 - 244	240 - 244
48	24	4	GLY	GLY	PRO	PRO	6	D	D	240 - 244	240 - 244
49	25	4	SER	SER	VAL	VAL	1	A	A	245 - 246	245 - 246
50	25	4	SER	SER	VAL	VAL	1	D	D	245 - 246	245 - 246
51	26	4	GLU	GLU	GLU	GLU	2	A	A	247	247
52	26	4	GLU	GLU	GLU	GLU	2	D	D	247	247
53	27	4	LEU	LEU	HIS	HIS	1	A	A	248 - 265	248 - 265
54	27	4	LEU	LEU	HIS	HIS	1	D	D	248 - 265	248 - 265
55	28	4	LYS	LYS	LYS	LYS	2	A	A	266	266
56	28	4	LYS	LYS	LYS	LYS	2	D	D	266	266
57	29	4	THR	THR	PRO	PRO	1	A	A	267 - 303	267 - 303
58	29	4	THR	THR	PRO	PRO	1	D	D	267 - 303	267 - 303
59	30	4	PRO	PRO	PRO	PRO	4	A	A	314	314
60	30	4	PRO	PRO	PRO	PRO	4	D	D	314	314
61	31	4	LYS	LYS	LYS	LYS	1	A	A	315 - 347	315 - 347
62	31	4	LYS	LYS	LYS	LYS	1	D	D	315 - 347	315 - 347
63	32	4	ASN	ASN	ARG	ARG	2	A	A	348 - 358	348 - 358
64	32	4	ASN	ASN	ARG	ARG	2	D	D	348 - 358	348 - 358
65	33	4	THR	THR	ARG	ARG	1	A	A	359 - 374	359 - 374
66	33	4	THR	THR	ARG	ARG	1	D	D	359 - 374	359 - 374
67	34	4	LYS	LYS	LYS	LYS	2	A	A	375	375
68	34	4	LYS	LYS	LYS	LYS	2	D	D	375	375
69	35	4	ALA	ALA	VAL	VAL	1	A	A	376 - 412	376 - 412
70	35	4	ALA	ALA	VAL	VAL	1	D	D	376 - 412	376 - 412
71	36	4	LEU	LEU	LEU	LEU	3	A	A	12	12
72	36	4	LEU	LEU	LEU	LEU	3	D	D	12	12
73	37	4	VAL	VAL	SER	SER	1	A	A	13 - 28	13 - 28
74	37	4	VAL	VAL	SER	SER	1	D	D	13 - 28	13 - 28
75	38	4	GLY	GLY	TRP	TRP	4	A	A	413 - 414	413 - 414
76	38	4	GLY	GLY	TRP	TRP	4	D	D	413 - 414	413 - 414
1	1	5	ASN	ASN	ILE	ILE	1	B	B	1 - 5	1 - 5
2	1	5	ASN	ASN	ILE	ILE	1	C	C	1 - 5	1 - 5
3	2	5	THR	THR	GLU	GLU	2	B	B	6 - 7	6 - 7
4	2	5	THR	THR	GLU	GLU	2	C	C	6 - 7	6 - 7
5	3	5	VAL	VAL	SER	SER	1	B	B	8 - 28	8 - 28
6	3	5	VAL	VAL	SER	SER	1	C	C	8 - 28	8 - 28
7	4	5	GLN	GLN	GLN	GLN	2	B	B	29 - 31	29 - 31
8	4	5	GLN	GLN	GLN	GLN	2	C	C	29 - 31	29 - 31
9	5	5	LEU	LEU	GLY	GLY	1	B	B	32 - 39	32 - 39
10	5	5	LEU	LEU	GLY	GLY	1	C	C	32 - 39	32 - 39
11	6	5	LEU	LEU	LEU	LEU	2	B	B	40	40
12	6	5	LEU	LEU	LEU	LEU	2	C	C	40	40
13	7	5	ARG	ARG	LYS	LYS	1	B	B	41 - 59	41 - 59
14	7	5	ARG	ARG	LYS	LYS	1	C	C	41 - 59	41 - 59
15	8	5	LEU	LEU	LEU	LEU	2	B	B	60 - 67	60 - 67
16	8	5	LEU	LEU	LEU	LEU	2	C	C	60 - 67	60 - 67
17	9	5	ARG	ARG	ALA	ALA	6	B	B	68 - 80	68 - 80
18	9	5	ARG	ARG	ALA	ALA	6	C	C	68 - 80	68 - 80
19	10	5	LYS	LYS	GLY	GLY	1	B	B	81 - 103	81 - 103
20	10	5	LYS	LYS	GLY	GLY	1	C	C	81 - 103	81 - 103
21	11	5	ARG	ARG	LYS	LYS	2	B	B	104 - 105	104 - 105
22	11	5	ARG	ARG	LYS	LYS	2	C	C	104 - 105	104 - 105
23	12	5	GLY	GLY	LYS	LYS	1	B	B	106 - 114	106 - 114
24	12	5	GLY	GLY	LYS	LYS	1	C	C	106 - 114	106 - 114
25	13	5	ARG	ARG	ARG	ARG	2	B	B	115	115
26	13	5	ARG	ARG	ARG	ARG	2	C	C	115	115
27	14	5	PHE	PHE	LYS	LYS	1	B	B	116 - 121	116 - 121
28	14	5	PHE	PHE	LYS	LYS	1	C	C	116 - 121	116 - 121
29	15	5	ARG	ARG	ARG	ARG	3	B	B	122	122
30	15	5	ARG	ARG	ARG	ARG	3	C	C	122	122
31	16	5	ALA	ALA	GLY	GLY	1	B	B	123 - 125	123 - 125
32	16	5	ALA	ALA	GLY	GLY	1	C	C	123 - 125	123 - 125
33	17	5	HIS	HIS	GLN	GLN	6	B	B	126 - 129	126 - 129
34	17	5	HIS	HIS	GLN	GLN	6	C	C	126 - 129	126 - 129
35	18	5	GLY	GLY	GLU	GLU	1	B	B	130 - 166	130 - 166
36	18	5	GLY	GLY	GLU	GLU	1	C	C	130 - 166	130 - 166
37	19	5	HIS	HIS	HIS	HIS	6	B	B	167 - 170	167 - 170
38	19	5	HIS	HIS	HIS	HIS	6	C	C	167 - 170	167 - 170
39	20	5	LEU	LEU	ASP	ASP	5	B	B	171 - 174	171 - 174
40	20	5	LEU	LEU	ASP	ASP	5	C	C	171 - 174	171 - 174
41	21	5	HIS	HIS	GLN	GLN	1	B	B	175 - 200	175 - 200
42	21	5	HIS	HIS	GLN	GLN	1	C	C	175 - 200	175 - 200
43	22	5	ARG	ARG	ARG	ARG	2	B	B	201	201
44	22	5	ARG	ARG	ARG	ARG	2	C	C	201	201
45	23	5	ASN	ASN	MET	MET	1	B	B	202 - 239	202 - 239
46	23	5	ASN	ASN	MET	MET	1	C	C	202 - 239	202 - 239
47	24	5	GLY	GLY	PRO	PRO	6	B	B	240 - 244	240 - 244
48	24	5	GLY	GLY	PRO	PRO	6	C	C	240 - 244	240 - 244
49	25	5	SER	SER	VAL	VAL	1	B	B	245 - 246	245 - 246
50	25	5	SER	SER	VAL	VAL	1	C	C	245 - 246	245 - 246
51	26	5	GLU	GLU	GLU	GLU	2	B	B	247	247
52	26	5	GLU	GLU	GLU	GLU	2	C	C	247	247
53	27	5	LEU	LEU	HIS	HIS	1	B	B	248 - 265	248 - 265
54	27	5	LEU	LEU	HIS	HIS	1	C	C	248 - 265	248 - 265
55	28	5	LYS	LYS	LYS	LYS	2	B	B	266	266
56	28	5	LYS	LYS	LYS	LYS	2	C	C	266	266
57	29	5	THR	THR	PRO	PRO	1	B	B	267 - 303	267 - 303
58	29	5	THR	THR	PRO	PRO	1	C	C	267 - 303	267 - 303
59	30	5	PRO	PRO	PRO	PRO	4	B	B	314	314
60	30	5	PRO	PRO	PRO	PRO	4	C	C	314	314
61	31	5	LYS	LYS	LYS	LYS	1	B	B	315 - 347	315 - 347
62	31	5	LYS	LYS	LYS	LYS	1	C	C	315 - 347	315 - 347
63	32	5	ASN	ASN	ARG	ARG	2	B	B	348 - 358	348 - 358
64	32	5	ASN	ASN	ARG	ARG	2	C	C	348 - 358	348 - 358
65	33	5	THR	THR	ARG	ARG	1	B	B	359 - 374	359 - 374
66	33	5	THR	THR	ARG	ARG	1	C	C	359 - 374	359 - 374
67	34	5	LYS	LYS	LYS	LYS	2	B	B	375	375
68	34	5	LYS	LYS	LYS	LYS	2	C	C	375	375
69	35	5	ALA	ALA	VAL	VAL	1	B	B	376 - 412	376 - 412
70	35	5	ALA	ALA	VAL	VAL	1	C	C	376 - 412	376 - 412
71	36	5	GLY	GLY	TRP	TRP	4	B	B	413 - 414	413 - 414
72	36	5	GLY	GLY	TRP	TRP	4	C	C	413 - 414	413 - 414
1	1	6	ASN	ASN	ILE	ILE	1	B	B	1 - 5	1 - 5
2	1	6	ASN	ASN	ILE	ILE	1	D	D	1 - 5	1 - 5
3	2	6	THR	THR	GLU	GLU	2	B	B	6 - 7	6 - 7
4	2	6	THR	THR	GLU	GLU	2	D	D	6 - 7	6 - 7
5	3	6	VAL	VAL	THR	THR	1	B	B	8 - 11	8 - 11
6	3	6	VAL	VAL	THR	THR	1	D	D	8 - 11	8 - 11
7	4	6	GLN	GLN	GLN	GLN	2	B	B	29 - 31	29 - 31
8	4	6	GLN	GLN	GLN	GLN	2	D	D	29 - 31	29 - 31
9	5	6	LEU	LEU	GLY	GLY	1	B	B	32 - 39	32 - 39
10	5	6	LEU	LEU	GLY	GLY	1	D	D	32 - 39	32 - 39
11	6	6	LEU	LEU	LEU	LEU	2	B	B	40	40
12	6	6	LEU	LEU	LEU	LEU	2	D	D	40	40
13	7	6	ARG	ARG	LYS	LYS	1	B	B	41 - 59	41 - 59
14	7	6	ARG	ARG	LYS	LYS	1	D	D	41 - 59	41 - 59
15	8	6	LEU	LEU	LEU	LEU	2	B	B	60 - 67	60 - 67
16	8	6	LEU	LEU	LEU	LEU	2	D	D	60 - 67	60 - 67
17	9	6	ARG	ARG	ALA	ALA	6	B	B	68 - 80	68 - 80
18	9	6	ARG	ARG	ALA	ALA	6	D	D	68 - 80	68 - 80
19	10	6	LYS	LYS	GLY	GLY	1	B	B	81 - 103	81 - 103
20	10	6	LYS	LYS	GLY	GLY	1	D	D	81 - 103	81 - 103
21	11	6	ARG	ARG	LYS	LYS	2	B	B	104 - 105	104 - 105
22	11	6	ARG	ARG	LYS	LYS	2	D	D	104 - 105	104 - 105
23	12	6	GLY	GLY	LYS	LYS	1	B	B	106 - 114	106 - 114
24	12	6	GLY	GLY	LYS	LYS	1	D	D	106 - 114	106 - 114
25	13	6	ARG	ARG	ARG	ARG	2	B	B	115	115
26	13	6	ARG	ARG	ARG	ARG	2	D	D	115	115
27	14	6	PHE	PHE	LYS	LYS	1	B	B	116 - 121	116 - 121
28	14	6	PHE	PHE	LYS	LYS	1	D	D	116 - 121	116 - 121
29	15	6	ARG	ARG	ARG	ARG	3	B	B	122	122
30	15	6	ARG	ARG	ARG	ARG	3	D	D	122	122
31	16	6	ALA	ALA	GLY	GLY	1	B	B	123 - 125	123 - 125
32	16	6	ALA	ALA	GLY	GLY	1	D	D	123 - 125	123 - 125
33	17	6	HIS	HIS	GLN	GLN	6	B	B	126 - 129	126 - 129
34	17	6	HIS	HIS	GLN	GLN	6	D	D	126 - 129	126 - 129
35	18	6	GLY	GLY	GLU	GLU	1	B	B	130 - 166	130 - 166
36	18	6	GLY	GLY	GLU	GLU	1	D	D	130 - 166	130 - 166
37	19	6	HIS	HIS	HIS	HIS	6	B	B	167 - 170	167 - 170
38	19	6	HIS	HIS	HIS	HIS	6	D	D	167 - 170	167 - 170
39	20	6	LEU	LEU	ASP	ASP	5	B	B	171 - 174	171 - 174
40	20	6	LEU	LEU	ASP	ASP	5	D	D	171 - 174	171 - 174
41	21	6	HIS	HIS	GLN	GLN	1	B	B	175 - 200	175 - 200
42	21	6	HIS	HIS	GLN	GLN	1	D	D	175 - 200	175 - 200
43	22	6	ARG	ARG	ARG	ARG	2	B	B	201	201
44	22	6	ARG	ARG	ARG	ARG	2	D	D	201	201
45	23	6	ASN	ASN	MET	MET	1	B	B	202 - 239	202 - 239
46	23	6	ASN	ASN	MET	MET	1	D	D	202 - 239	202 - 239
47	24	6	GLY	GLY	PRO	PRO	6	B	B	240 - 244	240 - 244
48	24	6	GLY	GLY	PRO	PRO	6	D	D	240 - 244	240 - 244
49	25	6	SER	SER	VAL	VAL	1	B	B	245 - 246	245 - 246
50	25	6	SER	SER	VAL	VAL	1	D	D	245 - 246	245 - 246
51	26	6	GLU	GLU	GLU	GLU	2	B	B	247	247
52	26	6	GLU	GLU	GLU	GLU	2	D	D	247	247
53	27	6	LEU	LEU	HIS	HIS	1	B	B	248 - 265	248 - 265
54	27	6	LEU	LEU	HIS	HIS	1	D	D	248 - 265	248 - 265
55	28	6	LYS	LYS	LYS	LYS	2	B	B	266	266
56	28	6	LYS	LYS	LYS	LYS	2	D	D	266	266
57	29	6	THR	THR	PRO	PRO	1	B	B	267 - 303	267 - 303
58	29	6	THR	THR	PRO	PRO	1	D	D	267 - 303	267 - 303
59	30	6	PRO	PRO	PRO	PRO	4	B	B	314	314
60	30	6	PRO	PRO	PRO	PRO	4	D	D	314	314
61	31	6	LYS	LYS	LYS	LYS	1	B	B	315 - 347	315 - 347
62	31	6	LYS	LYS	LYS	LYS	1	D	D	315 - 347	315 - 347
63	32	6	ASN	ASN	ARG	ARG	2	B	B	348 - 358	348 - 358
64	32	6	ASN	ASN	ARG	ARG	2	D	D	348 - 358	348 - 358
65	33	6	THR	THR	ARG	ARG	1	B	B	359 - 374	359 - 374
66	33	6	THR	THR	ARG	ARG	1	D	D	359 - 374	359 - 374
67	34	6	LYS	LYS	LYS	LYS	2	B	B	375	375
68	34	6	LYS	LYS	LYS	LYS	2	D	D	375	375
69	35	6	ALA	ALA	VAL	VAL	1	B	B	376 - 412	376 - 412
70	35	6	ALA	ALA	VAL	VAL	1	D	D	376 - 412	376 - 412
71	36	6	LEU	LEU	LEU	LEU	3	B	B	12	12
72	36	6	LEU	LEU	LEU	LEU	3	D	D	12	12
73	37	6	VAL	VAL	SER	SER	1	B	B	13 - 28	13 - 28
74	37	6	VAL	VAL	SER	SER	1	D	D	13 - 28	13 - 28
75	38	6	GLY	GLY	TRP	TRP	4	B	B	413 - 414	413 - 414
76	38	6	GLY	GLY	TRP	TRP	4	D	D	413 - 414	413 - 414

NCS ensembles :

ID
1
2
3
4
5
6

Components

#1: Protein

A B C D
Transcobalamin II / TCII / TC II

Details:

Mass: 46315.219 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bos taurus (cattle) / Gene: TCN2, TC2 / Production host: Pichia pastoris (fungus) / Strain (production host): SMD 1168 / References: UniProt: Q9XSC9

#2: Chemical

A-901 B-902 C-904 D-903
ChemComp-CL / CHLORIDE ION

Details:

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

#3: Chemical

A B C D A-0 B-0 C-0 D-0
ChemComp-B12 / COBALAMIN

Details:

Mass: 1330.356 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₆₂H₈₉CoN₁₃O₁₄P

#4: Water

ChemComp-HOH / water

Details:

Mass: 18.015 Da / Num. of mol.: 764 / Source method: isolated from a natural source / Formula: H₂O

Experimental details

Experiment

• Experiment: Method: X-RAY DIFFRACTION / Number of used crystals: 1

Sample preparation

• Crystal: Density Matthews: 2.56 ų/Da / Density % sol: 51.95 %
• Crystal grow: Temperature: 293 K / pH: 8.5 ; Details: 28% PEG 8000, 0.2M magnesium acetate, 20% 2-methyl-2,4-pentadiol, 0.1M TRIS, VAPOR DIFFUSION, HANGING DROP, temperature 293K, pH 8.50

Data collection

• Diffraction: Mean temperature: 100 K
• Diffraction source: Source: SYNCHROTRON / Site: ELETTRA / Beamline: 5.2R / Wavelength: 1.2
• Detector: Type: MARRESEARCH / Detector: CCD / Date: Dec 13, 2002
• Radiation: Monochromator: DOUBLE CRYSTAL (SI111, SI220) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
• Radiation wavelength: Wavelength: 1.2 Å / Relative weight: 1
• Reflection: Resolution: 2→18 Å / Num. obs: 121830 / % possible obs: 96.8 % / Observed criterion σ(I): 0 / Redundancy: 3.5 % / B_iso Wilson estimate: 25.8 Ų / R_merge(I) obs: 0.097 / R_sym value: 0.097 / Net I/σ(I): 12
• Reflection shell: Resolution: 2→2.07 Å / Redundancy: 3.2 % / R_merge(I) obs: 0.522 / Mean I/σ(I) obs: 2.2 / R_sym value: 0.522 / % possible all: 93.3

Processing

Software

Name	Version	Classification	NB
DENZO		data reduction
SCALEPACK		data scaling
REFMAC		refinement
PDB_EXTRACT	1.7	data extraction
AMoRE		phasing

Refinement

Method to determine structure: MOLECULAR REPLACEMENT
Starting model: UNREFINED PARTIAL MODEL FROM PHASING WITH SHARP V2.0 USING SINGLE-WAVELENGTH ANOMALOUS DISPERSION DATA

Resolution: 2→18 Å / Cor.coef. F_o:F_c: 0.938 / Cor.coef. F_o:F_c free: 0.911 / SU B: 10.347 / SU ML: 0.145 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.239 / ESU R Free: 0.2 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS

	Rfactor	Num. reflection	% reflection	Selection details
Rfree	0.28	4895	4 %	RANDOM
Rwork	0.241	-	-	-
obs	0.243	116949	96.8 %	-
all	-	116949	-	-

• 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: 32.24 Ų

	Baniso -1	Baniso -2	Baniso -3
1-	0.79 Å2	0 Å2	0.27 Å2
2-	-	-1.06 Å2	0 Å2
3-	-	-	0.33 Å2

Refinement step

Cycle: LAST / Resolution: 2→18 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	13016	0	368	764	14148

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.012	0.022	13700
X-RAY DIFFRACTION	r_bond_other_d
X-RAY DIFFRACTION	r_angle_refined_deg	1.355	2.021	18676
X-RAY DIFFRACTION	r_angle_other_deg
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	6.996	5	1652
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	39.024	23.81	588
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	20.727	15	2400
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	23.697	15	104
X-RAY DIFFRACTION	r_chiral_restr	0.093	0.2	2072
X-RAY DIFFRACTION	r_gen_planes_refined	0.005	0.02	10304
X-RAY DIFFRACTION	r_gen_planes_other
X-RAY DIFFRACTION	r_nbd_refined	0.218	0.2	6156
X-RAY DIFFRACTION	r_nbd_other
X-RAY DIFFRACTION	r_nbtor_refined	0.299	0.2	9206
X-RAY DIFFRACTION	r_nbtor_other
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.175	0.2	766
X-RAY DIFFRACTION	r_xyhbond_nbd_other
X-RAY DIFFRACTION	r_metal_ion_refined
X-RAY DIFFRACTION	r_metal_ion_other
X-RAY DIFFRACTION	r_symmetry_vdw_refined	0.259	0.2	173
X-RAY DIFFRACTION	r_symmetry_vdw_other
X-RAY DIFFRACTION	r_symmetry_hbond_refined	0.19	0.2	34
X-RAY DIFFRACTION	r_symmetry_hbond_other
X-RAY DIFFRACTION	r_symmetry_metal_ion_refined
X-RAY DIFFRACTION	r_symmetry_metal_ion_other
X-RAY DIFFRACTION	r_mcbond_it	0.789	1.5	8272
X-RAY DIFFRACTION	r_mcbond_other
X-RAY DIFFRACTION	r_mcangle_it	1.489	2	13308
X-RAY DIFFRACTION	r_scbond_it	1.953	3	5428
X-RAY DIFFRACTION	r_scangle_it	3.192	4.5	5368
X-RAY DIFFRACTION	r_rigid_bond_restr
X-RAY DIFFRACTION	r_sphericity_free
X-RAY DIFFRACTION	r_sphericity_bonded

Refine LS restraints NCS

Dom-ID: 1 / Refine-ID: X-RAY DIFFRACTION

Ens-ID	Auth asym-ID	Number	Type	Rms dev position (Å)	Weight position
1	A	2868	tight positional	0.02	0.05
2	C	2909	tight positional	0.02	0.05
3	A	2751	tight positional	0.03	0.05
4	A	2747	tight positional	0.03	0.05
5	B	2751	tight positional	0.03	0.05
6	B	2747	tight positional	0.03	0.05
1	A	192	medium positional	0.58	0.5
2	C	154	medium positional	0.55	0.5
3	A	199	medium positional	0.63	0.5
4	A	199	medium positional	0.68	0.5
5	B	199	medium positional	0.59	0.5
6	B	199	medium positional	0.66	0.5
1	A	194	loose positional	1.36	5
2	C	125	loose positional	3.02	5
3	A	231	loose positional	2.83	5
4	A	235	loose positional	2.33	5
5	B	231	loose positional	2.83	5
6	B	235	loose positional	2.36	5
1	A	2868	tight thermal	0.06	0.5
2	C	2909	tight thermal	0.06	0.5
3	A	2751	tight thermal	0.08	0.5
4	A	2747	tight thermal	0.08	0.5
5	B	2751	tight thermal	0.08	0.5
6	B	2747	tight thermal	0.08	0.5
1	A	192	medium thermal	0.34	2
2	C	154	medium thermal	0.31	2
3	A	199	medium thermal	0.45	2
4	A	199	medium thermal	0.46	2
5	B	199	medium thermal	0.44	2
6	B	199	medium thermal	0.45	2
1	A	194	loose thermal	0.67	10
2	C	125	loose thermal	0.48	10
3	A	231	loose thermal	1.39	10
4	A	235	loose thermal	1.26	10
5	B	231	loose thermal	1.46	10
6	B	235	loose thermal	1.35	10

LS refinement shell

Resolution: 2→2.05 Å / Total num. of bins used: 20

	Rfactor	Num. reflection	% reflection
Rfree	0.354	335	-
Rwork	0.336	8222	-
obs	-	-	93.14 %

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	4.7851	1.2166	0.8252	7.242	-0.3177	2.7449	0.0466	0.0852	0.1631	-0.2301	0.0203	0.3755	0.0155	0.0081	-0.0669	-0.0251	-0.0005	0.0075	-0.0234	0.0207	-0.0115	32.6467	5.3967	38.8917
2	1.0259	0.2099	-0.0315	1.6301	-0.5031	0.8818	-0.0146	0.0632	-0.0566	-0.1561	0.0326	0.0702	0.0155	-0.0318	-0.018	-0.036	-0.0182	0.0093	-0.0401	0.0111	-0.0639	33.8708	-7.0586	34.098
3	13.4333	11.7092	2.4263	109.4729	-0.0473	0.4853	-0.1089	-0.2162	-0.9393	2.983	0.9838	-5.3403	0.2607	-0.5764	-0.8749	0.0025	-0.0001	-0.003	0.001	0.0007	0.0053	62.0543	7.6215	50.4473
4	1.7572	0.1683	-0.1013	3.9478	1.482	1.255	-0.0631	-0.0314	0.2027	0.0768	0.0235	0.1204	0.0245	-0.0499	0.0396	-0.0223	0.0083	0.0069	-0.0913	-0.0175	-0.0347	36.4847	17.7946	46.4296
5	6.304	-0.3797	0.0613	10.2082	-0.6501	2.4092	0.0994	0.0258	0.1818	-0.114	-0.0185	0.4056	0.0516	-0.0391	-0.0809	-0.0012	-0.0077	0.006	-0.0368	0.0116	-0.027	80.5167	21.4992	38.9331
6	1.1443	0.2712	-0.0057	1.5001	-0.4422	1.0397	-0.0073	0.0664	-0.0199	-0.0885	0.0273	0.0826	-0.0028	-0.0011	-0.02	-0.0455	-0.0111	0.0157	-0.0545	0.005	-0.0583	81.8002	9.0903	34.0565
7	28.6736	16.8145	3.2354	47.7441	-3.4868	1.1303	-0.0244	0.1126	-1.9094	0.3591	1.5925	-7.738	-0.0623	-0.6761	-1.5681	0.0029	0.0021	-0.0007	0.001	-0.0023	0.0074	110.5138	23.972	50.5807
8	2.051	0.5143	-0.1998	3.2952	0.9665	1.2912	-0.0635	-0.0266	0.2694	0.0844	0.0542	0.1012	-0.0235	-0.0413	0.0093	0.0002	0.0207	0.0064	-0.0947	-0.0251	-0.0031	84.301	33.8679	46.5403
9	2.4926	0.8558	-0.0275	11.3342	-0.1764	3.0656	-0.0377	-0.0095	0.0525	-0.1771	0.1293	0.8012	0.0438	-0.0649	-0.0916	-0.01	-0.0006	-0.007	-0.0256	0.0021	-0.0112	38.6804	32.7693	10.0679
10	1.2317	-0.3828	-0.0468	1.9185	-0.3585	1.2114	-0.0184	0.0249	0.0567	-0.05	0.0714	0.1423	0.0429	-0.033	-0.053	-0.0632	-0.0014	-0.0148	-0.0398	0.0028	-0.0488	39.9333	44.8432	15.38
11	12.8509	31.2358	-0.6653	102.1298	-15.5623	7.4549	1.7991	0.3588	0.1954	-2.0184	-2.8388	0.4781	0.1014	-0.0516	1.0397	0.0035	-0.0045	-0.001	0.0021	0.0009	0.0014	66.8066	31.8949	-2.4913
12	1.8986	0.059	0.2495	3.5506	1.16	1.4267	-0.0455	0.0747	-0.11	-0.2353	0.0513	0.0711	-0.0005	-0.0237	-0.0059	0.0364	-0.0151	-0.005	-0.0779	-0.0154	-0.0786	42.5898	20.6443	2.1811
13	3.3512	0.3494	-0.3317	8.6053	0.9405	4.3763	0.0096	-0.0301	0.0175	0.1049	0.0151	0.5025	-0.0344	0.0305	-0.0247	-0.032	-0.0041	-0.0084	-0.025	0.0031	0.0013	86.6641	48.8656	10.0917
14	1.1027	-0.2455	0.0273	1.3722	-0.3623	1.0382	-0.0327	0.0267	0.0575	0.0146	0.0308	0.1171	0.0338	-0.0551	0.0018	-0.0467	0.006	-0.0072	-0.0326	-0.0019	-0.0421	87.7674	61.1386	15.3655
15	8.5571	-20.7319	-1.1183	291.5183	17.0481	0.9982	0.2196	0.225	0.4845	-5.2466	0.8665	-6.7402	-0.6593	-0.5262	-1.0861	0.0073	0.0007	0.0045	0.0035	-0.0038	0.0065	115.1282	47.8107	-0.3855
16	1.1434	0.3751	0.4563	4.056	1.334	1.4676	-0.0045	0.0626	-0.0874	-0.0878	-0.0289	0.113	-0.0438	-0.0459	0.0334	-0.0186	-0.0027	-0.005	-0.0667	-0.0236	-0.0483	90.5902	36.7345	2.2592

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	I	0	1
2	X-RAY DIFFRACTION	2	A	A	1 - 302	1 - 302
3	X-RAY DIFFRACTION	3	A	A	303 - 314	303 - 314
4	X-RAY DIFFRACTION	4	A	A	315 - 414	315 - 414
5	X-RAY DIFFRACTION	5	B	J	0	1
6	X-RAY DIFFRACTION	6	B	B	1 - 302	1 - 302
7	X-RAY DIFFRACTION	7	B	B	303 - 314	303 - 314
8	X-RAY DIFFRACTION	8	B	B	315 - 414	315 - 414
9	X-RAY DIFFRACTION	9	C	K	0	1
10	X-RAY DIFFRACTION	10	C	C	1 - 302	1 - 302
11	X-RAY DIFFRACTION	11	C	C	303 - 314	303 - 314
12	X-RAY DIFFRACTION	12	C	C	315 - 414	315 - 414
13	X-RAY DIFFRACTION	13	D	L	0	1
14	X-RAY DIFFRACTION	14	D	D	1 - 302	1 - 302
15	X-RAY DIFFRACTION	15	D	D	303 - 314	303 - 314
16	X-RAY DIFFRACTION	16	D	D	315 - 414	315 - 414