FMO DATABASE

FMODB ID: JK119

Calculation Name: 1U2C-A-Xray549

Preferred Name: Dystroglycan

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1U2C

Chain ID: A

ChEMBL ID: CHEMBL3739252

UniProt ID: Q62165

Base Structure: X-ray

Registration Date: 2025-10-11

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	227
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2438641.727705
FMO2-HF: Nuclear repulsion	2352719.595135
FMO2-HF: Total energy	-85922.13257
FMO2-MP2: Total energy	-86171.868653

3D Structure Molmil

Snapshot

Ligand structure

Ligand Interaction

Ligand binding energy

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
N/A	N/A	N/A	N/A	N/A	N/A

Interactive mode: IFIE and PIEDA for fragment #1(A:58:ALA)

Summations of interaction energy for fragment #1(A:58:ALA)

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
-44.937	-43.507	-0.017	-0.563	-0.851	-0.001

Interaction energy analysis for fragmet #1(A:58:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.847 / q_NPA : 0.906

Distance from base fragment(s) [Å]

Dist

Interaction energy by IFIE and PIEDA
[kcal/mol]

| Total | > | ES | > | EX | >
| CT+mix | > | DI(MP2) | >

Fragment charge [e]

FCHARGE q_Mulliken
q_NPA q(I=>J)

Residue

Res # RES

Sort

Graph Options

X Axis Label
Y Axis Max Y Axis Min
Display ES EX CT+mix DI(MP2)

frag_NumFragment number.	ChainChain species.	Res #Residue number.	RES3-letter code of amino acid residue, ligand and solvent molecule.	FCHARGEFormal charge [e].	q_MullikenFragment charge evaluated by Mulliken charge [e].	q_NPAFragment charge evaluated by natural population analysis(NPA) charge [e].	DISTDistance from Ligand [Å].	TotalIFIE at MP2 level [kcal/mol].	ESElectro static interaction energy by PIEDA [kcal/mol].	EXExchange-repulsion energy by PIEDA [kcal/mol].	CT+mixCharge transfer and mixing terms energy by PIEDA [kcal/mol].	DI(MP2)Dispersion energy by PIEDA [kcal/mol].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	60	PRO	0	0.031	0.027	3.856	2.484	3.914	-0.017	-0.563	-0.851	-0.001
4	A	61	THR	0	0.027	0.007	6.427	1.447	1.447	0.000	0.000	0.000	0.000
5	A	62	VAL	0	-0.004	0.007	9.511	1.098	1.098	0.000	0.000	0.000	0.000
6	A	63	VAL	0	0.027	0.014	12.880	0.319	0.319	0.000	0.000	0.000	0.000
7	A	64	GLY	0	-0.005	0.016	15.931	0.466	0.466	0.000	0.000	0.000	0.000
8	A	65	ILE	0	-0.001	-0.009	19.538	-0.013	-0.013	0.000	0.000	0.000	0.000
9	A	66	PRO	0	-0.029	-0.011	22.329	0.067	0.067	0.000	0.000	0.000	0.000
10	A	67	ASP	-1	-0.786	-0.886	25.835	-11.469	-11.469	0.000	0.000	0.000	0.000
11	A	68	GLY	0	-0.041	-0.018	28.525	0.171	0.171	0.000	0.000	0.000	0.000
12	A	69	THR	0	-0.015	-0.009	31.343	0.133	0.133	0.000	0.000	0.000	0.000
13	A	70	ALA	0	0.019	0.001	35.126	-0.053	-0.053	0.000	0.000	0.000	0.000
14	A	71	VAL	0	0.035	0.021	37.288	0.053	0.053	0.000	0.000	0.000	0.000
15	A	72	VAL	0	-0.021	-0.001	41.031	0.016	0.016	0.000	0.000	0.000	0.000
16	A	73	GLY	0	-0.001	-0.006	43.292	0.148	0.148	0.000	0.000	0.000	0.000
17	A	74	ARG	1	0.756	0.875	42.208	7.388	7.388	0.000	0.000	0.000	0.000
18	A	75	SER	0	-0.036	-0.029	39.732	-0.218	-0.218	0.000	0.000	0.000	0.000
19	A	76	PHE	0	0.025	0.013	31.132	-0.038	-0.038	0.000	0.000	0.000	0.000
20	A	77	ARG	1	0.901	0.924	33.100	9.170	9.170	0.000	0.000	0.000	0.000
21	A	78	VAL	0	0.003	0.019	28.277	0.037	0.037	0.000	0.000	0.000	0.000
22	A	79	SER	0	0.008	0.009	26.339	-0.122	-0.122	0.000	0.000	0.000	0.000
23	A	80	ILE	0	-0.001	0.002	21.632	-0.156	-0.156	0.000	0.000	0.000	0.000
24	A	81	PRO	0	0.035	0.024	19.577	-0.023	-0.023	0.000	0.000	0.000	0.000
25	A	82	THR	0	0.017	-0.033	18.529	-1.041	-1.041	0.000	0.000	0.000	0.000
26	A	83	ASP	-1	-0.885	-0.942	17.118	-15.850	-15.850	0.000	0.000	0.000	0.000
27	A	84	LEU	0	-0.067	-0.033	14.763	-0.932	-0.932	0.000	0.000	0.000	0.000
28	A	85	ILE	0	-0.053	-0.014	13.589	-1.357	-1.357	0.000	0.000	0.000	0.000
29	A	86	ALA	0	0.003	0.002	13.261	-1.260	-1.260	0.000	0.000	0.000	0.000
30	A	87	SER	0	-0.048	-0.045	10.746	0.323	0.323	0.000	0.000	0.000	0.000
31	A	88	SER	0	-0.008	-0.026	12.892	1.238	1.238	0.000	0.000	0.000	0.000
32	A	89	GLY	0	-0.002	0.011	13.828	1.063	1.063	0.000	0.000	0.000	0.000
33	A	90	GLU	-1	-0.922	-0.945	10.766	-25.753	-25.753	0.000	0.000	0.000	0.000
34	A	91	ILE	0	-0.013	-0.006	14.896	0.855	0.855	0.000	0.000	0.000	0.000
35	A	92	ILE	0	0.035	0.018	17.215	-0.539	-0.539	0.000	0.000	0.000	0.000
36	A	93	LYS	1	0.828	0.909	19.043	12.841	12.841	0.000	0.000	0.000	0.000
37	A	94	VAL	0	0.029	0.020	20.633	-0.424	-0.424	0.000	0.000	0.000	0.000
38	A	95	SER	0	-0.062	-0.034	23.443	0.273	0.273	0.000	0.000	0.000	0.000
39	A	96	ALA	0	0.058	0.024	25.505	-0.158	-0.158	0.000	0.000	0.000	0.000
40	A	97	ALA	0	0.013	0.004	24.330	-0.242	-0.242	0.000	0.000	0.000	0.000
41	A	98	GLY	0	-0.021	-0.010	24.125	0.392	0.392	0.000	0.000	0.000	0.000
42	A	99	LYS	1	0.883	0.943	25.631	10.211	10.211	0.000	0.000	0.000	0.000
43	A	100	GLU	-1	-0.883	-0.927	25.537	-11.155	-11.155	0.000	0.000	0.000	0.000
44	A	101	ALA	0	-0.004	-0.005	26.847	-0.136	-0.136	0.000	0.000	0.000	0.000
45	A	102	LEU	0	0.043	0.017	27.699	-0.306	-0.306	0.000	0.000	0.000	0.000
46	A	103	PRO	0	0.006	0.008	29.959	0.234	0.234	0.000	0.000	0.000	0.000
47	A	104	SER	0	-0.016	-0.011	33.137	-0.055	-0.055	0.000	0.000	0.000	0.000
48	A	105	TRP	0	-0.039	-0.018	33.809	0.192	0.192	0.000	0.000	0.000	0.000
49	A	106	LEU	0	-0.010	-0.005	30.465	0.005	0.005	0.000	0.000	0.000	0.000
50	A	107	HIS	0	-0.019	-0.015	32.290	0.115	0.115	0.000	0.000	0.000	0.000
51	A	108	TRP	0	0.032	0.008	23.475	-0.102	-0.102	0.000	0.000	0.000	0.000
52	A	109	ASP	-1	-0.818	-0.875	29.047	-10.046	-10.046	0.000	0.000	0.000	0.000
53	A	110	PRO	0	-0.068	-0.052	24.802	-0.260	-0.260	0.000	0.000	0.000	0.000
54	A	111	HIS	0	-0.010	-0.001	25.077	-0.540	-0.540	0.000	0.000	0.000	0.000
55	A	112	SER	0	-0.071	-0.058	27.480	-0.079	-0.079	0.000	0.000	0.000	0.000
56	A	113	HIS	0	0.024	0.033	22.226	0.173	0.173	0.000	0.000	0.000	0.000
57	A	114	ILE	0	-0.010	0.000	25.988	-0.059	-0.059	0.000	0.000	0.000	0.000
58	A	115	LEU	0	-0.012	0.003	27.183	-0.009	-0.009	0.000	0.000	0.000	0.000
59	A	116	GLU	-1	-0.794	-0.899	29.492	-8.779	-8.779	0.000	0.000	0.000	0.000
60	A	117	GLY	0	0.014	-0.013	33.354	-0.092	-0.092	0.000	0.000	0.000	0.000
61	A	118	LEU	0	-0.025	0.012	36.117	0.092	0.092	0.000	0.000	0.000	0.000
62	A	119	PRO	0	0.021	0.028	38.375	0.065	0.065	0.000	0.000	0.000	0.000
63	A	120	LEU	0	0.012	-0.008	40.063	0.242	0.242	0.000	0.000	0.000	0.000
64	A	121	ASP	-1	-0.786	-0.890	42.369	-6.966	-6.966	0.000	0.000	0.000	0.000
65	A	122	THR	0	-0.018	-0.021	42.448	0.007	0.007	0.000	0.000	0.000	0.000
66	A	123	ASP	-1	-0.832	-0.909	38.144	-8.099	-8.099	0.000	0.000	0.000	0.000
67	A	124	LYS	1	0.836	0.910	38.294	6.802	6.802	0.000	0.000	0.000	0.000
68	A	125	GLY	0	0.010	0.016	37.764	-0.019	-0.019	0.000	0.000	0.000	0.000
69	A	126	VAL	0	0.003	0.001	31.386	-0.099	-0.099	0.000	0.000	0.000	0.000
70	A	127	HIS	0	-0.033	-0.019	31.321	-0.270	-0.270	0.000	0.000	0.000	0.000
71	A	128	TYR	0	0.028	0.002	26.486	-0.146	-0.146	0.000	0.000	0.000	0.000
72	A	129	ILE	0	-0.032	-0.014	24.746	0.156	0.156	0.000	0.000	0.000	0.000
73	A	130	SER	0	-0.006	0.001	21.048	-0.345	-0.345	0.000	0.000	0.000	0.000
74	A	131	VAL	0	0.019	0.006	18.936	0.397	0.397	0.000	0.000	0.000	0.000
75	A	132	SER	0	-0.033	-0.016	16.433	-0.656	-0.656	0.000	0.000	0.000	0.000
76	A	133	ALA	0	0.055	0.046	12.989	0.868	0.868	0.000	0.000	0.000	0.000
77	A	134	ALA	0	0.016	0.000	13.575	-0.873	-0.873	0.000	0.000	0.000	0.000
78	A	135	ARG	1	0.972	1.002	9.199	25.125	25.125	0.000	0.000	0.000	0.000
79	A	136	LEU	0	0.012	0.015	13.307	0.399	0.399	0.000	0.000	0.000	0.000
80	A	137	GLY	0	-0.014	-0.004	14.615	-1.292	-1.292	0.000	0.000	0.000	0.000
81	A	138	ALA	0	-0.004	-0.018	15.989	0.755	0.755	0.000	0.000	0.000	0.000
82	A	139	ASN	0	-0.011	0.010	18.479	0.279	0.279	0.000	0.000	0.000	0.000
83	A	140	GLY	0	0.021	0.014	19.964	0.552	0.552	0.000	0.000	0.000	0.000
84	A	141	SER	0	-0.050	-0.031	17.938	0.021	0.021	0.000	0.000	0.000	0.000
85	A	142	HIS	0	0.056	0.013	16.805	-0.757	-0.757	0.000	0.000	0.000	0.000
86	A	143	VAL	0	-0.022	-0.005	11.194	0.195	0.195	0.000	0.000	0.000	0.000
87	A	144	PRO	0	-0.006	0.000	13.049	-0.593	-0.593	0.000	0.000	0.000	0.000
88	A	145	GLN	0	-0.048	-0.021	6.553	-0.641	-0.641	0.000	0.000	0.000	0.000
89	A	146	THR	0	-0.022	-0.022	9.549	-1.638	-1.638	0.000	0.000	0.000	0.000
90	A	147	SER	0	-0.021	-0.032	12.026	1.672	1.672	0.000	0.000	0.000	0.000
91	A	148	SER	0	-0.016	-0.008	15.509	-0.904	-0.904	0.000	0.000	0.000	0.000
92	A	149	VAL	0	-0.048	-0.032	17.993	0.632	0.632	0.000	0.000	0.000	0.000
93	A	150	PHE	0	0.007	0.014	21.452	-0.208	-0.208	0.000	0.000	0.000	0.000
94	A	151	SER	0	-0.074	-0.047	24.564	0.328	0.328	0.000	0.000	0.000	0.000
95	A	152	ILE	0	0.024	0.003	28.349	-0.049	-0.049	0.000	0.000	0.000	0.000
96	A	153	GLU	-1	-0.892	-0.915	31.477	-8.527	-8.527	0.000	0.000	0.000	0.000
97	A	154	VAL	0	-0.057	-0.017	34.941	0.074	0.074	0.000	0.000	0.000	0.000
98	A	155	TYR	0	0.004	-0.018	37.218	0.168	0.168	0.000	0.000	0.000	0.000
99	A	156	PRO	0	0.016	-0.027	40.956	0.052	0.052	0.000	0.000	0.000	0.000
100	A	157	GLU	-1	-0.892	-0.918	44.488	-6.483	-6.483	0.000	0.000	0.000	0.000
101	A	158	ASP	-1	-0.869	-0.927	44.762	-6.894	-6.894	0.000	0.000	0.000	0.000
102	A	159	HIS	0	-0.088	-0.078	45.612	-0.091	-0.091	0.000	0.000	0.000	0.000
103	A	160	ASN	-1	-0.833	-0.888	41.117	-7.398	-7.398	0.000	0.000	0.000	0.000
104	A	179	ALA	1	0.854	0.919	50.510	6.280	6.280	0.000	0.000	0.000	0.000
105	A	180	CYS	0	0.006	0.016	52.103	-0.118	-0.118	0.000	0.000	0.000	0.000
106	A	181	ALA	0	0.044	0.023	55.261	-0.085	-0.085	0.000	0.000	0.000	0.000
107	A	182	ALA	0	0.011	0.004	56.607	0.004	0.004	0.000	0.000	0.000	0.000
108	A	183	ASP	-1	-0.904	-0.954	57.613	-5.291	-5.291	0.000	0.000	0.000	0.000
109	A	184	GLU	-1	-0.936	-0.973	59.311	-5.287	-5.287	0.000	0.000	0.000	0.000
110	A	185	PRO	0	-0.027	-0.017	58.728	-0.102	-0.102	0.000	0.000	0.000	0.000
111	A	186	VAL	0	0.038	0.015	54.085	0.006	0.006	0.000	0.000	0.000	0.000
112	A	187	THR	0	-0.029	-0.017	57.378	0.049	0.049	0.000	0.000	0.000	0.000
113	A	188	VAL	0	-0.023	-0.019	54.545	-0.104	-0.104	0.000	0.000	0.000	0.000
114	A	189	LEU	0	0.023	0.025	56.246	0.133	0.133	0.000	0.000	0.000	0.000
115	A	190	THR	0	-0.022	-0.028	55.045	-0.170	-0.170	0.000	0.000	0.000	0.000
116	A	191	VAL	0	0.014	0.001	54.743	0.137	0.137	0.000	0.000	0.000	0.000
117	A	192	ILE	0	-0.026	-0.005	55.119	-0.111	-0.111	0.000	0.000	0.000	0.000
118	A	193	LEU	0	0.008	-0.003	51.741	0.062	0.062	0.000	0.000	0.000	0.000
119	A	194	ASP	-1	-0.788	-0.899	55.129	-5.578	-5.578	0.000	0.000	0.000	0.000
120	A	195	ALA	0	0.031	0.000	50.247	-0.065	-0.065	0.000	0.000	0.000	0.000
121	A	196	ASP	-1	-0.792	-0.882	48.989	-6.370	-6.370	0.000	0.000	0.000	0.000
122	A	197	LEU	0	0.014	-0.002	45.584	-0.117	-0.117	0.000	0.000	0.000	0.000
123	A	198	THR	0	-0.071	-0.059	44.512	-0.195	-0.195	0.000	0.000	0.000	0.000
124	A	199	LYS	1	0.819	0.898	44.224	6.024	6.024	0.000	0.000	0.000	0.000
125	A	200	MET	0	-0.079	-0.006	44.117	0.007	0.007	0.000	0.000	0.000	0.000
126	A	201	THR	0	0.034	-0.010	38.574	-0.161	-0.161	0.000	0.000	0.000	0.000
127	A	202	PRO	0	0.045	0.024	36.139	0.147	0.147	0.000	0.000	0.000	0.000
128	A	203	LYS	1	0.868	0.929	35.288	8.827	8.827	0.000	0.000	0.000	0.000
129	A	204	GLN	0	0.051	0.041	38.620	0.013	0.013	0.000	0.000	0.000	0.000
130	A	205	ARG	1	0.826	0.919	40.106	7.767	7.767	0.000	0.000	0.000	0.000
131	A	206	ILE	0	0.009	0.013	37.766	0.132	0.132	0.000	0.000	0.000	0.000
132	A	207	ASP	-1	-0.824	-0.912	41.202	-7.110	-7.110	0.000	0.000	0.000	0.000
133	A	208	LEU	0	-0.011	-0.002	43.210	0.153	0.153	0.000	0.000	0.000	0.000
134	A	209	LEU	0	0.019	0.000	43.132	0.141	0.141	0.000	0.000	0.000	0.000
135	A	210	ASN	0	-0.047	-0.030	42.684	0.086	0.086	0.000	0.000	0.000	0.000
136	A	211	ARG	1	0.799	0.892	44.694	6.881	6.881	0.000	0.000	0.000	0.000
137	A	212	MET	0	0.024	0.021	48.098	0.192	0.192	0.000	0.000	0.000	0.000
138	A	213	GLN	0	0.019	0.012	43.929	0.054	0.054	0.000	0.000	0.000	0.000
139	A	214	SER	0	-0.033	-0.006	49.195	0.024	0.024	0.000	0.000	0.000	0.000
140	A	215	PHE	0	-0.015	-0.014	51.961	0.117	0.117	0.000	0.000	0.000	0.000
141	A	216	SER	0	-0.008	-0.051	50.166	0.093	0.093	0.000	0.000	0.000	0.000
142	A	217	GLU	-1	-0.979	-0.971	51.520	-5.735	-5.735	0.000	0.000	0.000	0.000
143	A	218	VAL	0	-0.061	-0.027	48.219	-0.058	-0.058	0.000	0.000	0.000	0.000
144	A	219	GLU	-1	-0.840	-0.942	43.285	-7.374	-7.374	0.000	0.000	0.000	0.000
145	A	220	LEU	0	0.007	-0.008	40.618	0.028	0.028	0.000	0.000	0.000	0.000
146	A	221	HIS	0	-0.008	0.016	40.306	-0.093	-0.093	0.000	0.000	0.000	0.000
147	A	222	ASN	0	-0.034	-0.014	42.356	-0.034	-0.034	0.000	0.000	0.000	0.000
148	A	223	MET	0	-0.074	0.018	45.750	0.271	0.271	0.000	0.000	0.000	0.000
149	A	224	LYS	1	0.848	0.925	45.817	6.182	6.182	0.000	0.000	0.000	0.000
150	A	225	LEU	0	-0.045	-0.028	45.171	0.171	0.171	0.000	0.000	0.000	0.000
151	A	226	VAL	0	0.054	0.031	46.404	-0.164	-0.164	0.000	0.000	0.000	0.000
152	A	227	PRO	0	0.010	-0.007	47.726	0.104	0.104	0.000	0.000	0.000	0.000
153	A	228	VAL	0	-0.036	0.010	50.698	0.054	0.054	0.000	0.000	0.000	0.000
154	A	229	VAL	0	0.047	0.025	52.769	-0.040	-0.040	0.000	0.000	0.000	0.000
155	A	230	ASN	0	-0.055	-0.045	55.416	0.090	0.090	0.000	0.000	0.000	0.000
156	A	231	ASN	0	0.030	0.013	57.856	0.103	0.103	0.000	0.000	0.000	0.000
157	A	232	ARG	1	0.953	0.990	59.060	5.380	5.380	0.000	0.000	0.000	0.000
158	A	233	LEU	0	0.012	0.004	58.329	-0.067	-0.067	0.000	0.000	0.000	0.000
159	A	234	PHE	0	0.016	0.003	60.615	0.041	0.041	0.000	0.000	0.000	0.000
160	A	235	ASP	-1	-0.774	-0.846	60.989	-5.252	-5.252	0.000	0.000	0.000	0.000
161	A	236	MET	0	-0.011	-0.013	63.018	0.029	0.029	0.000	0.000	0.000	0.000
162	A	237	SER	0	-0.078	-0.059	63.538	0.045	0.045	0.000	0.000	0.000	0.000
163	A	238	ALA	0	-0.040	-0.018	63.642	-0.024	-0.024	0.000	0.000	0.000	0.000
164	A	239	PHE	0	-0.005	-0.002	63.582	0.089	0.089	0.000	0.000	0.000	0.000
165	A	240	MET	0	-0.027	0.001	65.016	0.062	0.062	0.000	0.000	0.000	0.000
166	A	241	ALA	0	0.020	-0.001	64.550	-0.091	-0.091	0.000	0.000	0.000	0.000
167	A	242	GLY	0	0.000	0.006	64.535	0.093	0.093	0.000	0.000	0.000	0.000
168	A	243	PRO	0	-0.044	-0.009	64.114	-0.068	-0.068	0.000	0.000	0.000	0.000
169	A	244	GLY	0	0.030	0.024	61.661	-0.041	-0.041	0.000	0.000	0.000	0.000
170	A	245	ASN	0	0.068	0.022	59.458	0.056	0.056	0.000	0.000	0.000	0.000
171	A	246	ALA	0	-0.048	-0.018	60.341	0.075	0.075	0.000	0.000	0.000	0.000
172	A	247	LYS	1	0.925	0.947	62.444	4.903	4.903	0.000	0.000	0.000	0.000
173	A	248	LYS	1	0.881	0.937	63.198	4.876	4.876	0.000	0.000	0.000	0.000
174	A	249	VAL	0	0.023	0.024	58.386	-0.033	-0.033	0.000	0.000	0.000	0.000
175	A	250	VAL	0	-0.052	-0.030	56.891	0.082	0.082	0.000	0.000	0.000	0.000
176	A	251	GLU	-1	-0.857	-0.904	52.800	-6.035	-6.035	0.000	0.000	0.000	0.000
177	A	252	ASN	0	-0.091	-0.057	52.955	0.142	0.142	0.000	0.000	0.000	0.000
178	A	253	GLY	0	0.014	0.019	54.180	0.095	0.095	0.000	0.000	0.000	0.000
179	A	254	ALA	0	-0.031	-0.025	50.577	-0.107	-0.107	0.000	0.000	0.000	0.000
180	A	255	LEU	0	-0.013	-0.007	51.901	0.148	0.148	0.000	0.000	0.000	0.000
181	A	256	LEU	0	0.027	0.016	49.135	-0.131	-0.131	0.000	0.000	0.000	0.000
182	A	257	SER	0	-0.040	-0.023	50.869	0.138	0.138	0.000	0.000	0.000	0.000
183	A	258	TRP	0	0.089	0.036	50.673	-0.166	-0.166	0.000	0.000	0.000	0.000
184	A	259	LYS	1	0.915	0.969	51.866	6.113	6.113	0.000	0.000	0.000	0.000
185	A	260	LEU	0	0.004	0.004	53.767	-0.031	-0.031	0.000	0.000	0.000	0.000
186	A	261	GLY	0	-0.016	-0.028	56.614	0.005	0.005	0.000	0.000	0.000	0.000
187	A	263	SER	0	0.036	0.016	59.212	0.078	0.078	0.000	0.000	0.000	0.000
188	A	264	LEU	0	-0.016	0.017	60.164	0.088	0.088	0.000	0.000	0.000	0.000
189	A	265	ASN	0	0.031	0.015	63.733	0.050	0.050	0.000	0.000	0.000	0.000
190	A	266	GLN	0	0.064	-0.001	66.268	-0.033	-0.033	0.000	0.000	0.000	0.000
191	A	267	ASN	0	-0.044	-0.020	67.688	0.005	0.005	0.000	0.000	0.000	0.000
192	A	268	SER	0	-0.044	-0.013	64.809	-0.002	-0.002	0.000	0.000	0.000	0.000
193	A	269	VAL	0	-0.015	0.003	62.142	-0.099	-0.099	0.000	0.000	0.000	0.000
194	A	270	PRO	0	0.025	0.018	58.832	0.064	0.064	0.000	0.000	0.000	0.000
195	A	271	ASP	-1	-0.803	-0.889	61.943	-4.992	-4.992	0.000	0.000	0.000	0.000
196	A	272	ILE	0	0.052	0.031	59.873	-0.084	-0.084	0.000	0.000	0.000	0.000
197	A	273	ARG	1	0.861	0.901	61.830	4.865	4.865	0.000	0.000	0.000	0.000
198	A	274	GLY	0	0.029	0.019	59.283	0.008	0.008	0.000	0.000	0.000	0.000
199	A	275	VAL	0	0.008	-0.001	56.973	-0.088	-0.088	0.000	0.000	0.000	0.000
200	A	276	GLU	-1	-0.876	-0.934	59.372	-4.848	-4.848	0.000	0.000	0.000	0.000
201	A	277	THR	0	-0.014	-0.014	62.957	0.033	0.033	0.000	0.000	0.000	0.000
202	A	278	PRO	0	0.042	0.009	58.880	0.021	0.021	0.000	0.000	0.000	0.000
203	A	279	ALA	0	0.003	0.015	59.980	-0.043	-0.043	0.000	0.000	0.000	0.000
204	A	280	ARG	1	0.834	0.920	60.889	4.757	4.757	0.000	0.000	0.000	0.000
205	A	281	GLU	-1	-0.953	-0.978	63.218	-4.907	-4.907	0.000	0.000	0.000	0.000
206	A	282	GLY	0	-0.056	-0.015	60.524	0.003	0.003	0.000	0.000	0.000	0.000
207	A	283	ALA	0	0.034	0.031	58.840	-0.105	-0.105	0.000	0.000	0.000	0.000
208	A	284	MET	0	0.016	0.014	55.259	-0.111	-0.111	0.000	0.000	0.000	0.000
209	A	285	SER	0	-0.074	-0.049	54.782	-0.096	-0.096	0.000	0.000	0.000	0.000
210	A	286	ALA	0	-0.017	-0.009	54.394	-0.098	-0.098	0.000	0.000	0.000	0.000
211	A	287	GLN	0	-0.050	-0.027	50.772	-0.026	-0.026	0.000	0.000	0.000	0.000
212	A	288	LEU	0	-0.011	-0.021	50.395	-0.164	-0.164	0.000	0.000	0.000	0.000
213	A	289	GLY	0	-0.004	0.009	49.687	-0.144	-0.144	0.000	0.000	0.000	0.000
214	A	290	TYR	0	-0.003	-0.010	47.230	-0.036	-0.036	0.000	0.000	0.000	0.000
215	A	291	PRO	0	-0.034	-0.012	53.132	0.061	0.061	0.000	0.000	0.000	0.000
216	A	292	VAL	0	0.042	0.023	56.418	-0.055	-0.055	0.000	0.000	0.000	0.000
217	A	293	VAL	0	-0.018	-0.018	58.304	0.109	0.109	0.000	0.000	0.000	0.000
218	A	294	GLY	0	0.000	-0.008	59.938	0.122	0.122	0.000	0.000	0.000	0.000
219	A	295	TRP	0	0.012	0.026	59.522	-0.136	-0.136	0.000	0.000	0.000	0.000
220	A	296	HIS	0	0.030	0.004	59.322	0.149	0.149	0.000	0.000	0.000	0.000
221	A	297	ILE	0	0.018	0.013	60.072	-0.115	-0.115	0.000	0.000	0.000	0.000
222	A	298	ALA	0	0.022	0.008	60.590	0.113	0.113	0.000	0.000	0.000	0.000
223	A	299	ASN	0	-0.001	0.011	60.305	-0.169	-0.169	0.000	0.000	0.000	0.000
224	A	300	LYS	1	0.826	0.889	57.286	5.395	5.395	0.000	0.000	0.000	0.000
225	A	301	LYS	1	0.879	0.922	56.214	5.729	5.729	0.000	0.000	0.000	0.000
226	A	302	PRO	0	0.023	0.031	55.556	-0.083	-0.083	0.000	0.000	0.000	0.000
227	A	303	THR	-1	-0.876	-0.926	51.632	-6.028	-6.028	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:58:ALA)