FMO DATABASE

FMODB ID: K2QR3

Calculation Name: 3DA5-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3DA5

Chain ID: A

ChEMBL ID:

UniProt ID: D0VWU1

Base Structure: X-ray

Registration Date: 2025-07-08

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptHSide
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	229
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1143581.559198
FMO2-HF: Nuclear repulsion	1094041.228171
FMO2-HF: Total energy	-49540.331026
FMO2-MP2: Total energy	-49689.700822

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:8:LYS)

Summations of interaction energy for fragment #1(A:8:LYS)

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.
0.216	1.934	-0.008	-0.74	-0.97	0.004

Interaction energy analysis for fragmet #1(A:8:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.177 / q_NPA : 0.068

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].
4	A	9	LYS	1	0.789	1.037	4.097	0.859	1.203	0.002	-0.170	-0.176	0.000
5	A	10	THR	0	0.044	-0.068	3.891	-1.662	-0.056	-0.005	-0.944	-0.656	0.004
6	A	10	THR	0	-0.007	0.080	5.804	0.070	0.070	0.000	0.000	0.000	0.000
7	A	11	LEU	0	0.167	-0.075	6.463	0.349	0.349	0.000	0.000	0.000	0.000
8	A	11	LEU	0	-0.118	0.101	9.904	0.005	0.005	0.000	0.000	0.000	0.000
9	A	12	TRP	0	0.097	-0.117	9.691	0.175	0.175	0.000	0.000	0.000	0.000
10	A	12	TRP	0	-0.096	0.078	11.429	-0.020	-0.020	0.000	0.000	0.000	0.000
11	A	13	GLU	0	0.079	-0.085	8.823	0.239	0.239	0.000	0.000	0.000	0.000
12	A	13	GLU	-1	-0.950	-0.822	8.011	-0.890	-0.890	0.000	0.000	0.000	0.000
13	A	14	LEU	0	0.039	-0.104	9.195	0.186	0.186	0.000	0.000	0.000	0.000
14	A	14	LEU	0	-0.100	0.072	6.422	0.022	0.022	0.000	0.000	0.000	0.000
15	A	15	VAL	0	-0.016	-0.105	9.948	0.136	0.136	0.000	0.000	0.000	0.000
16	A	15	VAL	0	-0.078	0.109	12.703	0.003	0.003	0.000	0.000	0.000	0.000
17	A	16	GLY	0	0.047	-0.094	13.054	0.074	0.074	0.000	0.000	0.000	0.000
18	A	17	ARG	0	0.016	-0.016	14.165	0.051	0.051	0.000	0.000	0.000	0.000
19	A	17	ARG	1	0.744	1.000	11.775	0.717	0.717	0.000	0.000	0.000	0.000
20	A	18	ASN	0	0.193	-0.054	15.807	0.039	0.039	0.000	0.000	0.000	0.000
21	A	18	ASN	0	-0.081	0.097	18.491	0.004	0.004	0.000	0.000	0.000	0.000
22	A	19	LYS	0	0.104	-0.101	18.223	-0.037	-0.037	0.000	0.000	0.000	0.000
23	A	19	LYS	1	0.855	1.069	20.616	0.298	0.298	0.000	0.000	0.000	0.000
24	A	20	ASP	0	0.087	-0.122	20.177	-0.019	-0.019	0.000	0.000	0.000	0.000
25	A	20	ASP	-1	-0.878	-0.801	22.848	-0.218	-0.218	0.000	0.000	0.000	0.000
26	A	21	ALA	0	0.097	-0.069	18.367	0.015	0.015	0.000	0.000	0.000	0.000
27	A	21	ALA	0	-0.064	0.117	17.647	-0.001	-0.001	0.000	0.000	0.000	0.000
28	A	22	LEU	0	0.068	-0.118	16.370	-0.001	-0.001	0.000	0.000	0.000	0.000
29	A	22	LEU	0	-0.083	0.093	14.655	-0.016	-0.016	0.000	0.000	0.000	0.000
30	A	23	ARG	0	0.080	-0.106	17.347	-0.027	-0.027	0.000	0.000	0.000	0.000
31	A	23	ARG	1	0.675	0.969	21.833	0.229	0.229	0.000	0.000	0.000	0.000
32	A	24	ASP	0	0.153	-0.101	20.393	0.001	0.001	0.000	0.000	0.000	0.000
33	A	24	ASP	-1	-0.923	-0.778	20.644	-0.212	-0.212	0.000	0.000	0.000	0.000
34	A	25	PHE	0	0.099	-0.077	15.884	0.038	0.038	0.000	0.000	0.000	0.000
35	A	25	PHE	0	-0.105	0.084	11.559	-0.027	-0.027	0.000	0.000	0.000	0.000
36	A	26	LEU	0	0.071	-0.094	17.047	0.009	0.009	0.000	0.000	0.000	0.000
37	A	26	LEU	0	-0.068	0.086	14.914	-0.007	-0.007	0.000	0.000	0.000	0.000
38	A	27	LYS	0	0.048	-0.097	17.860	0.011	0.011	0.000	0.000	0.000	0.000
39	A	27	LYS	1	0.817	1.025	22.021	0.176	0.176	0.000	0.000	0.000	0.000
40	A	28	GLU	0	0.030	-0.172	19.370	0.019	0.019	0.000	0.000	0.000	0.000
41	A	28	GLU	-1	-0.968	-0.831	18.155	-0.210	-0.210	0.000	0.000	0.000	0.000
42	A	29	HIS	0	0.049	-0.028	16.402	0.038	0.038	0.000	0.000	0.000	0.000
43	A	29	HIS	1	0.715	0.976	15.649	0.248	0.248	0.000	0.000	0.000	0.000
44	A	30	ARG	0	0.193	-0.099	17.936	-0.021	-0.021	0.000	0.000	0.000	0.000
45	A	30	ARG	1	0.723	1.027	21.354	0.183	0.183	0.000	0.000	0.000	0.000
46	A	31	GLY	0	-0.089	-0.151	19.654	0.027	0.027	0.000	0.000	0.000	0.000
47	A	32	THR	0	-0.004	0.002	17.746	0.014	0.014	0.000	0.000	0.000	0.000
48	A	32	THR	0	-0.011	0.091	17.313	-0.002	-0.002	0.000	0.000	0.000	0.000
49	A	33	ILE	0	0.082	-0.075	13.868	0.027	0.027	0.000	0.000	0.000	0.000
50	A	33	ILE	0	-0.079	0.099	12.142	-0.014	-0.014	0.000	0.000	0.000	0.000
51	A	34	LEU	0	0.001	-0.122	13.048	0.038	0.038	0.000	0.000	0.000	0.000
52	A	34	LEU	0	-0.097	0.084	13.309	0.001	0.001	0.000	0.000	0.000	0.000
53	A	35	LEU	0	0.084	-0.113	10.655	-0.082	-0.082	0.000	0.000	0.000	0.000
54	A	35	LEU	0	-0.048	0.121	11.100	-0.002	-0.002	0.000	0.000	0.000	0.000
55	A	36	ARG	0	0.179	-0.067	8.696	0.212	0.212	0.000	0.000	0.000	0.000
56	A	36	ARG	1	0.764	1.022	7.126	0.839	0.839	0.000	0.000	0.000	0.000
57	A	37	ASP	0	0.113	-0.076	8.645	-0.419	-0.419	0.000	0.000	0.000	0.000
58	A	37	ASP	-1	-0.852	-0.778	11.936	-0.868	-0.868	0.000	0.000	0.000	0.000
59	A	38	ILE	0	0.004	-0.108	6.803	0.311	0.311	0.000	0.000	0.000	0.000
60	A	38	ILE	0	-0.132	0.059	4.486	-0.295	-0.255	-0.001	-0.009	-0.030	0.000
61	A	39	ALA	0	0.179	-0.085	8.320	-0.020	-0.020	0.000	0.000	0.000	0.000
62	A	39	ALA	0	-0.028	0.129	11.252	0.015	0.015	0.000	0.000	0.000	0.000
63	A	40	SER	0	0.032	-0.064	11.384	0.148	0.148	0.000	0.000	0.000	0.000
64	A	40	SER	0	-0.041	0.054	13.472	-0.028	-0.028	0.000	0.000	0.000	0.000
65	A	41	GLU	0	0.126	-0.094	12.492	-0.098	-0.098	0.000	0.000	0.000	0.000
66	A	41	GLU	-1	-0.971	-0.822	15.169	-0.258	-0.258	0.000	0.000	0.000	0.000
67	A	42	HIS	0	0.009	-0.104	13.562	-0.006	-0.006	0.000	0.000	0.000	0.000
68	A	42	HIS	0	-0.078	0.093	15.887	-0.009	-0.009	0.000	0.000	0.000	0.000
69	A	43	LYS	0	0.261	-0.022	10.117	0.007	0.007	0.000	0.000	0.000	0.000
70	A	43	LYS	1	0.708	1.009	8.442	0.580	0.580	0.000	0.000	0.000	0.000
71	A	44	VAL	0	0.002	-0.158	11.443	-0.013	-0.013	0.000	0.000	0.000	0.000
72	A	44	VAL	0	-0.076	0.113	15.039	0.013	0.013	0.000	0.000	0.000	0.000
73	A	45	VAL	0	0.101	-0.087	12.540	-0.145	-0.145	0.000	0.000	0.000	0.000
74	A	45	VAL	0	-0.095	0.089	11.141	0.000	0.000	0.000	0.000	0.000	0.000
75	A	46	TYR	0	0.004	-0.124	13.450	0.100	0.100	0.000	0.000	0.000	0.000
76	A	46	TYR	0	-0.008	0.132	13.928	0.031	0.031	0.000	0.000	0.000	0.000
77	A	47	LYS	0	0.142	-0.088	15.103	-0.067	-0.067	0.000	0.000	0.000	0.000
78	A	47	LYS	1	0.806	1.049	18.622	0.284	0.284	0.000	0.000	0.000	0.000
79	A	48	PRO	0	0.024	-0.097	15.869	0.021	0.021	0.000	0.000	0.000	0.000
80	A	49	ILE	0	0.072	0.001	18.488	0.032	0.032	0.000	0.000	0.000	0.000
81	A	49	ILE	0	-0.051	0.139	21.634	0.004	0.004	0.000	0.000	0.000	0.000
82	A	50	PHE	0	0.098	-0.073	22.257	-0.020	-0.020	0.000	0.000	0.000	0.000
83	A	50	PHE	0	-0.143	0.054	20.031	0.006	0.006	0.000	0.000	0.000	0.000
84	A	51	LYS	0	0.152	-0.079	24.461	0.004	0.004	0.000	0.000	0.000	0.000
85	A	51	LYS	1	0.822	1.078	26.022	0.224	0.224	0.000	0.000	0.000	0.000
86	A	52	ARG	0	0.075	-0.073	27.647	0.006	0.006	0.000	0.000	0.000	0.000
87	A	52	ARG	1	0.867	1.061	31.136	0.132	0.132	0.000	0.000	0.000	0.000
88	A	53	TYR	0	-0.010	-0.109	30.526	0.003	0.003	0.000	0.000	0.000	0.000
89	A	53	TYR	0	-0.049	0.106	33.750	0.000	0.000	0.000	0.000	0.000	0.000
90	A	54	ASN	0	0.000	-0.087	28.010	0.008	0.008	0.000	0.000	0.000	0.000
91	A	54	ASN	0	-0.031	0.036	27.259	0.003	0.003	0.000	0.000	0.000	0.000
92	A	55	GLY	0	0.139	-0.022	27.904	0.004	0.004	0.000	0.000	0.000	0.000
93	A	56	ASP	0	0.081	-0.029	25.176	-0.007	-0.007	0.000	0.000	0.000	0.000
94	A	56	ASP	-1	-0.939	-0.786	25.920	-0.187	-0.187	0.000	0.000	0.000	0.000
95	A	57	PRO	0	-0.021	-0.125	20.838	0.009	0.009	0.000	0.000	0.000	0.000
96	A	58	ASP	0	0.167	0.033	22.828	0.009	0.009	0.000	0.000	0.000	0.000
97	A	58	ASP	-1	-0.985	-0.858	24.242	-0.223	-0.223	0.000	0.000	0.000	0.000
98	A	59	LEU	0	0.018	-0.132	21.827	-0.025	-0.025	0.000	0.000	0.000	0.000
99	A	59	LEU	0	-0.074	0.085	19.321	-0.008	-0.008	0.000	0.000	0.000	0.000
100	A	60	ILE	0	0.100	-0.071	22.402	0.030	0.030	0.000	0.000	0.000	0.000
101	A	60	ILE	0	-0.083	0.103	23.583	-0.002	-0.002	0.000	0.000	0.000	0.000
102	A	61	GLU	0	0.021	-0.138	22.956	-0.038	-0.038	0.000	0.000	0.000	0.000
103	A	61	GLU	-1	-0.989	-0.857	23.272	-0.267	-0.267	0.000	0.000	0.000	0.000
104	A	62	ASP	0	0.069	-0.137	24.794	-0.008	-0.008	0.000	0.000	0.000	0.000
105	A	62	ASP	-1	-0.929	-0.820	28.183	-0.216	-0.216	0.000	0.000	0.000	0.000
106	A	63	ASN	0	0.067	-0.080	25.813	0.015	0.015	0.000	0.000	0.000	0.000
107	A	63	ASN	0	-0.123	0.080	26.272	0.002	0.002	0.000	0.000	0.000	0.000
108	A	64	SER	0	0.120	-0.102	23.916	-0.025	-0.025	0.000	0.000	0.000	0.000
109	A	64	SER	0	0.018	0.112	24.526	0.007	0.007	0.000	0.000	0.000	0.000
110	A	65	ASN	0	0.135	-0.050	24.410	-0.020	-0.020	0.000	0.000	0.000	0.000
111	A	65	ASN	0	-0.092	0.072	28.095	0.001	0.001	0.000	0.000	0.000	0.000
112	A	66	ASP	0	0.152	-0.090	24.576	-0.003	-0.003	0.000	0.000	0.000	0.000
113	A	66	ASP	-1	-1.003	-0.851	23.927	-0.261	-0.261	0.000	0.000	0.000	0.000
114	A	67	VAL	0	0.002	-0.128	20.601	-0.024	-0.024	0.000	0.000	0.000	0.000
115	A	67	VAL	0	-0.093	0.104	19.080	-0.006	-0.006	0.000	0.000	0.000	0.000
116	A	68	GLU	0	0.068	-0.149	20.223	-0.057	-0.057	0.000	0.000	0.000	0.000
117	A	68	GLU	-1	-0.942	-0.809	22.835	-0.259	-0.259	0.000	0.000	0.000	0.000
118	A	69	HIS	0	0.063	-0.063	21.754	-0.013	-0.013	0.000	0.000	0.000	0.000
119	A	69	HIS	0	-0.088	0.084	23.791	0.015	0.015	0.000	0.000	0.000	0.000
120	A	70	TRP	0	0.071	-0.106	19.507	0.013	0.013	0.000	0.000	0.000	0.000
121	A	70	TRP	0	-0.093	0.089	18.574	-0.012	-0.012	0.000	0.000	0.000	0.000
122	A	71	TYR	0	0.199	-0.069	17.082	-0.051	-0.051	0.000	0.000	0.000	0.000
123	A	71	TYR	0	-0.128	0.062	14.628	0.011	0.011	0.000	0.000	0.000	0.000
124	A	72	ASP	0	0.039	-0.143	17.865	-0.041	-0.041	0.000	0.000	0.000	0.000
125	A	72	ASP	-1	-0.925	-0.794	20.900	-0.316	-0.316	0.000	0.000	0.000	0.000
126	A	73	TYR	0	0.084	-0.106	20.563	0.022	0.022	0.000	0.000	0.000	0.000
127	A	73	TYR	0	-0.094	0.080	19.213	0.016	0.016	0.000	0.000	0.000	0.000
128	A	74	HIS	0	-0.013	-0.088	16.234	0.032	0.032	0.000	0.000	0.000	0.000
129	A	74	HIS	1	0.717	0.914	14.540	0.610	0.610	0.000	0.000	0.000	0.000
130	A	75	LEU	0	0.129	-0.059	16.726	-0.002	-0.002	0.000	0.000	0.000	0.000
131	A	75	LEU	0	-0.116	0.093	17.209	0.006	0.006	0.000	0.000	0.000	0.000
132	A	76	GLU	0	0.079	-0.156	17.640	0.011	0.011	0.000	0.000	0.000	0.000
133	A	76	GLU	-1	-0.888	-0.783	22.170	-0.233	-0.233	0.000	0.000	0.000	0.000
134	A	77	ARG	0	0.033	-0.077	20.272	0.036	0.036	0.000	0.000	0.000	0.000
135	A	77	ARG	1	0.682	0.991	20.109	0.259	0.259	0.000	0.000	0.000	0.000
136	A	78	TYR	0	0.043	-0.085	16.640	0.045	0.045	0.000	0.000	0.000	0.000
137	A	78	TYR	0	-0.099	0.054	16.004	0.004	0.004	0.000	0.000	0.000	0.000
138	A	79	TRP	0	0.073	-0.066	15.770	0.017	0.017	0.000	0.000	0.000	0.000
139	A	79	TRP	0	-0.179	0.024	10.138	-0.063	-0.063	0.000	0.000	0.000	0.000
140	A	80	ASN	0	0.134	-0.086	16.875	0.003	0.003	0.000	0.000	0.000	0.000
141	A	80	ASN	0	-0.101	0.101	20.823	-0.005	-0.005	0.000	0.000	0.000	0.000
142	A	81	THR	0	-0.019	-0.104	19.381	0.019	0.019	0.000	0.000	0.000	0.000
143	A	81	THR	0	-0.004	0.046	19.775	-0.006	-0.006	0.000	0.000	0.000	0.000
144	A	82	PRO	0	0.081	-0.063	19.519	-0.023	-0.023	0.000	0.000	0.000	0.000
145	A	83	GLU	0	-0.024	-0.055	18.312	-0.022	-0.022	0.000	0.000	0.000	0.000
146	A	83	GLU	-1	-0.835	-0.772	17.761	-0.071	-0.071	0.000	0.000	0.000	0.000
147	A	84	LEU	0	0.102	-0.107	15.099	0.002	0.002	0.000	0.000	0.000	0.000
148	A	84	LEU	0	-0.026	0.155	14.578	-0.005	-0.005	0.000	0.000	0.000	0.000
149	A	85	LYS	0	0.161	-0.069	14.741	-0.072	-0.072	0.000	0.000	0.000	0.000
150	A	85	LYS	1	0.869	1.093	18.139	0.271	0.271	0.000	0.000	0.000	0.000
151	A	86	LYS	0	0.099	-0.076	15.826	-0.053	-0.053	0.000	0.000	0.000	0.000
152	A	86	LYS	1	0.757	1.014	14.980	0.089	0.089	0.000	0.000	0.000	0.000
153	A	87	GLU	0	0.048	-0.157	12.090	-0.024	-0.024	0.000	0.000	0.000	0.000
154	A	87	GLU	-1	-0.984	-0.838	9.989	-0.196	-0.196	0.000	0.000	0.000	0.000
155	A	88	PHE	0	0.102	-0.078	10.861	-0.108	-0.108	0.000	0.000	0.000	0.000
156	A	88	PHE	0	-0.082	0.101	12.910	-0.011	-0.011	0.000	0.000	0.000	0.000
157	A	89	TYR	0	0.104	-0.098	11.397	-0.156	-0.156	0.000	0.000	0.000	0.000
158	A	89	TYR	0	-0.081	0.100	15.094	0.006	0.006	0.000	0.000	0.000	0.000
159	A	90	LYS	0	0.037	-0.085	11.610	-0.070	-0.070	0.000	0.000	0.000	0.000
160	A	90	LYS	1	0.856	1.040	11.130	0.151	0.151	0.000	0.000	0.000	0.000
161	A	91	LYS	0	0.105	-0.075	7.544	0.030	0.030	0.000	0.000	0.000	0.000
162	A	91	LYS	1	0.673	1.011	5.997	1.336	1.336	0.000	0.000	0.000	0.000
163	A	92	PHE	0	0.016	-0.135	7.846	-0.313	-0.313	0.000	0.000	0.000	0.000
164	A	92	PHE	0	-0.070	0.099	8.253	-0.094	-0.094	0.000	0.000	0.000	0.000
165	A	93	GLY	0	0.010	-0.075	10.100	0.005	0.005	0.000	0.000	0.000	0.000
166	A	94	PRO	0	0.017	0.009	13.245	-0.023	-0.023	0.000	0.000	0.000	0.000
167	A	95	VAL	0	0.084	0.008	15.819	-0.073	-0.073	0.000	0.000	0.000	0.000
168	A	95	VAL	0	-0.022	0.130	17.792	-0.001	-0.001	0.000	0.000	0.000	0.000
169	A	96	ASP	0	0.145	-0.082	16.852	0.059	0.059	0.000	0.000	0.000	0.000
170	A	96	ASP	-1	-0.903	-0.768	16.325	-0.495	-0.495	0.000	0.000	0.000	0.000
171	A	97	LEU	0	0.049	-0.133	18.178	-0.045	-0.045	0.000	0.000	0.000	0.000
172	A	97	LEU	0	-0.011	0.128	21.504	0.001	0.001	0.000	0.000	0.000	0.000
173	A	98	ASN	0	0.052	-0.081	20.473	0.020	0.020	0.000	0.000	0.000	0.000
174	A	98	ASN	0	-0.114	0.059	20.135	0.027	0.027	0.000	0.000	0.000	0.000
175	A	99	GLN	0	0.055	-0.099	17.350	0.033	0.033	0.000	0.000	0.000	0.000
176	A	99	GLN	0	-0.128	0.066	15.236	-0.101	-0.101	0.000	0.000	0.000	0.000
177	A	100	PRO	0	-0.024	-0.105	17.819	0.023	0.023	0.000	0.000	0.000	0.000
178	A	101	ILE	0	0.080	-0.004	18.257	-0.078	-0.078	0.000	0.000	0.000	0.000
179	A	101	ILE	0	-0.077	0.117	19.642	0.001	0.001	0.000	0.000	0.000	0.000
180	A	102	ILE	0	0.104	-0.101	17.125	0.060	0.060	0.000	0.000	0.000	0.000
181	A	102	ILE	0	-0.110	0.068	14.506	-0.014	-0.014	0.000	0.000	0.000	0.000
182	A	103	LEU	0	0.108	-0.085	18.539	-0.036	-0.036	0.000	0.000	0.000	0.000
183	A	103	LEU	0	-0.072	0.122	22.074	0.006	0.006	0.000	0.000	0.000	0.000
184	A	104	ALA	0	0.112	-0.073	17.839	0.016	0.016	0.000	0.000	0.000	0.000
185	A	104	ALA	0	-0.087	0.081	17.433	-0.016	-0.016	0.000	0.000	0.000	0.000
186	A	105	LYS	0	0.033	-0.115	19.363	0.010	0.010	0.000	0.000	0.000	0.000
187	A	105	LYS	1	0.915	1.097	21.715	0.218	0.218	0.000	0.000	0.000	0.000
188	A	106	PRO	0	0.032	-0.082	18.908	-0.035	-0.035	0.000	0.000	0.000	0.000
189	A	107	LEU	0	0.074	-0.032	19.041	0.021	0.021	0.000	0.000	0.000	0.000
190	A	107	LEU	0	-0.062	0.108	16.296	0.000	0.000	0.000	0.000	0.000	0.000
191	A	108	ARG	0	0.015	-0.069	20.481	0.024	0.024	0.000	0.000	0.000	0.000
192	A	108	ARG	1	0.818	1.021	20.769	0.192	0.192	0.000	0.000	0.000	0.000
193	A	109	GLN	0	0.180	-0.068	22.874	-0.024	-0.024	0.000	0.000	0.000	0.000
194	A	109	GLN	0	-0.098	0.097	26.831	-0.006	-0.006	0.000	0.000	0.000	0.000
195	A	110	HIS	0	0.104	-0.120	22.546	0.009	0.009	0.000	0.000	0.000	0.000
196	A	110	HIS	0	-0.111	0.108	18.946	-0.017	-0.017	0.000	0.000	0.000	0.000
197	A	111	ASN	0	0.118	-0.064	23.572	0.008	0.008	0.000	0.000	0.000	0.000
198	A	111	ASN	0	-0.119	0.057	23.909	-0.004	-0.004	0.000	0.000	0.000	0.000
199	A	112	ARG	0	-0.010	-0.097	23.134	0.020	0.020	0.000	0.000	0.000	0.000
200	A	112	ARG	1	0.897	1.077	22.081	0.242	0.242	0.000	0.000	0.000	0.000
201	A	113	GLY	0	0.066	-0.079	24.396	-0.006	-0.006	0.000	0.000	0.000	0.000
202	A	114	ASP	0	0.097	0.000	23.881	-0.024	-0.024	0.000	0.000	0.000	0.000
203	A	114	ASP	-1	-0.965	-0.831	25.302	-0.190	-0.190	0.000	0.000	0.000	0.000
204	A	115	LEU	0	0.124	-0.142	22.938	-0.003	-0.003	0.000	0.000	0.000	0.000
205	A	115	LEU	0	-0.118	0.104	22.810	0.005	0.005	0.000	0.000	0.000	0.000
206	A	116	VAL	0	0.002	-0.091	19.429	0.024	0.024	0.000	0.000	0.000	0.000
207	A	116	VAL	0	-0.074	0.089	17.645	-0.006	-0.006	0.000	0.000	0.000	0.000
208	A	117	HIS	0	0.092	-0.097	19.735	-0.003	-0.003	0.000	0.000	0.000	0.000
209	A	117	HIS	0	-0.047	0.114	20.668	-0.005	-0.005	0.000	0.000	0.000	0.000
210	A	118	LEU	0	0.063	-0.107	15.336	0.001	0.001	0.000	0.000	0.000	0.000
211	A	118	LEU	0	-0.088	0.095	13.870	-0.021	-0.021	0.000	0.000	0.000	0.000
212	A	119	LEU	0	0.144	-0.127	14.865	0.059	0.059	0.000	0.000	0.000	0.000
213	A	119	LEU	0	-0.104	0.141	14.371	-0.010	-0.010	0.000	0.000	0.000	0.000
214	A	120	PRO	0	0.029	-0.096	12.630	-0.169	-0.169	0.000	0.000	0.000	0.000
215	A	121	GLN	0	0.155	0.005	10.805	-0.272	-0.272	0.000	0.000	0.000	0.000
216	A	121	GLN	0	-0.114	0.100	11.742	0.080	0.080	0.000	0.000	0.000	0.000
217	A	122	PHE	0	-0.031	-0.140	9.891	-0.286	-0.286	0.000	0.000	0.000	0.000
218	A	122	PHE	0	-0.081	0.111	11.415	0.031	0.031	0.000	0.000	0.000	0.000
219	A	123	VAL	0	0.050	-0.100	8.705	-0.173	-0.173	0.000	0.000	0.000	0.000
220	A	123	VAL	0	-0.033	0.128	10.056	0.041	0.041	0.000	0.000	0.000	0.000
221	A	124	VAL	0	0.069	-0.086	4.998	0.067	0.070	-0.002	-0.004	0.002	0.000
222	A	124	VAL	0	-0.084	0.069	3.332	-0.240	-0.515	-0.002	0.387	-0.110	0.000
223	A	125	PRO	0	0.021	-0.076	6.412	0.345	0.345	0.000	0.000	0.000	0.000
224	A	126	VAL	0	0.050	-0.017	7.547	-0.167	-0.167	0.000	0.000	0.000	0.000
225	A	126	VAL	0	-0.123	0.077	8.425	0.002	0.002	0.000	0.000	0.000	0.000
226	A	127	TYR	0	0.062	-0.119	9.973	0.002	0.002	0.000	0.000	0.000	0.000
227	A	127	TYR	0	-0.053	0.121	8.590	-0.022	-0.022	0.000	0.000	0.000	0.000
228	A	128	ASN	0	0.001	-0.092	12.638	0.041	0.041	0.000	0.000	0.000	0.000
229	A	128	ASN	0	0.028	0.015	14.782	0.033	0.033	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:8:LYS)