FMO DATABASE

FMODB ID: 4LGNN

Calculation Name: 3DA5-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

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	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

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	-1144880.572712
FMO2-HF: Nuclear repulsion	1095339.621362
FMO2-HF: Total energy	-49540.95135
FMO2-MP2: Total energy	-49690.303409

3D Structure

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.
-0.723	0.948	-0.002	-0.735	-0.934	0.006

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 : 0.176 / q_NPA : 0.057

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	0.712	0.999	4.202	0.879	1.231	0.002	-0.176	-0.178	0.000
5	A	10	THR	0	0.013	-0.069	3.886	-1.660	-0.184	-0.006	-0.836	-0.635	0.005
6	A	10	THR	0	-0.017	0.075	5.931	0.066	0.066	0.000	0.000	0.000	0.000
7	A	11	LEU	0	0.165	-0.079	6.408	0.378	0.378	0.000	0.000	0.000	0.000
8	A	11	LEU	0	-0.109	0.099	9.793	0.011	0.011	0.000	0.000	0.000	0.000
9	A	12	TRP	0	0.071	-0.112	9.544	0.189	0.189	0.000	0.000	0.000	0.000
10	A	12	TRP	0	-0.079	0.077	11.658	-0.021	-0.021	0.000	0.000	0.000	0.000
11	A	13	GLU	0	0.089	-0.090	8.596	0.264	0.264	0.000	0.000	0.000	0.000
12	A	13	GLU	-1	-0.897	-0.784	7.868	-0.951	-0.951	0.000	0.000	0.000	0.000
13	A	14	LEU	0	0.050	-0.082	9.066	0.152	0.152	0.000	0.000	0.000	0.000
14	A	14	LEU	0	-0.095	0.081	6.270	0.034	0.034	0.000	0.000	0.000	0.000
15	A	15	VAL	0	0.007	-0.115	9.661	0.149	0.149	0.000	0.000	0.000	0.000
16	A	15	VAL	0	-0.103	0.115	12.524	0.002	0.002	0.000	0.000	0.000	0.000
17	A	16	GLY	0	0.062	-0.105	12.749	0.062	0.062	0.000	0.000	0.000	0.000
18	A	17	ARG	0	0.034	0.001	13.921	0.054	0.054	0.000	0.000	0.000	0.000
19	A	17	ARG	1	0.720	0.976	11.838	0.742	0.742	0.000	0.000	0.000	0.000
20	A	18	ASN	0	0.170	-0.058	15.624	0.036	0.036	0.000	0.000	0.000	0.000
21	A	18	ASN	0	-0.084	0.089	18.159	0.005	0.005	0.000	0.000	0.000	0.000
22	A	19	LYS	0	0.129	-0.091	17.865	-0.038	-0.038	0.000	0.000	0.000	0.000
23	A	19	LYS	1	0.821	1.047	20.519	0.298	0.298	0.000	0.000	0.000	0.000
24	A	20	ASP	0	0.079	-0.109	20.044	-0.018	-0.018	0.000	0.000	0.000	0.000
25	A	20	ASP	-1	-0.887	-0.796	22.440	-0.213	-0.213	0.000	0.000	0.000	0.000
26	A	21	ALA	0	0.131	-0.079	17.914	0.015	0.015	0.000	0.000	0.000	0.000
27	A	21	ALA	0	-0.066	0.115	17.156	-0.001	-0.001	0.000	0.000	0.000	0.000
28	A	22	LEU	0	0.074	-0.107	16.112	-0.002	-0.002	0.000	0.000	0.000	0.000
29	A	22	LEU	0	-0.094	0.091	14.536	-0.015	-0.015	0.000	0.000	0.000	0.000
30	A	23	ARG	0	0.062	-0.105	17.113	-0.022	-0.022	0.000	0.000	0.000	0.000
31	A	23	ARG	1	0.653	0.936	21.768	0.217	0.217	0.000	0.000	0.000	0.000
32	A	24	ASP	0	0.126	-0.108	20.319	-0.001	-0.001	0.000	0.000	0.000	0.000
33	A	24	ASP	-1	-0.910	-0.757	20.677	-0.198	-0.198	0.000	0.000	0.000	0.000
34	A	25	PHE	0	0.148	-0.074	15.658	0.040	0.040	0.000	0.000	0.000	0.000
35	A	25	PHE	0	-0.076	0.078	11.355	-0.021	-0.021	0.000	0.000	0.000	0.000
36	A	26	LEU	0	0.028	-0.101	16.549	0.003	0.003	0.000	0.000	0.000	0.000
37	A	26	LEU	0	-0.089	0.086	14.912	-0.009	-0.009	0.000	0.000	0.000	0.000
38	A	27	LYS	0	0.082	-0.096	17.510	0.011	0.011	0.000	0.000	0.000	0.000
39	A	27	LYS	1	0.767	1.019	21.693	0.169	0.169	0.000	0.000	0.000	0.000
40	A	28	GLU	0	0.036	-0.163	18.856	0.019	0.019	0.000	0.000	0.000	0.000
41	A	28	GLU	-1	-0.947	-0.832	17.435	-0.188	-0.188	0.000	0.000	0.000	0.000
42	A	29	HIS	0	0.033	-0.041	16.341	0.039	0.039	0.000	0.000	0.000	0.000
43	A	29	HIS	1	0.737	0.979	15.551	0.219	0.219	0.000	0.000	0.000	0.000
44	A	30	ARG	0	0.137	-0.113	17.878	-0.025	-0.025	0.000	0.000	0.000	0.000
45	A	30	ARG	1	0.719	1.026	21.491	0.166	0.166	0.000	0.000	0.000	0.000
46	A	31	GLY	0	-0.061	-0.132	19.454	0.026	0.026	0.000	0.000	0.000	0.000
47	A	32	THR	0	0.011	0.038	17.852	0.008	0.008	0.000	0.000	0.000	0.000
48	A	32	THR	0	-0.013	0.071	17.344	-0.008	-0.008	0.000	0.000	0.000	0.000
49	A	33	ILE	0	0.057	-0.085	14.109	0.030	0.030	0.000	0.000	0.000	0.000
50	A	33	ILE	0	-0.062	0.091	11.937	-0.011	-0.011	0.000	0.000	0.000	0.000
51	A	34	LEU	0	-0.003	-0.119	13.260	0.037	0.037	0.000	0.000	0.000	0.000
52	A	34	LEU	0	-0.063	0.099	13.451	0.000	0.000	0.000	0.000	0.000	0.000
53	A	35	LEU	0	0.088	-0.116	10.798	-0.069	-0.069	0.000	0.000	0.000	0.000
54	A	35	LEU	0	-0.043	0.126	10.925	-0.003	-0.003	0.000	0.000	0.000	0.000
55	A	36	ARG	0	0.143	-0.080	9.285	0.218	0.218	0.000	0.000	0.000	0.000
56	A	36	ARG	1	0.751	1.024	7.643	0.791	0.791	0.000	0.000	0.000	0.000
57	A	37	ASP	0	0.144	-0.071	8.822	-0.423	-0.423	0.000	0.000	0.000	0.000
58	A	37	ASP	-1	-0.866	-0.776	12.215	-0.872	-0.872	0.000	0.000	0.000	0.000
59	A	38	ILE	0	-0.017	-0.108	7.220	0.242	0.242	0.000	0.000	0.000	0.000
60	A	38	ILE	0	-0.107	0.070	4.669	-0.317	-0.285	-0.001	-0.008	-0.022	0.000
61	A	39	ALA	0	0.175	-0.089	8.754	-0.026	-0.026	0.000	0.000	0.000	0.000
62	A	39	ALA	0	-0.037	0.121	11.558	0.017	0.017	0.000	0.000	0.000	0.000
63	A	40	SER	0	0.038	-0.064	11.823	0.150	0.150	0.000	0.000	0.000	0.000
64	A	40	SER	0	-0.066	0.042	13.457	-0.039	-0.039	0.000	0.000	0.000	0.000
65	A	41	GLU	0	0.105	-0.099	12.877	-0.096	-0.096	0.000	0.000	0.000	0.000
66	A	41	GLU	-1	-0.919	-0.804	14.902	-0.337	-0.337	0.000	0.000	0.000	0.000
67	A	42	HIS	0	0.120	-0.075	13.958	-0.027	-0.027	0.000	0.000	0.000	0.000
68	A	42	HIS	0	-0.102	0.097	16.733	-0.011	-0.011	0.000	0.000	0.000	0.000
69	A	43	LYS	0	0.109	-0.059	10.705	0.012	0.012	0.000	0.000	0.000	0.000
70	A	43	LYS	1	0.716	1.012	9.639	0.581	0.581	0.000	0.000	0.000	0.000
71	A	44	VAL	0	0.075	-0.137	11.718	-0.027	-0.027	0.000	0.000	0.000	0.000
72	A	44	VAL	0	-0.077	0.114	15.371	0.013	0.013	0.000	0.000	0.000	0.000
73	A	45	VAL	0	0.078	-0.103	12.683	-0.147	-0.147	0.000	0.000	0.000	0.000
74	A	45	VAL	0	-0.075	0.090	11.627	0.004	0.004	0.000	0.000	0.000	0.000
75	A	46	TYR	0	0.006	-0.117	13.800	0.094	0.094	0.000	0.000	0.000	0.000
76	A	46	TYR	0	-0.014	0.113	14.071	0.030	0.030	0.000	0.000	0.000	0.000
77	A	47	LYS	0	0.137	-0.075	15.237	-0.062	-0.062	0.000	0.000	0.000	0.000
78	A	47	LYS	1	0.804	1.044	18.831	0.274	0.274	0.000	0.000	0.000	0.000
79	A	48	PRO	0	0.024	-0.097	15.760	0.016	0.016	0.000	0.000	0.000	0.000
80	A	49	ILE	0	0.083	0.010	18.475	0.035	0.035	0.000	0.000	0.000	0.000
81	A	49	ILE	0	-0.057	0.120	21.876	0.003	0.003	0.000	0.000	0.000	0.000
82	A	50	PHE	0	0.058	-0.097	21.954	-0.024	-0.024	0.000	0.000	0.000	0.000
83	A	50	PHE	0	-0.124	0.067	20.055	0.004	0.004	0.000	0.000	0.000	0.000
84	A	51	LYS	0	0.156	-0.061	24.463	0.008	0.008	0.000	0.000	0.000	0.000
85	A	51	LYS	1	0.779	1.055	25.025	0.240	0.240	0.000	0.000	0.000	0.000
86	A	52	ARG	0	0.068	-0.092	27.703	0.006	0.006	0.000	0.000	0.000	0.000
87	A	52	ARG	1	0.862	1.050	31.418	0.128	0.128	0.000	0.000	0.000	0.000
88	A	53	TYR	0	0.057	-0.088	30.719	0.003	0.003	0.000	0.000	0.000	0.000
89	A	53	TYR	0	-0.076	0.107	33.718	0.000	0.000	0.000	0.000	0.000	0.000
90	A	54	ASN	0	0.067	-0.082	27.877	0.005	0.005	0.000	0.000	0.000	0.000
91	A	54	ASN	0	-0.102	0.068	27.155	0.005	0.005	0.000	0.000	0.000	0.000
92	A	55	GLY	0	0.107	-0.051	28.325	0.009	0.009	0.000	0.000	0.000	0.000
93	A	56	ASP	0	0.094	-0.032	24.981	-0.003	-0.003	0.000	0.000	0.000	0.000
94	A	56	ASP	-1	-0.895	-0.775	25.459	-0.183	-0.183	0.000	0.000	0.000	0.000
95	A	57	PRO	0	-0.017	-0.100	20.664	0.009	0.009	0.000	0.000	0.000	0.000
96	A	58	ASP	0	0.109	-0.006	22.566	0.013	0.013	0.000	0.000	0.000	0.000
97	A	58	ASP	-1	-0.946	-0.843	23.998	-0.227	-0.227	0.000	0.000	0.000	0.000
98	A	59	LEU	0	0.013	-0.140	21.883	-0.033	-0.033	0.000	0.000	0.000	0.000
99	A	59	LEU	0	-0.072	0.085	19.520	-0.006	-0.006	0.000	0.000	0.000	0.000
100	A	60	ILE	0	0.117	-0.054	22.654	0.031	0.031	0.000	0.000	0.000	0.000
101	A	60	ILE	0	-0.094	0.104	23.786	-0.002	-0.002	0.000	0.000	0.000	0.000
102	A	61	GLU	0	0.010	-0.141	23.007	-0.041	-0.041	0.000	0.000	0.000	0.000
103	A	61	GLU	-1	-0.942	-0.840	23.379	-0.266	-0.266	0.000	0.000	0.000	0.000
104	A	62	ASP	0	0.028	-0.126	24.775	-0.008	-0.008	0.000	0.000	0.000	0.000
105	A	62	ASP	-1	-0.865	-0.812	27.844	-0.223	-0.223	0.000	0.000	0.000	0.000
106	A	63	ASN	0	0.114	-0.074	26.096	0.017	0.017	0.000	0.000	0.000	0.000
107	A	63	ASN	0	-0.131	0.066	26.772	-0.001	-0.001	0.000	0.000	0.000	0.000
108	A	64	SER	0	0.067	-0.097	24.098	-0.027	-0.027	0.000	0.000	0.000	0.000
109	A	64	SER	0	-0.024	0.084	24.484	0.008	0.008	0.000	0.000	0.000	0.000
110	A	65	ASN	0	0.096	-0.069	24.297	-0.029	-0.029	0.000	0.000	0.000	0.000
111	A	65	ASN	0	-0.132	0.065	28.023	0.013	0.013	0.000	0.000	0.000	0.000
112	A	66	ASP	0	0.144	-0.092	24.708	-0.003	-0.003	0.000	0.000	0.000	0.000
113	A	66	ASP	-1	-0.945	-0.822	23.887	-0.276	-0.276	0.000	0.000	0.000	0.000
114	A	67	VAL	0	0.019	-0.121	20.708	-0.023	-0.023	0.000	0.000	0.000	0.000
115	A	67	VAL	0	-0.079	0.105	19.089	-0.007	-0.007	0.000	0.000	0.000	0.000
116	A	68	GLU	0	0.066	-0.112	20.395	-0.059	-0.059	0.000	0.000	0.000	0.000
117	A	68	GLU	-1	-0.847	-0.773	23.420	-0.261	-0.261	0.000	0.000	0.000	0.000
118	A	69	HIS	0	0.112	-0.067	22.039	-0.019	-0.019	0.000	0.000	0.000	0.000
119	A	69	HIS	0	-0.087	0.080	24.040	0.014	0.014	0.000	0.000	0.000	0.000
120	A	70	TRP	0	0.066	-0.105	19.988	0.005	0.005	0.000	0.000	0.000	0.000
121	A	70	TRP	0	-0.136	0.067	19.065	-0.015	-0.015	0.000	0.000	0.000	0.000
122	A	71	TYR	0	0.170	-0.067	17.465	-0.061	-0.061	0.000	0.000	0.000	0.000
123	A	71	TYR	0	-0.118	0.068	15.106	0.013	0.013	0.000	0.000	0.000	0.000
124	A	72	ASP	0	0.064	-0.137	18.265	-0.047	-0.047	0.000	0.000	0.000	0.000
125	A	72	ASP	-1	-0.934	-0.806	21.012	-0.340	-0.340	0.000	0.000	0.000	0.000
126	A	73	TYR	0	0.068	-0.116	20.824	0.021	0.021	0.000	0.000	0.000	0.000
127	A	73	TYR	0	-0.067	0.095	19.549	0.020	0.020	0.000	0.000	0.000	0.000
128	A	74	HIS	0	-0.005	-0.095	16.460	0.033	0.033	0.000	0.000	0.000	0.000
129	A	74	HIS	1	0.698	0.912	14.853	0.628	0.628	0.000	0.000	0.000	0.000
130	A	75	LEU	0	0.120	-0.075	17.513	-0.013	-0.013	0.000	0.000	0.000	0.000
131	A	75	LEU	0	-0.090	0.100	17.884	0.004	0.004	0.000	0.000	0.000	0.000
132	A	76	GLU	0	0.075	-0.167	18.404	0.010	0.010	0.000	0.000	0.000	0.000
133	A	76	GLU	-1	-0.894	-0.775	22.864	-0.243	-0.243	0.000	0.000	0.000	0.000
134	A	77	ARG	0	0.014	-0.093	20.583	0.039	0.039	0.000	0.000	0.000	0.000
135	A	77	ARG	1	0.717	1.004	20.621	0.272	0.272	0.000	0.000	0.000	0.000
136	A	78	TYR	0	0.032	-0.091	16.808	0.044	0.044	0.000	0.000	0.000	0.000
137	A	78	TYR	0	-0.088	0.075	16.169	0.010	0.010	0.000	0.000	0.000	0.000
138	A	79	TRP	0	0.086	-0.073	16.201	0.003	0.003	0.000	0.000	0.000	0.000
139	A	79	TRP	0	-0.149	0.041	11.340	-0.047	-0.047	0.000	0.000	0.000	0.000
140	A	80	ASN	0	0.145	-0.063	17.285	0.008	0.008	0.000	0.000	0.000	0.000
141	A	80	ASN	0	-0.135	0.077	21.510	0.006	0.006	0.000	0.000	0.000	0.000
142	A	81	THR	0	-0.023	-0.108	19.914	0.023	0.023	0.000	0.000	0.000	0.000
143	A	81	THR	0	-0.006	0.042	20.133	-0.009	-0.009	0.000	0.000	0.000	0.000
144	A	82	PRO	0	0.055	-0.075	19.859	-0.028	-0.028	0.000	0.000	0.000	0.000
145	A	83	GLU	0	-0.015	-0.054	18.591	-0.018	-0.018	0.000	0.000	0.000	0.000
146	A	83	GLU	-1	-0.831	-0.764	18.214	-0.114	-0.114	0.000	0.000	0.000	0.000
147	A	84	LEU	0	0.088	-0.098	15.374	0.002	0.002	0.000	0.000	0.000	0.000
148	A	84	LEU	0	-0.035	0.145	15.038	-0.004	-0.004	0.000	0.000	0.000	0.000
149	A	85	LYS	0	0.155	-0.069	14.940	-0.080	-0.080	0.000	0.000	0.000	0.000
150	A	85	LYS	1	0.862	1.080	18.369	0.307	0.307	0.000	0.000	0.000	0.000
151	A	86	LYS	0	0.082	-0.088	16.013	-0.054	-0.054	0.000	0.000	0.000	0.000
152	A	86	LYS	1	0.772	1.015	15.438	0.137	0.137	0.000	0.000	0.000	0.000
153	A	87	GLU	0	0.049	-0.124	12.261	0.007	0.007	0.000	0.000	0.000	0.000
154	A	87	GLU	-1	-0.933	-0.821	9.971	-0.493	-0.493	0.000	0.000	0.000	0.000
155	A	88	PHE	0	0.117	-0.074	11.392	-0.110	-0.110	0.000	0.000	0.000	0.000
156	A	88	PHE	0	-0.094	0.089	13.412	-0.004	-0.004	0.000	0.000	0.000	0.000
157	A	89	TYR	0	0.098	-0.100	11.979	-0.138	-0.138	0.000	0.000	0.000	0.000
158	A	89	TYR	0	-0.086	0.097	15.566	0.008	0.008	0.000	0.000	0.000	0.000
159	A	90	LYS	0	0.033	-0.101	11.942	-0.041	-0.041	0.000	0.000	0.000	0.000
160	A	90	LYS	1	0.875	1.051	11.459	0.206	0.206	0.000	0.000	0.000	0.000
161	A	91	LYS	0	0.106	-0.092	7.893	0.029	0.029	0.000	0.000	0.000	0.000
162	A	91	LYS	1	0.667	1.017	6.697	1.105	1.105	0.000	0.000	0.000	0.000
163	A	92	PHE	0	-0.006	-0.123	7.825	-0.417	-0.417	0.000	0.000	0.000	0.000
164	A	92	PHE	0	-0.062	0.102	8.215	-0.046	-0.046	0.000	0.000	0.000	0.000
165	A	93	GLY	0	0.042	-0.055	10.481	0.027	0.027	0.000	0.000	0.000	0.000
166	A	94	PRO	0	0.022	0.006	13.623	-0.022	-0.022	0.000	0.000	0.000	0.000
167	A	95	VAL	0	0.081	-0.001	16.265	-0.073	-0.073	0.000	0.000	0.000	0.000
168	A	95	VAL	0	-0.029	0.137	18.453	0.000	0.000	0.000	0.000	0.000	0.000
169	A	96	ASP	0	0.132	-0.085	16.926	0.062	0.062	0.000	0.000	0.000	0.000
170	A	96	ASP	-1	-0.875	-0.765	16.277	-0.512	-0.512	0.000	0.000	0.000	0.000
171	A	97	LEU	0	0.020	-0.128	18.188	-0.040	-0.040	0.000	0.000	0.000	0.000
172	A	97	LEU	0	-0.018	0.112	21.864	0.003	0.003	0.000	0.000	0.000	0.000
173	A	98	ASN	0	0.076	-0.075	20.309	0.023	0.023	0.000	0.000	0.000	0.000
174	A	98	ASN	0	-0.126	0.052	19.841	0.029	0.029	0.000	0.000	0.000	0.000
175	A	99	GLN	0	0.053	-0.093	17.307	0.039	0.039	0.000	0.000	0.000	0.000
176	A	99	GLN	0	-0.111	0.063	15.360	-0.103	-0.103	0.000	0.000	0.000	0.000
177	A	100	PRO	0	-0.027	-0.101	18.059	0.022	0.022	0.000	0.000	0.000	0.000
178	A	101	ILE	0	0.067	-0.018	18.368	-0.077	-0.077	0.000	0.000	0.000	0.000
179	A	101	ILE	0	-0.067	0.116	19.500	0.002	0.002	0.000	0.000	0.000	0.000
180	A	102	ILE	0	0.138	-0.085	17.258	0.062	0.062	0.000	0.000	0.000	0.000
181	A	102	ILE	0	-0.119	0.079	14.633	-0.014	-0.014	0.000	0.000	0.000	0.000
182	A	103	LEU	0	0.099	-0.089	18.656	-0.031	-0.031	0.000	0.000	0.000	0.000
183	A	103	LEU	0	-0.083	0.122	22.354	0.006	0.006	0.000	0.000	0.000	0.000
184	A	104	ALA	0	0.104	-0.088	18.066	0.011	0.011	0.000	0.000	0.000	0.000
185	A	104	ALA	0	-0.072	0.088	17.604	-0.015	-0.015	0.000	0.000	0.000	0.000
186	A	105	LYS	0	0.030	-0.106	19.586	0.009	0.009	0.000	0.000	0.000	0.000
187	A	105	LYS	1	0.928	1.097	21.915	0.211	0.211	0.000	0.000	0.000	0.000
188	A	106	PRO	0	0.021	-0.092	18.842	-0.030	-0.030	0.000	0.000	0.000	0.000
189	A	107	LEU	0	0.072	-0.015	19.035	0.021	0.021	0.000	0.000	0.000	0.000
190	A	107	LEU	0	-0.085	0.101	16.454	0.001	0.001	0.000	0.000	0.000	0.000
191	A	108	ARG	0	0.040	-0.082	20.482	0.025	0.025	0.000	0.000	0.000	0.000
192	A	108	ARG	1	0.824	1.028	21.635	0.192	0.192	0.000	0.000	0.000	0.000
193	A	109	GLN	0	0.191	-0.068	22.983	-0.025	-0.025	0.000	0.000	0.000	0.000
194	A	109	GLN	0	-0.090	0.095	27.191	-0.007	-0.007	0.000	0.000	0.000	0.000
195	A	110	HIS	0	0.067	-0.138	22.922	0.009	0.009	0.000	0.000	0.000	0.000
196	A	110	HIS	0	-0.106	0.103	19.704	-0.017	-0.017	0.000	0.000	0.000	0.000
197	A	111	ASN	0	0.096	-0.044	23.821	0.007	0.007	0.000	0.000	0.000	0.000
198	A	111	ASN	0	-0.095	0.066	23.912	-0.008	-0.008	0.000	0.000	0.000	0.000
199	A	112	ARG	0	-0.003	-0.120	23.598	0.016	0.016	0.000	0.000	0.000	0.000
200	A	112	ARG	1	0.905	1.073	22.403	0.255	0.255	0.000	0.000	0.000	0.000
201	A	113	GLY	0	0.064	-0.064	24.831	0.001	0.001	0.000	0.000	0.000	0.000
202	A	114	ASP	0	0.029	-0.018	24.005	-0.030	-0.030	0.000	0.000	0.000	0.000
203	A	114	ASP	-1	-0.947	-0.834	25.932	-0.183	-0.183	0.000	0.000	0.000	0.000
204	A	115	LEU	0	0.109	-0.128	23.321	-0.001	-0.001	0.000	0.000	0.000	0.000
205	A	115	LEU	0	-0.102	0.100	23.226	0.004	0.004	0.000	0.000	0.000	0.000
206	A	116	VAL	0	-0.017	-0.097	19.864	0.022	0.022	0.000	0.000	0.000	0.000
207	A	116	VAL	0	-0.073	0.079	18.093	-0.006	-0.006	0.000	0.000	0.000	0.000
208	A	117	HIS	0	0.128	-0.079	20.045	-0.006	-0.006	0.000	0.000	0.000	0.000
209	A	117	HIS	0	-0.062	0.113	20.958	-0.002	-0.002	0.000	0.000	0.000	0.000
210	A	118	LEU	0	0.036	-0.116	15.583	-0.003	-0.003	0.000	0.000	0.000	0.000
211	A	118	LEU	0	-0.085	0.092	14.127	-0.018	-0.018	0.000	0.000	0.000	0.000
212	A	119	LEU	0	0.145	-0.113	15.184	0.051	0.051	0.000	0.000	0.000	0.000
213	A	119	LEU	0	-0.098	0.140	14.662	-0.011	-0.011	0.000	0.000	0.000	0.000
214	A	120	PRO	0	0.036	-0.091	12.652	-0.175	-0.175	0.000	0.000	0.000	0.000
215	A	121	GLN	0	0.150	0.005	10.883	-0.270	-0.270	0.000	0.000	0.000	0.000
216	A	121	GLN	0	-0.121	0.087	12.092	0.082	0.082	0.000	0.000	0.000	0.000
217	A	122	PHE	0	-0.005	-0.145	10.122	-0.282	-0.282	0.000	0.000	0.000	0.000
218	A	122	PHE	0	-0.081	0.112	11.696	0.028	0.028	0.000	0.000	0.000	0.000
219	A	123	VAL	0	0.029	-0.089	8.954	-0.175	-0.175	0.000	0.000	0.000	0.000
220	A	123	VAL	0	-0.052	0.113	10.169	0.041	0.041	0.000	0.000	0.000	0.000
221	A	124	VAL	0	0.071	-0.091	5.137	-0.067	-0.073	-0.002	-0.003	0.010	0.000
222	A	124	VAL	0	-0.080	0.078	3.385	-0.364	-0.547	0.005	0.288	-0.109	0.001
223	A	125	PRO	0	0.030	-0.087	6.028	0.389	0.389	0.000	0.000	0.000	0.000
224	A	126	VAL	0	0.047	-0.005	7.449	-0.178	-0.178	0.000	0.000	0.000	0.000
225	A	126	VAL	0	-0.126	0.074	8.755	0.003	0.003	0.000	0.000	0.000	0.000
226	A	127	TYR	0	0.098	-0.099	10.136	0.004	0.004	0.000	0.000	0.000	0.000
227	A	127	TYR	0	-0.036	0.114	8.340	-0.042	-0.042	0.000	0.000	0.000	0.000
228	A	128	ASN	0	-0.027	-0.096	12.631	0.040	0.040	0.000	0.000	0.000	0.000
229	A	128	ASN	0	0.005	-0.001	14.511	0.015	0.015	0.000	0.000	0.000	0.000

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