FMO DATABASE

FMODB ID: KG3N3

Calculation Name: 2EEN-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2EEN

Chain ID: A

ChEMBL ID:

UniProt ID: O59483

Base Structure: X-ray

Registration Date: 2023-09-21

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

DOI:

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	177
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2112541.065275
FMO2-HF: Nuclear repulsion	2038887.217767
FMO2-HF: Total energy	-73653.847508
FMO2-MP2: Total energy	-73873.628163

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:2:TYR)

Summations of interaction energy for fragment #1(A:2:TYR)

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.
-40.453	-26.937	17.217	-9.576	-21.153	-0.027

Interaction energy analysis for fragmet #1(A:2:TYR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.041 / q_NPA : -0.043

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	4	VAL	0	-0.034	-0.018	3.681	-0.256	1.190	0.000	-0.492	-0.954	0.002
4	A	5	GLU	-1	-0.803	-0.893	5.145	0.130	0.217	-0.001	-0.003	-0.083	0.000
5	A	6	LEU	0	-0.012	-0.018	8.263	0.237	0.237	0.000	0.000	0.000	0.000
6	A	7	LYS	1	0.783	0.878	11.452	0.120	0.120	0.000	0.000	0.000	0.000
7	A	8	GLY	0	0.041	0.023	14.959	0.028	0.028	0.000	0.000	0.000	0.000
8	A	9	TYR	0	-0.091	-0.064	18.551	0.006	0.006	0.000	0.000	0.000	0.000
9	A	10	ALA	0	-0.002	0.004	22.007	-0.021	-0.021	0.000	0.000	0.000	0.000
10	A	11	ASN	0	-0.029	-0.028	24.028	0.012	0.012	0.000	0.000	0.000	0.000
11	A	12	ASP	-1	-0.805	-0.931	27.055	-0.119	-0.119	0.000	0.000	0.000	0.000
12	A	13	GLU	-1	-0.896	-0.926	29.263	-0.154	-0.154	0.000	0.000	0.000	0.000
13	A	14	ILE	0	0.015	0.004	22.925	-0.014	-0.014	0.000	0.000	0.000	0.000
14	A	15	PHE	0	-0.034	-0.031	23.594	-0.021	-0.021	0.000	0.000	0.000	0.000
15	A	16	GLU	-1	-0.855	-0.918	26.247	-0.166	-0.166	0.000	0.000	0.000	0.000
16	A	17	LYS	1	0.830	0.911	26.019	0.252	0.252	0.000	0.000	0.000	0.000
17	A	18	VAL	0	-0.015	0.001	21.848	-0.022	-0.022	0.000	0.000	0.000	0.000
18	A	19	ARG	1	0.786	0.863	24.620	0.152	0.152	0.000	0.000	0.000	0.000
19	A	20	GLU	-1	-0.929	-0.951	27.169	-0.188	-0.188	0.000	0.000	0.000	0.000
20	A	21	THR	0	-0.124	-0.070	24.032	-0.001	-0.001	0.000	0.000	0.000	0.000
21	A	22	PHE	0	-0.034	-0.031	20.954	-0.039	-0.039	0.000	0.000	0.000	0.000
22	A	23	GLU	-1	-0.865	-0.920	22.596	-0.251	-0.251	0.000	0.000	0.000	0.000
23	A	24	PHE	0	-0.009	-0.007	22.397	-0.021	-0.021	0.000	0.000	0.000	0.000
24	A	25	MET	0	-0.068	-0.017	17.001	-0.009	-0.009	0.000	0.000	0.000	0.000
25	A	26	ARG	1	0.767	0.859	18.612	0.141	0.141	0.000	0.000	0.000	0.000
26	A	27	LYS	1	0.860	0.923	22.456	0.096	0.096	0.000	0.000	0.000	0.000
27	A	28	GLU	-1	-0.772	-0.860	18.065	-0.135	-0.135	0.000	0.000	0.000	0.000
28	A	29	ILE	0	0.006	-0.002	22.456	-0.008	-0.008	0.000	0.000	0.000	0.000
29	A	30	HIS	0	-0.043	-0.036	16.411	0.035	0.035	0.000	0.000	0.000	0.000
30	A	31	GLU	-1	-0.802	-0.869	21.601	0.052	0.052	0.000	0.000	0.000	0.000
31	A	32	ASP	-1	-0.756	-0.828	17.773	0.098	0.098	0.000	0.000	0.000	0.000
32	A	33	ILE	0	-0.004	-0.005	20.259	-0.014	-0.014	0.000	0.000	0.000	0.000
33	A	34	TYR	0	-0.006	-0.022	15.364	0.039	0.039	0.000	0.000	0.000	0.000
34	A	35	TYR	0	0.023	0.000	19.213	-0.028	-0.028	0.000	0.000	0.000	0.000
35	A	36	GLN	0	0.021	0.007	19.264	0.079	0.079	0.000	0.000	0.000	0.000
36	A	37	HIS	0	0.029	0.012	18.380	-0.026	-0.026	0.000	0.000	0.000	0.000
37	A	38	PRO	0	-0.015	0.001	20.870	-0.021	-0.021	0.000	0.000	0.000	0.000
38	A	39	CYS	0	-0.070	-0.042	22.344	-0.025	-0.025	0.000	0.000	0.000	0.000
39	A	40	ARG	1	0.812	0.873	14.105	-0.854	-0.854	0.000	0.000	0.000	0.000
40	A	41	ASP	-1	-0.739	-0.824	20.633	0.401	0.401	0.000	0.000	0.000	0.000
41	A	42	PHE	0	0.039	0.012	15.758	0.033	0.033	0.000	0.000	0.000	0.000
42	A	43	SER	0	-0.041	-0.040	16.465	0.034	0.034	0.000	0.000	0.000	0.000
43	A	44	LYS	1	0.767	0.860	18.766	-0.416	-0.416	0.000	0.000	0.000	0.000
44	A	45	THR	0	-0.044	-0.056	14.023	-0.017	-0.017	0.000	0.000	0.000	0.000
45	A	46	ASP	-1	-0.775	-0.852	11.639	0.879	0.879	0.000	0.000	0.000	0.000
46	A	47	GLU	-1	-0.739	-0.778	11.500	1.160	1.160	0.000	0.000	0.000	0.000
47	A	48	ALA	0	0.012	-0.002	12.651	-0.140	-0.140	0.000	0.000	0.000	0.000
48	A	49	LEU	0	0.001	0.011	13.400	0.094	0.094	0.000	0.000	0.000	0.000
49	A	50	ARG	1	0.824	0.899	11.692	-0.309	-0.309	0.000	0.000	0.000	0.000
50	A	51	ILE	0	0.026	0.030	16.836	0.038	0.038	0.000	0.000	0.000	0.000
51	A	52	ARG	1	0.857	0.889	13.827	-0.065	-0.065	0.000	0.000	0.000	0.000
52	A	53	ILE	0	0.016	0.022	18.889	0.003	0.003	0.000	0.000	0.000	0.000
53	A	54	LYS	1	0.829	0.918	15.745	-0.035	-0.035	0.000	0.000	0.000	0.000
54	A	55	ARG	1	0.807	0.866	21.190	-0.048	-0.048	0.000	0.000	0.000	0.000
55	A	56	PHE	0	0.044	0.018	22.094	-0.022	-0.022	0.000	0.000	0.000	0.000
56	A	57	ASN	0	-0.010	-0.016	25.371	0.004	0.004	0.000	0.000	0.000	0.000
57	A	58	GLY	0	0.005	0.011	28.435	0.001	0.001	0.000	0.000	0.000	0.000
58	A	59	HIS	0	-0.008	0.002	25.373	0.021	0.021	0.000	0.000	0.000	0.000
59	A	60	ASN	0	-0.007	-0.019	24.803	0.000	0.000	0.000	0.000	0.000	0.000
60	A	61	GLU	-1	-0.720	-0.821	18.542	-0.010	-0.010	0.000	0.000	0.000	0.000
61	A	62	VAL	0	0.005	-0.013	20.431	-0.007	-0.007	0.000	0.000	0.000	0.000
62	A	63	PHE	0	0.018	0.020	15.230	-0.003	-0.003	0.000	0.000	0.000	0.000
63	A	64	LEU	0	0.012	0.010	16.377	-0.026	-0.026	0.000	0.000	0.000	0.000
64	A	65	THR	0	-0.019	-0.048	10.901	0.022	0.022	0.000	0.000	0.000	0.000
65	A	66	TYR	0	-0.080	-0.057	8.917	-0.004	-0.004	0.000	0.000	0.000	0.000
66	A	67	LYS	1	0.783	0.878	8.021	0.253	0.253	0.000	0.000	0.000	0.000
67	A	68	GLY	0	0.040	0.017	7.732	-0.099	-0.099	0.000	0.000	0.000	0.000
68	A	69	PRO	0	-0.012	-0.011	7.825	-0.218	-0.218	0.000	0.000	0.000	0.000
69	A	70	LYS	1	0.803	0.899	6.971	-0.210	-0.210	0.000	0.000	0.000	0.000
70	A	71	ILE	0	-0.090	-0.045	2.555	-0.116	0.024	3.316	-0.628	-2.828	0.007
71	A	72	ASP	-1	-0.760	-0.851	6.704	0.234	0.234	0.000	0.000	0.000	0.000
72	A	73	GLU	-1	-0.882	-0.941	8.835	0.239	0.239	0.000	0.000	0.000	0.000
73	A	74	LYS	1	0.849	0.922	11.259	-0.159	-0.159	0.000	0.000	0.000	0.000
74	A	75	SER	0	-0.048	-0.036	7.974	-0.184	-0.184	0.000	0.000	0.000	0.000
75	A	76	LYN	0	-0.008	0.022	9.364	0.298	0.298	0.000	0.000	0.000	0.000
76	A	77	THR	0	0.018	0.005	3.029	-0.656	-0.125	0.136	-0.125	-0.541	0.000
77	A	78	ARG	1	0.827	0.903	4.499	0.026	0.313	-0.001	-0.033	-0.254	0.000
78	A	79	LEU	0	-0.001	0.017	3.116	-3.154	-1.077	0.137	-0.834	-1.379	-0.006
79	A	80	GLU	-1	-0.805	-0.901	3.994	-0.660	-0.523	0.002	-0.027	-0.112	0.000
80	A	81	ILE	0	-0.011	-0.009	6.593	0.544	0.544	0.000	0.000	0.000	0.000
81	A	82	GLU	-1	-0.818	-0.870	9.325	0.104	0.104	0.000	0.000	0.000	0.000
82	A	83	VAL	0	-0.023	-0.008	11.609	0.028	0.028	0.000	0.000	0.000	0.000
83	A	84	GLU	-1	-0.850	-0.923	14.997	0.095	0.095	0.000	0.000	0.000	0.000
84	A	85	ILE	0	-0.064	-0.030	17.804	0.002	0.002	0.000	0.000	0.000	0.000
85	A	86	GLN	0	-0.069	-0.054	20.966	-0.023	-0.023	0.000	0.000	0.000	0.000
86	A	87	GLU	-1	-0.940	-0.963	23.320	0.110	0.110	0.000	0.000	0.000	0.000
87	A	88	ASP	-1	-0.812	-0.907	25.565	0.168	0.168	0.000	0.000	0.000	0.000
88	A	89	VAL	0	0.027	0.019	24.166	0.014	0.014	0.000	0.000	0.000	0.000
89	A	90	ASP	-1	-0.894	-0.947	25.832	0.151	0.151	0.000	0.000	0.000	0.000
90	A	91	LYS	1	0.837	0.892	28.097	-0.141	-0.141	0.000	0.000	0.000	0.000
91	A	92	TYR	0	0.000	0.006	21.434	0.031	0.031	0.000	0.000	0.000	0.000
92	A	93	PHE	0	0.005	-0.002	23.488	0.023	0.023	0.000	0.000	0.000	0.000
93	A	94	GLU	-1	-0.841	-0.898	25.878	0.186	0.186	0.000	0.000	0.000	0.000
94	A	95	LEU	0	-0.023	-0.008	23.518	0.008	0.008	0.000	0.000	0.000	0.000
95	A	96	LEU	0	0.001	-0.003	20.404	0.020	0.020	0.000	0.000	0.000	0.000
96	A	97	ASP	-1	-0.861	-0.917	24.470	0.232	0.232	0.000	0.000	0.000	0.000
97	A	98	ARG	1	0.807	0.871	27.709	-0.185	-0.185	0.000	0.000	0.000	0.000
98	A	99	LEU	0	-0.053	-0.017	23.246	0.001	0.001	0.000	0.000	0.000	0.000
99	A	100	GLY	0	-0.002	-0.001	25.664	0.021	0.021	0.000	0.000	0.000	0.000
100	A	101	PHE	0	-0.013	-0.004	18.912	0.016	0.016	0.000	0.000	0.000	0.000
101	A	102	LYS	1	0.783	0.883	24.106	-0.286	-0.286	0.000	0.000	0.000	0.000
102	A	103	GLU	-1	-0.795	-0.873	23.989	0.193	0.193	0.000	0.000	0.000	0.000
103	A	104	VAL	0	-0.052	-0.020	21.519	-0.009	-0.009	0.000	0.000	0.000	0.000
104	A	105	LEU	0	-0.033	-0.034	22.908	-0.022	-0.022	0.000	0.000	0.000	0.000
105	A	106	LYS	1	0.842	0.913	22.947	-0.133	-0.133	0.000	0.000	0.000	0.000
106	A	107	VAL	0	-0.039	-0.028	20.767	-0.008	-0.008	0.000	0.000	0.000	0.000
107	A	108	VAL	0	0.018	0.024	22.078	0.000	0.000	0.000	0.000	0.000	0.000
108	A	109	LYS	1	0.858	0.938	17.801	0.003	0.003	0.000	0.000	0.000	0.000
109	A	110	THR	0	-0.056	-0.021	23.616	-0.001	-0.001	0.000	0.000	0.000	0.000
110	A	111	ARG	1	0.799	0.852	14.134	0.270	0.270	0.000	0.000	0.000	0.000
111	A	112	GLU	-1	-0.795	-0.846	21.241	-0.154	-0.154	0.000	0.000	0.000	0.000
112	A	113	LYS	1	0.882	0.934	15.188	0.240	0.240	0.000	0.000	0.000	0.000
113	A	114	TYR	0	0.002	-0.022	18.864	0.038	0.038	0.000	0.000	0.000	0.000
114	A	115	TYR	0	0.023	0.003	16.773	-0.094	-0.094	0.000	0.000	0.000	0.000
115	A	116	VAL	0	-0.027	0.001	16.470	0.040	0.040	0.000	0.000	0.000	0.000
116	A	117	GLU	-1	-0.788	-0.891	14.776	-0.979	-0.979	0.000	0.000	0.000	0.000
117	A	118	LYS	1	0.924	0.956	12.525	1.081	1.081	0.000	0.000	0.000	0.000
118	A	119	GLY	0	-0.022	-0.015	11.087	-0.108	-0.108	0.000	0.000	0.000	0.000
119	A	120	VAL	0	-0.010	0.032	10.453	-0.275	-0.275	0.000	0.000	0.000	0.000
120	A	121	THR	0	-0.019	-0.021	12.747	0.168	0.168	0.000	0.000	0.000	0.000
121	A	122	ILE	0	0.009	0.009	14.119	-0.074	-0.074	0.000	0.000	0.000	0.000
122	A	123	THR	0	-0.063	-0.064	15.144	0.037	0.037	0.000	0.000	0.000	0.000
123	A	124	LEU	0	0.001	0.030	18.033	0.001	0.001	0.000	0.000	0.000	0.000
124	A	125	ASP	-1	-0.764	-0.861	18.769	-0.171	-0.171	0.000	0.000	0.000	0.000
125	A	126	GLU	-1	-0.846	-0.926	21.460	-0.073	-0.073	0.000	0.000	0.000	0.000
126	A	127	VAL	0	-0.008	-0.016	21.080	0.014	0.014	0.000	0.000	0.000	0.000
127	A	128	GLU	-1	-0.897	-0.953	24.368	0.020	0.020	0.000	0.000	0.000	0.000
128	A	129	GLY	0	-0.028	-0.018	26.467	0.014	0.014	0.000	0.000	0.000	0.000
129	A	130	LEU	0	-0.118	-0.066	22.119	0.009	0.009	0.000	0.000	0.000	0.000
130	A	131	GLY	0	-0.011	0.012	25.987	-0.006	-0.006	0.000	0.000	0.000	0.000
131	A	132	LYS	1	0.825	0.923	24.512	0.100	0.100	0.000	0.000	0.000	0.000
132	A	133	PHE	0	-0.029	-0.032	19.182	0.013	0.013	0.000	0.000	0.000	0.000
133	A	134	ILE	0	0.004	0.008	18.339	0.002	0.002	0.000	0.000	0.000	0.000
134	A	135	GLU	-1	-0.762	-0.842	13.130	-0.278	-0.278	0.000	0.000	0.000	0.000
135	A	136	ILE	0	-0.027	-0.015	12.180	0.018	0.018	0.000	0.000	0.000	0.000
136	A	137	GLU	-1	-0.850	-0.904	9.498	-0.740	-0.740	0.000	0.000	0.000	0.000
137	A	138	THR	0	-0.007	-0.037	7.162	0.156	0.156	0.000	0.000	0.000	0.000
138	A	139	LEU	0	-0.011	0.001	4.469	-0.769	-0.608	-0.001	-0.036	-0.124	0.000
139	A	140	VAL	0	-0.036	-0.004	2.365	0.369	1.634	1.626	-0.835	-2.057	-0.005
140	A	141	LYS	1	0.832	0.907	1.913	-6.104	-7.204	7.422	-3.455	-2.866	-0.038
141	A	142	GLU	-1	-0.865	-0.937	2.541	-9.095	-6.889	0.596	-0.839	-1.962	-0.009
142	A	143	LYS	1	0.939	0.961	2.708	-14.410	-9.617	3.109	-2.242	-5.660	0.013
143	A	144	ASP	-1	-0.918	-0.971	3.614	-0.470	-0.617	0.133	0.461	-0.446	0.002
144	A	145	GLU	-1	-0.787	-0.883	5.102	-5.300	-5.300	0.000	0.000	0.000	0.000
145	A	146	ILE	0	-0.042	-0.011	3.007	-1.676	-0.043	0.743	-0.488	-1.887	0.007
146	A	147	PRO	0	0.002	-0.005	5.759	0.078	0.078	0.000	0.000	0.000	0.000
147	A	148	GLU	-1	-0.889	-0.935	9.582	-1.431	-1.431	0.000	0.000	0.000	0.000
148	A	149	ALA	0	-0.010	-0.005	6.815	0.134	0.134	0.000	0.000	0.000	0.000
149	A	150	VAL	0	-0.005	-0.008	7.602	0.197	0.197	0.000	0.000	0.000	0.000
150	A	151	GLU	-1	-0.922	-0.960	10.103	-0.432	-0.432	0.000	0.000	0.000	0.000
151	A	152	LYS	1	0.776	0.875	11.813	1.268	1.268	0.000	0.000	0.000	0.000
152	A	153	LEU	0	0.005	-0.011	9.315	0.131	0.131	0.000	0.000	0.000	0.000
153	A	154	GLU	-1	-0.823	-0.895	13.265	-0.240	-0.240	0.000	0.000	0.000	0.000
154	A	155	LYS	1	0.875	0.932	15.289	0.534	0.534	0.000	0.000	0.000	0.000
155	A	156	ILE	0	-0.005	0.001	14.778	0.070	0.070	0.000	0.000	0.000	0.000
156	A	157	LEU	0	0.034	0.012	15.354	0.068	0.068	0.000	0.000	0.000	0.000
157	A	158	ARG	1	0.754	0.858	18.680	0.343	0.343	0.000	0.000	0.000	0.000
158	A	159	GLU	-1	-0.886	-0.930	21.174	-0.324	-0.324	0.000	0.000	0.000	0.000
159	A	160	LEU	0	-0.036	0.001	20.123	0.034	0.034	0.000	0.000	0.000	0.000
160	A	161	GLY	0	0.024	0.006	22.939	0.032	0.032	0.000	0.000	0.000	0.000
161	A	162	VAL	0	-0.023	-0.002	18.962	0.031	0.031	0.000	0.000	0.000	0.000
162	A	163	GLU	-1	-0.930	-0.956	21.633	-0.141	-0.141	0.000	0.000	0.000	0.000
163	A	164	LYS	1	0.879	0.947	21.863	0.077	0.077	0.000	0.000	0.000	0.000
164	A	165	PHE	0	0.061	0.011	15.212	0.005	0.005	0.000	0.000	0.000	0.000
165	A	166	GLU	-1	-0.793	-0.853	16.455	0.083	0.083	0.000	0.000	0.000	0.000
166	A	167	ARG	1	0.873	0.922	11.152	-0.325	-0.325	0.000	0.000	0.000	0.000
167	A	168	ARG	1	0.741	0.850	13.915	-0.023	-0.023	0.000	0.000	0.000	0.000
168	A	169	SER	0	0.031	-0.033	14.369	-0.070	-0.070	0.000	0.000	0.000	0.000
169	A	170	TYR	0	-0.007	-0.056	15.988	0.033	0.033	0.000	0.000	0.000	0.000
170	A	171	LEU	0	0.020	0.021	17.579	0.000	0.000	0.000	0.000	0.000	0.000
171	A	172	GLU	-1	-0.805	-0.876	15.416	0.312	0.312	0.000	0.000	0.000	0.000
172	A	173	LEU	0	0.004	0.011	19.285	-0.006	-0.006	0.000	0.000	0.000	0.000
173	A	174	LEU	0	0.027	0.015	21.971	-0.011	-0.011	0.000	0.000	0.000	0.000
174	A	175	LEU	0	-0.020	-0.010	21.198	-0.002	-0.002	0.000	0.000	0.000	0.000
175	A	176	GLU	-1	-0.869	-0.924	22.750	0.116	0.116	0.000	0.000	0.000	0.000
176	A	177	LYS	1	0.815	0.918	25.033	-0.081	-0.081	0.000	0.000	0.000	0.000
177	A	178	ARG	1	0.909	0.979	27.628	-0.135	-0.135	0.000	0.000	0.000	0.000

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Support

Interactive mode: IFIE and PIEDA for fragment #1(A:2:TYR)