FMO DATABASE

FMODB ID: R98J8

Calculation Name: 2RF4-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2RF4

Chain ID: A

ChEMBL ID:

UniProt ID: P50106

Base Structure: X-ray

Registration Date: 2023-06-22

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	OptHSide
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	175
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1610941.058559
FMO2-HF: Nuclear repulsion	1543043.028649
FMO2-HF: Total energy	-67898.02991
FMO2-MP2: Total energy	-68097.601911

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:22:LYS)

Summations of interaction energy for fragment #1(A:22: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.
-29.364	-22.405	-0.078	-3.732	-3.146	-0.006

Interaction energy analysis for fragmet #1(A:22:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.964 / q_NPA : 0.968

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	24	VAL	0	0.053	0.100	3.782	-5.303	1.221	-0.073	-3.686	-2.765	-0.006
4	A	25	THR	0	-0.023	-0.055	6.707	-0.660	-0.660	0.000	0.000	0.000	0.000
5	A	26	ASN	0	-0.028	-0.041	8.713	0.123	0.123	0.000	0.000	0.000	0.000
6	A	27	PRO	0	-0.014	0.001	11.212	0.714	0.714	0.000	0.000	0.000	0.000
7	A	28	ILE	0	0.033	-0.006	14.676	0.369	0.369	0.000	0.000	0.000	0.000
8	A	29	ASP	-1	-0.981	-0.998	16.954	-14.414	-14.414	0.000	0.000	0.000	0.000
9	A	30	GLU	-1	-0.854	-0.914	20.341	-11.229	-11.229	0.000	0.000	0.000	0.000
10	A	31	LYS	1	0.905	0.952	23.949	10.077	10.077	0.000	0.000	0.000	0.000
11	A	32	ASN	0	0.029	0.001	22.559	0.646	0.646	0.000	0.000	0.000	0.000
12	A	33	GLY	0	-0.044	-0.017	21.577	-0.017	-0.017	0.000	0.000	0.000	0.000
13	A	34	THR	0	-0.018	-0.017	17.744	-0.184	-0.184	0.000	0.000	0.000	0.000
14	A	35	SER	0	-0.021	-0.052	12.933	0.427	0.427	0.000	0.000	0.000	0.000
15	A	36	ASN	0	0.022	0.033	14.251	-0.609	-0.609	0.000	0.000	0.000	0.000
16	A	37	CYS	0	-0.009	-0.004	11.363	-1.246	-1.246	0.000	0.000	0.000	0.000
17	A	38	ILE	0	-0.055	-0.012	11.159	-1.473	-1.473	0.000	0.000	0.000	0.000
18	A	39	VAL	0	0.011	0.020	8.927	0.742	0.742	0.000	0.000	0.000	0.000
19	A	40	ARG	1	0.841	0.916	12.438	17.474	17.474	0.000	0.000	0.000	0.000
20	A	41	VAL	0	0.003	-0.023	8.632	-1.013	-1.013	0.000	0.000	0.000	0.000
21	A	42	PRO	0	-0.018	-0.003	12.065	0.685	0.685	0.000	0.000	0.000	0.000
22	A	43	ILE	0	-0.025	-0.012	9.783	-2.383	-2.383	0.000	0.000	0.000	0.000
23	A	44	ALA	0	0.044	0.033	12.387	1.809	1.809	0.000	0.000	0.000	0.000
24	A	45	LEU	0	-0.068	-0.049	13.233	-1.526	-1.526	0.000	0.000	0.000	0.000
25	A	46	TYR	0	0.022	0.016	15.184	1.261	1.261	0.000	0.000	0.000	0.000
26	A	47	VAL	0	-0.017	-0.019	17.507	-0.449	-0.449	0.000	0.000	0.000	0.000
27	A	48	SER	0	0.016	-0.002	19.636	0.652	0.652	0.000	0.000	0.000	0.000
28	A	49	LEU	0	-0.044	-0.004	22.485	0.066	0.066	0.000	0.000	0.000	0.000
29	A	50	ALA	0	0.020	0.017	25.260	0.224	0.224	0.000	0.000	0.000	0.000
30	A	51	PRO	0	0.054	0.006	28.202	0.068	0.068	0.000	0.000	0.000	0.000
31	A	52	MET	0	-0.017	-0.020	31.638	0.141	0.141	0.000	0.000	0.000	0.000
32	A	53	TYR	0	0.002	-0.007	27.823	0.104	0.104	0.000	0.000	0.000	0.000
33	A	54	LEU	0	0.090	0.055	30.017	-0.273	-0.273	0.000	0.000	0.000	0.000
34	A	55	GLU	-1	-0.976	-0.976	31.956	-8.278	-8.278	0.000	0.000	0.000	0.000
35	A	56	ASN	0	-0.019	-0.025	31.186	-0.188	-0.188	0.000	0.000	0.000	0.000
36	A	57	PRO	0	0.081	0.035	26.315	-0.166	-0.166	0.000	0.000	0.000	0.000
37	A	58	LEU	0	-0.015	0.013	25.570	-0.534	-0.534	0.000	0.000	0.000	0.000
38	A	59	GLN	0	0.051	-0.002	25.742	-0.462	-0.462	0.000	0.000	0.000	0.000
39	A	60	GLY	0	-0.004	0.000	26.682	-0.038	-0.038	0.000	0.000	0.000	0.000
40	A	61	VAL	0	0.027	0.001	20.402	-0.316	-0.316	0.000	0.000	0.000	0.000
41	A	62	MET	0	0.042	0.025	21.573	-0.532	-0.532	0.000	0.000	0.000	0.000
42	A	63	LYS	1	0.846	0.935	23.616	10.676	10.676	0.000	0.000	0.000	0.000
43	A	64	GLN	0	-0.036	-0.018	18.549	0.388	0.388	0.000	0.000	0.000	0.000
44	A	65	HIS	0	0.014	-0.007	15.910	-1.000	-1.000	0.000	0.000	0.000	0.000
45	A	66	LEU	0	0.008	0.009	19.375	-0.382	-0.382	0.000	0.000	0.000	0.000
46	A	67	ASN	0	0.053	0.043	20.340	-0.762	-0.762	0.000	0.000	0.000	0.000
47	A	68	PRO	0	-0.071	-0.023	19.323	-0.381	-0.381	0.000	0.000	0.000	0.000
48	A	69	LEU	0	0.010	0.002	14.062	-0.696	-0.696	0.000	0.000	0.000	0.000
49	A	70	VAL	0	0.042	0.028	16.013	-0.480	-0.480	0.000	0.000	0.000	0.000
50	A	71	MET	0	-0.028	-0.020	16.620	0.257	0.257	0.000	0.000	0.000	0.000
51	A	72	LYS	1	0.795	0.902	15.352	15.156	15.156	0.000	0.000	0.000	0.000
52	A	73	TYR	0	0.013	0.010	5.363	-0.803	-0.803	0.000	0.000	0.000	0.000
53	A	74	ASN	0	0.004	0.002	9.572	-1.777	-1.777	0.000	0.000	0.000	0.000
54	A	75	ASN	0	0.066	0.012	6.762	-1.480	-1.480	0.000	0.000	0.000	0.000
55	A	76	LYS	1	0.918	0.971	5.194	23.148	23.238	-0.001	0.000	-0.089	0.000
56	A	77	VAL	0	-0.012	-0.006	4.878	-7.657	-7.589	-0.001	-0.004	-0.063	0.000
57	A	78	GLY	0	-0.005	-0.003	3.847	0.657	0.782	-0.001	-0.022	-0.102	0.000
58	A	79	GLY	0	0.050	0.006	4.929	-0.270	-0.272	-0.001	-0.002	0.007	0.000
59	A	80	VAL	0	-0.057	-0.024	7.863	0.753	0.753	0.000	0.000	0.000	0.000
60	A	81	VAL	0	0.017	0.023	11.615	-0.504	-0.504	0.000	0.000	0.000	0.000
61	A	82	LEU	0	0.005	-0.006	13.629	1.332	1.332	0.000	0.000	0.000	0.000
62	A	83	GLY	0	0.016	0.008	16.508	1.141	1.141	0.000	0.000	0.000	0.000
63	A	84	TYR	0	-0.023	-0.016	17.346	-0.840	-0.840	0.000	0.000	0.000	0.000
64	A	85	GLU	-1	-0.781	-0.862	18.853	-14.236	-14.236	0.000	0.000	0.000	0.000
65	A	86	GLY	0	0.022	-0.005	19.923	-0.631	-0.631	0.000	0.000	0.000	0.000
66	A	87	LEU	0	-0.055	-0.017	19.794	-0.205	-0.205	0.000	0.000	0.000	0.000
67	A	88	LYS	1	0.859	0.919	21.188	14.806	14.806	0.000	0.000	0.000	0.000
68	A	89	ILE	0	0.024	-0.011	21.940	-0.515	-0.515	0.000	0.000	0.000	0.000
69	A	90	LEU	0	0.028	0.004	23.978	-0.121	-0.121	0.000	0.000	0.000	0.000
70	A	91	ASP	-1	-0.860	-0.871	21.123	-14.602	-14.602	0.000	0.000	0.000	0.000
71	A	92	ALA	0	-0.018	-0.052	23.089	-0.354	-0.354	0.000	0.000	0.000	0.000
72	A	93	ASP	-1	-0.925	-0.969	25.890	-9.942	-9.942	0.000	0.000	0.000	0.000
73	A	94	PRO	0	-0.041	0.012	29.412	-0.015	-0.015	0.000	0.000	0.000	0.000
74	A	112	PRO	0	0.013	-0.021	33.865	0.071	0.071	0.000	0.000	0.000	0.000
75	A	113	PHE	0	-0.051	-0.048	29.355	-0.096	-0.096	0.000	0.000	0.000	0.000
76	A	114	GLY	0	0.016	0.033	27.808	-0.208	-0.208	0.000	0.000	0.000	0.000
77	A	115	PHE	0	-0.012	0.010	21.828	-0.191	-0.191	0.000	0.000	0.000	0.000
78	A	116	THR	0	0.042	0.014	22.442	0.628	0.628	0.000	0.000	0.000	0.000
79	A	117	TRP	0	-0.002	0.016	14.941	-1.067	-1.067	0.000	0.000	0.000	0.000
80	A	118	CYS	0	-0.071	-0.010	18.772	0.546	0.546	0.000	0.000	0.000	0.000
81	A	119	HIS	0	0.061	0.025	15.230	-1.264	-1.264	0.000	0.000	0.000	0.000
82	A	120	VAL	0	-0.022	-0.008	15.865	1.067	1.067	0.000	0.000	0.000	0.000
83	A	121	ASN	0	0.000	-0.004	15.291	-1.822	-1.822	0.000	0.000	0.000	0.000
84	A	122	LEU	0	0.003	0.011	11.776	1.285	1.285	0.000	0.000	0.000	0.000
85	A	123	TYR	0	0.000	-0.019	14.395	-0.893	-0.893	0.000	0.000	0.000	0.000
86	A	124	VAL	0	-0.056	-0.041	8.599	0.381	0.381	0.000	0.000	0.000	0.000
87	A	125	TRP	0	0.045	0.045	11.221	-0.546	-0.546	0.000	0.000	0.000	0.000
88	A	126	GLN	0	0.011	-0.013	5.948	-4.094	-4.094	0.000	0.000	0.000	0.000
89	A	127	PRO	0	0.013	0.031	8.085	-0.827	-0.827	0.000	0.000	0.000	0.000
90	A	128	GLN	0	-0.016	-0.032	4.322	-0.311	-0.157	-0.001	-0.018	-0.134	0.000
91	A	129	VAL	0	-0.008	-0.026	6.605	2.282	2.282	0.000	0.000	0.000	0.000
92	A	130	GLY	0	-0.020	-0.006	8.637	-0.800	-0.800	0.000	0.000	0.000	0.000
93	A	131	ASP	-1	-0.727	-0.802	9.706	-21.691	-21.691	0.000	0.000	0.000	0.000
94	A	132	VAL	0	0.005	0.006	12.302	0.821	0.821	0.000	0.000	0.000	0.000
95	A	133	LEU	0	-0.007	0.001	12.661	-0.042	-0.042	0.000	0.000	0.000	0.000
96	A	134	GLU	-1	-0.787	-0.895	16.848	-11.094	-11.094	0.000	0.000	0.000	0.000
97	A	135	GLY	0	-0.044	-0.027	19.933	-0.458	-0.458	0.000	0.000	0.000	0.000
98	A	136	TYR	0	0.036	0.026	21.757	0.352	0.352	0.000	0.000	0.000	0.000
99	A	137	ILE	0	0.014	0.012	24.374	-0.382	-0.382	0.000	0.000	0.000	0.000
100	A	138	PHE	0	-0.036	-0.012	24.264	0.205	0.205	0.000	0.000	0.000	0.000
101	A	139	ILE	0	-0.010	-0.015	25.083	0.327	0.327	0.000	0.000	0.000	0.000
102	A	140	GLN	0	-0.025	0.000	27.188	-0.168	-0.168	0.000	0.000	0.000	0.000
103	A	141	SER	0	0.014	0.002	28.723	0.223	0.223	0.000	0.000	0.000	0.000
104	A	142	ALA	0	-0.023	0.004	29.393	-0.194	-0.194	0.000	0.000	0.000	0.000
105	A	143	SER	0	-0.118	-0.067	28.220	-0.113	-0.113	0.000	0.000	0.000	0.000
106	A	144	HIS	0	-0.029	-0.024	22.110	-0.428	-0.428	0.000	0.000	0.000	0.000
107	A	145	ILE	0	0.056	0.048	24.665	0.206	0.206	0.000	0.000	0.000	0.000
108	A	146	GLY	0	0.029	0.014	22.752	-0.466	-0.466	0.000	0.000	0.000	0.000
109	A	147	LEU	0	-0.034	-0.027	20.525	0.301	0.301	0.000	0.000	0.000	0.000
110	A	148	LEU	0	0.010	0.026	20.899	-0.459	-0.459	0.000	0.000	0.000	0.000
111	A	149	ILE	0	-0.010	-0.011	15.500	0.197	0.197	0.000	0.000	0.000	0.000
112	A	150	HIS	0	-0.027	-0.024	17.023	0.264	0.264	0.000	0.000	0.000	0.000
113	A	151	ASP	-1	-0.939	-0.973	21.016	-10.742	-10.742	0.000	0.000	0.000	0.000
114	A	152	ALA	0	-0.008	0.006	20.070	0.195	0.195	0.000	0.000	0.000	0.000
115	A	153	PHE	0	-0.035	-0.018	15.856	-0.562	-0.562	0.000	0.000	0.000	0.000
116	A	154	ASN	0	0.017	0.001	17.797	0.144	0.144	0.000	0.000	0.000	0.000
117	A	155	ALA	0	0.031	0.030	16.751	-0.808	-0.808	0.000	0.000	0.000	0.000
118	A	156	SER	0	0.004	0.016	17.951	0.729	0.729	0.000	0.000	0.000	0.000
119	A	157	ILE	0	0.034	0.031	18.662	-0.552	-0.552	0.000	0.000	0.000	0.000
120	A	158	LYS	1	0.853	0.895	18.094	13.633	13.633	0.000	0.000	0.000	0.000
121	A	159	LYS	1	1.024	1.005	22.607	8.855	8.855	0.000	0.000	0.000	0.000
122	A	160	ASN	0	-0.042	-0.031	23.078	0.039	0.039	0.000	0.000	0.000	0.000
123	A	161	ASN	0	0.008	0.011	19.537	-0.091	-0.091	0.000	0.000	0.000	0.000
124	A	162	ILE	0	0.010	0.034	23.007	-0.174	-0.174	0.000	0.000	0.000	0.000
125	A	163	PRO	0	0.011	0.002	25.961	0.076	0.076	0.000	0.000	0.000	0.000
126	A	164	VAL	0	-0.037	-0.002	28.394	0.096	0.096	0.000	0.000	0.000	0.000
127	A	165	ASP	-1	-0.811	-0.888	30.984	-8.356	-8.356	0.000	0.000	0.000	0.000
128	A	166	TRP	0	-0.010	0.000	27.250	0.041	0.041	0.000	0.000	0.000	0.000
129	A	167	THR	0	-0.025	-0.018	32.868	0.038	0.038	0.000	0.000	0.000	0.000
130	A	168	PHE	0	-0.004	-0.013	32.330	-0.066	-0.066	0.000	0.000	0.000	0.000
131	A	169	VAL	0	0.035	0.032	35.131	0.115	0.115	0.000	0.000	0.000	0.000
132	A	170	HIS	0	0.029	-0.006	37.125	-0.141	-0.141	0.000	0.000	0.000	0.000
133	A	171	ASN	0	0.032	-0.015	39.445	0.046	0.046	0.000	0.000	0.000	0.000
134	A	172	ASP	-1	-0.849	-0.893	41.809	-6.488	-6.488	0.000	0.000	0.000	0.000
135	A	210	GLY	0	-0.078	-0.047	40.735	-0.017	-0.017	0.000	0.000	0.000	0.000
136	A	211	ASN	0	0.024	0.025	40.965	0.001	0.001	0.000	0.000	0.000	0.000
137	A	212	ARG	1	0.918	0.945	40.863	6.477	6.477	0.000	0.000	0.000	0.000
138	A	213	SER	0	-0.053	-0.053	37.123	0.074	0.074	0.000	0.000	0.000	0.000
139	A	214	LEU	0	0.030	0.027	37.083	-0.180	-0.180	0.000	0.000	0.000	0.000
140	A	215	GLY	0	-0.028	-0.012	35.983	0.081	0.081	0.000	0.000	0.000	0.000
141	A	216	HIS	0	-0.039	-0.029	33.779	-0.174	-0.174	0.000	0.000	0.000	0.000
142	A	217	TRP	0	-0.048	-0.033	28.597	-0.218	-0.218	0.000	0.000	0.000	0.000
143	A	218	VAL	0	0.088	0.078	32.772	-0.186	-0.186	0.000	0.000	0.000	0.000
144	A	219	ASP	-1	-0.822	-0.905	32.900	-8.039	-8.039	0.000	0.000	0.000	0.000
145	A	220	SER	0	-0.014	-0.029	34.143	0.222	0.222	0.000	0.000	0.000	0.000
146	A	221	ASN	0	-0.142	-0.076	35.890	0.337	0.337	0.000	0.000	0.000	0.000
147	A	222	GLY	0	-0.018	-0.016	37.189	0.198	0.198	0.000	0.000	0.000	0.000
148	A	223	GLU	-1	-0.894	-0.936	35.794	-7.231	-7.231	0.000	0.000	0.000	0.000
149	A	224	PRO	0	-0.067	-0.058	35.234	-0.190	-0.190	0.000	0.000	0.000	0.000
150	A	225	ILE	0	-0.082	-0.037	29.531	-0.146	-0.146	0.000	0.000	0.000	0.000
151	A	226	ASP	-1	-0.854	-0.937	29.694	-9.296	-9.296	0.000	0.000	0.000	0.000
152	A	227	GLY	0	0.075	0.042	29.377	0.212	0.212	0.000	0.000	0.000	0.000
153	A	228	LYS	1	0.775	0.883	23.514	11.105	11.105	0.000	0.000	0.000	0.000
154	A	229	LEU	0	0.019	0.005	23.651	0.092	0.092	0.000	0.000	0.000	0.000
155	A	230	ARG	1	0.886	0.958	20.747	11.635	11.635	0.000	0.000	0.000	0.000
156	A	231	PHE	0	-0.014	-0.014	15.515	0.120	0.120	0.000	0.000	0.000	0.000
157	A	232	THR	0	0.022	0.013	15.572	-0.319	-0.319	0.000	0.000	0.000	0.000
158	A	233	VAL	0	-0.028	-0.025	10.114	0.452	0.452	0.000	0.000	0.000	0.000
159	A	234	ARG	1	0.931	0.972	12.645	13.348	13.348	0.000	0.000	0.000	0.000
160	A	235	ASN	0	-0.031	-0.040	9.881	-0.958	-0.958	0.000	0.000	0.000	0.000
161	A	236	VAL	0	-0.007	0.014	7.634	0.977	0.977	0.000	0.000	0.000	0.000
162	A	237	HIS	0	-0.016	-0.016	9.024	-1.647	-1.647	0.000	0.000	0.000	0.000
163	A	238	THR	0	-0.003	-0.002	8.123	1.115	1.115	0.000	0.000	0.000	0.000
164	A	239	THR	0	-0.002	-0.018	11.038	0.245	0.245	0.000	0.000	0.000	0.000
165	A	240	GLY	0	0.002	0.017	14.390	0.896	0.896	0.000	0.000	0.000	0.000
166	A	241	ARG	1	0.877	0.942	16.850	12.699	12.699	0.000	0.000	0.000	0.000
167	A	242	VAL	0	0.030	0.009	16.040	-0.722	-0.722	0.000	0.000	0.000	0.000
168	A	243	VAL	0	0.010	0.026	10.601	0.013	0.013	0.000	0.000	0.000	0.000
169	A	244	SER	0	-0.045	-0.026	13.482	0.975	0.975	0.000	0.000	0.000	0.000
170	A	245	VAL	0	0.006	-0.001	12.082	-0.899	-0.899	0.000	0.000	0.000	0.000
171	A	246	ASP	-1	-0.796	-0.880	13.320	-13.109	-13.109	0.000	0.000	0.000	0.000
172	A	247	GLY	0	0.012	-0.002	14.528	-0.670	-0.670	0.000	0.000	0.000	0.000
173	A	248	THR	0	-0.081	-0.065	16.633	0.708	0.708	0.000	0.000	0.000	0.000
174	A	249	LEU	0	0.031	0.020	19.244	-0.328	-0.328	0.000	0.000	0.000	0.000
175	A	250	ILE	0	-0.012	0.005	19.928	0.464	0.464	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:22:LYS)