FMO DATABASE

FMODB ID: N914Q

Calculation Name: 3TC2-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3TC2

Chain ID: A

ChEMBL ID:

UniProt ID: Q8S380

Base Structure: X-ray

Registration Date: 2023-06-21

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	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	184
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1953847.869666
FMO2-HF: Nuclear repulsion	1882832.53705
FMO2-HF: Total energy	-71015.332616
FMO2-MP2: Total energy	-71222.334873

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:PRO)

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

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.
0.853	3.25	-0.036	-0.954	-1.406	0

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.043 / q_NPA : -0.044

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].
3	A	4	ASP	-1	-0.943	-0.968	3.782	-2.022	-0.045	-0.033	-0.922	-1.022
4	A	5	ALA	0	-0.009	-0.003	7.215	0.225	0.225	0.000	0.000	0.000
5	A	6	THR	0	0.017	0.013	8.467	-0.010	-0.010	0.000	0.000	0.000
6	A	7	PRO	0	0.000	0.011	10.598	0.090	0.090	0.000	0.000	0.000
7	A	8	VAL	0	-0.031	-0.017	12.775	0.014	0.014	0.000	0.000	0.000
8	A	9	LEU	0	0.018	0.020	14.797	-0.030	-0.030	0.000	0.000	0.000
9	A	10	ASP	-1	-0.795	-0.888	18.387	0.087	0.087	0.000	0.000	0.000
10	A	11	VAL	0	-0.053	-0.050	21.693	-0.005	-0.005	0.000	0.000	0.000
11	A	12	THR	0	-0.146	-0.091	24.571	-0.008	-0.008	0.000	0.000	0.000
12	A	13	GLY	0	0.011	0.017	21.978	-0.008	-0.008	0.000	0.000	0.000
13	A	14	LYS	1	0.812	0.905	21.659	-0.068	-0.068	0.000	0.000	0.000
14	A	15	GLU	-1	-0.860	-0.940	16.941	0.025	0.025	0.000	0.000	0.000
15	A	16	LEU	0	-0.093	-0.052	16.684	-0.006	-0.006	0.000	0.000	0.000
16	A	17	ASP	-1	-0.761	-0.873	17.813	0.051	0.051	0.000	0.000	0.000
17	A	18	PRO	0	0.001	0.002	17.540	0.005	0.005	0.000	0.000	0.000
18	A	19	ARG	1	0.734	0.851	19.564	-0.043	-0.043	0.000	0.000	0.000
19	A	20	LEU	0	-0.052	-0.007	22.804	-0.006	-0.006	0.000	0.000	0.000
20	A	21	SER	0	-0.051	-0.028	23.437	0.008	0.008	0.000	0.000	0.000
21	A	22	TYR	0	0.045	0.017	21.815	-0.008	-0.008	0.000	0.000	0.000
22	A	23	ARG	1	0.851	0.933	24.818	-0.068	-0.068	0.000	0.000	0.000
23	A	24	ILE	0	0.050	0.035	21.807	0.001	0.001	0.000	0.000	0.000
24	A	25	ILE	0	-0.015	-0.012	24.355	-0.007	-0.007	0.000	0.000	0.000
25	A	26	SER	0	0.000	-0.008	25.065	0.009	0.009	0.000	0.000	0.000
26	A	27	THR	0	-0.059	-0.040	25.361	0.003	0.003	0.000	0.000	0.000
27	A	28	PHE	0	0.048	0.049	27.882	0.000	0.000	0.000	0.000	0.000
28	A	29	TRP	0	0.020	0.007	30.674	0.003	0.003	0.000	0.000	0.000
29	A	30	GLY	0	0.018	0.004	34.026	0.000	0.000	0.000	0.000	0.000
30	A	31	ALA	0	-0.011	-0.032	35.709	0.003	0.003	0.000	0.000	0.000
31	A	32	LEU	0	0.059	0.051	31.831	0.003	0.003	0.000	0.000	0.000
32	A	33	GLY	0	0.047	0.034	31.090	0.009	0.009	0.000	0.000	0.000
33	A	34	GLY	0	0.000	0.003	31.340	-0.002	-0.002	0.000	0.000	0.000
34	A	35	ASP	-1	-0.812	-0.911	28.612	0.095	0.095	0.000	0.000	0.000
35	A	36	VAL	0	0.033	0.006	24.416	-0.005	-0.005	0.000	0.000	0.000
36	A	37	TYR	0	-0.075	-0.044	27.787	-0.009	-0.009	0.000	0.000	0.000
37	A	38	LEU	0	0.010	0.028	29.394	0.004	0.004	0.000	0.000	0.000
38	A	39	GLY	0	-0.024	-0.021	30.968	-0.007	-0.007	0.000	0.000	0.000
39	A	40	LYS	1	0.950	0.959	33.046	-0.053	-0.053	0.000	0.000	0.000
40	A	41	SER	0	0.024	0.013	32.229	0.003	0.003	0.000	0.000	0.000
41	A	42	PRO	0	-0.046	-0.026	34.406	-0.004	-0.004	0.000	0.000	0.000
42	A	43	ASN	0	-0.046	-0.027	37.219	0.001	0.001	0.000	0.000	0.000
43	A	44	SER	0	0.029	0.029	34.394	0.001	0.001	0.000	0.000	0.000
44	A	45	ASP	-1	-0.884	-0.942	36.087	0.060	0.060	0.000	0.000	0.000
45	A	46	ALA	0	-0.025	0.000	33.902	-0.001	-0.001	0.000	0.000	0.000
46	A	47	PRO	0	-0.020	-0.011	35.282	-0.002	-0.002	0.000	0.000	0.000
47	A	48	CYS	0	-0.064	-0.019	34.100	-0.002	-0.002	0.000	0.000	0.000
48	A	49	ALA	0	-0.046	-0.031	33.852	0.002	0.002	0.000	0.000	0.000
49	A	50	ASN	0	0.110	0.060	30.576	-0.002	-0.002	0.000	0.000	0.000
50	A	51	GLY	0	0.022	0.034	29.441	0.006	0.006	0.000	0.000	0.000
51	A	52	VAL	0	0.028	0.024	24.370	-0.006	-0.006	0.000	0.000	0.000
52	A	53	PHE	0	-0.001	0.004	27.670	0.003	0.003	0.000	0.000	0.000
53	A	54	ARG	1	0.881	0.947	27.161	-0.107	-0.107	0.000	0.000	0.000
54	A	55	TYR	0	-0.035	-0.015	29.981	-0.004	-0.004	0.000	0.000	0.000
55	A	56	ASN	0	0.004	-0.025	32.727	0.008	0.008	0.000	0.000	0.000
56	A	57	SER	0	-0.007	-0.009	35.226	-0.003	-0.003	0.000	0.000	0.000
57	A	58	ASP	-1	-0.894	-0.943	33.848	0.065	0.065	0.000	0.000	0.000
58	A	59	VAL	0	0.016	0.028	35.506	-0.003	-0.003	0.000	0.000	0.000
59	A	60	GLY	0	0.010	-0.010	38.144	-0.001	-0.001	0.000	0.000	0.000
60	A	61	PRO	0	-0.061	-0.020	36.619	-0.001	-0.001	0.000	0.000	0.000
61	A	62	SER	0	0.018	0.011	32.700	0.002	0.002	0.000	0.000	0.000
62	A	63	GLY	0	-0.019	-0.014	30.183	-0.002	-0.002	0.000	0.000	0.000
63	A	64	THR	0	-0.034	-0.012	29.311	-0.006	-0.006	0.000	0.000	0.000
64	A	65	PRO	0	-0.027	-0.014	27.465	0.007	0.007	0.000	0.000	0.000
65	A	66	VAL	0	0.005	0.017	22.046	-0.003	-0.003	0.000	0.000	0.000
66	A	67	ARG	1	0.957	0.971	22.172	-0.094	-0.094	0.000	0.000	0.000
67	A	68	PHE	0	0.033	0.008	16.680	0.008	0.008	0.000	0.000	0.000
68	A	69	ILE	0	-0.010	-0.010	17.841	-0.019	-0.019	0.000	0.000	0.000
69	A	70	GLY	0	0.072	0.037	13.804	0.024	0.024	0.000	0.000	0.000
70	A	71	SER	0	0.015	0.004	11.051	-0.029	-0.029	0.000	0.000	0.000
71	A	72	SER	0	-0.020	-0.027	13.490	-0.008	-0.008	0.000	0.000	0.000
72	A	73	SER	0	-0.007	0.017	8.142	-0.040	-0.040	0.000	0.000	0.000
73	A	74	HIS	0	-0.013	0.010	8.590	-0.039	-0.039	0.000	0.000	0.000
74	A	75	PHE	0	-0.022	-0.007	10.700	-0.031	-0.031	0.000	0.000	0.000
75	A	76	GLY	0	0.060	0.014	12.355	0.011	0.011	0.000	0.000	0.000
76	A	77	GLN	0	-0.060	-0.033	13.257	-0.006	-0.006	0.000	0.000	0.000
77	A	78	GLY	0	0.063	0.023	15.229	0.005	0.005	0.000	0.000	0.000
78	A	79	ILE	0	-0.036	-0.010	13.418	0.007	0.007	0.000	0.000	0.000
79	A	80	PHE	0	-0.021	-0.020	9.125	-0.039	-0.039	0.000	0.000	0.000
80	A	81	GLU	-1	-0.847	-0.952	9.236	0.475	0.475	0.000	0.000	0.000
81	A	82	ASP	-1	-0.858	-0.927	5.037	3.033	3.164	-0.001	-0.001	-0.128
82	A	83	GLU	-1	-0.830	-0.899	6.143	0.455	0.455	0.000	0.000	0.000
83	A	84	LEU	0	-0.015	-0.009	7.923	-0.069	-0.069	0.000	0.000	0.000
84	A	85	LEU	0	-0.015	-0.021	10.322	-0.086	-0.086	0.000	0.000	0.000
85	A	86	ASN	0	0.050	0.029	14.012	-0.005	-0.005	0.000	0.000	0.000
86	A	87	ILE	0	0.006	0.011	17.327	-0.007	-0.007	0.000	0.000	0.000
87	A	88	GLN	0	0.025	0.014	20.072	-0.009	-0.009	0.000	0.000	0.000
88	A	89	PHE	0	0.009	-0.004	23.633	-0.002	-0.002	0.000	0.000	0.000
89	A	90	ALA	0	-0.042	-0.018	25.992	-0.006	-0.006	0.000	0.000	0.000
90	A	91	ILE	0	-0.035	-0.038	27.856	-0.005	-0.005	0.000	0.000	0.000
91	A	92	SER	0	0.009	0.007	31.546	0.000	0.000	0.000	0.000	0.000
92	A	93	THR	0	0.013	0.004	33.011	0.002	0.002	0.000	0.000	0.000
93	A	94	SER	0	0.020	0.010	35.705	-0.002	-0.002	0.000	0.000	0.000
94	A	95	LYS	1	1.022	0.991	35.908	-0.036	-0.036	0.000	0.000	0.000
95	A	96	MET	0	-0.002	-0.017	35.143	0.002	0.002	0.000	0.000	0.000
96	A	98	VAL	0	0.059	0.047	29.724	0.004	0.004	0.000	0.000	0.000
97	A	99	SER	0	0.076	0.033	28.418	0.004	0.004	0.000	0.000	0.000
98	A	100	TYR	0	0.016	0.012	27.771	0.006	0.006	0.000	0.000	0.000
99	A	101	THR	0	-0.047	-0.006	28.100	0.002	0.002	0.000	0.000	0.000
100	A	102	ILE	0	-0.039	-0.014	22.671	0.007	0.007	0.000	0.000	0.000
101	A	103	TRP	0	0.027	0.007	20.631	0.001	0.001	0.000	0.000	0.000
102	A	104	LYS	1	0.897	0.936	21.198	-0.108	-0.108	0.000	0.000	0.000
103	A	105	VAL	0	-0.026	-0.015	19.164	-0.001	-0.001	0.000	0.000	0.000
104	A	106	GLY	0	-0.009	-0.007	22.195	-0.007	-0.007	0.000	0.000	0.000
105	A	107	ASP	-1	-0.904	-0.954	24.672	0.111	0.111	0.000	0.000	0.000
106	A	108	TYR	0	-0.035	-0.022	26.612	0.002	0.002	0.000	0.000	0.000
107	A	109	ASP	-1	-0.806	-0.901	27.623	0.079	0.079	0.000	0.000	0.000
108	A	110	ALA	0	-0.003	-0.020	30.587	0.002	0.002	0.000	0.000	0.000
109	A	111	SER	0	-0.079	-0.052	33.003	-0.004	-0.004	0.000	0.000	0.000
110	A	112	LEU	0	-0.081	-0.053	30.327	-0.001	-0.001	0.000	0.000	0.000
111	A	113	GLY	0	-0.019	0.019	29.648	0.004	0.004	0.000	0.000	0.000
112	A	114	THR	0	-0.047	-0.052	24.080	0.010	0.010	0.000	0.000	0.000
113	A	115	MET	0	0.011	0.034	22.780	-0.009	-0.009	0.000	0.000	0.000
114	A	116	LEU	0	-0.009	-0.001	24.223	0.011	0.011	0.000	0.000	0.000
115	A	117	LEU	0	-0.007	-0.004	20.600	0.003	0.003	0.000	0.000	0.000
116	A	118	GLU	-1	-0.844	-0.925	24.493	0.092	0.092	0.000	0.000	0.000
117	A	119	THR	0	-0.077	-0.059	25.064	0.009	0.009	0.000	0.000	0.000
118	A	120	GLY	0	0.003	-0.009	26.987	-0.005	-0.005	0.000	0.000	0.000
119	A	121	GLY	0	-0.026	0.003	23.564	-0.002	-0.002	0.000	0.000	0.000
120	A	122	THR	0	-0.006	-0.008	22.353	-0.005	-0.005	0.000	0.000	0.000
121	A	123	ILE	0	-0.018	-0.020	19.969	0.013	0.013	0.000	0.000	0.000
122	A	124	GLY	0	0.008	0.001	17.546	-0.012	-0.012	0.000	0.000	0.000
123	A	125	GLN	0	-0.103	-0.062	18.585	-0.018	-0.018	0.000	0.000	0.000
124	A	126	ALA	0	-0.003	-0.011	17.448	0.015	0.015	0.000	0.000	0.000
125	A	127	ASP	-1	-0.830	-0.892	18.531	0.117	0.117	0.000	0.000	0.000
126	A	128	SER	0	-0.048	-0.021	17.894	-0.001	-0.001	0.000	0.000	0.000
127	A	129	SER	0	-0.034	-0.015	17.581	0.010	0.010	0.000	0.000	0.000
128	A	130	TRP	0	0.002	0.025	12.533	-0.007	-0.007	0.000	0.000	0.000
129	A	131	PHE	0	-0.013	-0.027	13.799	0.002	0.002	0.000	0.000	0.000
130	A	132	LYS	1	0.809	0.901	5.491	-1.906	-1.906	0.000	0.000	0.000
131	A	133	ILE	0	-0.036	-0.015	11.536	-0.049	-0.049	0.000	0.000	0.000
132	A	134	VAL	0	0.054	0.030	9.666	0.069	0.069	0.000	0.000	0.000
133	A	135	LYS	1	0.868	0.923	12.103	-0.317	-0.317	0.000	0.000	0.000
134	A	136	SER	0	-0.044	-0.041	14.351	0.033	0.033	0.000	0.000	0.000
135	A	137	SER	0	0.008	-0.001	17.325	-0.008	-0.008	0.000	0.000	0.000
136	A	138	GLN	0	-0.062	-0.017	18.320	-0.025	-0.025	0.000	0.000	0.000
137	A	139	PHE	0	0.001	-0.020	21.500	-0.018	-0.018	0.000	0.000	0.000
138	A	140	GLY	0	-0.019	0.012	20.322	0.008	0.008	0.000	0.000	0.000
139	A	141	TYR	0	0.041	0.018	14.422	0.000	0.000	0.000	0.000	0.000
140	A	142	ASN	0	-0.023	-0.029	15.877	-0.015	-0.015	0.000	0.000	0.000
141	A	143	LEU	0	-0.009	-0.006	15.240	0.034	0.034	0.000	0.000	0.000
142	A	144	LEU	0	0.019	0.013	10.714	-0.031	-0.031	0.000	0.000	0.000
143	A	145	TYR	0	0.044	0.003	13.885	-0.003	-0.003	0.000	0.000	0.000
144	A	146	CYS	0	-0.045	-0.004	9.574	-0.017	-0.017	0.000	0.000	0.000
145	A	147	PRO	0	-0.012	0.008	12.120	-0.037	-0.037	0.000	0.000	0.000
146	A	148	VAL	0	0.022	-0.003	12.825	0.015	0.015	0.000	0.000	0.000
147	A	149	THR	0	-0.005	-0.004	10.001	0.030	0.030	0.000	0.000	0.000
148	A	150	THR	0	0.000	-0.018	4.580	-0.040	0.019	-0.001	-0.007	-0.051
149	A	151	SER	0	-0.014	0.016	5.977	-0.045	-0.045	0.000	0.000	0.000
150	A	152	SER	0	0.021	-0.022	4.115	0.004	0.192	0.000	-0.021	-0.167
151	A	153	ASP	-1	-0.834	-0.895	5.158	1.802	1.844	-0.001	-0.003	-0.038
152	A	154	ASP	-1	-0.884	-0.948	7.170	0.224	0.224	0.000	0.000	0.000
153	A	155	GLN	0	-0.017	-0.004	10.154	-0.142	-0.142	0.000	0.000	0.000
154	A	156	PHE	0	-0.073	-0.017	8.353	-0.140	-0.140	0.000	0.000	0.000
155	A	158	LEU	0	-0.013	-0.009	11.704	-0.025	-0.025	0.000	0.000	0.000
156	A	159	LYS	1	0.911	0.954	14.251	-0.445	-0.445	0.000	0.000	0.000
157	A	160	VAL	0	0.027	0.024	17.141	-0.036	-0.036	0.000	0.000	0.000
158	A	161	GLY	0	0.045	0.007	19.623	0.003	0.003	0.000	0.000	0.000
159	A	162	VAL	0	-0.075	-0.033	22.919	-0.007	-0.007	0.000	0.000	0.000
160	A	163	VAL	0	0.028	0.029	26.625	-0.003	-0.003	0.000	0.000	0.000
161	A	164	HIS	0	-0.005	-0.010	29.254	-0.004	-0.004	0.000	0.000	0.000
162	A	165	GLN	0	0.091	0.040	32.283	-0.001	-0.001	0.000	0.000	0.000
163	A	166	ASN	0	-0.018	-0.019	34.434	-0.001	-0.001	0.000	0.000	0.000
164	A	167	GLY	0	0.038	0.032	37.431	-0.002	-0.002	0.000	0.000	0.000
165	A	168	LYS	1	0.881	0.947	34.128	-0.072	-0.072	0.000	0.000	0.000
166	A	169	ARG	1	0.869	0.929	30.112	-0.085	-0.085	0.000	0.000	0.000
167	A	170	ARG	1	0.856	0.926	28.181	-0.106	-0.106	0.000	0.000	0.000
168	A	171	LEU	0	-0.006	-0.017	22.850	0.004	0.004	0.000	0.000	0.000
169	A	172	ALA	0	0.027	0.017	24.009	-0.009	-0.009	0.000	0.000	0.000
170	A	173	LEU	0	0.018	0.022	18.476	0.014	0.014	0.000	0.000	0.000
171	A	174	VAL	0	-0.035	0.008	20.501	-0.024	-0.024	0.000	0.000	0.000
172	A	175	LYS	1	0.943	0.970	20.003	-0.120	-0.120	0.000	0.000	0.000
173	A	176	ASP	-1	-0.878	-0.939	20.229	0.184	0.184	0.000	0.000	0.000
174	A	177	ASN	0	-0.081	-0.046	22.333	-0.014	-0.014	0.000	0.000	0.000
175	A	178	PRO	0	0.017	0.012	18.794	-0.010	-0.010	0.000	0.000	0.000
176	A	179	LEU	0	-0.017	-0.019	21.002	-0.021	-0.021	0.000	0.000	0.000
177	A	180	ASP	-1	-0.798	-0.834	20.928	0.218	0.218	0.000	0.000	0.000
178	A	181	VAL	0	-0.059	-0.036	19.844	-0.022	-0.022	0.000	0.000	0.000
179	A	182	SER	0	0.006	0.006	20.787	0.006	0.006	0.000	0.000	0.000
180	A	183	PHE	0	0.050	0.028	17.326	-0.006	-0.006	0.000	0.000	0.000
181	A	184	LYS	1	1.002	1.007	22.620	-0.075	-0.075	0.000	0.000	0.000
182	A	185	GLN	0	0.066	0.033	25.605	0.001	0.001	0.000	0.000	0.000
183	A	186	VAL	0	-0.059	-0.032	26.526	-0.004	-0.004	0.000	0.000	0.000
184	A	187	GLN	0	0.002	0.010	29.452	-0.006	-0.006	0.000	0.000	0.000

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