FMO DATABASE

FMODB ID: L72Q9

Calculation Name: 5DFV-A-Xray540

Preferred Name: CD81 antigen

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 5DFV

Chain ID: A

ChEMBL ID: CHEMBL1075180

UniProt ID: P60033

Base Structure: X-ray

Registration Date: 2025-07-10

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

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	174
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-599925.794029
FMO2-HF: Nuclear repulsion	564620.682827
FMO2-HF: Total energy	-35305.111202
FMO2-MP2: Total energy	-35405.971954

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:113:PHE)

Summations of interaction energy for fragment #1(A:113:PHE)

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.
-1.694	-0.317	-0.002	-0.777	-0.599	0.003

Interaction energy analysis for fragmet #1(A:113:PHE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.084 / q_NPA : 0.008

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	114	VAL	0	-0.068	0.132	3.931	-0.131	0.278	0.002	-0.215	-0.197	0.000
5	A	115	ASN	0	0.137	-0.052	3.805	-3.329	-2.361	-0.004	-0.562	-0.402	0.003
6	A	115	ASN	0	-0.108	0.063	6.542	0.073	0.073	0.000	0.000	0.000	0.000
7	A	116	LYS	0	0.140	-0.060	6.350	0.667	0.667	0.000	0.000	0.000	0.000
8	A	116	LYS	1	0.802	1.016	7.015	1.334	1.334	0.000	0.000	0.000	0.000
9	A	117	ASP	0	0.138	-0.058	8.046	0.319	0.319	0.000	0.000	0.000	0.000
10	A	117	ASP	-1	-0.948	-0.842	11.329	-1.281	-1.281	0.000	0.000	0.000	0.000
11	A	118	GLN	0	0.043	-0.118	10.378	0.191	0.191	0.000	0.000	0.000	0.000
12	A	118	GLN	0	-0.105	0.068	10.199	-0.058	-0.058	0.000	0.000	0.000	0.000
13	A	119	ILE	0	0.100	-0.082	10.411	0.226	0.226	0.000	0.000	0.000	0.000
14	A	119	ILE	0	-0.069	0.104	8.799	-0.007	-0.007	0.000	0.000	0.000	0.000
15	A	120	ALA	0	0.158	-0.086	11.736	0.168	0.168	0.000	0.000	0.000	0.000
16	A	120	ALA	0	-0.085	0.103	13.121	-0.017	-0.017	0.000	0.000	0.000	0.000
17	A	121	LYS	0	0.023	-0.136	14.067	0.098	0.098	0.000	0.000	0.000	0.000
18	A	121	LYS	1	0.867	1.067	14.165	0.696	0.696	0.000	0.000	0.000	0.000
19	A	122	ASP	0	0.103	-0.087	14.841	0.067	0.067	0.000	0.000	0.000	0.000
20	A	122	ASP	-1	-0.959	-0.809	14.300	-0.285	-0.285	0.000	0.000	0.000	0.000
21	A	123	VAL	0	0.073	-0.085	15.942	0.085	0.085	0.000	0.000	0.000	0.000
22	A	123	VAL	0	-0.064	0.102	15.226	-0.003	-0.003	0.000	0.000	0.000	0.000
23	A	124	LYS	0	0.074	-0.092	17.666	0.050	0.050	0.000	0.000	0.000	0.000
24	A	124	LYS	1	0.698	0.947	17.453	0.517	0.517	0.000	0.000	0.000	0.000
25	A	125	GLN	0	0.131	-0.049	19.484	0.030	0.030	0.000	0.000	0.000	0.000
26	A	125	GLN	0	-0.134	0.076	19.298	-0.019	-0.019	0.000	0.000	0.000	0.000
27	A	126	PHE	0	0.091	-0.105	19.975	0.030	0.030	0.000	0.000	0.000	0.000
28	A	126	PHE	0	-0.134	0.070	19.924	0.006	0.006	0.000	0.000	0.000	0.000
29	A	127	TYR	0	0.106	-0.073	21.618	0.032	0.032	0.000	0.000	0.000	0.000
30	A	127	TYR	0	-0.153	0.025	22.565	-0.007	-0.007	0.000	0.000	0.000	0.000
31	A	128	ASP	0	0.083	-0.099	23.693	0.021	0.021	0.000	0.000	0.000	0.000
32	A	128	ASP	-1	-0.893	-0.797	24.211	-0.223	-0.223	0.000	0.000	0.000	0.000
33	A	129	GLN	0	0.095	-0.086	24.820	0.012	0.012	0.000	0.000	0.000	0.000
34	A	129	GLN	0	-0.074	0.091	23.247	-0.001	-0.001	0.000	0.000	0.000	0.000
35	A	130	ALA	0	0.147	-0.068	25.989	0.018	0.018	0.000	0.000	0.000	0.000
36	A	130	ALA	0	-0.089	0.099	26.174	-0.001	-0.001	0.000	0.000	0.000	0.000
37	A	131	LEU	0	0.106	-0.113	27.706	0.015	0.015	0.000	0.000	0.000	0.000
38	A	131	LEU	0	-0.138	0.083	28.303	-0.001	-0.001	0.000	0.000	0.000	0.000
39	A	132	GLN	0	0.073	-0.102	29.523	0.006	0.006	0.000	0.000	0.000	0.000
40	A	132	GLN	0	-0.113	0.064	28.620	-0.006	-0.006	0.000	0.000	0.000	0.000
41	A	133	GLN	0	0.087	-0.067	30.551	0.005	0.005	0.000	0.000	0.000	0.000
42	A	133	GLN	0	-0.124	0.065	30.195	-0.003	-0.003	0.000	0.000	0.000	0.000
43	A	134	ALA	0	0.067	-0.090	31.852	0.011	0.011	0.000	0.000	0.000	0.000
44	A	134	ALA	0	-0.084	0.092	32.051	-0.002	-0.002	0.000	0.000	0.000	0.000
45	A	135	VAL	0	-0.005	-0.109	33.626	0.007	0.007	0.000	0.000	0.000	0.000
46	A	135	VAL	0	-0.122	0.069	34.490	-0.001	-0.001	0.000	0.000	0.000	0.000
47	A	136	VAL	0	0.102	-0.073	35.376	0.004	0.004	0.000	0.000	0.000	0.000
48	A	136	VAL	0	-0.117	0.061	34.358	-0.001	-0.001	0.000	0.000	0.000	0.000
49	A	137	ASP	0	0.075	-0.101	35.527	0.004	0.004	0.000	0.000	0.000	0.000
50	A	137	ASP	-1	-0.928	-0.842	34.699	-0.029	-0.029	0.000	0.000	0.000	0.000
51	A	138	ASP	0	0.029	-0.105	36.798	-0.005	-0.005	0.000	0.000	0.000	0.000
52	A	138	ASP	-1	-0.968	-0.843	38.936	-0.014	-0.014	0.000	0.000	0.000	0.000
53	A	139	ASP	0	0.050	-0.118	37.861	0.002	0.002	0.000	0.000	0.000	0.000
54	A	139	ASP	-1	-0.996	-0.862	38.879	-0.024	-0.024	0.000	0.000	0.000	0.000
55	A	140	ALA	0	0.221	-0.055	33.623	0.006	0.006	0.000	0.000	0.000	0.000
56	A	140	ALA	0	-0.085	0.114	32.678	-0.001	-0.001	0.000	0.000	0.000	0.000
57	A	141	ASN	0	0.090	-0.102	34.105	-0.009	-0.009	0.000	0.000	0.000	0.000
58	A	141	ASN	0	-0.144	0.057	35.965	-0.004	-0.004	0.000	0.000	0.000	0.000
59	A	142	ASN	0	0.057	-0.096	30.689	-0.006	-0.006	0.000	0.000	0.000	0.000
60	A	142	ASN	0	-0.078	0.066	27.443	-0.002	-0.002	0.000	0.000	0.000	0.000
61	A	143	ALA	0	0.098	-0.115	29.451	-0.007	-0.007	0.000	0.000	0.000	0.000
62	A	143	ALA	0	-0.037	0.145	30.696	0.001	0.001	0.000	0.000	0.000	0.000
63	A	144	LYS	0	0.091	-0.077	30.287	-0.014	-0.014	0.000	0.000	0.000	0.000
64	A	144	LYS	1	0.768	1.027	34.354	0.050	0.050	0.000	0.000	0.000	0.000
65	A	145	ALA	0	0.088	-0.097	31.470	-0.011	-0.011	0.000	0.000	0.000	0.000
66	A	145	ALA	0	-0.074	0.106	30.994	0.002	0.002	0.000	0.000	0.000	0.000
67	A	146	VAL	0	0.070	-0.109	27.107	-0.008	-0.008	0.000	0.000	0.000	0.000
68	A	146	VAL	0	-0.087	0.106	25.121	0.000	0.000	0.000	0.000	0.000	0.000
69	A	147	VAL	0	0.117	-0.097	27.194	-0.017	-0.017	0.000	0.000	0.000	0.000
70	A	147	VAL	0	-0.086	0.117	28.665	0.000	0.000	0.000	0.000	0.000	0.000
71	A	148	LYS	0	0.054	-0.100	28.966	-0.014	-0.014	0.000	0.000	0.000	0.000
72	A	148	LYS	1	0.896	1.053	31.452	0.068	0.068	0.000	0.000	0.000	0.000
73	A	149	THR	0	0.015	-0.048	27.087	-0.009	-0.009	0.000	0.000	0.000	0.000
74	A	149	THR	0	-0.061	0.048	25.363	0.005	0.005	0.000	0.000	0.000	0.000
75	A	150	PHE	0	0.070	-0.066	24.579	-0.008	-0.008	0.000	0.000	0.000	0.000
76	A	150	PHE	0	-0.101	0.072	20.778	-0.004	-0.004	0.000	0.000	0.000	0.000
77	A	151	HIS	0	0.117	-0.036	25.488	-0.024	-0.024	0.000	0.000	0.000	0.000
78	A	151	HIS	0	-0.069	0.090	27.587	-0.011	-0.011	0.000	0.000	0.000	0.000
79	A	152	GLU	0	0.060	-0.113	28.224	-0.013	-0.013	0.000	0.000	0.000	0.000
80	A	152	GLU	-1	-1.001	-0.862	29.220	-0.120	-0.120	0.000	0.000	0.000	0.000
81	A	153	THR	0	0.028	-0.084	24.510	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	153	THR	0	-0.105	0.015	22.683	0.002	0.002	0.000	0.000	0.000	0.000
83	A	154	LEU	0	-0.005	-0.100	23.837	-0.013	-0.013	0.000	0.000	0.000	0.000
84	A	154	LEU	0	-0.097	0.066	20.626	-0.005	-0.005	0.000	0.000	0.000	0.000
85	A	155	ASP	0	0.169	-0.059	24.539	-0.017	-0.017	0.000	0.000	0.000	0.000
86	A	155	ASP	-1	-1.003	-0.845	27.397	-0.198	-0.198	0.000	0.000	0.000	0.000
87	A	156	CYS	0	0.146	-0.110	26.968	-0.013	-0.013	0.000	0.000	0.000	0.000
88	A	156	CYS	0	-0.269	0.245	24.177	0.000	0.000	0.000	0.000	0.000	0.000
89	A	157	CYS	0	0.148	-0.133	28.350	0.013	0.013	0.000	0.000	0.000	0.000
90	A	157	CYS	0	-0.266	0.177	32.106	0.004	0.004	0.000	0.000	0.000	0.000
91	A	158	GLY	0	0.048	-0.081	29.601	0.002	0.002	0.000	0.000	0.000	0.000
92	A	159	SER	0	0.109	0.043	27.565	-0.017	-0.017	0.000	0.000	0.000	0.000
93	A	159	SER	0	-0.044	0.065	26.424	-0.002	-0.002	0.000	0.000	0.000	0.000
94	A	160	SER	0	0.030	-0.110	27.728	0.021	0.021	0.000	0.000	0.000	0.000
95	A	160	SER	0	-0.053	0.049	27.007	-0.002	-0.002	0.000	0.000	0.000	0.000
96	A	161	THR	0	-0.085	-0.081	27.670	0.012	0.012	0.000	0.000	0.000	0.000
97	A	161	THR	0	-0.042	0.043	25.949	-0.005	-0.005	0.000	0.000	0.000	0.000
98	A	162	LEU	0	0.016	-0.103	28.968	0.010	0.010	0.000	0.000	0.000	0.000
99	A	162	LEU	0	-0.070	0.106	28.210	0.002	0.002	0.000	0.000	0.000	0.000
100	A	163	THR	0	0.188	-0.089	31.235	0.003	0.003	0.000	0.000	0.000	0.000
101	A	163	THR	0	-0.019	0.073	32.515	0.002	0.002	0.000	0.000	0.000	0.000
102	A	164	ALA	0	0.050	-0.050	33.806	0.003	0.003	0.000	0.000	0.000	0.000
103	A	164	ALA	0	-0.089	0.097	36.339	0.001	0.001	0.000	0.000	0.000	0.000
104	A	165	LEU	0	0.066	-0.119	34.421	0.006	0.006	0.000	0.000	0.000	0.000
105	A	165	LEU	0	-0.023	0.125	32.809	-0.001	-0.001	0.000	0.000	0.000	0.000
106	A	166	THR	0	0.044	-0.084	33.058	0.008	0.008	0.000	0.000	0.000	0.000
107	A	166	THR	0	-0.005	0.104	32.133	0.000	0.000	0.000	0.000	0.000	0.000
108	A	167	THR	0	0.020	-0.075	34.051	0.000	0.000	0.000	0.000	0.000	0.000
109	A	167	THR	0	-0.065	0.069	37.535	0.000	0.000	0.000	0.000	0.000	0.000
110	A	168	SER	0	0.006	-0.088	37.702	0.001	0.001	0.000	0.000	0.000	0.000
111	A	168	SER	0	0.001	0.081	37.393	0.002	0.002	0.000	0.000	0.000	0.000
112	A	169	VAL	0	0.062	-0.102	34.615	0.009	0.009	0.000	0.000	0.000	0.000
113	A	169	VAL	0	-0.076	0.101	32.612	0.000	0.000	0.000	0.000	0.000	0.000
114	A	170	LEU	0	0.095	-0.113	36.117	0.003	0.003	0.000	0.000	0.000	0.000
115	A	170	LEU	0	-0.095	0.099	36.245	0.000	0.000	0.000	0.000	0.000	0.000
116	A	171	LYS	0	0.054	-0.096	37.026	0.001	0.001	0.000	0.000	0.000	0.000
117	A	171	LYS	1	0.845	1.057	40.876	0.084	0.084	0.000	0.000	0.000	0.000
118	A	172	ASN	0	0.050	-0.047	39.125	0.005	0.005	0.000	0.000	0.000	0.000
119	A	172	ASN	0	-0.126	0.049	38.227	0.004	0.004	0.000	0.000	0.000	0.000
120	A	173	ASN	0	0.066	-0.075	38.567	0.003	0.003	0.000	0.000	0.000	0.000
121	A	173	ASN	0	-0.128	0.059	39.514	-0.001	-0.001	0.000	0.000	0.000	0.000
122	A	174	LEU	0	0.062	-0.098	34.458	0.005	0.005	0.000	0.000	0.000	0.000
123	A	174	LEU	0	-0.065	0.077	33.461	0.000	0.000	0.000	0.000	0.000	0.000
124	A	175	CYS	0	0.073	-0.072	32.803	-0.009	-0.009	0.000	0.000	0.000	0.000
125	A	176	PRO	0	0.143	-0.031	31.136	0.010	0.010	0.000	0.000	0.000	0.000
126	A	177	SER	0	0.059	0.046	34.073	-0.002	-0.002	0.000	0.000	0.000	0.000
127	A	177	SER	0	-0.065	0.064	36.764	0.003	0.003	0.000	0.000	0.000	0.000
128	A	178	GLY	0	0.042	-0.059	37.779	-0.003	-0.003	0.000	0.000	0.000	0.000
129	A	179	SER	0	-0.027	-0.034	39.986	0.006	0.006	0.000	0.000	0.000	0.000
130	A	179	SER	0	-0.057	0.059	38.876	-0.002	-0.002	0.000	0.000	0.000	0.000
131	A	180	ASN	0	0.048	-0.080	37.290	0.002	0.002	0.000	0.000	0.000	0.000
132	A	180	ASN	0	-0.061	0.070	34.795	0.007	0.007	0.000	0.000	0.000	0.000
133	A	181	ILE	0	0.029	-0.120	38.841	0.003	0.003	0.000	0.000	0.000	0.000
134	A	181	ILE	0	-0.073	0.088	41.643	0.002	0.002	0.000	0.000	0.000	0.000
135	A	182	ILE	0	0.130	-0.030	38.667	-0.003	-0.003	0.000	0.000	0.000	0.000
136	A	182	ILE	0	-0.115	0.048	39.030	0.001	0.001	0.000	0.000	0.000	0.000
137	A	183	SER	0	0.085	-0.071	36.992	-0.006	-0.006	0.000	0.000	0.000	0.000
138	A	183	SER	0	-0.050	0.058	37.298	-0.002	-0.002	0.000	0.000	0.000	0.000
139	A	184	ASN	0	0.067	-0.053	36.057	0.005	0.005	0.000	0.000	0.000	0.000
140	A	184	ASN	0	-0.097	0.072	36.139	0.002	0.002	0.000	0.000	0.000	0.000
141	A	185	LEU	0	0.154	-0.067	33.653	-0.010	-0.010	0.000	0.000	0.000	0.000
142	A	185	LEU	0	-0.082	0.089	33.918	0.001	0.001	0.000	0.000	0.000	0.000
143	A	186	PHE	0	0.174	-0.052	31.957	-0.009	-0.009	0.000	0.000	0.000	0.000
144	A	186	PHE	0	-0.100	0.067	33.091	0.003	0.003	0.000	0.000	0.000	0.000
145	A	187	LYS	0	-0.021	-0.154	30.940	-0.014	-0.014	0.000	0.000	0.000	0.000
146	A	187	LYS	1	0.806	1.020	32.193	0.150	0.150	0.000	0.000	0.000	0.000
147	A	188	GLU	0	-0.040	-0.074	29.598	-0.017	-0.017	0.000	0.000	0.000	0.000
148	A	188	GLU	-1	-0.864	-0.802	30.793	-0.145	-0.145	0.000	0.000	0.000	0.000
149	A	189	ASP	0	0.218	-0.054	27.094	0.010	0.010	0.000	0.000	0.000	0.000
150	A	189	ASP	-1	-0.894	-0.796	26.007	-0.264	-0.264	0.000	0.000	0.000	0.000
151	A	190	CYS	0	0.125	-0.119	24.515	-0.022	-0.022	0.000	0.000	0.000	0.000
152	A	191	HIS	0	0.102	-0.069	21.601	-0.030	-0.030	0.000	0.000	0.000	0.000
153	A	191	HIS	1	0.729	0.941	22.239	0.269	0.269	0.000	0.000	0.000	0.000
154	A	192	GLN	0	0.085	-0.080	20.526	-0.052	-0.052	0.000	0.000	0.000	0.000
155	A	192	GLN	0	-0.104	0.079	21.168	0.011	0.011	0.000	0.000	0.000	0.000
156	A	193	LYS	0	0.056	-0.108	20.860	-0.049	-0.049	0.000	0.000	0.000	0.000
157	A	193	LYS	1	0.777	1.021	22.574	0.258	0.258	0.000	0.000	0.000	0.000
158	A	194	ILE	0	0.101	-0.078	18.666	-0.025	-0.025	0.000	0.000	0.000	0.000
159	A	194	ILE	0	-0.103	0.080	17.043	-0.002	-0.002	0.000	0.000	0.000	0.000
160	A	195	ASP	0	0.088	-0.108	16.308	-0.074	-0.074	0.000	0.000	0.000	0.000
161	A	195	ASP	-1	-0.896	-0.785	16.934	-0.593	-0.593	0.000	0.000	0.000	0.000
162	A	196	ASP	0	0.085	-0.110	15.962	-0.129	-0.129	0.000	0.000	0.000	0.000
163	A	196	ASP	-1	-0.932	-0.808	19.765	-0.458	-0.458	0.000	0.000	0.000	0.000
164	A	197	LEU	0	0.062	-0.111	16.804	-0.028	-0.028	0.000	0.000	0.000	0.000
165	A	197	LEU	0	-0.080	0.116	15.699	0.011	0.011	0.000	0.000	0.000	0.000
166	A	198	PHE	0	0.007	-0.099	12.716	-0.005	-0.005	0.000	0.000	0.000	0.000
167	A	198	PHE	0	-0.095	0.077	11.157	-0.019	-0.019	0.000	0.000	0.000	0.000
168	A	199	SER	0	0.001	-0.096	11.757	-0.256	-0.256	0.000	0.000	0.000	0.000
169	A	199	SER	0	-0.105	0.027	14.684	-0.025	-0.025	0.000	0.000	0.000	0.000
170	A	200	GLY	0	0.019	-0.089	14.057	0.011	0.011	0.000	0.000	0.000	0.000
171	A	201	LYS	0	0.132	0.064	15.622	0.021	0.021	0.000	0.000	0.000	0.000
172	A	201	LYS	1	0.736	0.990	16.560	0.690	0.690	0.000	0.000	0.000	0.000
173	A	202	HIS	0	-0.103	-0.154	19.224	0.023	0.023	0.000	0.000	0.000	0.000
174	A	202	HIS	0	0.069	0.051	19.292	0.034	0.034	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:113:PHE)