FMO DATABASE

FMODB ID: M97RZ

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	OptH
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	-599853.795778
FMO2-HF: Nuclear repulsion	564550.106844
FMO2-HF: Total energy	-35303.688934
FMO2-MP2: Total energy	-35404.611632

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.
-1.623	-0.368	-0.004	-0.712	-0.539	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 : 0.091 / q_NPA : 0.002

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	-0.047	0.138	4.406	-0.037	0.281	0.000	-0.163	-0.155	0.000
5	A	115	ASN	0	0.148	-0.053	3.805	-3.290	-2.353	-0.004	-0.549	-0.384	0.003
6	A	115	ASN	0	-0.106	0.068	6.535	-0.048	-0.048	0.000	0.000	0.000	0.000
7	A	116	LYS	0	0.133	-0.067	6.350	0.705	0.705	0.000	0.000	0.000	0.000
8	A	116	LYS	1	0.863	1.066	7.051	1.371	1.371	0.000	0.000	0.000	0.000
9	A	117	ASP	0	0.092	-0.097	8.015	0.326	0.326	0.000	0.000	0.000	0.000
10	A	117	ASP	-1	-0.984	-0.862	11.590	-1.299	-1.299	0.000	0.000	0.000	0.000
11	A	118	GLN	0	0.057	-0.104	10.344	0.224	0.224	0.000	0.000	0.000	0.000
12	A	118	GLN	0	-0.118	0.066	10.119	-0.087	-0.087	0.000	0.000	0.000	0.000
13	A	119	ILE	0	0.113	-0.094	10.380	0.240	0.240	0.000	0.000	0.000	0.000
14	A	119	ILE	0	-0.062	0.105	8.336	-0.010	-0.010	0.000	0.000	0.000	0.000
15	A	120	ALA	0	0.137	-0.083	11.736	0.180	0.180	0.000	0.000	0.000	0.000
16	A	120	ALA	0	-0.087	0.114	13.151	-0.015	-0.015	0.000	0.000	0.000	0.000
17	A	121	LYS	0	0.007	-0.125	14.034	0.111	0.111	0.000	0.000	0.000	0.000
18	A	121	LYS	1	0.874	1.065	14.675	0.741	0.741	0.000	0.000	0.000	0.000
19	A	122	ASP	0	0.112	-0.096	14.845	0.077	0.077	0.000	0.000	0.000	0.000
20	A	122	ASP	-1	-0.939	-0.810	14.337	-0.375	-0.375	0.000	0.000	0.000	0.000
21	A	123	VAL	0	0.058	-0.087	15.918	0.092	0.092	0.000	0.000	0.000	0.000
22	A	123	VAL	0	-0.049	0.104	15.207	-0.002	-0.002	0.000	0.000	0.000	0.000
23	A	124	LYS	0	0.057	-0.089	17.645	0.056	0.056	0.000	0.000	0.000	0.000
24	A	124	LYS	1	0.732	0.973	17.512	0.550	0.550	0.000	0.000	0.000	0.000
25	A	125	GLN	0	0.141	-0.053	19.478	0.034	0.034	0.000	0.000	0.000	0.000
26	A	125	GLN	0	-0.112	0.093	19.246	-0.017	-0.017	0.000	0.000	0.000	0.000
27	A	126	PHE	0	0.091	-0.101	19.975	0.035	0.035	0.000	0.000	0.000	0.000
28	A	126	PHE	0	-0.120	0.075	19.969	0.007	0.007	0.000	0.000	0.000	0.000
29	A	127	TYR	0	0.084	-0.080	21.618	0.034	0.034	0.000	0.000	0.000	0.000
30	A	127	TYR	0	-0.131	0.046	22.626	-0.007	-0.007	0.000	0.000	0.000	0.000
31	A	128	ASP	0	0.091	-0.115	23.673	0.024	0.024	0.000	0.000	0.000	0.000
32	A	128	ASP	-1	-0.888	-0.769	24.459	-0.250	-0.250	0.000	0.000	0.000	0.000
33	A	129	GLN	0	0.049	-0.089	24.821	0.014	0.014	0.000	0.000	0.000	0.000
34	A	129	GLN	0	-0.090	0.066	23.868	0.001	0.001	0.000	0.000	0.000	0.000
35	A	130	ALA	0	0.156	-0.076	25.992	0.020	0.020	0.000	0.000	0.000	0.000
36	A	130	ALA	0	-0.085	0.106	26.169	-0.001	-0.001	0.000	0.000	0.000	0.000
37	A	131	LEU	0	0.111	-0.117	27.705	0.017	0.017	0.000	0.000	0.000	0.000
38	A	131	LEU	0	-0.143	0.094	28.390	-0.001	-0.001	0.000	0.000	0.000	0.000
39	A	132	GLN	0	0.079	-0.107	29.522	0.008	0.008	0.000	0.000	0.000	0.000
40	A	132	GLN	0	-0.105	0.075	28.618	-0.014	-0.014	0.000	0.000	0.000	0.000
41	A	133	GLN	0	0.119	-0.082	30.550	0.006	0.006	0.000	0.000	0.000	0.000
42	A	133	GLN	0	-0.078	0.104	29.882	-0.005	-0.005	0.000	0.000	0.000	0.000
43	A	134	ALA	0	0.062	-0.095	31.851	0.011	0.011	0.000	0.000	0.000	0.000
44	A	134	ALA	0	-0.086	0.094	32.061	-0.001	-0.001	0.000	0.000	0.000	0.000
45	A	135	VAL	0	-0.022	-0.099	33.626	0.008	0.008	0.000	0.000	0.000	0.000
46	A	135	VAL	0	-0.102	0.053	34.613	-0.001	-0.001	0.000	0.000	0.000	0.000
47	A	136	VAL	0	0.044	-0.069	35.380	0.005	0.005	0.000	0.000	0.000	0.000
48	A	136	VAL	0	-0.112	0.053	34.320	-0.001	-0.001	0.000	0.000	0.000	0.000
49	A	137	ASP	0	0.081	-0.097	35.565	0.004	0.004	0.000	0.000	0.000	0.000
50	A	137	ASP	-1	-0.938	-0.867	34.711	-0.040	-0.040	0.000	0.000	0.000	0.000
51	A	138	ASP	0	-0.027	-0.111	36.798	-0.005	-0.005	0.000	0.000	0.000	0.000
52	A	138	ASP	-1	-0.971	-0.864	38.391	-0.024	-0.024	0.000	0.000	0.000	0.000
53	A	139	ASP	0	0.064	-0.095	37.901	0.002	0.002	0.000	0.000	0.000	0.000
54	A	139	ASP	-1	-1.024	-0.890	38.964	-0.031	-0.031	0.000	0.000	0.000	0.000
55	A	140	ALA	0	0.247	-0.033	33.590	0.007	0.007	0.000	0.000	0.000	0.000
56	A	140	ALA	0	-0.106	0.108	32.659	-0.001	-0.001	0.000	0.000	0.000	0.000
57	A	141	ASN	0	0.038	-0.138	34.087	-0.010	-0.010	0.000	0.000	0.000	0.000
58	A	141	ASN	0	-0.074	0.087	35.531	-0.002	-0.002	0.000	0.000	0.000	0.000
59	A	142	ASN	0	0.086	-0.072	30.630	-0.006	-0.006	0.000	0.000	0.000	0.000
60	A	142	ASN	0	-0.068	0.074	27.490	0.000	0.000	0.000	0.000	0.000	0.000
61	A	143	ALA	0	0.102	-0.123	29.434	-0.007	-0.007	0.000	0.000	0.000	0.000
62	A	143	ALA	0	-0.044	0.156	30.725	0.001	0.001	0.000	0.000	0.000	0.000
63	A	144	LYS	0	0.096	-0.079	30.267	-0.014	-0.014	0.000	0.000	0.000	0.000
64	A	144	LYS	1	0.786	1.026	34.323	0.062	0.062	0.000	0.000	0.000	0.000
65	A	145	ALA	0	0.061	-0.119	31.450	-0.011	-0.011	0.000	0.000	0.000	0.000
66	A	145	ALA	0	-0.066	0.117	30.897	0.002	0.002	0.000	0.000	0.000	0.000
67	A	146	VAL	0	0.044	-0.127	27.106	-0.006	-0.006	0.000	0.000	0.000	0.000
68	A	146	VAL	0	-0.066	0.109	25.175	0.000	0.000	0.000	0.000	0.000	0.000
69	A	147	VAL	0	0.086	-0.080	27.172	-0.018	-0.018	0.000	0.000	0.000	0.000
70	A	147	VAL	0	-0.075	0.115	28.627	0.000	0.000	0.000	0.000	0.000	0.000
71	A	148	LYS	0	0.055	-0.103	28.933	-0.015	-0.015	0.000	0.000	0.000	0.000
72	A	148	LYS	1	0.884	1.057	31.490	0.075	0.075	0.000	0.000	0.000	0.000
73	A	149	THR	0	0.025	-0.047	27.005	-0.008	-0.008	0.000	0.000	0.000	0.000
74	A	149	THR	0	-0.043	0.048	25.019	0.005	0.005	0.000	0.000	0.000	0.000
75	A	150	PHE	0	0.086	-0.066	24.551	-0.006	-0.006	0.000	0.000	0.000	0.000
76	A	150	PHE	0	-0.105	0.078	20.855	-0.003	-0.003	0.000	0.000	0.000	0.000
77	A	151	HIS	0	0.107	-0.066	25.457	-0.024	-0.024	0.000	0.000	0.000	0.000
78	A	151	HIS	0	-0.071	0.088	28.320	-0.010	-0.010	0.000	0.000	0.000	0.000
79	A	152	GLU	0	0.060	-0.099	28.194	-0.013	-0.013	0.000	0.000	0.000	0.000
80	A	152	GLU	-1	-1.011	-0.862	29.104	-0.124	-0.124	0.000	0.000	0.000	0.000
81	A	153	THR	0	0.044	-0.077	24.481	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	153	THR	0	-0.110	0.017	22.660	0.003	0.003	0.000	0.000	0.000	0.000
83	A	154	LEU	0	-0.014	-0.103	23.816	-0.011	-0.011	0.000	0.000	0.000	0.000
84	A	154	LEU	0	-0.107	0.064	20.520	-0.007	-0.007	0.000	0.000	0.000	0.000
85	A	155	ASP	0	0.166	-0.093	24.510	-0.018	-0.018	0.000	0.000	0.000	0.000
86	A	155	ASP	-1	-1.037	-0.840	27.721	-0.185	-0.185	0.000	0.000	0.000	0.000
87	A	156	CYS	0	0.088	-0.128	27.024	-0.016	-0.016	0.000	0.000	0.000	0.000
88	A	156	CYS	0	-0.274	0.199	24.048	-0.004	-0.004	0.000	0.000	0.000	0.000
89	A	157	CYS	0	0.165	-0.119	28.320	0.014	0.014	0.000	0.000	0.000	0.000
90	A	157	CYS	0	-0.253	0.194	32.074	0.004	0.004	0.000	0.000	0.000	0.000
91	A	158	GLY	0	0.052	-0.077	29.633	0.001	0.001	0.000	0.000	0.000	0.000
92	A	159	SER	0	0.106	0.022	27.541	-0.018	-0.018	0.000	0.000	0.000	0.000
93	A	159	SER	0	-0.055	0.053	26.872	-0.006	-0.006	0.000	0.000	0.000	0.000
94	A	160	SER	0	0.024	-0.100	27.696	0.023	0.023	0.000	0.000	0.000	0.000
95	A	160	SER	0	-0.067	0.065	27.043	-0.002	-0.002	0.000	0.000	0.000	0.000
96	A	161	THR	0	-0.037	-0.084	27.609	0.013	0.013	0.000	0.000	0.000	0.000
97	A	161	THR	0	-0.018	0.062	25.777	-0.005	-0.005	0.000	0.000	0.000	0.000
98	A	162	LEU	0	0.000	-0.106	28.936	0.010	0.010	0.000	0.000	0.000	0.000
99	A	162	LEU	0	-0.078	0.115	27.868	0.002	0.002	0.000	0.000	0.000	0.000
100	A	163	THR	0	0.146	-0.080	31.202	0.005	0.005	0.000	0.000	0.000	0.000
101	A	163	THR	0	-0.050	0.066	32.168	0.004	0.004	0.000	0.000	0.000	0.000
102	A	164	ALA	0	0.152	-0.072	33.773	0.004	0.004	0.000	0.000	0.000	0.000
103	A	164	ALA	0	-0.085	0.107	36.313	0.001	0.001	0.000	0.000	0.000	0.000
104	A	165	LEU	0	0.059	-0.124	34.409	0.007	0.007	0.000	0.000	0.000	0.000
105	A	165	LEU	0	-0.035	0.130	32.935	-0.001	-0.001	0.000	0.000	0.000	0.000
106	A	166	THR	0	0.068	-0.078	33.156	0.008	0.008	0.000	0.000	0.000	0.000
107	A	166	THR	0	-0.040	0.100	32.254	-0.001	-0.001	0.000	0.000	0.000	0.000
108	A	167	THR	0	-0.002	-0.086	34.018	0.000	0.000	0.000	0.000	0.000	0.000
109	A	167	THR	0	-0.057	0.062	37.591	0.001	0.001	0.000	0.000	0.000	0.000
110	A	168	SER	0	-0.014	-0.057	37.670	0.002	0.002	0.000	0.000	0.000	0.000
111	A	168	SER	0	0.001	0.084	37.692	0.002	0.002	0.000	0.000	0.000	0.000
112	A	169	VAL	0	0.043	-0.105	34.567	0.009	0.009	0.000	0.000	0.000	0.000
113	A	169	VAL	0	-0.044	0.101	32.691	-0.001	-0.001	0.000	0.000	0.000	0.000
114	A	170	LEU	0	0.134	-0.117	36.083	0.003	0.003	0.000	0.000	0.000	0.000
115	A	170	LEU	0	-0.120	0.106	36.179	0.001	0.001	0.000	0.000	0.000	0.000
116	A	171	LYS	0	0.027	-0.108	36.993	0.001	0.001	0.000	0.000	0.000	0.000
117	A	171	LYS	1	0.858	1.063	40.742	0.093	0.093	0.000	0.000	0.000	0.000
118	A	172	ASN	0	0.060	-0.046	39.105	0.005	0.005	0.000	0.000	0.000	0.000
119	A	172	ASN	0	-0.123	0.043	38.087	0.003	0.003	0.000	0.000	0.000	0.000
120	A	173	ASN	0	0.050	-0.075	38.575	0.002	0.002	0.000	0.000	0.000	0.000
121	A	173	ASN	0	-0.124	0.060	39.447	-0.001	-0.001	0.000	0.000	0.000	0.000
122	A	174	LEU	0	0.062	-0.102	34.354	0.006	0.006	0.000	0.000	0.000	0.000
123	A	174	LEU	0	-0.059	0.085	33.350	0.000	0.000	0.000	0.000	0.000	0.000
124	A	175	CYS	0	0.077	-0.084	32.771	-0.009	-0.009	0.000	0.000	0.000	0.000
125	A	176	PRO	0	0.132	-0.027	31.323	0.012	0.012	0.000	0.000	0.000	0.000
126	A	177	SER	0	0.070	0.040	34.043	-0.002	-0.002	0.000	0.000	0.000	0.000
127	A	177	SER	0	-0.057	0.068	36.967	0.004	0.004	0.000	0.000	0.000	0.000
128	A	178	GLY	0	0.045	-0.052	37.750	-0.003	-0.003	0.000	0.000	0.000	0.000
129	A	179	SER	0	-0.045	-0.043	39.882	0.006	0.006	0.000	0.000	0.000	0.000
130	A	179	SER	0	-0.049	0.065	38.848	-0.002	-0.002	0.000	0.000	0.000	0.000
131	A	180	ASN	0	0.055	-0.104	37.272	0.002	0.002	0.000	0.000	0.000	0.000
132	A	180	ASN	0	-0.048	0.105	34.728	0.008	0.008	0.000	0.000	0.000	0.000
133	A	181	ILE	0	0.031	-0.121	38.812	0.003	0.003	0.000	0.000	0.000	0.000
134	A	181	ILE	0	-0.068	0.097	41.586	0.002	0.002	0.000	0.000	0.000	0.000
135	A	182	ILE	0	0.113	-0.043	38.652	-0.003	-0.003	0.000	0.000	0.000	0.000
136	A	182	ILE	0	-0.113	0.048	38.771	0.001	0.001	0.000	0.000	0.000	0.000
137	A	183	SER	0	0.085	-0.048	36.991	-0.006	-0.006	0.000	0.000	0.000	0.000
138	A	183	SER	0	-0.048	0.057	36.909	-0.003	-0.003	0.000	0.000	0.000	0.000
139	A	184	ASN	0	0.033	-0.085	36.057	0.005	0.005	0.000	0.000	0.000	0.000
140	A	184	ASN	0	-0.087	0.058	36.326	-0.001	-0.001	0.000	0.000	0.000	0.000
141	A	185	LEU	0	0.167	-0.050	33.607	-0.011	-0.011	0.000	0.000	0.000	0.000
142	A	185	LEU	0	-0.077	0.097	34.123	0.001	0.001	0.000	0.000	0.000	0.000
143	A	186	PHE	0	0.170	-0.036	31.927	-0.010	-0.010	0.000	0.000	0.000	0.000
144	A	186	PHE	0	-0.099	0.063	33.036	0.003	0.003	0.000	0.000	0.000	0.000
145	A	187	LYS	0	-0.009	-0.152	30.911	-0.015	-0.015	0.000	0.000	0.000	0.000
146	A	187	LYS	1	0.819	1.053	32.129	0.159	0.159	0.000	0.000	0.000	0.000
147	A	188	GLU	0	-0.051	-0.115	29.593	-0.017	-0.017	0.000	0.000	0.000	0.000
148	A	188	GLU	-1	-0.899	-0.828	30.721	-0.156	-0.156	0.000	0.000	0.000	0.000
149	A	189	ASP	0	0.206	-0.066	27.048	0.009	0.009	0.000	0.000	0.000	0.000
150	A	189	ASP	-1	-0.910	-0.799	26.365	-0.280	-0.280	0.000	0.000	0.000	0.000
151	A	190	CYS	0	0.090	-0.133	24.474	-0.022	-0.022	0.000	0.000	0.000	0.000
152	A	191	HIS	0	0.130	-0.048	21.568	-0.031	-0.031	0.000	0.000	0.000	0.000
153	A	191	HIS	1	0.699	0.927	22.209	0.296	0.296	0.000	0.000	0.000	0.000
154	A	192	GLN	0	0.090	-0.087	20.496	-0.054	-0.054	0.000	0.000	0.000	0.000
155	A	192	GLN	0	-0.087	0.102	21.195	0.006	0.006	0.000	0.000	0.000	0.000
156	A	193	LYS	0	0.064	-0.114	20.833	-0.049	-0.049	0.000	0.000	0.000	0.000
157	A	193	LYS	1	0.902	1.098	22.523	0.276	0.276	0.000	0.000	0.000	0.000
158	A	194	ILE	0	0.094	-0.093	18.638	-0.022	-0.022	0.000	0.000	0.000	0.000
159	A	194	ILE	0	-0.106	0.090	16.938	-0.003	-0.003	0.000	0.000	0.000	0.000
160	A	195	ASP	0	0.094	-0.125	16.290	-0.079	-0.079	0.000	0.000	0.000	0.000
161	A	195	ASP	-1	-0.930	-0.794	17.152	-0.625	-0.625	0.000	0.000	0.000	0.000
162	A	196	ASP	0	0.079	-0.138	15.935	-0.131	-0.131	0.000	0.000	0.000	0.000
163	A	196	ASP	-1	-0.953	-0.816	19.726	-0.468	-0.468	0.000	0.000	0.000	0.000
164	A	197	LEU	0	0.045	-0.118	16.778	-0.024	-0.024	0.000	0.000	0.000	0.000
165	A	197	LEU	0	-0.079	0.120	15.588	0.010	0.010	0.000	0.000	0.000	0.000
166	A	198	PHE	0	0.011	-0.096	12.684	0.004	0.004	0.000	0.000	0.000	0.000
167	A	198	PHE	0	-0.087	0.077	10.777	-0.021	-0.021	0.000	0.000	0.000	0.000
168	A	199	SER	0	-0.036	-0.102	11.734	-0.259	-0.259	0.000	0.000	0.000	0.000
169	A	199	SER	0	-0.087	0.041	14.517	-0.037	-0.037	0.000	0.000	0.000	0.000
170	A	200	GLY	0	0.006	-0.090	14.036	0.013	0.013	0.000	0.000	0.000	0.000
171	A	201	LYS	0	0.092	0.052	15.605	0.025	0.025	0.000	0.000	0.000	0.000
172	A	201	LYS	1	0.761	0.992	17.449	0.651	0.651	0.000	0.000	0.000	0.000
173	A	202	HIS	0	-0.047	-0.127	19.205	0.026	0.026	0.000	0.000	0.000	0.000
174	A	202	HIS	0	0.083	0.054	19.378	0.032	0.032	0.000	0.000	0.000	0.000

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