FMO DATABASE

FMODB ID: 9M6L2

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	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	174
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-601809.893684
FMO2-HF: Nuclear repulsion	566504.356625
FMO2-HF: Total energy	-35305.53706
FMO2-MP2: Total energy	-35406.382265

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.
-1.227	0.103	0.002	-0.735	-0.598	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 : 0.105 / q_NPA : 0.010

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	-0.050	0.133	3.764	-0.110	0.262	0.005	-0.186	-0.192	0.000
5	A	115	ASN	0	0.150	-0.042	3.867	-2.837	-1.879	-0.003	-0.549	-0.406	0.003
6	A	115	ASN	0	-0.111	0.060	6.688	0.081	0.081	0.000	0.000	0.000	0.000
7	A	116	LYS	0	0.116	-0.073	6.267	0.806	0.806	0.000	0.000	0.000	0.000
8	A	116	LYS	1	0.783	1.009	7.163	1.243	1.243	0.000	0.000	0.000	0.000
9	A	117	ASP	0	0.110	-0.070	8.182	0.359	0.359	0.000	0.000	0.000	0.000
10	A	117	ASP	-1	-0.901	-0.806	10.673	-1.361	-1.361	0.000	0.000	0.000	0.000
11	A	118	GLN	0	0.052	-0.080	10.145	0.192	0.192	0.000	0.000	0.000	0.000
12	A	118	GLN	0	-0.073	0.085	10.329	-0.087	-0.087	0.000	0.000	0.000	0.000
13	A	119	ILE	0	0.139	-0.073	10.339	0.183	0.183	0.000	0.000	0.000	0.000
14	A	119	ILE	0	-0.072	0.102	8.779	0.008	0.008	0.000	0.000	0.000	0.000
15	A	120	ALA	0	0.125	-0.105	11.929	0.154	0.154	0.000	0.000	0.000	0.000
16	A	120	ALA	0	-0.082	0.110	13.090	-0.024	-0.024	0.000	0.000	0.000	0.000
17	A	121	LYS	0	0.006	-0.122	14.188	0.067	0.067	0.000	0.000	0.000	0.000
18	A	121	LYS	1	0.751	0.978	13.805	0.627	0.627	0.000	0.000	0.000	0.000
19	A	122	ASP	0	0.112	-0.088	14.967	0.044	0.044	0.000	0.000	0.000	0.000
20	A	122	ASP	-1	-0.938	-0.812	13.873	-0.179	-0.179	0.000	0.000	0.000	0.000
21	A	123	VAL	0	0.072	-0.093	15.871	0.072	0.072	0.000	0.000	0.000	0.000
22	A	123	VAL	0	-0.059	0.102	15.122	-0.003	-0.003	0.000	0.000	0.000	0.000
23	A	124	LYS	0	0.069	-0.093	17.621	0.037	0.037	0.000	0.000	0.000	0.000
24	A	124	LYS	1	0.681	0.951	17.360	0.467	0.467	0.000	0.000	0.000	0.000
25	A	125	GLN	0	0.139	-0.063	19.560	0.023	0.023	0.000	0.000	0.000	0.000
26	A	125	GLN	0	-0.145	0.070	19.515	-0.021	-0.021	0.000	0.000	0.000	0.000
27	A	126	PHE	0	0.102	-0.095	20.166	0.025	0.025	0.000	0.000	0.000	0.000
28	A	126	PHE	0	-0.142	0.071	20.124	0.007	0.007	0.000	0.000	0.000	0.000
29	A	127	TYR	0	0.091	-0.079	21.814	0.027	0.027	0.000	0.000	0.000	0.000
30	A	127	TYR	0	-0.111	0.055	22.609	-0.009	-0.009	0.000	0.000	0.000	0.000
31	A	128	ASP	0	0.073	-0.097	23.781	0.015	0.015	0.000	0.000	0.000	0.000
32	A	128	ASP	-1	-0.845	-0.770	23.881	-0.184	-0.184	0.000	0.000	0.000	0.000
33	A	129	GLN	0	0.094	-0.079	24.994	0.006	0.006	0.000	0.000	0.000	0.000
34	A	129	GLN	0	-0.052	0.100	23.566	-0.001	-0.001	0.000	0.000	0.000	0.000
35	A	130	ALA	0	0.140	-0.073	26.034	0.014	0.014	0.000	0.000	0.000	0.000
36	A	130	ALA	0	-0.085	0.103	26.187	0.000	0.000	0.000	0.000	0.000	0.000
37	A	131	LEU	0	0.102	-0.109	27.772	0.012	0.012	0.000	0.000	0.000	0.000
38	A	131	LEU	0	-0.147	0.086	28.296	-0.002	-0.002	0.000	0.000	0.000	0.000
39	A	132	GLN	0	0.087	-0.105	29.568	0.002	0.002	0.000	0.000	0.000	0.000
40	A	132	GLN	0	-0.129	0.070	29.096	0.003	0.003	0.000	0.000	0.000	0.000
41	A	133	GLN	0	0.084	-0.073	30.618	0.002	0.002	0.000	0.000	0.000	0.000
42	A	133	GLN	0	-0.127	0.055	30.339	0.000	0.000	0.000	0.000	0.000	0.000
43	A	134	ALA	0	0.076	-0.113	31.890	0.010	0.010	0.000	0.000	0.000	0.000
44	A	134	ALA	0	-0.079	0.105	32.029	-0.002	-0.002	0.000	0.000	0.000	0.000
45	A	135	VAL	0	-0.083	-0.152	33.588	0.005	0.005	0.000	0.000	0.000	0.000
46	A	135	VAL	0	-0.079	0.088	34.685	-0.001	-0.001	0.000	0.000	0.000	0.000
47	A	136	VAL	0	0.089	-0.060	35.437	0.002	0.002	0.000	0.000	0.000	0.000
48	A	136	VAL	0	-0.093	0.067	34.251	-0.001	-0.001	0.000	0.000	0.000	0.000
49	A	137	ASP	0	0.098	-0.094	35.796	0.003	0.003	0.000	0.000	0.000	0.000
50	A	137	ASP	-1	-0.901	-0.808	34.868	-0.004	-0.004	0.000	0.000	0.000	0.000
51	A	138	ASP	0	0.025	-0.104	37.270	-0.006	-0.006	0.000	0.000	0.000	0.000
52	A	138	ASP	-1	-0.962	-0.837	39.280	0.005	0.005	0.000	0.000	0.000	0.000
53	A	139	ASP	0	0.065	-0.122	37.621	0.004	0.004	0.000	0.000	0.000	0.000
54	A	139	ASP	-1	-1.002	-0.858	38.722	-0.005	-0.005	0.000	0.000	0.000	0.000
55	A	140	ALA	0	0.218	-0.073	33.697	0.005	0.005	0.000	0.000	0.000	0.000
56	A	140	ALA	0	-0.072	0.117	32.712	0.000	0.000	0.000	0.000	0.000	0.000
57	A	141	ASN	0	0.010	-0.126	33.651	-0.008	-0.008	0.000	0.000	0.000	0.000
58	A	141	ASN	0	-0.138	0.041	36.130	-0.004	-0.004	0.000	0.000	0.000	0.000
59	A	142	ASN	0	0.099	-0.071	30.857	-0.007	-0.007	0.000	0.000	0.000	0.000
60	A	142	ASN	0	-0.086	0.059	27.683	-0.002	-0.002	0.000	0.000	0.000	0.000
61	A	143	ALA	0	0.086	-0.113	29.254	-0.004	-0.004	0.000	0.000	0.000	0.000
62	A	143	ALA	0	-0.034	0.139	30.366	0.000	0.000	0.000	0.000	0.000	0.000
63	A	144	LYS	0	0.069	-0.090	30.160	-0.012	-0.012	0.000	0.000	0.000	0.000
64	A	144	LYS	1	0.783	1.052	34.392	0.026	0.026	0.000	0.000	0.000	0.000
65	A	145	ALA	0	0.096	-0.103	31.363	-0.011	-0.011	0.000	0.000	0.000	0.000
66	A	145	ALA	0	-0.074	0.112	30.935	0.002	0.002	0.000	0.000	0.000	0.000
67	A	146	VAL	0	0.062	-0.095	26.973	-0.007	-0.007	0.000	0.000	0.000	0.000
68	A	146	VAL	0	-0.093	0.103	24.988	0.000	0.000	0.000	0.000	0.000	0.000
69	A	147	VAL	0	0.126	-0.088	27.057	-0.015	-0.015	0.000	0.000	0.000	0.000
70	A	147	VAL	0	-0.091	0.112	28.862	0.000	0.000	0.000	0.000	0.000	0.000
71	A	148	LYS	0	0.080	-0.084	28.872	-0.015	-0.015	0.000	0.000	0.000	0.000
72	A	148	LYS	1	0.871	1.051	31.496	0.044	0.044	0.000	0.000	0.000	0.000
73	A	149	THR	0	0.049	-0.053	27.112	-0.010	-0.010	0.000	0.000	0.000	0.000
74	A	149	THR	0	-0.071	0.040	25.285	0.004	0.004	0.000	0.000	0.000	0.000
75	A	150	PHE	0	0.072	-0.065	24.738	-0.008	-0.008	0.000	0.000	0.000	0.000
76	A	150	PHE	0	-0.099	0.070	20.631	-0.003	-0.003	0.000	0.000	0.000	0.000
77	A	151	HIS	0	0.105	-0.044	25.642	-0.022	-0.022	0.000	0.000	0.000	0.000
78	A	151	HIS	0	-0.089	0.059	27.897	-0.007	-0.007	0.000	0.000	0.000	0.000
79	A	152	GLU	0	0.062	-0.119	28.668	-0.013	-0.013	0.000	0.000	0.000	0.000
80	A	152	GLU	-1	-0.959	-0.853	29.507	-0.093	-0.093	0.000	0.000	0.000	0.000
81	A	153	THR	0	0.005	-0.084	24.873	-0.005	-0.005	0.000	0.000	0.000	0.000
82	A	153	THR	0	-0.086	0.023	23.071	0.004	0.004	0.000	0.000	0.000	0.000
83	A	154	LEU	0	-0.015	-0.104	24.040	-0.015	-0.015	0.000	0.000	0.000	0.000
84	A	154	LEU	0	-0.073	0.078	20.927	-0.005	-0.005	0.000	0.000	0.000	0.000
85	A	155	ASP	0	0.175	-0.060	24.784	-0.018	-0.018	0.000	0.000	0.000	0.000
86	A	155	ASP	-1	-0.986	-0.830	27.417	-0.175	-0.175	0.000	0.000	0.000	0.000
87	A	156	CYS	0	0.074	-0.095	27.277	-0.014	-0.014	0.000	0.000	0.000	0.000
88	A	156	CYS	0	-0.322	0.189	23.830	0.005	0.005	0.000	0.000	0.000	0.000
89	A	157	CYS	0	0.164	-0.102	28.646	0.012	0.012	0.000	0.000	0.000	0.000
90	A	157	CYS	0	-0.228	0.213	32.669	0.003	0.003	0.000	0.000	0.000	0.000
91	A	158	GLY	0	0.077	-0.100	29.126	0.009	0.009	0.000	0.000	0.000	0.000
92	A	159	SER	0	0.102	0.031	27.163	-0.018	-0.018	0.000	0.000	0.000	0.000
93	A	159	SER	0	-0.062	0.055	26.787	-0.001	-0.001	0.000	0.000	0.000	0.000
94	A	160	SER	0	-0.008	-0.091	27.391	0.020	0.020	0.000	0.000	0.000	0.000
95	A	160	SER	0	-0.075	0.028	26.361	-0.004	-0.004	0.000	0.000	0.000	0.000
96	A	161	THR	0	-0.054	-0.097	28.052	0.006	0.006	0.000	0.000	0.000	0.000
97	A	161	THR	0	-0.009	0.082	26.458	-0.008	-0.008	0.000	0.000	0.000	0.000
98	A	162	LEU	0	0.015	-0.101	29.226	0.009	0.009	0.000	0.000	0.000	0.000
99	A	162	LEU	0	-0.050	0.107	28.416	0.002	0.002	0.000	0.000	0.000	0.000
100	A	163	THR	0	0.145	-0.058	31.483	0.007	0.007	0.000	0.000	0.000	0.000
101	A	163	THR	0	-0.045	0.069	32.239	0.003	0.003	0.000	0.000	0.000	0.000
102	A	164	ALA	0	0.125	-0.069	33.881	0.002	0.002	0.000	0.000	0.000	0.000
103	A	164	ALA	0	-0.077	0.102	36.667	0.001	0.001	0.000	0.000	0.000	0.000
104	A	165	LEU	0	0.055	-0.112	34.548	0.006	0.006	0.000	0.000	0.000	0.000
105	A	165	LEU	0	-0.018	0.133	32.762	0.000	0.000	0.000	0.000	0.000	0.000
106	A	166	THR	0	0.028	-0.060	33.048	0.009	0.009	0.000	0.000	0.000	0.000
107	A	166	THR	0	-0.016	0.080	32.305	0.000	0.000	0.000	0.000	0.000	0.000
108	A	167	THR	0	0.044	-0.095	34.266	0.000	0.000	0.000	0.000	0.000	0.000
109	A	167	THR	0	-0.065	0.061	37.318	0.000	0.000	0.000	0.000	0.000	0.000
110	A	168	SER	0	-0.013	-0.087	37.798	0.002	0.002	0.000	0.000	0.000	0.000
111	A	168	SER	0	-0.037	0.060	37.475	0.003	0.003	0.000	0.000	0.000	0.000
112	A	169	VAL	0	0.102	-0.084	34.704	0.008	0.008	0.000	0.000	0.000	0.000
113	A	169	VAL	0	-0.088	0.106	32.737	0.000	0.000	0.000	0.000	0.000	0.000
114	A	170	LEU	0	0.150	-0.096	36.212	0.004	0.004	0.000	0.000	0.000	0.000
115	A	170	LEU	0	-0.107	0.090	36.610	0.000	0.000	0.000	0.000	0.000	0.000
116	A	171	LYS	0	0.021	-0.103	37.286	0.002	0.002	0.000	0.000	0.000	0.000
117	A	171	LYS	1	0.867	1.062	41.111	0.068	0.068	0.000	0.000	0.000	0.000
118	A	172	ASN	0	0.070	-0.055	39.109	0.004	0.004	0.000	0.000	0.000	0.000
119	A	172	ASN	0	-0.149	0.025	38.249	0.005	0.005	0.000	0.000	0.000	0.000
120	A	173	ASN	0	0.049	-0.080	39.086	0.003	0.003	0.000	0.000	0.000	0.000
121	A	173	ASN	0	-0.118	0.061	39.987	-0.001	-0.001	0.000	0.000	0.000	0.000
122	A	174	LEU	0	0.026	-0.109	34.871	0.004	0.004	0.000	0.000	0.000	0.000
123	A	174	LEU	0	-0.060	0.088	33.864	0.001	0.001	0.000	0.000	0.000	0.000
124	A	175	CYS	0	0.065	-0.105	33.152	-0.006	-0.006	0.000	0.000	0.000	0.000
125	A	176	PRO	0	0.129	-0.014	31.371	0.009	0.009	0.000	0.000	0.000	0.000
126	A	177	SER	0	-0.012	0.005	34.286	-0.002	-0.002	0.000	0.000	0.000	0.000
127	A	177	SER	0	-0.042	0.090	36.401	0.002	0.002	0.000	0.000	0.000	0.000
128	A	178	GLY	0	0.066	-0.093	37.884	0.000	0.000	0.000	0.000	0.000	0.000
129	A	179	SER	0	-0.016	0.008	39.638	0.005	0.005	0.000	0.000	0.000	0.000
130	A	179	SER	0	-0.051	0.070	39.715	-0.002	-0.002	0.000	0.000	0.000	0.000
131	A	180	ASN	0	0.066	-0.097	37.123	0.000	0.000	0.000	0.000	0.000	0.000
132	A	180	ASN	0	-0.086	0.072	34.784	0.006	0.006	0.000	0.000	0.000	0.000
133	A	181	ILE	0	0.035	-0.126	38.653	0.003	0.003	0.000	0.000	0.000	0.000
134	A	181	ILE	0	-0.114	0.098	41.826	0.002	0.002	0.000	0.000	0.000	0.000
135	A	182	ILE	0	0.168	-0.030	38.665	-0.002	-0.002	0.000	0.000	0.000	0.000
136	A	182	ILE	0	-0.103	0.052	39.221	0.001	0.001	0.000	0.000	0.000	0.000
137	A	183	SER	0	0.017	-0.083	37.016	-0.005	-0.005	0.000	0.000	0.000	0.000
138	A	183	SER	0	-0.047	0.061	37.577	-0.001	-0.001	0.000	0.000	0.000	0.000
139	A	184	ASN	0	0.034	-0.061	36.641	0.004	0.004	0.000	0.000	0.000	0.000
140	A	184	ASN	0	-0.105	0.064	35.870	0.001	0.001	0.000	0.000	0.000	0.000
141	A	185	LEU	0	0.163	-0.096	33.750	-0.010	-0.010	0.000	0.000	0.000	0.000
142	A	185	LEU	0	-0.077	0.103	33.858	0.001	0.001	0.000	0.000	0.000	0.000
143	A	186	PHE	0	0.155	-0.058	31.954	-0.007	-0.007	0.000	0.000	0.000	0.000
144	A	186	PHE	0	-0.090	0.073	32.803	0.002	0.002	0.000	0.000	0.000	0.000
145	A	187	LYS	0	0.004	-0.141	30.693	-0.016	-0.016	0.000	0.000	0.000	0.000
146	A	187	LYS	1	0.808	1.023	32.153	0.136	0.136	0.000	0.000	0.000	0.000
147	A	188	GLU	0	0.014	-0.068	29.562	-0.016	-0.016	0.000	0.000	0.000	0.000
148	A	188	GLU	-1	-0.834	-0.785	30.943	-0.124	-0.124	0.000	0.000	0.000	0.000
149	A	189	ASP	0	0.169	-0.067	27.152	0.011	0.011	0.000	0.000	0.000	0.000
150	A	189	ASP	-1	-0.856	-0.765	25.957	-0.236	-0.236	0.000	0.000	0.000	0.000
151	A	190	CYS	0	0.119	-0.136	24.441	-0.026	-0.026	0.000	0.000	0.000	0.000
152	A	191	HIS	0	0.113	-0.055	21.575	-0.025	-0.025	0.000	0.000	0.000	0.000
153	A	191	HIS	1	0.688	0.908	22.108	0.227	0.227	0.000	0.000	0.000	0.000
154	A	192	GLN	0	0.157	-0.052	20.461	-0.048	-0.048	0.000	0.000	0.000	0.000
155	A	192	GLN	0	-0.130	0.068	21.236	0.008	0.008	0.000	0.000	0.000	0.000
156	A	193	LYS	0	0.067	-0.107	20.617	-0.053	-0.053	0.000	0.000	0.000	0.000
157	A	193	LYS	1	0.732	1.004	22.893	0.227	0.227	0.000	0.000	0.000	0.000
158	A	194	ILE	0	0.106	-0.073	18.670	-0.015	-0.015	0.000	0.000	0.000	0.000
159	A	194	ILE	0	-0.091	0.081	17.044	0.000	0.000	0.000	0.000	0.000	0.000
160	A	195	ASP	0	0.091	-0.106	16.208	-0.066	-0.066	0.000	0.000	0.000	0.000
161	A	195	ASP	-1	-0.887	-0.785	16.724	-0.549	-0.549	0.000	0.000	0.000	0.000
162	A	196	ASP	0	0.088	-0.110	16.060	-0.121	-0.121	0.000	0.000	0.000	0.000
163	A	196	ASP	-1	-0.916	-0.809	19.935	-0.405	-0.405	0.000	0.000	0.000	0.000
164	A	197	LEU	0	0.060	-0.102	16.906	-0.037	-0.037	0.000	0.000	0.000	0.000
165	A	197	LEU	0	-0.083	0.113	15.925	0.009	0.009	0.000	0.000	0.000	0.000
166	A	198	PHE	0	0.001	-0.099	12.810	-0.014	-0.014	0.000	0.000	0.000	0.000
167	A	198	PHE	0	-0.084	0.082	11.651	-0.008	-0.008	0.000	0.000	0.000	0.000
168	A	199	SER	0	-0.008	-0.101	11.700	-0.260	-0.260	0.000	0.000	0.000	0.000
169	A	199	SER	0	-0.070	0.039	14.253	-0.046	-0.046	0.000	0.000	0.000	0.000
170	A	200	GLY	0	0.037	-0.086	13.899	0.016	0.016	0.000	0.000	0.000	0.000
171	A	201	LYS	0	0.128	0.054	15.554	0.016	0.016	0.000	0.000	0.000	0.000
172	A	201	LYS	1	0.741	1.000	16.526	0.665	0.665	0.000	0.000	0.000	0.000
173	A	202	HIS	0	-0.129	-0.161	19.219	0.049	0.049	0.000	0.000	0.000	0.000
174	A	202	HIS	0	0.054	0.036	19.439	0.027	0.027	0.000	0.000	0.000	0.000

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