FMO DATABASE

FMODB ID: JY369

Calculation Name: 2X83-B-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2X83

Chain ID: B

ChEMBL ID:

UniProt ID: B0ZE32

Base Structure: X-ray

Registration Date: 2025-10-04

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	163
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1632386.470635
FMO2-HF: Nuclear repulsion	1569407.646336
FMO2-HF: Total energy	-62978.824299
FMO2-MP2: Total energy	-63160.074131

3D Structure Molmil

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:VAL)

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

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.
10.635	13.746	1.214	-1.405	-2.921	-0.004

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.858 / q_NPA : 0.919

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	4	PRO	0	0.022	0.031	3.713	-5.327	-3.737	0.003	-0.642	-0.950	0.001
25	A	26	ALA	0	0.055	0.010	3.576	2.668	2.872	0.003	-0.038	-0.170	0.000
26	A	27	ASP	-1	-0.856	-0.932	2.359	-44.193	-43.043	1.206	-0.692	-1.665	-0.005
27	A	28	LYS	1	0.788	0.889	4.260	38.745	38.912	0.002	-0.033	-0.136	0.000
4	A	5	THR	0	-0.007	-0.007	5.807	3.670	3.670	0.000	0.000	0.000	0.000
5	A	6	VAL	0	0.002	0.013	8.636	0.797	0.797	0.000	0.000	0.000	0.000
6	A	7	PHE	0	-0.011	-0.008	12.179	0.220	0.220	0.000	0.000	0.000	0.000
7	A	8	PHE	0	0.008	-0.009	15.634	0.409	0.409	0.000	0.000	0.000	0.000
8	A	9	ASP	-1	-0.774	-0.847	19.274	-15.061	-15.061	0.000	0.000	0.000	0.000
9	A	10	ILE	0	-0.014	-0.019	22.201	0.353	0.353	0.000	0.000	0.000	0.000
10	A	11	ALA	0	0.041	0.020	24.911	0.214	0.214	0.000	0.000	0.000	0.000
11	A	12	VAL	0	-0.035	-0.020	28.623	-0.063	-0.063	0.000	0.000	0.000	0.000
12	A	13	ASP	-1	-0.838	-0.917	31.860	-8.630	-8.630	0.000	0.000	0.000	0.000
13	A	14	GLY	0	-0.014	0.001	32.022	0.221	0.221	0.000	0.000	0.000	0.000
14	A	15	GLU	-1	-0.879	-0.933	31.844	-9.332	-9.332	0.000	0.000	0.000	0.000
15	A	16	PRO	0	-0.036	-0.023	27.840	-0.305	-0.305	0.000	0.000	0.000	0.000
16	A	17	LEU	0	-0.040	-0.013	27.258	0.226	0.226	0.000	0.000	0.000	0.000
17	A	18	GLY	0	0.030	0.001	24.887	0.068	0.068	0.000	0.000	0.000	0.000
18	A	19	ARG	1	0.820	0.884	17.197	16.509	16.509	0.000	0.000	0.000	0.000
19	A	20	VAL	0	-0.031	-0.009	17.743	0.120	0.120	0.000	0.000	0.000	0.000
20	A	21	SER	0	-0.001	-0.006	13.541	-0.783	-0.783	0.000	0.000	0.000	0.000
21	A	22	PHE	0	0.019	-0.005	12.797	0.889	0.889	0.000	0.000	0.000	0.000
22	A	23	GLU	-1	-0.803	-0.882	6.051	-40.876	-40.876	0.000	0.000	0.000	0.000
23	A	24	LEU	0	0.012	-0.002	8.002	3.241	3.241	0.000	0.000	0.000	0.000
24	A	25	PHE	0	-0.020	-0.006	5.770	-5.865	-5.865	0.000	0.000	0.000	0.000
28	A	29	VAL	0	-0.017	0.009	7.737	2.575	2.575	0.000	0.000	0.000	0.000
29	A	30	PRO	0	0.036	0.026	6.273	-0.604	-0.604	0.000	0.000	0.000	0.000
30	A	31	LYS	1	0.863	0.928	7.640	16.541	16.541	0.000	0.000	0.000	0.000
31	A	32	THR	0	-0.004	-0.036	11.324	1.487	1.487	0.000	0.000	0.000	0.000
32	A	33	ALA	0	-0.023	-0.006	7.792	0.579	0.579	0.000	0.000	0.000	0.000
33	A	34	GLU	-1	-0.802	-0.881	9.456	-24.775	-24.775	0.000	0.000	0.000	0.000
34	A	35	ASN	0	0.003	-0.006	10.563	1.842	1.842	0.000	0.000	0.000	0.000
35	A	36	PHE	0	0.042	0.013	12.956	0.809	0.809	0.000	0.000	0.000	0.000
36	A	37	ARG	1	0.773	0.841	9.011	26.292	26.292	0.000	0.000	0.000	0.000
37	A	38	ALA	0	0.005	0.006	12.571	0.995	0.995	0.000	0.000	0.000	0.000
38	A	39	LEU	0	-0.049	-0.018	15.067	1.328	1.328	0.000	0.000	0.000	0.000
39	A	40	SER	0	-0.009	-0.023	15.195	1.220	1.220	0.000	0.000	0.000	0.000
40	A	41	THR	0	-0.025	-0.032	14.159	0.729	0.729	0.000	0.000	0.000	0.000
41	A	42	GLY	0	-0.003	0.018	17.153	0.809	0.809	0.000	0.000	0.000	0.000
42	A	43	GLU	-1	-0.770	-0.845	14.722	-20.321	-20.321	0.000	0.000	0.000	0.000
43	A	44	LYS	1	0.837	0.917	14.835	19.068	19.068	0.000	0.000	0.000	0.000
44	A	45	GLY	0	0.016	0.018	20.808	0.629	0.629	0.000	0.000	0.000	0.000
45	A	46	PHE	0	-0.040	-0.038	21.269	0.702	0.702	0.000	0.000	0.000	0.000
46	A	47	GLY	0	0.033	0.005	21.108	-0.764	-0.764	0.000	0.000	0.000	0.000
47	A	48	TYR	0	-0.064	-0.036	17.104	0.676	0.676	0.000	0.000	0.000	0.000
48	A	49	LYS	1	0.907	0.966	22.346	13.719	13.719	0.000	0.000	0.000	0.000
49	A	50	GLY	0	0.003	0.008	24.188	0.400	0.400	0.000	0.000	0.000	0.000
50	A	51	SER	0	-0.106	-0.056	24.596	0.403	0.403	0.000	0.000	0.000	0.000
51	A	52	CYS	0	-0.012	-0.014	27.036	-0.131	-0.131	0.000	0.000	0.000	0.000
52	A	53	PHE	0	0.008	-0.015	21.584	-0.348	-0.348	0.000	0.000	0.000	0.000
53	A	54	HIS	0	-0.014	-0.008	27.039	0.549	0.549	0.000	0.000	0.000	0.000
54	A	55	ARG	1	0.910	0.964	28.731	10.799	10.799	0.000	0.000	0.000	0.000
55	A	56	ILE	0	0.030	0.015	27.753	-0.454	-0.454	0.000	0.000	0.000	0.000
56	A	57	ILE	0	-0.014	0.005	28.987	0.493	0.493	0.000	0.000	0.000	0.000
57	A	58	PRO	0	0.014	0.002	29.280	-0.302	-0.302	0.000	0.000	0.000	0.000
58	A	59	GLY	0	0.003	0.008	29.122	-0.317	-0.317	0.000	0.000	0.000	0.000
59	A	60	PHE	0	-0.035	-0.012	26.703	0.041	0.041	0.000	0.000	0.000	0.000
60	A	61	MET	0	0.012	0.016	23.924	-0.600	-0.600	0.000	0.000	0.000	0.000
61	A	62	CYS	0	-0.012	0.015	23.839	0.661	0.661	0.000	0.000	0.000	0.000
62	A	63	GLN	0	0.064	0.018	23.413	-0.454	-0.454	0.000	0.000	0.000	0.000
63	A	64	GLY	0	0.013	0.001	23.725	0.473	0.473	0.000	0.000	0.000	0.000
64	A	65	GLY	0	0.051	0.027	22.172	-0.264	-0.264	0.000	0.000	0.000	0.000
65	A	66	ASP	-1	-0.761	-0.873	23.113	-10.891	-10.891	0.000	0.000	0.000	0.000
66	A	67	PHE	0	0.044	0.005	21.714	0.362	0.362	0.000	0.000	0.000	0.000
67	A	68	THR	0	-0.035	-0.007	26.746	0.088	0.088	0.000	0.000	0.000	0.000
68	A	69	HIS	0	-0.058	-0.046	29.320	0.338	0.338	0.000	0.000	0.000	0.000
69	A	70	HIS	0	-0.036	-0.005	29.165	0.151	0.151	0.000	0.000	0.000	0.000
70	A	71	ASN	0	0.017	0.016	30.794	-0.040	-0.040	0.000	0.000	0.000	0.000
71	A	72	GLY	0	-0.001	0.006	28.820	0.142	0.142	0.000	0.000	0.000	0.000
72	A	73	THR	0	-0.037	-0.032	29.609	-0.090	-0.090	0.000	0.000	0.000	0.000
73	A	74	GLY	0	0.001	0.017	29.113	0.070	0.070	0.000	0.000	0.000	0.000
74	A	75	GLY	0	0.001	-0.007	25.004	-0.308	-0.308	0.000	0.000	0.000	0.000
75	A	76	LYS	1	0.831	0.919	23.380	12.390	12.390	0.000	0.000	0.000	0.000
76	A	77	SER	0	0.015	-0.006	18.927	-0.451	-0.451	0.000	0.000	0.000	0.000
77	A	78	ILE	0	-0.033	-0.027	14.470	0.629	0.629	0.000	0.000	0.000	0.000
78	A	79	TYR	0	-0.041	-0.043	13.259	-0.078	-0.078	0.000	0.000	0.000	0.000
79	A	80	GLY	0	-0.017	0.010	19.872	0.378	0.378	0.000	0.000	0.000	0.000
80	A	81	GLU	-1	-0.906	-0.937	22.432	-11.678	-11.678	0.000	0.000	0.000	0.000
81	A	82	LYS	1	0.838	0.933	22.248	11.125	11.125	0.000	0.000	0.000	0.000
82	A	83	PHE	0	0.008	0.001	15.433	0.111	0.111	0.000	0.000	0.000	0.000
83	A	84	GLU	-1	-0.751	-0.872	16.604	-16.020	-16.020	0.000	0.000	0.000	0.000
84	A	85	ASP	-1	-0.828	-0.912	17.890	-14.440	-14.440	0.000	0.000	0.000	0.000
85	A	86	GLU	-1	-0.778	-0.857	11.034	-22.632	-22.632	0.000	0.000	0.000	0.000
86	A	87	ASN	0	-0.006	-0.025	11.701	0.011	0.011	0.000	0.000	0.000	0.000
87	A	88	PHE	0	0.012	0.002	15.852	-0.205	-0.205	0.000	0.000	0.000	0.000
88	A	89	ILE	0	0.006	0.014	12.665	0.594	0.594	0.000	0.000	0.000	0.000
89	A	90	LEU	0	-0.078	-0.027	9.615	0.023	0.023	0.000	0.000	0.000	0.000
90	A	91	LYS	1	0.985	0.996	14.171	16.261	16.261	0.000	0.000	0.000	0.000
91	A	92	HIS	0	0.003	-0.014	16.717	-0.954	-0.954	0.000	0.000	0.000	0.000
92	A	93	THR	0	-0.035	-0.028	16.407	0.766	0.766	0.000	0.000	0.000	0.000
93	A	94	GLY	0	0.026	0.015	19.235	0.625	0.625	0.000	0.000	0.000	0.000
94	A	95	PRO	0	0.014	0.006	19.877	-0.421	-0.421	0.000	0.000	0.000	0.000
95	A	96	GLY	0	0.056	0.017	18.198	-0.540	-0.540	0.000	0.000	0.000	0.000
96	A	97	ILE	0	-0.053	-0.011	14.648	-1.241	-1.241	0.000	0.000	0.000	0.000
97	A	98	LEU	0	-0.022	0.009	13.414	1.146	1.146	0.000	0.000	0.000	0.000
98	A	99	SER	0	0.020	-0.020	14.911	-1.072	-1.072	0.000	0.000	0.000	0.000
99	A	100	MET	0	0.012	0.018	16.305	0.231	0.231	0.000	0.000	0.000	0.000
100	A	101	ALA	0	-0.055	-0.030	18.882	0.520	0.520	0.000	0.000	0.000	0.000
101	A	102	ASN	0	-0.056	-0.034	21.776	0.830	0.830	0.000	0.000	0.000	0.000
102	A	103	ALA	0	0.020	0.009	23.726	0.292	0.292	0.000	0.000	0.000	0.000
103	A	104	GLY	0	0.009	0.017	26.239	0.457	0.457	0.000	0.000	0.000	0.000
104	A	105	PRO	0	-0.001	-0.002	24.222	-0.403	-0.403	0.000	0.000	0.000	0.000
105	A	106	ASN	0	-0.024	-0.011	21.779	-0.174	-0.174	0.000	0.000	0.000	0.000
106	A	107	THR	0	0.012	0.002	22.882	0.161	0.161	0.000	0.000	0.000	0.000
107	A	108	ASN	0	-0.064	-0.045	18.567	0.279	0.279	0.000	0.000	0.000	0.000
108	A	109	GLY	0	0.050	0.009	20.711	0.196	0.196	0.000	0.000	0.000	0.000
109	A	110	SER	0	-0.008	-0.003	19.307	-0.565	-0.565	0.000	0.000	0.000	0.000
110	A	111	GLN	0	-0.026	-0.012	20.374	-0.434	-0.434	0.000	0.000	0.000	0.000
111	A	112	PHE	0	0.012	0.023	18.497	-0.355	-0.355	0.000	0.000	0.000	0.000
112	A	113	PHE	0	-0.018	-0.025	20.013	0.788	0.788	0.000	0.000	0.000	0.000
113	A	114	ILE	0	0.032	0.028	18.721	-0.878	-0.878	0.000	0.000	0.000	0.000
114	A	115	CYS	0	-0.030	0.000	19.895	0.696	0.696	0.000	0.000	0.000	0.000
115	A	116	THR	0	-0.042	-0.055	21.789	-0.377	-0.377	0.000	0.000	0.000	0.000
116	A	117	ALA	0	0.002	0.003	24.327	0.405	0.405	0.000	0.000	0.000	0.000
117	A	118	LYS	1	0.850	0.925	21.847	12.540	12.540	0.000	0.000	0.000	0.000
118	A	119	THR	0	-0.002	-0.008	22.781	0.351	0.351	0.000	0.000	0.000	0.000
119	A	120	GLU	-1	-0.795	-0.915	22.885	-12.018	-12.018	0.000	0.000	0.000	0.000
120	A	121	TRP	0	-0.014	0.003	23.972	-0.172	-0.172	0.000	0.000	0.000	0.000
121	A	122	LEU	0	-0.067	-0.028	22.708	0.304	0.304	0.000	0.000	0.000	0.000
122	A	123	ASP	-1	-0.744	-0.871	20.331	-14.777	-14.777	0.000	0.000	0.000	0.000
123	A	124	GLY	0	-0.040	-0.020	20.776	0.548	0.548	0.000	0.000	0.000	0.000
124	A	125	LYS	1	0.916	0.963	22.456	10.907	10.907	0.000	0.000	0.000	0.000
125	A	126	HIS	1	0.852	0.938	20.456	13.090	13.090	0.000	0.000	0.000	0.000
126	A	127	VAL	0	0.022	0.035	14.177	-0.150	-0.150	0.000	0.000	0.000	0.000
127	A	128	VAL	0	0.018	0.015	13.024	-0.254	-0.254	0.000	0.000	0.000	0.000
128	A	129	PHE	0	0.009	-0.017	11.227	-0.740	-0.740	0.000	0.000	0.000	0.000
129	A	130	GLY	0	0.038	0.010	10.179	-2.816	-2.816	0.000	0.000	0.000	0.000
130	A	131	LYS	1	0.836	0.929	9.564	29.839	29.839	0.000	0.000	0.000	0.000
131	A	132	VAL	0	-0.006	-0.008	12.639	-1.406	-1.406	0.000	0.000	0.000	0.000
132	A	133	LYS	1	0.854	0.936	8.846	30.384	30.384	0.000	0.000	0.000	0.000
133	A	134	GLU	-1	-0.851	-0.920	13.719	-19.426	-19.426	0.000	0.000	0.000	0.000
134	A	135	GLY	0	0.054	0.013	16.487	-0.043	-0.043	0.000	0.000	0.000	0.000
135	A	136	MET	0	0.032	0.023	18.837	0.423	0.423	0.000	0.000	0.000	0.000
136	A	137	ASN	0	0.002	-0.004	21.000	0.375	0.375	0.000	0.000	0.000	0.000
137	A	138	ILE	0	-0.003	0.015	22.744	0.612	0.612	0.000	0.000	0.000	0.000
138	A	139	VAL	0	0.053	0.018	20.801	0.409	0.409	0.000	0.000	0.000	0.000
139	A	140	GLU	-1	-0.850	-0.922	24.137	-11.258	-11.258	0.000	0.000	0.000	0.000
140	A	141	ALA	0	-0.007	0.004	26.853	0.592	0.592	0.000	0.000	0.000	0.000
141	A	142	MET	0	-0.008	-0.002	23.821	0.278	0.278	0.000	0.000	0.000	0.000
142	A	143	LYS	1	0.809	0.899	27.118	11.808	11.808	0.000	0.000	0.000	0.000
143	A	144	ARG	1	0.854	0.930	29.515	10.451	10.451	0.000	0.000	0.000	0.000
144	A	145	PHE	0	0.006	0.009	31.142	0.380	0.380	0.000	0.000	0.000	0.000
145	A	146	GLY	0	0.042	0.031	32.265	0.046	0.046	0.000	0.000	0.000	0.000
146	A	147	SER	0	0.010	0.005	33.075	0.227	0.227	0.000	0.000	0.000	0.000
147	A	148	ARG	1	0.993	0.978	34.245	7.805	7.805	0.000	0.000	0.000	0.000
148	A	149	ASN	0	-0.048	-0.038	35.353	0.070	0.070	0.000	0.000	0.000	0.000
149	A	150	GLY	0	0.037	0.016	32.644	-0.135	-0.135	0.000	0.000	0.000	0.000
150	A	151	LYS	1	0.965	1.000	32.840	7.796	7.796	0.000	0.000	0.000	0.000
151	A	152	THR	0	-0.018	-0.015	31.459	0.116	0.116	0.000	0.000	0.000	0.000
152	A	153	SER	0	-0.052	-0.032	34.625	0.182	0.182	0.000	0.000	0.000	0.000
153	A	154	LYS	1	0.913	0.951	35.019	8.847	8.847	0.000	0.000	0.000	0.000
154	A	155	LYS	1	0.946	0.983	32.167	9.597	9.597	0.000	0.000	0.000	0.000
155	A	156	ILE	0	0.012	0.016	27.731	-0.126	-0.126	0.000	0.000	0.000	0.000
156	A	157	THR	0	-0.051	-0.049	27.790	0.021	0.021	0.000	0.000	0.000	0.000
157	A	158	ILE	0	0.035	0.030	21.575	-0.161	-0.161	0.000	0.000	0.000	0.000
158	A	159	ALA	0	0.000	0.005	24.574	0.203	0.203	0.000	0.000	0.000	0.000
159	A	160	ASP	-1	-0.816	-0.910	22.054	-14.029	-14.029	0.000	0.000	0.000	0.000
160	A	161	CYS	0	-0.105	-0.047	18.457	0.029	0.029	0.000	0.000	0.000	0.000
161	A	162	GLY	0	0.068	0.046	16.118	0.528	0.528	0.000	0.000	0.000	0.000
162	A	163	GLN	0	-0.013	-0.011	8.223	0.919	0.919	0.000	0.000	0.000	0.000
163	A	164	LEU	-1	-0.934	-0.963	8.927	-29.749	-29.749	0.000	0.000	0.000	0.000

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