FMO DATABASE

FMODB ID: 97JR2

Calculation Name: 6XOD-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 6XOD

Chain ID: A

ChEMBL ID:

UniProt ID:

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	154
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1485346.901588
FMO2-HF: Nuclear repulsion	1423445.20016
FMO2-HF: Total energy	-61901.701428
FMO2-MP2: Total energy	-62078.779538

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:1:MET)

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

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.
-46.458	-39.225	21.92	-12.755	-16.396	-0.051

Interaction energy analysis for fragmet #1(A:1:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.927 / q_NPA : 0.988

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	3	ALA	0	0.049	0.018	3.555	5.477	7.156	0.014	-0.562	-1.131	0.001
4	A	4	SER	0	0.013	0.012	2.809	7.384	9.318	0.154	-0.739	-1.349	-0.004
5	A	5	ARG	1	0.970	0.963	2.217	37.384	32.970	14.349	-4.741	-5.195	0.039
6	A	6	ALA	0	0.003	0.005	6.363	4.367	4.413	-0.001	-0.003	-0.042	0.000
35	A	35	PHE	0	0.010	-0.003	2.368	-3.814	-2.542	1.153	-0.533	-1.891	-0.006
62	A	62	GLU	-1	-0.845	-0.950	2.452	-82.234	-78.998	4.997	-3.652	-4.581	-0.048
63	A	63	PRO	0	-0.048	-0.035	2.318	-31.989	-28.564	1.255	-2.520	-2.159	-0.033
64	A	64	TYR	0	-0.049	-0.002	4.522	5.913	5.968	-0.001	-0.005	-0.048	0.000
7	A	7	ARG	1	0.738	0.845	7.766	27.754	27.754	0.000	0.000	0.000	0.000
8	A	8	LEU	0	0.015	0.000	7.012	2.790	2.790	0.000	0.000	0.000	0.000
9	A	9	PHE	0	0.028	0.013	10.217	2.602	2.602	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.810	0.904	12.081	20.859	20.859	0.000	0.000	0.000	0.000
11	A	11	GLU	-1	-0.685	-0.819	12.743	-21.409	-21.409	0.000	0.000	0.000	0.000
12	A	12	TYR	0	0.016	0.013	13.829	0.833	0.833	0.000	0.000	0.000	0.000
13	A	13	LYS	1	0.921	0.959	15.607	18.110	18.110	0.000	0.000	0.000	0.000
14	A	14	GLU	-1	-0.869	-0.935	17.502	-16.517	-16.517	0.000	0.000	0.000	0.000
15	A	15	VAL	0	0.006	0.003	18.090	0.612	0.612	0.000	0.000	0.000	0.000
16	A	16	GLN	0	-0.027	-0.001	18.175	0.775	0.775	0.000	0.000	0.000	0.000
17	A	17	ARG	1	0.837	0.930	21.802	13.020	13.020	0.000	0.000	0.000	0.000
18	A	18	GLU	-1	-0.860	-0.936	23.462	-12.926	-12.926	0.000	0.000	0.000	0.000
19	A	19	LYS	1	0.937	0.958	26.059	9.519	9.519	0.000	0.000	0.000	0.000
20	A	20	VAL	0	-0.037	-0.005	28.256	0.373	0.373	0.000	0.000	0.000	0.000
21	A	21	ALA	0	0.009	0.005	30.654	-0.006	-0.006	0.000	0.000	0.000	0.000
22	A	22	ASP	-1	-0.843	-0.928	31.949	-9.192	-9.192	0.000	0.000	0.000	0.000
23	A	23	PRO	0	0.004	0.026	28.330	-0.297	-0.297	0.000	0.000	0.000	0.000
24	A	24	ASP	-1	-0.874	-0.956	28.828	-10.165	-10.165	0.000	0.000	0.000	0.000
25	A	25	ILE	0	-0.086	-0.055	22.613	-0.244	-0.244	0.000	0.000	0.000	0.000
26	A	26	GLN	0	-0.016	0.001	21.874	0.569	0.569	0.000	0.000	0.000	0.000
27	A	27	LEU	0	-0.017	-0.009	16.974	-0.243	-0.243	0.000	0.000	0.000	0.000
28	A	28	ILE	0	0.008	0.010	18.056	0.339	0.339	0.000	0.000	0.000	0.000
29	A	29	CYS	0	-0.041	-0.015	12.454	-1.092	-1.092	0.000	0.000	0.000	0.000
30	A	30	ASP	-1	-0.763	-0.870	12.201	-17.314	-17.314	0.000	0.000	0.000	0.000
31	A	31	ASP	-1	-0.901	-0.941	13.205	-15.639	-15.639	0.000	0.000	0.000	0.000
32	A	32	THR	0	-0.095	-0.046	12.256	-0.176	-0.176	0.000	0.000	0.000	0.000
33	A	33	ASN	0	-0.043	-0.030	7.071	-3.604	-3.604	0.000	0.000	0.000	0.000
34	A	34	ILE	0	0.040	0.014	5.924	0.048	0.048	0.000	0.000	0.000	0.000
36	A	36	LYS	1	0.838	0.919	7.653	18.534	18.534	0.000	0.000	0.000	0.000
37	A	37	TRP	0	0.009	-0.011	10.555	1.037	1.037	0.000	0.000	0.000	0.000
38	A	38	THR	0	-0.014	-0.008	14.206	0.548	0.548	0.000	0.000	0.000	0.000
39	A	39	ALA	0	0.016	0.001	17.961	-0.228	-0.228	0.000	0.000	0.000	0.000
40	A	40	LEU	0	-0.002	0.013	20.903	0.328	0.328	0.000	0.000	0.000	0.000
41	A	41	ILE	0	0.006	-0.007	23.888	-0.008	-0.008	0.000	0.000	0.000	0.000
42	A	42	LYS	1	0.876	0.948	26.468	11.069	11.069	0.000	0.000	0.000	0.000
43	A	43	GLY	0	-0.001	-0.007	30.313	-0.186	-0.186	0.000	0.000	0.000	0.000
44	A	44	PRO	0	-0.026	-0.004	31.717	0.167	0.167	0.000	0.000	0.000	0.000
45	A	45	SER	0	0.030	0.018	34.103	0.073	0.073	0.000	0.000	0.000	0.000
46	A	46	GLU	-1	-0.958	-0.968	37.767	-7.619	-7.619	0.000	0.000	0.000	0.000
47	A	47	THR	0	-0.058	-0.042	35.815	-0.051	-0.051	0.000	0.000	0.000	0.000
48	A	48	PRO	0	-0.078	-0.034	37.801	0.073	0.073	0.000	0.000	0.000	0.000
49	A	49	TYR	0	-0.038	-0.060	33.721	-0.009	-0.009	0.000	0.000	0.000	0.000
50	A	50	GLU	-1	-0.821	-0.901	35.115	-8.230	-8.230	0.000	0.000	0.000	0.000
51	A	51	GLY	0	-0.008	-0.009	36.319	0.171	0.171	0.000	0.000	0.000	0.000
52	A	52	GLY	0	-0.015	0.004	33.808	-0.005	-0.005	0.000	0.000	0.000	0.000
53	A	53	VAL	0	-0.031	-0.024	28.119	-0.243	-0.243	0.000	0.000	0.000	0.000
54	A	54	PHE	0	-0.022	-0.028	27.595	-0.001	-0.001	0.000	0.000	0.000	0.000
55	A	55	GLN	0	-0.005	-0.004	23.624	-0.608	-0.608	0.000	0.000	0.000	0.000
56	A	56	LEU	0	0.008	0.003	20.652	-0.001	-0.001	0.000	0.000	0.000	0.000
57	A	57	ALA	0	-0.008	-0.009	17.685	-0.272	-0.272	0.000	0.000	0.000	0.000
58	A	58	PHE	0	0.025	-0.006	14.159	-0.161	-0.161	0.000	0.000	0.000	0.000
59	A	59	SER	0	-0.032	-0.011	11.433	-0.988	-0.988	0.000	0.000	0.000	0.000
60	A	60	VAL	0	0.012	0.003	8.242	0.316	0.316	0.000	0.000	0.000	0.000
61	A	61	PRO	0	0.012	0.023	7.634	-2.667	-2.667	0.000	0.000	0.000	0.000
65	A	65	PRO	0	-0.025	-0.035	5.522	-5.698	-5.698	0.000	0.000	0.000	0.000
66	A	66	LEU	0	0.016	-0.013	6.974	3.493	3.493	0.000	0.000	0.000	0.000
67	A	67	GLN	0	-0.010	-0.001	8.546	-0.745	-0.745	0.000	0.000	0.000	0.000
68	A	68	PRO	0	0.033	0.024	10.094	-1.571	-1.571	0.000	0.000	0.000	0.000
69	A	69	PRO	0	-0.033	-0.022	12.145	-1.453	-1.453	0.000	0.000	0.000	0.000
70	A	70	GLN	0	0.016	0.009	13.069	1.916	1.916	0.000	0.000	0.000	0.000
71	A	71	VAL	0	-0.016	-0.020	15.510	-0.332	-0.332	0.000	0.000	0.000	0.000
72	A	72	ARG	1	0.916	0.984	17.262	16.086	16.086	0.000	0.000	0.000	0.000
73	A	73	PHE	0	0.043	0.001	21.283	-0.266	-0.266	0.000	0.000	0.000	0.000
74	A	74	LEU	0	-0.072	-0.035	20.716	-0.132	-0.132	0.000	0.000	0.000	0.000
75	A	75	THR	0	-0.004	0.021	24.621	0.200	0.200	0.000	0.000	0.000	0.000
76	A	76	LYS	1	0.836	0.920	28.019	10.334	10.334	0.000	0.000	0.000	0.000
77	A	77	ILE	0	0.073	0.037	29.011	0.235	0.235	0.000	0.000	0.000	0.000
78	A	78	PHE	0	-0.010	-0.002	31.896	-0.099	-0.099	0.000	0.000	0.000	0.000
79	A	79	HIS	0	0.077	0.033	30.822	0.087	0.087	0.000	0.000	0.000	0.000
80	A	80	PRO	0	0.029	0.031	33.046	-0.139	-0.139	0.000	0.000	0.000	0.000
81	A	81	ASN	0	0.030	0.006	29.040	-0.008	-0.008	0.000	0.000	0.000	0.000
82	A	82	VAL	0	0.016	0.014	26.961	-0.587	-0.587	0.000	0.000	0.000	0.000
83	A	83	HIS	0	0.042	0.038	27.606	0.334	0.334	0.000	0.000	0.000	0.000
84	A	84	PHE	0	0.007	0.011	28.733	-0.206	-0.206	0.000	0.000	0.000	0.000
85	A	85	LYS	1	0.937	0.963	30.487	8.960	8.960	0.000	0.000	0.000	0.000
86	A	86	THR	0	0.001	-0.023	25.023	-0.105	-0.105	0.000	0.000	0.000	0.000
87	A	87	GLY	0	0.020	0.025	24.760	-0.337	-0.337	0.000	0.000	0.000	0.000
88	A	88	GLU	-1	-0.886	-0.954	21.340	-15.061	-15.061	0.000	0.000	0.000	0.000
89	A	89	ILE	0	0.031	0.014	22.304	0.644	0.644	0.000	0.000	0.000	0.000
90	A	90	CYS	0	-0.066	-0.017	23.481	-0.686	-0.686	0.000	0.000	0.000	0.000
91	A	91	LEU	0	0.046	0.031	22.003	0.393	0.393	0.000	0.000	0.000	0.000
92	A	92	ASP	-1	-0.815	-0.923	22.317	-13.729	-13.729	0.000	0.000	0.000	0.000
93	A	93	ILE	0	0.003	-0.003	19.373	-0.731	-0.731	0.000	0.000	0.000	0.000
94	A	94	LEU	0	-0.040	-0.016	17.499	-1.133	-1.133	0.000	0.000	0.000	0.000
95	A	95	LYS	1	0.852	0.925	17.402	12.884	12.884	0.000	0.000	0.000	0.000
96	A	96	ASN	0	-0.046	-0.030	18.006	-0.402	-0.402	0.000	0.000	0.000	0.000
97	A	97	ALA	0	0.031	0.022	19.850	-0.205	-0.205	0.000	0.000	0.000	0.000
98	A	98	TRP	0	-0.014	-0.008	11.677	0.521	0.521	0.000	0.000	0.000	0.000
99	A	99	SER	0	0.045	0.006	15.495	-0.022	-0.022	0.000	0.000	0.000	0.000
100	A	100	PRO	0	-0.002	0.001	11.672	-0.080	-0.080	0.000	0.000	0.000	0.000
101	A	101	ALA	0	0.000	0.009	13.272	-0.333	-0.333	0.000	0.000	0.000	0.000
102	A	102	TRP	0	0.003	0.021	15.857	0.814	0.814	0.000	0.000	0.000	0.000
103	A	103	THR	0	-0.029	0.000	14.479	-1.269	-1.269	0.000	0.000	0.000	0.000
104	A	104	LEU	0	0.044	0.025	12.790	0.874	0.874	0.000	0.000	0.000	0.000
105	A	105	GLN	0	0.049	0.022	16.327	0.634	0.634	0.000	0.000	0.000	0.000
106	A	106	SER	0	-0.044	-0.042	18.561	0.725	0.725	0.000	0.000	0.000	0.000
107	A	107	VAL	0	0.028	0.012	16.670	0.604	0.604	0.000	0.000	0.000	0.000
108	A	108	CYS	0	-0.023	-0.008	19.738	0.614	0.614	0.000	0.000	0.000	0.000
109	A	109	ARG	1	0.980	0.991	22.131	13.276	13.276	0.000	0.000	0.000	0.000
110	A	110	ALA	0	0.003	0.004	22.545	0.544	0.544	0.000	0.000	0.000	0.000
111	A	111	ILE	0	0.004	0.005	21.395	0.399	0.399	0.000	0.000	0.000	0.000
112	A	112	ILE	0	0.035	0.014	25.323	0.395	0.395	0.000	0.000	0.000	0.000
113	A	113	ALA	0	-0.022	-0.012	27.569	0.441	0.441	0.000	0.000	0.000	0.000
114	A	114	LEU	0	0.007	0.007	26.630	0.308	0.308	0.000	0.000	0.000	0.000
115	A	115	MET	0	-0.067	-0.021	29.292	0.194	0.194	0.000	0.000	0.000	0.000
116	A	116	ALA	0	0.006	0.002	31.436	0.339	0.339	0.000	0.000	0.000	0.000
117	A	117	HIS	0	-0.067	-0.020	32.451	0.429	0.429	0.000	0.000	0.000	0.000
118	A	118	PRO	0	-0.027	-0.017	32.337	-0.284	-0.284	0.000	0.000	0.000	0.000
119	A	119	GLU	-1	-0.857	-0.912	31.827	-9.060	-9.060	0.000	0.000	0.000	0.000
120	A	120	PRO	0	-0.026	-0.019	33.793	-0.077	-0.077	0.000	0.000	0.000	0.000
121	A	121	ASP	-1	-0.877	-0.915	34.618	-8.873	-8.873	0.000	0.000	0.000	0.000
122	A	122	SER	0	-0.043	-0.047	29.694	-0.371	-0.371	0.000	0.000	0.000	0.000
123	A	123	PRO	0	-0.035	-0.007	30.968	-0.309	-0.309	0.000	0.000	0.000	0.000
124	A	124	LEU	0	-0.059	-0.038	26.815	-0.141	-0.141	0.000	0.000	0.000	0.000
125	A	125	ASN	0	-0.079	-0.030	31.559	0.309	0.309	0.000	0.000	0.000	0.000
126	A	126	CYS	0	0.035	0.001	34.511	0.029	0.029	0.000	0.000	0.000	0.000
127	A	127	ASP	-1	-0.872	-0.926	37.731	-7.842	-7.842	0.000	0.000	0.000	0.000
128	A	128	SER	0	-0.001	-0.012	36.364	0.111	0.111	0.000	0.000	0.000	0.000
129	A	129	GLY	0	0.042	0.020	37.645	0.035	0.035	0.000	0.000	0.000	0.000
130	A	130	ASN	0	-0.015	-0.007	38.227	0.080	0.080	0.000	0.000	0.000	0.000
131	A	131	LEU	0	-0.015	0.016	41.557	0.167	0.167	0.000	0.000	0.000	0.000
132	A	132	LEU	0	0.020	0.013	37.716	0.152	0.152	0.000	0.000	0.000	0.000
133	A	133	ARG	1	0.855	0.912	38.240	8.251	8.251	0.000	0.000	0.000	0.000
134	A	134	SER	0	-0.070	-0.045	42.622	0.168	0.168	0.000	0.000	0.000	0.000
135	A	135	GLY	0	0.034	0.022	44.989	0.179	0.179	0.000	0.000	0.000	0.000
136	A	136	ASP	-1	-0.855	-0.910	46.104	-6.712	-6.712	0.000	0.000	0.000	0.000
137	A	137	VAL	0	0.018	-0.015	42.571	-0.147	-0.147	0.000	0.000	0.000	0.000
138	A	138	ARG	1	0.927	0.975	44.132	6.311	6.311	0.000	0.000	0.000	0.000
139	A	139	GLY	0	0.034	0.008	45.699	-0.037	-0.037	0.000	0.000	0.000	0.000
140	A	140	PHE	0	-0.001	-0.009	36.658	-0.078	-0.078	0.000	0.000	0.000	0.000
141	A	141	ASN	0	0.038	0.001	40.864	-0.294	-0.294	0.000	0.000	0.000	0.000
142	A	142	SER	0	-0.027	-0.005	41.756	-0.085	-0.085	0.000	0.000	0.000	0.000
143	A	143	MET	0	0.015	0.012	39.558	-0.083	-0.083	0.000	0.000	0.000	0.000
144	A	144	ALA	0	0.030	0.013	37.324	-0.147	-0.147	0.000	0.000	0.000	0.000
145	A	145	GLN	0	0.048	0.041	37.540	0.013	0.013	0.000	0.000	0.000	0.000
146	A	146	MET	0	-0.067	-0.022	39.799	0.060	0.060	0.000	0.000	0.000	0.000
147	A	147	TYR	0	0.013	-0.027	35.443	-0.068	-0.068	0.000	0.000	0.000	0.000
148	A	148	THR	0	0.002	-0.008	34.912	-0.279	-0.279	0.000	0.000	0.000	0.000
149	A	149	ARG	1	0.922	0.947	35.991	7.265	7.265	0.000	0.000	0.000	0.000
150	A	150	LEU	0	-0.059	-0.020	37.906	0.052	0.052	0.000	0.000	0.000	0.000
151	A	151	ALA	0	-0.056	-0.028	32.544	-0.058	-0.058	0.000	0.000	0.000	0.000
152	A	152	ALA	0	-0.018	-0.007	31.812	-0.289	-0.289	0.000	0.000	0.000	0.000
153	A	153	MET	0	-0.046	-0.006	32.828	0.019	0.019	0.000	0.000	0.000	0.000
154	A	154	PRO	-1	-0.933	-0.942	30.666	-8.679	-8.679	0.000	0.000	0.000	0.000

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