FMO DATABASE

FMODB ID: 8Q24Y

Calculation Name: 1R6E-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1R6E

Chain ID: A

ChEMBL ID:

UniProt ID: Q7CQD4

Base Structure: SolutionNMR

Registration Date: 2025-10-05

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	168
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1623350.122307
FMO2-HF: Nuclear repulsion	1559045.407009
FMO2-HF: Total energy	-64304.715298
FMO2-MP2: Total energy	-64491.275134

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:73:GLU)

Summations of interaction energy for fragment #1(A:73:GLU)

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.
-152.282	-162.519	62.846	-27.647	-24.959	0.029

Interaction energy analysis for fragmet #1(A:73:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.009 / q_NPA : 0.007

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	75	ARG	1	0.899	0.925	1.717	-87.950	-93.873	32.694	-14.556	-12.215	0.130
4	A	76	ALA	0	0.024	0.013	4.049	-7.036	-6.883	0.009	-0.120	-0.041	0.001
6	A	78	LEU	0	-0.058	-0.014	2.201	-7.798	-6.617	3.227	-1.603	-2.805	0.013
7	A	79	THR	0	0.033	0.004	4.826	-1.392	-1.290	-0.001	-0.006	-0.094	0.000
10	A	82	THR	0	0.068	0.048	4.285	-2.091	-1.788	-0.001	-0.034	-0.269	0.000
11	A	83	VAL	0	0.048	0.035	4.572	-7.975	-7.899	-0.001	-0.008	-0.066	0.000
13	A	85	ASP	-1	-0.803	-0.864	1.717	-59.458	-64.413	18.381	-7.528	-5.897	-0.074
14	A	86	PHE	0	0.074	0.027	3.374	-3.645	-2.876	0.025	-0.286	-0.507	-0.002
15	A	87	MET	0	0.016	0.030	3.860	4.038	4.186	0.002	-0.031	-0.119	0.000
17	A	89	GLN	0	-0.030	-0.015	1.924	-22.046	-24.174	8.512	-3.467	-2.917	-0.039
112	A	184	TYR	0	-0.034	-0.028	4.985	-2.539	-2.502	-0.001	-0.008	-0.029	0.000
5	A	77	VAL	0	0.042	0.019	5.896	-1.797	-1.797	0.000	0.000	0.000	0.000
8	A	80	SER	0	0.063	0.042	6.628	-0.719	-0.719	0.000	0.000	0.000	0.000
9	A	81	LYS	1	0.852	0.894	4.825	10.707	10.707	0.000	0.000	0.000	0.000
12	A	84	LYS	1	0.866	0.928	6.362	0.324	0.324	0.000	0.000	0.000	0.000
16	A	88	LEU	0	0.049	0.017	6.215	2.304	2.304	0.000	0.000	0.000	0.000
18	A	90	LYS	1	0.901	0.959	6.304	9.624	9.624	0.000	0.000	0.000	0.000
19	A	91	LEU	0	0.021	0.007	9.066	1.452	1.452	0.000	0.000	0.000	0.000
20	A	92	ASN	0	-0.004	-0.005	7.507	2.468	2.468	0.000	0.000	0.000	0.000
21	A	93	SER	0	-0.024	-0.011	9.613	1.408	1.408	0.000	0.000	0.000	0.000
22	A	94	LEU	0	-0.055	-0.013	11.534	0.706	0.706	0.000	0.000	0.000	0.000
23	A	95	ASP	-1	-0.790	-0.879	13.982	-2.754	-2.754	0.000	0.000	0.000	0.000
24	A	96	ILE	0	0.016	0.011	15.973	0.420	0.420	0.000	0.000	0.000	0.000
25	A	97	LYS	1	0.830	0.887	16.102	4.000	4.000	0.000	0.000	0.000	0.000
26	A	98	GLY	0	0.034	0.023	19.303	0.264	0.264	0.000	0.000	0.000	0.000
27	A	99	ASN	0	-0.018	-0.019	17.985	0.466	0.466	0.000	0.000	0.000	0.000
28	A	100	ALA	0	-0.028	-0.011	21.607	0.198	0.198	0.000	0.000	0.000	0.000
29	A	101	SER	0	-0.033	-0.007	23.768	0.205	0.205	0.000	0.000	0.000	0.000
30	A	102	LYS	1	0.823	0.906	21.477	2.432	2.432	0.000	0.000	0.000	0.000
31	A	103	ASP	-1	-0.848	-0.909	24.669	-1.791	-1.791	0.000	0.000	0.000	0.000
32	A	104	PRO	0	0.044	0.018	26.961	-0.060	-0.060	0.000	0.000	0.000	0.000
33	A	105	ALA	0	0.026	-0.002	29.227	0.014	0.014	0.000	0.000	0.000	0.000
34	A	106	TYR	0	0.027	0.009	18.947	-0.042	-0.042	0.000	0.000	0.000	0.000
35	A	107	ALA	0	0.046	0.016	25.566	-0.082	-0.082	0.000	0.000	0.000	0.000
36	A	108	ARG	1	0.835	0.900	26.786	1.287	1.287	0.000	0.000	0.000	0.000
37	A	109	GLN	0	-0.001	-0.009	26.075	0.051	0.051	0.000	0.000	0.000	0.000
38	A	110	THR	0	-0.056	-0.045	21.188	-0.198	-0.198	0.000	0.000	0.000	0.000
39	A	111	CYS	0	-0.050	0.006	23.705	-0.095	-0.095	0.000	0.000	0.000	0.000
40	A	112	GLU	-1	-0.696	-0.829	26.399	-1.352	-1.352	0.000	0.000	0.000	0.000
41	A	113	ALA	0	-0.001	-0.017	24.974	0.010	0.010	0.000	0.000	0.000	0.000
42	A	114	ILE	0	0.008	0.012	20.350	-0.102	-0.102	0.000	0.000	0.000	0.000
43	A	115	LEU	0	0.000	0.012	23.708	-0.023	-0.023	0.000	0.000	0.000	0.000
44	A	116	SER	0	0.042	0.004	26.483	0.116	0.116	0.000	0.000	0.000	0.000
45	A	117	ALA	0	-0.062	-0.002	22.025	0.031	0.031	0.000	0.000	0.000	0.000
46	A	118	VAL	0	0.003	0.004	22.237	0.039	0.039	0.000	0.000	0.000	0.000
47	A	119	TYR	0	0.047	0.002	24.474	0.060	0.060	0.000	0.000	0.000	0.000
48	A	120	SER	0	-0.038	-0.029	25.417	0.137	0.137	0.000	0.000	0.000	0.000
49	A	121	ASN	0	-0.027	-0.035	20.965	-0.012	-0.012	0.000	0.000	0.000	0.000
50	A	122	ASN	0	-0.008	0.000	24.308	0.150	0.150	0.000	0.000	0.000	0.000
51	A	123	LYS	1	0.883	0.934	27.449	1.390	1.390	0.000	0.000	0.000	0.000
52	A	124	ASP	-1	-0.874	-0.901	24.167	-1.564	-1.564	0.000	0.000	0.000	0.000
53	A	125	GLN	0	0.053	0.028	23.158	0.147	0.147	0.000	0.000	0.000	0.000
54	A	126	CYS	0	-0.013	0.022	25.979	0.107	0.107	0.000	0.000	0.000	0.000
55	A	127	CYS	0	0.009	0.017	29.728	0.093	0.093	0.000	0.000	0.000	0.000
56	A	128	LYS	1	0.871	0.924	24.814	1.172	1.172	0.000	0.000	0.000	0.000
57	A	129	LEU	0	0.006	0.010	28.947	0.042	0.042	0.000	0.000	0.000	0.000
58	A	130	LEU	0	-0.014	0.003	31.135	0.065	0.065	0.000	0.000	0.000	0.000
59	A	131	ILE	0	-0.005	-0.018	32.093	0.048	0.048	0.000	0.000	0.000	0.000
60	A	132	SER	0	-0.092	-0.059	32.993	0.045	0.045	0.000	0.000	0.000	0.000
61	A	133	LYS	1	0.815	0.901	34.124	0.596	0.596	0.000	0.000	0.000	0.000
62	A	134	GLY	0	-0.008	0.016	37.607	0.029	0.029	0.000	0.000	0.000	0.000
63	A	135	VAL	0	-0.007	0.016	36.564	0.014	0.014	0.000	0.000	0.000	0.000
64	A	136	SER	0	-0.005	-0.014	38.916	-0.013	-0.013	0.000	0.000	0.000	0.000
65	A	137	ILE	0	0.050	0.004	32.661	-0.009	-0.009	0.000	0.000	0.000	0.000
66	A	138	THR	0	-0.001	0.004	36.174	-0.039	-0.039	0.000	0.000	0.000	0.000
67	A	139	PRO	0	0.021	0.020	38.334	-0.021	-0.021	0.000	0.000	0.000	0.000
68	A	140	PHE	0	0.071	0.036	30.189	-0.028	-0.028	0.000	0.000	0.000	0.000
69	A	141	LEU	0	-0.028	-0.034	33.211	-0.039	-0.039	0.000	0.000	0.000	0.000
70	A	142	LYS	1	0.890	0.940	35.092	0.688	0.688	0.000	0.000	0.000	0.000
71	A	143	GLU	-1	-0.797	-0.873	36.543	-0.696	-0.696	0.000	0.000	0.000	0.000
72	A	144	ILE	0	-0.046	-0.016	30.609	-0.028	-0.028	0.000	0.000	0.000	0.000
73	A	145	GLY	0	0.015	0.003	32.988	-0.065	-0.065	0.000	0.000	0.000	0.000
74	A	146	GLU	-1	-0.830	-0.895	35.172	-0.744	-0.744	0.000	0.000	0.000	0.000
75	A	147	ALA	0	0.018	0.021	32.157	-0.004	-0.004	0.000	0.000	0.000	0.000
76	A	148	ALA	0	-0.009	-0.027	31.657	-0.032	-0.032	0.000	0.000	0.000	0.000
77	A	149	GLN	0	-0.055	-0.024	33.096	-0.011	-0.011	0.000	0.000	0.000	0.000
78	A	150	ASN	0	-0.003	-0.025	34.642	-0.032	-0.032	0.000	0.000	0.000	0.000
79	A	151	ALA	0	-0.043	-0.014	31.089	0.001	0.001	0.000	0.000	0.000	0.000
80	A	152	GLY	0	0.010	0.012	32.607	-0.051	-0.051	0.000	0.000	0.000	0.000
81	A	153	LEU	0	-0.084	-0.038	29.331	-0.050	-0.050	0.000	0.000	0.000	0.000
82	A	154	PRO	0	0.038	0.011	33.032	0.007	0.007	0.000	0.000	0.000	0.000
83	A	155	GLY	0	-0.007	-0.023	34.791	-0.064	-0.064	0.000	0.000	0.000	0.000
84	A	156	GLU	-1	-0.834	-0.883	35.701	-0.818	-0.818	0.000	0.000	0.000	0.000
85	A	157	ILE	0	-0.015	-0.004	37.820	0.000	0.000	0.000	0.000	0.000	0.000
86	A	158	LYS	1	0.837	0.896	40.146	0.769	0.769	0.000	0.000	0.000	0.000
87	A	159	ASN	0	0.022	-0.006	43.357	-0.008	-0.008	0.000	0.000	0.000	0.000
88	A	160	GLY	0	0.021	0.030	44.552	-0.001	-0.001	0.000	0.000	0.000	0.000
89	A	161	VAL	0	-0.033	-0.011	38.673	-0.016	-0.016	0.000	0.000	0.000	0.000
90	A	162	PHE	0	0.074	0.039	35.104	0.010	0.010	0.000	0.000	0.000	0.000
91	A	163	THR	0	-0.035	-0.021	32.892	-0.041	-0.041	0.000	0.000	0.000	0.000
92	A	164	PRO	0	0.031	0.037	30.595	0.026	0.026	0.000	0.000	0.000	0.000
93	A	165	GLY	0	0.025	0.009	32.457	-0.009	-0.009	0.000	0.000	0.000	0.000
94	A	166	GLY	0	-0.010	0.000	28.429	-0.021	-0.021	0.000	0.000	0.000	0.000
95	A	167	ALA	0	-0.005	0.014	27.444	-0.130	-0.130	0.000	0.000	0.000	0.000
96	A	168	GLY	0	0.042	0.020	26.665	0.053	0.053	0.000	0.000	0.000	0.000
97	A	169	ALA	0	-0.012	0.001	22.819	-0.004	-0.004	0.000	0.000	0.000	0.000
98	A	170	ASN	0	0.022	0.001	19.266	-0.319	-0.319	0.000	0.000	0.000	0.000
99	A	171	PRO	0	0.035	0.025	20.804	-0.135	-0.135	0.000	0.000	0.000	0.000
100	A	172	PHE	0	0.050	0.016	17.108	-0.188	-0.188	0.000	0.000	0.000	0.000
101	A	173	VAL	0	-0.022	-0.025	15.687	-0.523	-0.523	0.000	0.000	0.000	0.000
102	A	174	VAL	0	0.033	0.033	16.385	-0.220	-0.220	0.000	0.000	0.000	0.000
103	A	175	PRO	0	0.056	0.032	16.529	-0.166	-0.166	0.000	0.000	0.000	0.000
104	A	176	LEU	0	-0.040	-0.005	11.360	-0.564	-0.564	0.000	0.000	0.000	0.000
105	A	177	ILE	0	0.021	0.002	12.220	-0.732	-0.732	0.000	0.000	0.000	0.000
106	A	178	ALA	0	0.008	0.033	14.498	0.067	0.067	0.000	0.000	0.000	0.000
107	A	179	SER	0	-0.027	-0.048	11.440	-0.028	-0.028	0.000	0.000	0.000	0.000
108	A	180	ALA	0	-0.040	-0.025	10.332	-0.467	-0.467	0.000	0.000	0.000	0.000
109	A	181	SER	0	-0.036	-0.035	11.286	0.378	0.378	0.000	0.000	0.000	0.000
110	A	182	ILE	0	-0.019	-0.007	13.527	0.337	0.337	0.000	0.000	0.000	0.000
111	A	183	LYS	1	0.882	0.965	5.824	14.406	14.406	0.000	0.000	0.000	0.000
113	A	185	PRO	0	0.105	0.054	11.297	0.243	0.243	0.000	0.000	0.000	0.000
114	A	186	HIS	0	0.024	-0.009	11.747	-0.082	-0.082	0.000	0.000	0.000	0.000
115	A	187	MET	0	-0.078	-0.040	10.255	0.114	0.114	0.000	0.000	0.000	0.000
116	A	188	PHE	0	-0.003	-0.023	11.489	-0.227	-0.227	0.000	0.000	0.000	0.000
117	A	189	ILE	0	0.009	0.036	16.039	0.077	0.077	0.000	0.000	0.000	0.000
118	A	190	ASN	0	0.004	0.004	18.729	0.153	0.153	0.000	0.000	0.000	0.000
119	A	191	HIS	0	0.067	0.033	20.096	-0.119	-0.119	0.000	0.000	0.000	0.000
120	A	192	ASN	0	0.002	0.002	21.713	-0.028	-0.028	0.000	0.000	0.000	0.000
121	A	193	GLN	0	0.016	0.026	15.185	0.075	0.075	0.000	0.000	0.000	0.000
122	A	194	GLN	0	0.032	0.001	16.253	-0.298	-0.298	0.000	0.000	0.000	0.000
123	A	195	VAL	0	0.009	-0.001	17.324	-0.250	-0.250	0.000	0.000	0.000	0.000
124	A	196	SER	0	0.041	0.009	17.863	-0.023	-0.023	0.000	0.000	0.000	0.000
125	A	197	PHE	0	-0.046	-0.037	10.996	-0.356	-0.356	0.000	0.000	0.000	0.000
126	A	198	LYS	1	0.831	0.896	14.668	1.455	1.455	0.000	0.000	0.000	0.000
127	A	199	ALA	0	0.044	0.039	16.849	-0.060	-0.060	0.000	0.000	0.000	0.000
128	A	200	TYR	0	0.005	-0.017	9.920	0.141	0.141	0.000	0.000	0.000	0.000
129	A	201	ALA	0	0.000	-0.012	13.420	-0.366	-0.366	0.000	0.000	0.000	0.000
130	A	202	GLU	-1	-0.762	-0.895	14.403	-2.823	-2.823	0.000	0.000	0.000	0.000
131	A	203	LYS	1	0.857	0.935	16.115	2.010	2.010	0.000	0.000	0.000	0.000
132	A	204	ILE	0	-0.030	-0.008	10.518	-0.132	-0.132	0.000	0.000	0.000	0.000
133	A	205	VAL	0	0.014	0.005	14.102	-0.151	-0.151	0.000	0.000	0.000	0.000
134	A	206	MET	0	0.023	0.027	16.045	0.242	0.242	0.000	0.000	0.000	0.000
135	A	207	LYS	1	0.839	0.905	11.722	5.873	5.873	0.000	0.000	0.000	0.000
136	A	208	GLU	-1	-0.818	-0.894	14.363	-4.434	-4.434	0.000	0.000	0.000	0.000
137	A	209	VAL	0	0.024	0.000	16.709	0.237	0.237	0.000	0.000	0.000	0.000
138	A	210	THR	0	-0.020	-0.022	19.933	0.318	0.318	0.000	0.000	0.000	0.000
139	A	211	PRO	0	-0.008	-0.008	19.930	0.204	0.204	0.000	0.000	0.000	0.000
140	A	212	LEU	0	-0.001	0.008	21.791	0.137	0.137	0.000	0.000	0.000	0.000
141	A	213	PHE	0	-0.007	-0.025	22.906	0.108	0.108	0.000	0.000	0.000	0.000
142	A	214	ASN	0	-0.026	0.007	26.094	0.110	0.110	0.000	0.000	0.000	0.000
143	A	215	LYS	1	0.858	0.914	27.755	1.595	1.595	0.000	0.000	0.000	0.000
144	A	216	GLY	0	0.011	-0.007	29.746	0.040	0.040	0.000	0.000	0.000	0.000
145	A	217	THR	0	-0.003	0.009	32.249	-0.008	-0.008	0.000	0.000	0.000	0.000
146	A	218	MET	0	-0.036	0.013	29.332	-0.014	-0.014	0.000	0.000	0.000	0.000
147	A	219	PRO	0	0.004	0.014	29.566	-0.015	-0.015	0.000	0.000	0.000	0.000
148	A	220	THR	0	0.044	-0.010	24.743	-0.112	-0.112	0.000	0.000	0.000	0.000
149	A	221	PRO	0	0.005	0.022	21.293	0.080	0.080	0.000	0.000	0.000	0.000
150	A	222	GLN	0	0.034	0.009	21.756	-0.056	-0.056	0.000	0.000	0.000	0.000
151	A	223	GLN	0	0.089	0.059	23.871	0.040	0.040	0.000	0.000	0.000	0.000
152	A	224	PHE	0	-0.009	0.017	26.859	0.072	0.072	0.000	0.000	0.000	0.000
153	A	225	GLN	0	0.043	0.006	21.709	-0.058	-0.058	0.000	0.000	0.000	0.000
154	A	226	LEU	0	0.037	0.016	25.853	0.056	0.056	0.000	0.000	0.000	0.000
155	A	227	THR	0	-0.020	-0.014	27.775	0.105	0.105	0.000	0.000	0.000	0.000
156	A	228	ILE	0	-0.035	0.002	27.097	0.059	0.059	0.000	0.000	0.000	0.000
157	A	229	GLU	-1	-0.849	-0.947	23.395	-1.547	-1.547	0.000	0.000	0.000	0.000
158	A	230	ASN	0	-0.066	-0.021	28.371	0.123	0.123	0.000	0.000	0.000	0.000
159	A	231	ILE	0	-0.042	-0.007	31.609	0.070	0.070	0.000	0.000	0.000	0.000
160	A	232	ALA	0	-0.001	-0.020	28.897	0.037	0.037	0.000	0.000	0.000	0.000
161	A	233	ASN	0	-0.026	-0.054	27.434	0.090	0.090	0.000	0.000	0.000	0.000
162	A	234	LYS	1	0.834	0.909	31.271	0.734	0.734	0.000	0.000	0.000	0.000
163	A	235	TYR	0	-0.021	-0.036	34.161	0.048	0.048	0.000	0.000	0.000	0.000
164	A	236	LEU	0	-0.050	-0.018	28.338	0.020	0.020	0.000	0.000	0.000	0.000
165	A	237	GLN	0	0.026	0.021	32.457	0.051	0.051	0.000	0.000	0.000	0.000
166	A	238	ASN	0	-0.033	-0.025	34.983	0.035	0.035	0.000	0.000	0.000	0.000
167	A	239	ALA	0	0.015	0.018	38.406	0.015	0.015	0.000	0.000	0.000	0.000
168	A	240	SER	-1	-0.896	-0.931	35.113	-0.454	-0.454	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:73:GLU)