FMO DATABASE

FMODB ID: G82V1

Calculation Name: 1RH8-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1RH8

Chain ID: A

ChEMBL ID:

UniProt ID: Q9JKS6

Base Structure: SolutionNMR

Registration Date: 2025-10-03

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	142
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1364986.085976
FMO2-HF: Nuclear repulsion	1307719.56909
FMO2-HF: Total energy	-57266.516886
FMO2-MP2: Total energy	-57435.431743

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:4635:ALA)

Summations of interaction energy for fragment #1(A:4635:ALA)

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.
-66.497	-64.513	-0.013	-1.036	-0.936	-0.003

Interaction energy analysis for fragmet #1(A:4635:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.838 / q_NPA : 0.908

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	4637	HIS	0	0.044	0.024	3.827	-3.181	-1.197	-0.013	-1.036	-0.936	-0.003
4	A	4638	PRO	0	0.012	0.023	6.323	2.291	2.291	0.000	0.000	0.000	0.000
5	A	4639	ILE	0	0.013	0.021	9.505	0.768	0.768	0.000	0.000	0.000	0.000
6	A	4640	THR	0	-0.027	-0.020	12.069	1.153	1.153	0.000	0.000	0.000	0.000
7	A	4641	GLY	0	0.016	0.019	14.660	-0.016	-0.016	0.000	0.000	0.000	0.000
8	A	4642	GLU	-1	-0.924	-0.967	17.579	-12.258	-12.258	0.000	0.000	0.000	0.000
9	A	4643	ILE	0	0.008	-0.005	20.663	-0.282	-0.282	0.000	0.000	0.000	0.000
10	A	4644	GLN	0	0.000	0.001	22.920	0.336	0.336	0.000	0.000	0.000	0.000
11	A	4645	LEU	0	-0.015	-0.012	25.548	-0.133	-0.133	0.000	0.000	0.000	0.000
12	A	4646	GLN	0	0.005	0.003	28.994	0.353	0.353	0.000	0.000	0.000	0.000
13	A	4647	ILE	0	-0.004	0.004	31.191	-0.105	-0.105	0.000	0.000	0.000	0.000
14	A	4648	ASN	0	0.025	-0.002	34.930	0.205	0.205	0.000	0.000	0.000	0.000
15	A	4649	TYR	0	-0.014	-0.012	38.506	-0.125	-0.125	0.000	0.000	0.000	0.000
16	A	4650	ASP	-1	-0.807	-0.901	40.989	-6.962	-6.962	0.000	0.000	0.000	0.000
17	A	4651	LEU	0	-0.072	-0.041	43.813	-0.078	-0.078	0.000	0.000	0.000	0.000
18	A	4652	GLY	0	0.014	0.023	45.177	0.032	0.032	0.000	0.000	0.000	0.000
19	A	4653	ASN	0	-0.031	-0.026	40.853	-0.112	-0.112	0.000	0.000	0.000	0.000
20	A	4654	LEU	0	0.026	0.023	34.863	0.075	0.075	0.000	0.000	0.000	0.000
21	A	4655	ILE	0	-0.037	-0.015	36.334	-0.120	-0.120	0.000	0.000	0.000	0.000
22	A	4656	ILE	0	0.009	0.005	30.237	-0.035	-0.035	0.000	0.000	0.000	0.000
23	A	4657	HIS	0	0.042	0.030	31.924	-0.129	-0.129	0.000	0.000	0.000	0.000
24	A	4658	ILE	0	0.009	0.005	25.402	-0.145	-0.145	0.000	0.000	0.000	0.000
25	A	4659	LEU	0	-0.027	-0.004	27.259	0.119	0.119	0.000	0.000	0.000	0.000
26	A	4660	GLN	0	0.048	0.003	23.356	-0.375	-0.375	0.000	0.000	0.000	0.000
27	A	4661	ALA	0	0.031	0.025	19.044	0.242	0.242	0.000	0.000	0.000	0.000
28	A	4662	ARG	1	0.815	0.911	19.771	13.590	13.590	0.000	0.000	0.000	0.000
29	A	4663	ASN	0	-0.039	-0.032	16.478	0.604	0.604	0.000	0.000	0.000	0.000
30	A	4664	LEU	0	0.036	0.032	13.815	-0.220	-0.220	0.000	0.000	0.000	0.000
31	A	4665	VAL	0	0.010	0.024	7.917	-0.344	-0.344	0.000	0.000	0.000	0.000
32	A	4666	PRO	0	-0.010	0.004	8.733	0.042	0.042	0.000	0.000	0.000	0.000
33	A	4667	ARG	1	0.904	0.938	5.934	28.286	28.286	0.000	0.000	0.000	0.000
34	A	4668	ASP	-1	-0.930	-0.951	5.509	-38.093	-38.093	0.000	0.000	0.000	0.000
35	A	4669	ASN	0	-0.058	-0.038	8.085	1.952	1.952	0.000	0.000	0.000	0.000
36	A	4670	ASN	0	0.018	0.007	11.861	-0.258	-0.258	0.000	0.000	0.000	0.000
37	A	4671	GLY	0	0.037	0.024	14.079	0.849	0.849	0.000	0.000	0.000	0.000
38	A	4672	TYR	0	-0.027	-0.035	10.673	-0.283	-0.283	0.000	0.000	0.000	0.000
39	A	4673	SER	0	-0.024	-0.022	13.713	1.805	1.805	0.000	0.000	0.000	0.000
40	A	4674	ASP	-1	-0.835	-0.926	15.524	-14.082	-14.082	0.000	0.000	0.000	0.000
41	A	4675	PRO	0	0.058	0.037	15.099	0.409	0.409	0.000	0.000	0.000	0.000
42	A	4676	PHE	0	-0.046	-0.011	17.181	1.175	1.175	0.000	0.000	0.000	0.000
43	A	4677	VAL	0	0.032	0.011	19.337	-0.516	-0.516	0.000	0.000	0.000	0.000
44	A	4678	LYS	1	0.853	0.932	18.955	16.338	16.338	0.000	0.000	0.000	0.000
45	A	4679	VAL	0	0.008	0.010	23.660	-0.170	-0.170	0.000	0.000	0.000	0.000
46	A	4680	TYR	0	-0.045	-0.043	24.137	0.425	0.425	0.000	0.000	0.000	0.000
47	A	4681	LEU	0	-0.029	-0.007	29.285	0.033	0.033	0.000	0.000	0.000	0.000
48	A	4682	LEU	0	0.062	0.040	28.327	0.105	0.105	0.000	0.000	0.000	0.000
49	A	4683	PRO	0	0.015	0.027	31.431	0.059	0.059	0.000	0.000	0.000	0.000
50	A	4684	GLY	0	-0.022	-0.001	33.565	0.371	0.371	0.000	0.000	0.000	0.000
51	A	4685	ARG	1	0.920	0.941	34.618	8.467	8.467	0.000	0.000	0.000	0.000
52	A	4686	GLY	0	0.075	0.041	30.466	-0.028	-0.028	0.000	0.000	0.000	0.000
53	A	4687	GLN	0	-0.058	-0.025	29.694	-0.159	-0.159	0.000	0.000	0.000	0.000
54	A	4688	VAL	0	0.027	0.021	24.589	0.100	0.100	0.000	0.000	0.000	0.000
55	A	4689	MET	0	-0.019	0.000	28.018	0.151	0.151	0.000	0.000	0.000	0.000
56	A	4690	VAL	0	-0.001	-0.002	23.068	-0.335	-0.335	0.000	0.000	0.000	0.000
57	A	4691	VAL	0	-0.036	-0.006	24.251	0.533	0.533	0.000	0.000	0.000	0.000
58	A	4692	GLN	0	-0.004	0.001	24.511	-0.333	-0.333	0.000	0.000	0.000	0.000
59	A	4693	ASN	0	0.019	-0.009	22.297	-0.198	-0.198	0.000	0.000	0.000	0.000
60	A	4694	ALA	0	0.027	0.027	26.348	0.346	0.346	0.000	0.000	0.000	0.000
61	A	4695	SER	0	0.018	-0.003	28.393	-0.294	-0.294	0.000	0.000	0.000	0.000
62	A	4696	ALA	0	0.050	0.006	27.158	-0.100	-0.100	0.000	0.000	0.000	0.000
63	A	4697	GLU	-1	-0.950	-0.963	27.998	-9.158	-9.158	0.000	0.000	0.000	0.000
64	A	4698	TYR	0	-0.033	-0.045	27.580	0.065	0.065	0.000	0.000	0.000	0.000
65	A	4699	LYS	1	0.843	0.938	24.125	11.891	11.891	0.000	0.000	0.000	0.000
66	A	4700	ARG	1	0.926	0.949	24.660	11.303	11.303	0.000	0.000	0.000	0.000
67	A	4701	ARG	1	0.942	0.978	25.560	9.352	9.352	0.000	0.000	0.000	0.000
68	A	4702	THR	0	0.044	0.023	24.139	-0.093	-0.093	0.000	0.000	0.000	0.000
69	A	4703	LYS	1	0.759	0.860	21.051	12.962	12.962	0.000	0.000	0.000	0.000
70	A	4704	TYR	0	-0.010	0.014	19.509	-0.713	-0.713	0.000	0.000	0.000	0.000
71	A	4705	VAL	0	0.032	0.009	18.251	-0.789	-0.789	0.000	0.000	0.000	0.000
72	A	4706	GLN	0	0.004	-0.002	18.078	-0.887	-0.887	0.000	0.000	0.000	0.000
73	A	4707	LYS	1	0.787	0.888	16.865	15.625	15.625	0.000	0.000	0.000	0.000
74	A	4708	SER	0	-0.019	-0.006	14.085	-0.829	-0.829	0.000	0.000	0.000	0.000
75	A	4709	LEU	0	0.003	0.012	13.248	-1.209	-1.209	0.000	0.000	0.000	0.000
76	A	4710	ASN	0	-0.028	0.001	15.549	-0.522	-0.522	0.000	0.000	0.000	0.000
77	A	4711	PRO	0	0.041	0.037	17.000	0.747	0.747	0.000	0.000	0.000	0.000
78	A	4712	GLU	-1	-0.747	-0.865	19.693	-11.401	-11.401	0.000	0.000	0.000	0.000
79	A	4713	TRP	0	-0.066	-0.058	19.706	0.142	0.142	0.000	0.000	0.000	0.000
80	A	4714	ASN	0	-0.005	-0.017	25.793	0.077	0.077	0.000	0.000	0.000	0.000
81	A	4715	GLN	0	-0.045	-0.005	28.070	0.440	0.440	0.000	0.000	0.000	0.000
82	A	4716	THR	0	0.005	-0.012	30.538	-0.019	-0.019	0.000	0.000	0.000	0.000
83	A	4717	VAL	0	0.000	0.008	30.007	0.023	0.023	0.000	0.000	0.000	0.000
84	A	4718	ILE	0	-0.011	-0.020	33.343	0.202	0.202	0.000	0.000	0.000	0.000
85	A	4719	TYR	0	-0.028	-0.010	30.214	0.031	0.031	0.000	0.000	0.000	0.000
86	A	4720	LYS	1	0.976	0.973	37.089	7.578	7.578	0.000	0.000	0.000	0.000
87	A	4721	SER	0	-0.042	-0.010	40.544	-0.046	-0.046	0.000	0.000	0.000	0.000
88	A	4722	ILE	0	-0.023	-0.010	37.573	-0.122	-0.122	0.000	0.000	0.000	0.000
89	A	4723	SER	0	0.017	-0.006	42.025	-0.010	-0.010	0.000	0.000	0.000	0.000
90	A	4724	MET	0	0.048	0.011	41.994	-0.182	-0.182	0.000	0.000	0.000	0.000
91	A	4725	GLU	-1	-0.867	-0.904	43.292	-6.802	-6.802	0.000	0.000	0.000	0.000
92	A	4726	GLN	0	-0.050	-0.029	41.208	-0.230	-0.230	0.000	0.000	0.000	0.000
93	A	4727	LEU	0	-0.017	-0.012	38.036	-0.209	-0.209	0.000	0.000	0.000	0.000
94	A	4728	MET	0	0.002	0.022	38.337	-0.233	-0.233	0.000	0.000	0.000	0.000
95	A	4729	LYS	1	0.928	0.958	38.809	7.449	7.449	0.000	0.000	0.000	0.000
96	A	4730	LYS	1	0.799	0.892	35.503	8.481	8.481	0.000	0.000	0.000	0.000
97	A	4731	THR	0	0.022	-0.016	29.980	0.203	0.203	0.000	0.000	0.000	0.000
98	A	4732	LEU	0	-0.030	-0.020	29.478	-0.080	-0.080	0.000	0.000	0.000	0.000
99	A	4733	GLU	-1	-0.769	-0.876	23.877	-13.147	-13.147	0.000	0.000	0.000	0.000
100	A	4734	VAL	0	-0.035	-0.028	23.348	0.132	0.132	0.000	0.000	0.000	0.000
101	A	4735	THR	0	0.047	0.034	19.845	-0.528	-0.528	0.000	0.000	0.000	0.000
102	A	4736	VAL	0	-0.009	-0.015	17.158	0.500	0.500	0.000	0.000	0.000	0.000
103	A	4737	TRP	0	0.030	-0.005	15.482	-1.019	-1.019	0.000	0.000	0.000	0.000
104	A	4738	ASP	-1	-0.726	-0.836	12.244	-20.387	-20.387	0.000	0.000	0.000	0.000
105	A	4739	TYR	0	-0.087	-0.034	14.276	0.083	0.083	0.000	0.000	0.000	0.000
106	A	4740	ASP	-1	-0.778	-0.869	11.233	-27.427	-27.427	0.000	0.000	0.000	0.000
107	A	4741	ARG	1	0.846	0.893	9.401	26.721	26.721	0.000	0.000	0.000	0.000
108	A	4742	PHE	0	-0.011	-0.015	12.705	1.420	1.420	0.000	0.000	0.000	0.000
109	A	4743	SER	0	-0.014	-0.022	16.010	1.536	1.536	0.000	0.000	0.000	0.000
110	A	4744	SER	0	-0.037	0.004	12.847	1.072	1.072	0.000	0.000	0.000	0.000
111	A	4745	ASN	0	-0.009	-0.011	14.447	0.703	0.703	0.000	0.000	0.000	0.000
112	A	4746	ASP	-1	-0.846	-0.890	9.548	-29.425	-29.425	0.000	0.000	0.000	0.000
113	A	4747	PHE	0	0.001	-0.001	12.181	1.591	1.591	0.000	0.000	0.000	0.000
114	A	4748	LEU	0	-0.042	-0.036	11.509	-1.738	-1.738	0.000	0.000	0.000	0.000
115	A	4749	GLY	0	0.035	0.013	13.888	0.034	0.034	0.000	0.000	0.000	0.000
116	A	4750	GLU	-1	-0.830	-0.898	16.851	-14.303	-14.303	0.000	0.000	0.000	0.000
117	A	4751	VAL	0	-0.027	0.000	20.398	0.115	0.115	0.000	0.000	0.000	0.000
118	A	4752	LEU	0	0.013	0.010	23.851	0.183	0.183	0.000	0.000	0.000	0.000
119	A	4753	ILE	0	0.000	0.000	27.213	0.153	0.153	0.000	0.000	0.000	0.000
120	A	4754	ASP	-1	-0.843	-0.900	30.303	-9.786	-9.786	0.000	0.000	0.000	0.000
121	A	4755	LEU	0	-0.029	-0.035	33.458	0.223	0.223	0.000	0.000	0.000	0.000
122	A	4756	SER	0	0.026	0.009	36.278	0.230	0.230	0.000	0.000	0.000	0.000
123	A	4757	SER	0	-0.027	-0.029	37.290	0.280	0.280	0.000	0.000	0.000	0.000
124	A	4758	THR	0	-0.002	0.025	35.599	-0.189	-0.189	0.000	0.000	0.000	0.000
125	A	4759	SER	0	0.003	-0.016	36.823	0.082	0.082	0.000	0.000	0.000	0.000
126	A	4760	HIS	0	-0.023	-0.006	32.137	-0.085	-0.085	0.000	0.000	0.000	0.000
127	A	4761	LEU	0	-0.012	0.001	36.555	-0.079	-0.079	0.000	0.000	0.000	0.000
128	A	4762	ASP	-1	-0.893	-0.924	38.808	-7.317	-7.317	0.000	0.000	0.000	0.000
129	A	4763	ASN	0	0.001	-0.015	37.584	-0.144	-0.144	0.000	0.000	0.000	0.000
130	A	4764	THR	0	-0.016	-0.004	35.601	0.009	0.009	0.000	0.000	0.000	0.000
131	A	4765	PRO	0	-0.061	-0.024	32.172	-0.226	-0.226	0.000	0.000	0.000	0.000
132	A	4766	ARG	1	0.918	0.956	30.926	9.118	9.118	0.000	0.000	0.000	0.000
133	A	4767	TRP	0	0.021	0.001	23.097	-0.258	-0.258	0.000	0.000	0.000	0.000
134	A	4768	TYR	0	-0.024	-0.030	25.452	0.372	0.372	0.000	0.000	0.000	0.000
135	A	4769	PRO	0	0.039	0.023	22.342	-0.427	-0.427	0.000	0.000	0.000	0.000
136	A	4770	LEU	0	-0.071	-0.018	17.827	0.243	0.243	0.000	0.000	0.000	0.000
137	A	4771	LYS	1	0.865	0.928	18.513	14.159	14.159	0.000	0.000	0.000	0.000
138	A	4772	GLU	-1	-0.829	-0.947	13.704	-23.271	-23.271	0.000	0.000	0.000	0.000
139	A	4773	GLN	0	-0.060	-0.041	16.993	0.661	0.661	0.000	0.000	0.000	0.000
140	A	4774	THR	0	-0.071	-0.039	17.602	-0.662	-0.662	0.000	0.000	0.000	0.000
141	A	4775	GLU	-1	-0.957	-0.971	17.750	-16.653	-16.653	0.000	0.000	0.000	0.000
142	A	4776	SER	-1	-0.976	-0.980	19.824	-13.828	-13.828	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4635:ALA)