FMO DATABASE

FMODB ID: 9Q382

Calculation Name: 1RLH-A-Xray549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1RLH

Chain ID: A

ChEMBL ID:

UniProt ID: Q9HII6

Base Structure: X-ray

Registration Date: 2025-10-11

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	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	151
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1332681.722014
FMO2-HF: Nuclear repulsion	1275227.90036
FMO2-HF: Total energy	-57453.821654
FMO2-MP2: Total energy	-57622.319437

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:-15:HIS)

Summations of interaction energy for fragment #1(A:-15:HIS)

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.
-12.488	-7.531	4.007	-3.043	-5.92	-0.027

Interaction energy analysis for fragmet #1(A:-15:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.846 / q_NPA : 0.914

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	-13	HIS	0	0.027	0.015	2.496	-13.515	-8.663	4.008	-3.029	-5.830	-0.027
4	A	-12	HIS	0	0.021	0.006	4.560	1.643	1.748	-0.001	-0.014	-0.090	0.000
5	A	-11	HIS	0	-0.029	-0.015	7.683	1.563	1.563	0.000	0.000	0.000	0.000
6	A	-10	HIS	0	0.030	0.001	10.485	0.752	0.752	0.000	0.000	0.000	0.000
7	A	-9	SER	0	-0.041	-0.014	13.443	1.330	1.330	0.000	0.000	0.000	0.000
8	A	-8	SER	0	-0.025	-0.011	12.087	1.187	1.187	0.000	0.000	0.000	0.000
9	A	-7	GLY	0	0.025	0.009	15.008	0.048	0.048	0.000	0.000	0.000	0.000
10	A	-6	LEU	0	-0.012	-0.003	17.514	0.069	0.069	0.000	0.000	0.000	0.000
11	A	-5	VAL	0	-0.008	-0.003	21.198	0.132	0.132	0.000	0.000	0.000	0.000
12	A	-4	PRO	0	-0.036	-0.020	22.677	0.482	0.482	0.000	0.000	0.000	0.000
13	A	-3	ARG	1	0.922	0.965	25.719	10.454	10.454	0.000	0.000	0.000	0.000
14	A	-2	GLY	0	0.066	0.040	27.516	-0.321	-0.321	0.000	0.000	0.000	0.000
15	A	-1	SER	0	-0.012	-0.014	27.090	0.192	0.192	0.000	0.000	0.000	0.000
16	A	0	HIS	0	0.007	0.005	29.565	0.235	0.235	0.000	0.000	0.000	0.000
17	A	1	MET	0	-0.046	-0.001	30.690	-0.172	-0.172	0.000	0.000	0.000	0.000
18	A	2	VAL	0	-0.027	-0.019	34.748	0.286	0.286	0.000	0.000	0.000	0.000
19	A	3	ILE	0	0.055	0.028	37.196	-0.129	-0.129	0.000	0.000	0.000	0.000
20	A	4	PRO	0	-0.021	-0.008	40.053	0.171	0.171	0.000	0.000	0.000	0.000
21	A	5	ALA	0	0.033	0.014	43.136	0.011	0.011	0.000	0.000	0.000	0.000
22	A	6	GLU	-1	-0.907	-0.963	46.586	-6.347	-6.347	0.000	0.000	0.000	0.000
23	A	7	ALA	0	-0.054	-0.010	42.888	0.029	0.029	0.000	0.000	0.000	0.000
24	A	8	ASN	0	-0.008	-0.009	42.510	-0.028	-0.028	0.000	0.000	0.000	0.000
25	A	9	ILE	0	-0.031	-0.019	35.462	-0.090	-0.090	0.000	0.000	0.000	0.000
26	A	10	ILE	0	0.006	0.001	34.773	0.054	0.054	0.000	0.000	0.000	0.000
27	A	11	VAL	0	-0.018	-0.014	30.116	-0.158	-0.158	0.000	0.000	0.000	0.000
28	A	12	GLY	0	0.060	0.026	29.673	0.152	0.152	0.000	0.000	0.000	0.000
29	A	13	TYR	0	-0.010	0.008	21.082	-0.562	-0.562	0.000	0.000	0.000	0.000
30	A	14	SER	0	0.007	-0.005	25.944	0.279	0.279	0.000	0.000	0.000	0.000
31	A	15	HIS	0	-0.021	-0.006	24.926	-0.873	-0.873	0.000	0.000	0.000	0.000
32	A	16	PHE	0	-0.035	-0.026	21.294	0.186	0.186	0.000	0.000	0.000	0.000
33	A	17	ILE	0	0.029	0.039	24.969	0.058	0.058	0.000	0.000	0.000	0.000
34	A	18	LYS	1	0.933	0.953	24.630	11.278	11.278	0.000	0.000	0.000	0.000
35	A	19	THR	0	0.012	0.007	26.565	-0.187	-0.187	0.000	0.000	0.000	0.000
36	A	20	VAL	0	0.014	0.012	29.744	-0.040	-0.040	0.000	0.000	0.000	0.000
37	A	21	GLU	-1	-0.912	-0.954	32.413	-8.905	-8.905	0.000	0.000	0.000	0.000
38	A	22	ASP	-1	-0.869	-0.937	31.442	-9.959	-9.959	0.000	0.000	0.000	0.000
39	A	23	LEU	0	-0.018	-0.019	30.685	0.151	0.151	0.000	0.000	0.000	0.000
40	A	24	ASN	0	-0.005	-0.008	34.830	0.411	0.411	0.000	0.000	0.000	0.000
41	A	25	GLU	-1	-0.916	-0.973	37.742	-7.541	-7.541	0.000	0.000	0.000	0.000
42	A	26	ILE	0	-0.024	0.005	35.933	0.241	0.241	0.000	0.000	0.000	0.000
43	A	27	ILE	0	0.012	-0.007	38.021	0.191	0.191	0.000	0.000	0.000	0.000
44	A	28	ARG	1	0.964	1.003	40.719	7.668	7.668	0.000	0.000	0.000	0.000
45	A	29	THR	0	0.006	-0.012	43.191	0.146	0.146	0.000	0.000	0.000	0.000
46	A	30	HIS	0	-0.071	-0.035	42.708	0.304	0.304	0.000	0.000	0.000	0.000
47	A	31	VAL	0	0.031	0.028	42.564	0.124	0.124	0.000	0.000	0.000	0.000
48	A	32	PRO	0	0.004	0.025	45.734	0.090	0.090	0.000	0.000	0.000	0.000
49	A	33	GLY	0	-0.039	-0.015	49.051	0.066	0.066	0.000	0.000	0.000	0.000
50	A	34	SER	0	-0.082	-0.036	46.840	0.013	0.013	0.000	0.000	0.000	0.000
51	A	35	LYS	1	0.872	0.939	46.794	6.716	6.716	0.000	0.000	0.000	0.000
52	A	36	TYR	0	0.012	-0.030	40.217	0.017	0.017	0.000	0.000	0.000	0.000
53	A	37	GLY	0	0.015	0.011	39.717	0.077	0.077	0.000	0.000	0.000	0.000
54	A	38	ILE	0	0.022	0.009	33.914	-0.051	-0.051	0.000	0.000	0.000	0.000
55	A	39	GLY	0	-0.010	-0.003	32.601	0.043	0.043	0.000	0.000	0.000	0.000
56	A	40	PHE	0	0.009	-0.012	25.875	-0.035	-0.035	0.000	0.000	0.000	0.000
57	A	41	SER	0	-0.022	-0.021	23.929	-0.015	-0.015	0.000	0.000	0.000	0.000
58	A	42	GLU	-1	-0.757	-0.855	23.299	-13.171	-13.171	0.000	0.000	0.000	0.000
59	A	43	ALA	0	-0.014	-0.016	19.137	-0.475	-0.475	0.000	0.000	0.000	0.000
60	A	44	SER	0	-0.105	-0.049	18.292	-1.130	-1.130	0.000	0.000	0.000	0.000
61	A	45	GLY	0	0.044	0.014	19.535	0.571	0.571	0.000	0.000	0.000	0.000
62	A	46	ASP	-1	-0.832	-0.902	21.324	-12.770	-12.770	0.000	0.000	0.000	0.000
63	A	47	ARG	1	0.839	0.930	15.856	17.605	17.605	0.000	0.000	0.000	0.000
64	A	48	LEU	0	0.005	0.010	22.629	0.119	0.119	0.000	0.000	0.000	0.000
65	A	49	ILE	0	-0.039	-0.020	26.185	-0.065	-0.065	0.000	0.000	0.000	0.000
66	A	50	ARG	1	0.785	0.869	26.685	11.962	11.962	0.000	0.000	0.000	0.000
67	A	51	TYR	0	-0.011	-0.024	30.902	-0.093	-0.093	0.000	0.000	0.000	0.000
68	A	52	ASP	-1	-0.801	-0.906	34.360	-8.603	-8.603	0.000	0.000	0.000	0.000
69	A	53	GLY	0	-0.009	-0.011	37.738	-0.061	-0.061	0.000	0.000	0.000	0.000
70	A	54	ASN	0	-0.036	-0.010	41.164	0.029	0.029	0.000	0.000	0.000	0.000
71	A	55	ASP	-1	-0.823	-0.932	43.763	-6.968	-6.968	0.000	0.000	0.000	0.000
72	A	56	ASP	-1	-0.795	-0.898	42.537	-7.734	-7.734	0.000	0.000	0.000	0.000
73	A	57	ASP	-1	-0.928	-0.952	41.341	-7.477	-7.477	0.000	0.000	0.000	0.000
74	A	58	LEU	0	-0.047	-0.022	40.569	-0.243	-0.243	0.000	0.000	0.000	0.000
75	A	59	VAL	0	0.027	0.021	37.667	-0.285	-0.285	0.000	0.000	0.000	0.000
76	A	60	LYS	1	0.831	0.909	36.873	7.640	7.640	0.000	0.000	0.000	0.000
77	A	61	ALA	0	-0.003	0.004	35.824	-0.281	-0.281	0.000	0.000	0.000	0.000
78	A	62	CYS	0	-0.041	-0.003	34.831	-0.262	-0.262	0.000	0.000	0.000	0.000
79	A	63	ILE	0	0.013	0.010	31.693	-0.412	-0.412	0.000	0.000	0.000	0.000
80	A	64	GLU	-1	-0.767	-0.840	30.937	-10.403	-10.403	0.000	0.000	0.000	0.000
81	A	65	ASN	0	0.009	-0.001	30.750	-0.357	-0.357	0.000	0.000	0.000	0.000
82	A	66	ILE	0	0.002	0.004	27.268	-0.386	-0.386	0.000	0.000	0.000	0.000
83	A	67	ARG	1	0.838	0.890	26.731	10.220	10.220	0.000	0.000	0.000	0.000
84	A	68	ARG	1	0.736	0.850	26.040	9.322	9.322	0.000	0.000	0.000	0.000
85	A	69	ILE	0	0.020	0.020	25.019	-0.402	-0.402	0.000	0.000	0.000	0.000
86	A	70	SER	0	-0.009	-0.001	21.015	-0.611	-0.611	0.000	0.000	0.000	0.000
87	A	71	ALA	0	0.011	0.016	21.035	-0.927	-0.927	0.000	0.000	0.000	0.000
88	A	72	GLY	0	0.012	0.023	20.276	0.656	0.656	0.000	0.000	0.000	0.000
89	A	73	HIS	0	0.024	0.006	21.259	0.126	0.126	0.000	0.000	0.000	0.000
90	A	74	THR	0	-0.021	-0.004	23.785	0.505	0.505	0.000	0.000	0.000	0.000
91	A	75	PHE	0	0.005	-0.003	26.237	0.059	0.059	0.000	0.000	0.000	0.000
92	A	76	VAL	0	-0.023	-0.017	29.942	0.017	0.017	0.000	0.000	0.000	0.000
93	A	77	ILE	0	0.015	0.010	33.023	0.065	0.065	0.000	0.000	0.000	0.000
94	A	78	LEU	0	-0.017	-0.012	36.649	0.046	0.046	0.000	0.000	0.000	0.000
95	A	79	ILE	0	0.014	-0.001	39.896	0.080	0.080	0.000	0.000	0.000	0.000
96	A	80	ARG	1	0.921	0.963	43.306	7.039	7.039	0.000	0.000	0.000	0.000
97	A	81	ASN	0	-0.003	-0.007	46.824	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	82	ALA	0	0.049	0.024	47.131	0.044	0.044	0.000	0.000	0.000	0.000
99	A	83	TYR	0	0.020	0.018	49.196	0.019	0.019	0.000	0.000	0.000	0.000
100	A	84	PRO	0	0.055	0.009	47.944	-0.136	-0.136	0.000	0.000	0.000	0.000
101	A	85	ILE	0	0.003	0.006	46.849	-0.153	-0.153	0.000	0.000	0.000	0.000
102	A	86	ASN	0	-0.010	-0.013	46.510	-0.024	-0.024	0.000	0.000	0.000	0.000
103	A	87	ILE	0	0.028	0.025	42.447	-0.192	-0.192	0.000	0.000	0.000	0.000
104	A	88	LEU	0	-0.006	-0.012	42.204	-0.216	-0.216	0.000	0.000	0.000	0.000
105	A	89	ASN	0	-0.011	-0.012	42.118	-0.192	-0.192	0.000	0.000	0.000	0.000
106	A	90	ALA	0	0.044	0.031	40.435	-0.156	-0.156	0.000	0.000	0.000	0.000
107	A	91	VAL	0	0.011	0.001	37.178	-0.270	-0.270	0.000	0.000	0.000	0.000
108	A	92	LYS	1	0.923	0.963	37.193	7.361	7.361	0.000	0.000	0.000	0.000
109	A	93	MET	0	0.009	0.016	37.637	-0.131	-0.131	0.000	0.000	0.000	0.000
110	A	94	CYS	0	-0.023	-0.021	34.017	-0.265	-0.265	0.000	0.000	0.000	0.000
111	A	95	GLN	0	-0.073	-0.037	33.055	-0.115	-0.115	0.000	0.000	0.000	0.000
112	A	96	GLU	-1	-0.948	-0.962	33.078	-8.552	-8.552	0.000	0.000	0.000	0.000
113	A	97	VAL	0	-0.015	-0.005	31.295	-0.208	-0.208	0.000	0.000	0.000	0.000
114	A	98	GLY	0	0.002	-0.012	28.707	-0.464	-0.464	0.000	0.000	0.000	0.000
115	A	99	SER	0	-0.049	-0.017	27.447	0.312	0.312	0.000	0.000	0.000	0.000
116	A	100	ILE	0	-0.033	-0.019	29.541	-0.173	-0.173	0.000	0.000	0.000	0.000
117	A	101	PHE	0	-0.034	-0.027	24.879	-0.128	-0.128	0.000	0.000	0.000	0.000
118	A	102	ALA	0	0.016	-0.005	30.974	0.139	0.139	0.000	0.000	0.000	0.000
119	A	103	ALA	0	-0.001	-0.007	34.587	-0.067	-0.067	0.000	0.000	0.000	0.000
120	A	104	THR	0	-0.034	-0.020	37.962	0.261	0.261	0.000	0.000	0.000	0.000
121	A	105	ALA	0	0.045	0.014	40.575	-0.031	-0.031	0.000	0.000	0.000	0.000
122	A	106	ASN	0	-0.065	-0.018	40.968	0.310	0.310	0.000	0.000	0.000	0.000
123	A	107	PRO	0	-0.009	-0.017	40.060	-0.176	-0.176	0.000	0.000	0.000	0.000
124	A	108	LEU	0	0.030	0.033	34.499	-0.075	-0.075	0.000	0.000	0.000	0.000
125	A	109	GLN	0	-0.020	-0.006	31.655	-0.219	-0.219	0.000	0.000	0.000	0.000
126	A	110	ILE	0	0.027	0.006	27.862	-0.053	-0.053	0.000	0.000	0.000	0.000
127	A	111	ILE	0	-0.008	-0.003	25.976	-0.148	-0.148	0.000	0.000	0.000	0.000
128	A	112	VAL	0	0.022	0.007	22.094	-0.277	-0.277	0.000	0.000	0.000	0.000
129	A	113	TYR	0	0.020	0.015	14.612	0.375	0.375	0.000	0.000	0.000	0.000
130	A	114	LYS	1	0.944	0.979	15.715	16.889	16.889	0.000	0.000	0.000	0.000
131	A	115	GLY	0	0.032	-0.003	13.974	-0.442	-0.442	0.000	0.000	0.000	0.000
132	A	116	GLU	-1	-0.845	-0.917	8.380	-28.897	-28.897	0.000	0.000	0.000	0.000
133	A	117	ARG	1	0.919	0.948	7.520	33.520	33.520	0.000	0.000	0.000	0.000
134	A	118	GLY	0	0.018	0.023	13.678	1.103	1.103	0.000	0.000	0.000	0.000
135	A	119	ASN	0	-0.038	-0.027	16.539	-1.533	-1.533	0.000	0.000	0.000	0.000
136	A	120	GLY	0	0.010	0.004	19.291	-0.322	-0.322	0.000	0.000	0.000	0.000
137	A	121	VAL	0	-0.019	-0.004	20.544	0.184	0.184	0.000	0.000	0.000	0.000
138	A	122	LEU	0	-0.039	-0.021	21.084	-0.322	-0.322	0.000	0.000	0.000	0.000
139	A	123	GLY	0	0.037	0.022	24.755	0.257	0.257	0.000	0.000	0.000	0.000
140	A	124	VAL	0	-0.033	-0.016	28.558	-0.180	-0.180	0.000	0.000	0.000	0.000
141	A	125	ILE	0	-0.031	-0.006	31.819	0.080	0.080	0.000	0.000	0.000	0.000
142	A	126	ASP	-1	-0.786	-0.874	34.901	-8.391	-8.391	0.000	0.000	0.000	0.000
143	A	127	GLY	0	0.027	0.017	37.747	0.168	0.168	0.000	0.000	0.000	0.000
144	A	128	TYR	0	-0.028	-0.025	39.757	-0.152	-0.152	0.000	0.000	0.000	0.000
145	A	129	SER	0	0.000	0.007	40.381	-0.048	-0.048	0.000	0.000	0.000	0.000
146	A	130	PRO	0	0.002	0.003	41.910	0.125	0.125	0.000	0.000	0.000	0.000
147	A	131	VAL	0	-0.010	-0.017	45.358	-0.041	-0.041	0.000	0.000	0.000	0.000
148	A	132	GLY	0	-0.008	-0.005	47.878	0.140	0.140	0.000	0.000	0.000	0.000
149	A	133	VAL	0	-0.067	-0.031	48.926	-0.162	-0.162	0.000	0.000	0.000	0.000
150	A	134	GLU	-1	-0.943	-0.961	51.121	-6.140	-6.140	0.000	0.000	0.000	0.000
151	A	135	SER	-1	-0.968	-0.980	53.782	-5.589	-5.589	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-15:HIS)