FMO DATABASE

FMODB ID: 7KGQK

Calculation Name: 1R9H-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1R9H

Chain ID: A

ChEMBL ID:

UniProt ID: O45418

Base Structure: X-ray

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	118
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-915713.95295
FMO2-HF: Nuclear repulsion	871919.879744
FMO2-HF: Total energy	-43794.073205
FMO2-MP2: Total energy	-43924.560165

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:5:LYS)

Summations of interaction energy for fragment #1(A:5:LYS)

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.
-200.54	-189.822	17.256	-12.458	-15.515	-0.143

Interaction energy analysis for fragmet #1(A:5:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 2 / q_Mulliken : 1.719 / q_NPA : 1.861

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	7	ASP	-1	-0.751	-0.845	3.863	-57.573	-56.179	-0.014	-0.544	-0.836	0.000
13	A	17	LEU	0	-0.018	0.000	2.257	-5.143	-3.731	1.180	-0.618	-1.973	-0.006
14	A	18	LYS	1	0.812	0.912	4.196	52.056	52.745	0.002	-0.168	-0.522	-0.001
15	A	19	LEU	0	-0.041	-0.042	2.192	-36.595	-32.576	6.333	-4.786	-5.567	-0.049
16	A	20	ILE	0	0.015	0.018	3.731	6.642	6.843	0.012	-0.093	-0.120	-0.001
83	A	87	GLU	-1	-0.802	-0.891	1.925	-155.592	-154.449	8.230	-5.076	-4.297	-0.071
85	A	89	THR	0	-0.006	-0.002	2.639	-10.957	-9.270	1.515	-1.155	-2.048	-0.015
86	A	90	ILE	0	-0.024	-0.011	4.816	1.451	1.494	-0.001	-0.009	-0.032	0.000
108	A	112	ILE	0	0.006	0.004	4.337	-8.393	-8.263	-0.001	-0.009	-0.120	0.000
4	A	8	ILE	0	-0.015	-0.015	5.989	5.168	5.168	0.000	0.000	0.000	0.000
5	A	9	THR	0	-0.013	-0.006	8.815	5.919	5.919	0.000	0.000	0.000	0.000
6	A	10	PRO	0	-0.023	-0.027	11.148	0.178	0.178	0.000	0.000	0.000	0.000
7	A	11	LYS	1	0.893	0.933	13.822	32.442	32.442	0.000	0.000	0.000	0.000
8	A	12	LYS	1	0.875	0.962	9.185	50.252	50.252	0.000	0.000	0.000	0.000
9	A	13	ASP	-1	-0.705	-0.819	10.994	-43.192	-43.192	0.000	0.000	0.000	0.000
10	A	14	GLY	0	0.034	0.027	7.817	1.379	1.379	0.000	0.000	0.000	0.000
11	A	15	GLY	0	-0.036	-0.015	7.880	-3.199	-3.199	0.000	0.000	0.000	0.000
12	A	16	VAL	0	-0.005	-0.010	7.702	-0.102	-0.102	0.000	0.000	0.000	0.000
17	A	21	LYS	1	0.854	0.922	4.927	81.208	81.208	0.000	0.000	0.000	0.000
18	A	22	LYS	1	0.960	0.983	9.745	38.203	38.203	0.000	0.000	0.000	0.000
19	A	23	GLU	-1	-0.894	-0.946	11.510	-44.898	-44.898	0.000	0.000	0.000	0.000
20	A	24	GLY	0	0.008	0.010	13.262	1.744	1.744	0.000	0.000	0.000	0.000
21	A	25	GLN	0	-0.045	-0.031	16.169	0.660	0.660	0.000	0.000	0.000	0.000
22	A	26	GLY	0	0.009	0.004	19.479	0.754	0.754	0.000	0.000	0.000	0.000
23	A	27	VAL	0	0.041	0.006	17.568	-1.549	-1.549	0.000	0.000	0.000	0.000
24	A	28	VAL	0	-0.019	-0.006	17.957	-1.081	-1.081	0.000	0.000	0.000	0.000
25	A	29	LYS	1	0.907	0.955	13.736	35.690	35.690	0.000	0.000	0.000	0.000
26	A	30	PRO	0	0.016	0.038	17.204	1.708	1.708	0.000	0.000	0.000	0.000
27	A	31	THR	0	0.001	-0.015	19.265	-0.621	-0.621	0.000	0.000	0.000	0.000
28	A	32	THR	0	-0.017	-0.017	21.741	-0.088	-0.088	0.000	0.000	0.000	0.000
29	A	33	GLY	0	-0.044	-0.011	23.650	0.877	0.877	0.000	0.000	0.000	0.000
30	A	34	THR	0	-0.041	-0.012	23.086	0.240	0.240	0.000	0.000	0.000	0.000
31	A	35	THR	0	0.009	-0.004	24.265	-0.687	-0.687	0.000	0.000	0.000	0.000
32	A	36	VAL	0	-0.023	-0.020	19.417	0.063	0.063	0.000	0.000	0.000	0.000
33	A	37	LYS	1	0.876	0.930	21.973	23.925	23.925	0.000	0.000	0.000	0.000
34	A	38	VAL	0	0.000	-0.015	16.752	-1.000	-1.000	0.000	0.000	0.000	0.000
35	A	39	HIS	0	0.037	0.036	17.630	0.650	0.650	0.000	0.000	0.000	0.000
36	A	40	TYR	0	-0.065	-0.069	13.809	-2.141	-2.141	0.000	0.000	0.000	0.000
37	A	41	VAL	0	-0.001	-0.004	12.341	2.745	2.745	0.000	0.000	0.000	0.000
38	A	42	GLY	0	0.029	0.015	11.710	-3.644	-3.644	0.000	0.000	0.000	0.000
39	A	43	THR	0	-0.011	-0.024	9.676	2.408	2.408	0.000	0.000	0.000	0.000
40	A	44	LEU	0	0.024	0.019	10.481	-2.780	-2.780	0.000	0.000	0.000	0.000
41	A	45	GLU	-1	-0.875	-0.950	6.647	-61.756	-61.756	0.000	0.000	0.000	0.000
42	A	46	ASN	0	-0.017	0.015	8.744	-2.636	-2.636	0.000	0.000	0.000	0.000
43	A	47	GLY	0	0.041	0.028	10.441	2.176	2.176	0.000	0.000	0.000	0.000
44	A	48	THR	0	-0.051	-0.049	11.510	2.826	2.826	0.000	0.000	0.000	0.000
45	A	49	LYS	1	0.858	0.907	14.154	30.690	30.690	0.000	0.000	0.000	0.000
46	A	50	PHE	0	-0.023	-0.026	12.322	2.681	2.681	0.000	0.000	0.000	0.000
47	A	51	ASP	-1	-0.788	-0.845	16.030	-27.978	-27.978	0.000	0.000	0.000	0.000
48	A	52	SER	0	-0.042	-0.052	15.917	-2.653	-2.653	0.000	0.000	0.000	0.000
49	A	53	SER	0	-0.011	-0.001	17.753	0.853	0.853	0.000	0.000	0.000	0.000
50	A	54	ARG	1	0.854	0.907	14.628	37.374	37.374	0.000	0.000	0.000	0.000
51	A	55	ASP	-1	-0.834	-0.882	18.994	-29.183	-29.183	0.000	0.000	0.000	0.000
52	A	56	ARG	1	0.843	0.904	20.534	28.006	28.006	0.000	0.000	0.000	0.000
53	A	57	GLY	0	0.003	0.025	23.326	0.932	0.932	0.000	0.000	0.000	0.000
54	A	58	ASP	-1	-0.901	-0.941	24.433	-21.916	-21.916	0.000	0.000	0.000	0.000
55	A	59	GLN	0	-0.079	-0.046	22.104	-0.597	-0.597	0.000	0.000	0.000	0.000
56	A	60	PHE	0	0.008	0.004	18.744	0.914	0.914	0.000	0.000	0.000	0.000
57	A	61	SER	0	0.003	-0.004	21.569	-0.552	-0.552	0.000	0.000	0.000	0.000
58	A	62	PHE	0	-0.023	-0.009	17.524	0.418	0.418	0.000	0.000	0.000	0.000
59	A	63	ASN	0	0.038	0.031	23.200	-0.150	-0.150	0.000	0.000	0.000	0.000
60	A	64	LEU	0	0.003	0.018	17.744	-0.459	-0.459	0.000	0.000	0.000	0.000
61	A	65	GLY	0	0.018	0.005	20.832	1.148	1.148	0.000	0.000	0.000	0.000
62	A	66	ARG	1	0.828	0.891	22.063	24.563	24.563	0.000	0.000	0.000	0.000
63	A	67	GLY	0	0.024	0.025	21.588	0.832	0.832	0.000	0.000	0.000	0.000
64	A	68	ASN	0	-0.056	-0.036	22.598	0.668	0.668	0.000	0.000	0.000	0.000
65	A	69	VAL	0	0.013	0.023	17.422	-0.059	-0.059	0.000	0.000	0.000	0.000
66	A	70	ILE	0	0.017	0.022	12.998	0.380	0.380	0.000	0.000	0.000	0.000
67	A	71	LYS	1	0.975	0.987	15.900	29.621	29.621	0.000	0.000	0.000	0.000
68	A	72	GLY	0	0.033	0.005	11.895	-0.488	-0.488	0.000	0.000	0.000	0.000
69	A	73	TRP	0	-0.029	-0.011	11.895	-2.257	-2.257	0.000	0.000	0.000	0.000
70	A	74	ASP	-1	-0.757	-0.886	13.939	-29.783	-29.783	0.000	0.000	0.000	0.000
71	A	75	LEU	0	-0.054	-0.017	11.501	0.794	0.794	0.000	0.000	0.000	0.000
72	A	76	GLY	0	0.044	0.012	11.136	-0.889	-0.889	0.000	0.000	0.000	0.000
73	A	77	VAL	0	0.031	0.007	11.887	-1.256	-1.256	0.000	0.000	0.000	0.000
74	A	78	ALA	0	0.024	0.028	14.564	0.921	0.921	0.000	0.000	0.000	0.000
75	A	79	THR	0	-0.059	-0.048	10.467	-1.239	-1.239	0.000	0.000	0.000	0.000
76	A	80	MET	0	-0.116	-0.044	11.574	-1.960	-1.960	0.000	0.000	0.000	0.000
77	A	81	THR	0	-0.008	-0.021	13.379	2.977	2.977	0.000	0.000	0.000	0.000
78	A	82	LYS	1	0.913	0.960	15.870	25.853	25.853	0.000	0.000	0.000	0.000
79	A	83	GLY	0	0.000	-0.003	18.241	0.567	0.567	0.000	0.000	0.000	0.000
80	A	84	GLU	-1	-0.768	-0.846	10.726	-49.215	-49.215	0.000	0.000	0.000	0.000
81	A	85	VAL	0	0.006	-0.009	11.286	1.136	1.136	0.000	0.000	0.000	0.000
82	A	86	ALA	0	-0.020	-0.010	7.998	-3.818	-3.818	0.000	0.000	0.000	0.000
84	A	88	PHE	0	-0.021	-0.025	5.244	-7.875	-7.875	0.000	0.000	0.000	0.000
87	A	91	ARG	1	0.814	0.864	8.578	46.205	46.205	0.000	0.000	0.000	0.000
88	A	92	SER	0	0.079	0.043	10.445	1.069	1.069	0.000	0.000	0.000	0.000
89	A	93	ASP	-1	-0.787	-0.862	13.386	-38.653	-38.653	0.000	0.000	0.000	0.000
90	A	94	TYR	0	-0.089	-0.087	12.145	1.999	1.999	0.000	0.000	0.000	0.000
91	A	95	GLY	0	0.006	-0.001	14.080	-0.517	-0.517	0.000	0.000	0.000	0.000
92	A	96	TYR	0	0.007	-0.008	14.797	1.149	1.149	0.000	0.000	0.000	0.000
93	A	97	GLY	0	-0.005	0.002	16.929	1.625	1.625	0.000	0.000	0.000	0.000
94	A	98	ASP	-1	-0.880	-0.955	17.906	-30.162	-30.162	0.000	0.000	0.000	0.000
95	A	99	ALA	0	-0.034	-0.008	20.080	0.838	0.838	0.000	0.000	0.000	0.000
96	A	100	GLY	0	-0.009	0.008	18.341	0.179	0.179	0.000	0.000	0.000	0.000
97	A	101	SER	0	-0.027	-0.033	19.319	1.245	1.245	0.000	0.000	0.000	0.000
98	A	102	PRO	0	0.027	0.029	20.537	-0.638	-0.638	0.000	0.000	0.000	0.000
99	A	103	PRO	0	-0.023	-0.017	23.168	0.055	0.055	0.000	0.000	0.000	0.000
100	A	104	LYS	1	0.942	0.957	18.476	26.875	26.875	0.000	0.000	0.000	0.000
101	A	105	ILE	0	-0.010	0.014	15.190	-1.436	-1.436	0.000	0.000	0.000	0.000
102	A	106	PRO	0	0.029	0.011	15.820	1.311	1.311	0.000	0.000	0.000	0.000
103	A	107	GLY	0	0.025	0.026	17.049	-1.227	-1.227	0.000	0.000	0.000	0.000
104	A	108	GLY	0	0.002	-0.018	16.205	-0.090	-0.090	0.000	0.000	0.000	0.000
105	A	109	ALA	0	-0.072	-0.024	13.205	-1.952	-1.952	0.000	0.000	0.000	0.000
106	A	110	THR	0	-0.038	-0.014	6.648	0.837	0.837	0.000	0.000	0.000	0.000
107	A	111	LEU	0	-0.060	-0.029	9.366	1.724	1.724	0.000	0.000	0.000	0.000
109	A	113	PHE	0	0.028	0.005	7.243	7.572	7.572	0.000	0.000	0.000	0.000
110	A	114	GLU	-1	-0.941	-0.962	7.631	-60.612	-60.612	0.000	0.000	0.000	0.000
111	A	115	VAL	0	-0.008	-0.017	9.757	5.009	5.009	0.000	0.000	0.000	0.000
112	A	116	GLU	-1	-0.836	-0.902	12.375	-37.040	-37.040	0.000	0.000	0.000	0.000
113	A	117	LEU	0	0.006	0.010	15.235	2.016	2.016	0.000	0.000	0.000	0.000
114	A	118	PHE	0	-0.002	-0.004	17.415	0.328	0.328	0.000	0.000	0.000	0.000
115	A	119	GLU	-1	-0.900	-0.954	20.949	-22.838	-22.838	0.000	0.000	0.000	0.000
116	A	120	TRP	0	0.017	-0.006	18.950	-1.526	-1.526	0.000	0.000	0.000	0.000
117	A	121	SER	0	-0.048	-0.011	24.132	0.354	0.354	0.000	0.000	0.000	0.000
118	A	122	ALA	-1	-0.861	-0.916	26.892	-20.977	-20.977	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:5:LYS)