FMO DATABASE

FMODB ID: RQKR8

Calculation Name: 1J1H-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1J1H

Chain ID: A

ChEMBL ID:

UniProt ID: Q8RR57

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	123
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1067245.598696
FMO2-HF: Nuclear repulsion	1018846.64644
FMO2-HF: Total energy	-48398.952256
FMO2-MP2: Total energy	-48544.062794

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.
134.732	135.981	-0.006	-0.446	-0.796	0

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 : 0.862 / 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].
3	A	3	PRO	0	-0.003	0.017	3.845	-6.329	-5.279	-0.005	-0.426	-0.619
35	A	35	ARG	1	0.918	0.961	4.458	48.391	48.590	-0.001	-0.020	-0.177
4	A	4	VAL	0	0.000	0.000	6.081	2.716	2.716	0.000	0.000	0.000
5	A	5	LEU	0	-0.021	0.003	8.750	2.671	2.671	0.000	0.000	0.000
6	A	6	GLU	-1	-0.912	-0.962	10.669	-25.703	-25.703	0.000	0.000	0.000
7	A	7	ASN	0	0.030	0.019	12.680	0.007	0.007	0.000	0.000	0.000
8	A	8	ARG	1	0.942	0.969	15.572	18.567	18.567	0.000	0.000	0.000
9	A	9	ARG	1	0.957	0.973	17.409	12.930	12.930	0.000	0.000	0.000
10	A	10	ALA	0	0.016	0.024	19.806	0.545	0.545	0.000	0.000	0.000
11	A	11	ARG	1	0.917	0.951	15.393	18.630	18.630	0.000	0.000	0.000
12	A	12	HIS	0	-0.052	-0.024	19.072	-0.608	-0.608	0.000	0.000	0.000
13	A	13	ASP	-1	-0.921	-0.958	20.808	-12.041	-12.041	0.000	0.000	0.000
14	A	14	TYR	0	-0.014	-0.005	23.707	0.512	0.512	0.000	0.000	0.000
15	A	15	GLU	-1	-0.906	-0.944	24.146	-11.738	-11.738	0.000	0.000	0.000
16	A	16	ILE	0	-0.096	-0.030	22.345	0.178	0.178	0.000	0.000	0.000
17	A	17	LEU	0	-0.016	0.002	25.390	0.110	0.110	0.000	0.000	0.000
18	A	18	GLU	-1	-0.860	-0.935	27.663	-10.115	-10.115	0.000	0.000	0.000
19	A	19	THR	0	-0.006	-0.020	22.785	-0.228	-0.228	0.000	0.000	0.000
20	A	20	TYR	0	0.080	0.026	21.543	0.206	0.206	0.000	0.000	0.000
21	A	21	GLU	-1	-0.928	-0.970	19.391	-16.099	-16.099	0.000	0.000	0.000
22	A	22	ALA	0	-0.021	-0.024	20.106	0.554	0.554	0.000	0.000	0.000
23	A	23	GLY	0	0.008	0.006	18.865	-0.993	-0.993	0.000	0.000	0.000
24	A	24	ILE	0	-0.072	-0.023	17.128	0.690	0.690	0.000	0.000	0.000
25	A	25	ALA	0	0.029	0.011	16.944	-0.970	-0.970	0.000	0.000	0.000
26	A	26	LEU	0	-0.041	-0.018	12.928	-0.176	-0.176	0.000	0.000	0.000
27	A	27	LYS	1	0.959	0.966	17.340	14.127	14.127	0.000	0.000	0.000
28	A	28	GLY	0	0.081	0.042	16.301	-1.002	-1.002	0.000	0.000	0.000
29	A	29	THR	0	-0.009	-0.032	15.325	-1.242	-1.242	0.000	0.000	0.000
30	A	30	GLU	-1	-0.821	-0.907	14.686	-17.880	-17.880	0.000	0.000	0.000
31	A	31	VAL	0	0.029	0.035	9.409	-1.402	-1.402	0.000	0.000	0.000
32	A	32	LYS	1	0.915	0.963	10.049	19.583	19.583	0.000	0.000	0.000
33	A	33	SER	0	0.012	-0.002	10.268	-0.844	-0.844	0.000	0.000	0.000
34	A	34	LEU	0	0.013	0.009	11.458	0.351	0.351	0.000	0.000	0.000
36	A	36	ALA	0	-0.032	-0.005	6.220	-5.542	-5.542	0.000	0.000	0.000
37	A	37	GLY	0	0.018	0.016	8.024	2.489	2.489	0.000	0.000	0.000
38	A	38	LYS	1	0.936	0.969	9.447	24.241	24.241	0.000	0.000	0.000
39	A	39	VAL	0	-0.010	-0.019	12.735	1.079	1.079	0.000	0.000	0.000
40	A	40	ASP	-1	-0.888	-0.928	15.580	-16.190	-16.190	0.000	0.000	0.000
41	A	41	PHE	0	-0.019	-0.029	15.257	0.571	0.571	0.000	0.000	0.000
42	A	42	THR	0	0.017	-0.018	18.129	0.115	0.115	0.000	0.000	0.000
43	A	43	GLY	0	0.021	0.016	21.447	0.100	0.100	0.000	0.000	0.000
44	A	44	SER	0	-0.017	0.005	21.593	0.394	0.394	0.000	0.000	0.000
45	A	45	PHE	0	0.058	0.005	24.332	0.253	0.253	0.000	0.000	0.000
46	A	46	ALA	0	-0.028	-0.017	23.872	-0.402	-0.402	0.000	0.000	0.000
47	A	47	ARG	1	0.912	0.945	25.966	9.756	9.756	0.000	0.000	0.000
48	A	48	PHE	0	0.006	-0.021	28.458	-0.457	-0.457	0.000	0.000	0.000
49	A	49	GLU	-1	-0.806	-0.878	30.885	-9.123	-9.123	0.000	0.000	0.000
50	A	50	ASP	-1	-0.857	-0.944	33.114	-8.862	-8.862	0.000	0.000	0.000
51	A	51	GLY	0	-0.011	-0.043	31.932	0.242	0.242	0.000	0.000	0.000
52	A	52	GLU	-1	-0.904	-0.901	28.504	-10.590	-10.590	0.000	0.000	0.000
53	A	53	LEU	0	0.001	0.009	22.700	0.184	0.184	0.000	0.000	0.000
54	A	54	TYR	0	-0.040	-0.065	25.069	-0.744	-0.744	0.000	0.000	0.000
55	A	55	LEU	0	-0.034	-0.015	19.268	-0.047	-0.047	0.000	0.000	0.000
56	A	56	GLU	-1	-0.933	-0.960	23.786	-10.298	-10.298	0.000	0.000	0.000
57	A	57	ASN	0	-0.019	-0.006	25.692	0.400	0.400	0.000	0.000	0.000
58	A	58	LEU	0	-0.017	-0.005	19.637	-0.471	-0.471	0.000	0.000	0.000
59	A	59	TYR	0	0.008	0.005	21.088	-0.116	-0.116	0.000	0.000	0.000
60	A	60	ILE	0	-0.026	-0.020	15.191	-0.607	-0.607	0.000	0.000	0.000
61	A	61	ALA	0	0.062	0.025	16.555	0.597	0.597	0.000	0.000	0.000
62	A	62	PRO	0	-0.055	-0.025	13.398	-1.060	-1.060	0.000	0.000	0.000
63	A	63	TYR	0	0.067	0.000	13.346	-0.343	-0.343	0.000	0.000	0.000
64	A	64	GLU	-1	-0.851	-0.943	15.919	-14.130	-14.130	0.000	0.000	0.000
65	A	65	LYS	1	0.869	0.942	17.994	15.905	15.905	0.000	0.000	0.000
66	A	66	GLY	0	0.026	0.027	19.926	0.382	0.382	0.000	0.000	0.000
67	A	67	SER	0	-0.014	0.002	23.603	-0.029	-0.029	0.000	0.000	0.000
68	A	68	TYR	0	0.005	-0.008	24.863	0.411	0.411	0.000	0.000	0.000
69	A	69	ALA	0	0.005	0.000	28.311	-0.134	-0.134	0.000	0.000	0.000
70	A	70	ASN	0	-0.012	-0.019	27.558	-0.137	-0.137	0.000	0.000	0.000
71	A	71	VAL	0	-0.064	0.000	23.161	0.120	0.120	0.000	0.000	0.000
72	A	72	ASP	-1	-0.861	-0.921	23.714	-12.078	-12.078	0.000	0.000	0.000
73	A	73	PRO	0	-0.029	-0.006	18.208	-0.356	-0.356	0.000	0.000	0.000
74	A	74	ARG	1	0.847	0.905	16.780	14.694	14.694	0.000	0.000	0.000
75	A	75	ARG	1	1.002	1.010	17.489	14.884	14.884	0.000	0.000	0.000
76	A	76	LYS	1	0.921	0.982	18.517	12.620	12.620	0.000	0.000	0.000
77	A	77	ARG	1	0.943	0.954	21.485	11.927	11.927	0.000	0.000	0.000
78	A	78	LYS	1	0.924	0.964	22.830	11.492	11.492	0.000	0.000	0.000
79	A	79	LEU	0	0.015	0.016	19.420	-0.461	-0.461	0.000	0.000	0.000
80	A	80	LEU	0	0.018	0.001	21.794	0.632	0.632	0.000	0.000	0.000
81	A	81	LEU	0	0.006	0.016	22.725	-0.553	-0.553	0.000	0.000	0.000
82	A	82	HIS	0	0.042	0.038	25.161	0.708	0.708	0.000	0.000	0.000
83	A	83	LYS	1	0.974	0.990	27.625	8.919	8.919	0.000	0.000	0.000
84	A	84	HIS	0	-0.007	-0.013	30.716	0.073	0.073	0.000	0.000	0.000
85	A	85	GLU	-1	-0.883	-0.937	25.763	-11.677	-11.677	0.000	0.000	0.000
86	A	86	LEU	0	-0.075	-0.030	27.831	-0.076	-0.076	0.000	0.000	0.000
87	A	87	ARG	1	0.942	0.970	28.694	8.677	8.677	0.000	0.000	0.000
88	A	88	ARG	1	0.933	0.978	30.309	9.847	9.847	0.000	0.000	0.000
89	A	89	LEU	0	0.008	0.022	25.844	0.135	0.135	0.000	0.000	0.000
90	A	90	LEU	0	0.014	-0.006	29.005	0.050	0.050	0.000	0.000	0.000
91	A	91	GLY	0	0.016	0.006	30.852	0.182	0.182	0.000	0.000	0.000
92	A	92	LYS	1	0.903	0.965	31.465	9.440	9.440	0.000	0.000	0.000
93	A	93	VAL	0	-0.022	-0.040	28.927	0.070	0.070	0.000	0.000	0.000
94	A	94	GLU	-1	-0.964	-0.972	32.260	-8.407	-8.407	0.000	0.000	0.000
95	A	95	GLN	0	-0.026	0.005	35.535	0.060	0.060	0.000	0.000	0.000
96	A	96	LYS	1	0.957	0.951	36.305	7.923	7.923	0.000	0.000	0.000
97	A	97	GLY	0	-0.006	0.014	35.091	-0.006	-0.006	0.000	0.000	0.000
98	A	98	LEU	0	-0.012	0.024	31.560	-0.216	-0.216	0.000	0.000	0.000
99	A	99	THR	0	-0.033	-0.023	27.050	-0.035	-0.035	0.000	0.000	0.000
100	A	100	LEU	0	0.032	0.031	26.341	-0.183	-0.183	0.000	0.000	0.000
101	A	101	VAL	0	0.073	0.040	20.466	-0.160	-0.160	0.000	0.000	0.000
102	A	102	PRO	0	-0.027	-0.014	19.167	-0.176	-0.176	0.000	0.000	0.000
103	A	103	LEU	0	0.007	-0.006	17.569	-1.157	-1.157	0.000	0.000	0.000
104	A	104	LYS	1	0.891	0.947	11.132	23.398	23.398	0.000	0.000	0.000
105	A	105	ILE	0	0.020	0.036	12.536	0.827	0.827	0.000	0.000	0.000
106	A	106	TYR	0	0.016	-0.005	7.148	-2.626	-2.626	0.000	0.000	0.000
107	A	107	PHE	0	0.037	0.007	9.272	2.223	2.223	0.000	0.000	0.000
108	A	108	ASN	0	-0.047	-0.023	8.923	-5.173	-5.173	0.000	0.000	0.000
109	A	109	GLU	-1	-0.910	-0.973	11.012	-20.315	-20.315	0.000	0.000	0.000
110	A	110	ARG	1	0.950	0.985	13.255	19.298	19.298	0.000	0.000	0.000
111	A	111	GLY	0	0.024	0.014	15.974	0.857	0.857	0.000	0.000	0.000
112	A	112	TYR	0	-0.005	-0.010	15.163	0.616	0.616	0.000	0.000	0.000
113	A	113	ALA	0	0.003	-0.001	13.551	-2.009	-2.009	0.000	0.000	0.000
114	A	114	LYS	1	0.938	0.979	13.771	20.686	20.686	0.000	0.000	0.000
115	A	115	VAL	0	-0.022	-0.022	14.784	-1.229	-1.229	0.000	0.000	0.000
116	A	116	LEU	0	0.044	0.027	16.804	0.749	0.749	0.000	0.000	0.000
117	A	117	LEU	0	-0.078	-0.015	18.591	-0.383	-0.383	0.000	0.000	0.000
118	A	118	GLY	0	0.035	-0.028	21.609	-0.041	-0.041	0.000	0.000	0.000
119	A	119	LEU	0	-0.025	0.001	23.248	0.038	0.038	0.000	0.000	0.000
120	A	120	ALA	0	-0.030	-0.006	25.793	0.003	0.003	0.000	0.000	0.000
121	A	121	ARG	1	0.875	0.896	27.575	9.741	9.741	0.000	0.000	0.000
122	A	122	GLY	0	0.017	0.020	31.353	0.003	0.003	0.000	0.000	0.000
123	A	123	LYS	0	0.088	0.068	32.816	-0.078	-0.078	0.000	0.000	0.000

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