FMO DATABASE

FMODB ID: Y94M2

Calculation Name: 1ORJ-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1ORJ

Chain ID: A

ChEMBL ID:

UniProt ID: O67806

Base Structure: X-ray

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	126
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1148125.016522
FMO2-HF: Nuclear repulsion	1096444.871263
FMO2-HF: Total energy	-51680.145258
FMO2-MP2: Total energy	-51833.684288

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:1002:ARG)

Summations of interaction energy for fragment #1(A:1002:ARG)

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.
-335.213	-333.313	19.171	-10.375	-10.697	-0.122

Interaction energy analysis for fragmet #1(A:1002:ARG)

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 : 1.832

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	1004	ILE	0	0.120	0.065	3.860	-4.034	-2.727	-0.006	-0.504	-0.798	-0.002
75	A	1076	LYS	1	0.740	0.857	4.568	57.413	57.541	-0.001	-0.005	-0.121	0.000
76	A	1077	GLU	-1	-0.792	-0.902	1.706	-166.254	-166.458	16.896	-9.194	-7.499	-0.112
77	A	1078	ILE	0	-0.077	-0.023	2.308	-2.644	-1.999	2.283	-0.670	-2.258	-0.008
78	A	1079	ALA	0	0.099	0.048	5.255	5.481	5.505	-0.001	-0.002	-0.021	0.000
4	A	1005	ALA	0	0.049	0.028	6.035	5.564	5.564	0.000	0.000	0.000	0.000
5	A	1006	GLU	-1	-0.816	-0.902	5.116	-60.377	-60.377	0.000	0.000	0.000	0.000
6	A	1007	ALA	0	-0.047	-0.006	7.258	2.843	2.843	0.000	0.000	0.000	0.000
7	A	1008	TYR	0	-0.035	-0.020	8.728	3.307	3.307	0.000	0.000	0.000	0.000
8	A	1009	PHE	0	-0.014	-0.002	10.708	3.603	3.603	0.000	0.000	0.000	0.000
9	A	1010	GLN	0	-0.010	0.001	10.403	-3.930	-3.930	0.000	0.000	0.000	0.000
10	A	1011	ASN	0	-0.058	-0.054	7.530	4.760	4.760	0.000	0.000	0.000	0.000
11	A	1012	MET	0	-0.016	0.005	10.426	-0.785	-0.785	0.000	0.000	0.000	0.000
12	A	1013	VAL	0	-0.033	-0.008	13.697	3.062	3.062	0.000	0.000	0.000	0.000
13	A	1014	GLU	-1	-0.827	-0.921	14.851	-33.557	-33.557	0.000	0.000	0.000	0.000
14	A	1015	THR	0	-0.077	-0.043	17.454	1.090	1.090	0.000	0.000	0.000	0.000
15	A	1016	ALA	0	0.053	0.022	17.997	-1.056	-1.056	0.000	0.000	0.000	0.000
16	A	1017	THR	0	0.017	0.020	18.948	-0.552	-0.552	0.000	0.000	0.000	0.000
17	A	1018	PRO	0	-0.025	-0.026	17.364	0.236	0.236	0.000	0.000	0.000	0.000
18	A	1019	LEU	0	0.026	0.018	13.180	-0.683	-0.683	0.000	0.000	0.000	0.000
19	A	1020	GLU	-1	-0.867	-0.938	16.531	-27.870	-27.870	0.000	0.000	0.000	0.000
20	A	1021	GLN	0	0.014	0.001	19.364	0.676	0.676	0.000	0.000	0.000	0.000
21	A	1022	ILE	0	-0.033	-0.003	13.702	0.575	0.575	0.000	0.000	0.000	0.000
22	A	1023	ILE	0	0.007	0.011	15.423	-0.029	-0.029	0.000	0.000	0.000	0.000
23	A	1024	LEU	0	0.034	0.019	17.440	0.888	0.888	0.000	0.000	0.000	0.000
24	A	1025	LEU	0	-0.037	-0.010	18.957	1.080	1.080	0.000	0.000	0.000	0.000
25	A	1026	TYR	0	0.011	-0.023	12.559	-0.222	-0.222	0.000	0.000	0.000	0.000
26	A	1027	ASP	-1	-0.825	-0.898	18.106	-27.683	-27.683	0.000	0.000	0.000	0.000
27	A	1028	LYS	1	0.839	0.910	20.865	22.575	22.575	0.000	0.000	0.000	0.000
28	A	1029	ALA	0	0.014	0.006	19.806	0.968	0.968	0.000	0.000	0.000	0.000
29	A	1030	ILE	0	-0.005	-0.009	17.314	0.616	0.616	0.000	0.000	0.000	0.000
30	A	1031	GLU	-1	-0.858	-0.908	21.615	-20.596	-20.596	0.000	0.000	0.000	0.000
31	A	1032	CYS	0	-0.066	-0.035	25.223	1.081	1.081	0.000	0.000	0.000	0.000
32	A	1033	LEU	0	0.034	0.009	21.376	0.737	0.737	0.000	0.000	0.000	0.000
33	A	1034	GLU	-1	-0.863	-0.942	23.323	-23.825	-23.825	0.000	0.000	0.000	0.000
34	A	1035	ARG	1	0.806	0.870	26.258	18.334	18.334	0.000	0.000	0.000	0.000
35	A	1036	ALA	0	0.010	-0.003	27.752	0.706	0.706	0.000	0.000	0.000	0.000
36	A	1037	ILE	0	-0.014	-0.018	24.432	0.578	0.578	0.000	0.000	0.000	0.000
37	A	1038	GLU	-1	-0.947	-0.951	28.990	-17.864	-17.864	0.000	0.000	0.000	0.000
38	A	1039	ILE	0	-0.033	-0.028	31.654	0.686	0.686	0.000	0.000	0.000	0.000
39	A	1040	TYR	0	-0.027	-0.021	30.679	0.594	0.594	0.000	0.000	0.000	0.000
40	A	1041	ASP	-1	-0.855	-0.926	33.366	-17.459	-17.459	0.000	0.000	0.000	0.000
41	A	1042	GLN	0	0.009	0.007	36.360	0.779	0.779	0.000	0.000	0.000	0.000
42	A	1043	VAL	0	-0.004	0.017	35.246	0.470	0.470	0.000	0.000	0.000	0.000
43	A	1044	ASN	0	0.010	0.010	38.512	0.208	0.208	0.000	0.000	0.000	0.000
44	A	1045	GLU	-1	-0.872	-0.933	41.522	-14.379	-14.379	0.000	0.000	0.000	0.000
45	A	1046	LEU	0	-0.015	-0.014	41.242	-0.361	-0.361	0.000	0.000	0.000	0.000
46	A	1047	GLU	-1	-0.912	-0.965	41.314	-14.168	-14.168	0.000	0.000	0.000	0.000
47	A	1048	LYS	1	0.900	0.955	37.655	14.907	14.907	0.000	0.000	0.000	0.000
48	A	1049	ARG	1	0.882	0.932	36.692	14.519	14.519	0.000	0.000	0.000	0.000
49	A	1050	LYS	1	0.927	0.967	36.634	14.100	14.100	0.000	0.000	0.000	0.000
50	A	1051	GLU	-1	-0.766	-0.853	34.357	-17.422	-17.422	0.000	0.000	0.000	0.000
51	A	1052	PHE	0	0.003	0.002	30.470	-0.634	-0.634	0.000	0.000	0.000	0.000
52	A	1053	VAL	0	-0.031	-0.016	31.737	-0.611	-0.611	0.000	0.000	0.000	0.000
53	A	1054	GLU	-1	-0.831	-0.896	31.819	-17.542	-17.542	0.000	0.000	0.000	0.000
54	A	1055	ASN	0	-0.094	-0.060	29.173	-0.887	-0.887	0.000	0.000	0.000	0.000
55	A	1056	ILE	0	0.007	0.001	27.186	-0.955	-0.955	0.000	0.000	0.000	0.000
56	A	1057	ASP	-1	-0.902	-0.948	27.129	-20.115	-20.115	0.000	0.000	0.000	0.000
57	A	1058	ARG	1	0.841	0.907	27.369	18.238	18.238	0.000	0.000	0.000	0.000
58	A	1059	VAL	0	-0.006	0.000	21.960	-0.895	-0.895	0.000	0.000	0.000	0.000
59	A	1060	TYR	0	-0.004	-0.003	22.765	-1.540	-1.540	0.000	0.000	0.000	0.000
60	A	1061	ASP	-1	-0.866	-0.934	23.600	-22.856	-22.856	0.000	0.000	0.000	0.000
61	A	1062	ILE	0	-0.044	-0.016	20.512	-0.801	-0.801	0.000	0.000	0.000	0.000
62	A	1063	ILE	0	0.000	0.000	17.367	-1.568	-1.568	0.000	0.000	0.000	0.000
63	A	1064	SER	0	-0.010	-0.015	19.092	-1.452	-1.452	0.000	0.000	0.000	0.000
64	A	1065	ALA	0	-0.048	0.000	20.994	-0.576	-0.576	0.000	0.000	0.000	0.000
65	A	1066	LEU	0	0.020	0.012	15.781	-1.023	-1.023	0.000	0.000	0.000	0.000
66	A	1067	LYS	1	0.865	0.922	15.899	31.462	31.462	0.000	0.000	0.000	0.000
67	A	1068	SER	0	-0.080	-0.062	16.772	-0.863	-0.863	0.000	0.000	0.000	0.000
68	A	1069	PHE	0	-0.018	-0.019	17.102	0.621	0.621	0.000	0.000	0.000	0.000
69	A	1070	LEU	0	-0.068	-0.008	11.174	-1.716	-1.716	0.000	0.000	0.000	0.000
70	A	1071	ASP	-1	-0.791	-0.896	11.406	-40.159	-40.159	0.000	0.000	0.000	0.000
71	A	1072	HIS	0	-0.051	-0.042	11.402	-5.316	-5.316	0.000	0.000	0.000	0.000
72	A	1073	GLU	-1	-0.910	-0.928	12.741	-34.784	-34.784	0.000	0.000	0.000	0.000
73	A	1074	LYS	1	0.801	0.883	11.085	35.213	35.213	0.000	0.000	0.000	0.000
74	A	1075	GLY	0	0.095	0.054	8.214	-4.280	-4.280	0.000	0.000	0.000	0.000
79	A	1080	LYS	1	0.905	0.967	8.848	46.510	46.510	0.000	0.000	0.000	0.000
80	A	1081	ASN	0	-0.020	-0.017	5.476	11.263	11.263	0.000	0.000	0.000	0.000
81	A	1082	LEU	0	0.057	0.030	7.469	3.685	3.685	0.000	0.000	0.000	0.000
82	A	1083	ASP	-1	-0.790	-0.874	10.361	-33.953	-33.953	0.000	0.000	0.000	0.000
83	A	1084	THR	0	-0.071	-0.028	12.174	4.523	4.523	0.000	0.000	0.000	0.000
84	A	1085	ILE	0	0.014	0.003	9.666	2.970	2.970	0.000	0.000	0.000	0.000
85	A	1086	TYR	0	0.059	0.016	13.405	2.329	2.329	0.000	0.000	0.000	0.000
86	A	1087	THR	0	-0.037	-0.023	16.029	2.872	2.872	0.000	0.000	0.000	0.000
87	A	1088	ILE	0	-0.029	-0.007	15.454	1.960	1.960	0.000	0.000	0.000	0.000
88	A	1089	ILE	0	0.019	0.023	15.672	1.854	1.854	0.000	0.000	0.000	0.000
89	A	1090	LEU	0	0.009	0.006	19.572	1.557	1.557	0.000	0.000	0.000	0.000
90	A	1091	ASN	0	-0.006	-0.016	21.868	1.664	1.664	0.000	0.000	0.000	0.000
91	A	1092	THR	0	-0.051	-0.034	21.893	1.354	1.354	0.000	0.000	0.000	0.000
92	A	1093	LEU	0	0.018	0.007	22.290	1.013	1.013	0.000	0.000	0.000	0.000
93	A	1094	VAL	0	-0.007	0.008	25.660	1.091	1.091	0.000	0.000	0.000	0.000
94	A	1095	LYS	1	0.803	0.912	26.097	23.737	23.737	0.000	0.000	0.000	0.000
95	A	1096	VAL	0	-0.014	-0.016	29.502	0.123	0.123	0.000	0.000	0.000	0.000
96	A	1097	ASP	-1	-0.920	-0.962	31.641	-19.207	-19.207	0.000	0.000	0.000	0.000
97	A	1098	LYS	1	0.819	0.925	27.794	20.560	20.560	0.000	0.000	0.000	0.000
98	A	1099	THR	0	0.005	-0.009	27.955	0.481	0.481	0.000	0.000	0.000	0.000
99	A	1100	LYS	1	0.858	0.913	27.887	18.333	18.333	0.000	0.000	0.000	0.000
100	A	1101	GLU	-1	-0.840	-0.893	25.601	-23.783	-23.783	0.000	0.000	0.000	0.000
101	A	1102	GLU	-1	-0.784	-0.881	23.431	-24.190	-24.190	0.000	0.000	0.000	0.000
102	A	1103	LEU	0	0.028	0.017	22.492	-1.158	-1.158	0.000	0.000	0.000	0.000
103	A	1104	GLN	0	0.024	-0.002	22.703	-0.151	-0.151	0.000	0.000	0.000	0.000
104	A	1105	LYS	1	0.843	0.911	19.720	24.773	24.773	0.000	0.000	0.000	0.000
105	A	1106	ILE	0	0.000	-0.001	18.337	-1.617	-1.617	0.000	0.000	0.000	0.000
106	A	1107	LEU	0	-0.042	-0.008	18.102	-1.221	-1.221	0.000	0.000	0.000	0.000
107	A	1108	GLU	-1	-0.864	-0.943	17.282	-29.403	-29.403	0.000	0.000	0.000	0.000
108	A	1109	ILE	0	-0.031	-0.005	13.070	-1.571	-1.571	0.000	0.000	0.000	0.000
109	A	1110	LEU	0	-0.005	-0.008	13.592	-2.073	-2.073	0.000	0.000	0.000	0.000
110	A	1111	LYS	1	0.846	0.928	15.031	26.223	26.223	0.000	0.000	0.000	0.000
111	A	1112	ASP	-1	-0.863	-0.929	10.433	-47.422	-47.422	0.000	0.000	0.000	0.000
112	A	1113	LEU	0	-0.052	-0.024	8.731	-3.341	-3.341	0.000	0.000	0.000	0.000
113	A	1114	ARG	1	0.843	0.915	10.749	29.012	29.012	0.000	0.000	0.000	0.000
114	A	1115	GLU	-1	-0.948	-0.969	12.211	-40.100	-40.100	0.000	0.000	0.000	0.000
115	A	1116	ALA	0	0.025	0.009	7.216	-1.035	-1.035	0.000	0.000	0.000	0.000
116	A	1117	TRP	0	-0.018	-0.023	9.288	-3.491	-3.491	0.000	0.000	0.000	0.000
117	A	1118	GLU	-1	-0.843	-0.927	11.611	-31.451	-31.451	0.000	0.000	0.000	0.000
118	A	1119	GLU	-1	-0.882	-0.921	8.288	-56.005	-56.005	0.000	0.000	0.000	0.000
119	A	1120	VAL	0	-0.052	-0.034	8.320	-0.473	-0.473	0.000	0.000	0.000	0.000
120	A	1121	LYS	1	0.861	0.935	10.641	31.764	31.764	0.000	0.000	0.000	0.000
121	A	1122	LYS	1	0.942	0.972	13.322	39.479	39.479	0.000	0.000	0.000	0.000
122	A	1123	LYS	1	0.728	0.836	6.921	59.645	59.645	0.000	0.000	0.000	0.000
123	A	1124	VAL	0	0.031	0.016	12.254	0.968	0.968	0.000	0.000	0.000	0.000
124	A	1125	HIS	0	0.011	0.003	14.473	1.908	1.908	0.000	0.000	0.000	0.000
125	A	1126	HIS	0	-0.126	-0.054	15.809	2.564	2.564	0.000	0.000	0.000	0.000
126	A	1127	HIS	-1	-0.935	-0.940	14.815	-31.430	-31.430	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:1002:ARG)