FMO DATABASE

FMODB ID: 7N3VK

Calculation Name: 2OJ4-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2OJ4

Chain ID: A

ChEMBL ID:

UniProt ID: P49796

Base Structure: X-ray

Registration Date: 2025-10-04

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	127
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1146956.872988
FMO2-HF: Nuclear repulsion	1094725.048058
FMO2-HF: Total energy	-52231.824931
FMO2-MP2: Total energy	-52383.920443

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:2:SER)

Summations of interaction energy for fragment #1(A:2:SER)

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.
-115.159	-111.285	17.226	-10.24	-10.862	-0.109

Interaction energy analysis for fragmet #1(A:2:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.816 / q_NPA : 0.892

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	4	GLU	-1	-0.823	-0.893	3.819	-25.471	-23.586	-0.015	-0.860	-1.011	-0.001
4	A	5	ALA	0	0.067	0.034	3.254	5.751	6.089	0.014	-0.076	-0.275	0.000
5	A	6	LEU	0	0.041	0.030	3.359	5.393	6.155	0.039	-0.261	-0.541	0.001
125	A	126	LEU	0	-0.101	-0.051	4.567	-4.020	-3.806	-0.001	-0.085	-0.129	0.000
126	A	127	ILE	0	-0.067	-0.051	1.999	-19.147	-18.604	7.119	-4.047	-3.615	-0.030
127	A	128	ASN	-1	-0.948	-0.941	1.787	-90.576	-90.444	10.070	-4.911	-5.291	-0.079
6	A	7	LYS	1	0.837	0.903	5.869	37.094	37.094	0.000	0.000	0.000	0.000
7	A	8	TRP	0	-0.009	0.008	8.035	2.257	2.257	0.000	0.000	0.000	0.000
8	A	9	GLY	0	0.061	0.048	9.088	1.982	1.982	0.000	0.000	0.000	0.000
9	A	10	GLU	-1	-0.952	-0.965	10.498	-18.544	-18.544	0.000	0.000	0.000	0.000
10	A	11	SER	0	0.023	-0.003	13.088	1.358	1.358	0.000	0.000	0.000	0.000
11	A	12	LEU	0	0.028	0.037	14.550	-0.986	-0.986	0.000	0.000	0.000	0.000
12	A	13	GLU	-1	-0.860	-0.951	16.586	-15.284	-15.284	0.000	0.000	0.000	0.000
13	A	14	LYS	1	0.854	0.935	13.226	18.443	18.443	0.000	0.000	0.000	0.000
14	A	15	LEU	0	-0.024	0.001	12.381	-1.037	-1.037	0.000	0.000	0.000	0.000
15	A	16	LEU	0	-0.035	-0.018	13.548	-0.117	-0.117	0.000	0.000	0.000	0.000
16	A	17	VAL	0	-0.039	-0.014	15.767	0.631	0.631	0.000	0.000	0.000	0.000
17	A	18	HIS	0	-0.053	-0.018	9.642	1.123	1.123	0.000	0.000	0.000	0.000
18	A	19	LYS	1	0.911	0.952	13.941	19.242	19.242	0.000	0.000	0.000	0.000
19	A	20	TYR	0	0.001	-0.010	10.214	1.094	1.094	0.000	0.000	0.000	0.000
20	A	21	GLY	0	0.087	0.035	10.696	-0.024	-0.024	0.000	0.000	0.000	0.000
21	A	22	LEU	0	-0.006	0.000	11.432	0.970	0.970	0.000	0.000	0.000	0.000
22	A	23	ALA	0	-0.028	-0.014	14.163	0.921	0.921	0.000	0.000	0.000	0.000
23	A	24	VAL	0	-0.004	-0.005	10.051	0.916	0.916	0.000	0.000	0.000	0.000
24	A	25	PHE	0	0.038	0.026	13.081	0.712	0.712	0.000	0.000	0.000	0.000
25	A	26	GLN	0	0.031	0.005	14.895	0.985	0.985	0.000	0.000	0.000	0.000
26	A	27	ALA	0	-0.035	-0.017	15.455	0.819	0.819	0.000	0.000	0.000	0.000
27	A	28	PHE	0	0.047	0.020	14.844	0.419	0.419	0.000	0.000	0.000	0.000
28	A	29	LEU	0	-0.001	0.013	16.854	0.753	0.753	0.000	0.000	0.000	0.000
29	A	30	ARG	1	0.851	0.919	20.093	12.644	12.644	0.000	0.000	0.000	0.000
30	A	31	THR	0	-0.120	-0.074	18.848	0.403	0.403	0.000	0.000	0.000	0.000
31	A	32	GLU	-1	-0.805	-0.864	20.714	-13.357	-13.357	0.000	0.000	0.000	0.000
32	A	33	PHE	0	-0.093	-0.035	23.230	0.508	0.508	0.000	0.000	0.000	0.000
33	A	34	SER	0	0.026	0.007	22.803	0.264	0.264	0.000	0.000	0.000	0.000
34	A	35	GLU	-1	-0.740	-0.871	22.572	-12.301	-12.301	0.000	0.000	0.000	0.000
35	A	36	GLU	-1	-0.856	-0.927	23.519	-11.320	-11.320	0.000	0.000	0.000	0.000
36	A	37	ASN	0	-0.050	-0.048	24.158	0.550	0.550	0.000	0.000	0.000	0.000
37	A	38	LEU	0	0.036	0.006	18.491	0.059	0.059	0.000	0.000	0.000	0.000
38	A	39	GLU	-1	-0.876	-0.915	22.905	-11.761	-11.761	0.000	0.000	0.000	0.000
39	A	40	PHE	0	0.031	0.014	25.233	0.302	0.302	0.000	0.000	0.000	0.000
40	A	41	TRP	0	0.022	0.018	21.366	0.164	0.164	0.000	0.000	0.000	0.000
41	A	42	LEU	0	0.038	0.011	20.772	0.152	0.152	0.000	0.000	0.000	0.000
42	A	43	ALA	0	-0.006	0.005	24.831	0.326	0.326	0.000	0.000	0.000	0.000
43	A	44	CYS	0	-0.040	-0.033	28.266	0.558	0.558	0.000	0.000	0.000	0.000
44	A	45	GLU	-1	-0.791	-0.877	23.927	-11.530	-11.530	0.000	0.000	0.000	0.000
45	A	46	ASP	-1	-0.923	-0.966	26.952	-11.509	-11.509	0.000	0.000	0.000	0.000
46	A	47	PHE	0	-0.086	-0.042	28.975	0.392	0.392	0.000	0.000	0.000	0.000
47	A	48	LYS	1	0.832	0.907	27.891	11.206	11.206	0.000	0.000	0.000	0.000
48	A	49	LYS	1	0.936	0.977	24.993	12.192	12.192	0.000	0.000	0.000	0.000
49	A	50	VAL	0	-0.079	-0.021	31.621	0.239	0.239	0.000	0.000	0.000	0.000
50	A	51	LYS	1	1.012	1.001	34.911	8.336	8.336	0.000	0.000	0.000	0.000
51	A	52	SER	0	-0.033	-0.019	37.724	0.195	0.195	0.000	0.000	0.000	0.000
52	A	53	GLN	0	0.145	0.054	40.107	-0.235	-0.235	0.000	0.000	0.000	0.000
53	A	54	SER	0	0.023	0.013	42.406	-0.065	-0.065	0.000	0.000	0.000	0.000
54	A	55	LYS	1	0.949	0.974	37.782	7.956	7.956	0.000	0.000	0.000	0.000
55	A	56	MET	0	0.015	0.022	37.143	-0.149	-0.149	0.000	0.000	0.000	0.000
56	A	57	ALA	0	0.041	0.019	38.655	-0.081	-0.081	0.000	0.000	0.000	0.000
57	A	58	SER	0	-0.049	-0.039	40.698	-0.036	-0.036	0.000	0.000	0.000	0.000
58	A	59	LYS	1	0.866	0.943	30.469	9.976	9.976	0.000	0.000	0.000	0.000
59	A	60	ALA	0	0.061	0.022	36.107	-0.147	-0.147	0.000	0.000	0.000	0.000
60	A	61	LYS	1	0.968	0.981	37.565	7.065	7.065	0.000	0.000	0.000	0.000
61	A	62	LYS	1	0.921	0.966	36.394	8.267	8.267	0.000	0.000	0.000	0.000
62	A	63	ILE	0	0.020	0.020	32.390	-0.061	-0.061	0.000	0.000	0.000	0.000
63	A	64	PHE	0	0.035	0.002	34.921	-0.069	-0.069	0.000	0.000	0.000	0.000
64	A	65	ALA	0	-0.020	-0.016	37.602	0.028	0.028	0.000	0.000	0.000	0.000
65	A	66	GLU	-1	-0.903	-0.946	31.970	-9.768	-9.768	0.000	0.000	0.000	0.000
66	A	67	TYR	0	-0.012	-0.015	28.791	-0.203	-0.203	0.000	0.000	0.000	0.000
67	A	68	ILE	0	-0.042	-0.008	33.599	-0.045	-0.045	0.000	0.000	0.000	0.000
68	A	69	ALA	0	-0.045	-0.020	36.299	0.161	0.161	0.000	0.000	0.000	0.000
69	A	70	ILE	0	0.013	0.000	38.475	-0.122	-0.122	0.000	0.000	0.000	0.000
70	A	71	GLN	0	-0.059	-0.035	39.139	0.227	0.227	0.000	0.000	0.000	0.000
71	A	72	ALA	0	-0.015	0.017	36.384	0.030	0.030	0.000	0.000	0.000	0.000
72	A	73	CYS	0	-0.050	-0.046	34.581	-0.072	-0.072	0.000	0.000	0.000	0.000
73	A	74	LYS	1	0.836	0.916	27.810	10.617	10.617	0.000	0.000	0.000	0.000
74	A	75	GLU	-1	-0.867	-0.929	31.693	-8.418	-8.418	0.000	0.000	0.000	0.000
75	A	76	VAL	0	0.036	0.024	29.282	-0.163	-0.163	0.000	0.000	0.000	0.000
76	A	77	ASN	0	0.036	0.015	30.769	0.573	0.573	0.000	0.000	0.000	0.000
77	A	78	LEU	0	-0.001	0.010	32.488	-0.083	-0.083	0.000	0.000	0.000	0.000
78	A	79	ASP	-1	-0.785	-0.862	34.939	-8.197	-8.197	0.000	0.000	0.000	0.000
79	A	80	SER	0	0.048	-0.012	37.944	-0.066	-0.066	0.000	0.000	0.000	0.000
80	A	81	TYR	0	-0.001	0.021	38.658	0.143	0.143	0.000	0.000	0.000	0.000
81	A	82	THR	0	0.008	-0.022	34.661	-0.004	-0.004	0.000	0.000	0.000	0.000
82	A	83	ARG	1	0.914	0.977	37.835	7.904	7.904	0.000	0.000	0.000	0.000
83	A	84	GLU	-1	-0.852	-0.913	39.357	-6.924	-6.924	0.000	0.000	0.000	0.000
84	A	85	HIS	0	0.040	0.032	38.150	-0.134	-0.134	0.000	0.000	0.000	0.000
85	A	86	THR	0	-0.022	-0.036	36.356	-0.060	-0.060	0.000	0.000	0.000	0.000
86	A	87	LYS	1	0.828	0.901	39.377	6.871	6.871	0.000	0.000	0.000	0.000
87	A	88	ASP	-1	-0.928	-0.962	42.405	-6.780	-6.780	0.000	0.000	0.000	0.000
88	A	89	ASN	0	-0.040	-0.041	38.726	0.253	0.253	0.000	0.000	0.000	0.000
89	A	90	LEU	0	-0.061	-0.038	39.730	-0.014	-0.014	0.000	0.000	0.000	0.000
90	A	91	GLN	0	-0.042	-0.021	42.960	0.105	0.105	0.000	0.000	0.000	0.000
91	A	92	SER	0	-0.062	-0.026	44.934	0.109	0.109	0.000	0.000	0.000	0.000
92	A	93	VAL	0	-0.005	0.019	39.353	-0.116	-0.116	0.000	0.000	0.000	0.000
93	A	94	THR	0	0.059	0.032	40.079	-0.050	-0.050	0.000	0.000	0.000	0.000
94	A	95	ARG	1	0.866	0.899	34.673	8.480	8.480	0.000	0.000	0.000	0.000
95	A	96	GLY	0	0.099	0.064	34.603	-0.260	-0.260	0.000	0.000	0.000	0.000
96	A	97	CYS	0	-0.120	-0.045	36.185	0.053	0.053	0.000	0.000	0.000	0.000
97	A	98	PHE	0	0.063	0.030	32.683	0.126	0.126	0.000	0.000	0.000	0.000
98	A	99	ASP	-1	-0.862	-0.913	31.824	-9.660	-9.660	0.000	0.000	0.000	0.000
99	A	100	LEU	0	-0.032	-0.008	31.692	-0.278	-0.278	0.000	0.000	0.000	0.000
100	A	101	ALA	0	0.046	0.010	32.549	-0.156	-0.156	0.000	0.000	0.000	0.000
101	A	102	GLN	0	-0.006	-0.018	25.989	0.147	0.147	0.000	0.000	0.000	0.000
102	A	103	LYS	1	0.969	0.977	27.564	9.550	9.550	0.000	0.000	0.000	0.000
103	A	104	ARG	1	0.807	0.897	28.149	8.938	8.938	0.000	0.000	0.000	0.000
104	A	105	ILE	0	-0.003	0.001	26.080	-0.152	-0.152	0.000	0.000	0.000	0.000
105	A	106	PHE	0	-0.013	-0.004	20.770	-0.268	-0.268	0.000	0.000	0.000	0.000
106	A	107	GLY	0	0.048	0.029	23.569	-0.435	-0.435	0.000	0.000	0.000	0.000
107	A	108	LEU	0	-0.051	-0.026	24.885	-0.130	-0.130	0.000	0.000	0.000	0.000
108	A	109	MET	0	-0.008	0.008	20.465	-0.427	-0.427	0.000	0.000	0.000	0.000
109	A	110	GLU	-1	-0.940	-0.980	20.014	-13.574	-13.574	0.000	0.000	0.000	0.000
110	A	111	LYS	1	0.831	0.904	20.402	10.740	10.740	0.000	0.000	0.000	0.000
111	A	112	ASP	-1	-0.878	-0.919	22.518	-11.586	-11.586	0.000	0.000	0.000	0.000
112	A	113	SER	0	0.023	0.000	20.162	-0.378	-0.378	0.000	0.000	0.000	0.000
113	A	114	TYR	0	-0.008	-0.022	12.867	-0.305	-0.305	0.000	0.000	0.000	0.000
114	A	115	PRO	0	0.010	-0.004	15.472	-1.157	-1.157	0.000	0.000	0.000	0.000
115	A	116	ARG	1	0.787	0.870	16.383	12.998	12.998	0.000	0.000	0.000	0.000
116	A	117	PHE	0	0.031	0.024	10.604	-0.676	-0.676	0.000	0.000	0.000	0.000
117	A	118	LEU	0	-0.004	0.004	10.697	-1.295	-1.295	0.000	0.000	0.000	0.000
118	A	119	ARG	1	0.883	0.942	11.791	15.350	15.350	0.000	0.000	0.000	0.000
119	A	120	SER	0	-0.025	-0.017	12.867	0.773	0.773	0.000	0.000	0.000	0.000
120	A	121	ASP	-1	-0.825	-0.913	11.363	-21.823	-21.823	0.000	0.000	0.000	0.000
121	A	122	LEU	0	-0.046	-0.019	10.156	-2.112	-2.112	0.000	0.000	0.000	0.000
122	A	123	TYR	0	-0.064	-0.049	7.158	-1.611	-1.611	0.000	0.000	0.000	0.000
123	A	124	LEU	0	-0.014	-0.022	6.643	-4.596	-4.596	0.000	0.000	0.000	0.000
124	A	125	ASP	-1	-0.867	-0.931	6.327	-32.027	-32.027	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:SER)