FMO DATABASE

FMODB ID: 9LJV2

Calculation Name: 2D9J-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2D9J

Chain ID: A

ChEMBL ID:

UniProt ID: P49802

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	139
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1239896.417905
FMO2-HF: Nuclear repulsion	1184847.504063
FMO2-HF: Total energy	-55048.913842
FMO2-MP2: Total energy	-55211.883676

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:GLY)

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

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.
17.074	18.179	-0.005	-0.496	-0.604	-0.002

Interaction energy analysis for fragmet #1(A:1:GLY)

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 : 0.916

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	3	SER	0	0.034	0.042	3.710	9.492	10.608	-0.004	-0.452	-0.660	-0.002
4	A	4	GLY	0	0.012	0.010	4.315	-10.668	-10.679	-0.001	-0.044	0.056	0.000
5	A	5	SER	0	-0.036	-0.037	6.575	3.045	3.045	0.000	0.000	0.000	0.000
6	A	6	SER	0	0.016	0.016	9.911	-0.390	-0.390	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.035	0.019	13.090	-0.112	-0.112	0.000	0.000	0.000	0.000
8	A	8	SER	0	-0.005	-0.009	13.082	-1.527	-1.527	0.000	0.000	0.000	0.000
9	A	9	GLN	0	0.042	0.038	14.095	-0.181	-0.181	0.000	0.000	0.000	0.000
10	A	10	GLN	0	0.047	-0.003	15.850	0.295	0.295	0.000	0.000	0.000	0.000
11	A	11	ARG	1	0.845	0.926	6.320	36.352	36.352	0.000	0.000	0.000	0.000
12	A	12	VAL	0	0.043	0.014	13.572	-0.002	-0.002	0.000	0.000	0.000	0.000
13	A	13	LYS	1	0.894	0.950	15.763	14.645	14.645	0.000	0.000	0.000	0.000
14	A	14	ARG	1	0.947	0.977	13.747	20.881	20.881	0.000	0.000	0.000	0.000
15	A	15	TRP	0	0.007	-0.020	11.673	1.145	1.145	0.000	0.000	0.000	0.000
16	A	16	GLY	0	0.004	0.009	17.187	0.565	0.565	0.000	0.000	0.000	0.000
17	A	17	PHE	0	-0.079	-0.029	18.800	0.686	0.686	0.000	0.000	0.000	0.000
18	A	18	GLY	0	0.068	0.016	19.752	0.737	0.737	0.000	0.000	0.000	0.000
19	A	19	MET	0	0.018	0.021	18.642	-0.862	-0.862	0.000	0.000	0.000	0.000
20	A	20	ASP	-1	-0.799	-0.878	17.045	-17.189	-17.189	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.918	-0.944	14.698	-21.981	-21.981	0.000	0.000	0.000	0.000
22	A	22	ALA	0	-0.004	-0.007	13.502	-1.877	-1.877	0.000	0.000	0.000	0.000
23	A	23	LEU	0	-0.019	0.004	13.417	-1.342	-1.342	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.843	0.915	10.279	19.843	19.843	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.825	-0.890	8.124	-37.696	-37.696	0.000	0.000	0.000	0.000
26	A	26	PRO	0	-0.022	-0.012	5.530	2.521	2.521	0.000	0.000	0.000	0.000
27	A	27	VAL	0	0.038	0.004	8.622	2.556	2.556	0.000	0.000	0.000	0.000
28	A	28	GLY	0	0.035	0.021	11.164	2.216	2.216	0.000	0.000	0.000	0.000
29	A	29	ARG	1	0.897	0.937	10.917	27.115	27.115	0.000	0.000	0.000	0.000
30	A	30	GLU	-1	-0.866	-0.925	12.695	-21.050	-21.050	0.000	0.000	0.000	0.000
31	A	31	GLN	0	0.002	0.000	14.899	1.140	1.140	0.000	0.000	0.000	0.000
32	A	32	PHE	0	0.005	0.004	16.669	1.153	1.153	0.000	0.000	0.000	0.000
33	A	33	LEU	0	0.011	0.001	17.559	0.877	0.877	0.000	0.000	0.000	0.000
34	A	34	LYS	1	0.876	0.927	16.357	19.315	19.315	0.000	0.000	0.000	0.000
35	A	35	PHE	0	-0.056	-0.028	21.047	0.777	0.777	0.000	0.000	0.000	0.000
36	A	36	LEU	0	0.000	0.004	21.314	0.555	0.555	0.000	0.000	0.000	0.000
37	A	37	GLU	-1	-0.951	-0.987	21.592	-14.029	-14.029	0.000	0.000	0.000	0.000
38	A	38	SER	0	-0.058	-0.009	25.096	0.604	0.604	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.905	-0.971	26.961	-11.101	-11.101	0.000	0.000	0.000	0.000
40	A	40	PHE	0	-0.022	-0.011	28.426	0.339	0.339	0.000	0.000	0.000	0.000
41	A	41	SER	0	0.089	0.061	26.710	0.168	0.168	0.000	0.000	0.000	0.000
42	A	42	SER	0	-0.043	-0.038	22.837	-0.209	-0.209	0.000	0.000	0.000	0.000
43	A	43	GLU	-1	-0.905	-0.945	23.091	-11.450	-11.450	0.000	0.000	0.000	0.000
44	A	44	ASN	0	0.019	0.008	24.652	-0.146	-0.146	0.000	0.000	0.000	0.000
45	A	45	LEU	0	0.028	-0.012	17.548	-0.346	-0.346	0.000	0.000	0.000	0.000
46	A	46	ARG	1	0.812	0.894	19.975	12.973	12.973	0.000	0.000	0.000	0.000
47	A	47	PHE	0	0.018	0.017	20.840	-0.385	-0.385	0.000	0.000	0.000	0.000
48	A	48	TRP	0	-0.006	-0.009	16.225	-0.703	-0.703	0.000	0.000	0.000	0.000
49	A	49	LEU	0	-0.002	-0.020	14.519	-0.698	-0.698	0.000	0.000	0.000	0.000
50	A	50	ALA	0	0.016	0.020	17.230	-0.745	-0.745	0.000	0.000	0.000	0.000
51	A	51	VAL	0	0.002	0.012	19.621	0.092	0.092	0.000	0.000	0.000	0.000
52	A	52	GLU	-1	-0.949	-0.970	15.462	-19.312	-19.312	0.000	0.000	0.000	0.000
53	A	53	ASP	-1	-0.887	-0.947	15.295	-19.580	-19.580	0.000	0.000	0.000	0.000
54	A	54	LEU	0	-0.002	0.014	16.636	0.086	0.086	0.000	0.000	0.000	0.000
55	A	55	LYS	1	0.839	0.909	18.134	15.729	15.729	0.000	0.000	0.000	0.000
56	A	56	LYS	1	0.872	0.939	13.864	20.068	20.068	0.000	0.000	0.000	0.000
57	A	57	ARG	1	0.835	0.930	15.459	17.953	17.953	0.000	0.000	0.000	0.000
58	A	58	PRO	0	-0.003	-0.008	19.199	0.542	0.542	0.000	0.000	0.000	0.000
59	A	59	ILE	0	0.060	0.010	21.691	0.204	0.204	0.000	0.000	0.000	0.000
60	A	60	LYS	1	0.956	0.980	22.591	13.753	13.753	0.000	0.000	0.000	0.000
61	A	61	GLU	-1	-0.865	-0.941	20.705	-15.025	-15.025	0.000	0.000	0.000	0.000
62	A	62	VAL	0	-0.044	-0.003	23.056	0.018	0.018	0.000	0.000	0.000	0.000
63	A	63	PRO	0	0.036	0.013	24.806	0.036	0.036	0.000	0.000	0.000	0.000
64	A	64	SER	0	0.022	0.001	26.530	0.290	0.290	0.000	0.000	0.000	0.000
65	A	65	ARG	1	0.975	0.991	19.379	14.799	14.799	0.000	0.000	0.000	0.000
66	A	66	VAL	0	-0.015	0.002	25.285	-0.025	-0.025	0.000	0.000	0.000	0.000
67	A	67	GLN	0	0.022	0.007	27.373	0.046	0.046	0.000	0.000	0.000	0.000
68	A	68	GLU	-1	-0.921	-0.956	26.191	-10.963	-10.963	0.000	0.000	0.000	0.000
69	A	69	ILE	0	-0.020	-0.012	22.238	-0.031	-0.031	0.000	0.000	0.000	0.000
70	A	70	TRP	0	0.008	-0.011	26.245	0.026	0.026	0.000	0.000	0.000	0.000
71	A	71	GLN	0	-0.040	-0.047	29.838	0.519	0.519	0.000	0.000	0.000	0.000
72	A	72	GLU	-1	-0.815	-0.892	25.079	-11.988	-11.988	0.000	0.000	0.000	0.000
73	A	73	PHE	0	-0.019	-0.027	23.143	-0.156	-0.156	0.000	0.000	0.000	0.000
74	A	74	LEU	0	-0.041	-0.002	28.749	0.216	0.216	0.000	0.000	0.000	0.000
75	A	75	ALA	0	0.037	0.044	31.512	0.360	0.360	0.000	0.000	0.000	0.000
76	A	76	PRO	0	-0.003	-0.008	34.155	-0.074	-0.074	0.000	0.000	0.000	0.000
77	A	77	GLY	0	-0.026	-0.016	36.647	0.078	0.078	0.000	0.000	0.000	0.000
78	A	78	ALA	0	-0.010	0.015	31.042	-0.063	-0.063	0.000	0.000	0.000	0.000
79	A	79	PRO	0	-0.034	-0.012	28.806	0.153	0.153	0.000	0.000	0.000	0.000
80	A	80	SER	0	-0.045	-0.018	26.743	-0.219	-0.219	0.000	0.000	0.000	0.000
81	A	81	ALA	0	0.039	0.015	28.794	-0.264	-0.264	0.000	0.000	0.000	0.000
82	A	82	ILE	0	0.029	0.032	27.274	0.161	0.161	0.000	0.000	0.000	0.000
83	A	83	ASN	0	-0.041	-0.024	30.661	0.353	0.353	0.000	0.000	0.000	0.000
84	A	84	LEU	0	-0.030	-0.023	29.825	-0.343	-0.343	0.000	0.000	0.000	0.000
85	A	85	ASP	-1	-0.837	-0.924	33.705	-8.097	-8.097	0.000	0.000	0.000	0.000
86	A	86	SER	0	0.011	0.012	36.592	-0.102	-0.102	0.000	0.000	0.000	0.000
87	A	87	LYS	1	0.940	0.967	36.973	8.332	8.332	0.000	0.000	0.000	0.000
88	A	88	SER	0	-0.010	-0.007	32.853	0.004	0.004	0.000	0.000	0.000	0.000
89	A	89	TYR	0	0.001	0.002	33.932	-0.102	-0.102	0.000	0.000	0.000	0.000
90	A	90	ASP	-1	-0.907	-0.929	35.444	-7.971	-7.971	0.000	0.000	0.000	0.000
91	A	91	LYS	1	0.923	0.964	33.798	9.146	9.146	0.000	0.000	0.000	0.000
92	A	92	THR	0	-0.012	-0.022	30.748	-0.208	-0.208	0.000	0.000	0.000	0.000
93	A	93	THR	0	0.003	-0.019	33.417	-0.129	-0.129	0.000	0.000	0.000	0.000
94	A	94	HIS	0	-0.061	-0.035	35.941	0.018	0.018	0.000	0.000	0.000	0.000
95	A	95	ASN	0	0.003	-0.014	31.379	0.314	0.314	0.000	0.000	0.000	0.000
96	A	96	VAL	0	-0.039	-0.022	31.351	-0.110	-0.110	0.000	0.000	0.000	0.000
97	A	97	LYS	1	0.824	0.938	33.262	8.220	8.220	0.000	0.000	0.000	0.000
98	A	98	GLU	-1	-0.942	-0.958	33.315	-9.172	-9.172	0.000	0.000	0.000	0.000
99	A	99	PRO	0	-0.019	-0.005	29.469	-0.350	-0.350	0.000	0.000	0.000	0.000
100	A	100	GLY	0	0.039	0.007	27.613	0.065	0.065	0.000	0.000	0.000	0.000
101	A	101	ARG	1	0.863	0.929	21.669	14.018	14.018	0.000	0.000	0.000	0.000
102	A	102	TYR	0	0.029	0.001	22.070	-0.855	-0.855	0.000	0.000	0.000	0.000
103	A	103	THR	0	0.023	0.036	26.024	-0.001	-0.001	0.000	0.000	0.000	0.000
104	A	104	PHE	0	0.048	0.017	25.506	0.299	0.299	0.000	0.000	0.000	0.000
105	A	105	GLU	-1	-0.929	-0.963	24.092	-13.050	-13.050	0.000	0.000	0.000	0.000
106	A	106	ASP	-1	-0.817	-0.913	26.407	-10.230	-10.230	0.000	0.000	0.000	0.000
107	A	107	ALA	0	0.029	0.009	28.184	0.001	0.001	0.000	0.000	0.000	0.000
108	A	108	GLN	0	0.010	0.000	20.741	-0.444	-0.444	0.000	0.000	0.000	0.000
109	A	109	GLU	-1	-0.823	-0.903	24.344	-11.192	-11.192	0.000	0.000	0.000	0.000
110	A	110	HIS	0	-0.019	-0.018	26.427	0.023	0.023	0.000	0.000	0.000	0.000
111	A	111	ILE	0	0.040	0.012	24.294	0.094	0.094	0.000	0.000	0.000	0.000
112	A	112	TYR	0	-0.095	-0.055	20.125	0.205	0.205	0.000	0.000	0.000	0.000
113	A	113	LYS	1	0.830	0.875	24.124	10.465	10.465	0.000	0.000	0.000	0.000
114	A	114	LEU	0	0.005	0.030	27.320	0.220	0.220	0.000	0.000	0.000	0.000
115	A	115	MET	0	0.020	0.019	21.188	-0.130	-0.130	0.000	0.000	0.000	0.000
116	A	116	LYS	1	0.905	0.947	23.307	11.711	11.711	0.000	0.000	0.000	0.000
117	A	117	SER	0	-0.102	-0.067	24.267	0.001	0.001	0.000	0.000	0.000	0.000
118	A	118	ASP	-1	-0.771	-0.862	26.993	-10.976	-10.976	0.000	0.000	0.000	0.000
119	A	119	SER	0	-0.004	-0.024	24.608	0.154	0.154	0.000	0.000	0.000	0.000
120	A	120	TYR	0	-0.042	-0.014	20.988	-0.278	-0.278	0.000	0.000	0.000	0.000
121	A	121	PRO	0	-0.042	-0.021	23.853	-0.113	-0.113	0.000	0.000	0.000	0.000
122	A	122	ARG	1	0.926	0.970	26.952	10.485	10.485	0.000	0.000	0.000	0.000
123	A	123	PHE	0	0.022	0.016	18.782	0.054	0.054	0.000	0.000	0.000	0.000
124	A	124	ILE	0	-0.021	-0.009	23.122	-0.023	-0.023	0.000	0.000	0.000	0.000
125	A	125	ARG	1	0.895	0.949	25.302	10.196	10.196	0.000	0.000	0.000	0.000
126	A	126	SER	0	0.023	0.028	26.161	0.445	0.445	0.000	0.000	0.000	0.000
127	A	127	SER	0	0.034	-0.006	26.505	-0.166	-0.166	0.000	0.000	0.000	0.000
128	A	128	ALA	0	-0.020	-0.005	23.144	-0.413	-0.413	0.000	0.000	0.000	0.000
129	A	129	TYR	0	0.006	0.017	19.337	-0.375	-0.375	0.000	0.000	0.000	0.000
130	A	130	GLN	0	0.010	-0.009	21.018	-0.814	-0.814	0.000	0.000	0.000	0.000
131	A	131	GLU	-1	-0.857	-0.913	22.019	-12.764	-12.764	0.000	0.000	0.000	0.000
132	A	132	LEU	0	-0.050	-0.023	16.929	-0.456	-0.456	0.000	0.000	0.000	0.000
133	A	133	LEU	0	-0.083	-0.028	18.695	-0.635	-0.635	0.000	0.000	0.000	0.000
134	A	134	SER	0	0.021	0.009	20.581	0.086	0.086	0.000	0.000	0.000	0.000
135	A	135	GLY	0	-0.007	-0.005	20.332	-0.112	-0.112	0.000	0.000	0.000	0.000
136	A	136	PRO	0	-0.026	0.001	19.150	0.566	0.566	0.000	0.000	0.000	0.000
137	A	137	SER	0	-0.063	-0.052	21.696	-0.632	-0.632	0.000	0.000	0.000	0.000
138	A	138	SER	0	-0.047	-0.017	23.967	0.287	0.287	0.000	0.000	0.000	0.000
139	A	139	GLY	-1	-0.912	-0.939	27.200	-11.180	-11.180	0.000	0.000	0.000	0.000

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