FMO DATABASE

FMODB ID: 7KMLK

Calculation Name: 2DBA-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2DBA

Chain ID: A

ChEMBL ID:

UniProt ID: Q9H3U1

Base Structure: SolutionNMR

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	148
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1201233.854426
FMO2-HF: Nuclear repulsion	1145923.23807
FMO2-HF: Total energy	-55310.616356
FMO2-MP2: Total energy	-55471.233544

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.
-16.682	-15.663	-0.013	-0.428	-0.578	-0.001

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 : 0.861 / q_NPA : 0.918

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	0.042	0.015	3.843	2.612	3.631	-0.013	-0.428	-0.578	-0.001
4	A	4	GLY	0	0.037	0.020	7.227	0.183	0.183	0.000	0.000	0.000	0.000
5	A	5	SER	0	-0.017	0.003	10.882	0.954	0.954	0.000	0.000	0.000	0.000
6	A	6	SER	0	0.005	-0.015	14.190	0.056	0.056	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.048	0.014	17.129	0.021	0.021	0.000	0.000	0.000	0.000
8	A	8	MET	0	-0.021	-0.001	20.772	0.092	0.092	0.000	0.000	0.000	0.000
9	A	9	THR	0	0.003	0.020	23.753	0.333	0.333	0.000	0.000	0.000	0.000
10	A	10	VAL	0	-0.003	-0.003	26.163	0.319	0.319	0.000	0.000	0.000	0.000
11	A	11	SER	0	-0.014	-0.016	28.635	0.048	0.048	0.000	0.000	0.000	0.000
12	A	12	GLY	0	0.026	0.008	32.030	0.219	0.219	0.000	0.000	0.000	0.000
13	A	13	PRO	0	-0.020	0.004	33.425	-0.249	-0.249	0.000	0.000	0.000	0.000
14	A	14	GLY	0	0.012	0.012	33.967	-0.166	-0.166	0.000	0.000	0.000	0.000
15	A	15	THR	0	-0.017	-0.026	34.552	0.377	0.377	0.000	0.000	0.000	0.000
16	A	16	PRO	0	-0.047	-0.007	35.458	-0.243	-0.243	0.000	0.000	0.000	0.000
17	A	17	GLU	-1	-0.889	-0.944	32.688	-9.629	-9.629	0.000	0.000	0.000	0.000
18	A	18	PRO	0	-0.068	-0.042	37.333	0.072	0.072	0.000	0.000	0.000	0.000
19	A	19	ARG	1	0.977	0.994	35.994	8.014	8.014	0.000	0.000	0.000	0.000
20	A	20	PRO	0	-0.024	0.002	35.376	0.301	0.301	0.000	0.000	0.000	0.000
21	A	21	ALA	0	0.001	-0.011	38.170	-0.062	-0.062	0.000	0.000	0.000	0.000
22	A	22	THR	0	0.006	0.004	36.764	0.293	0.293	0.000	0.000	0.000	0.000
23	A	23	PRO	0	0.035	0.026	36.475	-0.275	-0.275	0.000	0.000	0.000	0.000
24	A	24	GLY	0	0.023	0.008	32.987	0.047	0.047	0.000	0.000	0.000	0.000
25	A	25	ALA	0	-0.007	-0.004	31.614	-0.348	-0.348	0.000	0.000	0.000	0.000
26	A	26	SER	0	-0.019	-0.003	27.265	-0.028	-0.028	0.000	0.000	0.000	0.000
27	A	27	SER	0	0.044	0.026	27.356	-0.523	-0.523	0.000	0.000	0.000	0.000
28	A	28	VAL	0	0.033	0.012	26.113	0.262	0.262	0.000	0.000	0.000	0.000
29	A	29	GLU	-1	-0.830	-0.930	28.080	-9.401	-9.401	0.000	0.000	0.000	0.000
30	A	30	GLN	0	-0.028	-0.014	31.616	0.508	0.508	0.000	0.000	0.000	0.000
31	A	31	LEU	0	0.043	0.022	26.132	0.195	0.195	0.000	0.000	0.000	0.000
32	A	32	ARG	1	0.881	0.921	29.675	10.019	10.019	0.000	0.000	0.000	0.000
33	A	33	LYS	1	0.779	0.884	30.529	9.436	9.436	0.000	0.000	0.000	0.000
34	A	34	GLU	-1	-0.860	-0.918	30.340	-10.298	-10.298	0.000	0.000	0.000	0.000
35	A	35	GLY	0	0.059	0.027	30.253	0.023	0.023	0.000	0.000	0.000	0.000
36	A	36	ASN	0	-0.051	-0.035	30.932	-0.022	-0.022	0.000	0.000	0.000	0.000
37	A	37	GLU	-1	-0.978	-1.000	34.174	-8.300	-8.300	0.000	0.000	0.000	0.000
38	A	38	LEU	0	0.052	0.040	31.226	0.181	0.181	0.000	0.000	0.000	0.000
39	A	39	PHE	0	-0.019	-0.026	31.427	0.151	0.151	0.000	0.000	0.000	0.000
40	A	40	LYS	1	0.814	0.909	34.240	8.549	8.549	0.000	0.000	0.000	0.000
41	A	41	CYS	0	-0.053	-0.012	36.949	0.341	0.341	0.000	0.000	0.000	0.000
42	A	42	GLY	0	0.028	0.023	36.138	0.174	0.174	0.000	0.000	0.000	0.000
43	A	43	ASP	-1	-0.866	-0.914	32.955	-9.395	-9.395	0.000	0.000	0.000	0.000
44	A	44	TYR	0	0.019	-0.028	30.083	-0.260	-0.260	0.000	0.000	0.000	0.000
45	A	45	GLY	0	0.023	0.010	27.187	-0.382	-0.382	0.000	0.000	0.000	0.000
46	A	46	GLY	0	0.039	0.015	26.762	-0.439	-0.439	0.000	0.000	0.000	0.000
47	A	47	ALA	0	-0.010	-0.005	28.314	-0.233	-0.233	0.000	0.000	0.000	0.000
48	A	48	LEU	0	0.009	0.002	21.871	-0.193	-0.193	0.000	0.000	0.000	0.000
49	A	49	ALA	0	0.029	0.030	23.705	-0.564	-0.564	0.000	0.000	0.000	0.000
50	A	50	ALA	0	0.070	0.043	24.271	-0.412	-0.412	0.000	0.000	0.000	0.000
51	A	51	TYR	0	-0.015	-0.045	25.634	-0.086	-0.086	0.000	0.000	0.000	0.000
52	A	52	THR	0	-0.090	-0.055	19.416	-0.673	-0.673	0.000	0.000	0.000	0.000
53	A	53	GLN	0	0.017	0.000	21.063	-0.247	-0.247	0.000	0.000	0.000	0.000
54	A	54	ALA	0	-0.021	-0.003	22.723	-0.124	-0.124	0.000	0.000	0.000	0.000
55	A	55	LEU	0	-0.036	-0.028	20.272	0.116	0.116	0.000	0.000	0.000	0.000
56	A	56	GLY	0	-0.061	-0.007	18.650	-0.735	-0.735	0.000	0.000	0.000	0.000
57	A	57	LEU	0	-0.008	-0.005	19.626	0.065	0.065	0.000	0.000	0.000	0.000
58	A	58	ASP	-1	-0.916	-0.943	22.126	-12.758	-12.758	0.000	0.000	0.000	0.000
59	A	59	ALA	0	-0.019	-0.010	23.622	0.592	0.592	0.000	0.000	0.000	0.000
60	A	60	THR	0	0.080	0.035	25.170	-0.411	-0.411	0.000	0.000	0.000	0.000
61	A	61	PRO	0	0.016	-0.006	25.646	-0.174	-0.174	0.000	0.000	0.000	0.000
62	A	62	GLN	0	0.010	0.008	26.666	-0.221	-0.221	0.000	0.000	0.000	0.000
63	A	63	ASP	-1	-0.784	-0.890	28.347	-10.317	-10.317	0.000	0.000	0.000	0.000
64	A	64	GLN	0	-0.037	-0.031	22.478	-0.420	-0.420	0.000	0.000	0.000	0.000
65	A	65	ALA	0	0.043	0.032	25.098	-0.360	-0.360	0.000	0.000	0.000	0.000
66	A	66	VAL	0	-0.057	-0.045	27.058	0.075	0.075	0.000	0.000	0.000	0.000
67	A	67	LEU	0	-0.002	0.005	25.120	0.195	0.195	0.000	0.000	0.000	0.000
68	A	68	HIS	0	0.024	0.014	19.689	-0.193	-0.193	0.000	0.000	0.000	0.000
69	A	69	ARG	1	0.871	0.918	24.661	10.153	10.153	0.000	0.000	0.000	0.000
70	A	70	ASN	0	-0.053	-0.014	27.713	0.577	0.577	0.000	0.000	0.000	0.000
71	A	71	ARG	1	0.922	0.963	18.374	16.232	16.232	0.000	0.000	0.000	0.000
72	A	72	ALA	0	0.024	0.021	25.477	0.014	0.014	0.000	0.000	0.000	0.000
73	A	73	ALA	0	-0.025	-0.012	26.462	0.215	0.215	0.000	0.000	0.000	0.000
74	A	74	CYS	0	-0.058	-0.017	26.642	0.382	0.382	0.000	0.000	0.000	0.000
75	A	75	HIS	0	0.056	0.015	21.220	0.396	0.396	0.000	0.000	0.000	0.000
76	A	76	LEU	0	-0.045	-0.021	26.175	0.144	0.144	0.000	0.000	0.000	0.000
77	A	77	LYS	1	0.849	0.938	29.336	9.503	9.503	0.000	0.000	0.000	0.000
78	A	78	LEU	0	-0.041	-0.017	25.943	0.292	0.292	0.000	0.000	0.000	0.000
79	A	79	GLU	-1	-0.935	-0.953	26.773	-11.318	-11.318	0.000	0.000	0.000	0.000
80	A	80	ASP	-1	-0.791	-0.859	22.474	-14.603	-14.603	0.000	0.000	0.000	0.000
81	A	81	TYR	0	0.012	-0.020	24.459	-0.191	-0.191	0.000	0.000	0.000	0.000
82	A	82	ASP	-1	-0.876	-0.947	21.682	-13.683	-13.683	0.000	0.000	0.000	0.000
83	A	83	LYS	1	0.813	0.896	18.359	15.373	15.373	0.000	0.000	0.000	0.000
84	A	84	ALA	0	-0.023	-0.017	21.596	-0.100	-0.100	0.000	0.000	0.000	0.000
85	A	85	GLU	-1	-0.839	-0.922	23.073	-13.718	-13.718	0.000	0.000	0.000	0.000
86	A	86	THR	0	0.003	-0.010	18.722	-0.175	-0.175	0.000	0.000	0.000	0.000
87	A	87	GLU	-1	-0.842	-0.919	20.286	-16.446	-16.446	0.000	0.000	0.000	0.000
88	A	88	ALA	0	0.000	0.000	22.563	0.281	0.281	0.000	0.000	0.000	0.000
89	A	89	SER	0	0.015	-0.005	22.806	0.496	0.496	0.000	0.000	0.000	0.000
90	A	90	LYS	1	0.859	0.930	17.455	17.904	17.904	0.000	0.000	0.000	0.000
91	A	91	ALA	0	-0.056	-0.029	22.793	0.098	0.098	0.000	0.000	0.000	0.000
92	A	92	ILE	0	-0.060	-0.032	26.317	0.395	0.395	0.000	0.000	0.000	0.000
93	A	93	GLU	-1	-0.944	-0.976	21.206	-14.968	-14.968	0.000	0.000	0.000	0.000
94	A	94	LYS	1	0.867	0.948	21.276	14.404	14.404	0.000	0.000	0.000	0.000
95	A	95	ASP	-1	-0.890	-0.933	26.537	-9.594	-9.594	0.000	0.000	0.000	0.000
96	A	96	GLY	0	0.037	0.029	30.312	0.092	0.092	0.000	0.000	0.000	0.000
97	A	97	GLY	0	-0.021	-0.013	31.505	0.200	0.200	0.000	0.000	0.000	0.000
98	A	98	ASP	-1	-0.813	-0.887	30.684	-10.127	-10.127	0.000	0.000	0.000	0.000
99	A	99	VAL	0	0.015	-0.012	32.332	-0.248	-0.248	0.000	0.000	0.000	0.000
100	A	100	LYS	1	0.893	0.947	33.145	8.794	8.794	0.000	0.000	0.000	0.000
101	A	101	ALA	0	0.021	0.014	28.588	-0.063	-0.063	0.000	0.000	0.000	0.000
102	A	102	LEU	0	-0.009	0.008	30.544	-0.122	-0.122	0.000	0.000	0.000	0.000
103	A	103	TYR	0	0.044	0.009	32.252	-0.030	-0.030	0.000	0.000	0.000	0.000
104	A	104	ARG	1	0.835	0.912	30.318	10.244	10.244	0.000	0.000	0.000	0.000
105	A	105	ARG	1	0.824	0.891	26.012	11.672	11.672	0.000	0.000	0.000	0.000
106	A	106	SER	0	-0.006	-0.005	29.859	-0.114	-0.114	0.000	0.000	0.000	0.000
107	A	107	GLN	0	-0.048	-0.022	32.546	0.011	0.011	0.000	0.000	0.000	0.000
108	A	108	ALA	0	0.005	0.009	27.367	0.062	0.062	0.000	0.000	0.000	0.000
109	A	109	LEU	0	-0.011	-0.015	27.382	-0.131	-0.131	0.000	0.000	0.000	0.000
110	A	110	GLU	-1	-0.813	-0.914	29.791	-9.179	-9.179	0.000	0.000	0.000	0.000
111	A	111	LYS	1	0.836	0.928	30.125	9.941	9.941	0.000	0.000	0.000	0.000
112	A	112	LEU	0	-0.043	-0.010	25.218	-0.075	-0.075	0.000	0.000	0.000	0.000
113	A	113	GLY	0	0.036	0.030	28.744	-0.110	-0.110	0.000	0.000	0.000	0.000
114	A	114	ARG	1	0.889	0.947	23.128	13.111	13.111	0.000	0.000	0.000	0.000
115	A	115	LEU	0	0.078	0.026	31.223	-0.070	-0.070	0.000	0.000	0.000	0.000
116	A	116	ASP	-1	-0.853	-0.927	33.898	-9.092	-9.092	0.000	0.000	0.000	0.000
117	A	117	GLN	0	-0.024	-0.022	28.916	0.143	0.143	0.000	0.000	0.000	0.000
118	A	118	ALA	0	0.018	0.019	32.257	0.028	0.028	0.000	0.000	0.000	0.000
119	A	119	VAL	0	0.025	0.002	33.851	0.185	0.185	0.000	0.000	0.000	0.000
120	A	120	LEU	0	0.008	0.005	33.298	0.152	0.152	0.000	0.000	0.000	0.000
121	A	121	ASP	-1	-0.789	-0.873	30.814	-10.683	-10.683	0.000	0.000	0.000	0.000
122	A	122	LEU	0	0.023	0.004	34.178	0.162	0.162	0.000	0.000	0.000	0.000
123	A	123	GLN	0	-0.013	-0.017	37.595	0.113	0.113	0.000	0.000	0.000	0.000
124	A	124	ARG	1	0.939	0.980	30.983	10.210	10.210	0.000	0.000	0.000	0.000
125	A	125	CYS	0	-0.057	-0.031	36.135	0.045	0.045	0.000	0.000	0.000	0.000
126	A	126	VAL	0	-0.031	-0.025	38.443	0.176	0.176	0.000	0.000	0.000	0.000
127	A	127	SER	0	-0.053	-0.009	39.937	0.254	0.254	0.000	0.000	0.000	0.000
128	A	128	LEU	0	0.006	0.006	36.955	0.134	0.134	0.000	0.000	0.000	0.000
129	A	129	GLU	-1	-0.921	-0.950	40.799	-7.528	-7.528	0.000	0.000	0.000	0.000
130	A	130	PRO	0	0.043	0.025	43.191	0.086	0.086	0.000	0.000	0.000	0.000
131	A	131	LYS	1	0.881	0.929	46.252	6.574	6.574	0.000	0.000	0.000	0.000
132	A	132	ASN	0	-0.001	0.010	42.004	0.225	0.225	0.000	0.000	0.000	0.000
133	A	133	LYS	1	0.969	0.976	44.527	6.239	6.239	0.000	0.000	0.000	0.000
134	A	134	VAL	0	0.006	0.017	41.464	-0.017	-0.017	0.000	0.000	0.000	0.000
135	A	135	PHE	0	0.013	0.000	38.778	-0.135	-0.135	0.000	0.000	0.000	0.000
136	A	136	GLN	0	0.001	0.002	42.085	0.043	0.043	0.000	0.000	0.000	0.000
137	A	137	GLU	-1	-0.907	-0.969	45.199	-6.727	-6.727	0.000	0.000	0.000	0.000
138	A	138	ALA	0	-0.025	-0.013	39.979	-0.019	-0.019	0.000	0.000	0.000	0.000
139	A	139	LEU	0	0.002	0.007	39.910	-0.098	-0.098	0.000	0.000	0.000	0.000
140	A	140	ARG	1	0.950	0.965	41.904	6.994	6.994	0.000	0.000	0.000	0.000
141	A	141	ASN	0	-0.051	-0.017	40.241	0.136	0.136	0.000	0.000	0.000	0.000
142	A	142	ILE	0	-0.021	-0.002	36.830	-0.008	-0.008	0.000	0.000	0.000	0.000
143	A	143	SER	0	-0.045	-0.008	39.826	-0.092	-0.092	0.000	0.000	0.000	0.000
144	A	144	GLY	0	0.016	0.023	41.803	0.030	0.030	0.000	0.000	0.000	0.000
145	A	145	PRO	0	-0.055	-0.029	44.799	0.114	0.114	0.000	0.000	0.000	0.000
146	A	146	SER	0	0.020	0.005	45.721	-0.182	-0.182	0.000	0.000	0.000	0.000
147	A	147	SER	0	-0.055	-0.051	45.206	0.129	0.129	0.000	0.000	0.000	0.000
148	A	148	GLY	-1	-0.941	-0.940	45.396	-6.876	-6.876	0.000	0.000	0.000	0.000

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