FMO DATABASE

FMODB ID: G8VM1

Calculation Name: 1D8B-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1D8B

Chain ID: A

ChEMBL ID:

UniProt ID: P35187

Base Structure: SolutionNMR

Registration Date: 2025-09-02

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	81
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-558055.488121
FMO2-HF: Nuclear repulsion	524660.010131
FMO2-HF: Total energy	-33395.47799
FMO2-MP2: Total energy	-33490.661508

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:11:GLU)

Summations of interaction energy for fragment #1(A:11:GLU)

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.
1.238	3.322	0.014	-0.824	-1.273	0.002

Interaction energy analysis for fragmet #1(A:11:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.012 / q_NPA : -0.027

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	13	ASN	0	0.018	0.012	3.341	2.668	4.594	0.015	-0.812	-1.128	0.002
4	A	14	ASN	0	0.076	0.017	4.696	2.351	2.509	-0.001	-0.012	-0.145	0.000
5	A	15	LEU	0	-0.012	0.025	7.997	1.016	1.016	0.000	0.000	0.000	0.000
6	A	16	ARG	1	0.954	0.969	7.249	1.607	1.607	0.000	0.000	0.000	0.000
7	A	17	MET	0	0.057	0.026	8.814	0.557	0.557	0.000	0.000	0.000	0.000
8	A	18	THR	0	0.024	0.013	10.756	0.560	0.560	0.000	0.000	0.000	0.000
9	A	19	TYR	0	-0.081	-0.070	12.399	0.342	0.342	0.000	0.000	0.000	0.000
10	A	20	GLU	-1	-0.892	-0.925	11.878	-2.045	-2.045	0.000	0.000	0.000	0.000
11	A	21	ARG	1	0.819	0.859	14.508	1.935	1.935	0.000	0.000	0.000	0.000
12	A	22	LEU	0	-0.022	-0.005	16.547	0.188	0.188	0.000	0.000	0.000	0.000
13	A	23	ARG	1	0.877	0.937	17.046	0.350	0.350	0.000	0.000	0.000	0.000
14	A	24	GLU	-1	-0.793	-0.872	18.353	-1.123	-1.123	0.000	0.000	0.000	0.000
15	A	25	LEU	0	0.048	0.013	20.424	0.078	0.078	0.000	0.000	0.000	0.000
16	A	26	SER	0	-0.068	-0.054	21.930	0.099	0.099	0.000	0.000	0.000	0.000
17	A	27	LEU	0	0.008	0.004	22.874	0.060	0.060	0.000	0.000	0.000	0.000
18	A	28	ASN	0	-0.014	0.005	23.584	0.058	0.058	0.000	0.000	0.000	0.000
19	A	29	LEU	0	-0.012	-0.009	25.625	0.030	0.030	0.000	0.000	0.000	0.000
20	A	30	GLY	0	-0.008	-0.003	27.652	0.040	0.040	0.000	0.000	0.000	0.000
21	A	31	ASN	0	-0.045	-0.030	29.260	0.028	0.028	0.000	0.000	0.000	0.000
22	A	32	ARG	1	0.940	0.969	27.894	0.545	0.545	0.000	0.000	0.000	0.000
23	A	33	MET	0	-0.046	-0.005	32.763	0.009	0.009	0.000	0.000	0.000	0.000
24	A	34	VAL	0	0.023	0.024	34.593	0.009	0.009	0.000	0.000	0.000	0.000
25	A	35	PRO	0	0.018	-0.006	38.016	0.004	0.004	0.000	0.000	0.000	0.000
26	A	36	PRO	0	0.013	0.003	33.160	-0.008	-0.008	0.000	0.000	0.000	0.000
27	A	37	VAL	0	-0.034	-0.015	30.496	0.021	0.021	0.000	0.000	0.000	0.000
28	A	38	GLY	0	0.029	0.025	29.887	0.030	0.030	0.000	0.000	0.000	0.000
29	A	39	ASN	0	-0.022	-0.016	25.984	-0.045	-0.045	0.000	0.000	0.000	0.000
30	A	40	PHE	0	0.033	0.011	25.456	0.019	0.019	0.000	0.000	0.000	0.000
31	A	41	MET	0	0.004	0.004	23.280	0.018	0.018	0.000	0.000	0.000	0.000
32	A	42	PRO	0	0.017	0.026	23.635	0.003	0.003	0.000	0.000	0.000	0.000
33	A	43	ASP	-1	-0.709	-0.831	18.537	0.120	0.120	0.000	0.000	0.000	0.000
34	A	44	SER	0	0.010	0.005	19.103	-0.012	-0.012	0.000	0.000	0.000	0.000
35	A	45	ILE	0	0.012	-0.008	20.310	0.016	0.016	0.000	0.000	0.000	0.000
36	A	46	LEU	0	-0.015	0.000	18.243	-0.042	-0.042	0.000	0.000	0.000	0.000
37	A	47	LYS	1	0.926	0.954	14.563	-0.535	-0.535	0.000	0.000	0.000	0.000
38	A	48	LYS	1	0.874	0.961	15.879	-0.174	-0.174	0.000	0.000	0.000	0.000
39	A	49	MET	0	-0.026	-0.006	17.868	-0.078	-0.078	0.000	0.000	0.000	0.000
40	A	50	ALA	0	0.010	0.001	13.688	-0.113	-0.113	0.000	0.000	0.000	0.000
41	A	51	ALA	0	0.017	0.016	13.428	-0.217	-0.217	0.000	0.000	0.000	0.000
42	A	52	ILE	0	0.000	-0.007	14.448	-0.122	-0.122	0.000	0.000	0.000	0.000
43	A	53	LEU	0	-0.031	0.007	14.238	-0.060	-0.060	0.000	0.000	0.000	0.000
44	A	54	PRO	0	0.001	0.014	18.144	-0.033	-0.033	0.000	0.000	0.000	0.000
45	A	55	MET	0	0.021	0.006	21.516	-0.017	-0.017	0.000	0.000	0.000	0.000
46	A	56	ASN	0	-0.015	-0.013	23.771	0.024	0.024	0.000	0.000	0.000	0.000
47	A	57	ASP	-1	-0.892	-0.951	26.817	-0.213	-0.213	0.000	0.000	0.000	0.000
48	A	58	SER	0	0.032	0.013	29.040	0.013	0.013	0.000	0.000	0.000	0.000
49	A	59	ALA	0	0.002	0.014	24.075	0.019	0.019	0.000	0.000	0.000	0.000
50	A	60	PHE	0	-0.005	-0.005	23.687	0.026	0.026	0.000	0.000	0.000	0.000
51	A	61	ALA	0	0.017	0.022	26.094	0.041	0.041	0.000	0.000	0.000	0.000
52	A	62	THR	0	-0.007	-0.019	23.189	0.040	0.040	0.000	0.000	0.000	0.000
53	A	63	LEU	0	-0.020	-0.004	20.953	0.041	0.041	0.000	0.000	0.000	0.000
54	A	64	GLY	0	0.016	0.016	23.668	0.059	0.059	0.000	0.000	0.000	0.000
55	A	65	THR	0	-0.023	-0.030	26.175	-0.003	-0.003	0.000	0.000	0.000	0.000
56	A	66	VAL	0	-0.050	-0.015	25.844	-0.006	-0.006	0.000	0.000	0.000	0.000
57	A	67	GLU	-1	-0.812	-0.914	28.430	-0.044	-0.044	0.000	0.000	0.000	0.000
58	A	68	ASP	-1	-0.761	-0.857	31.198	-0.158	-0.158	0.000	0.000	0.000	0.000
59	A	69	LYS	1	0.933	0.961	32.338	0.013	0.013	0.000	0.000	0.000	0.000
60	A	70	TYR	0	-0.024	-0.028	27.842	-0.029	-0.029	0.000	0.000	0.000	0.000
61	A	71	ARG	1	0.931	0.945	29.315	0.070	0.070	0.000	0.000	0.000	0.000
62	A	72	ARG	1	0.956	0.988	30.573	0.135	0.135	0.000	0.000	0.000	0.000
63	A	73	ARG	1	0.811	0.892	28.208	0.188	0.188	0.000	0.000	0.000	0.000
64	A	74	PHE	0	0.064	0.007	23.015	-0.038	-0.038	0.000	0.000	0.000	0.000
65	A	75	LYS	1	0.898	0.960	26.859	0.251	0.251	0.000	0.000	0.000	0.000
66	A	76	TYR	0	0.012	-0.001	28.252	-0.023	-0.023	0.000	0.000	0.000	0.000
67	A	77	PHE	0	0.025	0.016	21.971	-0.031	-0.031	0.000	0.000	0.000	0.000
68	A	78	LYS	1	0.927	0.977	23.228	0.393	0.393	0.000	0.000	0.000	0.000
69	A	79	ALA	0	0.048	0.024	24.109	-0.043	-0.043	0.000	0.000	0.000	0.000
70	A	80	THR	0	0.038	0.010	19.084	-0.055	-0.055	0.000	0.000	0.000	0.000
71	A	81	ILE	0	-0.005	-0.006	19.318	-0.130	-0.130	0.000	0.000	0.000	0.000
72	A	82	ALA	0	-0.009	-0.009	19.624	-0.070	-0.070	0.000	0.000	0.000	0.000
73	A	83	ASP	-1	-0.926	-0.958	18.708	-1.672	-1.672	0.000	0.000	0.000	0.000
74	A	84	LEU	0	0.024	0.000	14.129	-0.120	-0.120	0.000	0.000	0.000	0.000
75	A	85	SER	0	-0.038	-0.032	15.145	-0.203	-0.203	0.000	0.000	0.000	0.000
76	A	86	LYS	1	0.923	0.964	16.622	1.253	1.253	0.000	0.000	0.000	0.000
77	A	87	LYS	1	0.856	0.906	13.684	2.899	2.899	0.000	0.000	0.000	0.000
78	A	88	ARG	1	0.908	0.951	11.492	0.821	0.821	0.000	0.000	0.000	0.000
79	A	89	SER	0	-0.068	-0.029	11.722	-0.019	-0.019	0.000	0.000	0.000	0.000
80	A	90	SER	0	-0.083	-0.037	12.492	0.333	0.333	0.000	0.000	0.000	0.000
81	A	91	GLU	-2	-1.724	-1.811	7.310	-10.661	-10.661	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

Interactive mode: IFIE and PIEDA for fragment #1(A:11:GLU)