FMO DATABASE

FMODB ID: N8V1Q

Calculation Name: 2M19-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2M19

Chain ID: A

ChEMBL ID:

UniProt ID: D4GVB0

Base Structure: SolutionNMR

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	106
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-760733.200304
FMO2-HF: Nuclear repulsion	720350.562891
FMO2-HF: Total energy	-40382.637413
FMO2-MP2: Total energy	-40501.172409

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:-13:GLY)

Summations of interaction energy for fragment #1(A:-13: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.
-199.359	-198.385	0.014	-0.518	-0.47	-0.002

Interaction energy analysis for fragmet #1(A:-13:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.856 / q_NPA : 0.915

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	-11	GLY	0	0.086	0.049	3.655	-7.236	-6.262	0.014	-0.518	-0.470	-0.002
4	A	-10	ARG	1	0.893	0.952	6.479	28.817	28.817	0.000	0.000	0.000	0.000
5	A	-9	ASP	-1	-0.848	-0.935	6.240	-40.871	-40.871	0.000	0.000	0.000	0.000
6	A	-8	TYR	0	0.016	0.008	9.294	0.783	0.783	0.000	0.000	0.000	0.000
7	A	-7	LYS	1	0.752	0.854	9.272	29.577	29.577	0.000	0.000	0.000	0.000
8	A	-6	ASP	-1	-0.836	-0.921	14.203	-17.576	-17.576	0.000	0.000	0.000	0.000
9	A	-5	ASP	-1	-0.881	-0.954	14.554	-20.046	-20.046	0.000	0.000	0.000	0.000
10	A	-4	ASP	-1	-0.875	-0.921	8.868	-32.329	-32.329	0.000	0.000	0.000	0.000
11	A	-3	ASP	-1	-0.938	-0.970	7.452	-29.107	-29.107	0.000	0.000	0.000	0.000
12	A	-2	LYS	1	0.695	0.851	8.263	19.532	19.532	0.000	0.000	0.000	0.000
13	A	-1	GLY	0	0.068	0.049	9.265	-0.223	-0.223	0.000	0.000	0.000	0.000
14	A	0	THR	0	-0.036	-0.008	11.694	1.651	1.651	0.000	0.000	0.000	0.000
15	A	1	MET	0	0.019	0.047	14.220	1.097	1.097	0.000	0.000	0.000	0.000
16	A	2	GLU	-1	-0.909	-0.966	17.866	-13.865	-13.865	0.000	0.000	0.000	0.000
17	A	3	LEU	0	0.025	0.019	20.947	0.506	0.506	0.000	0.000	0.000	0.000
18	A	4	GLU	-1	-0.811	-0.874	23.969	-9.827	-9.827	0.000	0.000	0.000	0.000
19	A	5	LEU	0	-0.006	0.001	24.485	0.163	0.163	0.000	0.000	0.000	0.000
20	A	6	ARG	1	0.829	0.878	28.588	9.608	9.608	0.000	0.000	0.000	0.000
21	A	7	PHE	0	0.066	0.036	28.413	0.133	0.133	0.000	0.000	0.000	0.000
22	A	8	PHE	0	-0.044	-0.037	34.286	0.358	0.358	0.000	0.000	0.000	0.000
23	A	9	ALA	0	0.000	-0.022	37.988	-0.040	-0.040	0.000	0.000	0.000	0.000
24	A	10	THR	0	0.010	0.003	38.864	-0.027	-0.027	0.000	0.000	0.000	0.000
25	A	11	PHE	0	0.073	0.035	34.234	-0.052	-0.052	0.000	0.000	0.000	0.000
26	A	12	ARG	1	0.925	0.990	34.920	7.820	7.820	0.000	0.000	0.000	0.000
27	A	13	GLU	-1	-1.014	-1.024	36.769	-8.097	-8.097	0.000	0.000	0.000	0.000
28	A	14	VAL	0	0.014	0.013	33.464	-0.049	-0.049	0.000	0.000	0.000	0.000
29	A	15	VAL	0	0.039	0.026	30.642	-0.110	-0.110	0.000	0.000	0.000	0.000
30	A	16	GLY	0	-0.025	0.005	32.984	-0.115	-0.115	0.000	0.000	0.000	0.000
31	A	17	GLN	0	-0.047	-0.029	30.594	0.068	0.068	0.000	0.000	0.000	0.000
32	A	18	LYS	1	0.964	0.967	34.011	8.026	8.026	0.000	0.000	0.000	0.000
33	A	19	SER	0	-0.081	-0.051	32.157	0.102	0.102	0.000	0.000	0.000	0.000
34	A	20	ILE	0	-0.020	0.021	27.124	0.225	0.225	0.000	0.000	0.000	0.000
35	A	21	TYR	0	-0.020	-0.020	24.882	0.092	0.092	0.000	0.000	0.000	0.000
36	A	22	TRP	0	0.011	-0.004	21.257	-0.156	-0.156	0.000	0.000	0.000	0.000
37	A	23	ARG	1	0.804	0.892	16.931	16.680	16.680	0.000	0.000	0.000	0.000
38	A	24	VAL	0	-0.005	0.007	16.508	-0.104	-0.104	0.000	0.000	0.000	0.000
39	A	25	ASP	-1	-0.837	-0.936	11.413	-25.828	-25.828	0.000	0.000	0.000	0.000
40	A	26	ASP	-1	-0.933	-0.974	13.392	-20.914	-20.914	0.000	0.000	0.000	0.000
41	A	27	ASP	-1	-0.940	-0.963	14.089	-18.874	-18.874	0.000	0.000	0.000	0.000
42	A	28	ALA	0	-0.044	-0.011	16.034	1.001	1.001	0.000	0.000	0.000	0.000
43	A	29	THR	0	0.002	-0.019	18.182	0.767	0.767	0.000	0.000	0.000	0.000
44	A	30	VAL	0	-0.022	-0.033	21.793	-0.018	-0.018	0.000	0.000	0.000	0.000
45	A	31	GLY	0	0.043	-0.009	24.399	0.185	0.185	0.000	0.000	0.000	0.000
46	A	32	ASP	-1	-0.910	-0.944	18.475	-17.188	-17.188	0.000	0.000	0.000	0.000
47	A	33	VAL	0	0.026	0.023	21.360	0.078	0.078	0.000	0.000	0.000	0.000
48	A	34	LEU	0	-0.055	-0.033	22.883	0.296	0.296	0.000	0.000	0.000	0.000
49	A	35	ARG	1	0.866	0.918	22.159	14.118	14.118	0.000	0.000	0.000	0.000
50	A	36	SER	0	-0.006	-0.014	20.459	-0.148	-0.148	0.000	0.000	0.000	0.000
51	A	37	LEU	0	-0.033	-0.028	22.675	0.317	0.317	0.000	0.000	0.000	0.000
52	A	38	GLU	-1	-0.910	-0.953	26.067	-11.660	-11.660	0.000	0.000	0.000	0.000
53	A	39	ALA	0	-0.038	-0.002	23.489	0.248	0.248	0.000	0.000	0.000	0.000
54	A	40	GLU	-1	-0.965	-0.966	23.053	-13.468	-13.468	0.000	0.000	0.000	0.000
55	A	41	TYR	0	-0.018	-0.006	26.376	0.346	0.346	0.000	0.000	0.000	0.000
56	A	42	ASP	-1	-0.827	-0.916	30.139	-9.858	-9.858	0.000	0.000	0.000	0.000
57	A	43	GLY	0	-0.049	-0.029	32.723	0.188	0.188	0.000	0.000	0.000	0.000
58	A	44	LEU	0	-0.038	-0.042	29.795	0.323	0.323	0.000	0.000	0.000	0.000
59	A	45	ALA	0	0.062	0.042	31.050	-0.115	-0.115	0.000	0.000	0.000	0.000
60	A	46	GLY	0	-0.003	0.004	31.084	0.346	0.346	0.000	0.000	0.000	0.000
61	A	47	ARG	1	0.800	0.898	32.675	8.828	8.828	0.000	0.000	0.000	0.000
62	A	48	LEU	0	-0.047	-0.029	28.813	0.324	0.324	0.000	0.000	0.000	0.000
63	A	49	ILE	0	0.049	0.031	26.417	-0.302	-0.302	0.000	0.000	0.000	0.000
64	A	50	GLU	-1	-0.907	-0.953	30.801	-8.790	-8.790	0.000	0.000	0.000	0.000
65	A	51	ASP	-1	-0.949	-0.971	31.971	-9.877	-9.877	0.000	0.000	0.000	0.000
66	A	52	GLY	0	0.002	0.014	27.797	-0.197	-0.197	0.000	0.000	0.000	0.000
67	A	53	GLU	-1	-0.914	-0.963	27.814	-9.804	-9.804	0.000	0.000	0.000	0.000
68	A	54	VAL	0	-0.014	-0.008	29.564	-0.164	-0.164	0.000	0.000	0.000	0.000
69	A	55	LYS	1	0.814	0.891	31.583	9.337	9.337	0.000	0.000	0.000	0.000
70	A	56	PRO	0	0.039	0.031	35.285	0.068	0.068	0.000	0.000	0.000	0.000
71	A	57	HIS	0	-0.015	-0.021	38.775	-0.122	-0.122	0.000	0.000	0.000	0.000
72	A	58	VAL	0	-0.006	0.023	34.323	0.126	0.126	0.000	0.000	0.000	0.000
73	A	59	ASN	0	0.008	0.017	36.589	-0.152	-0.152	0.000	0.000	0.000	0.000
74	A	60	VAL	0	0.052	0.015	31.859	-0.063	-0.063	0.000	0.000	0.000	0.000
75	A	61	LEU	0	-0.063	-0.040	32.787	0.133	0.133	0.000	0.000	0.000	0.000
76	A	62	LYS	1	0.870	0.935	26.229	11.423	11.423	0.000	0.000	0.000	0.000
77	A	63	ASN	0	0.011	0.012	29.935	0.144	0.144	0.000	0.000	0.000	0.000
78	A	64	GLY	0	-0.024	-0.002	31.536	0.302	0.302	0.000	0.000	0.000	0.000
79	A	65	ARG	1	0.915	0.954	33.760	8.911	8.911	0.000	0.000	0.000	0.000
80	A	66	GLU	-1	-0.869	-0.956	33.949	-8.498	-8.498	0.000	0.000	0.000	0.000
81	A	67	VAL	0	0.037	0.004	30.403	0.200	0.200	0.000	0.000	0.000	0.000
82	A	68	VAL	0	0.050	0.037	33.466	-0.107	-0.107	0.000	0.000	0.000	0.000
83	A	69	HIS	1	0.737	0.869	35.767	8.488	8.488	0.000	0.000	0.000	0.000
84	A	70	LEU	0	-0.040	-0.013	31.154	0.166	0.166	0.000	0.000	0.000	0.000
85	A	71	ASP	-1	-0.855	-0.916	28.092	-10.695	-10.695	0.000	0.000	0.000	0.000
86	A	72	GLY	0	-0.034	-0.024	28.921	-0.267	-0.267	0.000	0.000	0.000	0.000
87	A	73	MET	0	-0.006	0.029	25.617	-0.389	-0.389	0.000	0.000	0.000	0.000
88	A	74	ALA	0	-0.001	-0.002	23.556	-0.538	-0.538	0.000	0.000	0.000	0.000
89	A	75	THR	0	-0.011	0.003	24.945	0.031	0.031	0.000	0.000	0.000	0.000
90	A	76	ALA	0	0.014	0.000	24.286	-0.111	-0.111	0.000	0.000	0.000	0.000
91	A	77	LEU	0	-0.072	-0.033	22.193	0.578	0.578	0.000	0.000	0.000	0.000
92	A	78	ASP	-1	-0.838	-0.899	21.445	-14.093	-14.093	0.000	0.000	0.000	0.000
93	A	79	ASP	-1	-0.935	-0.989	20.197	-14.202	-14.202	0.000	0.000	0.000	0.000
94	A	80	GLY	0	-0.028	-0.012	22.118	0.500	0.500	0.000	0.000	0.000	0.000
95	A	81	ASP	-1	-0.803	-0.883	24.939	-10.828	-10.828	0.000	0.000	0.000	0.000
96	A	82	ALA	0	-0.001	-0.004	26.845	0.006	0.006	0.000	0.000	0.000	0.000
97	A	83	VAL	0	0.006	0.012	26.120	0.360	0.360	0.000	0.000	0.000	0.000
98	A	84	SER	0	-0.079	-0.039	29.291	0.226	0.226	0.000	0.000	0.000	0.000
99	A	85	VAL	0	0.002	0.005	30.667	0.031	0.031	0.000	0.000	0.000	0.000
100	A	86	PHE	0	-0.018	-0.022	33.791	0.227	0.227	0.000	0.000	0.000	0.000
101	A	87	PRO	0	-0.018	0.000	36.778	-0.127	-0.127	0.000	0.000	0.000	0.000
102	A	88	PRO	0	0.001	-0.004	37.507	0.109	0.109	0.000	0.000	0.000	0.000
103	A	89	VAL	0	-0.044	-0.015	39.994	0.190	0.190	0.000	0.000	0.000	0.000
104	A	90	ALA	0	0.008	-0.004	43.480	-0.008	-0.008	0.000	0.000	0.000	0.000
105	A	91	GLY	0	-0.044	-0.025	46.273	0.103	0.103	0.000	0.000	0.000	0.000
106	A	92	GLY	-1	-0.959	-0.968	47.540	-6.386	-6.386	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-13:GLY)