FMO DATABASE

FMODB ID: VV7L1

Calculation Name: 2DGP-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

PDB ID: 2DGP

Chain ID: A

ChEMBL ID:

UniProt ID: Q9BZC1

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

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	-713950.111723
FMO2-HF: Nuclear repulsion	672753.455013
FMO2-HF: Total energy	-41196.65671
FMO2-MP2: Total energy	-41314.471002

3D Structure

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:41:GLY)

Summations of interaction energy for fragment #1(A:41: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.
19.558	20.937	-0.013	-0.585	-0.78	-0.003

Interaction energy analysis for fragmet #1(A:41:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.868 / 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	43	SER	0	0.042	0.040	3.841	5.594	6.785	-0.011	-0.560	-0.620	-0.003
4	A	44	GLY	0	-0.007	-0.010	4.031	1.542	1.643	-0.001	-0.021	-0.079	0.000
5	A	45	SER	0	0.014	0.007	5.049	5.421	5.508	-0.001	-0.004	-0.081	0.000
6	A	46	SER	0	0.016	0.003	8.059	3.092	3.092	0.000	0.000	0.000	0.000
7	A	47	GLY	0	0.038	0.010	9.484	-0.697	-0.697	0.000	0.000	0.000	0.000
8	A	48	MET	0	-0.031	0.000	12.785	0.193	0.193	0.000	0.000	0.000	0.000
9	A	49	LYS	1	0.899	0.968	16.427	13.448	13.448	0.000	0.000	0.000	0.000
10	A	50	ASP	-1	-0.855	-0.934	19.018	-14.239	-14.239	0.000	0.000	0.000	0.000
11	A	51	HIS	0	-0.036	-0.036	20.859	0.250	0.250	0.000	0.000	0.000	0.000
12	A	52	ASP	-1	-0.934	-0.960	24.135	-11.037	-11.037	0.000	0.000	0.000	0.000
13	A	53	ALA	0	-0.002	0.015	22.949	0.066	0.066	0.000	0.000	0.000	0.000
14	A	54	ILE	0	-0.021	-0.022	24.603	0.536	0.536	0.000	0.000	0.000	0.000
15	A	55	LYS	1	0.940	0.983	25.557	10.120	10.120	0.000	0.000	0.000	0.000
16	A	56	LEU	0	0.012	0.004	24.728	0.413	0.413	0.000	0.000	0.000	0.000
17	A	57	PHE	0	-0.016	-0.019	28.217	0.003	0.003	0.000	0.000	0.000	0.000
18	A	58	ILE	0	0.004	0.008	27.164	0.026	0.026	0.000	0.000	0.000	0.000
19	A	59	GLY	0	0.013	-0.006	31.122	0.200	0.200	0.000	0.000	0.000	0.000
20	A	60	GLN	0	0.000	-0.001	33.834	-0.095	-0.095	0.000	0.000	0.000	0.000
21	A	61	ILE	0	0.025	0.009	30.460	-0.119	-0.119	0.000	0.000	0.000	0.000
22	A	62	PRO	0	0.032	0.024	33.982	0.204	0.204	0.000	0.000	0.000	0.000
23	A	63	ARG	1	0.873	0.917	35.114	7.415	7.415	0.000	0.000	0.000	0.000
24	A	64	ASN	0	-0.020	-0.024	34.398	0.276	0.276	0.000	0.000	0.000	0.000
25	A	65	LEU	0	0.020	0.026	30.303	-0.138	-0.138	0.000	0.000	0.000	0.000
26	A	66	ASP	-1	-0.847	-0.920	28.249	-10.118	-10.118	0.000	0.000	0.000	0.000
27	A	67	GLU	-1	-0.811	-0.936	26.031	-11.141	-11.141	0.000	0.000	0.000	0.000
28	A	68	LYS	1	0.879	0.929	23.709	10.750	10.750	0.000	0.000	0.000	0.000
29	A	69	ASP	-1	-0.856	-0.916	23.460	-11.860	-11.860	0.000	0.000	0.000	0.000
30	A	70	LEU	0	-0.022	-0.023	24.682	-0.158	-0.158	0.000	0.000	0.000	0.000
31	A	71	LYS	1	0.948	0.983	16.817	16.729	16.729	0.000	0.000	0.000	0.000
32	A	72	PRO	0	-0.027	-0.027	18.960	-0.653	-0.653	0.000	0.000	0.000	0.000
33	A	73	LEU	0	0.046	0.038	18.984	-0.482	-0.482	0.000	0.000	0.000	0.000
34	A	74	PHE	0	0.000	-0.008	20.357	-0.215	-0.215	0.000	0.000	0.000	0.000
35	A	75	GLU	-1	-0.948	-0.972	13.711	-21.733	-21.733	0.000	0.000	0.000	0.000
36	A	76	GLU	-1	-0.907	-0.948	15.451	-16.525	-16.525	0.000	0.000	0.000	0.000
37	A	77	PHE	0	-0.063	-0.030	15.985	-0.240	-0.240	0.000	0.000	0.000	0.000
38	A	78	GLY	0	-0.025	-0.015	15.048	-0.173	-0.173	0.000	0.000	0.000	0.000
39	A	79	LYS	1	0.901	0.958	9.015	29.906	29.906	0.000	0.000	0.000	0.000
40	A	80	ILE	0	0.000	0.000	14.755	0.592	0.592	0.000	0.000	0.000	0.000
41	A	81	TYR	0	-0.018	0.003	17.583	-0.666	-0.666	0.000	0.000	0.000	0.000
42	A	82	GLU	-1	-0.898	-0.957	19.261	-13.220	-13.220	0.000	0.000	0.000	0.000
43	A	83	LEU	0	-0.038	-0.023	22.717	0.110	0.110	0.000	0.000	0.000	0.000
44	A	84	THR	0	0.001	0.001	24.937	0.262	0.262	0.000	0.000	0.000	0.000
45	A	85	VAL	0	-0.020	-0.001	28.689	0.186	0.186	0.000	0.000	0.000	0.000
46	A	86	LEU	0	0.001	-0.003	31.159	0.204	0.204	0.000	0.000	0.000	0.000
47	A	87	LYS	1	0.841	0.921	31.489	9.944	9.944	0.000	0.000	0.000	0.000
48	A	88	ASP	-1	-0.853	-0.915	36.760	-7.577	-7.577	0.000	0.000	0.000	0.000
49	A	89	ARG	1	0.938	0.960	38.669	7.841	7.841	0.000	0.000	0.000	0.000
50	A	90	PHE	0	-0.015	0.010	42.346	0.115	0.115	0.000	0.000	0.000	0.000
51	A	91	THR	0	0.025	0.011	44.881	0.065	0.065	0.000	0.000	0.000	0.000
52	A	92	GLY	0	0.035	0.024	42.579	-0.031	-0.031	0.000	0.000	0.000	0.000
53	A	93	MET	0	-0.030	-0.020	37.510	-0.211	-0.211	0.000	0.000	0.000	0.000
54	A	94	HIS	0	0.061	0.017	33.908	-0.003	-0.003	0.000	0.000	0.000	0.000
55	A	95	LYS	1	0.874	0.930	37.523	8.239	8.239	0.000	0.000	0.000	0.000
56	A	96	GLY	0	0.056	0.047	37.231	0.048	0.048	0.000	0.000	0.000	0.000
57	A	97	CYS	0	-0.095	-0.049	33.939	-0.058	-0.058	0.000	0.000	0.000	0.000
58	A	98	ALA	0	-0.017	-0.011	29.405	0.006	0.006	0.000	0.000	0.000	0.000
59	A	99	PHE	0	-0.012	-0.004	29.331	0.105	0.105	0.000	0.000	0.000	0.000
60	A	100	LEU	0	0.013	0.012	22.010	-0.170	-0.170	0.000	0.000	0.000	0.000
61	A	101	THR	0	-0.014	0.005	22.867	0.409	0.409	0.000	0.000	0.000	0.000
62	A	102	TYR	0	-0.017	-0.035	18.424	-0.152	-0.152	0.000	0.000	0.000	0.000
63	A	103	CYS	0	-0.068	-0.039	15.731	0.166	0.166	0.000	0.000	0.000	0.000
64	A	104	GLU	-1	-0.849	-0.919	15.479	-18.411	-18.411	0.000	0.000	0.000	0.000
65	A	105	ARG	1	1.003	0.994	18.669	12.892	12.892	0.000	0.000	0.000	0.000
66	A	106	GLU	-1	-0.868	-0.957	19.717	-13.495	-13.495	0.000	0.000	0.000	0.000
67	A	107	SER	0	-0.052	-0.024	17.577	-0.205	-0.205	0.000	0.000	0.000	0.000
68	A	108	ALA	0	0.016	0.013	19.392	0.309	0.309	0.000	0.000	0.000	0.000
69	A	109	LEU	0	-0.020	-0.003	22.661	0.518	0.518	0.000	0.000	0.000	0.000
70	A	110	LYS	1	0.948	0.977	18.341	16.722	16.722	0.000	0.000	0.000	0.000
71	A	111	ALA	0	0.037	0.017	21.143	0.370	0.370	0.000	0.000	0.000	0.000
72	A	112	GLN	0	0.008	-0.011	22.919	0.724	0.724	0.000	0.000	0.000	0.000
73	A	113	SER	0	-0.006	-0.007	26.380	0.407	0.407	0.000	0.000	0.000	0.000
74	A	114	ALA	0	0.000	0.020	23.568	0.239	0.239	0.000	0.000	0.000	0.000
75	A	115	LEU	0	-0.040	-0.015	23.450	0.014	0.014	0.000	0.000	0.000	0.000
76	A	116	HIS	0	0.067	0.030	27.220	0.223	0.223	0.000	0.000	0.000	0.000
77	A	117	GLU	-1	-0.965	-0.989	30.591	-8.626	-8.626	0.000	0.000	0.000	0.000
78	A	118	GLN	0	-0.062	-0.015	26.169	0.258	0.258	0.000	0.000	0.000	0.000
79	A	119	LYS	1	0.954	0.983	23.689	12.522	12.522	0.000	0.000	0.000	0.000
80	A	120	THR	0	0.023	0.007	30.188	0.240	0.240	0.000	0.000	0.000	0.000
81	A	121	LEU	0	-0.020	0.003	29.923	-0.125	-0.125	0.000	0.000	0.000	0.000
82	A	122	PRO	0	0.036	0.014	32.766	0.264	0.264	0.000	0.000	0.000	0.000
83	A	123	GLY	0	0.007	-0.001	35.741	0.031	0.031	0.000	0.000	0.000	0.000
84	A	124	MET	0	-0.080	-0.024	36.331	0.303	0.303	0.000	0.000	0.000	0.000
85	A	125	ASN	0	-0.001	-0.013	38.350	-0.200	-0.200	0.000	0.000	0.000	0.000
86	A	126	ARG	1	0.937	0.975	38.749	7.492	7.492	0.000	0.000	0.000	0.000
87	A	127	PRO	0	0.054	0.037	33.800	-0.082	-0.082	0.000	0.000	0.000	0.000
88	A	128	ILE	0	-0.033	-0.016	28.749	0.142	0.142	0.000	0.000	0.000	0.000
89	A	129	GLN	0	0.013	0.007	32.538	-0.063	-0.063	0.000	0.000	0.000	0.000
90	A	130	VAL	0	-0.027	-0.023	27.454	-0.089	-0.089	0.000	0.000	0.000	0.000
91	A	131	LYS	1	0.939	0.973	30.854	9.023	9.023	0.000	0.000	0.000	0.000
92	A	132	PRO	0	0.018	0.018	29.940	-0.168	-0.168	0.000	0.000	0.000	0.000
93	A	133	ALA	0	-0.061	-0.040	31.124	0.331	0.331	0.000	0.000	0.000	0.000
94	A	134	ASP	-1	-0.900	-0.942	32.761	-9.396	-9.396	0.000	0.000	0.000	0.000
95	A	135	SER	0	-0.059	-0.037	34.599	0.260	0.260	0.000	0.000	0.000	0.000
96	A	136	GLU	-1	-0.849	-0.907	38.323	-8.090	-8.090	0.000	0.000	0.000	0.000
97	A	137	SER	0	-0.021	-0.017	39.540	0.147	0.147	0.000	0.000	0.000	0.000
98	A	138	ARG	1	0.863	0.922	42.103	7.524	7.524	0.000	0.000	0.000	0.000
99	A	139	GLY	0	0.009	-0.006	45.637	-0.018	-0.018	0.000	0.000	0.000	0.000
100	A	140	GLY	0	0.004	0.006	49.045	0.131	0.131	0.000	0.000	0.000	0.000
101	A	141	SER	0	-0.074	-0.033	50.949	-0.104	-0.104	0.000	0.000	0.000	0.000
102	A	142	GLY	0	0.042	0.017	53.460	0.066	0.066	0.000	0.000	0.000	0.000
103	A	143	PRO	0	-0.012	0.011	55.463	0.033	0.033	0.000	0.000	0.000	0.000
104	A	144	SER	0	-0.005	-0.018	57.927	0.100	0.100	0.000	0.000	0.000	0.000
105	A	145	SER	0	-0.047	-0.035	61.508	-0.001	-0.001	0.000	0.000	0.000	0.000
106	A	146	GLY	-1	-0.915	-0.928	59.827	-5.419	-5.419	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:41:GLY)