FMO DATABASE

FMODB ID: Q59JY

Calculation Name: 2F76-X-Other549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2F76

Chain ID: X

ChEMBL ID:

UniProt ID: P07567

Base Structure: SolutionNMR

Registration Date: 2025-10-11

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	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	100
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-787727.502723
FMO2-HF: Nuclear repulsion	745839.325378
FMO2-HF: Total energy	-41888.177344
FMO2-MP2: Total energy	-42010.218951

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(X:1:MET)

Summations of interaction energy for fragment #1(X:1:MET)

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.
-25.769	-20.214	1.933	-3.717	-3.772	-0.045

Interaction energy analysis for fragmet #1(X:1:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.828 / q_NPA : 0.904

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	X	3	GLN	0	-0.012	0.004	3.069	9.399	11.414	0.015	-0.787	-1.243	-0.001
4	X	4	GLU	-1	-0.906	-0.962	2.160	-71.573	-68.189	1.920	-2.925	-2.380	-0.044
5	X	5	LEU	0	0.006	0.012	4.599	3.773	3.895	-0.001	-0.004	-0.117	0.000
9	X	9	GLU	-1	-0.797	-0.866	4.826	-50.162	-50.128	-0.001	-0.001	-0.032	0.000
6	X	6	SER	0	-0.053	-0.060	5.476	3.556	3.556	0.000	0.000	0.000	0.000
7	X	7	GLN	0	0.001	-0.020	7.387	2.678	2.678	0.000	0.000	0.000	0.000
8	X	8	HIS	0	0.040	0.016	8.153	2.346	2.346	0.000	0.000	0.000	0.000
10	X	10	ARG	1	0.955	0.977	9.394	25.797	25.797	0.000	0.000	0.000	0.000
11	X	11	TYR	0	0.032	0.027	12.653	1.882	1.882	0.000	0.000	0.000	0.000
12	X	12	VAL	0	0.010	0.006	10.689	1.598	1.598	0.000	0.000	0.000	0.000
13	X	13	GLU	-1	-0.765	-0.895	12.657	-20.100	-20.100	0.000	0.000	0.000	0.000
14	X	14	GLN	0	-0.018	0.008	15.092	1.286	1.286	0.000	0.000	0.000	0.000
15	X	15	LEU	0	0.007	0.009	15.737	1.148	1.148	0.000	0.000	0.000	0.000
16	X	16	LYS	1	0.801	0.886	14.742	20.859	20.859	0.000	0.000	0.000	0.000
17	X	17	GLN	0	-0.064	-0.032	18.154	1.363	1.363	0.000	0.000	0.000	0.000
18	X	18	ALA	0	0.051	0.025	21.127	0.725	0.725	0.000	0.000	0.000	0.000
19	X	19	LEU	0	0.017	0.000	19.422	0.653	0.653	0.000	0.000	0.000	0.000
20	X	20	LYS	1	0.930	0.980	20.201	15.474	15.474	0.000	0.000	0.000	0.000
21	X	21	THR	0	-0.076	-0.035	23.955	0.596	0.596	0.000	0.000	0.000	0.000
22	X	22	ARG	1	0.805	0.892	26.059	11.105	11.105	0.000	0.000	0.000	0.000
23	X	23	GLY	0	0.019	0.019	26.943	0.236	0.236	0.000	0.000	0.000	0.000
24	X	24	VAL	0	-0.066	-0.024	20.907	-0.038	-0.038	0.000	0.000	0.000	0.000
25	X	25	LYS	1	0.899	0.935	22.257	11.288	11.288	0.000	0.000	0.000	0.000
26	X	26	VAL	0	0.028	0.029	16.253	0.057	0.057	0.000	0.000	0.000	0.000
27	X	27	LYS	1	0.921	0.967	14.464	17.110	17.110	0.000	0.000	0.000	0.000
28	X	28	TYR	0	0.048	0.006	7.255	0.891	0.891	0.000	0.000	0.000	0.000
29	X	29	ALA	0	0.033	0.023	9.453	-1.169	-1.169	0.000	0.000	0.000	0.000
30	X	30	ASP	-1	-0.816	-0.921	10.110	-21.446	-21.446	0.000	0.000	0.000	0.000
31	X	31	LEU	0	-0.001	-0.006	12.473	-0.080	-0.080	0.000	0.000	0.000	0.000
32	X	32	LEU	0	-0.009	0.001	5.395	0.566	0.566	0.000	0.000	0.000	0.000
33	X	33	LYS	1	0.952	0.979	7.242	28.133	28.133	0.000	0.000	0.000	0.000
34	X	34	PHE	0	0.033	0.019	9.029	0.328	0.328	0.000	0.000	0.000	0.000
35	X	35	PHE	0	-0.019	-0.020	10.400	1.042	1.042	0.000	0.000	0.000	0.000
36	X	36	ASP	-1	-0.876	-0.926	5.284	-43.289	-43.289	0.000	0.000	0.000	0.000
37	X	37	PHE	0	0.017	0.007	8.527	0.765	0.765	0.000	0.000	0.000	0.000
38	X	38	VAL	0	-0.024	0.003	10.359	1.277	1.277	0.000	0.000	0.000	0.000
39	X	39	LYS	1	0.966	0.982	7.569	34.992	34.992	0.000	0.000	0.000	0.000
40	X	40	ASP	-1	-0.862	-0.936	6.737	-32.208	-32.208	0.000	0.000	0.000	0.000
41	X	41	THR	0	-0.050	-0.029	9.568	1.729	1.729	0.000	0.000	0.000	0.000
42	X	42	CYS	0	-0.071	-0.029	13.221	2.090	2.090	0.000	0.000	0.000	0.000
43	X	43	PRO	0	0.004	0.026	13.129	-0.560	-0.560	0.000	0.000	0.000	0.000
44	X	44	TRP	0	-0.033	-0.028	14.391	0.180	0.180	0.000	0.000	0.000	0.000
45	X	45	PHE	0	-0.017	-0.022	16.239	-0.501	-0.501	0.000	0.000	0.000	0.000
46	X	46	PRO	0	-0.029	-0.012	19.232	0.434	0.434	0.000	0.000	0.000	0.000
47	X	47	GLN	0	-0.034	-0.013	22.037	0.167	0.167	0.000	0.000	0.000	0.000
48	X	48	GLU	-1	-0.847	-0.906	24.917	-10.548	-10.548	0.000	0.000	0.000	0.000
49	X	49	GLY	0	0.038	0.021	28.277	-0.152	-0.152	0.000	0.000	0.000	0.000
50	X	50	THR	0	-0.042	-0.008	30.015	0.132	0.132	0.000	0.000	0.000	0.000
51	X	51	ILE	0	0.017	-0.010	25.441	-0.444	-0.444	0.000	0.000	0.000	0.000
52	X	52	ASP	-1	-0.740	-0.860	22.037	-14.584	-14.584	0.000	0.000	0.000	0.000
53	X	53	ILE	0	-0.002	-0.013	20.201	-0.414	-0.414	0.000	0.000	0.000	0.000
54	X	54	LYS	1	0.938	0.972	21.924	10.357	10.357	0.000	0.000	0.000	0.000
55	X	55	ARG	1	0.814	0.879	22.857	11.717	11.717	0.000	0.000	0.000	0.000
56	X	56	TRP	0	-0.001	0.006	14.284	0.351	0.351	0.000	0.000	0.000	0.000
57	X	57	ARG	1	0.944	0.966	18.498	15.265	15.265	0.000	0.000	0.000	0.000
58	X	58	ARG	1	0.952	0.991	20.292	11.865	11.865	0.000	0.000	0.000	0.000
59	X	59	VAL	0	0.030	0.015	16.601	0.389	0.389	0.000	0.000	0.000	0.000
60	X	60	GLY	0	0.010	0.003	16.476	-0.179	-0.179	0.000	0.000	0.000	0.000
61	X	61	ASP	-1	-0.879	-0.960	17.488	-13.945	-13.945	0.000	0.000	0.000	0.000
62	X	62	CYS	0	-0.085	-0.039	20.646	0.548	0.548	0.000	0.000	0.000	0.000
63	X	63	PHE	0	0.012	-0.003	15.831	0.398	0.398	0.000	0.000	0.000	0.000
64	X	64	GLN	0	-0.021	-0.020	17.231	0.588	0.588	0.000	0.000	0.000	0.000
65	X	65	ASP	-1	-0.925	-0.940	18.156	-11.767	-11.767	0.000	0.000	0.000	0.000
66	X	66	TYR	0	0.031	0.022	19.529	0.168	0.168	0.000	0.000	0.000	0.000
67	X	67	TYR	0	-0.032	-0.020	11.912	0.029	0.029	0.000	0.000	0.000	0.000
68	X	68	ASN	0	-0.021	-0.022	17.245	-0.668	-0.668	0.000	0.000	0.000	0.000
69	X	69	THR	0	-0.053	-0.039	19.492	0.223	0.223	0.000	0.000	0.000	0.000
70	X	70	PHE	0	-0.045	-0.021	18.020	0.340	0.340	0.000	0.000	0.000	0.000
71	X	71	GLY	0	0.017	0.028	17.982	0.023	0.023	0.000	0.000	0.000	0.000
72	X	72	PRO	0	-0.058	-0.041	12.703	-0.657	-0.657	0.000	0.000	0.000	0.000
73	X	73	GLU	-1	-0.886	-0.935	14.225	-17.182	-17.182	0.000	0.000	0.000	0.000
74	X	74	LYS	1	0.704	0.847	6.018	32.543	32.543	0.000	0.000	0.000	0.000
75	X	75	VAL	0	0.008	0.004	11.965	-1.261	-1.261	0.000	0.000	0.000	0.000
76	X	76	PRO	0	0.067	0.040	14.463	1.215	1.215	0.000	0.000	0.000	0.000
77	X	77	VAL	0	0.087	0.039	17.615	-0.005	-0.005	0.000	0.000	0.000	0.000
78	X	78	THR	0	-0.030	-0.011	20.044	0.233	0.233	0.000	0.000	0.000	0.000
79	X	79	ALA	0	-0.003	-0.005	18.024	0.356	0.356	0.000	0.000	0.000	0.000
80	X	80	PHE	0	0.046	0.024	20.133	0.206	0.206	0.000	0.000	0.000	0.000
81	X	81	SER	0	-0.018	-0.010	23.364	0.487	0.487	0.000	0.000	0.000	0.000
82	X	82	TYR	0	0.033	-0.017	20.854	0.179	0.179	0.000	0.000	0.000	0.000
83	X	83	TRP	0	0.042	0.017	22.394	0.087	0.087	0.000	0.000	0.000	0.000
84	X	84	ASN	0	0.006	-0.002	23.881	0.287	0.287	0.000	0.000	0.000	0.000
85	X	85	LEU	0	-0.003	0.002	25.717	0.229	0.229	0.000	0.000	0.000	0.000
86	X	86	ILE	0	-0.011	-0.010	20.974	0.024	0.024	0.000	0.000	0.000	0.000
87	X	87	LYS	1	0.882	0.971	25.346	11.205	11.205	0.000	0.000	0.000	0.000
88	X	88	GLU	-1	-0.740	-0.858	28.168	-9.572	-9.572	0.000	0.000	0.000	0.000
89	X	89	LEU	0	-0.072	-0.027	24.608	0.184	0.184	0.000	0.000	0.000	0.000
90	X	90	ILE	0	-0.022	-0.017	23.996	-0.070	-0.070	0.000	0.000	0.000	0.000
91	X	91	ASP	-1	-0.829	-0.928	28.448	-9.944	-9.944	0.000	0.000	0.000	0.000
92	X	92	LYS	1	0.885	0.929	31.842	9.517	9.517	0.000	0.000	0.000	0.000
93	X	93	LYS	1	0.908	0.961	26.005	12.046	12.046	0.000	0.000	0.000	0.000
94	X	94	GLU	-1	-0.914	-0.946	30.128	-10.332	-10.332	0.000	0.000	0.000	0.000
95	X	95	VAL	0	-0.075	-0.030	33.475	0.355	0.355	0.000	0.000	0.000	0.000
96	X	96	ASN	0	-0.046	-0.025	35.886	-0.137	-0.137	0.000	0.000	0.000	0.000
97	X	97	PRO	0	0.059	0.032	34.661	-0.114	-0.114	0.000	0.000	0.000	0.000
98	X	98	GLN	0	-0.054	-0.025	33.403	0.248	0.248	0.000	0.000	0.000	0.000
99	X	99	VAL	0	-0.047	-0.030	33.173	-0.252	-0.252	0.000	0.000	0.000	0.000
100	X	100	MET	-1	-0.937	-0.950	30.689	-9.733	-9.733	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(X:1:MET)