FMO DATABASE

FMODB ID: 9L692

Calculation Name: 2GFF-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2GFF

Chain ID: A

ChEMBL ID:

UniProt ID: Q7CG46

Base Structure: X-ray

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	97
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-731007.59281
FMO2-HF: Nuclear repulsion	691835.075982
FMO2-HF: Total energy	-39172.516828
FMO2-MP2: Total energy	-39286.422441

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:MET)

Summations of interaction energy for fragment #1(A: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.
-125.322	-110.291	18.868	-13.057	-20.844	-0.122

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.821 / q_NPA : 0.921

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	VAL	0	0.033	0.014	2.656	1.858	4.042	0.681	-0.763	-2.101	-0.002
4	A	4	THR	0	-0.054	-0.035	4.884	3.023	3.076	-0.001	-0.009	-0.044	0.000
36	A	36	LEU	0	-0.031	-0.012	2.217	-2.249	-1.511	2.981	-0.785	-2.934	-0.006
37	A	37	ARG	1	0.913	0.954	3.241	32.745	33.934	0.246	-0.262	-1.173	-0.002
53	A	53	TYR	0	0.011	0.003	4.632	-1.682	-1.577	-0.001	-0.005	-0.099	0.000
55	A	55	ALA	0	-0.019	-0.018	2.381	-2.546	-2.722	1.768	-0.466	-1.125	0.000
56	A	56	TYR	0	-0.021	-0.024	3.788	4.602	5.111	0.003	-0.112	-0.401	0.000
57	A	57	THR	0	0.055	0.006	2.376	-22.349	-19.209	2.985	-3.013	-3.111	-0.036
58	A	58	ASP	-1	-0.867	-0.935	2.157	-81.626	-79.906	6.795	-4.639	-3.877	-0.052
59	A	59	GLU	-1	-0.880	-0.956	4.265	-26.833	-26.702	-0.001	-0.030	-0.101	0.000
92	A	92	ILE	0	0.025	0.017	4.204	-4.858	-4.729	-0.001	-0.038	-0.090	0.000
93	A	93	GLY	0	-0.022	-0.012	2.287	6.626	7.628	1.782	-1.291	-1.494	0.000
94	A	94	LEU	0	0.005	-0.006	2.815	-11.577	-10.379	0.360	-0.279	-1.279	-0.015
96	A	96	PRO	0	-0.078	-0.052	2.947	0.406	1.642	0.962	-0.479	-1.719	0.000
97	A	97	GLY	-1	-0.902	-0.942	3.551	-47.156	-45.283	0.309	-0.886	-1.296	-0.009
5	A	5	LEU	0	0.031	0.032	8.681	0.427	0.427	0.000	0.000	0.000	0.000
6	A	6	VAL	0	-0.024	-0.025	10.745	0.787	0.787	0.000	0.000	0.000	0.000
7	A	7	GLU	-1	-0.785	-0.851	13.959	-13.131	-13.131	0.000	0.000	0.000	0.000
8	A	8	ILE	0	-0.008	-0.025	17.024	0.171	0.171	0.000	0.000	0.000	0.000
9	A	9	ASN	0	-0.033	-0.009	19.873	0.395	0.395	0.000	0.000	0.000	0.000
10	A	10	VAL	0	0.007	0.013	22.746	0.018	0.018	0.000	0.000	0.000	0.000
11	A	11	LYS	1	0.891	0.932	25.468	9.937	9.937	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.885	-0.956	28.803	-8.972	-8.972	0.000	0.000	0.000	0.000
13	A	13	ASP	-1	-0.877	-0.934	30.368	-8.872	-8.872	0.000	0.000	0.000	0.000
14	A	14	LYS	1	0.830	0.916	28.539	9.034	9.034	0.000	0.000	0.000	0.000
15	A	15	VAL	0	0.029	0.015	24.786	-0.413	-0.413	0.000	0.000	0.000	0.000
16	A	16	ASP	-1	-0.846	-0.919	25.408	-9.923	-9.923	0.000	0.000	0.000	0.000
17	A	17	GLN	0	-0.001	-0.018	26.343	-0.119	-0.119	0.000	0.000	0.000	0.000
18	A	18	PHE	0	0.001	-0.002	18.701	-0.388	-0.388	0.000	0.000	0.000	0.000
19	A	19	ILE	0	-0.004	-0.004	20.851	-0.618	-0.618	0.000	0.000	0.000	0.000
20	A	20	GLU	-1	-0.863	-0.901	21.976	-11.142	-11.142	0.000	0.000	0.000	0.000
21	A	21	VAL	0	-0.009	-0.009	21.157	-0.390	-0.390	0.000	0.000	0.000	0.000
22	A	22	PHE	0	0.023	-0.016	15.506	-0.749	-0.749	0.000	0.000	0.000	0.000
23	A	23	ARG	1	0.851	0.926	17.554	10.741	10.741	0.000	0.000	0.000	0.000
24	A	24	ALA	0	0.005	0.005	18.677	-0.412	-0.412	0.000	0.000	0.000	0.000
25	A	25	ASN	0	0.025	-0.013	15.807	-0.849	-0.849	0.000	0.000	0.000	0.000
26	A	26	HIS	0	-0.037	-0.006	12.681	-0.361	-0.361	0.000	0.000	0.000	0.000
27	A	27	LEU	0	-0.017	-0.009	14.094	-0.665	-0.665	0.000	0.000	0.000	0.000
28	A	28	GLY	0	-0.004	-0.009	16.297	0.000	0.000	0.000	0.000	0.000	0.000
29	A	29	SER	0	0.001	-0.023	11.297	-0.703	-0.703	0.000	0.000	0.000	0.000
30	A	30	ILE	0	-0.034	-0.012	10.291	-1.507	-1.507	0.000	0.000	0.000	0.000
31	A	31	ARG	1	0.902	0.960	11.554	14.816	14.816	0.000	0.000	0.000	0.000
32	A	32	GLU	-1	-0.773	-0.859	11.040	-22.455	-22.455	0.000	0.000	0.000	0.000
33	A	33	ALA	0	0.003	-0.007	10.536	-1.493	-1.493	0.000	0.000	0.000	0.000
34	A	34	GLY	0	0.044	0.027	8.055	-1.054	-1.054	0.000	0.000	0.000	0.000
35	A	35	ASN	0	-0.055	-0.043	6.641	-5.112	-5.112	0.000	0.000	0.000	0.000
38	A	38	PHE	0	0.014	0.017	5.762	-0.650	-0.650	0.000	0.000	0.000	0.000
39	A	39	ASP	-1	-0.832	-0.908	8.172	-21.137	-21.137	0.000	0.000	0.000	0.000
40	A	40	VAL	0	-0.032	-0.022	10.648	-0.171	-0.171	0.000	0.000	0.000	0.000
41	A	41	LEU	0	0.014	0.012	11.585	0.629	0.629	0.000	0.000	0.000	0.000
42	A	42	ARG	1	0.859	0.924	15.495	11.430	11.430	0.000	0.000	0.000	0.000
43	A	43	ASP	-1	-0.814	-0.889	18.399	-12.798	-12.798	0.000	0.000	0.000	0.000
44	A	44	GLU	-1	-0.858	-0.900	20.276	-11.345	-11.345	0.000	0.000	0.000	0.000
45	A	45	HIS	0	-0.070	-0.054	22.051	0.708	0.708	0.000	0.000	0.000	0.000
46	A	46	ILE	0	-0.049	-0.025	23.620	0.385	0.385	0.000	0.000	0.000	0.000
47	A	47	PRO	0	0.001	-0.013	23.987	-0.383	-0.383	0.000	0.000	0.000	0.000
48	A	48	THR	0	0.041	0.022	25.032	-0.255	-0.255	0.000	0.000	0.000	0.000
49	A	49	ARG	1	0.844	0.936	20.030	12.200	12.200	0.000	0.000	0.000	0.000
50	A	50	PHE	0	0.029	0.003	17.948	0.028	0.028	0.000	0.000	0.000	0.000
51	A	51	TYR	0	-0.029	-0.052	13.964	-0.240	-0.240	0.000	0.000	0.000	0.000
52	A	52	ILE	0	-0.017	0.002	11.411	0.080	0.080	0.000	0.000	0.000	0.000
54	A	54	GLU	-1	-0.803	-0.871	7.490	-23.631	-23.631	0.000	0.000	0.000	0.000
60	A	60	ALA	0	0.005	0.018	7.649	4.289	4.289	0.000	0.000	0.000	0.000
61	A	61	ALA	0	0.026	0.019	6.715	3.419	3.419	0.000	0.000	0.000	0.000
62	A	62	VAL	0	-0.034	-0.008	7.011	3.377	3.377	0.000	0.000	0.000	0.000
63	A	63	ALA	0	-0.020	-0.015	9.556	2.838	2.838	0.000	0.000	0.000	0.000
64	A	64	ILE	0	0.027	0.011	11.511	1.825	1.825	0.000	0.000	0.000	0.000
65	A	65	HIS	1	0.829	0.902	11.362	24.655	24.655	0.000	0.000	0.000	0.000
66	A	66	LYS	1	0.867	0.941	12.851	24.509	24.509	0.000	0.000	0.000	0.000
67	A	67	THR	0	-0.054	-0.029	15.887	1.306	1.306	0.000	0.000	0.000	0.000
68	A	68	THR	0	-0.030	-0.013	15.593	1.185	1.185	0.000	0.000	0.000	0.000
69	A	69	PRO	0	0.028	0.000	18.506	0.235	0.235	0.000	0.000	0.000	0.000
70	A	70	HIS	0	-0.001	0.002	14.564	1.553	1.553	0.000	0.000	0.000	0.000
71	A	71	TYR	0	0.000	0.011	15.393	-0.068	-0.068	0.000	0.000	0.000	0.000
72	A	72	LEU	0	-0.002	-0.005	17.986	0.449	0.449	0.000	0.000	0.000	0.000
73	A	73	GLN	0	0.014	-0.009	21.499	0.704	0.704	0.000	0.000	0.000	0.000
74	A	74	CYS	0	-0.031	0.001	19.170	0.264	0.264	0.000	0.000	0.000	0.000
75	A	75	VAL	0	-0.077	-0.033	19.644	0.199	0.199	0.000	0.000	0.000	0.000
76	A	76	GLU	-1	-0.945	-0.966	22.046	-10.895	-10.895	0.000	0.000	0.000	0.000
77	A	77	GLN	0	-0.007	-0.017	24.732	0.316	0.316	0.000	0.000	0.000	0.000
78	A	78	LEU	0	0.023	0.008	20.064	0.242	0.242	0.000	0.000	0.000	0.000
79	A	79	ALA	0	-0.008	0.008	24.134	0.195	0.195	0.000	0.000	0.000	0.000
80	A	80	PRO	0	0.000	0.000	26.235	0.186	0.186	0.000	0.000	0.000	0.000
81	A	81	LEU	0	0.007	0.008	24.812	0.347	0.347	0.000	0.000	0.000	0.000
82	A	82	MET	0	-0.020	0.016	22.906	-0.334	-0.334	0.000	0.000	0.000	0.000
83	A	83	THR	0	-0.012	-0.016	26.155	0.267	0.267	0.000	0.000	0.000	0.000
84	A	84	GLY	0	0.012	0.007	26.304	0.327	0.327	0.000	0.000	0.000	0.000
85	A	85	PRO	0	-0.015	-0.001	23.548	-0.242	-0.242	0.000	0.000	0.000	0.000
86	A	86	ARG	1	0.930	0.966	18.072	14.824	14.824	0.000	0.000	0.000	0.000
87	A	87	LYS	1	0.846	0.914	18.548	13.147	13.147	0.000	0.000	0.000	0.000
88	A	88	LYS	1	0.929	0.958	12.938	19.939	19.939	0.000	0.000	0.000	0.000
89	A	89	THR	0	0.012	0.024	12.049	0.814	0.814	0.000	0.000	0.000	0.000
90	A	90	VAL	0	-0.020	-0.017	8.806	-0.685	-0.685	0.000	0.000	0.000	0.000
91	A	91	PHE	0	0.013	-0.007	6.447	2.501	2.501	0.000	0.000	0.000	0.000
95	A	95	MET	0	-0.003	0.013	5.120	2.758	2.758	0.000	0.000	0.000	0.000

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