FMO DATABASE

FMODB ID: 9LQ12

Calculation Name: 1FYC-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1FYC

Chain ID: A

ChEMBL ID:

UniProt ID: P10515

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

Total energy (hartree)

FMO2-HF: Electronic energy	-694284.495589
FMO2-HF: Nuclear repulsion	652900.36936
FMO2-HF: Total energy	-41384.126229
FMO2-MP2: Total energy	-41502.752712

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:GLY)

Summations of interaction energy for fragment #1(A:1: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.
-119.031	-118.08	-0.005	-0.387	-0.559	-0.001

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.839 / 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	A	3	ASN	0	0.017	0.011	3.807	-3.994	-3.043	-0.005	-0.387	-0.559	-0.001
4	A	4	MET	0	0.055	0.033	6.583	3.566	3.566	0.000	0.000	0.000	0.000
5	A	5	SER	0	-0.038	-0.037	9.155	-0.197	-0.197	0.000	0.000	0.000	0.000
6	A	6	TYR	0	0.006	0.013	12.023	1.177	1.177	0.000	0.000	0.000	0.000
7	A	7	PRO	0	-0.010	0.008	14.764	-0.843	-0.843	0.000	0.000	0.000	0.000
8	A	8	PRO	0	0.064	0.041	15.934	0.644	0.644	0.000	0.000	0.000	0.000
9	A	9	HIS	0	-0.016	-0.038	18.499	0.819	0.819	0.000	0.000	0.000	0.000
10	A	10	MET	0	-0.011	0.035	20.106	0.230	0.230	0.000	0.000	0.000	0.000
11	A	11	GLN	0	0.022	-0.017	24.439	0.711	0.711	0.000	0.000	0.000	0.000
12	A	12	VAL	0	-0.024	0.001	27.569	0.078	0.078	0.000	0.000	0.000	0.000
13	A	13	LEU	0	-0.046	0.010	30.352	0.259	0.259	0.000	0.000	0.000	0.000
14	A	14	LEU	0	0.075	0.030	30.114	-0.363	-0.363	0.000	0.000	0.000	0.000
15	A	15	PRO	0	-0.014	0.004	26.724	0.274	0.274	0.000	0.000	0.000	0.000
16	A	16	ALA	0	0.032	0.017	29.363	-0.100	-0.100	0.000	0.000	0.000	0.000
17	A	17	LEU	0	-0.037	-0.036	30.522	-0.053	-0.053	0.000	0.000	0.000	0.000
18	A	18	SER	0	-0.051	-0.022	32.770	0.252	0.252	0.000	0.000	0.000	0.000
19	A	19	PRO	0	0.046	0.021	35.315	0.065	0.065	0.000	0.000	0.000	0.000
20	A	20	THR	0	-0.064	-0.027	37.352	0.185	0.185	0.000	0.000	0.000	0.000
21	A	21	MET	0	0.031	0.039	40.472	0.268	0.268	0.000	0.000	0.000	0.000
22	A	22	THR	0	-0.019	-0.041	41.130	-0.118	-0.118	0.000	0.000	0.000	0.000
23	A	23	MET	0	-0.033	-0.032	43.040	0.082	0.082	0.000	0.000	0.000	0.000
24	A	24	GLY	0	0.035	0.021	40.115	0.055	0.055	0.000	0.000	0.000	0.000
25	A	25	THR	0	-0.053	-0.051	40.441	0.053	0.053	0.000	0.000	0.000	0.000
26	A	26	VAL	0	0.023	0.011	35.455	-0.124	-0.124	0.000	0.000	0.000	0.000
27	A	27	GLN	0	-0.051	-0.020	37.624	0.072	0.072	0.000	0.000	0.000	0.000
28	A	28	ARG	1	0.971	0.975	36.022	8.628	8.628	0.000	0.000	0.000	0.000
29	A	29	TRP	0	0.003	-0.028	28.360	-0.439	-0.439	0.000	0.000	0.000	0.000
30	A	30	GLU	-1	-0.936	-0.959	33.379	-8.799	-8.799	0.000	0.000	0.000	0.000
31	A	31	LYS	1	0.807	0.951	26.592	11.723	11.723	0.000	0.000	0.000	0.000
32	A	32	LYS	1	0.963	0.978	30.984	10.545	10.545	0.000	0.000	0.000	0.000
33	A	33	VAL	0	0.033	-0.016	30.598	-0.302	-0.302	0.000	0.000	0.000	0.000
34	A	34	GLY	0	-0.001	0.007	28.308	0.026	0.026	0.000	0.000	0.000	0.000
35	A	35	GLU	0	-0.084	-0.060	26.381	0.129	0.129	0.000	0.000	0.000	0.000
36	A	36	LYS	1	0.969	0.963	20.466	14.454	14.454	0.000	0.000	0.000	0.000
37	A	37	LEU	0	-0.088	-0.030	22.083	0.360	0.360	0.000	0.000	0.000	0.000
38	A	38	SER	0	0.022	-0.005	16.754	0.001	0.001	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.942	-0.973	17.448	-16.427	-16.427	0.000	0.000	0.000	0.000
40	A	40	GLY	0	-0.026	0.004	19.687	0.262	0.262	0.000	0.000	0.000	0.000
41	A	41	ASP	-1	-0.803	-0.876	21.974	-11.825	-11.825	0.000	0.000	0.000	0.000
42	A	42	LEU	0	-0.121	-0.044	24.964	0.212	0.212	0.000	0.000	0.000	0.000
43	A	43	LEU	0	0.032	0.024	27.278	-0.303	-0.303	0.000	0.000	0.000	0.000
44	A	44	ALA	0	-0.046	-0.037	28.974	0.380	0.380	0.000	0.000	0.000	0.000
45	A	45	GLU	-1	-0.815	-0.877	31.868	-9.408	-9.408	0.000	0.000	0.000	0.000
46	A	46	ILE	0	-0.060	-0.016	33.785	0.302	0.302	0.000	0.000	0.000	0.000
47	A	47	GLU	-1	-0.780	-0.885	36.442	-7.833	-7.833	0.000	0.000	0.000	0.000
48	A	48	THR	0	-0.047	-0.069	39.494	0.045	0.045	0.000	0.000	0.000	0.000
49	A	49	ASP	-1	-0.877	-0.896	42.832	-6.712	-6.712	0.000	0.000	0.000	0.000
50	A	50	LYS	1	0.795	0.878	42.801	7.353	7.353	0.000	0.000	0.000	0.000
51	A	51	ALA	0	-0.021	-0.003	37.437	-0.092	-0.092	0.000	0.000	0.000	0.000
52	A	52	THR	0	-0.020	-0.035	35.432	0.114	0.114	0.000	0.000	0.000	0.000
53	A	53	ILE	0	-0.060	-0.023	31.363	-0.168	-0.168	0.000	0.000	0.000	0.000
54	A	54	GLY	0	0.115	0.048	30.100	0.160	0.160	0.000	0.000	0.000	0.000
55	A	55	PHE	0	-0.061	-0.037	25.398	-0.361	-0.361	0.000	0.000	0.000	0.000
56	A	56	GLU	-1	-0.930	-0.986	24.450	-12.548	-12.548	0.000	0.000	0.000	0.000
57	A	57	VAL	0	-0.037	-0.003	22.158	-0.473	-0.473	0.000	0.000	0.000	0.000
58	A	58	GLN	0	-0.010	-0.021	18.673	-0.464	-0.464	0.000	0.000	0.000	0.000
59	A	59	GLU	-1	-0.984	-0.978	15.074	-22.129	-22.129	0.000	0.000	0.000	0.000
60	A	60	GLU	-1	-0.835	-0.923	16.877	-18.507	-18.507	0.000	0.000	0.000	0.000
61	A	61	GLY	0	-0.030	-0.049	20.201	0.701	0.701	0.000	0.000	0.000	0.000
62	A	62	TYR	0	-0.030	-0.032	23.046	0.686	0.686	0.000	0.000	0.000	0.000
63	A	63	LEU	0	-0.047	0.008	24.687	0.429	0.429	0.000	0.000	0.000	0.000
64	A	64	ALA	0	0.001	0.012	25.655	0.137	0.137	0.000	0.000	0.000	0.000
65	A	65	LYS	1	0.935	0.956	27.724	10.319	10.319	0.000	0.000	0.000	0.000
66	A	66	ILE	0	0.041	0.004	29.148	0.011	0.011	0.000	0.000	0.000	0.000
67	A	67	LEU	0	-0.026	-0.015	32.457	0.146	0.146	0.000	0.000	0.000	0.000
68	A	68	VAL	0	-0.035	0.006	35.443	0.262	0.262	0.000	0.000	0.000	0.000
69	A	69	PRO	0	0.050	0.017	35.895	-0.271	-0.271	0.000	0.000	0.000	0.000
70	A	70	GLU	-1	-0.938	-0.987	37.438	-8.176	-8.176	0.000	0.000	0.000	0.000
71	A	71	GLY	0	0.047	0.021	38.628	0.145	0.145	0.000	0.000	0.000	0.000
72	A	72	THR	0	-0.019	0.006	39.513	0.248	0.248	0.000	0.000	0.000	0.000
73	A	73	ARG	1	0.890	0.964	40.647	6.878	6.878	0.000	0.000	0.000	0.000
74	A	74	ASP	-1	-0.855	-0.917	39.531	-7.805	-7.805	0.000	0.000	0.000	0.000
75	A	75	VAL	0	-0.023	-0.042	38.752	0.146	0.146	0.000	0.000	0.000	0.000
76	A	76	PRO	0	-0.028	0.011	38.046	-0.163	-0.163	0.000	0.000	0.000	0.000
77	A	77	LEU	0	0.050	0.008	32.957	-0.146	-0.146	0.000	0.000	0.000	0.000
78	A	78	GLY	0	-0.013	-0.010	34.424	-0.180	-0.180	0.000	0.000	0.000	0.000
79	A	79	THR	0	-0.015	-0.004	35.120	0.048	0.048	0.000	0.000	0.000	0.000
80	A	80	PRO	0	-0.011	0.004	33.973	-0.288	-0.288	0.000	0.000	0.000	0.000
81	A	81	LEU	0	0.037	0.002	31.907	0.176	0.176	0.000	0.000	0.000	0.000
82	A	82	CYS	0	-0.078	-0.014	30.884	0.120	0.120	0.000	0.000	0.000	0.000
83	A	83	ILE	0	-0.059	-0.014	26.093	-0.109	-0.109	0.000	0.000	0.000	0.000
84	A	84	ILE	0	-0.015	-0.020	23.362	0.065	0.065	0.000	0.000	0.000	0.000
85	A	85	VAL	0	-0.029	-0.035	20.249	-0.029	-0.029	0.000	0.000	0.000	0.000
86	A	86	GLU	-1	-0.850	-0.897	17.459	-18.574	-18.574	0.000	0.000	0.000	0.000
87	A	87	LYS	1	0.869	0.937	19.702	12.706	12.706	0.000	0.000	0.000	0.000
88	A	88	GLU	-1	-0.865	-0.941	17.586	-16.968	-16.968	0.000	0.000	0.000	0.000
89	A	89	ALA	0	-0.065	-0.025	20.939	0.570	0.570	0.000	0.000	0.000	0.000
90	A	90	ASP	-1	-0.847	-0.914	22.751	-13.878	-13.878	0.000	0.000	0.000	0.000
91	A	91	ILE	0	-0.011	-0.004	24.871	0.348	0.348	0.000	0.000	0.000	0.000
92	A	92	SER	0	-0.021	-0.028	28.156	0.067	0.067	0.000	0.000	0.000	0.000
93	A	93	ALA	0	-0.048	-0.009	30.001	-0.092	-0.092	0.000	0.000	0.000	0.000
94	A	94	PHE	0	-0.024	-0.019	29.683	-0.088	-0.088	0.000	0.000	0.000	0.000
95	A	95	ALA	0	0.046	0.025	31.402	-0.201	-0.201	0.000	0.000	0.000	0.000
96	A	96	ASP	-1	-0.944	-0.952	33.938	-8.769	-8.769	0.000	0.000	0.000	0.000
97	A	97	TYR	0	-0.026	-0.024	28.950	-0.279	-0.279	0.000	0.000	0.000	0.000
98	A	98	ARG	1	0.933	0.969	30.726	9.523	9.523	0.000	0.000	0.000	0.000
99	A	99	PRO	0	0.004	0.006	26.148	0.215	0.215	0.000	0.000	0.000	0.000
100	A	100	THR	0	0.005	-0.010	27.424	0.108	0.108	0.000	0.000	0.000	0.000
101	A	101	GLU	-1	-0.845	-0.911	20.975	-14.711	-14.711	0.000	0.000	0.000	0.000
102	A	102	VAL	0	-0.022	-0.014	17.410	0.069	0.069	0.000	0.000	0.000	0.000
103	A	103	THR	0	-0.075	-0.050	19.401	-0.803	-0.803	0.000	0.000	0.000	0.000
104	A	104	ASP	-1	-0.947	-0.968	20.211	-13.889	-13.889	0.000	0.000	0.000	0.000
105	A	105	LEU	0	-0.100	-0.041	21.980	-0.262	-0.262	0.000	0.000	0.000	0.000
106	A	106	LYS	0	0.026	0.016	21.626	1.625	1.625	0.000	0.000	0.000	0.000

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