FMO DATABASE

FMODB ID: N6K8Q

Calculation Name: 1AC6-A-Xray549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1AC6

Chain ID: A

ChEMBL ID:

UniProt ID: P06323

Base Structure: X-ray

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	109
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-843792.415312
FMO2-HF: Nuclear repulsion	801524.269572
FMO2-HF: Total energy	-42268.14574
FMO2-MP2: Total energy	-42392.542227

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:ASP)

Summations of interaction energy for fragment #1(A:1:ASP)

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.
-47.633	-38.626	12.687	-9.538	-12.159	0.015

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.073 / q_NPA : -0.060

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	0.047	0.011	3.843	1.959	3.856	-0.024	-0.861	-1.013	0.000
25	A	25	SER	0	-0.005	0.004	4.475	1.198	1.574	-0.001	-0.148	-0.227	0.000
26	A	26	ALA	0	0.023	-0.004	2.130	-17.914	-15.947	11.056	-7.457	-5.567	-0.012
27	A	27	SER	0	-0.003	0.011	2.650	-9.627	-9.171	0.462	0.778	-1.697	0.016
28	A	28	GLY	0	-0.011	-0.001	4.746	3.225	3.361	-0.001	-0.013	-0.122	0.000
30	A	30	PRO	0	0.008	0.023	4.605	-0.109	0.020	-0.001	-0.008	-0.120	0.000
90	A	91	LEU	0	0.004	0.008	2.419	-0.790	0.531	0.739	-0.721	-1.339	0.002
92	A	93	GLY	0	0.075	0.021	3.518	-1.119	-0.810	0.026	-0.152	-0.183	0.001
93	A	96	GLY	0	0.012	0.013	3.182	-2.301	-0.769	0.355	-0.634	-1.253	0.005
94	A	97	ASN	0	-0.024	-0.027	3.651	-6.054	-5.716	0.062	-0.173	-0.227	0.003
96	A	99	LYS	1	0.941	0.990	3.964	-2.174	-2.058	-0.001	-0.012	-0.103	0.000
98	A	101	THR	0	-0.050	-0.023	3.600	-2.697	-2.267	0.015	-0.137	-0.308	0.000
4	A	4	THR	0	0.005	0.010	7.051	-0.238	-0.238	0.000	0.000	0.000	0.000
5	A	5	GLN	0	0.000	-0.026	10.455	0.354	0.354	0.000	0.000	0.000	0.000
6	A	6	THR	0	0.017	0.010	13.810	-0.129	-0.129	0.000	0.000	0.000	0.000
7	A	7	GLU	-1	-0.900	-0.913	16.917	-1.880	-1.880	0.000	0.000	0.000	0.000
8	A	8	GLY	0	0.006	0.005	18.355	0.158	0.158	0.000	0.000	0.000	0.000
9	A	9	GLN	0	-0.036	-0.034	21.515	0.051	0.051	0.000	0.000	0.000	0.000
10	A	10	VAL	0	-0.006	0.007	22.193	-0.014	-0.014	0.000	0.000	0.000	0.000
11	A	11	ALA	0	-0.034	-0.026	24.852	0.029	0.029	0.000	0.000	0.000	0.000
12	A	12	LEU	0	-0.021	-0.009	26.550	-0.009	-0.009	0.000	0.000	0.000	0.000
13	A	13	SER	0	-0.028	-0.016	30.256	-0.007	-0.007	0.000	0.000	0.000	0.000
14	A	14	GLU	-1	-0.862	-0.945	32.185	-0.102	-0.102	0.000	0.000	0.000	0.000
15	A	15	GLU	-1	-0.953	-0.981	33.510	-0.036	-0.036	0.000	0.000	0.000	0.000
16	A	16	ASP	-1	-0.863	-0.909	30.623	-0.215	-0.215	0.000	0.000	0.000	0.000
17	A	17	PHE	0	-0.051	-0.022	25.492	0.031	0.031	0.000	0.000	0.000	0.000
18	A	18	LEU	0	-0.022	-0.008	22.500	-0.053	-0.053	0.000	0.000	0.000	0.000
19	A	19	THR	0	-0.010	-0.028	21.059	0.067	0.067	0.000	0.000	0.000	0.000
20	A	20	ILE	0	-0.025	-0.002	17.006	-0.094	-0.094	0.000	0.000	0.000	0.000
21	A	21	HIS	0	-0.009	-0.012	16.446	0.090	0.090	0.000	0.000	0.000	0.000
22	A	22	CYS	0	-0.046	-0.023	10.858	0.136	0.136	0.000	0.000	0.000	0.000
23	A	23	ASN	0	-0.015	0.001	10.315	0.531	0.531	0.000	0.000	0.000	0.000
24	A	24	TYR	0	-0.008	-0.001	5.671	-0.503	-0.503	0.000	0.000	0.000	0.000
29	A	29	TYR	0	-0.014	0.000	7.657	-1.544	-1.544	0.000	0.000	0.000	0.000
31	A	31	ALA	0	0.002	0.008	6.651	-2.307	-2.307	0.000	0.000	0.000	0.000
32	A	32	LEU	0	-0.001	0.007	7.588	0.543	0.543	0.000	0.000	0.000	0.000
33	A	33	PHE	0	-0.001	-0.027	9.435	-0.003	-0.003	0.000	0.000	0.000	0.000
34	A	34	TRP	0	0.029	0.019	11.917	-0.401	-0.401	0.000	0.000	0.000	0.000
35	A	35	TYR	0	-0.025	-0.018	12.554	0.173	0.173	0.000	0.000	0.000	0.000
36	A	36	VAL	0	0.040	0.025	16.166	-0.158	-0.158	0.000	0.000	0.000	0.000
37	A	37	GLN	0	-0.021	-0.009	19.364	-0.041	-0.041	0.000	0.000	0.000	0.000
38	A	38	TYR	0	0.042	0.038	21.153	-0.052	-0.052	0.000	0.000	0.000	0.000
39	A	39	PRO	0	-0.007	-0.023	24.895	-0.028	-0.028	0.000	0.000	0.000	0.000
40	A	40	GLY	0	0.008	0.013	26.352	0.038	0.038	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.860	-0.910	23.934	-0.029	-0.029	0.000	0.000	0.000	0.000
42	A	42	GLY	0	0.002	0.006	21.003	-0.095	-0.095	0.000	0.000	0.000	0.000
43	A	43	PRO	0	-0.039	-0.031	16.265	0.062	0.062	0.000	0.000	0.000	0.000
44	A	44	GLN	0	0.040	0.031	18.358	0.192	0.192	0.000	0.000	0.000	0.000
45	A	45	PHE	0	-0.017	-0.012	15.413	-0.006	-0.006	0.000	0.000	0.000	0.000
46	A	46	LEU	0	-0.025	0.007	17.369	-0.035	-0.035	0.000	0.000	0.000	0.000
47	A	47	PHE	0	-0.013	-0.016	16.114	0.053	0.053	0.000	0.000	0.000	0.000
48	A	48	ARG	1	0.911	0.958	11.716	-3.020	-3.020	0.000	0.000	0.000	0.000
49	A	49	ALA	0	0.028	0.028	13.648	-0.200	-0.200	0.000	0.000	0.000	0.000
50	A	50	SER	0	-0.169	-0.123	12.832	0.483	0.483	0.000	0.000	0.000	0.000
51	A	51	ARG	1	0.941	0.969	12.633	-1.468	-1.468	0.000	0.000	0.000	0.000
52	A	52	ASP	-1	-0.744	-0.905	14.386	1.328	1.328	0.000	0.000	0.000	0.000
53	A	53	LYS	1	0.783	0.869	15.466	-1.243	-1.243	0.000	0.000	0.000	0.000
54	A	54	GLU	-1	-0.801	-0.850	16.814	1.822	1.822	0.000	0.000	0.000	0.000
55	A	55	LYS	1	0.842	0.903	17.475	-0.443	-0.443	0.000	0.000	0.000	0.000
56	A	56	GLY	0	0.023	0.029	17.573	0.039	0.039	0.000	0.000	0.000	0.000
57	A	57	SER	0	-0.010	-0.024	18.552	-0.150	-0.150	0.000	0.000	0.000	0.000
58	A	58	SER	0	-0.005	-0.007	21.475	0.040	0.040	0.000	0.000	0.000	0.000
59	A	59	ARG	1	0.855	0.920	22.115	-0.286	-0.286	0.000	0.000	0.000	0.000
60	A	60	GLY	0	0.034	0.022	26.031	-0.051	-0.051	0.000	0.000	0.000	0.000
61	A	61	PHE	0	0.019	0.013	21.323	-0.026	-0.026	0.000	0.000	0.000	0.000
62	A	62	GLU	-1	-0.851	-0.931	20.618	0.452	0.452	0.000	0.000	0.000	0.000
63	A	63	ALA	0	0.021	0.023	16.115	-0.125	-0.125	0.000	0.000	0.000	0.000
64	A	64	THR	0	-0.033	-0.018	17.667	0.169	0.169	0.000	0.000	0.000	0.000
65	A	65	TYR	0	-0.080	-0.043	9.502	-0.279	-0.279	0.000	0.000	0.000	0.000
66	A	66	ASN	0	0.029	0.021	13.904	0.060	0.060	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.976	0.981	10.264	-2.885	-2.885	0.000	0.000	0.000	0.000
68	A	68	GLU	-1	-0.862	-0.919	12.844	0.852	0.852	0.000	0.000	0.000	0.000
69	A	69	ALA	0	-0.002	0.000	14.595	-0.178	-0.178	0.000	0.000	0.000	0.000
70	A	70	THR	0	-0.050	-0.021	8.858	-0.260	-0.260	0.000	0.000	0.000	0.000
71	A	71	SER	0	-0.005	-0.005	10.241	-0.525	-0.525	0.000	0.000	0.000	0.000
72	A	72	PHE	0	0.017	-0.023	11.597	0.512	0.512	0.000	0.000	0.000	0.000
73	A	73	HIS	0	0.046	0.036	13.523	-0.153	-0.153	0.000	0.000	0.000	0.000
74	A	74	LEU	0	-0.007	0.019	16.549	0.179	0.179	0.000	0.000	0.000	0.000
75	A	75	GLN	0	0.018	-0.002	18.402	-0.157	-0.157	0.000	0.000	0.000	0.000
76	A	76	LYS	1	0.850	0.911	22.200	0.052	0.052	0.000	0.000	0.000	0.000
77	A	77	ALA	0	-0.025	-0.001	25.362	-0.039	-0.039	0.000	0.000	0.000	0.000
78	A	78	SER	0	0.036	0.029	28.789	-0.010	-0.010	0.000	0.000	0.000	0.000
79	A	79	VAL	0	-0.056	-0.012	26.882	0.026	0.026	0.000	0.000	0.000	0.000
80	A	80	GLN	0	0.078	0.051	29.581	-0.017	-0.017	0.000	0.000	0.000	0.000
81	A	81	GLU	-1	-0.805	-0.921	30.326	-0.226	-0.226	0.000	0.000	0.000	0.000
82	A	82	SER	0	-0.109	-0.073	30.672	-0.021	-0.021	0.000	0.000	0.000	0.000
83	A	83	ASP	-1	-0.825	-0.903	26.154	-0.031	-0.031	0.000	0.000	0.000	0.000
84	A	84	SER	0	0.001	0.010	25.518	-0.055	-0.055	0.000	0.000	0.000	0.000
85	A	85	ALA	0	-0.030	-0.011	22.991	0.018	0.018	0.000	0.000	0.000	0.000
86	A	86	VAL	0	-0.034	-0.010	18.166	-0.064	-0.064	0.000	0.000	0.000	0.000
87	A	87	TYR	0	-0.016	-0.025	17.860	0.115	0.115	0.000	0.000	0.000	0.000
88	A	88	TYR	0	-0.034	-0.027	12.895	-0.228	-0.228	0.000	0.000	0.000	0.000
89	A	90	ALA	0	0.013	-0.013	8.299	-0.565	-0.565	0.000	0.000	0.000	0.000
91	A	92	SER	0	-0.026	-0.005	5.890	0.026	0.026	0.000	0.000	0.000	0.000
95	A	98	ASN	0	-0.013	-0.004	6.974	-1.699	-1.699	0.000	0.000	0.000	0.000
97	A	100	LEU	0	-0.011	-0.001	6.174	1.736	1.736	0.000	0.000	0.000	0.000
99	A	102	PHE	0	0.025	-0.001	5.997	0.821	0.821	0.000	0.000	0.000	0.000
100	A	103	GLY	0	0.021	0.019	8.480	-1.293	-1.293	0.000	0.000	0.000	0.000
101	A	104	ALA	0	-0.027	-0.033	10.273	0.321	0.321	0.000	0.000	0.000	0.000
102	A	105	GLY	0	0.007	0.015	13.628	0.231	0.231	0.000	0.000	0.000	0.000
103	A	106	THR	0	-0.038	-0.031	15.792	-0.103	-0.103	0.000	0.000	0.000	0.000
104	A	107	LYS	1	0.925	0.967	18.746	0.730	0.730	0.000	0.000	0.000	0.000
105	A	108	LEU	0	-0.006	0.009	22.259	-0.014	-0.014	0.000	0.000	0.000	0.000
106	A	109	THR	0	-0.056	-0.048	24.074	0.026	0.026	0.000	0.000	0.000	0.000
107	A	110	ILE	0	-0.023	0.001	27.816	-0.014	-0.014	0.000	0.000	0.000	0.000
108	A	111	LYS	1	0.913	0.958	30.605	0.218	0.218	0.000	0.000	0.000	0.000
109	A	112	PRO	-1	-0.875	-0.919	34.396	-0.187	-0.187	0.000	0.000	0.000	0.000

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