FMO DATABASE

FMODB ID: 4644N

Calculation Name: 1A1X-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1A1X

Chain ID: A

ChEMBL ID:

UniProt ID: P56278

Base Structure: X-ray

Registration Date: 2025-10-05

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	-879822.036544
FMO2-HF: Nuclear repulsion	836285.096792
FMO2-HF: Total energy	-43536.939752
FMO2-MP2: Total energy	-43664.753151

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:3:ALA)

Summations of interaction energy for fragment #1(A:3:ALA)

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.
-151.08	-147.431	1.023	-1.811	-2.86	-0.014

Interaction energy analysis for fragmet #1(A:3:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.858 / q_NPA : 0.915

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	5	GLU	-1	-0.842	-0.930	2.117	-54.448	-51.361	1.026	-1.725	-2.387	-0.014
4	A	6	ASP	-1	-0.910	-0.950	3.949	-36.545	-36.340	-0.001	-0.020	-0.185	0.000
5	A	7	VAL	0	-0.094	-0.040	4.294	4.914	4.995	-0.001	-0.007	-0.072	0.000
89	A	91	HIS	1	0.865	0.928	4.566	45.966	46.028	-0.001	-0.005	-0.056	0.000
90	A	92	LEU	0	-0.034	-0.008	4.050	-15.086	-14.872	0.000	-0.054	-0.160	0.000
6	A	8	GLY	0	0.013	0.015	6.730	3.860	3.860	0.000	0.000	0.000	0.000
7	A	9	ALA	0	-0.005	-0.014	7.070	-4.494	-4.494	0.000	0.000	0.000	0.000
8	A	10	PRO	0	-0.033	-0.005	8.012	0.468	0.468	0.000	0.000	0.000	0.000
9	A	11	PRO	0	-0.017	0.003	10.397	1.016	1.016	0.000	0.000	0.000	0.000
10	A	12	ASP	-1	-0.829	-0.893	14.285	-16.711	-16.711	0.000	0.000	0.000	0.000
11	A	13	HIS	0	-0.072	-0.061	16.627	0.750	0.750	0.000	0.000	0.000	0.000
12	A	14	LEU	0	-0.020	-0.007	15.515	-0.204	-0.204	0.000	0.000	0.000	0.000
13	A	15	TRP	0	0.016	0.012	19.625	0.524	0.524	0.000	0.000	0.000	0.000
14	A	16	VAL	0	-0.007	0.005	23.455	-0.161	-0.161	0.000	0.000	0.000	0.000
15	A	17	HIS	0	-0.074	-0.040	25.188	0.134	0.134	0.000	0.000	0.000	0.000
16	A	18	GLN	0	-0.024	-0.038	26.900	0.512	0.512	0.000	0.000	0.000	0.000
17	A	19	GLU	-1	-0.805	-0.884	26.613	-12.267	-12.267	0.000	0.000	0.000	0.000
18	A	20	GLY	0	0.030	0.035	23.498	0.028	0.028	0.000	0.000	0.000	0.000
19	A	21	ILE	0	-0.062	-0.025	22.722	-0.655	-0.655	0.000	0.000	0.000	0.000
20	A	22	TYR	0	0.036	-0.016	20.280	0.287	0.287	0.000	0.000	0.000	0.000
21	A	23	ARG	1	0.879	0.934	21.715	11.795	11.795	0.000	0.000	0.000	0.000
22	A	24	ASP	-1	-0.703	-0.813	17.306	-17.492	-17.492	0.000	0.000	0.000	0.000
23	A	25	GLU	-1	-0.766	-0.884	16.884	-17.453	-17.453	0.000	0.000	0.000	0.000
24	A	26	TYR	0	-0.106	-0.048	16.508	0.923	0.923	0.000	0.000	0.000	0.000
25	A	27	GLN	0	-0.075	-0.044	21.411	0.734	0.734	0.000	0.000	0.000	0.000
26	A	28	ARG	1	0.840	0.917	14.581	19.601	19.601	0.000	0.000	0.000	0.000
27	A	29	THR	0	-0.012	-0.035	20.551	-0.096	-0.096	0.000	0.000	0.000	0.000
28	A	30	TRP	0	-0.049	-0.039	11.942	-1.256	-1.256	0.000	0.000	0.000	0.000
29	A	31	VAL	0	-0.019	-0.004	18.763	0.888	0.888	0.000	0.000	0.000	0.000
30	A	32	ALA	0	0.009	0.000	18.473	-1.119	-1.119	0.000	0.000	0.000	0.000
31	A	33	VAL	0	-0.030	-0.010	18.535	0.988	0.988	0.000	0.000	0.000	0.000
32	A	34	VAL	0	0.022	0.013	19.297	-0.928	-0.928	0.000	0.000	0.000	0.000
33	A	35	GLU	-1	-0.865	-0.920	16.593	-18.270	-18.270	0.000	0.000	0.000	0.000
34	A	36	GLU	-1	-0.901	-0.948	19.645	-12.853	-12.853	0.000	0.000	0.000	0.000
35	A	37	GLU	-1	-0.853	-0.909	19.018	-15.845	-15.845	0.000	0.000	0.000	0.000
36	A	38	THR	0	-0.039	-0.034	22.487	0.304	0.304	0.000	0.000	0.000	0.000
37	A	39	SER	0	-0.023	-0.019	23.292	0.412	0.412	0.000	0.000	0.000	0.000
38	A	40	PHE	0	0.041	0.011	17.553	-0.386	-0.386	0.000	0.000	0.000	0.000
39	A	41	LEU	0	0.043	0.044	20.209	-0.140	-0.140	0.000	0.000	0.000	0.000
40	A	42	ARG	1	0.822	0.885	14.357	19.062	19.062	0.000	0.000	0.000	0.000
41	A	43	ALA	0	0.046	0.027	16.573	1.072	1.072	0.000	0.000	0.000	0.000
42	A	44	ARG	1	0.759	0.865	13.291	18.153	18.153	0.000	0.000	0.000	0.000
43	A	45	VAL	0	0.001	-0.007	14.050	1.471	1.471	0.000	0.000	0.000	0.000
44	A	46	GLN	0	-0.016	-0.029	13.717	-0.912	-0.912	0.000	0.000	0.000	0.000
45	A	47	GLN	0	-0.052	-0.027	14.502	1.149	1.149	0.000	0.000	0.000	0.000
46	A	48	ILE	0	0.002	0.004	16.217	0.008	0.008	0.000	0.000	0.000	0.000
47	A	49	GLN	0	-0.017	0.012	19.451	0.710	0.710	0.000	0.000	0.000	0.000
48	A	50	VAL	0	0.017	0.005	22.617	0.257	0.257	0.000	0.000	0.000	0.000
49	A	51	PRO	0	-0.015	-0.006	25.385	0.087	0.087	0.000	0.000	0.000	0.000
50	A	52	LEU	0	-0.009	-0.004	26.325	-0.151	-0.151	0.000	0.000	0.000	0.000
51	A	53	GLY	0	0.020	0.013	30.107	0.294	0.294	0.000	0.000	0.000	0.000
52	A	54	ASP	-1	-0.915	-0.961	32.875	-8.791	-8.791	0.000	0.000	0.000	0.000
53	A	55	ALA	0	-0.030	-0.001	31.746	-0.253	-0.253	0.000	0.000	0.000	0.000
54	A	56	ALA	0	-0.016	-0.008	31.130	0.361	0.361	0.000	0.000	0.000	0.000
55	A	57	ARG	1	0.944	0.964	33.021	8.260	8.260	0.000	0.000	0.000	0.000
56	A	58	PRO	0	0.086	0.021	32.807	-0.016	-0.016	0.000	0.000	0.000	0.000
57	A	59	SER	0	-0.004	-0.002	33.763	-0.112	-0.112	0.000	0.000	0.000	0.000
58	A	60	HIS	0	-0.008	-0.004	34.075	0.025	0.025	0.000	0.000	0.000	0.000
59	A	61	LEU	0	0.022	0.011	28.904	-0.085	-0.085	0.000	0.000	0.000	0.000
60	A	62	LEU	0	-0.044	-0.014	30.234	-0.239	-0.239	0.000	0.000	0.000	0.000
61	A	63	THR	0	-0.072	-0.034	32.328	0.018	0.018	0.000	0.000	0.000	0.000
62	A	64	SER	0	-0.022	-0.015	26.859	-0.134	-0.134	0.000	0.000	0.000	0.000
63	A	65	GLN	0	-0.033	-0.029	24.968	-0.007	-0.007	0.000	0.000	0.000	0.000
64	A	66	LEU	0	-0.014	-0.011	21.216	-0.681	-0.681	0.000	0.000	0.000	0.000
65	A	67	PRO	0	-0.024	0.017	21.217	0.663	0.663	0.000	0.000	0.000	0.000
66	A	68	LEU	0	0.002	-0.011	24.000	-0.137	-0.137	0.000	0.000	0.000	0.000
67	A	69	MET	0	-0.039	-0.023	22.060	0.249	0.249	0.000	0.000	0.000	0.000
68	A	70	TRP	0	0.022	0.010	17.486	-0.142	-0.142	0.000	0.000	0.000	0.000
69	A	71	GLN	0	0.006	-0.007	18.819	0.186	0.186	0.000	0.000	0.000	0.000
70	A	72	LEU	0	-0.017	0.000	11.722	-0.178	-0.178	0.000	0.000	0.000	0.000
71	A	73	TYR	0	-0.009	-0.010	14.888	1.220	1.220	0.000	0.000	0.000	0.000
72	A	74	PRO	0	0.011	0.001	14.250	-1.483	-1.483	0.000	0.000	0.000	0.000
73	A	75	GLU	-1	-0.928	-0.966	11.646	-20.724	-20.724	0.000	0.000	0.000	0.000
74	A	76	GLU	-1	-0.907	-0.955	7.241	-35.088	-35.088	0.000	0.000	0.000	0.000
75	A	77	ARG	1	0.899	0.947	10.273	18.357	18.357	0.000	0.000	0.000	0.000
76	A	78	TYR	0	0.007	-0.020	12.003	-0.213	-0.213	0.000	0.000	0.000	0.000
77	A	79	MET	0	-0.009	0.019	15.885	0.520	0.520	0.000	0.000	0.000	0.000
78	A	80	ASP	-1	-0.745	-0.873	19.560	-13.506	-13.506	0.000	0.000	0.000	0.000
79	A	81	ASN	0	-0.013	-0.016	21.896	0.061	0.061	0.000	0.000	0.000	0.000
80	A	82	ASN	0	-0.111	-0.060	25.026	0.978	0.978	0.000	0.000	0.000	0.000
81	A	83	SER	0	0.013	0.001	24.231	0.287	0.287	0.000	0.000	0.000	0.000
82	A	84	ARG	1	0.986	1.008	22.398	11.943	11.943	0.000	0.000	0.000	0.000
83	A	85	LEU	0	0.024	0.010	17.629	-0.570	-0.570	0.000	0.000	0.000	0.000
84	A	86	TRP	0	-0.026	-0.027	16.002	-0.104	-0.104	0.000	0.000	0.000	0.000
85	A	87	GLN	0	-0.030	-0.016	10.119	0.914	0.914	0.000	0.000	0.000	0.000
86	A	88	ILE	0	0.006	0.005	7.176	0.110	0.110	0.000	0.000	0.000	0.000
87	A	89	GLN	0	-0.034	-0.018	8.633	-0.046	-0.046	0.000	0.000	0.000	0.000
88	A	90	HIS	0	-0.047	-0.045	5.379	-5.446	-5.446	0.000	0.000	0.000	0.000
91	A	93	MET	0	0.017	0.020	5.882	7.090	7.090	0.000	0.000	0.000	0.000
92	A	94	VAL	0	0.007	0.007	8.929	0.971	0.971	0.000	0.000	0.000	0.000
93	A	95	ARG	1	0.911	0.941	11.721	21.769	21.769	0.000	0.000	0.000	0.000
94	A	96	GLY	0	0.018	0.014	13.173	1.413	1.413	0.000	0.000	0.000	0.000
95	A	97	VAL	0	0.000	0.016	14.246	0.395	0.395	0.000	0.000	0.000	0.000
96	A	98	GLN	0	0.061	0.033	9.697	-2.673	-2.673	0.000	0.000	0.000	0.000
97	A	99	GLU	-1	-0.790	-0.872	9.855	-22.976	-22.976	0.000	0.000	0.000	0.000
98	A	100	LEU	0	0.018	0.008	8.782	-5.096	-5.096	0.000	0.000	0.000	0.000
99	A	101	LEU	0	-0.025	0.000	9.581	2.780	2.780	0.000	0.000	0.000	0.000
100	A	102	LEU	0	0.018	0.016	10.727	-2.085	-2.085	0.000	0.000	0.000	0.000
101	A	103	LYS	1	0.851	0.933	13.391	19.417	19.417	0.000	0.000	0.000	0.000
102	A	104	LEU	0	-0.016	0.012	15.540	-0.301	-0.301	0.000	0.000	0.000	0.000
103	A	105	LEU	0	-0.064	-0.033	15.737	-0.144	-0.144	0.000	0.000	0.000	0.000
104	A	106	PRO	0	-0.062	-0.037	19.561	0.469	0.469	0.000	0.000	0.000	0.000
105	A	107	ASP	-1	-0.960	-0.988	22.241	-12.499	-12.499	0.000	0.000	0.000	0.000
106	A	108	ASP	-2	-1.928	-1.945	23.080	-24.702	-24.702	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:ALA)