FMO DATABASE

FMODB ID: LQK39

Calculation Name: 1X5A-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1X5A

Chain ID: A

ChEMBL ID:

UniProt ID: Q60750

Base Structure: SolutionNMR

Registration Date: 2025-10-03

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	107
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-729983.117039
FMO2-HF: Nuclear repulsion	689624.893664
FMO2-HF: Total energy	-40358.223375
FMO2-MP2: Total energy	-40477.87594

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.
-6.947	-5.991	-0.006	-0.335	-0.615	-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 : 0.867 / q_NPA : 0.920

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	SER	0	0.044	0.023	3.833	0.286	1.242	-0.006	-0.335	-0.615	-0.001
4	A	4	GLY	0	-0.007	-0.003	6.339	1.575	1.575	0.000	0.000	0.000	0.000
5	A	5	SER	0	0.012	0.013	8.988	1.814	1.814	0.000	0.000	0.000	0.000
6	A	6	SER	0	0.035	0.001	9.634	-1.917	-1.917	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.049	0.033	9.253	-0.497	-0.497	0.000	0.000	0.000	0.000
8	A	8	ALA	0	-0.039	-0.008	6.496	-2.439	-2.439	0.000	0.000	0.000	0.000
9	A	9	GLU	-1	-0.917	-0.966	7.469	-22.583	-22.583	0.000	0.000	0.000	0.000
10	A	10	SER	0	-0.068	-0.043	8.384	0.887	0.887	0.000	0.000	0.000	0.000
11	A	11	LEU	0	-0.001	0.016	9.239	1.757	1.757	0.000	0.000	0.000	0.000
12	A	12	SER	0	-0.011	-0.009	9.926	-1.753	-1.753	0.000	0.000	0.000	0.000
13	A	13	GLY	0	-0.021	-0.009	10.781	1.493	1.493	0.000	0.000	0.000	0.000
14	A	14	LEU	0	-0.056	-0.017	11.803	1.402	1.402	0.000	0.000	0.000	0.000
15	A	15	SER	0	0.012	0.004	10.201	-0.375	-0.375	0.000	0.000	0.000	0.000
16	A	16	LEU	0	-0.032	0.012	12.339	0.546	0.546	0.000	0.000	0.000	0.000
17	A	17	LYS	1	0.904	0.950	15.209	15.675	15.675	0.000	0.000	0.000	0.000
18	A	18	LEU	0	0.051	0.021	16.582	0.890	0.890	0.000	0.000	0.000	0.000
19	A	19	VAL	0	-0.080	-0.042	19.913	-0.318	-0.318	0.000	0.000	0.000	0.000
20	A	20	LYS	1	0.879	0.940	22.074	11.141	11.141	0.000	0.000	0.000	0.000
21	A	21	LYS	1	0.948	0.987	24.536	12.282	12.282	0.000	0.000	0.000	0.000
22	A	22	GLU	-1	-0.856	-0.926	26.472	-9.555	-9.555	0.000	0.000	0.000	0.000
23	A	23	PRO	0	-0.020	0.003	30.087	-0.190	-0.190	0.000	0.000	0.000	0.000
24	A	24	ARG	1	0.954	0.972	32.679	8.417	8.417	0.000	0.000	0.000	0.000
25	A	25	GLN	0	0.000	-0.020	29.529	-0.032	-0.032	0.000	0.000	0.000	0.000
26	A	26	LEU	0	0.028	0.029	24.714	-0.191	-0.191	0.000	0.000	0.000	0.000
27	A	27	GLU	-1	-0.896	-0.936	24.580	-11.520	-11.520	0.000	0.000	0.000	0.000
28	A	28	LEU	0	0.021	0.010	20.163	-0.485	-0.485	0.000	0.000	0.000	0.000
29	A	29	THR	0	-0.026	-0.020	18.115	0.430	0.430	0.000	0.000	0.000	0.000
30	A	30	TRP	0	0.027	0.023	15.729	-0.963	-0.963	0.000	0.000	0.000	0.000
31	A	31	ALA	0	0.004	-0.005	14.584	0.914	0.914	0.000	0.000	0.000	0.000
32	A	32	GLY	0	0.041	0.018	12.138	-1.752	-1.752	0.000	0.000	0.000	0.000
33	A	33	SER	0	-0.028	-0.007	12.948	-0.214	-0.214	0.000	0.000	0.000	0.000
34	A	34	ARG	1	0.965	0.989	15.613	18.246	18.246	0.000	0.000	0.000	0.000
35	A	35	PRO	0	0.057	0.024	16.982	0.751	0.751	0.000	0.000	0.000	0.000
36	A	36	ARG	1	0.916	0.942	20.499	13.039	13.039	0.000	0.000	0.000	0.000
37	A	37	ASN	0	-0.006	0.004	21.538	-0.661	-0.661	0.000	0.000	0.000	0.000
38	A	38	PRO	0	0.004	0.009	23.152	0.444	0.444	0.000	0.000	0.000	0.000
39	A	39	GLY	0	0.040	0.020	26.363	-0.172	-0.172	0.000	0.000	0.000	0.000
40	A	40	GLY	0	0.000	0.002	28.173	-0.107	-0.107	0.000	0.000	0.000	0.000
41	A	41	ASN	0	-0.038	-0.028	26.878	-0.370	-0.370	0.000	0.000	0.000	0.000
42	A	42	LEU	0	0.041	0.030	21.094	0.147	0.147	0.000	0.000	0.000	0.000
43	A	43	SER	0	-0.014	-0.010	24.405	0.533	0.533	0.000	0.000	0.000	0.000
44	A	44	TYR	0	-0.009	-0.015	19.420	-0.480	-0.480	0.000	0.000	0.000	0.000
45	A	45	GLU	-1	-0.877	-0.938	22.987	-11.160	-11.160	0.000	0.000	0.000	0.000
46	A	46	LEU	0	-0.034	-0.010	21.948	-0.805	-0.805	0.000	0.000	0.000	0.000
47	A	47	HIS	0	0.005	-0.017	22.941	0.483	0.483	0.000	0.000	0.000	0.000
48	A	48	VAL	0	0.002	-0.005	23.214	-0.754	-0.754	0.000	0.000	0.000	0.000
49	A	49	LEU	0	-0.005	0.003	23.566	0.351	0.351	0.000	0.000	0.000	0.000
50	A	50	ASN	0	-0.006	-0.007	25.777	-0.549	-0.549	0.000	0.000	0.000	0.000
51	A	51	GLN	0	-0.064	-0.036	28.477	-0.148	-0.148	0.000	0.000	0.000	0.000
52	A	52	ASP	-1	-0.883	-0.940	30.240	-9.164	-9.164	0.000	0.000	0.000	0.000
53	A	53	GLU	-1	-0.969	-0.979	31.572	-8.687	-8.687	0.000	0.000	0.000	0.000
54	A	54	GLU	-1	-0.947	-0.982	28.938	-10.683	-10.683	0.000	0.000	0.000	0.000
55	A	55	TRP	0	-0.033	-0.013	29.046	0.317	0.317	0.000	0.000	0.000	0.000
56	A	56	HIS	0	0.027	0.019	27.539	-0.489	-0.489	0.000	0.000	0.000	0.000
57	A	57	GLN	0	-0.005	-0.017	27.575	0.508	0.508	0.000	0.000	0.000	0.000
58	A	58	MET	0	-0.005	0.010	26.954	-0.427	-0.427	0.000	0.000	0.000	0.000
59	A	59	VAL	0	-0.009	0.004	24.588	0.402	0.402	0.000	0.000	0.000	0.000
60	A	60	LEU	0	-0.007	-0.016	26.196	-0.320	-0.320	0.000	0.000	0.000	0.000
61	A	61	GLU	-1	-0.833	-0.900	24.895	-11.357	-11.357	0.000	0.000	0.000	0.000
62	A	62	PRO	0	-0.013	-0.006	19.791	-0.031	-0.031	0.000	0.000	0.000	0.000
63	A	63	ARG	1	0.831	0.895	20.487	10.901	10.901	0.000	0.000	0.000	0.000
64	A	64	VAL	0	0.041	0.015	23.047	0.361	0.361	0.000	0.000	0.000	0.000
65	A	65	LEU	0	-0.024	-0.005	25.239	-0.238	-0.238	0.000	0.000	0.000	0.000
66	A	66	LEU	0	0.020	0.029	25.594	0.311	0.311	0.000	0.000	0.000	0.000
67	A	67	THR	0	-0.003	-0.022	29.425	0.058	0.058	0.000	0.000	0.000	0.000
68	A	68	LYS	1	0.940	0.960	32.897	8.456	8.456	0.000	0.000	0.000	0.000
69	A	69	LEU	0	0.007	0.027	28.778	0.032	0.032	0.000	0.000	0.000	0.000
70	A	70	GLN	0	0.039	0.017	32.604	0.382	0.382	0.000	0.000	0.000	0.000
71	A	71	PRO	0	0.028	0.013	31.860	-0.341	-0.341	0.000	0.000	0.000	0.000
72	A	72	ASP	-1	-0.968	-0.992	30.354	-10.007	-10.007	0.000	0.000	0.000	0.000
73	A	73	THR	0	-0.014	0.009	29.390	0.129	0.129	0.000	0.000	0.000	0.000
74	A	74	THR	0	-0.028	-0.026	23.631	-0.390	-0.390	0.000	0.000	0.000	0.000
75	A	75	TYR	0	0.030	0.022	25.160	0.339	0.339	0.000	0.000	0.000	0.000
76	A	76	ILE	0	0.013	0.017	20.250	-0.629	-0.629	0.000	0.000	0.000	0.000
77	A	77	VAL	0	-0.018	-0.008	20.575	0.488	0.488	0.000	0.000	0.000	0.000
78	A	78	ARG	1	0.938	0.964	18.404	13.662	13.662	0.000	0.000	0.000	0.000
79	A	79	VAL	0	0.021	0.011	17.389	0.866	0.866	0.000	0.000	0.000	0.000
80	A	80	ARG	1	0.891	0.948	17.617	13.138	13.138	0.000	0.000	0.000	0.000
81	A	81	THR	0	0.010	-0.003	18.007	0.644	0.644	0.000	0.000	0.000	0.000
82	A	82	LEU	0	-0.014	0.000	20.394	-0.106	-0.106	0.000	0.000	0.000	0.000
83	A	83	THR	0	-0.022	-0.022	20.875	0.000	0.000	0.000	0.000	0.000	0.000
84	A	84	PRO	0	0.013	0.007	24.157	0.236	0.236	0.000	0.000	0.000	0.000
85	A	85	LEU	0	-0.002	-0.010	25.289	0.406	0.406	0.000	0.000	0.000	0.000
86	A	86	GLY	0	0.016	0.023	22.468	-0.459	-0.459	0.000	0.000	0.000	0.000
87	A	87	PRO	0	-0.014	-0.002	21.327	-0.603	-0.603	0.000	0.000	0.000	0.000
88	A	88	GLY	0	0.047	0.024	18.404	-0.239	-0.239	0.000	0.000	0.000	0.000
89	A	89	PRO	0	0.037	0.014	14.767	0.969	0.969	0.000	0.000	0.000	0.000
90	A	90	PHE	0	-0.044	-0.030	17.018	-0.203	-0.203	0.000	0.000	0.000	0.000
91	A	91	SER	0	0.006	0.016	14.222	-0.317	-0.317	0.000	0.000	0.000	0.000
92	A	92	PRO	0	0.001	0.003	11.560	0.961	0.961	0.000	0.000	0.000	0.000
93	A	93	ASP	-1	-0.885	-0.947	14.869	-16.920	-16.920	0.000	0.000	0.000	0.000
94	A	94	HIS	0	-0.047	-0.028	13.463	-2.036	-2.036	0.000	0.000	0.000	0.000
95	A	95	GLU	-1	-0.906	-0.959	17.023	-13.665	-13.665	0.000	0.000	0.000	0.000
96	A	96	PHE	0	-0.036	-0.020	17.339	-0.475	-0.475	0.000	0.000	0.000	0.000
97	A	97	ARG	1	0.953	0.978	21.671	12.674	12.674	0.000	0.000	0.000	0.000
98	A	98	THR	0	-0.040	-0.028	25.009	-0.273	-0.273	0.000	0.000	0.000	0.000
99	A	99	SER	0	-0.023	-0.033	27.985	-0.173	-0.173	0.000	0.000	0.000	0.000
100	A	100	PRO	0	0.016	0.013	29.949	0.152	0.152	0.000	0.000	0.000	0.000
101	A	101	PRO	0	0.024	0.001	32.562	0.092	0.092	0.000	0.000	0.000	0.000
102	A	102	SER	0	-0.049	-0.028	36.231	-0.081	-0.081	0.000	0.000	0.000	0.000
103	A	103	GLY	0	0.038	0.016	37.981	0.094	0.094	0.000	0.000	0.000	0.000
104	A	104	PRO	0	-0.031	-0.007	38.315	0.018	0.018	0.000	0.000	0.000	0.000
105	A	105	SER	0	-0.004	0.000	36.090	-0.220	-0.220	0.000	0.000	0.000	0.000
106	A	106	SER	0	-0.080	-0.043	35.133	0.126	0.126	0.000	0.000	0.000	0.000
107	A	107	GLY	-1	-0.891	-0.936	36.902	-8.649	-8.649	0.000	0.000	0.000	0.000

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