FMO DATABASE

FMODB ID: 5R8QZ

Calculation Name: 1L5C-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1L5C

Chain ID: A

ChEMBL ID:

UniProt ID: P01175

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	85
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-533502.718125
FMO2-HF: Nuclear repulsion	497301.078325
FMO2-HF: Total energy	-36201.6398
FMO2-MP2: Total energy	-36294.597634

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:ALA)

Summations of interaction energy for fragment #1(A:1: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.
-137.454	-131.483	5.487	-5.651	-5.809	-0.067

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.837 / q_NPA : 0.919

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

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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	LEU	0	-0.019	-0.033	3.237	-5.471	-3.957	0.069	-0.811	-0.773	-0.002
10	A	10	CYS	0	0.132	0.107	4.709	4.828	4.889	-0.002	-0.015	-0.044	0.000
51	A	55	GLN	0	-0.034	-0.038	2.010	-44.020	-39.826	5.419	-4.795	-4.818	-0.065
52	A	56	SER	0	0.003	-0.027	3.482	9.151	9.392	0.002	-0.027	-0.217	0.000
53	A	57	GLY	0	-0.059	-0.039	4.776	-4.545	-4.584	-0.001	-0.003	0.043	0.000
4	A	4	ASP	-1	-0.835	-0.918	5.984	-30.506	-30.506	0.000	0.000	0.000	0.000
5	A	5	LEU	0	0.001	0.004	7.264	2.223	2.223	0.000	0.000	0.000	0.000
6	A	6	ASP	-1	-0.942	-0.967	10.979	-19.616	-19.616	0.000	0.000	0.000	0.000
7	A	7	VAL	0	-0.049	-0.023	13.280	-0.087	-0.087	0.000	0.000	0.000	0.000
8	A	8	ARG	1	0.954	0.969	9.636	23.395	23.395	0.000	0.000	0.000	0.000
9	A	9	THR	0	-0.095	-0.049	8.690	2.079	2.079	0.000	0.000	0.000	0.000
11	A	11	LEU	0	0.057	0.041	8.848	1.662	1.662	0.000	0.000	0.000	0.000
12	A	12	PRO	0	-0.004	-0.005	11.955	-0.808	-0.808	0.000	0.000	0.000	0.000
13	A	13	CYS	0	-0.060	0.018	11.463	-1.721	-1.721	0.000	0.000	0.000	0.000
14	A	14	GLY	0	0.064	0.048	16.113	0.439	0.439	0.000	0.000	0.000	0.000
15	A	15	PRO	0	0.022	0.017	19.578	0.289	0.289	0.000	0.000	0.000	0.000
16	A	16	GLY	0	-0.014	-0.032	21.353	-0.252	-0.252	0.000	0.000	0.000	0.000
17	A	17	GLY	0	0.004	-0.019	17.919	-0.249	-0.249	0.000	0.000	0.000	0.000
18	A	18	LYS	1	0.831	0.907	17.189	14.140	14.140	0.000	0.000	0.000	0.000
19	A	19	GLY	0	0.032	0.019	14.848	-0.416	-0.416	0.000	0.000	0.000	0.000
20	A	20	ARG	1	0.865	0.956	8.296	30.240	30.240	0.000	0.000	0.000	0.000
21	A	21	CYS	0	0.109	0.051	8.791	0.520	0.520	0.000	0.000	0.000	0.000
22	A	22	PHE	0	-0.084	-0.034	7.342	-3.338	-3.338	0.000	0.000	0.000	0.000
23	A	23	GLY	0	0.038	0.023	5.956	-6.693	-6.693	0.000	0.000	0.000	0.000
24	A	24	PRO	0	0.050	0.032	7.349	-0.178	-0.178	0.000	0.000	0.000	0.000
25	A	25	SER	0	0.021	0.014	9.936	-0.263	-0.263	0.000	0.000	0.000	0.000
26	A	26	ILE	0	-0.043	-0.030	10.360	1.490	1.490	0.000	0.000	0.000	0.000
27	A	28	CYS	0	-0.036	-0.014	12.201	0.238	0.238	0.000	0.000	0.000	0.000
28	A	29	GLY	0	0.099	0.034	13.195	-1.327	-1.327	0.000	0.000	0.000	0.000
29	A	30	ASP	-1	-0.887	-0.921	14.619	-19.211	-19.211	0.000	0.000	0.000	0.000
30	A	31	GLU	-1	-0.820	-0.897	16.283	-14.559	-14.559	0.000	0.000	0.000	0.000
31	A	32	LEU	0	-0.085	-0.041	17.752	0.742	0.742	0.000	0.000	0.000	0.000
32	A	33	GLY	0	0.061	0.039	19.009	0.324	0.324	0.000	0.000	0.000	0.000
33	A	35	PHE	0	0.011	0.008	16.233	1.165	1.165	0.000	0.000	0.000	0.000
34	A	36	VAL	0	0.056	0.013	15.015	-1.465	-1.465	0.000	0.000	0.000	0.000
35	A	37	GLY	0	-0.008	0.000	16.207	1.036	1.036	0.000	0.000	0.000	0.000
36	A	38	THR	0	-0.017	-0.007	18.053	0.699	0.699	0.000	0.000	0.000	0.000
37	A	39	ALA	0	0.022	0.007	20.231	-0.399	-0.399	0.000	0.000	0.000	0.000
38	A	40	GLU	-1	-0.895	-0.958	19.911	-13.857	-13.857	0.000	0.000	0.000	0.000
39	A	41	ALA	0	0.011	-0.015	16.158	-0.909	-0.909	0.000	0.000	0.000	0.000
40	A	42	LEU	0	-0.024	-0.008	16.121	-1.087	-1.087	0.000	0.000	0.000	0.000
41	A	43	ARG	1	0.885	0.924	15.459	15.924	15.924	0.000	0.000	0.000	0.000
42	A	45	GLN	0	-0.035	-0.019	13.519	0.048	0.048	0.000	0.000	0.000	0.000
43	A	46	GLU	-1	-0.917	-0.964	11.877	-22.512	-22.512	0.000	0.000	0.000	0.000
44	A	47	GLU	-1	-0.828	-0.945	7.442	-33.371	-33.371	0.000	0.000	0.000	0.000
45	A	48	ASN	0	-0.117	-0.048	11.150	0.514	0.514	0.000	0.000	0.000	0.000
46	A	49	TYR	0	-0.080	-0.039	13.896	1.313	1.313	0.000	0.000	0.000	0.000
47	A	50	LEU	0	-0.007	-0.010	14.446	1.244	1.244	0.000	0.000	0.000	0.000
48	A	51	PRO	0	-0.039	-0.014	12.253	-1.268	-1.268	0.000	0.000	0.000	0.000
49	A	52	SER	0	-0.010	0.012	9.576	1.785	1.785	0.000	0.000	0.000	0.000
50	A	53	PRO	0	-0.051	-0.015	5.755	-1.677	-1.677	0.000	0.000	0.000	0.000
54	A	58	GLN	0	0.014	0.002	5.686	6.571	6.571	0.000	0.000	0.000	0.000
55	A	59	LYS	1	0.788	0.879	7.677	21.771	21.771	0.000	0.000	0.000	0.000
56	A	60	PRO	0	-0.025	-0.031	9.309	1.320	1.320	0.000	0.000	0.000	0.000
57	A	61	CYS	0	-0.046	0.011	11.473	-0.344	-0.344	0.000	0.000	0.000	0.000
58	A	62	GLY	0	-0.012	-0.003	14.521	-0.610	-0.610	0.000	0.000	0.000	0.000
59	A	63	SER	0	-0.022	-0.027	16.652	0.865	0.865	0.000	0.000	0.000	0.000
60	A	64	GLY	0	0.045	0.013	15.520	-0.646	-0.646	0.000	0.000	0.000	0.000
61	A	65	GLY	0	0.020	0.011	11.434	-1.273	-1.273	0.000	0.000	0.000	0.000
62	A	66	ARG	1	0.843	0.897	7.343	31.961	31.961	0.000	0.000	0.000	0.000
63	A	67	CYS	0	-0.030	-0.014	10.702	-0.985	-0.985	0.000	0.000	0.000	0.000
64	A	68	ALA	0	-0.047	-0.038	10.896	-2.733	-2.733	0.000	0.000	0.000	0.000
65	A	69	ALA	0	0.019	0.012	12.099	0.460	0.460	0.000	0.000	0.000	0.000
66	A	70	ALA	0	0.025	0.015	15.186	0.045	0.045	0.000	0.000	0.000	0.000
67	A	71	GLY	0	0.005	-0.033	18.234	0.477	0.477	0.000	0.000	0.000	0.000
68	A	72	ILE	0	-0.027	-0.012	13.878	-0.113	-0.113	0.000	0.000	0.000	0.000
69	A	74	CYS	0	-0.110	-0.051	9.696	-0.452	-0.452	0.000	0.000	0.000	0.000
70	A	75	SER	0	0.056	0.017	10.467	-1.990	-1.990	0.000	0.000	0.000	0.000
71	A	76	PRO	0	-0.084	-0.063	9.374	-1.256	-1.256	0.000	0.000	0.000	0.000
72	A	77	ASP	-1	-0.901	-0.940	10.440	-20.442	-20.442	0.000	0.000	0.000	0.000
73	A	78	GLY	0	-0.021	-0.009	12.644	0.683	0.683	0.000	0.000	0.000	0.000
74	A	80	GLU	-1	-0.900	-0.931	14.555	-15.090	-15.090	0.000	0.000	0.000	0.000
75	A	81	GLU	0	-0.043	-0.070	17.518	-0.708	-0.708	0.000	0.000	0.000	0.000
76	A	82	ASP	-1	-0.719	-0.851	17.095	-17.393	-17.393	0.000	0.000	0.000	0.000
77	A	83	PRO	0	0.035	-0.003	19.839	-0.034	-0.034	0.000	0.000	0.000	0.000
78	A	84	ALA	0	-0.058	-0.033	18.004	0.213	0.213	0.000	0.000	0.000	0.000
79	A	86	ASP	0	-0.069	-0.018	19.485	0.205	0.205	0.000	0.000	0.000	0.000
80	A	87	PRO	0	0.017	0.037	21.133	0.478	0.478	0.000	0.000	0.000	0.000
81	A	88	GLU	-1	-0.867	-0.890	23.642	-11.716	-11.716	0.000	0.000	0.000	0.000
82	A	89	ALA	0	-0.044	-0.006	23.050	0.082	0.082	0.000	0.000	0.000	0.000
83	A	90	ALA	0	-0.051	-0.023	25.136	0.533	0.533	0.000	0.000	0.000	0.000
84	A	91	PHE	0	-0.051	-0.031	26.869	-0.144	-0.144	0.000	0.000	0.000	0.000
85	A	92	SER	-1	-0.880	-0.895	23.566	-12.872	-12.872	0.000	0.000	0.000	0.000

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