FMO DATABASE

FMODB ID: NZLKQ

Calculation Name: 1BWO-A-Xray547

Preferred Name:

Target Type:

Ligand Name: [1-myristoyl-glycerol-3-yl]phosphonylcholine

Ligand 3-letter code: LPC

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1BWO

Chain ID: A

ChEMBL ID:

UniProt ID: P24296

Base Structure: X-ray

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	86
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-575629.644009
FMO2-HF: Nuclear repulsion	540151.634807
FMO2-HF: Total energy	-35478.009202
FMO2-MP2: Total energy	-35575.39221

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:ILE)

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

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.
-49.408	-39.768	24.194	-14.494	-19.336	-0.148

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.776 / q_NPA : 0.870

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	CYS	0	-0.061	-0.015	2.978	2.183	5.523	0.359	-1.765	-1.934	-0.014
4	A	4	GLY	0	0.081	0.037	4.648	4.148	4.293	-0.001	-0.010	-0.133	0.000
5	A	5	HIS	0	-0.035	-0.023	2.349	3.481	4.159	0.998	-0.303	-1.373	-0.001
6	A	6	VAL	0	0.002	0.001	2.577	1.698	2.414	1.274	-0.341	-1.649	-0.002
7	A	7	ASP	-1	-0.850	-0.918	5.085	-19.085	-19.003	-0.001	-0.004	-0.077	0.000
9	A	9	LEU	0	-0.015	0.000	4.270	1.880	2.002	-0.001	-0.012	-0.109	0.000
33	A	34	LEU	0	0.010	0.009	2.730	-3.198	-2.628	0.553	-0.169	-0.954	0.000
34	A	35	HIS	0	-0.004	-0.004	4.961	-4.207	-4.130	-0.001	-0.001	-0.074	0.000
36	A	37	GLN	0	-0.001	0.017	3.406	-3.335	-2.689	0.044	-0.218	-0.471	-0.001
37	A	38	ALA	0	-0.003	-0.003	2.681	-4.704	-3.849	0.245	-0.260	-0.839	0.000
38	A	39	ARG	1	0.922	0.965	3.749	28.963	29.084	0.010	-0.016	-0.115	0.000
42	A	43	ASP	-1	-0.796	-0.887	1.726	-121.238	-121.042	13.259	-7.598	-5.857	-0.090
43	A	44	ARG	1	0.817	0.889	3.399	26.082	26.932	0.050	-0.327	-0.572	-0.003
45	A	46	SER	0	-0.056	-0.017	1.959	-18.406	-18.281	6.383	-3.087	-3.422	-0.033
46	A	47	ALA	0	0.053	0.010	2.358	2.392	3.570	0.971	-0.553	-1.596	-0.004
47	A	48	CYS	0	-0.051	-0.011	3.553	6.410	6.349	0.052	0.170	-0.161	0.000
8	A	8	SER	0	-0.085	-0.054	7.600	2.737	2.737	0.000	0.000	0.000	0.000
10	A	10	VAL	0	-0.003	-0.012	7.615	1.829	1.829	0.000	0.000	0.000	0.000
11	A	11	ARG	1	0.915	0.949	10.135	20.353	20.353	0.000	0.000	0.000	0.000
12	A	12	PRO	0	-0.020	-0.014	12.404	1.170	1.170	0.000	0.000	0.000	0.000
13	A	13	CYS	0	-0.096	-0.019	13.422	-0.429	-0.429	0.000	0.000	0.000	0.000
14	A	14	LEU	0	0.022	0.023	15.561	0.543	0.543	0.000	0.000	0.000	0.000
15	A	15	SER	0	0.055	0.015	17.316	0.220	0.220	0.000	0.000	0.000	0.000
16	A	16	TYR	0	-0.030	-0.009	18.311	0.542	0.542	0.000	0.000	0.000	0.000
17	A	17	VAL	0	0.000	-0.001	16.010	0.377	0.377	0.000	0.000	0.000	0.000
18	A	18	GLN	0	-0.033	-0.014	19.245	0.081	0.081	0.000	0.000	0.000	0.000
19	A	19	GLY	0	-0.031	-0.010	22.245	0.494	0.494	0.000	0.000	0.000	0.000
20	A	20	GLY	0	0.006	0.017	23.755	0.480	0.480	0.000	0.000	0.000	0.000
21	A	21	PRO	0	-0.012	-0.016	24.208	-0.210	-0.210	0.000	0.000	0.000	0.000
22	A	22	GLY	0	-0.018	-0.002	21.559	-0.316	-0.316	0.000	0.000	0.000	0.000
23	A	23	PRO	0	0.008	-0.010	17.575	0.324	0.324	0.000	0.000	0.000	0.000
24	A	24	SER	0	0.030	0.015	18.039	0.276	0.276	0.000	0.000	0.000	0.000
25	A	25	GLY	0	0.051	0.018	17.662	-0.498	-0.498	0.000	0.000	0.000	0.000
26	A	26	GLN	0	0.075	0.028	15.540	-0.525	-0.525	0.000	0.000	0.000	0.000
27	A	28	CYS	0	-0.013	0.000	12.702	-0.742	-0.742	0.000	0.000	0.000	0.000
28	A	29	ASP	-1	-0.873	-0.940	13.027	-16.509	-16.509	0.000	0.000	0.000	0.000
29	A	30	GLY	0	0.010	0.017	9.720	-1.178	-1.178	0.000	0.000	0.000	0.000
30	A	31	VAL	0	0.007	-0.008	8.250	-2.329	-2.329	0.000	0.000	0.000	0.000
31	A	32	LYS	1	0.891	0.952	8.846	14.551	14.551	0.000	0.000	0.000	0.000
32	A	33	ASN	0	-0.052	-0.033	7.267	-0.814	-0.814	0.000	0.000	0.000	0.000
35	A	36	ASN	0	-0.012	-0.015	7.743	0.382	0.382	0.000	0.000	0.000	0.000
39	A	40	SER	0	-0.002	-0.004	5.256	3.586	3.586	0.000	0.000	0.000	0.000
40	A	41	GLN	0	0.031	-0.001	6.845	-3.983	-3.983	0.000	0.000	0.000	0.000
41	A	42	SER	0	0.060	0.034	5.518	-0.702	-0.702	0.000	0.000	0.000	0.000
44	A	45	GLN	0	0.047	0.034	6.049	1.337	1.337	0.000	0.000	0.000	0.000
48	A	49	ASN	0	0.014	-0.012	6.645	5.540	5.540	0.000	0.000	0.000	0.000
49	A	51	LEU	0	0.030	0.007	6.173	3.582	3.582	0.000	0.000	0.000	0.000
50	A	52	LYS	1	0.875	0.942	8.425	24.599	24.599	0.000	0.000	0.000	0.000
51	A	53	GLY	0	-0.007	-0.004	10.021	2.002	2.002	0.000	0.000	0.000	0.000
52	A	54	ILE	0	0.017	-0.001	7.531	1.675	1.675	0.000	0.000	0.000	0.000
53	A	55	ALA	0	-0.006	-0.008	11.401	1.675	1.675	0.000	0.000	0.000	0.000
54	A	56	ARG	1	0.888	0.938	13.983	17.463	17.463	0.000	0.000	0.000	0.000
55	A	57	GLY	0	0.020	0.027	14.830	0.853	0.853	0.000	0.000	0.000	0.000
56	A	58	ILE	0	-0.071	-0.021	14.467	0.654	0.654	0.000	0.000	0.000	0.000
57	A	59	HIS	0	0.048	0.020	17.923	0.090	0.090	0.000	0.000	0.000	0.000
58	A	60	ASN	0	-0.024	-0.023	21.719	0.009	0.009	0.000	0.000	0.000	0.000
59	A	61	LEU	0	0.011	0.018	16.948	-0.002	-0.002	0.000	0.000	0.000	0.000
60	A	62	ASN	0	0.023	0.014	20.711	0.200	0.200	0.000	0.000	0.000	0.000
61	A	63	GLU	-1	-0.785	-0.918	18.353	-15.001	-15.001	0.000	0.000	0.000	0.000
62	A	64	ASP	-1	-0.940	-0.955	19.706	-12.271	-12.271	0.000	0.000	0.000	0.000
63	A	65	ASN	0	0.020	0.000	20.830	-0.032	-0.032	0.000	0.000	0.000	0.000
64	A	66	ALA	0	0.009	0.007	15.873	-0.373	-0.373	0.000	0.000	0.000	0.000
65	A	67	ARG	1	0.832	0.895	16.456	13.235	13.235	0.000	0.000	0.000	0.000
66	A	68	SER	0	-0.025	-0.013	18.191	0.040	0.040	0.000	0.000	0.000	0.000
67	A	69	ILE	0	0.032	0.004	13.886	0.231	0.231	0.000	0.000	0.000	0.000
68	A	70	PRO	0	-0.008	-0.006	13.804	0.189	0.189	0.000	0.000	0.000	0.000
69	A	71	PRO	0	0.016	0.009	15.831	0.230	0.230	0.000	0.000	0.000	0.000
70	A	72	LYS	1	0.932	0.973	19.504	12.253	12.253	0.000	0.000	0.000	0.000
71	A	74	GLY	0	-0.001	0.001	17.135	-0.213	-0.213	0.000	0.000	0.000	0.000
72	A	75	VAL	0	-0.064	-0.028	12.019	-0.299	-0.299	0.000	0.000	0.000	0.000
73	A	76	ASN	0	-0.016	-0.021	15.493	-0.229	-0.229	0.000	0.000	0.000	0.000
74	A	77	LEU	0	0.028	0.027	11.855	-0.548	-0.548	0.000	0.000	0.000	0.000
75	A	78	PRO	0	-0.029	-0.010	14.822	0.884	0.884	0.000	0.000	0.000	0.000
76	A	79	TYR	0	-0.011	-0.025	11.602	0.486	0.486	0.000	0.000	0.000	0.000
77	A	80	THR	0	-0.010	0.001	16.935	-0.120	-0.120	0.000	0.000	0.000	0.000
78	A	81	ILE	0	-0.004	0.008	12.962	-0.378	-0.378	0.000	0.000	0.000	0.000
79	A	82	SER	0	0.046	-0.006	15.431	0.718	0.718	0.000	0.000	0.000	0.000
80	A	83	LEU	0	0.004	0.009	15.176	-1.285	-1.285	0.000	0.000	0.000	0.000
81	A	84	ASN	0	-0.062	-0.030	16.359	-0.686	-0.686	0.000	0.000	0.000	0.000
82	A	85	ILE	0	0.037	0.043	12.558	0.160	0.160	0.000	0.000	0.000	0.000
83	A	86	ASP	-1	-0.761	-0.862	13.986	-20.754	-20.754	0.000	0.000	0.000	0.000
84	A	88	SER	0	-0.055	-0.046	10.264	-1.985	-1.985	0.000	0.000	0.000	0.000
85	A	89	ARG	1	0.850	0.912	12.886	18.790	18.790	0.000	0.000	0.000	0.000
86	A	90	VAL	-1	-0.792	-0.834	8.714	-24.901	-24.901	0.000	0.000	0.000	0.000

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