FMO DATABASE

FMODB ID: 1Y2JZ

Calculation Name: 2LV4-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2LV4

Chain ID: A

ChEMBL ID:

UniProt ID: Q8ZP79

Base Structure: SolutionNMR

Registration Date: 2025-10-04

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	146
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1023667.176365
FMO2-HF: Nuclear repulsion	967488.262579
FMO2-HF: Total energy	-56178.913786
FMO2-MP2: Total energy	-56343.453648

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:131:GLY)

Summations of interaction energy for fragment #1(A:131: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.
14.273	15.238	-0.004	-0.363	-0.597	-0.001

Interaction energy analysis for fragmet #1(A:131:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.881 / q_NPA : 0.928

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	133	LEU	0	0.072	0.028	3.858	7.598	8.563	-0.004	-0.363	-0.597	-0.001
4	A	134	GLY	0	-0.005	0.016	5.871	6.224	6.224	0.000	0.000	0.000	0.000
5	A	135	SER	0	-0.002	-0.004	8.362	3.151	3.151	0.000	0.000	0.000	0.000
6	A	136	GLY	0	0.023	0.006	10.629	1.234	1.234	0.000	0.000	0.000	0.000
7	A	137	SER	0	-0.031	-0.024	13.370	0.991	0.991	0.000	0.000	0.000	0.000
8	A	138	LYS	1	0.922	0.969	15.629	16.707	16.707	0.000	0.000	0.000	0.000
9	A	139	ILE	0	0.042	0.023	19.181	-0.089	-0.089	0.000	0.000	0.000	0.000
10	A	140	LYS	1	0.946	0.970	21.985	13.534	13.534	0.000	0.000	0.000	0.000
11	A	141	LEU	0	0.000	0.010	24.182	0.233	0.233	0.000	0.000	0.000	0.000
12	A	142	GLU	-1	-0.954	-0.974	27.551	-11.187	-11.187	0.000	0.000	0.000	0.000
13	A	143	ILE	0	-0.007	-0.011	29.622	0.142	0.142	0.000	0.000	0.000	0.000
14	A	144	TYR	0	-0.006	0.000	33.449	0.043	0.043	0.000	0.000	0.000	0.000
15	A	145	ASN	0	-0.038	-0.032	35.615	0.028	0.028	0.000	0.000	0.000	0.000
16	A	146	GLU	-1	-0.852	-0.923	36.595	-8.394	-8.394	0.000	0.000	0.000	0.000
17	A	147	THR	0	-0.072	-0.033	39.210	0.226	0.226	0.000	0.000	0.000	0.000
18	A	148	ASP	-1	-0.926	-0.963	38.748	-8.092	-8.092	0.000	0.000	0.000	0.000
19	A	149	MET	0	-0.058	-0.023	38.392	0.161	0.161	0.000	0.000	0.000	0.000
20	A	150	ALA	0	0.036	0.027	43.392	0.127	0.127	0.000	0.000	0.000	0.000
21	A	151	SER	0	-0.023	-0.014	46.806	0.014	0.014	0.000	0.000	0.000	0.000
22	A	152	ALA	0	0.014	-0.010	49.973	0.078	0.078	0.000	0.000	0.000	0.000
23	A	153	SER	0	-0.025	-0.008	51.527	0.134	0.134	0.000	0.000	0.000	0.000
24	A	154	GLY	0	-0.018	-0.003	54.822	0.025	0.025	0.000	0.000	0.000	0.000
25	A	155	TYR	0	-0.022	-0.012	56.678	0.048	0.048	0.000	0.000	0.000	0.000
26	A	156	THR	0	-0.005	0.000	60.391	-0.051	-0.051	0.000	0.000	0.000	0.000
27	A	157	PRO	0	-0.009	-0.009	63.305	0.028	0.028	0.000	0.000	0.000	0.000
28	A	158	VAL	0	0.011	0.010	66.515	-0.017	-0.017	0.000	0.000	0.000	0.000
29	A	159	PRO	0	0.003	-0.007	69.829	-0.010	-0.010	0.000	0.000	0.000	0.000
30	A	160	SER	0	-0.007	-0.003	71.631	0.013	0.013	0.000	0.000	0.000	0.000
31	A	161	VAL	0	-0.012	0.000	74.492	0.012	0.012	0.000	0.000	0.000	0.000
32	A	162	SER	0	-0.024	-0.009	77.976	-0.004	-0.004	0.000	0.000	0.000	0.000
33	A	163	GLU	-1	-0.950	-0.969	81.564	-3.929	-3.929	0.000	0.000	0.000	0.000
34	A	164	PHE	0	-0.026	-0.017	84.402	0.004	0.004	0.000	0.000	0.000	0.000
35	A	165	GLN	0	-0.011	-0.004	88.208	-0.015	-0.015	0.000	0.000	0.000	0.000
36	A	166	TYR	0	0.026	0.019	90.851	0.004	0.004	0.000	0.000	0.000	0.000
37	A	167	ILE	0	-0.054	-0.033	93.942	-0.011	-0.011	0.000	0.000	0.000	0.000
38	A	168	GLU	-1	-0.822	-0.882	95.247	-3.352	-3.352	0.000	0.000	0.000	0.000
39	A	169	THR	0	-0.077	-0.064	97.623	0.046	0.046	0.000	0.000	0.000	0.000
40	A	170	GLU	-1	-0.964	-0.982	97.599	-3.313	-3.313	0.000	0.000	0.000	0.000
41	A	171	THR	0	-0.056	-0.031	99.433	-0.035	-0.035	0.000	0.000	0.000	0.000
42	A	172	ILE	0	0.018	0.013	97.518	0.031	0.031	0.000	0.000	0.000	0.000
43	A	173	SER	0	-0.031	-0.019	100.609	0.013	0.013	0.000	0.000	0.000	0.000
44	A	174	ASN	0	-0.044	-0.031	98.722	0.009	0.009	0.000	0.000	0.000	0.000
45	A	175	THR	0	-0.008	-0.011	99.697	0.026	0.026	0.000	0.000	0.000	0.000
46	A	176	PRO	0	0.019	0.007	99.609	-0.032	-0.032	0.000	0.000	0.000	0.000
47	A	177	SER	0	0.001	-0.041	98.690	0.019	0.019	0.000	0.000	0.000	0.000
48	A	178	PRO	0	-0.052	-0.036	99.829	-0.019	-0.019	0.000	0.000	0.000	0.000
49	A	179	ASP	-1	-0.853	-0.904	97.529	-3.291	-3.291	0.000	0.000	0.000	0.000
50	A	180	LEU	0	-0.029	0.002	93.288	-0.031	-0.031	0.000	0.000	0.000	0.000
51	A	181	THR	0	-0.054	-0.041	96.602	-0.009	-0.009	0.000	0.000	0.000	0.000
52	A	182	VAL	0	0.026	0.024	98.921	0.016	0.016	0.000	0.000	0.000	0.000
53	A	183	MET	0	0.011	0.009	100.745	0.041	0.041	0.000	0.000	0.000	0.000
54	A	184	SER	0	-0.014	-0.021	103.784	0.006	0.006	0.000	0.000	0.000	0.000
55	A	185	ILE	0	0.039	0.005	105.814	0.003	0.003	0.000	0.000	0.000	0.000
56	A	186	ASP	-1	-0.902	-0.921	104.375	-3.109	-3.109	0.000	0.000	0.000	0.000
57	A	187	LYS	1	0.912	0.928	106.511	3.032	3.032	0.000	0.000	0.000	0.000
58	A	188	SER	0	0.013	0.023	110.030	0.025	0.025	0.000	0.000	0.000	0.000
59	A	189	VAL	0	-0.047	-0.042	112.602	0.017	0.017	0.000	0.000	0.000	0.000
60	A	190	LEU	0	-0.022	0.009	114.766	-0.014	-0.014	0.000	0.000	0.000	0.000
61	A	191	SER	0	0.007	-0.015	116.965	0.029	0.029	0.000	0.000	0.000	0.000
62	A	192	PRO	0	-0.044	-0.028	119.502	0.000	0.000	0.000	0.000	0.000	0.000
63	A	193	GLY	0	-0.018	-0.003	121.859	0.007	0.007	0.000	0.000	0.000	0.000
64	A	194	GLU	-1	-0.861	-0.890	114.529	-2.857	-2.857	0.000	0.000	0.000	0.000
65	A	195	SER	0	-0.007	-0.029	114.958	0.020	0.020	0.000	0.000	0.000	0.000
66	A	196	ALA	0	0.012	0.024	112.451	-0.029	-0.029	0.000	0.000	0.000	0.000
67	A	197	THR	0	-0.014	-0.016	109.269	0.018	0.018	0.000	0.000	0.000	0.000
68	A	198	ILE	0	-0.045	-0.010	108.976	-0.026	-0.026	0.000	0.000	0.000	0.000
69	A	199	THR	0	-0.001	-0.008	103.588	0.004	0.004	0.000	0.000	0.000	0.000
70	A	200	THR	0	-0.029	-0.014	104.812	-0.013	-0.013	0.000	0.000	0.000	0.000
71	A	201	ILE	0	0.011	0.018	99.257	0.018	0.018	0.000	0.000	0.000	0.000
72	A	202	VAL	0	-0.033	-0.006	101.207	-0.018	-0.018	0.000	0.000	0.000	0.000
73	A	203	LYS	1	0.904	0.954	93.749	3.443	3.443	0.000	0.000	0.000	0.000
74	A	204	ASP	-1	-0.815	-0.898	96.170	-3.304	-3.304	0.000	0.000	0.000	0.000
75	A	205	ILE	0	-0.020	-0.018	95.557	-0.021	-0.021	0.000	0.000	0.000	0.000
76	A	206	ASP	-1	-0.905	-0.941	90.782	-3.637	-3.637	0.000	0.000	0.000	0.000
77	A	207	GLY	0	0.020	0.010	91.801	-0.035	-0.035	0.000	0.000	0.000	0.000
78	A	208	ASN	0	-0.058	-0.022	92.005	-0.025	-0.025	0.000	0.000	0.000	0.000
79	A	209	PRO	0	-0.013	-0.031	94.086	0.034	0.034	0.000	0.000	0.000	0.000
80	A	210	VAL	0	0.055	0.050	97.233	0.013	0.013	0.000	0.000	0.000	0.000
81	A	211	ASN	0	0.027	0.008	100.696	0.000	0.000	0.000	0.000	0.000	0.000
82	A	212	GLU	-1	-0.864	-0.933	102.986	-2.997	-2.997	0.000	0.000	0.000	0.000
83	A	213	VAL	0	-0.006	-0.006	105.653	-0.009	-0.009	0.000	0.000	0.000	0.000
84	A	214	HIS	0	-0.018	-0.010	108.385	0.028	0.028	0.000	0.000	0.000	0.000
85	A	215	ILE	0	0.021	-0.002	108.451	-0.018	-0.018	0.000	0.000	0.000	0.000
86	A	216	ASN	0	-0.084	-0.030	112.829	0.024	0.024	0.000	0.000	0.000	0.000
87	A	217	LYS	1	0.882	0.947	115.771	2.740	2.740	0.000	0.000	0.000	0.000
88	A	218	THR	0	-0.012	-0.006	117.858	0.021	0.021	0.000	0.000	0.000	0.000
89	A	219	VAL	0	0.017	0.014	118.853	-0.016	-0.016	0.000	0.000	0.000	0.000
90	A	220	ALA	0	0.044	0.034	119.087	0.033	0.033	0.000	0.000	0.000	0.000
91	A	221	ARG	1	0.911	0.944	120.939	2.592	2.592	0.000	0.000	0.000	0.000
92	A	222	GLU	-1	-0.923	-0.945	123.784	-2.603	-2.603	0.000	0.000	0.000	0.000
93	A	223	ASN	0	-0.039	-0.032	125.469	0.038	0.038	0.000	0.000	0.000	0.000
94	A	224	LEU	0	-0.021	-0.025	127.910	-0.013	-0.013	0.000	0.000	0.000	0.000
95	A	225	LYS	1	0.924	0.963	129.438	2.494	2.494	0.000	0.000	0.000	0.000
96	A	226	GLY	0	0.029	0.017	126.233	0.004	0.004	0.000	0.000	0.000	0.000
97	A	227	LEU	0	-0.015	-0.003	126.981	0.007	0.007	0.000	0.000	0.000	0.000
98	A	228	TRP	0	0.023	-0.004	122.008	-0.026	-0.026	0.000	0.000	0.000	0.000
99	A	229	ASP	-1	-0.883	-0.934	123.106	-2.601	-2.601	0.000	0.000	0.000	0.000
100	A	230	TYR	0	-0.031	-0.031	120.027	-0.041	-0.041	0.000	0.000	0.000	0.000
101	A	231	GLY	0	0.035	0.032	119.293	0.011	0.011	0.000	0.000	0.000	0.000
102	A	232	PRO	0	-0.012	-0.017	118.185	-0.008	-0.008	0.000	0.000	0.000	0.000
103	A	233	LEU	0	-0.011	-0.003	111.591	-0.016	-0.016	0.000	0.000	0.000	0.000
104	A	234	LYS	1	0.874	0.934	109.920	2.975	2.975	0.000	0.000	0.000	0.000
105	A	235	LYS	1	0.884	0.936	108.348	2.982	2.982	0.000	0.000	0.000	0.000
106	A	236	GLU	-1	-0.856	-0.922	105.937	-3.042	-3.042	0.000	0.000	0.000	0.000
107	A	237	ASN	0	0.001	-0.007	104.977	-0.006	-0.006	0.000	0.000	0.000	0.000
108	A	238	VAL	0	0.027	0.023	101.409	-0.029	-0.029	0.000	0.000	0.000	0.000
109	A	239	PRO	0	0.049	0.026	98.070	0.026	0.026	0.000	0.000	0.000	0.000
110	A	240	GLY	0	0.055	0.044	100.848	-0.014	-0.014	0.000	0.000	0.000	0.000
111	A	241	LYS	1	0.800	0.905	102.668	3.114	3.114	0.000	0.000	0.000	0.000
112	A	242	TYR	0	0.031	0.022	104.263	0.024	0.024	0.000	0.000	0.000	0.000
113	A	243	THR	0	-0.021	-0.021	107.081	-0.024	-0.024	0.000	0.000	0.000	0.000
114	A	244	GLN	0	0.011	-0.008	109.666	0.045	0.045	0.000	0.000	0.000	0.000
115	A	245	VAL	0	0.017	0.028	113.244	-0.012	-0.012	0.000	0.000	0.000	0.000
116	A	246	ILE	0	-0.020	-0.010	115.268	0.028	0.028	0.000	0.000	0.000	0.000
117	A	247	THR	0	0.044	0.011	117.334	-0.020	-0.020	0.000	0.000	0.000	0.000
118	A	248	TYR	0	-0.023	-0.020	120.002	0.018	0.018	0.000	0.000	0.000	0.000
119	A	249	ARG	1	0.913	0.962	122.261	2.590	2.590	0.000	0.000	0.000	0.000
120	A	250	GLY	0	0.038	0.016	125.486	0.003	0.003	0.000	0.000	0.000	0.000
121	A	251	HIS	0	-0.044	-0.001	126.244	0.011	0.011	0.000	0.000	0.000	0.000
122	A	252	SER	0	0.025	-0.011	126.668	0.015	0.015	0.000	0.000	0.000	0.000
123	A	253	ASN	0	-0.025	0.006	121.951	-0.035	-0.035	0.000	0.000	0.000	0.000
124	A	254	GLU	-1	-0.787	-0.872	122.628	-2.590	-2.590	0.000	0.000	0.000	0.000
125	A	255	ARG	1	0.929	0.951	115.486	2.782	2.782	0.000	0.000	0.000	0.000
126	A	256	ILE	0	-0.018	0.000	118.905	0.026	0.026	0.000	0.000	0.000	0.000
127	A	257	ASP	-1	-0.796	-0.869	114.686	-2.870	-2.870	0.000	0.000	0.000	0.000
128	A	258	ILE	0	-0.041	-0.033	115.565	0.028	0.028	0.000	0.000	0.000	0.000
129	A	259	SER	0	0.025	-0.019	114.469	-0.022	-0.022	0.000	0.000	0.000	0.000
130	A	260	PHE	0	-0.066	-0.041	110.557	0.018	0.018	0.000	0.000	0.000	0.000
131	A	261	LYS	1	0.933	0.971	112.240	2.808	2.808	0.000	0.000	0.000	0.000
132	A	262	TYR	0	0.017	-0.008	106.447	0.018	0.018	0.000	0.000	0.000	0.000
133	A	263	ALA	0	0.087	0.025	108.319	0.029	0.029	0.000	0.000	0.000	0.000
134	A	264	MET	0	-0.034	-0.020	110.462	0.006	0.006	0.000	0.000	0.000	0.000
135	A	265	SER	0	-0.001	0.003	106.815	-0.009	-0.009	0.000	0.000	0.000	0.000
136	A	266	PHE	0	0.036	0.013	104.112	-0.006	-0.006	0.000	0.000	0.000	0.000
137	A	267	THR	0	-0.065	-0.029	108.734	0.033	0.033	0.000	0.000	0.000	0.000
138	A	268	LYS	1	0.887	0.957	106.559	3.025	3.025	0.000	0.000	0.000	0.000
139	A	269	GLU	-1	-0.846	-0.900	110.099	-2.813	-2.813	0.000	0.000	0.000	0.000
140	A	270	ILE	0	-0.061	-0.026	109.373	-0.042	-0.042	0.000	0.000	0.000	0.000
141	A	271	SER	0	0.024	-0.006	111.830	0.020	0.020	0.000	0.000	0.000	0.000
142	A	272	ILE	0	-0.050	-0.018	113.289	-0.019	-0.019	0.000	0.000	0.000	0.000
143	A	273	ARG	1	0.924	0.953	115.681	2.795	2.795	0.000	0.000	0.000	0.000
144	A	274	GLY	0	0.014	0.011	117.777	-0.012	-0.012	0.000	0.000	0.000	0.000
145	A	275	ARG	1	0.872	0.931	116.915	2.769	2.769	0.000	0.000	0.000	0.000
146	A	276	LEU	-1	-0.900	-0.952	120.470	-2.654	-2.654	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:131:GLY)