FMO DATABASE

FMODB ID: 7Y7VK

Calculation Name: 1V5J-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1V5J

Chain ID: A

ChEMBL ID:

UniProt ID: Q9P2J2

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	108
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-712549.628554
FMO2-HF: Nuclear repulsion	674111.557548
FMO2-HF: Total energy	-38438.071006
FMO2-MP2: Total energy	-38553.259426

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.
-57.926	-57.131	-0.003	-0.326	-0.466	-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 : 0.870 / q_NPA : 0.918

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	0.053	0.037	3.856	-1.342	-0.547	-0.003	-0.326	-0.466	-0.001
4	A	4	GLY	0	0.042	0.034	5.917	5.680	5.680	0.000	0.000	0.000	0.000
5	A	5	SER	0	-0.051	-0.048	7.789	-2.255	-2.255	0.000	0.000	0.000	0.000
6	A	6	SER	0	-0.020	0.001	10.319	2.268	2.268	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.028	0.010	12.976	-0.686	-0.686	0.000	0.000	0.000	0.000
8	A	8	LEU	0	-0.050	-0.001	14.606	1.286	1.286	0.000	0.000	0.000	0.000
9	A	9	SER	0	-0.045	-0.022	14.136	-1.158	-1.158	0.000	0.000	0.000	0.000
10	A	10	PRO	0	0.050	0.016	13.498	0.583	0.583	0.000	0.000	0.000	0.000
11	A	11	PRO	0	-0.009	0.003	15.997	0.587	0.587	0.000	0.000	0.000	0.000
12	A	12	ARG	1	0.932	0.951	18.564	14.047	14.047	0.000	0.000	0.000	0.000
13	A	13	GLY	0	0.043	0.025	21.035	0.432	0.432	0.000	0.000	0.000	0.000
14	A	14	LEU	0	0.003	0.021	20.742	0.551	0.551	0.000	0.000	0.000	0.000
15	A	15	VAL	0	-0.034	-0.016	23.644	-0.083	-0.083	0.000	0.000	0.000	0.000
16	A	16	ALA	0	0.024	0.005	26.822	0.024	0.024	0.000	0.000	0.000	0.000
17	A	17	VAL	0	0.005	0.007	29.110	0.215	0.215	0.000	0.000	0.000	0.000
18	A	18	ARG	1	0.918	0.950	32.957	9.007	9.007	0.000	0.000	0.000	0.000
19	A	19	THR	0	-0.036	-0.021	34.961	0.343	0.343	0.000	0.000	0.000	0.000
20	A	20	PRO	0	0.019	-0.002	37.950	-0.066	-0.066	0.000	0.000	0.000	0.000
21	A	21	ARG	1	0.951	0.966	39.336	7.656	7.656	0.000	0.000	0.000	0.000
22	A	22	GLY	0	0.030	0.019	35.912	-0.066	-0.066	0.000	0.000	0.000	0.000
23	A	23	VAL	0	-0.043	-0.004	30.512	0.208	0.208	0.000	0.000	0.000	0.000
24	A	24	LEU	0	-0.003	0.018	32.137	-0.113	-0.113	0.000	0.000	0.000	0.000
25	A	25	LEU	0	-0.032	0.001	26.323	-0.132	-0.132	0.000	0.000	0.000	0.000
26	A	26	HIS	0	0.029	0.001	28.111	0.121	0.121	0.000	0.000	0.000	0.000
27	A	27	TRP	0	-0.026	-0.011	23.522	-0.479	-0.479	0.000	0.000	0.000	0.000
28	A	28	ASP	-1	-0.873	-0.932	24.093	-11.410	-11.410	0.000	0.000	0.000	0.000
29	A	29	PRO	0	-0.019	-0.012	22.984	-0.665	-0.665	0.000	0.000	0.000	0.000
30	A	30	PRO	0	-0.062	-0.021	19.079	0.014	0.014	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.932	-0.973	21.027	-11.741	-11.741	0.000	0.000	0.000	0.000
32	A	32	LEU	0	-0.051	-0.019	17.681	0.133	0.133	0.000	0.000	0.000	0.000
33	A	33	VAL	0	0.079	0.037	18.830	-0.843	-0.843	0.000	0.000	0.000	0.000
34	A	34	PRO	0	-0.018	-0.003	17.873	0.442	0.442	0.000	0.000	0.000	0.000
35	A	35	LYS	1	0.931	0.948	20.258	12.770	12.770	0.000	0.000	0.000	0.000
36	A	36	ARG	1	0.925	0.967	23.486	11.264	11.264	0.000	0.000	0.000	0.000
37	A	37	LEU	0	-0.011	0.021	21.043	-0.537	-0.537	0.000	0.000	0.000	0.000
38	A	38	ASP	-1	-0.934	-0.975	22.354	-12.860	-12.860	0.000	0.000	0.000	0.000
39	A	39	GLY	0	0.003	-0.017	22.506	0.702	0.702	0.000	0.000	0.000	0.000
40	A	40	TYR	0	0.011	0.003	20.641	-1.086	-1.086	0.000	0.000	0.000	0.000
41	A	41	VAL	0	-0.027	0.009	18.049	0.610	0.610	0.000	0.000	0.000	0.000
42	A	42	LEU	0	0.006	0.006	20.276	-0.556	-0.556	0.000	0.000	0.000	0.000
43	A	43	GLU	-1	-0.850	-0.910	17.277	-18.281	-18.281	0.000	0.000	0.000	0.000
44	A	44	GLY	0	0.050	0.003	21.177	-0.053	-0.053	0.000	0.000	0.000	0.000
45	A	45	ARG	1	0.821	0.922	18.673	15.257	15.257	0.000	0.000	0.000	0.000
46	A	46	GLN	0	0.026	0.014	24.177	0.259	0.259	0.000	0.000	0.000	0.000
47	A	47	GLY	0	0.034	0.014	25.146	-0.053	-0.053	0.000	0.000	0.000	0.000
48	A	48	SER	0	-0.011	-0.008	22.047	-0.341	-0.341	0.000	0.000	0.000	0.000
49	A	49	GLN	0	-0.042	-0.015	22.451	-0.317	-0.317	0.000	0.000	0.000	0.000
50	A	50	GLY	0	-0.005	-0.009	20.355	-0.758	-0.758	0.000	0.000	0.000	0.000
51	A	51	TRP	0	-0.027	-0.025	16.609	0.260	0.260	0.000	0.000	0.000	0.000
52	A	52	GLU	-1	-0.880	-0.938	20.025	-12.287	-12.287	0.000	0.000	0.000	0.000
53	A	53	VAL	0	0.002	-0.028	19.972	-0.186	-0.186	0.000	0.000	0.000	0.000
54	A	54	LEU	0	-0.046	-0.010	22.579	0.521	0.521	0.000	0.000	0.000	0.000
55	A	55	ASP	-1	-0.839	-0.931	24.544	-10.872	-10.872	0.000	0.000	0.000	0.000
56	A	56	PRO	0	-0.041	-0.020	22.077	-0.483	-0.483	0.000	0.000	0.000	0.000
57	A	57	ALA	0	-0.032	-0.007	23.100	-0.408	-0.408	0.000	0.000	0.000	0.000
58	A	58	VAL	0	0.039	0.030	24.898	0.584	0.584	0.000	0.000	0.000	0.000
59	A	59	ALA	0	0.042	0.019	25.636	-0.358	-0.358	0.000	0.000	0.000	0.000
60	A	60	GLY	0	0.033	0.013	24.838	-0.166	-0.166	0.000	0.000	0.000	0.000
61	A	61	THR	0	-0.086	-0.062	25.655	-0.245	-0.245	0.000	0.000	0.000	0.000
62	A	62	GLU	-1	-0.855	-0.927	27.881	-9.925	-9.925	0.000	0.000	0.000	0.000
63	A	63	THR	0	-0.074	-0.032	26.958	-0.319	-0.319	0.000	0.000	0.000	0.000
64	A	64	GLU	-1	-0.962	-0.987	28.502	-9.650	-9.650	0.000	0.000	0.000	0.000
65	A	65	LEU	0	0.102	0.045	27.672	-0.117	-0.117	0.000	0.000	0.000	0.000
66	A	66	LEU	0	-0.054	-0.018	30.361	0.001	0.001	0.000	0.000	0.000	0.000
67	A	67	VAL	0	0.058	0.019	28.027	-0.032	-0.032	0.000	0.000	0.000	0.000
68	A	68	PRO	0	-0.006	-0.021	31.455	0.059	0.059	0.000	0.000	0.000	0.000
69	A	69	GLY	0	-0.041	0.005	32.355	0.207	0.207	0.000	0.000	0.000	0.000
70	A	70	LEU	0	-0.021	-0.008	29.359	-0.324	-0.324	0.000	0.000	0.000	0.000
71	A	71	ILE	0	-0.058	-0.019	32.024	0.377	0.377	0.000	0.000	0.000	0.000
72	A	72	LYS	1	0.877	0.921	33.412	7.878	7.878	0.000	0.000	0.000	0.000
73	A	73	ASP	-1	-0.833	-0.928	35.336	-8.350	-8.350	0.000	0.000	0.000	0.000
74	A	74	VAL	0	-0.051	-0.009	30.739	-0.162	-0.162	0.000	0.000	0.000	0.000
75	A	75	LEU	0	-0.028	-0.014	26.811	0.165	0.165	0.000	0.000	0.000	0.000
76	A	76	TYR	0	0.021	0.009	26.884	-0.243	-0.243	0.000	0.000	0.000	0.000
77	A	77	GLU	-1	-0.837	-0.917	20.998	-14.711	-14.711	0.000	0.000	0.000	0.000
78	A	78	PHE	0	0.028	-0.005	22.848	0.285	0.285	0.000	0.000	0.000	0.000
79	A	79	ARG	1	0.806	0.893	15.238	18.801	18.801	0.000	0.000	0.000	0.000
80	A	80	LEU	0	0.039	0.037	19.363	0.206	0.206	0.000	0.000	0.000	0.000
81	A	81	VAL	0	0.028	0.038	15.119	-0.423	-0.423	0.000	0.000	0.000	0.000
82	A	82	ALA	0	0.035	0.031	17.101	0.882	0.882	0.000	0.000	0.000	0.000
83	A	83	PHE	0	0.003	-0.003	16.613	-1.522	-1.522	0.000	0.000	0.000	0.000
84	A	84	ALA	0	0.032	0.004	18.276	1.038	1.038	0.000	0.000	0.000	0.000
85	A	85	GLY	0	0.018	0.016	19.285	-0.511	-0.511	0.000	0.000	0.000	0.000
86	A	86	SER	0	-0.056	-0.030	17.581	-0.479	-0.479	0.000	0.000	0.000	0.000
87	A	87	PHE	0	-0.064	-0.031	14.814	-1.369	-1.369	0.000	0.000	0.000	0.000
88	A	88	VAL	0	0.036	0.010	11.785	1.085	1.085	0.000	0.000	0.000	0.000
89	A	89	SER	0	-0.048	-0.025	12.434	-0.881	-0.881	0.000	0.000	0.000	0.000
90	A	90	ASP	-1	-0.874	-0.950	9.398	-30.872	-30.872	0.000	0.000	0.000	0.000
91	A	91	PRO	0	-0.052	-0.035	11.970	1.735	1.735	0.000	0.000	0.000	0.000
92	A	92	SER	0	-0.015	-0.022	14.862	-0.238	-0.238	0.000	0.000	0.000	0.000
93	A	93	ASN	0	-0.072	-0.043	17.207	-0.211	-0.211	0.000	0.000	0.000	0.000
94	A	94	THR	0	0.000	-0.003	18.299	0.225	0.225	0.000	0.000	0.000	0.000
95	A	95	ALA	0	-0.003	0.028	20.273	0.444	0.444	0.000	0.000	0.000	0.000
96	A	96	ASN	0	-0.006	-0.026	23.984	0.165	0.165	0.000	0.000	0.000	0.000
97	A	97	VAL	0	0.006	0.016	26.379	0.364	0.364	0.000	0.000	0.000	0.000
98	A	98	SER	0	0.007	0.001	29.971	0.045	0.045	0.000	0.000	0.000	0.000
99	A	99	THR	0	-0.013	-0.026	32.894	0.248	0.248	0.000	0.000	0.000	0.000
100	A	100	SER	0	-0.018	0.003	35.499	0.156	0.156	0.000	0.000	0.000	0.000
101	A	101	GLY	0	0.059	0.026	38.007	0.181	0.181	0.000	0.000	0.000	0.000
102	A	102	LEU	0	-0.033	0.000	37.513	0.105	0.105	0.000	0.000	0.000	0.000
103	A	103	SER	0	-0.030	-0.028	40.215	0.110	0.110	0.000	0.000	0.000	0.000
104	A	104	GLY	0	0.040	0.023	43.144	0.124	0.124	0.000	0.000	0.000	0.000
105	A	105	PRO	0	-0.038	-0.008	45.704	-0.018	-0.018	0.000	0.000	0.000	0.000
106	A	106	SER	0	-0.015	-0.021	44.360	-0.167	-0.167	0.000	0.000	0.000	0.000
107	A	107	SER	0	-0.071	-0.039	46.366	0.166	0.166	0.000	0.000	0.000	0.000
108	A	108	GLY	-1	-0.894	-0.926	43.014	-7.392	-7.392	0.000	0.000	0.000	0.000

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