FMO DATABASE

FMODB ID: LVZY9

Calculation Name: 1V38-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1V38

Chain ID: A

ChEMBL ID:

UniProt ID: P57725

Base Structure: SolutionNMR

Registration Date: 2025-10-05

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	78
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-471370.170951
FMO2-HF: Nuclear repulsion	441457.199727
FMO2-HF: Total energy	-29912.971224
FMO2-MP2: Total energy	-30001.909139

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.
-149.639	-147.537	0.145	-1.324	-0.923	-0.013

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 : 0.853 / q_NPA : 0.917

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	SER	0	-0.026	-0.013	2.811	-14.570	-12.468	0.145	-1.324	-0.923	-0.013
4	A	4	GLY	0	0.049	0.036	5.431	1.729	1.729	0.000	0.000	0.000	0.000
5	A	5	SER	0	0.001	0.003	5.330	-6.524	-6.524	0.000	0.000	0.000	0.000
6	A	6	SER	0	0.016	-0.010	6.146	2.978	2.978	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.005	0.007	8.559	3.375	3.375	0.000	0.000	0.000	0.000
8	A	8	ARG	1	0.811	0.917	8.967	16.204	16.204	0.000	0.000	0.000	0.000
9	A	9	ARG	1	0.975	0.984	8.053	29.266	29.266	0.000	0.000	0.000	0.000
10	A	10	GLU	-1	-0.883	-0.955	11.219	-16.061	-16.061	0.000	0.000	0.000	0.000
11	A	11	ASN	0	0.008	0.006	14.243	0.004	0.004	0.000	0.000	0.000	0.000
12	A	12	HIS	0	0.046	0.034	11.455	-1.081	-1.081	0.000	0.000	0.000	0.000
13	A	13	GLN	0	0.055	0.039	10.913	-3.557	-3.557	0.000	0.000	0.000	0.000
14	A	14	THR	0	0.021	-0.009	6.928	0.742	0.742	0.000	0.000	0.000	0.000
15	A	15	ILE	0	0.024	0.014	9.998	0.897	0.897	0.000	0.000	0.000	0.000
16	A	16	GLN	0	0.050	0.024	6.983	1.933	1.933	0.000	0.000	0.000	0.000
17	A	17	GLU	-1	-0.915	-0.970	7.050	-33.165	-33.165	0.000	0.000	0.000	0.000
18	A	18	PHE	0	-0.060	-0.032	10.486	1.892	1.892	0.000	0.000	0.000	0.000
19	A	19	LEU	0	0.007	0.015	13.064	1.453	1.453	0.000	0.000	0.000	0.000
20	A	20	GLU	-1	-0.870	-0.927	10.559	-23.232	-23.232	0.000	0.000	0.000	0.000
21	A	21	ARG	1	0.880	0.948	13.914	18.198	18.198	0.000	0.000	0.000	0.000
22	A	22	ILE	0	-0.068	-0.019	16.538	1.028	1.028	0.000	0.000	0.000	0.000
23	A	23	HIS	0	-0.087	-0.054	17.303	1.281	1.281	0.000	0.000	0.000	0.000
24	A	24	LEU	0	0.037	0.042	17.457	0.339	0.339	0.000	0.000	0.000	0.000
25	A	25	GLN	0	-0.045	-0.035	12.402	0.819	0.819	0.000	0.000	0.000	0.000
26	A	26	GLU	-1	-0.916	-0.940	14.422	-15.681	-15.681	0.000	0.000	0.000	0.000
27	A	27	TYR	0	-0.007	-0.022	17.134	-0.203	-0.203	0.000	0.000	0.000	0.000
28	A	28	THR	0	-0.039	-0.044	10.502	-0.592	-0.592	0.000	0.000	0.000	0.000
29	A	29	SER	0	-0.026	-0.011	13.868	-0.294	-0.294	0.000	0.000	0.000	0.000
30	A	30	THR	0	0.027	0.015	14.717	-0.102	-0.102	0.000	0.000	0.000	0.000
31	A	31	LEU	0	0.032	0.022	15.380	0.469	0.469	0.000	0.000	0.000	0.000
32	A	32	LEU	0	-0.020	-0.012	9.851	-0.216	-0.216	0.000	0.000	0.000	0.000
33	A	33	LEU	0	-0.074	-0.040	14.082	0.161	0.161	0.000	0.000	0.000	0.000
34	A	34	ASN	0	-0.085	-0.049	16.865	1.324	1.324	0.000	0.000	0.000	0.000
35	A	35	GLY	0	-0.009	0.005	16.238	0.762	0.762	0.000	0.000	0.000	0.000
36	A	36	TYR	0	0.020	0.002	15.763	-0.171	-0.171	0.000	0.000	0.000	0.000
37	A	37	GLU	-1	-0.948	-0.970	10.080	-27.944	-27.944	0.000	0.000	0.000	0.000
38	A	38	THR	0	-0.106	-0.092	10.083	-2.244	-2.244	0.000	0.000	0.000	0.000
39	A	39	LEU	0	0.014	-0.012	12.549	1.221	1.221	0.000	0.000	0.000	0.000
40	A	40	ASP	-1	-0.940	-0.945	14.818	-17.738	-17.738	0.000	0.000	0.000	0.000
41	A	41	ASP	-1	-0.814	-0.906	15.776	-17.114	-17.114	0.000	0.000	0.000	0.000
42	A	42	LEU	0	-0.052	-0.035	16.128	0.784	0.784	0.000	0.000	0.000	0.000
43	A	43	LYS	1	0.898	0.960	19.303	14.644	14.644	0.000	0.000	0.000	0.000
44	A	44	ASP	-1	-0.920	-0.948	21.835	-12.192	-12.192	0.000	0.000	0.000	0.000
45	A	45	ILE	0	-0.118	-0.036	20.434	0.281	0.281	0.000	0.000	0.000	0.000
46	A	46	LYS	0	0.050	0.010	23.555	0.344	0.344	0.000	0.000	0.000	0.000
47	A	47	GLU	-1	-0.873	-0.933	26.375	-10.157	-10.157	0.000	0.000	0.000	0.000
48	A	48	SER	0	0.002	-0.008	28.148	-0.003	-0.003	0.000	0.000	0.000	0.000
49	A	49	HIS	0	0.036	0.016	24.425	0.203	0.203	0.000	0.000	0.000	0.000
50	A	50	LEU	0	0.005	0.009	22.197	-0.296	-0.296	0.000	0.000	0.000	0.000
51	A	51	ILE	0	-0.019	-0.004	24.882	-0.099	-0.099	0.000	0.000	0.000	0.000
52	A	52	GLU	-1	-0.947	-0.968	26.776	-10.540	-10.540	0.000	0.000	0.000	0.000
53	A	53	LEU	0	-0.087	-0.032	20.523	-0.316	-0.316	0.000	0.000	0.000	0.000
54	A	54	ASN	0	-0.039	-0.033	22.633	-0.099	-0.099	0.000	0.000	0.000	0.000
55	A	55	ILE	0	0.021	0.025	20.927	0.029	0.029	0.000	0.000	0.000	0.000
56	A	56	ALA	0	0.008	-0.011	25.133	0.321	0.321	0.000	0.000	0.000	0.000
57	A	57	ASP	-1	-0.876	-0.924	27.187	-10.208	-10.208	0.000	0.000	0.000	0.000
58	A	58	PRO	0	-0.030	-0.029	27.626	-0.294	-0.294	0.000	0.000	0.000	0.000
59	A	59	GLU	-1	-0.968	-0.986	27.276	-10.720	-10.720	0.000	0.000	0.000	0.000
60	A	60	ASP	-1	-0.801	-0.895	23.043	-13.030	-13.030	0.000	0.000	0.000	0.000
61	A	61	ARG	1	0.808	0.895	23.560	10.117	10.117	0.000	0.000	0.000	0.000
62	A	62	ALA	0	0.007	0.005	25.156	-0.210	-0.210	0.000	0.000	0.000	0.000
63	A	63	ARG	1	0.922	0.960	22.299	12.263	12.263	0.000	0.000	0.000	0.000
64	A	64	LEU	0	0.022	0.012	19.300	-0.461	-0.461	0.000	0.000	0.000	0.000
65	A	65	LEU	0	0.012	-0.002	21.566	-0.347	-0.347	0.000	0.000	0.000	0.000
66	A	66	SER	0	0.023	0.023	23.969	-0.173	-0.173	0.000	0.000	0.000	0.000
67	A	67	ALA	0	-0.022	-0.012	19.698	-0.047	-0.047	0.000	0.000	0.000	0.000
68	A	68	ALA	0	0.015	0.002	20.023	-0.379	-0.379	0.000	0.000	0.000	0.000
69	A	69	GLU	-1	-0.933	-0.978	21.005	-11.133	-11.133	0.000	0.000	0.000	0.000
70	A	70	SER	0	-0.061	-0.033	22.735	0.073	0.073	0.000	0.000	0.000	0.000
71	A	71	LEU	0	-0.054	-0.028	16.994	-0.268	-0.268	0.000	0.000	0.000	0.000
72	A	72	LEU	0	-0.026	0.014	19.138	-0.191	-0.191	0.000	0.000	0.000	0.000
73	A	73	SER	0	-0.059	-0.033	22.120	0.294	0.294	0.000	0.000	0.000	0.000
74	A	74	GLY	0	0.054	0.020	24.417	0.418	0.418	0.000	0.000	0.000	0.000
75	A	75	PRO	0	-0.068	-0.010	23.822	-0.425	-0.425	0.000	0.000	0.000	0.000
76	A	76	SER	0	-0.052	-0.035	22.392	0.359	0.359	0.000	0.000	0.000	0.000
77	A	77	SER	0	-0.050	-0.033	23.133	-0.323	-0.323	0.000	0.000	0.000	0.000
78	A	78	GLY	-1	-0.937	-0.953	21.867	-13.444	-13.444	0.000	0.000	0.000	0.000

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