FMO DATABASE

FMODB ID: 15KMZ

Calculation Name: 1V32-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1V32

Chain ID: A

ChEMBL ID:

UniProt ID: Q9FT92

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	101
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-718370.129792
FMO2-HF: Nuclear repulsion	678448.580039
FMO2-HF: Total energy	-39921.549752
FMO2-MP2: Total energy	-40037.954201

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.
30.539	31.719	-0.014	-0.535	-0.631	-0.002

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 : 0.875 / q_NPA : 0.925

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	0.036	0.013	3.848	5.045	6.225	-0.014	-0.535	-0.631	-0.002
4	A	4	GLY	0	0.030	0.029	6.770	0.380	0.380	0.000	0.000	0.000	0.000
5	A	5	SER	0	-0.002	0.003	9.238	-1.278	-1.278	0.000	0.000	0.000	0.000
6	A	6	SER	0	0.017	-0.013	11.835	1.591	1.591	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.000	0.005	15.544	-0.245	-0.245	0.000	0.000	0.000	0.000
8	A	8	LYS	1	0.928	0.959	18.389	12.215	12.215	0.000	0.000	0.000	0.000
9	A	9	ARG	1	0.983	1.000	21.446	13.470	13.470	0.000	0.000	0.000	0.000
10	A	10	PHE	0	0.031	0.008	22.514	0.399	0.399	0.000	0.000	0.000	0.000
11	A	11	GLU	-1	-0.879	-0.930	25.192	-10.659	-10.659	0.000	0.000	0.000	0.000
12	A	12	PHE	0	-0.050	-0.030	25.615	-0.058	-0.058	0.000	0.000	0.000	0.000
13	A	13	VAL	0	-0.026	-0.001	19.155	-0.352	-0.352	0.000	0.000	0.000	0.000
14	A	14	GLY	0	0.030	0.017	21.349	-0.264	-0.264	0.000	0.000	0.000	0.000
15	A	15	TRP	0	0.038	0.013	21.143	0.871	0.871	0.000	0.000	0.000	0.000
16	A	16	GLY	0	0.036	0.022	24.039	0.575	0.575	0.000	0.000	0.000	0.000
17	A	17	SER	0	0.016	0.013	24.775	-0.519	-0.519	0.000	0.000	0.000	0.000
18	A	18	ARG	1	0.981	0.968	19.133	14.614	14.614	0.000	0.000	0.000	0.000
19	A	19	GLN	0	-0.026	-0.009	23.572	-0.333	-0.333	0.000	0.000	0.000	0.000
20	A	20	LEU	0	0.023	0.011	25.639	-0.088	-0.088	0.000	0.000	0.000	0.000
21	A	21	ILE	0	-0.002	0.008	19.767	-0.155	-0.155	0.000	0.000	0.000	0.000
22	A	22	GLU	-1	-0.940	-0.968	20.001	-14.673	-14.673	0.000	0.000	0.000	0.000
23	A	23	PHE	0	-0.034	-0.019	21.398	-0.166	-0.166	0.000	0.000	0.000	0.000
24	A	24	LEU	0	-0.011	-0.015	21.920	0.000	0.000	0.000	0.000	0.000	0.000
25	A	25	HIS	0	0.033	0.011	16.047	0.085	0.085	0.000	0.000	0.000	0.000
26	A	26	SER	0	-0.058	-0.024	18.547	-0.265	-0.265	0.000	0.000	0.000	0.000
27	A	27	LEU	0	-0.083	-0.040	20.678	0.121	0.121	0.000	0.000	0.000	0.000
28	A	28	GLY	0	-0.003	0.015	18.314	0.191	0.191	0.000	0.000	0.000	0.000
29	A	29	LYS	1	0.782	0.890	19.111	12.088	12.088	0.000	0.000	0.000	0.000
30	A	30	ASP	-1	-0.849	-0.933	15.625	-19.091	-19.091	0.000	0.000	0.000	0.000
31	A	31	THR	0	-0.053	-0.036	17.745	0.493	0.493	0.000	0.000	0.000	0.000
32	A	32	SER	0	-0.026	0.003	16.049	0.357	0.357	0.000	0.000	0.000	0.000
33	A	33	GLU	-1	-0.874	-0.942	17.673	-12.933	-12.933	0.000	0.000	0.000	0.000
34	A	34	MET	0	-0.049	-0.020	21.264	0.185	0.185	0.000	0.000	0.000	0.000
35	A	35	ILE	0	0.014	0.015	21.880	0.451	0.451	0.000	0.000	0.000	0.000
36	A	36	SER	0	0.058	0.038	25.650	0.282	0.282	0.000	0.000	0.000	0.000
37	A	37	ARG	1	0.902	0.964	29.464	9.038	9.038	0.000	0.000	0.000	0.000
38	A	38	TYR	0	0.033	0.010	31.304	-0.009	-0.009	0.000	0.000	0.000	0.000
39	A	39	ASP	-1	-0.833	-0.903	27.493	-11.187	-11.187	0.000	0.000	0.000	0.000
40	A	40	VAL	0	0.023	0.012	26.441	-0.115	-0.115	0.000	0.000	0.000	0.000
41	A	41	SER	0	0.021	-0.010	28.978	0.107	0.107	0.000	0.000	0.000	0.000
42	A	42	ASP	-1	-0.949	-0.962	31.781	-9.334	-9.334	0.000	0.000	0.000	0.000
43	A	43	THR	0	-0.022	-0.017	26.160	-0.123	-0.123	0.000	0.000	0.000	0.000
44	A	44	ILE	0	0.003	0.005	29.605	-0.032	-0.032	0.000	0.000	0.000	0.000
45	A	45	ALA	0	-0.041	-0.022	31.307	0.160	0.160	0.000	0.000	0.000	0.000
46	A	46	LYS	1	0.953	0.972	30.081	10.214	10.214	0.000	0.000	0.000	0.000
47	A	47	TYR	0	-0.045	-0.056	28.453	0.084	0.084	0.000	0.000	0.000	0.000
48	A	48	ILE	0	-0.001	-0.010	30.890	0.105	0.105	0.000	0.000	0.000	0.000
49	A	49	SER	0	-0.036	-0.023	34.286	0.215	0.215	0.000	0.000	0.000	0.000
50	A	50	LYS	1	0.884	0.942	29.858	10.236	10.236	0.000	0.000	0.000	0.000
51	A	51	GLU	-1	-0.803	-0.879	29.739	-10.832	-10.832	0.000	0.000	0.000	0.000
52	A	52	GLY	0	-0.004	0.017	33.269	0.152	0.152	0.000	0.000	0.000	0.000
53	A	53	LEU	0	0.004	0.002	32.817	0.186	0.186	0.000	0.000	0.000	0.000
54	A	54	LEU	0	-0.063	-0.029	37.141	0.183	0.183	0.000	0.000	0.000	0.000
55	A	55	ASP	-1	-0.837	-0.922	40.221	-7.022	-7.022	0.000	0.000	0.000	0.000
56	A	56	PRO	0	-0.039	-0.025	43.445	0.087	0.087	0.000	0.000	0.000	0.000
57	A	57	SER	0	-0.006	0.013	46.127	0.183	0.183	0.000	0.000	0.000	0.000
58	A	58	ASN	0	0.004	-0.014	47.087	0.080	0.080	0.000	0.000	0.000	0.000
59	A	59	LYS	1	1.028	1.023	43.721	6.879	6.879	0.000	0.000	0.000	0.000
60	A	60	LYS	1	0.937	0.965	43.034	6.597	6.597	0.000	0.000	0.000	0.000
61	A	61	LYS	1	0.902	0.957	42.966	6.746	6.746	0.000	0.000	0.000	0.000
62	A	62	VAL	0	-0.006	-0.001	36.741	-0.035	-0.035	0.000	0.000	0.000	0.000
63	A	63	VAL	0	0.021	0.009	39.457	0.110	0.110	0.000	0.000	0.000	0.000
64	A	64	CYS	0	-0.087	-0.043	35.635	-0.211	-0.211	0.000	0.000	0.000	0.000
65	A	65	ASP	-1	-0.868	-0.928	33.704	-9.109	-9.109	0.000	0.000	0.000	0.000
66	A	66	LYS	1	0.965	0.979	28.309	11.023	11.023	0.000	0.000	0.000	0.000
67	A	67	ARG	1	0.916	0.960	24.034	12.207	12.207	0.000	0.000	0.000	0.000
68	A	68	LEU	0	0.052	0.020	29.424	-0.051	-0.051	0.000	0.000	0.000	0.000
69	A	69	VAL	0	-0.024	0.010	32.213	0.142	0.142	0.000	0.000	0.000	0.000
70	A	70	LEU	0	0.022	-0.010	27.256	0.082	0.082	0.000	0.000	0.000	0.000
71	A	71	LEU	0	-0.011	0.030	27.939	-0.149	-0.149	0.000	0.000	0.000	0.000
72	A	72	PHE	0	0.009	-0.020	30.145	0.068	0.068	0.000	0.000	0.000	0.000
73	A	73	GLY	0	0.033	0.033	33.837	0.176	0.176	0.000	0.000	0.000	0.000
74	A	74	THR	0	-0.020	-0.013	35.617	0.183	0.183	0.000	0.000	0.000	0.000
75	A	75	ARG	1	1.003	0.987	37.358	8.026	8.026	0.000	0.000	0.000	0.000
76	A	76	THR	0	0.013	0.006	39.865	0.032	0.032	0.000	0.000	0.000	0.000
77	A	77	ILE	0	-0.004	0.010	36.423	0.036	0.036	0.000	0.000	0.000	0.000
78	A	78	PHE	0	0.009	-0.008	40.736	0.136	0.136	0.000	0.000	0.000	0.000
79	A	79	ARG	1	0.984	0.977	38.623	7.816	7.816	0.000	0.000	0.000	0.000
80	A	80	MET	0	0.006	0.002	38.713	-0.097	-0.097	0.000	0.000	0.000	0.000
81	A	81	LYS	1	0.973	0.986	39.708	7.267	7.267	0.000	0.000	0.000	0.000
82	A	82	VAL	0	-0.007	0.016	33.838	-0.106	-0.106	0.000	0.000	0.000	0.000
83	A	83	TYR	0	0.040	0.023	35.039	-0.326	-0.326	0.000	0.000	0.000	0.000
84	A	84	ASP	-1	-0.864	-0.938	35.771	-7.952	-7.952	0.000	0.000	0.000	0.000
85	A	85	LEU	0	-0.061	-0.039	35.270	-0.051	-0.051	0.000	0.000	0.000	0.000
86	A	86	LEU	0	-0.031	-0.030	30.030	-0.259	-0.259	0.000	0.000	0.000	0.000
87	A	87	GLU	-1	-0.855	-0.909	32.492	-8.603	-8.603	0.000	0.000	0.000	0.000
88	A	88	LYS	1	0.928	0.978	35.066	8.253	8.253	0.000	0.000	0.000	0.000
89	A	89	HIS	0	-0.022	-0.018	29.583	-0.326	-0.326	0.000	0.000	0.000	0.000
90	A	90	TYR	0	-0.071	-0.072	27.849	-0.440	-0.440	0.000	0.000	0.000	0.000
91	A	91	LYS	1	0.874	0.947	27.583	11.237	11.237	0.000	0.000	0.000	0.000
92	A	92	GLU	-1	-0.876	-0.940	30.407	-9.242	-9.242	0.000	0.000	0.000	0.000
93	A	93	ASN	0	-0.091	-0.044	32.216	0.213	0.213	0.000	0.000	0.000	0.000
94	A	94	GLN	0	0.006	-0.010	35.865	-0.155	-0.155	0.000	0.000	0.000	0.000
95	A	95	ASP	-1	-0.944	-0.953	38.317	-7.486	-7.486	0.000	0.000	0.000	0.000
96	A	96	SER	0	0.004	-0.029	41.868	-0.003	-0.003	0.000	0.000	0.000	0.000
97	A	97	GLY	0	-0.018	0.029	44.697	0.003	0.003	0.000	0.000	0.000	0.000
98	A	98	PRO	0	-0.036	-0.032	48.337	0.013	0.013	0.000	0.000	0.000	0.000
99	A	99	SER	0	-0.031	-0.027	50.909	0.023	0.023	0.000	0.000	0.000	0.000
100	A	100	SER	0	-0.002	-0.014	46.338	-0.179	-0.179	0.000	0.000	0.000	0.000
101	A	101	GLY	-1	-0.955	-0.952	46.687	-6.659	-6.659	0.000	0.000	0.000	0.000

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