FMO DATABASE

FMODB ID: 9L9V2

Calculation Name: 1V5P-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1V5P

Chain ID: A

ChEMBL ID:

UniProt ID: Q9ERS5

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	126
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1014287.809811
FMO2-HF: Nuclear repulsion	965061.871893
FMO2-HF: Total energy	-49225.937918
FMO2-MP2: Total energy	-49368.031681

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.
-6.383	-5.764	-0.002	-0.242	-0.375	-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 : 0.857 / q_NPA : 0.913

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	0.069	0.041	3.855	-1.966	-1.347	-0.002	-0.242	-0.375	-0.001
4	A	4	GLY	0	0.010	0.017	6.549	3.306	3.306	0.000	0.000	0.000	0.000
5	A	5	SER	0	0.014	0.007	9.404	1.113	1.113	0.000	0.000	0.000	0.000
6	A	6	SER	0	0.009	-0.005	12.763	0.356	0.356	0.000	0.000	0.000	0.000
7	A	7	GLY	0	-0.021	-0.007	15.939	0.506	0.506	0.000	0.000	0.000	0.000
8	A	8	MET	0	0.016	-0.007	19.457	0.626	0.626	0.000	0.000	0.000	0.000
9	A	9	PRO	0	-0.018	0.015	17.261	0.349	0.349	0.000	0.000	0.000	0.000
10	A	10	TYR	0	-0.013	-0.019	19.877	0.863	0.863	0.000	0.000	0.000	0.000
11	A	11	VAL	0	-0.033	-0.012	21.409	-0.392	-0.392	0.000	0.000	0.000	0.000
12	A	12	ASP	-1	-0.813	-0.929	20.463	-15.349	-15.349	0.000	0.000	0.000	0.000
13	A	13	ARG	1	0.884	0.962	21.517	12.695	12.695	0.000	0.000	0.000	0.000
14	A	14	GLN	0	0.050	0.008	18.274	0.685	0.685	0.000	0.000	0.000	0.000
15	A	15	ASN	0	-0.029	-0.019	22.381	0.676	0.676	0.000	0.000	0.000	0.000
16	A	16	ARG	1	0.927	0.994	24.428	10.889	10.889	0.000	0.000	0.000	0.000
17	A	17	ILE	0	0.032	0.019	25.252	0.405	0.405	0.000	0.000	0.000	0.000
18	A	18	CYS	0	-0.056	-0.046	27.545	-0.190	-0.190	0.000	0.000	0.000	0.000
19	A	19	GLY	0	0.050	0.044	30.235	0.235	0.235	0.000	0.000	0.000	0.000
20	A	20	PHE	0	-0.062	-0.032	32.388	-0.146	-0.146	0.000	0.000	0.000	0.000
21	A	21	LEU	0	0.048	0.044	28.931	0.113	0.113	0.000	0.000	0.000	0.000
22	A	22	ASP	-1	-0.856	-0.928	32.982	-8.756	-8.756	0.000	0.000	0.000	0.000
23	A	23	ILE	0	-0.008	0.011	26.870	-0.114	-0.114	0.000	0.000	0.000	0.000
24	A	24	GLU	-1	-0.808	-0.896	31.026	-9.239	-9.239	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.829	-0.917	30.837	-9.785	-9.785	0.000	0.000	0.000	0.000
26	A	26	ASN	0	-0.066	-0.037	27.585	-0.194	-0.194	0.000	0.000	0.000	0.000
27	A	27	GLU	-1	-0.915	-0.947	31.160	-9.252	-9.252	0.000	0.000	0.000	0.000
28	A	28	ASN	0	-0.128	-0.078	34.551	0.580	0.580	0.000	0.000	0.000	0.000
29	A	29	SER	0	0.005	0.009	35.385	-0.216	-0.216	0.000	0.000	0.000	0.000
30	A	30	GLY	0	-0.025	-0.013	36.176	0.289	0.289	0.000	0.000	0.000	0.000
31	A	31	LYS	1	0.916	0.967	37.439	8.128	8.128	0.000	0.000	0.000	0.000
32	A	32	PHE	0	0.030	0.009	33.899	-0.248	-0.248	0.000	0.000	0.000	0.000
33	A	33	LEU	0	-0.042	-0.021	32.615	0.334	0.334	0.000	0.000	0.000	0.000
34	A	34	ARG	1	0.984	1.003	33.777	8.038	8.038	0.000	0.000	0.000	0.000
35	A	35	ARG	1	0.856	0.924	31.903	9.300	9.300	0.000	0.000	0.000	0.000
36	A	36	TYR	0	0.038	0.014	32.437	-0.100	-0.100	0.000	0.000	0.000	0.000
37	A	37	PHE	0	0.036	0.011	26.563	-0.298	-0.298	0.000	0.000	0.000	0.000
38	A	38	ILE	0	0.007	-0.023	25.837	0.306	0.306	0.000	0.000	0.000	0.000
39	A	39	LEU	0	0.004	0.016	21.084	-0.389	-0.389	0.000	0.000	0.000	0.000
40	A	40	ASP	-1	-0.826	-0.941	21.217	-13.953	-13.953	0.000	0.000	0.000	0.000
41	A	41	THR	0	0.045	0.000	19.158	-0.471	-0.471	0.000	0.000	0.000	0.000
42	A	42	GLN	0	-0.054	-0.021	17.870	-0.571	-0.571	0.000	0.000	0.000	0.000
43	A	43	ALA	0	0.014	0.015	17.849	-0.497	-0.497	0.000	0.000	0.000	0.000
44	A	44	ASN	0	0.013	0.023	12.776	-0.419	-0.419	0.000	0.000	0.000	0.000
45	A	45	CYS	0	-0.072	-0.035	16.072	-1.002	-1.002	0.000	0.000	0.000	0.000
46	A	46	LEU	0	-0.035	0.017	18.838	0.491	0.491	0.000	0.000	0.000	0.000
47	A	47	LEU	0	0.021	0.012	22.249	-0.011	-0.011	0.000	0.000	0.000	0.000
48	A	48	TRP	0	0.033	0.011	24.295	0.247	0.247	0.000	0.000	0.000	0.000
49	A	49	TYR	0	0.033	0.014	26.497	0.131	0.131	0.000	0.000	0.000	0.000
50	A	50	MET	0	-0.043	-0.035	31.527	0.128	0.128	0.000	0.000	0.000	0.000
51	A	51	ASP	-1	-0.856	-0.941	35.105	-8.040	-8.040	0.000	0.000	0.000	0.000
52	A	52	ASN	0	-0.001	-0.006	34.535	-0.417	-0.417	0.000	0.000	0.000	0.000
53	A	53	PRO	0	0.018	0.007	31.047	0.205	0.205	0.000	0.000	0.000	0.000
54	A	54	GLN	0	-0.013	-0.014	33.873	0.213	0.213	0.000	0.000	0.000	0.000
55	A	55	ASN	0	-0.011	0.003	36.514	0.264	0.264	0.000	0.000	0.000	0.000
56	A	56	LEU	0	-0.069	-0.014	33.666	0.134	0.134	0.000	0.000	0.000	0.000
57	A	57	ALA	0	0.032	0.015	37.296	0.056	0.056	0.000	0.000	0.000	0.000
58	A	58	VAL	0	0.024	-0.005	33.656	-0.217	-0.217	0.000	0.000	0.000	0.000
59	A	59	GLY	0	-0.013	0.001	33.270	-0.255	-0.255	0.000	0.000	0.000	0.000
60	A	60	ALA	0	-0.042	-0.006	33.742	0.036	0.036	0.000	0.000	0.000	0.000
61	A	61	GLY	0	0.041	0.007	29.872	-0.274	-0.274	0.000	0.000	0.000	0.000
62	A	62	ALA	0	-0.047	-0.015	26.839	0.294	0.294	0.000	0.000	0.000	0.000
63	A	63	VAL	0	-0.048	-0.033	28.996	0.040	0.040	0.000	0.000	0.000	0.000
64	A	64	GLY	0	0.013	0.001	26.546	0.058	0.058	0.000	0.000	0.000	0.000
65	A	65	SER	0	-0.041	-0.016	21.991	-0.184	-0.184	0.000	0.000	0.000	0.000
66	A	66	LEU	0	-0.011	-0.008	19.964	-0.092	-0.092	0.000	0.000	0.000	0.000
67	A	67	GLN	0	0.038	0.021	15.391	-0.803	-0.803	0.000	0.000	0.000	0.000
68	A	68	LEU	0	0.009	-0.009	15.444	-0.275	-0.275	0.000	0.000	0.000	0.000
69	A	69	THR	0	-0.022	-0.007	10.620	-1.378	-1.378	0.000	0.000	0.000	0.000
70	A	70	TYR	0	-0.021	-0.014	11.964	-0.993	-0.993	0.000	0.000	0.000	0.000
71	A	71	ILE	0	-0.034	-0.011	14.647	0.419	0.419	0.000	0.000	0.000	0.000
72	A	72	SER	0	-0.002	0.002	14.066	-1.521	-1.521	0.000	0.000	0.000	0.000
73	A	73	LYS	1	0.933	0.959	15.502	15.432	15.432	0.000	0.000	0.000	0.000
74	A	74	VAL	0	0.014	0.023	19.078	0.272	0.272	0.000	0.000	0.000	0.000
75	A	75	SER	0	-0.011	0.008	22.585	0.115	0.115	0.000	0.000	0.000	0.000
76	A	76	ILE	0	0.036	0.023	25.692	0.075	0.075	0.000	0.000	0.000	0.000
77	A	77	ALA	0	0.006	0.014	28.938	-0.237	-0.237	0.000	0.000	0.000	0.000
78	A	78	THR	0	0.062	0.012	30.168	0.215	0.215	0.000	0.000	0.000	0.000
79	A	79	PRO	0	0.037	0.004	32.653	0.003	0.003	0.000	0.000	0.000	0.000
80	A	80	LYS	1	0.938	0.956	33.844	8.858	8.858	0.000	0.000	0.000	0.000
81	A	81	GLN	0	-0.033	-0.004	27.492	-0.368	-0.368	0.000	0.000	0.000	0.000
82	A	82	LYS	1	0.860	0.919	32.509	9.405	9.405	0.000	0.000	0.000	0.000
83	A	83	PRO	0	0.011	0.018	34.421	0.047	0.047	0.000	0.000	0.000	0.000
84	A	84	LYS	1	0.909	0.941	37.652	7.622	7.622	0.000	0.000	0.000	0.000
85	A	85	THR	0	0.040	0.031	35.747	0.012	0.012	0.000	0.000	0.000	0.000
86	A	86	PRO	0	-0.012	0.013	36.975	-0.132	-0.132	0.000	0.000	0.000	0.000
87	A	87	PHE	0	0.032	-0.007	35.177	-0.136	-0.136	0.000	0.000	0.000	0.000
88	A	88	CYS	0	0.000	0.007	32.518	-0.018	-0.018	0.000	0.000	0.000	0.000
89	A	89	PHE	0	-0.007	-0.010	25.922	-0.073	-0.073	0.000	0.000	0.000	0.000
90	A	90	VAL	0	-0.024	-0.015	24.401	0.081	0.081	0.000	0.000	0.000	0.000
91	A	91	ILE	0	0.027	0.021	20.742	-0.315	-0.315	0.000	0.000	0.000	0.000
92	A	92	ASN	0	-0.044	-0.026	19.444	0.147	0.147	0.000	0.000	0.000	0.000
93	A	93	ALA	0	0.030	0.009	17.149	-0.692	-0.692	0.000	0.000	0.000	0.000
94	A	94	LEU	0	-0.003	-0.003	12.473	0.375	0.375	0.000	0.000	0.000	0.000
95	A	95	SER	0	0.000	0.000	15.488	-0.051	-0.051	0.000	0.000	0.000	0.000
96	A	96	GLN	0	0.000	0.009	18.707	0.359	0.359	0.000	0.000	0.000	0.000
97	A	97	ARG	1	0.919	0.962	21.159	11.047	11.047	0.000	0.000	0.000	0.000
98	A	98	TYR	0	0.031	0.025	21.045	0.609	0.609	0.000	0.000	0.000	0.000
99	A	99	PHE	0	-0.010	-0.022	25.610	-0.035	-0.035	0.000	0.000	0.000	0.000
100	A	100	LEU	0	0.043	0.021	26.327	0.075	0.075	0.000	0.000	0.000	0.000
101	A	101	GLN	0	-0.062	-0.037	30.327	0.122	0.122	0.000	0.000	0.000	0.000
102	A	102	ALA	0	0.033	0.015	32.708	-0.149	-0.149	0.000	0.000	0.000	0.000
103	A	103	ASN	0	-0.067	-0.043	34.547	0.416	0.416	0.000	0.000	0.000	0.000
104	A	104	ASP	-1	-0.840	-0.924	37.147	-8.193	-8.193	0.000	0.000	0.000	0.000
105	A	105	GLN	0	-0.021	-0.021	36.343	-0.291	-0.291	0.000	0.000	0.000	0.000
106	A	106	LYS	1	0.925	0.974	35.329	7.949	7.949	0.000	0.000	0.000	0.000
107	A	107	ASP	-1	-0.742	-0.874	33.427	-9.832	-9.832	0.000	0.000	0.000	0.000
108	A	108	LEU	0	-0.054	-0.012	30.928	-0.382	-0.382	0.000	0.000	0.000	0.000
109	A	109	LYS	1	0.825	0.892	30.449	9.742	9.742	0.000	0.000	0.000	0.000
110	A	110	ASP	-1	-0.848	-0.926	29.436	-10.367	-10.367	0.000	0.000	0.000	0.000
111	A	111	TRP	0	-0.025	-0.008	25.297	-0.804	-0.804	0.000	0.000	0.000	0.000
112	A	112	VAL	0	-0.017	-0.011	25.968	-0.614	-0.614	0.000	0.000	0.000	0.000
113	A	113	GLU	-1	-0.839	-0.898	24.809	-11.411	-11.411	0.000	0.000	0.000	0.000
114	A	114	ALA	0	0.047	0.020	24.045	-0.634	-0.634	0.000	0.000	0.000	0.000
115	A	115	LEU	0	0.002	-0.008	21.754	-0.779	-0.779	0.000	0.000	0.000	0.000
116	A	116	ASN	0	-0.085	-0.045	20.292	-1.441	-1.441	0.000	0.000	0.000	0.000
117	A	117	GLN	0	-0.045	-0.006	19.770	-0.850	-0.850	0.000	0.000	0.000	0.000
118	A	118	ALA	0	-0.002	-0.014	18.400	-0.741	-0.741	0.000	0.000	0.000	0.000
119	A	119	SER	0	-0.068	-0.053	15.855	-0.974	-0.974	0.000	0.000	0.000	0.000
120	A	120	LYS	1	0.896	0.943	14.671	16.361	16.361	0.000	0.000	0.000	0.000
121	A	121	SER	0	-0.008	0.008	13.539	-1.196	-1.196	0.000	0.000	0.000	0.000
122	A	122	GLY	0	0.012	0.021	15.629	-0.056	-0.056	0.000	0.000	0.000	0.000
123	A	123	PRO	0	-0.028	-0.009	16.928	-0.651	-0.651	0.000	0.000	0.000	0.000
124	A	124	SER	0	-0.044	-0.050	13.289	-1.569	-1.569	0.000	0.000	0.000	0.000
125	A	125	SER	0	-0.055	-0.014	11.084	0.125	0.125	0.000	0.000	0.000	0.000
126	A	126	GLY	-1	-0.929	-0.946	13.301	-17.357	-17.357	0.000	0.000	0.000	0.000

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