FMO DATABASE

FMODB ID: Y12V2

Calculation Name: 1BPV-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1BPV

Chain ID: A

ChEMBL ID:

UniProt ID: Q8WZ42

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	104
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-755784.262822
FMO2-HF: Nuclear repulsion	716336.732712
FMO2-HF: Total energy	-39447.53011
FMO2-MP2: Total energy	-39564.985015

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:0:SER)

Summations of interaction energy for fragment #1(A:0:SER)

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.
-21.142	-18.375	0.181	-1.11	-1.837	-0.006

Interaction energy analysis for fragmet #1(A:0:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.847 / q_NPA : 0.908

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	2	ILE	0	-0.017	-0.026	3.479	-4.093	-2.579	0.010	-0.673	-0.850	-0.002
28	A	27	TYR	0	0.013	0.012	4.172	-4.284	-4.126	-0.001	-0.024	-0.132	0.000
30	A	29	GLY	0	-0.009	-0.006	2.855	-3.301	-2.934	0.121	-0.222	-0.267	-0.002
31	A	30	GLY	0	0.001	0.006	3.663	1.316	1.526	0.000	0.012	-0.222	0.000
32	A	31	PHE	0	-0.100	-0.048	3.198	2.138	2.656	0.051	-0.203	-0.366	-0.002
4	A	3	ASP	-1	-0.775	-0.890	6.305	-33.107	-33.107	0.000	0.000	0.000	0.000
5	A	4	PRO	0	0.015	0.005	9.668	0.099	0.099	0.000	0.000	0.000	0.000
6	A	5	PRO	0	0.000	-0.005	12.882	-0.018	-0.018	0.000	0.000	0.000	0.000
7	A	6	GLY	0	0.009	0.024	15.635	0.037	0.037	0.000	0.000	0.000	0.000
8	A	7	LYS	1	0.972	0.982	18.367	12.181	12.181	0.000	0.000	0.000	0.000
9	A	8	PRO	0	-0.059	-0.025	21.220	0.321	0.321	0.000	0.000	0.000	0.000
10	A	9	VAL	0	0.018	0.007	23.686	0.250	0.250	0.000	0.000	0.000	0.000
11	A	10	PRO	0	0.024	-0.006	27.200	-0.073	-0.073	0.000	0.000	0.000	0.000
12	A	11	LEU	0	-0.052	-0.016	28.519	0.112	0.112	0.000	0.000	0.000	0.000
13	A	12	ASN	0	-0.021	-0.019	32.216	0.318	0.318	0.000	0.000	0.000	0.000
14	A	13	ILE	0	0.043	0.006	33.644	-0.357	-0.357	0.000	0.000	0.000	0.000
15	A	14	THR	0	0.056	0.038	35.868	0.193	0.193	0.000	0.000	0.000	0.000
16	A	15	ARG	1	1.021	1.004	37.547	7.107	7.107	0.000	0.000	0.000	0.000
17	A	16	HIS	0	-0.061	-0.022	38.230	0.215	0.215	0.000	0.000	0.000	0.000
18	A	17	THR	0	-0.109	-0.074	34.635	-0.115	-0.115	0.000	0.000	0.000	0.000
19	A	18	VAL	0	0.033	0.057	30.938	0.104	0.104	0.000	0.000	0.000	0.000
20	A	19	THR	0	-0.033	-0.017	30.391	-0.240	-0.240	0.000	0.000	0.000	0.000
21	A	20	LEU	0	-0.006	-0.001	25.265	0.032	0.032	0.000	0.000	0.000	0.000
22	A	21	LYS	1	0.925	0.980	23.129	12.407	12.407	0.000	0.000	0.000	0.000
23	A	22	TRP	0	0.009	0.027	18.496	-0.011	-0.011	0.000	0.000	0.000	0.000
24	A	23	ALA	0	-0.005	0.008	19.217	0.361	0.361	0.000	0.000	0.000	0.000
25	A	24	LYS	1	0.923	0.955	15.725	17.168	17.168	0.000	0.000	0.000	0.000
26	A	25	PRO	0	0.041	0.001	11.783	0.209	0.209	0.000	0.000	0.000	0.000
27	A	26	GLU	-1	-0.933	-0.959	12.440	-17.808	-17.808	0.000	0.000	0.000	0.000
29	A	28	THR	0	-0.089	-0.045	6.949	0.348	0.348	0.000	0.000	0.000	0.000
33	A	32	LYS	1	0.985	0.990	7.561	19.659	19.659	0.000	0.000	0.000	0.000
34	A	33	ILE	0	-0.001	0.013	10.681	1.143	1.143	0.000	0.000	0.000	0.000
35	A	34	THR	0	-0.035	-0.025	12.458	0.537	0.537	0.000	0.000	0.000	0.000
36	A	35	SER	0	-0.046	-0.032	15.604	1.013	1.013	0.000	0.000	0.000	0.000
37	A	36	TYR	0	-0.015	-0.005	15.232	-1.716	-1.716	0.000	0.000	0.000	0.000
38	A	37	ILE	0	-0.045	-0.017	17.633	0.836	0.836	0.000	0.000	0.000	0.000
39	A	38	VAL	0	0.073	0.029	20.190	-0.442	-0.442	0.000	0.000	0.000	0.000
40	A	39	GLU	-1	-0.903	-0.962	21.979	-13.341	-13.341	0.000	0.000	0.000	0.000
41	A	40	LYS	1	0.912	0.959	24.703	9.663	9.663	0.000	0.000	0.000	0.000
42	A	41	ARG	1	0.830	0.901	28.244	11.040	11.040	0.000	0.000	0.000	0.000
43	A	42	ASP	-1	-0.784	-0.899	30.216	-9.711	-9.711	0.000	0.000	0.000	0.000
44	A	43	LEU	0	-0.030	0.000	32.189	0.137	0.137	0.000	0.000	0.000	0.000
45	A	44	PRO	0	0.044	0.023	35.459	0.142	0.142	0.000	0.000	0.000	0.000
46	A	45	ASN	0	-0.045	-0.032	36.186	0.055	0.055	0.000	0.000	0.000	0.000
47	A	46	GLY	0	0.048	0.039	32.720	0.035	0.035	0.000	0.000	0.000	0.000
48	A	47	ARG	1	0.880	0.922	29.508	10.256	10.256	0.000	0.000	0.000	0.000
49	A	48	TRP	0	-0.062	-0.027	24.912	-0.430	-0.430	0.000	0.000	0.000	0.000
50	A	49	LEU	0	0.016	-0.001	26.542	-0.056	-0.056	0.000	0.000	0.000	0.000
51	A	50	LYS	1	0.929	0.973	21.612	13.805	13.805	0.000	0.000	0.000	0.000
52	A	51	ALA	0	0.028	0.025	25.036	0.289	0.289	0.000	0.000	0.000	0.000
53	A	52	ASN	0	0.004	0.026	22.580	0.191	0.191	0.000	0.000	0.000	0.000
54	A	53	PHE	0	-0.013	-0.031	25.684	-0.400	-0.400	0.000	0.000	0.000	0.000
55	A	54	SER	0	0.005	0.004	26.983	0.029	0.029	0.000	0.000	0.000	0.000
56	A	55	ASN	0	-0.041	-0.006	20.228	-0.393	-0.393	0.000	0.000	0.000	0.000
57	A	56	ILE	0	0.050	0.050	21.605	0.260	0.260	0.000	0.000	0.000	0.000
58	A	57	LEU	0	0.012	0.004	18.396	-0.859	-0.859	0.000	0.000	0.000	0.000
59	A	58	GLU	-1	-0.902	-0.943	19.745	-12.171	-12.171	0.000	0.000	0.000	0.000
60	A	59	ASN	0	-0.084	-0.070	19.711	-0.074	-0.074	0.000	0.000	0.000	0.000
61	A	60	GLU	-1	-0.873	-0.959	21.520	-11.144	-11.144	0.000	0.000	0.000	0.000
62	A	61	PHE	0	0.024	0.003	25.142	0.038	0.038	0.000	0.000	0.000	0.000
63	A	62	THR	0	0.020	0.018	26.930	0.201	0.201	0.000	0.000	0.000	0.000
64	A	63	VAL	0	-0.029	-0.009	27.563	-0.035	-0.035	0.000	0.000	0.000	0.000
65	A	64	SER	0	0.083	0.040	30.204	0.240	0.240	0.000	0.000	0.000	0.000
66	A	65	GLY	0	-0.064	-0.036	32.567	-0.219	-0.219	0.000	0.000	0.000	0.000
67	A	66	LEU	0	-0.082	-0.025	32.067	-0.139	-0.139	0.000	0.000	0.000	0.000
68	A	67	THR	0	-0.059	-0.041	35.889	0.195	0.195	0.000	0.000	0.000	0.000
69	A	68	GLU	-1	-0.879	-0.946	39.231	-7.149	-7.149	0.000	0.000	0.000	0.000
70	A	69	ASP	-1	-0.911	-0.964	41.891	-7.161	-7.161	0.000	0.000	0.000	0.000
71	A	70	ALA	0	-0.014	0.010	38.377	0.013	0.013	0.000	0.000	0.000	0.000
72	A	71	ALA	0	-0.019	0.004	36.078	-0.120	-0.120	0.000	0.000	0.000	0.000
73	A	72	TYR	0	-0.019	-0.023	32.341	-0.183	-0.183	0.000	0.000	0.000	0.000
74	A	73	GLU	-1	-0.806	-0.879	28.041	-11.203	-11.203	0.000	0.000	0.000	0.000
75	A	74	PHE	0	0.018	-0.021	26.505	-0.176	-0.176	0.000	0.000	0.000	0.000
76	A	75	ARG	1	0.897	0.988	21.134	13.876	13.876	0.000	0.000	0.000	0.000
77	A	76	VAL	0	0.041	0.009	17.847	0.184	0.184	0.000	0.000	0.000	0.000
78	A	77	ILE	0	-0.047	0.003	16.226	-0.892	-0.892	0.000	0.000	0.000	0.000
79	A	78	ALA	0	0.049	0.031	14.102	0.631	0.631	0.000	0.000	0.000	0.000
80	A	79	LYS	1	0.933	0.995	12.267	17.880	17.880	0.000	0.000	0.000	0.000
81	A	80	ASN	0	0.063	0.020	6.179	2.572	2.572	0.000	0.000	0.000	0.000
82	A	81	ALA	0	0.007	-0.013	9.207	1.173	1.173	0.000	0.000	0.000	0.000
83	A	82	ALA	0	0.005	0.015	6.967	0.587	0.587	0.000	0.000	0.000	0.000
84	A	83	GLY	0	-0.010	0.007	8.874	0.578	0.578	0.000	0.000	0.000	0.000
85	A	84	ALA	0	-0.024	-0.009	7.962	1.562	1.562	0.000	0.000	0.000	0.000
86	A	85	ILE	0	-0.033	-0.030	9.942	0.907	0.907	0.000	0.000	0.000	0.000
87	A	86	SER	0	-0.038	-0.026	10.636	-0.902	-0.902	0.000	0.000	0.000	0.000
88	A	87	PRO	0	0.032	-0.003	11.692	1.516	1.516	0.000	0.000	0.000	0.000
89	A	88	PRO	0	-0.039	-0.030	14.631	0.123	0.123	0.000	0.000	0.000	0.000
90	A	89	SER	0	-0.027	-0.036	17.437	0.383	0.383	0.000	0.000	0.000	0.000
91	A	90	GLU	-1	-0.937	-0.984	18.477	-13.475	-13.475	0.000	0.000	0.000	0.000
92	A	91	PRO	0	-0.058	-0.041	21.631	0.161	0.161	0.000	0.000	0.000	0.000
93	A	92	SER	0	-0.011	0.008	24.632	0.209	0.209	0.000	0.000	0.000	0.000
94	A	93	ASP	-1	-0.901	-0.965	27.157	-10.611	-10.611	0.000	0.000	0.000	0.000
95	A	94	ALA	0	-0.019	-0.021	30.499	0.016	0.016	0.000	0.000	0.000	0.000
96	A	95	ILE	0	0.027	0.012	32.252	0.213	0.213	0.000	0.000	0.000	0.000
97	A	96	THR	0	0.030	0.013	35.650	-0.147	-0.147	0.000	0.000	0.000	0.000
98	A	97	CYS	0	-0.072	-0.022	36.360	0.002	0.002	0.000	0.000	0.000	0.000
99	A	98	ARG	1	0.891	0.912	39.016	7.240	7.240	0.000	0.000	0.000	0.000
100	A	99	ASP	-1	-0.808	-0.882	40.183	-7.820	-7.820	0.000	0.000	0.000	0.000
101	A	100	ASP	-1	-0.865	-0.948	40.858	-7.560	-7.560	0.000	0.000	0.000	0.000
102	A	101	VAL	0	-0.142	-0.067	43.016	0.062	0.062	0.000	0.000	0.000	0.000
103	A	102	GLU	-1	-0.969	-0.985	46.102	-6.715	-6.715	0.000	0.000	0.000	0.000
104	A	103	ALA	-1	-0.942	-0.949	44.868	-7.059	-7.059	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:SER)