FMO DATABASE

FMODB ID: VZQ51

Calculation Name: 4BTS-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4BTS

Chain ID: A

ChEMBL ID:

UniProt ID: P06147

Base Structure: X-ray

Registration Date: 2025-10-06

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	153
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1358233.955778
FMO2-HF: Nuclear repulsion	1297135.741901
FMO2-HF: Total energy	-61098.213877
FMO2-MP2: Total energy	-61276.812616

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:2:SER)

Summations of interaction energy for fragment #1(A:2: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.
91.543	97.005	0.233	-2.706	-2.986	-0.019

Interaction energy analysis for fragmet #1(A:2:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.849 / q_NPA : 0.915

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	4	VAL	0	0.023	0.023	2.903	1.782	5.079	0.164	-1.629	-1.832	-0.010
4	A	5	ILE	0	-0.002	0.004	3.026	-15.317	-13.482	0.073	-1.036	-0.871	-0.009
52	A	53	ASP	-1	-0.788	-0.901	4.904	-51.315	-51.255	-0.001	-0.002	-0.056	0.000
55	A	56	ALA	0	-0.023	0.003	4.215	-5.086	-5.007	-0.001	-0.016	-0.061	0.000
56	A	57	ARG	1	0.949	0.961	5.060	42.849	42.915	-0.001	-0.008	-0.057	0.000
59	A	60	LEU	0	-0.029	-0.009	4.281	-0.486	-0.361	-0.001	-0.015	-0.109	0.000
5	A	6	GLU	-1	-0.842	-0.915	5.567	-20.809	-20.809	0.000	0.000	0.000	0.000
6	A	7	LYS	1	0.873	0.930	8.757	23.268	23.268	0.000	0.000	0.000	0.000
7	A	8	GLU	-1	-0.945	-0.967	10.302	-21.190	-21.190	0.000	0.000	0.000	0.000
8	A	9	SER	0	-0.033	-0.023	12.172	0.630	0.630	0.000	0.000	0.000	0.000
9	A	10	ASP	-1	-0.929	-0.962	10.179	-22.861	-22.861	0.000	0.000	0.000	0.000
10	A	11	PHE	0	-0.001	0.007	8.102	-2.376	-2.376	0.000	0.000	0.000	0.000
11	A	12	LYS	1	0.848	0.919	11.152	19.613	19.613	0.000	0.000	0.000	0.000
12	A	13	TYR	0	0.047	0.009	13.819	-0.663	-0.663	0.000	0.000	0.000	0.000
13	A	14	ILE	0	-0.048	-0.019	15.344	0.097	0.097	0.000	0.000	0.000	0.000
14	A	15	HIS	0	0.068	0.031	13.539	0.154	0.154	0.000	0.000	0.000	0.000
15	A	16	ARG	1	0.878	0.925	17.874	12.761	12.761	0.000	0.000	0.000	0.000
16	A	17	ILE	0	0.048	0.027	17.141	-0.063	-0.063	0.000	0.000	0.000	0.000
17	A	18	LEU	0	0.063	0.037	21.782	0.356	0.356	0.000	0.000	0.000	0.000
18	A	19	ASN	0	-0.040	-0.002	25.140	0.169	0.169	0.000	0.000	0.000	0.000
19	A	20	THR	0	-0.006	-0.002	23.320	0.511	0.511	0.000	0.000	0.000	0.000
20	A	21	ASN	0	0.020	0.013	21.665	-0.310	-0.310	0.000	0.000	0.000	0.000
21	A	22	ILE	0	-0.034	-0.021	15.632	0.025	0.025	0.000	0.000	0.000	0.000
22	A	23	ASP	-1	-0.842	-0.926	16.581	-18.996	-18.996	0.000	0.000	0.000	0.000
23	A	24	GLY	0	0.097	0.041	13.365	-1.043	-1.043	0.000	0.000	0.000	0.000
24	A	25	LYS	1	0.972	0.993	11.535	15.500	15.500	0.000	0.000	0.000	0.000
25	A	26	ARG	1	0.846	0.920	11.586	19.457	19.457	0.000	0.000	0.000	0.000
26	A	27	ILE	0	0.005	0.001	7.909	-1.274	-1.274	0.000	0.000	0.000	0.000
27	A	28	THR	0	0.043	0.019	8.686	2.607	2.607	0.000	0.000	0.000	0.000
28	A	29	PRO	0	0.037	0.016	10.990	2.248	2.248	0.000	0.000	0.000	0.000
29	A	30	ILE	0	-0.063	-0.048	13.079	1.950	1.950	0.000	0.000	0.000	0.000
30	A	31	ALA	0	-0.017	0.009	13.628	1.172	1.172	0.000	0.000	0.000	0.000
31	A	32	LEU	0	0.034	0.014	14.884	1.310	1.310	0.000	0.000	0.000	0.000
32	A	33	THR	0	-0.060	-0.041	17.423	1.020	1.020	0.000	0.000	0.000	0.000
33	A	34	GLY	0	-0.034	-0.005	19.382	0.672	0.672	0.000	0.000	0.000	0.000
34	A	35	ILE	0	-0.022	0.001	20.589	0.698	0.698	0.000	0.000	0.000	0.000
35	A	36	ARG	1	0.883	0.921	23.414	10.223	10.223	0.000	0.000	0.000	0.000
36	A	37	GLY	0	0.041	0.023	26.517	0.037	0.037	0.000	0.000	0.000	0.000
37	A	38	ILE	0	-0.013	0.013	19.910	-0.065	-0.065	0.000	0.000	0.000	0.000
38	A	39	GLY	0	0.036	0.021	22.522	-0.144	-0.144	0.000	0.000	0.000	0.000
39	A	40	ARG	1	0.982	0.972	18.418	14.834	14.834	0.000	0.000	0.000	0.000
40	A	41	ARG	1	0.986	0.982	18.364	12.518	12.518	0.000	0.000	0.000	0.000
41	A	42	PHE	0	0.057	0.034	19.843	-0.454	-0.454	0.000	0.000	0.000	0.000
42	A	43	ALA	0	0.038	0.039	16.700	-0.282	-0.282	0.000	0.000	0.000	0.000
43	A	44	TYR	0	0.031	-0.001	11.804	-0.310	-0.310	0.000	0.000	0.000	0.000
44	A	45	ILE	0	-0.052	-0.008	16.214	-0.552	-0.552	0.000	0.000	0.000	0.000
45	A	46	ILE	0	0.032	0.020	16.615	-0.188	-0.188	0.000	0.000	0.000	0.000
46	A	47	CYS	0	-0.044	-0.020	12.452	-0.545	-0.545	0.000	0.000	0.000	0.000
47	A	48	LYS	1	0.959	0.978	14.169	17.086	17.086	0.000	0.000	0.000	0.000
48	A	49	VAL	0	-0.017	-0.008	16.016	0.036	0.036	0.000	0.000	0.000	0.000
49	A	50	LEU	0	-0.002	-0.005	16.136	0.163	0.163	0.000	0.000	0.000	0.000
50	A	51	LYS	1	0.902	0.962	13.777	17.273	17.273	0.000	0.000	0.000	0.000
51	A	52	ILE	0	-0.004	0.011	10.294	-1.383	-1.383	0.000	0.000	0.000	0.000
53	A	54	PRO	0	-0.044	-0.035	8.109	0.238	0.238	0.000	0.000	0.000	0.000
54	A	55	ASN	0	-0.029	-0.027	5.327	6.119	6.119	0.000	0.000	0.000	0.000
57	A	58	ALA	0	0.027	0.014	7.752	0.196	0.196	0.000	0.000	0.000	0.000
58	A	59	GLY	0	0.026	0.018	10.898	1.151	1.151	0.000	0.000	0.000	0.000
60	A	61	LEU	0	-0.056	-0.013	8.437	0.222	0.222	0.000	0.000	0.000	0.000
61	A	62	THR	0	0.034	0.010	11.607	1.163	1.163	0.000	0.000	0.000	0.000
62	A	63	GLU	-1	-0.841	-0.920	13.432	-15.495	-15.495	0.000	0.000	0.000	0.000
63	A	64	ASP	-1	-0.758	-0.872	16.814	-15.986	-15.986	0.000	0.000	0.000	0.000
64	A	65	GLN	0	0.049	0.022	11.043	-0.035	-0.035	0.000	0.000	0.000	0.000
65	A	66	CYS	0	-0.054	-0.017	15.927	0.174	0.174	0.000	0.000	0.000	0.000
66	A	67	ASN	0	-0.028	-0.002	18.364	0.360	0.360	0.000	0.000	0.000	0.000
67	A	68	LYS	1	0.977	0.978	18.198	16.593	16.593	0.000	0.000	0.000	0.000
68	A	69	ILE	0	-0.029	-0.024	15.419	0.277	0.277	0.000	0.000	0.000	0.000
69	A	70	THR	0	-0.084	-0.060	19.976	0.569	0.569	0.000	0.000	0.000	0.000
70	A	71	ASP	-1	-0.848	-0.933	23.398	-12.206	-12.206	0.000	0.000	0.000	0.000
71	A	72	LEU	0	-0.050	-0.024	20.422	0.306	0.306	0.000	0.000	0.000	0.000
72	A	73	ILE	0	-0.104	-0.064	22.494	0.326	0.326	0.000	0.000	0.000	0.000
73	A	74	ALA	0	-0.050	-0.007	25.600	0.424	0.424	0.000	0.000	0.000	0.000
74	A	75	ASP	-1	-0.869	-0.930	27.919	-9.586	-9.586	0.000	0.000	0.000	0.000
75	A	76	PRO	0	-0.068	-0.028	26.359	-0.249	-0.249	0.000	0.000	0.000	0.000
76	A	77	GLU	-1	-0.902	-0.965	27.199	-9.575	-9.575	0.000	0.000	0.000	0.000
77	A	78	ALA	0	0.005	0.012	29.372	0.088	0.088	0.000	0.000	0.000	0.000
78	A	79	HIS	0	-0.085	-0.048	23.381	-0.511	-0.511	0.000	0.000	0.000	0.000
79	A	80	GLY	0	-0.019	0.001	24.978	-0.500	-0.500	0.000	0.000	0.000	0.000
80	A	81	ILE	0	-0.027	-0.030	22.982	-0.034	-0.034	0.000	0.000	0.000	0.000
81	A	82	PRO	0	-0.009	0.001	26.550	0.348	0.348	0.000	0.000	0.000	0.000
82	A	83	THR	0	0.104	0.045	29.328	-0.254	-0.254	0.000	0.000	0.000	0.000
83	A	84	TRP	0	-0.022	-0.022	27.448	-0.184	-0.184	0.000	0.000	0.000	0.000
84	A	85	LEU	0	-0.060	-0.027	25.175	-0.165	-0.165	0.000	0.000	0.000	0.000
85	A	86	LEU	0	-0.004	0.008	27.896	-0.380	-0.380	0.000	0.000	0.000	0.000
86	A	87	ASN	0	-0.053	-0.051	27.352	0.345	0.345	0.000	0.000	0.000	0.000
87	A	88	ARG	1	0.770	0.851	31.320	8.675	8.675	0.000	0.000	0.000	0.000
88	A	89	ILE	0	0.047	0.038	33.481	-0.093	-0.093	0.000	0.000	0.000	0.000
89	A	90	ASN	0	0.033	0.035	35.847	-0.107	-0.107	0.000	0.000	0.000	0.000
90	A	91	ASP	-1	-0.789	-0.873	38.813	-8.061	-8.061	0.000	0.000	0.000	0.000
91	A	92	PHE	0	-0.013	-0.023	40.265	0.178	0.178	0.000	0.000	0.000	0.000
92	A	93	LYS	1	0.891	0.946	43.003	6.953	6.953	0.000	0.000	0.000	0.000
93	A	94	ASP	-1	-0.799	-0.876	39.976	-7.839	-7.839	0.000	0.000	0.000	0.000
94	A	95	GLY	0	0.031	0.006	40.855	-0.153	-0.153	0.000	0.000	0.000	0.000
95	A	96	LYS	1	0.959	0.990	36.847	8.097	8.097	0.000	0.000	0.000	0.000
96	A	97	ASN	0	0.009	0.004	33.532	-0.055	-0.055	0.000	0.000	0.000	0.000
97	A	98	TYR	0	-0.020	-0.038	31.988	-0.242	-0.242	0.000	0.000	0.000	0.000
98	A	99	GLN	0	0.025	0.014	24.399	0.026	0.026	0.000	0.000	0.000	0.000
99	A	100	MET	0	-0.076	-0.029	29.386	0.282	0.282	0.000	0.000	0.000	0.000
100	A	101	ALA	0	0.079	0.038	27.288	-0.298	-0.298	0.000	0.000	0.000	0.000
101	A	102	SER	0	-0.010	-0.031	26.917	0.536	0.536	0.000	0.000	0.000	0.000
102	A	103	ASN	0	0.046	0.016	28.661	0.353	0.353	0.000	0.000	0.000	0.000
103	A	104	THR	0	0.034	0.021	31.516	0.309	0.309	0.000	0.000	0.000	0.000
104	A	105	LEU	0	0.040	0.025	30.184	0.318	0.318	0.000	0.000	0.000	0.000
105	A	106	ASP	-1	-0.826	-0.907	33.029	-9.267	-9.267	0.000	0.000	0.000	0.000
106	A	107	THR	0	-0.066	-0.033	35.013	0.352	0.352	0.000	0.000	0.000	0.000
107	A	108	LYS	1	0.951	0.967	35.779	8.609	8.609	0.000	0.000	0.000	0.000
108	A	109	MET	0	-0.045	-0.023	35.784	0.216	0.216	0.000	0.000	0.000	0.000
109	A	110	ARG	1	0.928	0.964	38.234	8.444	8.444	0.000	0.000	0.000	0.000
110	A	111	GLU	-1	-0.890	-0.944	40.662	-7.660	-7.660	0.000	0.000	0.000	0.000
111	A	112	ASP	-1	-0.834	-0.907	40.343	-7.605	-7.605	0.000	0.000	0.000	0.000
112	A	113	LEU	0	-0.021	-0.019	41.739	0.213	0.213	0.000	0.000	0.000	0.000
113	A	114	GLU	-1	-0.816	-0.892	44.756	-6.318	-6.318	0.000	0.000	0.000	0.000
114	A	115	ARG	1	0.868	0.937	44.075	7.245	7.245	0.000	0.000	0.000	0.000
115	A	116	LEU	0	-0.001	-0.008	44.849	0.136	0.136	0.000	0.000	0.000	0.000
116	A	117	LYS	1	0.900	0.949	47.916	6.733	6.733	0.000	0.000	0.000	0.000
117	A	118	LYS	1	0.913	0.964	51.049	6.288	6.288	0.000	0.000	0.000	0.000
118	A	119	ILE	0	-0.028	-0.017	49.627	0.107	0.107	0.000	0.000	0.000	0.000
119	A	120	LYS	1	0.965	0.987	53.409	5.591	5.591	0.000	0.000	0.000	0.000
120	A	121	SER	0	0.022	0.026	50.334	0.008	0.008	0.000	0.000	0.000	0.000
121	A	122	HIS	0	0.077	0.031	51.767	-0.046	-0.046	0.000	0.000	0.000	0.000
122	A	123	ARG	1	0.958	0.976	42.664	7.198	7.198	0.000	0.000	0.000	0.000
123	A	124	GLY	0	0.015	0.019	47.454	-0.173	-0.173	0.000	0.000	0.000	0.000
124	A	125	LEU	0	0.020	0.012	48.884	-0.067	-0.067	0.000	0.000	0.000	0.000
125	A	126	ARG	1	0.875	0.952	48.109	6.339	6.339	0.000	0.000	0.000	0.000
126	A	127	HIS	0	-0.018	-0.025	42.737	-0.247	-0.247	0.000	0.000	0.000	0.000
127	A	128	PHE	0	-0.031	-0.007	46.643	-0.080	-0.080	0.000	0.000	0.000	0.000
128	A	129	TRP	0	0.016	-0.003	49.233	0.015	0.015	0.000	0.000	0.000	0.000
129	A	130	GLY	0	0.040	0.035	46.473	0.026	0.026	0.000	0.000	0.000	0.000
130	A	131	LEU	0	-0.003	0.011	46.983	-0.054	-0.054	0.000	0.000	0.000	0.000
131	A	132	LYS	1	0.927	0.944	43.043	7.215	7.215	0.000	0.000	0.000	0.000
132	A	133	VAL	0	0.008	-0.002	43.516	0.147	0.147	0.000	0.000	0.000	0.000
133	A	134	ARG	1	0.884	0.939	37.957	8.107	8.107	0.000	0.000	0.000	0.000
134	A	135	GLY	0	0.062	0.038	44.990	0.023	0.023	0.000	0.000	0.000	0.000
135	A	136	GLN	0	0.029	0.023	42.594	0.151	0.151	0.000	0.000	0.000	0.000
136	A	137	HIS	0	0.070	0.018	47.503	-0.028	-0.028	0.000	0.000	0.000	0.000
137	A	138	THR	0	-0.012	-0.021	48.663	-0.071	-0.071	0.000	0.000	0.000	0.000
138	A	139	LYS	1	0.996	1.021	50.304	5.628	5.628	0.000	0.000	0.000	0.000
139	A	140	THR	0	0.031	0.016	49.052	0.097	0.097	0.000	0.000	0.000	0.000
140	A	141	SER	0	0.030	0.019	44.784	-0.122	-0.122	0.000	0.000	0.000	0.000
141	A	142	GLY	0	-0.014	-0.020	44.643	0.069	0.069	0.000	0.000	0.000	0.000
142	A	143	ARG	1	0.926	0.957	45.661	6.178	6.178	0.000	0.000	0.000	0.000
143	A	144	HIS	0	0.034	0.009	46.461	-0.104	-0.104	0.000	0.000	0.000	0.000
144	A	145	GLY	0	0.038	0.054	45.816	-0.015	-0.015	0.000	0.000	0.000	0.000
145	A	146	VAL	0	-0.033	-0.024	40.330	-0.153	-0.153	0.000	0.000	0.000	0.000
146	A	147	VAL	0	0.003	0.006	37.297	0.100	0.100	0.000	0.000	0.000	0.000
147	A	148	CYS	0	-0.045	-0.029	40.270	-0.010	-0.010	0.000	0.000	0.000	0.000
148	A	149	GLY	0	-0.027	-0.017	39.553	-0.205	-0.205	0.000	0.000	0.000	0.000
149	A	150	VAL	0	-0.018	-0.016	36.719	0.031	0.031	0.000	0.000	0.000	0.000
150	A	151	VAL	0	0.049	0.027	33.430	0.023	0.023	0.000	0.000	0.000	0.000
151	A	152	ARG	1	0.820	0.907	33.249	8.736	8.736	0.000	0.000	0.000	0.000
152	A	153	LYS	1	0.958	0.983	24.839	12.543	12.543	0.000	0.000	0.000	0.000
153	A	154	ASN	-1	-0.895	-0.933	29.340	-10.725	-10.725	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:SER)