FMO DATABASE

FMODB ID: JK2N9

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	152
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1345427.455389
FMO2-HF: Nuclear repulsion	1285266.283265
FMO2-HF: Total energy	-60161.172124
FMO2-MP2: Total energy	-60338.894817

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:GLY)

Summations of interaction energy for fragment #1(A:2: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.
327.924	330.592	2.839	-2.722	-2.784	-0.02

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.880 / q_NPA : 0.927

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	MET	0	0.063	0.024	3.382	-6.220	-5.237	0.008	-0.519	-0.471	-0.001
5	A	6	MET	0	0.004	0.028	4.554	3.857	3.953	-0.001	-0.011	-0.083	0.000
6	A	7	LYS	1	0.991	0.993	3.841	18.555	18.716	-0.001	-0.106	-0.055	-0.001
8	A	9	LYS	1	0.970	0.974	5.188	17.295	17.348	-0.001	-0.001	-0.051	0.000
9	A	10	GLY	0	0.073	0.042	3.967	5.604	5.705	-0.001	-0.030	-0.071	0.000
10	A	11	LYS	1	0.845	0.905	2.137	27.726	29.079	2.799	-2.250	-1.901	-0.016
11	A	12	GLY	0	0.096	0.053	3.204	7.922	7.779	0.037	0.199	-0.093	-0.002
12	A	13	ILE	0	0.000	0.008	5.164	-5.518	-5.454	-0.001	-0.004	-0.059	0.000
4	A	5	GLN	0	-0.037	-0.023	5.583	4.454	4.454	0.000	0.000	0.000	0.000
7	A	8	GLY	0	0.078	0.045	5.931	3.586	3.586	0.000	0.000	0.000	0.000
13	A	14	SER	0	-0.014	-0.004	7.893	2.644	2.644	0.000	0.000	0.000	0.000
14	A	15	GLY	0	0.047	0.021	10.276	-0.274	-0.274	0.000	0.000	0.000	0.000
15	A	16	SER	0	-0.023	-0.023	13.706	1.113	1.113	0.000	0.000	0.000	0.000
16	A	17	ALA	0	0.028	0.017	14.584	-1.010	-1.010	0.000	0.000	0.000	0.000
17	A	18	LEU	0	-0.048	-0.013	17.215	0.835	0.835	0.000	0.000	0.000	0.000
18	A	19	PRO	0	0.042	0.025	20.352	-0.127	-0.127	0.000	0.000	0.000	0.000
19	A	20	PHE	0	0.043	0.014	23.467	-0.097	-0.097	0.000	0.000	0.000	0.000
20	A	21	LYS	0	0.025	0.025	24.972	0.425	0.425	0.000	0.000	0.000	0.000
21	A	22	ARG	1	0.987	0.985	23.710	11.945	11.945	0.000	0.000	0.000	0.000
22	A	23	ARG	1	0.899	0.947	27.750	9.094	9.094	0.000	0.000	0.000	0.000
23	A	24	SER	0	0.034	-0.003	30.394	-0.232	-0.232	0.000	0.000	0.000	0.000
24	A	25	PRO	0	-0.032	-0.015	30.314	0.146	0.146	0.000	0.000	0.000	0.000
25	A	26	LYS	1	0.983	0.980	32.906	9.068	9.068	0.000	0.000	0.000	0.000
26	A	27	TRP	0	0.086	0.056	30.474	0.152	0.152	0.000	0.000	0.000	0.000
27	A	28	LEU	0	-0.054	-0.019	32.500	0.060	0.060	0.000	0.000	0.000	0.000
28	A	29	HIS	0	0.025	0.010	36.265	0.126	0.126	0.000	0.000	0.000	0.000
29	A	30	MET	0	-0.011	0.001	36.298	0.061	0.061	0.000	0.000	0.000	0.000
30	A	31	THR	0	0.076	0.036	37.372	-0.191	-0.191	0.000	0.000	0.000	0.000
31	A	32	PRO	0	0.026	-0.005	35.175	-0.113	-0.113	0.000	0.000	0.000	0.000
32	A	33	SER	0	0.021	0.013	36.184	-0.217	-0.217	0.000	0.000	0.000	0.000
33	A	34	THR	0	0.090	0.049	38.435	-0.067	-0.067	0.000	0.000	0.000	0.000
34	A	35	VAL	0	0.021	0.011	32.183	-0.134	-0.134	0.000	0.000	0.000	0.000
35	A	36	VAL	0	-0.037	-0.004	34.131	-0.314	-0.314	0.000	0.000	0.000	0.000
36	A	37	ASP	-1	-0.864	-0.936	35.460	-7.980	-7.980	0.000	0.000	0.000	0.000
37	A	38	LEU	0	-0.049	-0.022	34.845	-0.008	-0.008	0.000	0.000	0.000	0.000
38	A	39	SER	0	-0.026	-0.041	31.287	-0.156	-0.156	0.000	0.000	0.000	0.000
39	A	40	VAL	0	0.003	-0.005	32.867	-0.180	-0.180	0.000	0.000	0.000	0.000
40	A	41	LYS	1	0.953	0.981	35.297	8.005	8.005	0.000	0.000	0.000	0.000
41	A	42	LEU	0	-0.020	-0.007	31.457	0.007	0.007	0.000	0.000	0.000	0.000
42	A	43	ALA	0	-0.006	-0.010	31.712	-0.099	-0.099	0.000	0.000	0.000	0.000
43	A	44	LYS	1	0.956	0.969	32.765	8.073	8.073	0.000	0.000	0.000	0.000
44	A	45	LYS	1	0.939	0.982	35.119	8.508	8.508	0.000	0.000	0.000	0.000
45	A	46	GLY	0	0.025	0.022	32.792	-0.057	-0.057	0.000	0.000	0.000	0.000
46	A	47	LEU	0	-0.044	-0.004	29.208	-0.380	-0.380	0.000	0.000	0.000	0.000
47	A	48	THR	0	-0.002	-0.030	23.500	-0.065	-0.065	0.000	0.000	0.000	0.000
48	A	49	PRO	0	-0.023	-0.033	24.262	0.035	0.035	0.000	0.000	0.000	0.000
49	A	50	SER	0	-0.027	-0.034	20.879	0.215	0.215	0.000	0.000	0.000	0.000
50	A	51	GLN	0	0.049	0.035	22.744	0.343	0.343	0.000	0.000	0.000	0.000
51	A	52	ILE	0	-0.009	0.015	25.220	0.285	0.285	0.000	0.000	0.000	0.000
52	A	53	GLY	0	0.003	-0.011	24.637	0.289	0.289	0.000	0.000	0.000	0.000
53	A	54	VAL	0	-0.046	-0.010	22.594	0.050	0.050	0.000	0.000	0.000	0.000
54	A	55	ILE	0	0.056	0.027	25.255	0.270	0.270	0.000	0.000	0.000	0.000
55	A	56	LEU	0	-0.035	-0.026	28.793	0.332	0.332	0.000	0.000	0.000	0.000
56	A	57	ARG	1	0.826	0.905	21.522	13.402	13.402	0.000	0.000	0.000	0.000
57	A	58	ASP	-1	-0.825	-0.903	26.160	-11.975	-11.975	0.000	0.000	0.000	0.000
58	A	59	GLN	0	-0.053	-0.023	28.887	0.061	0.061	0.000	0.000	0.000	0.000
59	A	60	HIS	0	0.011	-0.001	32.008	0.365	0.365	0.000	0.000	0.000	0.000
60	A	61	GLY	0	0.065	0.053	31.300	0.184	0.184	0.000	0.000	0.000	0.000
61	A	62	ILE	0	-0.038	-0.030	29.497	0.028	0.028	0.000	0.000	0.000	0.000
62	A	63	PRO	0	-0.022	-0.005	26.244	-0.371	-0.371	0.000	0.000	0.000	0.000
63	A	64	GLN	0	0.012	-0.009	21.581	-0.626	-0.626	0.000	0.000	0.000	0.000
64	A	65	VAL	0	0.072	0.039	25.899	0.243	0.243	0.000	0.000	0.000	0.000
65	A	66	ARG	1	0.894	0.952	21.538	13.453	13.453	0.000	0.000	0.000	0.000
66	A	67	PHE	0	0.006	-0.017	23.808	-0.083	-0.083	0.000	0.000	0.000	0.000
67	A	68	LEU	0	0.039	0.062	28.584	0.191	0.191	0.000	0.000	0.000	0.000
68	A	69	THR	0	-0.010	-0.007	30.892	0.325	0.325	0.000	0.000	0.000	0.000
69	A	70	GLY	0	0.030	0.032	29.850	0.199	0.199	0.000	0.000	0.000	0.000
70	A	71	GLN	0	-0.031	-0.023	29.064	-0.594	-0.594	0.000	0.000	0.000	0.000
71	A	72	LYS	1	0.967	0.969	21.297	13.758	13.758	0.000	0.000	0.000	0.000
72	A	73	ILE	0	0.099	0.056	25.091	0.247	0.247	0.000	0.000	0.000	0.000
73	A	74	LEU	0	0.041	0.019	24.125	0.337	0.337	0.000	0.000	0.000	0.000
74	A	75	ARG	1	0.883	0.931	26.348	11.544	11.544	0.000	0.000	0.000	0.000
75	A	76	ILE	0	0.026	0.024	29.359	0.308	0.308	0.000	0.000	0.000	0.000
76	A	77	LEU	0	0.016	0.013	28.389	0.266	0.266	0.000	0.000	0.000	0.000
77	A	78	LYS	1	0.940	0.968	27.169	11.677	11.677	0.000	0.000	0.000	0.000
78	A	79	LYS	1	0.924	0.963	32.399	9.436	9.436	0.000	0.000	0.000	0.000
79	A	80	ASN	0	-0.026	-0.013	34.896	0.441	0.441	0.000	0.000	0.000	0.000
80	A	81	GLY	0	0.045	0.030	36.094	0.142	0.142	0.000	0.000	0.000	0.000
81	A	82	CYS	0	-0.012	0.005	32.924	0.020	0.020	0.000	0.000	0.000	0.000
82	A	83	ALA	0	-0.024	-0.017	31.400	-0.372	-0.372	0.000	0.000	0.000	0.000
83	A	84	PRO	0	-0.022	-0.012	27.383	0.106	0.106	0.000	0.000	0.000	0.000
84	A	85	GLN	0	0.024	0.005	28.429	-0.480	-0.480	0.000	0.000	0.000	0.000
85	A	86	LEU	0	0.010	0.023	25.256	-0.236	-0.236	0.000	0.000	0.000	0.000
86	A	87	PRO	0	-0.025	-0.013	22.216	-0.063	-0.063	0.000	0.000	0.000	0.000
87	A	88	GLU	-1	-0.782	-0.894	20.377	-15.220	-15.220	0.000	0.000	0.000	0.000
88	A	89	ASP	-1	-0.935	-0.963	16.622	-19.504	-19.504	0.000	0.000	0.000	0.000
89	A	90	LEU	0	0.035	0.002	18.905	-0.467	-0.467	0.000	0.000	0.000	0.000
90	A	91	TYR	0	0.035	0.030	20.624	-0.137	-0.137	0.000	0.000	0.000	0.000
91	A	92	PHE	0	0.042	0.012	19.478	0.272	0.272	0.000	0.000	0.000	0.000
92	A	93	LEU	0	-0.066	-0.032	15.109	-0.462	-0.462	0.000	0.000	0.000	0.000
93	A	94	ILE	0	0.039	0.017	19.202	0.027	0.027	0.000	0.000	0.000	0.000
94	A	95	LYS	1	1.015	1.025	22.752	12.342	12.342	0.000	0.000	0.000	0.000
95	A	96	LYS	1	0.918	0.977	16.959	18.283	18.283	0.000	0.000	0.000	0.000
96	A	97	ALA	0	0.017	0.001	20.648	0.155	0.155	0.000	0.000	0.000	0.000
97	A	98	LEU	0	0.023	0.014	21.822	0.304	0.304	0.000	0.000	0.000	0.000
98	A	99	SER	0	-0.006	-0.018	23.522	0.532	0.532	0.000	0.000	0.000	0.000
99	A	100	ILE	0	-0.054	-0.029	18.944	0.156	0.156	0.000	0.000	0.000	0.000
100	A	101	ARG	1	0.857	0.927	23.514	12.881	12.881	0.000	0.000	0.000	0.000
101	A	102	LYS	1	0.977	1.000	26.344	10.346	10.346	0.000	0.000	0.000	0.000
102	A	103	HIS	0	-0.026	-0.012	24.878	0.575	0.575	0.000	0.000	0.000	0.000
103	A	104	LEU	0	-0.035	-0.031	24.144	0.204	0.204	0.000	0.000	0.000	0.000
104	A	105	GLU	-1	-0.947	-0.975	27.515	-9.881	-9.881	0.000	0.000	0.000	0.000
105	A	106	LYS	1	0.980	1.000	30.969	9.454	9.454	0.000	0.000	0.000	0.000
106	A	107	ASN	0	-0.014	0.000	28.322	0.417	0.417	0.000	0.000	0.000	0.000
107	A	108	ARG	1	0.988	0.985	28.435	9.102	9.102	0.000	0.000	0.000	0.000
108	A	109	LYS	1	0.949	0.967	29.397	9.661	9.661	0.000	0.000	0.000	0.000
109	A	110	ASP	-1	-0.779	-0.849	23.479	-13.751	-13.751	0.000	0.000	0.000	0.000
110	A	111	LYS	1	0.983	0.970	22.723	11.876	11.876	0.000	0.000	0.000	0.000
111	A	112	ASP	-1	-0.799	-0.860	17.669	-18.758	-18.758	0.000	0.000	0.000	0.000
112	A	113	SER	0	0.022	-0.021	19.052	-1.023	-1.023	0.000	0.000	0.000	0.000
113	A	114	LYS	1	0.986	0.993	20.668	12.207	12.207	0.000	0.000	0.000	0.000
114	A	115	TYR	0	0.006	0.006	12.885	-0.909	-0.909	0.000	0.000	0.000	0.000
115	A	116	ARG	1	0.820	0.868	12.655	19.743	19.743	0.000	0.000	0.000	0.000
116	A	117	LEU	0	0.008	0.021	16.864	-0.739	-0.739	0.000	0.000	0.000	0.000
117	A	118	ILE	0	0.044	0.032	16.710	-0.464	-0.464	0.000	0.000	0.000	0.000
118	A	119	LEU	0	-0.054	-0.024	11.485	-1.002	-1.002	0.000	0.000	0.000	0.000
119	A	120	VAL	0	-0.015	-0.010	14.090	-1.542	-1.542	0.000	0.000	0.000	0.000
120	A	121	GLU	-1	-0.726	-0.846	16.201	-14.144	-14.144	0.000	0.000	0.000	0.000
121	A	122	SER	0	-0.034	-0.006	14.632	-0.179	-0.179	0.000	0.000	0.000	0.000
122	A	123	ARG	1	0.829	0.904	11.532	24.495	24.495	0.000	0.000	0.000	0.000
123	A	124	ILE	0	0.052	0.036	14.827	0.078	0.078	0.000	0.000	0.000	0.000
124	A	125	HIS	0	0.036	0.033	18.507	0.407	0.407	0.000	0.000	0.000	0.000
125	A	126	ARG	1	0.888	0.940	9.341	28.260	28.260	0.000	0.000	0.000	0.000
126	A	127	LEU	0	-0.015	0.002	14.545	-0.016	-0.016	0.000	0.000	0.000	0.000
127	A	128	SER	0	0.029	-0.015	17.229	0.959	0.959	0.000	0.000	0.000	0.000
128	A	129	ARG	1	0.944	0.982	15.856	18.362	18.362	0.000	0.000	0.000	0.000
129	A	130	TYR	0	0.019	0.016	17.208	0.513	0.513	0.000	0.000	0.000	0.000
130	A	131	TYR	0	0.051	0.002	19.338	0.571	0.571	0.000	0.000	0.000	0.000
131	A	132	LYS	1	0.806	0.907	22.240	12.666	12.666	0.000	0.000	0.000	0.000
132	A	133	LEU	0	0.013	0.013	20.766	0.409	0.409	0.000	0.000	0.000	0.000
133	A	134	ASN	0	-0.012	0.014	20.923	0.557	0.557	0.000	0.000	0.000	0.000
134	A	135	GLN	0	0.027	0.020	24.527	0.070	0.070	0.000	0.000	0.000	0.000
135	A	136	LYS	1	0.778	0.869	24.061	12.288	12.288	0.000	0.000	0.000	0.000
136	A	137	LEU	0	0.029	0.020	23.625	-0.084	-0.084	0.000	0.000	0.000	0.000
137	A	138	PRO	0	0.067	0.037	27.013	0.038	0.038	0.000	0.000	0.000	0.000
138	A	139	PRO	0	0.087	0.044	29.037	-0.321	-0.321	0.000	0.000	0.000	0.000
139	A	140	LYS	1	0.966	0.967	29.471	9.294	9.294	0.000	0.000	0.000	0.000
140	A	141	TRP	0	0.046	0.045	24.143	-0.109	-0.109	0.000	0.000	0.000	0.000
141	A	142	LYS	1	0.977	0.971	26.854	10.366	10.366	0.000	0.000	0.000	0.000
142	A	143	TYR	0	-0.016	-0.018	23.294	0.276	0.276	0.000	0.000	0.000	0.000
143	A	144	ASN	0	-0.017	-0.019	25.740	-0.118	-0.118	0.000	0.000	0.000	0.000
144	A	145	ALA	0	-0.054	-0.042	27.905	-0.085	-0.085	0.000	0.000	0.000	0.000
145	A	146	GLN	0	0.124	0.053	28.797	-0.187	-0.187	0.000	0.000	0.000	0.000
146	A	147	THR	0	-0.002	0.009	29.540	0.120	0.120	0.000	0.000	0.000	0.000
147	A	148	ALA	0	-0.019	-0.028	26.589	0.058	0.058	0.000	0.000	0.000	0.000
148	A	149	SER	0	0.013	0.006	28.652	-0.098	-0.098	0.000	0.000	0.000	0.000
149	A	150	ALA	0	0.066	0.047	30.635	0.263	0.263	0.000	0.000	0.000	0.000
150	A	151	LEU	0	-0.111	-0.047	29.180	0.166	0.166	0.000	0.000	0.000	0.000
151	A	152	VAL	0	-0.045	-0.034	29.925	-0.304	-0.304	0.000	0.000	0.000	0.000
152	A	153	GLN	-1	-0.923	-0.953	25.317	-10.899	-10.899	0.000	0.000	0.000	0.000

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