FMO DATABASE

FMODB ID: NL1YQ

Calculation Name: 1S03-G-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1S03

Chain ID: G

ChEMBL ID:

UniProt ID: P0A7W7

Base Structure: X-ray

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1006777.794383
FMO2-HF: Nuclear repulsion	958763.535707
FMO2-HF: Total energy	-48014.258676
FMO2-MP2: Total energy	-48153.270695

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:4:ASP)

Summations of interaction energy for fragment #1(A:4:ASP)

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.
-103.615	-91.189	19.805	-13.503	-18.727	0.154

Interaction energy analysis for fragmet #1(A:4:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.070 / q_NPA : 0.016

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	6	ILE	0	0.067	0.050	2.353	-7.659	-2.307	1.812	-3.152	-4.013	0.026
4	A	7	ALA	0	-0.011	0.001	2.450	-9.426	-5.872	2.459	-2.695	-3.318	0.031
5	A	8	ASP	-1	-0.831	-0.887	4.308	-7.717	-7.311	0.008	-0.113	-0.300	0.000
73	A	76	ARG	1	0.816	0.899	1.945	-51.301	-52.211	10.299	-3.962	-5.427	0.056
76	A	79	ARG	1	0.925	0.946	2.131	-23.999	-22.147	3.759	-2.278	-3.333	0.030
77	A	80	PRO	0	-0.056	-0.028	2.669	-9.382	-7.290	1.469	-1.298	-2.263	0.011
78	A	81	GLY	0	0.034	0.012	5.079	-0.201	-0.121	-0.001	-0.005	-0.073	0.000
6	A	9	MET	0	0.026	0.020	6.423	1.187	1.187	0.000	0.000	0.000	0.000
7	A	10	LEU	0	0.021	-0.006	6.787	-0.542	-0.542	0.000	0.000	0.000	0.000
8	A	11	THR	0	-0.024	-0.023	7.135	-0.483	-0.483	0.000	0.000	0.000	0.000
9	A	12	ARG	1	0.823	0.894	9.442	2.317	2.317	0.000	0.000	0.000	0.000
10	A	13	ILE	0	0.035	0.029	11.223	-0.144	-0.144	0.000	0.000	0.000	0.000
11	A	14	ARG	1	0.853	0.926	8.519	-4.920	-4.920	0.000	0.000	0.000	0.000
12	A	15	ASN	0	0.013	-0.009	12.635	0.114	0.114	0.000	0.000	0.000	0.000
13	A	16	GLY	0	0.015	0.006	15.364	-0.215	-0.215	0.000	0.000	0.000	0.000
14	A	17	GLN	0	-0.001	-0.005	17.316	0.046	0.046	0.000	0.000	0.000	0.000
15	A	18	ALA	0	0.008	0.010	18.181	-0.091	-0.091	0.000	0.000	0.000	0.000
16	A	19	ALA	0	-0.037	-0.015	19.484	-0.119	-0.119	0.000	0.000	0.000	0.000
17	A	20	ASN	0	-0.005	-0.005	21.237	-0.068	-0.068	0.000	0.000	0.000	0.000
18	A	21	LYS	1	0.867	0.949	19.373	-0.031	-0.031	0.000	0.000	0.000	0.000
19	A	22	ALA	0	0.091	0.046	21.473	0.136	0.136	0.000	0.000	0.000	0.000
20	A	23	ALA	0	0.040	0.023	20.160	0.118	0.118	0.000	0.000	0.000	0.000
21	A	24	VAL	0	-0.064	-0.026	14.876	-0.163	-0.163	0.000	0.000	0.000	0.000
22	A	25	THR	0	0.079	0.056	16.403	0.179	0.179	0.000	0.000	0.000	0.000
23	A	26	MET	0	-0.031	-0.003	10.888	-0.162	-0.162	0.000	0.000	0.000	0.000
24	A	27	PRO	0	0.025	0.016	10.187	0.287	0.287	0.000	0.000	0.000	0.000
25	A	28	SER	0	0.049	0.033	11.091	0.307	0.307	0.000	0.000	0.000	0.000
26	A	29	SER	0	0.007	-0.012	9.691	-0.092	-0.092	0.000	0.000	0.000	0.000
27	A	30	LYS	1	1.024	1.001	12.333	0.029	0.029	0.000	0.000	0.000	0.000
28	A	31	LEU	0	0.015	0.020	7.058	0.275	0.275	0.000	0.000	0.000	0.000
29	A	32	LYS	1	0.828	0.910	7.343	2.206	2.206	0.000	0.000	0.000	0.000
30	A	33	VAL	0	0.034	0.023	10.344	0.134	0.134	0.000	0.000	0.000	0.000
31	A	34	ALA	0	0.009	0.006	12.986	0.011	0.011	0.000	0.000	0.000	0.000
32	A	35	ILE	0	-0.027	-0.023	7.965	0.387	0.387	0.000	0.000	0.000	0.000
33	A	36	ALA	0	0.004	-0.002	12.263	-0.097	-0.097	0.000	0.000	0.000	0.000
34	A	37	ASN	0	-0.047	-0.019	14.625	-0.383	-0.383	0.000	0.000	0.000	0.000
35	A	38	VAL	0	0.031	0.022	15.019	-0.068	-0.068	0.000	0.000	0.000	0.000
36	A	39	LEU	0	-0.039	-0.031	12.774	0.015	0.015	0.000	0.000	0.000	0.000
37	A	40	LYS	1	0.863	0.934	16.634	-1.220	-1.220	0.000	0.000	0.000	0.000
38	A	41	GLU	-1	-0.898	-0.947	19.930	1.770	1.770	0.000	0.000	0.000	0.000
39	A	42	GLU	-1	-0.912	-0.957	19.049	1.957	1.957	0.000	0.000	0.000	0.000
40	A	43	GLY	0	-0.014	-0.001	19.832	0.134	0.134	0.000	0.000	0.000	0.000
41	A	44	PHE	0	0.005	-0.013	17.615	-0.076	-0.076	0.000	0.000	0.000	0.000
42	A	45	ILE	0	-0.087	-0.044	16.130	-0.050	-0.050	0.000	0.000	0.000	0.000
43	A	46	GLU	-1	-0.963	-0.981	19.486	0.725	0.725	0.000	0.000	0.000	0.000
44	A	47	ASP	-1	-0.820	-0.915	21.603	0.749	0.749	0.000	0.000	0.000	0.000
45	A	48	PHE	0	-0.041	-0.016	17.439	0.079	0.079	0.000	0.000	0.000	0.000
46	A	49	LYS	1	0.958	0.997	19.207	-0.195	-0.195	0.000	0.000	0.000	0.000
47	A	50	VAL	0	-0.047	-0.037	17.208	-0.033	-0.033	0.000	0.000	0.000	0.000
48	A	51	GLU	-1	-0.921	-0.955	19.661	-0.631	-0.631	0.000	0.000	0.000	0.000
49	A	52	GLY	0	0.010	0.005	21.309	0.053	0.053	0.000	0.000	0.000	0.000
50	A	53	ASP	-1	-0.834	-0.923	20.736	-0.722	-0.722	0.000	0.000	0.000	0.000
51	A	54	THR	0	-0.044	-0.013	19.571	-0.143	-0.143	0.000	0.000	0.000	0.000
52	A	55	LYS	1	0.866	0.918	14.152	2.375	2.375	0.000	0.000	0.000	0.000
53	A	56	PRO	0	0.019	0.030	15.895	0.074	0.074	0.000	0.000	0.000	0.000
54	A	57	GLU	-1	-0.917	-0.957	15.424	-1.687	-1.687	0.000	0.000	0.000	0.000
55	A	58	LEU	0	-0.066	-0.050	12.512	0.291	0.291	0.000	0.000	0.000	0.000
56	A	59	GLU	-1	-0.876	-0.940	15.680	-0.037	-0.037	0.000	0.000	0.000	0.000
57	A	60	LEU	0	-0.048	-0.040	12.659	0.319	0.319	0.000	0.000	0.000	0.000
58	A	61	THR	0	0.029	0.008	17.316	-0.178	-0.178	0.000	0.000	0.000	0.000
59	A	62	LEU	0	-0.072	-0.034	16.214	0.227	0.227	0.000	0.000	0.000	0.000
60	A	63	LYS	1	0.942	0.978	20.163	-1.401	-1.401	0.000	0.000	0.000	0.000
61	A	64	TYR	0	-0.009	-0.028	21.424	0.119	0.119	0.000	0.000	0.000	0.000
62	A	65	PHE	0	0.004	0.008	25.245	-0.053	-0.053	0.000	0.000	0.000	0.000
63	A	66	GLN	0	-0.032	-0.027	27.904	-0.012	-0.012	0.000	0.000	0.000	0.000
64	A	67	GLY	0	0.046	0.031	29.104	-0.038	-0.038	0.000	0.000	0.000	0.000
65	A	68	LYS	1	0.933	0.975	25.440	-0.937	-0.937	0.000	0.000	0.000	0.000
66	A	69	ALA	0	0.002	0.006	20.621	-0.042	-0.042	0.000	0.000	0.000	0.000
67	A	70	VAL	0	-0.021	-0.015	21.558	0.001	0.001	0.000	0.000	0.000	0.000
68	A	71	VAL	0	-0.045	-0.008	15.283	0.206	0.206	0.000	0.000	0.000	0.000
69	A	72	GLU	-1	-0.936	-0.958	18.712	1.400	1.400	0.000	0.000	0.000	0.000
70	A	73	SER	0	-0.105	-0.065	15.227	0.139	0.139	0.000	0.000	0.000	0.000
71	A	74	ILE	0	0.041	0.024	10.736	0.323	0.323	0.000	0.000	0.000	0.000
72	A	75	GLN	0	0.005	0.004	9.368	0.639	0.639	0.000	0.000	0.000	0.000
74	A	77	VAL	0	-0.018	0.006	6.341	-1.688	-1.688	0.000	0.000	0.000	0.000
75	A	78	SER	0	-0.070	-0.042	7.102	-0.764	-0.764	0.000	0.000	0.000	0.000
79	A	82	LEU	0	0.021	0.005	7.295	-0.748	-0.748	0.000	0.000	0.000	0.000
80	A	83	ARG	1	0.832	0.917	6.592	-5.884	-5.884	0.000	0.000	0.000	0.000
81	A	84	ILE	0	0.006	0.008	9.412	-1.121	-1.121	0.000	0.000	0.000	0.000
82	A	85	TYR	0	0.038	0.007	11.225	0.577	0.577	0.000	0.000	0.000	0.000
83	A	86	LYS	1	0.926	0.972	14.134	-3.598	-3.598	0.000	0.000	0.000	0.000
84	A	87	ARG	1	0.987	0.984	17.283	-1.730	-1.730	0.000	0.000	0.000	0.000
85	A	88	LYS	1	0.948	0.965	20.838	-1.409	-1.409	0.000	0.000	0.000	0.000
86	A	89	ASP	-1	-0.860	-0.931	22.663	1.555	1.555	0.000	0.000	0.000	0.000
87	A	90	GLU	-1	-0.883	-0.930	20.047	2.353	2.353	0.000	0.000	0.000	0.000
88	A	91	LEU	0	-0.025	0.006	17.546	0.287	0.287	0.000	0.000	0.000	0.000
89	A	92	PRO	0	0.034	0.024	17.727	-0.272	-0.272	0.000	0.000	0.000	0.000
90	A	93	LYS	1	0.977	0.994	20.523	-1.613	-1.613	0.000	0.000	0.000	0.000
91	A	94	VAL	0	-0.038	-0.021	23.586	-0.144	-0.144	0.000	0.000	0.000	0.000
92	A	95	MET	0	0.038	0.018	23.187	-0.063	-0.063	0.000	0.000	0.000	0.000
93	A	96	ALA	0	-0.001	0.010	20.785	-0.046	-0.046	0.000	0.000	0.000	0.000
94	A	97	GLY	0	-0.014	-0.020	22.768	0.013	0.013	0.000	0.000	0.000	0.000
95	A	98	LEU	0	0.015	0.003	22.869	-0.126	-0.126	0.000	0.000	0.000	0.000
96	A	99	GLY	0	-0.002	0.022	19.080	0.072	0.072	0.000	0.000	0.000	0.000
97	A	100	ILE	0	-0.011	0.006	15.864	-0.095	-0.095	0.000	0.000	0.000	0.000
98	A	101	ALA	0	-0.052	-0.040	14.299	0.521	0.521	0.000	0.000	0.000	0.000
99	A	102	VAL	0	0.015	0.012	11.403	-0.407	-0.407	0.000	0.000	0.000	0.000
100	A	103	VAL	0	-0.017	-0.020	11.968	1.116	1.116	0.000	0.000	0.000	0.000
101	A	104	SER	0	-0.011	-0.006	11.118	-0.649	-0.649	0.000	0.000	0.000	0.000
102	A	105	THR	0	0.040	0.008	13.219	-0.185	-0.185	0.000	0.000	0.000	0.000
103	A	106	SER	0	-0.018	-0.016	16.861	-0.040	-0.040	0.000	0.000	0.000	0.000
104	A	107	LYS	1	0.932	0.955	19.255	-1.525	-1.525	0.000	0.000	0.000	0.000
105	A	108	GLY	0	0.050	0.042	16.694	-0.122	-0.122	0.000	0.000	0.000	0.000
106	A	109	VAL	0	-0.040	-0.023	12.089	0.267	0.267	0.000	0.000	0.000	0.000
107	A	110	MET	0	0.020	0.030	14.957	-0.420	-0.420	0.000	0.000	0.000	0.000
108	A	111	THR	0	0.101	0.052	15.839	0.509	0.509	0.000	0.000	0.000	0.000
109	A	112	ASP	-1	-0.833	-0.933	17.963	2.822	2.822	0.000	0.000	0.000	0.000
110	A	113	ARG	1	0.981	0.990	19.174	-2.194	-2.194	0.000	0.000	0.000	0.000
111	A	114	ALA	0	0.061	0.043	20.565	-0.170	-0.170	0.000	0.000	0.000	0.000
112	A	115	ALA	0	0.008	-0.001	18.904	-0.151	-0.151	0.000	0.000	0.000	0.000
113	A	116	ARG	1	0.764	0.844	21.063	-2.232	-2.232	0.000	0.000	0.000	0.000
114	A	117	GLN	0	-0.040	-0.010	23.957	-0.073	-0.073	0.000	0.000	0.000	0.000
115	A	118	ALA	0	-0.011	-0.003	23.248	-0.121	-0.121	0.000	0.000	0.000	0.000
116	A	119	GLY	0	0.004	0.009	25.391	-0.073	-0.073	0.000	0.000	0.000	0.000
117	A	120	LEU	0	-0.067	-0.033	20.610	-0.006	-0.006	0.000	0.000	0.000	0.000
118	A	121	GLY	0	0.029	0.003	19.473	0.072	0.072	0.000	0.000	0.000	0.000
119	A	122	GLY	0	-0.008	-0.020	15.762	-0.146	-0.146	0.000	0.000	0.000	0.000
120	A	123	GLU	-1	-0.824	-0.856	7.895	10.881	10.881	0.000	0.000	0.000	0.000
121	A	124	ILE	0	0.014	0.010	10.963	0.027	0.027	0.000	0.000	0.000	0.000
122	A	125	ILE	0	-0.003	-0.007	6.639	2.289	2.289	0.000	0.000	0.000	0.000
123	A	126	CYS	0	-0.023	-0.038	7.016	4.359	4.359	0.000	0.000	0.000	0.000
124	A	127	TYR	0	0.022	0.020	9.400	-1.150	-1.150	0.000	0.000	0.000	0.000
125	A	128	VAL	0	0.004	-0.006	12.227	0.649	0.649	0.000	0.000	0.000	0.000
126	A	129	ALA	-1	-0.755	-0.852	14.816	2.371	2.371	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:ASP)