FMO DATABASE

FMODB ID: 1VL2Z

Calculation Name: 1ECS-A-Xray549

Preferred Name:

Target Type:

Ligand Name: tetraethylene glycol | calcium ion

Ligand 3-letter code: PG4 | CA

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1ECS

Chain ID: A

ChEMBL ID:

UniProt ID: P13081

Base Structure: X-ray

Registration Date: 2025-10-11

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	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	120
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-988032.412806
FMO2-HF: Nuclear repulsion	940319.718106
FMO2-HF: Total energy	-47712.6947
FMO2-MP2: Total energy	-47849.744507

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:THR)

Summations of interaction energy for fragment #1(A:2:THR)

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.
-114.839	-112.223	0.187	-1.196	-1.607	-0.011

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.821 / q_NPA : 0.893

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	GLN	0	0.009	-0.008	2.923	-2.303	0.306	0.188	-1.194	-1.604	-0.011
4	A	5	ALA	0	-0.026	-0.006	5.260	2.144	2.151	-0.001	-0.002	-0.003	0.000
5	A	6	THR	0	-0.007	-0.025	8.994	0.052	0.052	0.000	0.000	0.000	0.000
6	A	7	PRO	0	-0.042	-0.026	11.051	1.418	1.418	0.000	0.000	0.000	0.000
7	A	8	ASN	0	0.030	0.021	14.641	-0.671	-0.671	0.000	0.000	0.000	0.000
8	A	9	LEU	0	-0.039	-0.027	17.357	0.758	0.758	0.000	0.000	0.000	0.000
9	A	10	PRO	0	0.007	0.016	20.339	-0.081	-0.081	0.000	0.000	0.000	0.000
10	A	11	SER	0	-0.022	-0.032	23.912	-0.049	-0.049	0.000	0.000	0.000	0.000
11	A	12	ARG	1	0.826	0.911	25.917	10.120	10.120	0.000	0.000	0.000	0.000
12	A	13	ASP	-1	-0.816	-0.889	28.392	-10.256	-10.256	0.000	0.000	0.000	0.000
13	A	14	PHE	0	0.011	0.002	23.114	-0.170	-0.170	0.000	0.000	0.000	0.000
14	A	15	ASP	-1	-0.812	-0.870	25.499	-11.439	-11.439	0.000	0.000	0.000	0.000
15	A	16	SER	0	-0.062	-0.057	27.716	-0.029	-0.029	0.000	0.000	0.000	0.000
16	A	17	THR	0	-0.044	-0.024	22.805	0.011	0.011	0.000	0.000	0.000	0.000
17	A	18	ALA	0	0.019	0.003	22.866	-0.317	-0.317	0.000	0.000	0.000	0.000
18	A	19	ALA	0	0.015	0.008	23.896	-0.158	-0.158	0.000	0.000	0.000	0.000
19	A	20	PHE	0	-0.048	-0.027	24.547	0.353	0.353	0.000	0.000	0.000	0.000
20	A	21	TYR	0	-0.011	-0.053	20.073	-0.184	-0.184	0.000	0.000	0.000	0.000
21	A	22	GLU	-1	-0.921	-0.942	21.703	-12.563	-12.563	0.000	0.000	0.000	0.000
22	A	23	ARG	1	0.908	0.959	23.065	10.680	10.680	0.000	0.000	0.000	0.000
23	A	24	LEU	0	-0.015	-0.010	21.497	0.221	0.221	0.000	0.000	0.000	0.000
24	A	25	GLY	0	-0.013	-0.006	20.251	-0.517	-0.517	0.000	0.000	0.000	0.000
25	A	26	PHE	0	-0.047	-0.030	15.306	-0.740	-0.740	0.000	0.000	0.000	0.000
26	A	27	GLY	0	0.038	0.028	17.280	0.900	0.900	0.000	0.000	0.000	0.000
27	A	28	ILE	0	-0.012	-0.023	17.255	-0.791	-0.791	0.000	0.000	0.000	0.000
28	A	29	VAL	0	-0.041	-0.011	12.605	0.093	0.093	0.000	0.000	0.000	0.000
29	A	30	PHE	0	-0.022	-0.018	15.936	-0.080	-0.080	0.000	0.000	0.000	0.000
30	A	31	ARG	1	0.816	0.868	17.750	12.359	12.359	0.000	0.000	0.000	0.000
31	A	32	ASP	-1	-0.835	-0.899	21.113	-14.179	-14.179	0.000	0.000	0.000	0.000
32	A	33	ALA	0	-0.035	-0.031	23.338	0.237	0.237	0.000	0.000	0.000	0.000
33	A	34	GLY	0	-0.024	-0.013	24.193	0.435	0.435	0.000	0.000	0.000	0.000
34	A	35	TRP	0	-0.046	-0.036	15.641	0.771	0.771	0.000	0.000	0.000	0.000
35	A	36	MET	0	-0.022	-0.001	19.561	0.523	0.523	0.000	0.000	0.000	0.000
36	A	37	ILE	0	-0.014	0.007	12.886	-0.332	-0.332	0.000	0.000	0.000	0.000
37	A	38	LEU	0	0.010	0.001	15.883	0.669	0.669	0.000	0.000	0.000	0.000
38	A	39	GLN	0	-0.002	-0.008	10.741	-1.566	-1.566	0.000	0.000	0.000	0.000
39	A	40	ARG	1	0.815	0.916	13.776	17.102	17.102	0.000	0.000	0.000	0.000
40	A	41	GLY	0	-0.007	-0.004	12.405	-0.116	-0.116	0.000	0.000	0.000	0.000
41	A	42	ASP	-1	-0.890	-0.955	7.144	-32.518	-32.518	0.000	0.000	0.000	0.000
42	A	43	LEU	0	-0.059	-0.015	8.952	-1.165	-1.165	0.000	0.000	0.000	0.000
43	A	44	MET	0	0.005	0.009	9.274	0.530	0.530	0.000	0.000	0.000	0.000
44	A	45	LEU	0	-0.033	-0.020	11.676	0.091	0.091	0.000	0.000	0.000	0.000
45	A	46	GLU	-1	-0.798	-0.863	12.483	-24.236	-24.236	0.000	0.000	0.000	0.000
46	A	47	PHE	0	-0.007	-0.011	16.167	0.705	0.705	0.000	0.000	0.000	0.000
47	A	48	PHE	0	-0.012	-0.001	19.971	0.135	0.135	0.000	0.000	0.000	0.000
48	A	49	ALA	0	0.002	-0.001	22.430	0.429	0.429	0.000	0.000	0.000	0.000
49	A	50	HIS	0	-0.025	-0.027	26.061	0.189	0.189	0.000	0.000	0.000	0.000
50	A	51	PRO	0	0.039	0.005	28.396	0.159	0.159	0.000	0.000	0.000	0.000
51	A	52	GLY	0	-0.045	-0.015	31.781	0.311	0.311	0.000	0.000	0.000	0.000
52	A	53	LEU	0	-0.035	-0.006	27.630	0.125	0.125	0.000	0.000	0.000	0.000
53	A	54	ASP	-1	-0.822	-0.925	31.498	-8.741	-8.741	0.000	0.000	0.000	0.000
54	A	55	PRO	0	-0.052	-0.028	30.493	-0.159	-0.159	0.000	0.000	0.000	0.000
55	A	56	LEU	0	-0.058	-0.036	31.349	-0.124	-0.124	0.000	0.000	0.000	0.000
56	A	57	ALA	0	-0.014	0.008	33.284	0.051	0.051	0.000	0.000	0.000	0.000
57	A	58	SER	0	-0.018	-0.007	27.080	-0.291	-0.291	0.000	0.000	0.000	0.000
58	A	59	TRP	0	-0.019	-0.012	26.997	0.022	0.022	0.000	0.000	0.000	0.000
59	A	60	PHE	0	-0.011	0.005	22.470	-0.409	-0.409	0.000	0.000	0.000	0.000
60	A	61	SER	0	-0.004	0.000	21.833	0.299	0.299	0.000	0.000	0.000	0.000
61	A	62	CYS	0	-0.002	0.009	16.400	-0.398	-0.398	0.000	0.000	0.000	0.000
62	A	63	CYS	0	-0.054	-0.023	15.432	1.081	1.081	0.000	0.000	0.000	0.000
63	A	64	LEU	0	0.022	0.022	14.798	-1.118	-1.118	0.000	0.000	0.000	0.000
64	A	65	ARG	1	0.926	0.966	12.864	18.528	18.528	0.000	0.000	0.000	0.000
65	A	66	LEU	0	0.008	0.003	13.400	-1.146	-1.146	0.000	0.000	0.000	0.000
66	A	67	ASP	-1	-0.789	-0.882	13.048	-19.083	-19.083	0.000	0.000	0.000	0.000
67	A	68	ASP	-1	-0.818	-0.902	16.153	-12.073	-12.073	0.000	0.000	0.000	0.000
68	A	69	LEU	0	-0.007	-0.006	19.467	-0.080	-0.080	0.000	0.000	0.000	0.000
69	A	70	ALA	0	-0.020	-0.015	21.122	0.449	0.449	0.000	0.000	0.000	0.000
70	A	71	GLU	-1	-0.958	-0.984	19.802	-13.919	-13.919	0.000	0.000	0.000	0.000
71	A	72	PHE	0	0.065	0.033	18.674	0.368	0.368	0.000	0.000	0.000	0.000
72	A	73	TYR	0	-0.007	-0.037	21.894	0.289	0.289	0.000	0.000	0.000	0.000
73	A	74	ARG	1	0.910	0.963	24.947	11.762	11.762	0.000	0.000	0.000	0.000
74	A	75	GLN	0	0.011	0.016	22.092	0.002	0.002	0.000	0.000	0.000	0.000
75	A	76	CYS	0	-0.006	-0.004	23.955	0.250	0.250	0.000	0.000	0.000	0.000
76	A	77	LYS	1	0.943	0.968	26.659	9.792	9.792	0.000	0.000	0.000	0.000
77	A	78	SER	0	-0.128	-0.056	28.194	0.287	0.287	0.000	0.000	0.000	0.000
78	A	79	VAL	0	-0.018	-0.008	27.027	0.257	0.257	0.000	0.000	0.000	0.000
79	A	80	GLY	0	-0.002	0.008	30.183	0.073	0.073	0.000	0.000	0.000	0.000
80	A	81	ILE	0	-0.017	0.006	26.911	0.210	0.210	0.000	0.000	0.000	0.000
81	A	82	GLN	0	-0.018	-0.021	31.140	0.257	0.257	0.000	0.000	0.000	0.000
82	A	83	GLU	-1	-0.840	-0.895	32.338	-9.506	-9.506	0.000	0.000	0.000	0.000
83	A	84	THR	0	-0.027	-0.016	33.412	0.329	0.329	0.000	0.000	0.000	0.000
84	A	85	SER	0	-0.005	-0.009	33.699	-0.218	-0.218	0.000	0.000	0.000	0.000
85	A	86	SER	0	-0.035	-0.014	34.842	-0.069	-0.069	0.000	0.000	0.000	0.000
86	A	87	GLY	0	0.057	0.032	35.412	0.036	0.036	0.000	0.000	0.000	0.000
87	A	88	TYR	0	-0.024	0.002	30.549	-0.235	-0.235	0.000	0.000	0.000	0.000
88	A	89	PRO	0	0.009	0.014	28.910	0.216	0.216	0.000	0.000	0.000	0.000
89	A	90	ARG	1	0.789	0.879	29.311	10.039	10.039	0.000	0.000	0.000	0.000
90	A	91	ILE	0	-0.003	-0.009	26.811	-0.491	-0.491	0.000	0.000	0.000	0.000
91	A	92	HIS	0	0.027	0.016	28.366	0.398	0.398	0.000	0.000	0.000	0.000
92	A	93	ALA	0	0.057	0.022	28.209	-0.381	-0.381	0.000	0.000	0.000	0.000
93	A	94	PRO	0	-0.038	-0.023	26.329	-0.068	-0.068	0.000	0.000	0.000	0.000
94	A	95	GLU	-1	-0.852	-0.906	27.508	-10.238	-10.238	0.000	0.000	0.000	0.000
95	A	96	LEU	0	-0.018	-0.013	27.383	-0.362	-0.362	0.000	0.000	0.000	0.000
96	A	97	GLN	0	-0.016	-0.022	25.454	0.385	0.385	0.000	0.000	0.000	0.000
97	A	98	GLY	0	-0.009	-0.004	27.670	0.126	0.126	0.000	0.000	0.000	0.000
98	A	99	TRP	0	-0.065	-0.056	22.078	-0.162	-0.162	0.000	0.000	0.000	0.000
99	A	100	GLY	0	-0.034	0.005	24.962	-0.270	-0.270	0.000	0.000	0.000	0.000
100	A	101	GLY	0	0.094	0.050	22.929	0.108	0.108	0.000	0.000	0.000	0.000
101	A	102	THR	0	-0.048	-0.031	23.211	0.530	0.530	0.000	0.000	0.000	0.000
102	A	103	MET	0	-0.049	-0.018	22.143	-0.889	-0.889	0.000	0.000	0.000	0.000
103	A	104	ALA	0	0.047	0.041	23.399	0.515	0.515	0.000	0.000	0.000	0.000
104	A	105	ALA	0	-0.032	-0.012	23.755	-0.493	-0.493	0.000	0.000	0.000	0.000
105	A	106	LEU	0	0.026	0.015	22.155	0.376	0.376	0.000	0.000	0.000	0.000
106	A	107	VAL	0	-0.044	-0.009	24.730	-0.247	-0.247	0.000	0.000	0.000	0.000
107	A	108	ASP	-1	-0.717	-0.834	23.594	-12.469	-12.469	0.000	0.000	0.000	0.000
108	A	109	PRO	0	0.008	-0.023	26.274	0.387	0.387	0.000	0.000	0.000	0.000
109	A	110	ASP	-1	-0.768	-0.854	26.261	-10.971	-10.971	0.000	0.000	0.000	0.000
110	A	111	GLY	0	0.009	0.007	28.167	0.136	0.136	0.000	0.000	0.000	0.000
111	A	112	THR	0	-0.030	-0.004	21.419	0.004	0.004	0.000	0.000	0.000	0.000
112	A	113	LEU	0	-0.032	-0.021	23.871	0.100	0.100	0.000	0.000	0.000	0.000
113	A	114	LEU	0	0.008	-0.011	18.806	-0.593	-0.593	0.000	0.000	0.000	0.000
114	A	115	ARG	1	0.912	0.937	19.912	13.508	13.508	0.000	0.000	0.000	0.000
115	A	116	LEU	0	0.006	0.008	19.090	-0.868	-0.868	0.000	0.000	0.000	0.000
116	A	117	ILE	0	-0.025	-0.027	17.769	0.676	0.676	0.000	0.000	0.000	0.000
117	A	118	GLN	0	-0.023	-0.018	17.909	-0.417	-0.417	0.000	0.000	0.000	0.000
118	A	119	ASN	0	-0.071	-0.055	13.028	0.280	0.280	0.000	0.000	0.000	0.000
119	A	120	GLU	-1	-0.954	-0.979	16.949	-12.426	-12.426	0.000	0.000	0.000	0.000
120	A	121	LEU	-1	-0.972	-0.971	16.460	-15.111	-15.111	0.000	0.000	0.000	0.000

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