FMO DATABASE

FMODB ID: 1956Z

Calculation Name: 2ESH-A-Xray547

Preferred Name:

Target Type:

Ligand Name: calcium ion

Ligand 3-letter code: CA

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2ESH

Chain ID: A

ChEMBL ID:

UniProt ID: Q9X035

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	114
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-884243.252707
FMO2-HF: Nuclear repulsion	838597.644983
FMO2-HF: Total energy	-45645.607724
FMO2-MP2: Total energy	-45780.980975

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:ARG)

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

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.
50.199	52.88	9.17	-5.148	-6.702	-0.055

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 2 / q_Mulliken : 1.831 / q_NPA : 1.904

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	6	GLY	0	0.037	0.030	1.847	-34.199	-33.883	8.629	-4.540	-4.404	-0.056
4	A	7	ARG	1	0.935	0.943	2.861	88.925	91.237	0.542	-0.604	-2.250	0.001
5	A	8	GLY	0	0.056	0.037	4.789	3.894	3.947	-0.001	-0.004	-0.048	0.000
6	A	9	PHE	0	0.065	0.033	7.574	-0.554	-0.554	0.000	0.000	0.000	0.000
7	A	10	ARG	1	0.884	0.949	8.061	54.190	54.190	0.000	0.000	0.000	0.000
8	A	11	GLY	0	-0.038	-0.014	7.811	0.609	0.609	0.000	0.000	0.000	0.000
9	A	12	TRP	0	0.041	0.026	8.719	1.365	1.365	0.000	0.000	0.000	0.000
10	A	13	TRP	0	0.094	0.046	11.819	1.770	1.770	0.000	0.000	0.000	0.000
11	A	14	LEU	0	-0.014	0.009	9.712	1.305	1.305	0.000	0.000	0.000	0.000
12	A	15	ALA	0	-0.005	-0.009	11.446	1.817	1.817	0.000	0.000	0.000	0.000
13	A	16	SER	0	0.007	-0.017	13.297	2.554	2.554	0.000	0.000	0.000	0.000
14	A	17	THR	0	-0.022	-0.014	16.198	2.224	2.224	0.000	0.000	0.000	0.000
15	A	18	ILE	0	-0.008	-0.003	13.893	1.296	1.296	0.000	0.000	0.000	0.000
16	A	19	LEU	0	-0.031	-0.010	17.367	1.492	1.492	0.000	0.000	0.000	0.000
17	A	20	LEU	0	0.002	0.007	19.011	1.385	1.385	0.000	0.000	0.000	0.000
18	A	21	LEU	0	0.026	0.018	19.831	1.024	1.024	0.000	0.000	0.000	0.000
19	A	22	VAL	0	-0.031	-0.010	19.656	1.143	1.143	0.000	0.000	0.000	0.000
20	A	23	ALA	0	-0.075	-0.042	22.730	1.015	1.015	0.000	0.000	0.000	0.000
21	A	24	GLU	-1	-0.941	-0.968	25.035	-22.518	-22.518	0.000	0.000	0.000	0.000
22	A	25	LYS	1	0.854	0.905	26.085	23.003	23.003	0.000	0.000	0.000	0.000
23	A	26	PRO	0	-0.011	-0.003	24.539	-0.854	-0.854	0.000	0.000	0.000	0.000
24	A	27	SER	0	-0.021	-0.033	22.973	0.852	0.852	0.000	0.000	0.000	0.000
25	A	28	HIS	0	0.083	0.038	20.549	-1.864	-1.864	0.000	0.000	0.000	0.000
26	A	29	GLY	0	0.013	-0.014	17.120	0.051	0.051	0.000	0.000	0.000	0.000
27	A	30	TYR	0	-0.109	-0.049	18.025	-1.378	-1.378	0.000	0.000	0.000	0.000
28	A	31	GLU	-1	-0.713	-0.810	20.246	-24.259	-24.259	0.000	0.000	0.000	0.000
29	A	32	LEU	0	0.018	0.000	18.932	-0.001	-0.001	0.000	0.000	0.000	0.000
30	A	33	ALA	0	-0.040	-0.030	17.948	-0.873	-0.873	0.000	0.000	0.000	0.000
31	A	34	GLU	-1	-0.880	-0.936	19.443	-24.084	-24.084	0.000	0.000	0.000	0.000
32	A	35	ARG	1	0.865	0.917	23.061	24.977	24.977	0.000	0.000	0.000	0.000
33	A	36	LEU	0	-0.035	-0.023	15.865	-0.618	-0.618	0.000	0.000	0.000	0.000
34	A	37	ALA	0	-0.085	-0.033	19.950	-0.454	-0.454	0.000	0.000	0.000	0.000
35	A	38	GLU	-1	-0.933	-0.971	21.519	-22.912	-22.912	0.000	0.000	0.000	0.000
36	A	39	PHE	0	-0.021	-0.004	20.096	0.277	0.277	0.000	0.000	0.000	0.000
37	A	40	GLY	0	0.001	0.015	20.631	0.325	0.325	0.000	0.000	0.000	0.000
38	A	41	ILE	0	-0.080	-0.064	17.436	-1.714	-1.714	0.000	0.000	0.000	0.000
39	A	42	GLU	-1	-0.823	-0.899	20.652	-22.826	-22.826	0.000	0.000	0.000	0.000
40	A	43	ILE	0	-0.082	-0.030	17.098	0.065	0.065	0.000	0.000	0.000	0.000
41	A	44	PRO	0	0.033	0.002	18.365	-1.219	-1.219	0.000	0.000	0.000	0.000
42	A	45	GLY	0	0.004	0.003	15.680	-1.311	-1.311	0.000	0.000	0.000	0.000
43	A	46	ILE	0	-0.059	-0.022	12.884	-2.941	-2.941	0.000	0.000	0.000	0.000
44	A	47	GLY	0	0.038	0.018	13.017	-3.032	-3.032	0.000	0.000	0.000	0.000
45	A	48	HIS	0	-0.015	-0.010	11.129	1.738	1.738	0.000	0.000	0.000	0.000
46	A	49	MET	0	0.065	0.059	13.942	-0.202	-0.202	0.000	0.000	0.000	0.000
47	A	50	GLY	0	0.059	-0.002	11.484	-4.170	-4.170	0.000	0.000	0.000	0.000
48	A	51	ASN	0	-0.058	-0.051	8.071	3.205	3.205	0.000	0.000	0.000	0.000
49	A	52	ILE	0	0.134	0.086	10.358	-3.330	-3.330	0.000	0.000	0.000	0.000
50	A	53	TYR	0	0.052	0.021	12.123	0.095	0.095	0.000	0.000	0.000	0.000
51	A	54	ARG	1	0.902	0.958	4.884	65.245	65.245	0.000	0.000	0.000	0.000
52	A	55	VAL	0	0.038	0.021	8.783	-0.957	-0.957	0.000	0.000	0.000	0.000
53	A	56	LEU	0	-0.008	0.011	10.773	1.857	1.857	0.000	0.000	0.000	0.000
54	A	57	ALA	0	0.000	0.003	10.385	1.822	1.822	0.000	0.000	0.000	0.000
55	A	58	ASP	-1	-0.900	-0.953	7.624	-65.102	-65.102	0.000	0.000	0.000	0.000
56	A	59	LEU	0	-0.028	-0.011	10.835	2.165	2.165	0.000	0.000	0.000	0.000
57	A	60	GLU	-1	-0.836	-0.911	14.429	-30.314	-30.314	0.000	0.000	0.000	0.000
58	A	61	GLU	-1	-0.965	-0.979	10.985	-43.466	-43.466	0.000	0.000	0.000	0.000
59	A	62	SER	0	-0.063	-0.041	12.991	0.796	0.796	0.000	0.000	0.000	0.000
60	A	63	GLY	0	0.011	0.021	15.452	1.546	1.546	0.000	0.000	0.000	0.000
61	A	64	PHE	0	-0.027	-0.007	15.348	1.947	1.947	0.000	0.000	0.000	0.000
62	A	65	LEU	0	-0.029	-0.018	16.901	1.434	1.434	0.000	0.000	0.000	0.000
63	A	66	SER	0	-0.010	-0.008	19.878	0.147	0.147	0.000	0.000	0.000	0.000
64	A	67	THR	0	-0.018	-0.022	19.810	-0.508	-0.508	0.000	0.000	0.000	0.000
65	A	68	GLU	-1	-0.930	-0.958	22.129	-20.068	-20.068	0.000	0.000	0.000	0.000
66	A	69	TRP	0	-0.030	-0.018	20.219	-0.959	-0.959	0.000	0.000	0.000	0.000
67	A	70	ASP	-1	-0.787	-0.865	25.506	-19.451	-19.451	0.000	0.000	0.000	0.000
68	A	71	THR	0	-0.034	-0.040	27.247	-0.533	-0.533	0.000	0.000	0.000	0.000
69	A	72	THR	0	-0.049	-0.034	29.622	0.577	0.577	0.000	0.000	0.000	0.000
70	A	73	VAL	0	-0.017	0.008	27.663	0.363	0.363	0.000	0.000	0.000	0.000
71	A	74	SER	0	-0.015	0.003	28.914	-0.515	-0.515	0.000	0.000	0.000	0.000
72	A	75	PRO	0	-0.018	-0.025	24.544	0.141	0.141	0.000	0.000	0.000	0.000
73	A	76	PRO	0	0.055	0.014	25.150	-0.248	-0.248	0.000	0.000	0.000	0.000
74	A	77	ARG	1	0.867	0.943	22.265	23.604	23.604	0.000	0.000	0.000	0.000
75	A	78	LYS	1	0.823	0.914	17.278	31.914	31.914	0.000	0.000	0.000	0.000
76	A	79	ILE	0	-0.020	-0.010	20.915	-1.030	-1.030	0.000	0.000	0.000	0.000
77	A	80	TYR	0	0.010	-0.004	15.758	-0.031	-0.031	0.000	0.000	0.000	0.000
78	A	81	ARG	1	1.003	0.986	21.369	22.473	22.473	0.000	0.000	0.000	0.000
79	A	82	ILE	0	-0.009	0.020	22.067	-0.332	-0.332	0.000	0.000	0.000	0.000
80	A	83	THR	0	0.005	-0.006	22.138	1.338	1.338	0.000	0.000	0.000	0.000
81	A	84	PRO	0	0.005	-0.018	24.566	-0.214	-0.214	0.000	0.000	0.000	0.000
82	A	85	GLN	0	0.055	0.024	21.881	0.814	0.814	0.000	0.000	0.000	0.000
83	A	86	GLY	0	0.066	0.036	20.589	-0.798	-0.798	0.000	0.000	0.000	0.000
84	A	87	LYS	1	0.939	0.959	21.596	21.074	21.074	0.000	0.000	0.000	0.000
85	A	88	LEU	0	-0.056	-0.016	23.866	0.555	0.555	0.000	0.000	0.000	0.000
86	A	89	TYR	0	0.061	0.037	14.273	-0.499	-0.499	0.000	0.000	0.000	0.000
87	A	90	LEU	0	0.017	-0.003	20.558	-0.397	-0.397	0.000	0.000	0.000	0.000
88	A	91	ARG	1	0.929	0.964	22.010	21.680	21.680	0.000	0.000	0.000	0.000
89	A	92	GLU	-1	-0.906	-0.947	20.413	-28.372	-28.372	0.000	0.000	0.000	0.000
90	A	93	ILE	0	-0.030	-0.004	17.144	-0.080	-0.080	0.000	0.000	0.000	0.000
91	A	94	LEU	0	0.014	0.008	20.328	0.139	0.139	0.000	0.000	0.000	0.000
92	A	95	ARG	1	0.996	0.996	23.874	22.334	22.334	0.000	0.000	0.000	0.000
93	A	96	SER	0	0.003	-0.004	19.326	0.119	0.119	0.000	0.000	0.000	0.000
94	A	97	LEU	0	-0.013	-0.012	19.734	-0.143	-0.143	0.000	0.000	0.000	0.000
95	A	98	GLU	-1	-0.957	-0.973	22.478	-20.556	-20.556	0.000	0.000	0.000	0.000
96	A	99	ASP	-1	-0.852	-0.912	22.836	-22.906	-22.906	0.000	0.000	0.000	0.000
97	A	100	MET	0	-0.067	-0.032	18.325	-0.220	-0.220	0.000	0.000	0.000	0.000
98	A	101	LYS	1	0.967	0.995	22.559	20.295	20.295	0.000	0.000	0.000	0.000
99	A	102	ARG	1	0.898	0.937	25.824	21.720	21.720	0.000	0.000	0.000	0.000
100	A	103	ARG	1	0.895	0.954	22.880	23.487	23.487	0.000	0.000	0.000	0.000
101	A	104	ILE	0	0.038	0.017	22.460	0.324	0.324	0.000	0.000	0.000	0.000
102	A	105	GLU	-1	-0.839	-0.920	26.144	-18.843	-18.843	0.000	0.000	0.000	0.000
103	A	106	THR	0	-0.096	-0.067	28.011	0.464	0.464	0.000	0.000	0.000	0.000
104	A	107	LEU	0	-0.079	-0.043	24.179	0.296	0.296	0.000	0.000	0.000	0.000
105	A	108	GLU	-1	-0.892	-0.946	28.795	-18.773	-18.773	0.000	0.000	0.000	0.000
106	A	109	GLU	-1	-0.852	-0.931	30.999	-16.236	-16.236	0.000	0.000	0.000	0.000
107	A	110	ARG	1	0.843	0.927	27.837	19.966	19.966	0.000	0.000	0.000	0.000
108	A	111	ILE	0	0.006	0.003	28.224	0.257	0.257	0.000	0.000	0.000	0.000
109	A	112	LYS	1	0.902	0.936	32.842	17.660	17.660	0.000	0.000	0.000	0.000
110	A	113	ARG	1	0.931	0.976	35.128	16.673	16.673	0.000	0.000	0.000	0.000
111	A	114	VAL	0	0.028	0.010	33.677	0.206	0.206	0.000	0.000	0.000	0.000
112	A	115	LEU	0	-0.060	-0.023	33.983	-0.023	-0.023	0.000	0.000	0.000	0.000
113	A	116	GLN	0	-0.102	-0.040	37.904	0.291	0.291	0.000	0.000	0.000	0.000
114	A	117	GLU	-2	-1.913	-1.941	39.177	-29.233	-29.233	0.000	0.000	0.000	0.000

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