FMO DATABASE

FMODB ID: 67JQZ

Calculation Name: 1EXR-A-Xray547

Preferred Name:

Target Type:

Ligand Name: calcium ion

Ligand 3-letter code: CA

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1EXR

Chain ID: A

ChEMBL ID:

UniProt ID: P07463

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	146
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1166491.174389
FMO2-HF: Nuclear repulsion	1107098.885578
FMO2-HF: Total energy	-59392.288811
FMO2-MP2: Total energy	-59560.587415

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:GLU)

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

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.
9.345	13.928	-0.018	-2.018	-2.547	-0.008

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.146 / q_NPA : -0.081

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	LEU	0	0.048	0.047	3.654	1.472	5.963	-0.017	-2.008	-2.466	-0.008
4	A	5	THR	0	-0.032	-0.033	4.818	-3.350	-3.258	-0.001	-0.010	-0.081	0.000
5	A	6	GLU	-1	-0.934	-0.982	6.512	-1.232	-1.232	0.000	0.000	0.000	0.000
6	A	7	GLU	-1	-0.894	-0.942	9.893	1.314	1.314	0.000	0.000	0.000	0.000
7	A	8	GLN	0	0.076	0.050	6.766	0.181	0.181	0.000	0.000	0.000	0.000
8	A	9	ILE	0	-0.008	-0.003	8.097	-0.361	-0.361	0.000	0.000	0.000	0.000
9	A	10	ALA	0	-0.018	-0.001	11.514	-0.220	-0.220	0.000	0.000	0.000	0.000
10	A	11	GLU	0	0.043	0.020	14.179	-0.040	-0.040	0.000	0.000	0.000	0.000
11	A	12	PHE	0	0.001	-0.013	10.168	-0.054	-0.054	0.000	0.000	0.000	0.000
12	A	13	LYS	1	0.916	0.964	14.713	0.473	0.473	0.000	0.000	0.000	0.000
13	A	14	GLU	-1	-0.935	-0.963	17.561	0.698	0.698	0.000	0.000	0.000	0.000
14	A	15	ALA	0	-0.025	-0.015	18.027	-0.040	-0.040	0.000	0.000	0.000	0.000
15	A	16	PHE	0	-0.025	-0.010	18.770	-0.023	-0.023	0.000	0.000	0.000	0.000
16	A	17	ALA	0	0.036	0.015	20.622	-0.051	-0.051	0.000	0.000	0.000	0.000
17	A	18	LEU	0	-0.050	-0.002	23.124	-0.021	-0.021	0.000	0.000	0.000	0.000
18	A	19	PHE	0	-0.052	-0.046	22.717	-0.002	-0.002	0.000	0.000	0.000	0.000
19	A	20	ASP	-1	-0.770	-0.881	24.515	-0.132	-0.132	0.000	0.000	0.000	0.000
20	A	21	LYS	1	0.764	0.864	26.307	-0.263	-0.263	0.000	0.000	0.000	0.000
21	A	22	ASP	-1	-0.982	-0.995	29.665	-0.095	-0.095	0.000	0.000	0.000	0.000
22	A	23	GLY	0	-0.041	-0.009	26.694	-0.023	-0.023	0.000	0.000	0.000	0.000
23	A	24	ASP	-1	-0.909	-0.929	26.818	-0.298	-0.298	0.000	0.000	0.000	0.000
24	A	25	GLY	0	-0.050	-0.023	23.114	-0.088	-0.088	0.000	0.000	0.000	0.000
25	A	26	THR	0	-0.104	-0.075	22.617	-0.041	-0.041	0.000	0.000	0.000	0.000
26	A	27	ILE	0	-0.010	0.003	22.510	0.081	0.081	0.000	0.000	0.000	0.000
27	A	28	THR	0	0.038	-0.021	26.383	0.004	0.004	0.000	0.000	0.000	0.000
28	A	29	THR	0	0.033	-0.011	29.855	0.048	0.048	0.000	0.000	0.000	0.000
29	A	30	LYS	1	0.934	0.970	31.863	-0.055	-0.055	0.000	0.000	0.000	0.000
30	A	31	GLU	-1	-0.762	-0.845	29.492	0.057	0.057	0.000	0.000	0.000	0.000
31	A	32	LEU	0	0.088	0.055	26.758	0.050	0.050	0.000	0.000	0.000	0.000
32	A	33	GLY	0	0.037	0.000	29.506	0.047	0.047	0.000	0.000	0.000	0.000
33	A	34	THR	0	-0.138	-0.097	32.461	0.000	0.000	0.000	0.000	0.000	0.000
34	A	35	VAL	0	0.004	0.023	27.162	0.010	0.010	0.000	0.000	0.000	0.000
35	A	36	MET	0	0.027	0.032	30.135	0.021	0.021	0.000	0.000	0.000	0.000
36	A	37	ARG	1	0.882	0.957	32.013	-0.208	-0.208	0.000	0.000	0.000	0.000
37	A	38	SER	0	-0.126	-0.072	31.819	0.005	0.005	0.000	0.000	0.000	0.000
38	A	39	LEU	0	-0.006	0.000	28.381	0.021	0.021	0.000	0.000	0.000	0.000
39	A	40	GLY	0	-0.017	0.000	33.039	0.018	0.018	0.000	0.000	0.000	0.000
40	A	41	GLN	0	-0.003	-0.003	32.683	0.006	0.006	0.000	0.000	0.000	0.000
41	A	42	ASN	0	-0.079	-0.064	35.878	-0.035	-0.035	0.000	0.000	0.000	0.000
42	A	43	PRO	0	0.022	0.030	33.741	-0.013	-0.013	0.000	0.000	0.000	0.000
43	A	44	THR	0	-0.071	-0.079	36.810	-0.034	-0.034	0.000	0.000	0.000	0.000
44	A	45	GLU	-1	-0.841	-0.915	36.048	0.095	0.095	0.000	0.000	0.000	0.000
45	A	46	ALA	0	-0.033	-0.006	35.891	-0.011	-0.011	0.000	0.000	0.000	0.000
46	A	47	GLU	-1	-0.779	-0.864	34.350	0.286	0.286	0.000	0.000	0.000	0.000
47	A	48	LEU	0	-0.055	-0.016	31.910	0.026	0.026	0.000	0.000	0.000	0.000
48	A	49	GLN	0	-0.019	-0.023	31.048	-0.005	-0.005	0.000	0.000	0.000	0.000
49	A	50	ASP	-1	-0.900	-0.944	30.830	0.169	0.169	0.000	0.000	0.000	0.000
50	A	51	MET	0	-0.062	-0.051	28.022	0.018	0.018	0.000	0.000	0.000	0.000
51	A	52	ILE	0	-0.042	-0.006	26.537	0.041	0.041	0.000	0.000	0.000	0.000
52	A	53	ASN	0	0.023	0.013	26.173	-0.060	-0.060	0.000	0.000	0.000	0.000
53	A	54	GLU	-1	-0.988	-0.980	24.751	0.278	0.278	0.000	0.000	0.000	0.000
54	A	55	VAL	0	-0.122	-0.077	20.473	0.104	0.104	0.000	0.000	0.000	0.000
55	A	56	ASP	-1	-0.818	-0.898	21.552	-0.289	-0.289	0.000	0.000	0.000	0.000
56	A	57	ALA	0	-0.059	-0.031	19.902	0.008	0.008	0.000	0.000	0.000	0.000
57	A	58	ASP	-1	-0.955	-0.972	21.839	-0.649	-0.649	0.000	0.000	0.000	0.000
58	A	59	GLY	0	-0.026	-0.001	23.313	-0.005	-0.005	0.000	0.000	0.000	0.000
59	A	60	ASN	0	-0.121	-0.061	24.464	0.088	0.088	0.000	0.000	0.000	0.000
60	A	61	GLY	0	-0.017	-0.014	27.879	0.013	0.013	0.000	0.000	0.000	0.000
61	A	62	THR	0	-0.116	-0.065	26.443	0.046	0.046	0.000	0.000	0.000	0.000
62	A	63	ILE	0	0.018	0.019	21.446	0.001	0.001	0.000	0.000	0.000	0.000
63	A	64	ASP	-1	-0.791	-0.904	18.962	-0.686	-0.686	0.000	0.000	0.000	0.000
64	A	65	PHE	0	-0.018	-0.025	13.792	0.054	0.054	0.000	0.000	0.000	0.000
65	A	66	PRO	0	-0.039	-0.040	14.419	0.118	0.118	0.000	0.000	0.000	0.000
66	A	67	GLU	-1	-0.742	-0.855	15.165	-0.202	-0.202	0.000	0.000	0.000	0.000
67	A	68	PHE	0	0.010	0.007	16.938	0.288	0.288	0.000	0.000	0.000	0.000
68	A	69	LEU	0	-0.062	-0.028	11.421	0.311	0.311	0.000	0.000	0.000	0.000
69	A	70	SER	0	-0.048	-0.019	13.170	0.632	0.632	0.000	0.000	0.000	0.000
70	A	71	LEU	0	0.017	0.004	14.214	0.397	0.397	0.000	0.000	0.000	0.000
71	A	72	MET	0	-0.015	0.001	15.189	0.247	0.247	0.000	0.000	0.000	0.000
72	A	73	ALA	0	0.015	-0.006	10.295	0.398	0.398	0.000	0.000	0.000	0.000
73	A	74	ARG	1	0.854	0.931	11.977	-0.445	-0.445	0.000	0.000	0.000	0.000
74	A	75	LYS	1	1.041	1.016	14.467	-0.885	-0.885	0.000	0.000	0.000	0.000
75	A	76	MET	0	-0.028	-0.009	11.040	-0.114	-0.114	0.000	0.000	0.000	0.000
76	A	77	LYS	1	0.943	0.985	9.389	-4.520	-4.520	0.000	0.000	0.000	0.000
77	A	78	GLU	-1	-0.934	-0.967	14.065	1.441	1.441	0.000	0.000	0.000	0.000
78	A	79	GLN	0	-0.037	-0.025	17.460	-0.013	-0.013	0.000	0.000	0.000	0.000
79	A	80	ASP	-1	-0.925	-0.959	13.074	4.079	4.079	0.000	0.000	0.000	0.000
80	A	81	SER	0	-0.068	-0.031	16.551	-0.126	-0.126	0.000	0.000	0.000	0.000
81	A	82	GLU	-1	-0.867	-0.913	18.494	1.131	1.131	0.000	0.000	0.000	0.000
82	A	83	GLU	-1	-0.874	-0.949	19.761	1.478	1.478	0.000	0.000	0.000	0.000
83	A	84	GLU	-1	-0.941	-0.962	19.198	2.202	2.202	0.000	0.000	0.000	0.000
84	A	85	LEU	0	0.012	0.006	21.463	-0.176	-0.176	0.000	0.000	0.000	0.000
85	A	86	ILE	0	0.005	-0.002	24.296	-0.161	-0.161	0.000	0.000	0.000	0.000
86	A	87	GLU	-1	-1.006	-1.014	22.353	1.771	1.771	0.000	0.000	0.000	0.000
87	A	88	ALA	0	-0.008	-0.007	25.368	-0.107	-0.107	0.000	0.000	0.000	0.000
88	A	89	PHE	0	-0.035	-0.007	27.142	-0.089	-0.089	0.000	0.000	0.000	0.000
89	A	90	LYS	1	0.866	0.932	26.070	-1.373	-1.373	0.000	0.000	0.000	0.000
90	A	91	VAL	0	-0.071	-0.013	28.695	-0.048	-0.048	0.000	0.000	0.000	0.000
91	A	92	PHE	0	-0.040	-0.035	29.817	-0.072	-0.072	0.000	0.000	0.000	0.000
92	A	93	ASP	-1	-0.816	-0.905	33.554	0.680	0.680	0.000	0.000	0.000	0.000
93	A	94	ARG	1	0.860	0.932	35.222	-0.664	-0.664	0.000	0.000	0.000	0.000
94	A	95	ASP	-1	-0.949	-0.973	37.300	0.581	0.581	0.000	0.000	0.000	0.000
95	A	96	GLY	0	-0.013	0.009	36.289	-0.008	-0.008	0.000	0.000	0.000	0.000
96	A	97	ASN	0	-0.130	-0.074	37.280	0.004	0.004	0.000	0.000	0.000	0.000
97	A	98	GLY	0	0.009	0.003	35.836	-0.022	-0.022	0.000	0.000	0.000	0.000
98	A	99	LEU	0	-0.057	-0.036	36.672	0.006	0.006	0.000	0.000	0.000	0.000
99	A	100	ILE	0	0.001	0.019	32.936	-0.018	-0.018	0.000	0.000	0.000	0.000
100	A	101	SER	0	-0.011	-0.052	37.608	-0.036	-0.036	0.000	0.000	0.000	0.000
101	A	102	ALA	0	0.093	0.036	40.127	0.025	0.025	0.000	0.000	0.000	0.000
102	A	103	ALA	0	-0.056	-0.034	41.742	0.010	0.010	0.000	0.000	0.000	0.000
103	A	104	GLU	-1	-0.805	-0.866	38.188	0.649	0.649	0.000	0.000	0.000	0.000
104	A	105	LEU	0	0.097	0.058	35.359	0.029	0.029	0.000	0.000	0.000	0.000
105	A	106	ARG	1	0.836	0.901	37.618	-0.470	-0.470	0.000	0.000	0.000	0.000
106	A	107	HIS	0	-0.085	-0.028	37.692	-0.021	-0.021	0.000	0.000	0.000	0.000
107	A	108	VAL	0	-0.014	-0.016	32.904	0.003	0.003	0.000	0.000	0.000	0.000
108	A	109	MET	0	0.050	0.032	34.106	0.048	0.048	0.000	0.000	0.000	0.000
109	A	110	THR	0	-0.053	-0.039	36.133	-0.011	-0.011	0.000	0.000	0.000	0.000
110	A	111	ASN	0	-0.077	-0.053	35.163	-0.031	-0.031	0.000	0.000	0.000	0.000
111	A	112	LEU	0	-0.028	0.004	30.090	0.039	0.039	0.000	0.000	0.000	0.000
112	A	113	GLY	0	-0.053	-0.019	33.449	0.016	0.016	0.000	0.000	0.000	0.000
113	A	114	GLU	-1	-0.909	-0.950	34.975	0.639	0.639	0.000	0.000	0.000	0.000
114	A	115	LYS	1	0.854	0.932	37.579	-0.508	-0.508	0.000	0.000	0.000	0.000
115	A	116	LEU	0	0.020	0.019	38.119	-0.031	-0.031	0.000	0.000	0.000	0.000
116	A	117	THR	0	-0.148	-0.117	42.198	-0.016	-0.016	0.000	0.000	0.000	0.000
117	A	118	ASP	-1	-0.819	-0.908	44.159	0.457	0.457	0.000	0.000	0.000	0.000
118	A	119	ASP	-1	-0.900	-0.946	45.143	0.395	0.395	0.000	0.000	0.000	0.000
119	A	120	GLU	-1	-0.798	-0.871	41.953	0.485	0.485	0.000	0.000	0.000	0.000
120	A	121	VAL	0	-0.026	-0.015	39.990	0.023	0.023	0.000	0.000	0.000	0.000
121	A	122	ASP	-1	-0.892	-0.957	41.133	0.459	0.459	0.000	0.000	0.000	0.000
122	A	123	GLU	-1	-1.029	-1.008	41.609	0.434	0.434	0.000	0.000	0.000	0.000
123	A	124	MET	0	-0.027	-0.031	35.284	0.008	0.008	0.000	0.000	0.000	0.000
124	A	125	ILE	0	-0.025	0.011	37.871	0.024	0.024	0.000	0.000	0.000	0.000
125	A	126	ARG	1	0.896	0.935	39.806	-0.415	-0.415	0.000	0.000	0.000	0.000
126	A	127	GLU	-1	-0.980	-0.979	37.702	0.468	0.468	0.000	0.000	0.000	0.000
127	A	128	ALA	0	-0.027	-0.021	35.206	0.012	0.012	0.000	0.000	0.000	0.000
128	A	129	ASP	-1	-0.867	-0.926	36.977	0.496	0.496	0.000	0.000	0.000	0.000
129	A	130	ILE	0	-0.109	-0.057	35.936	-0.025	-0.025	0.000	0.000	0.000	0.000
130	A	131	ASP	-1	-0.954	-0.981	40.224	0.478	0.478	0.000	0.000	0.000	0.000
131	A	132	GLY	0	-0.026	-0.008	42.317	-0.031	-0.031	0.000	0.000	0.000	0.000
132	A	133	ASP	-1	-0.891	-0.953	42.378	0.486	0.486	0.000	0.000	0.000	0.000
133	A	134	GLY	0	-0.058	-0.024	43.961	-0.007	-0.007	0.000	0.000	0.000	0.000
134	A	135	HIS	1	0.725	0.854	40.131	-0.505	-0.505	0.000	0.000	0.000	0.000
135	A	136	ILE	0	0.032	0.039	34.356	-0.001	-0.001	0.000	0.000	0.000	0.000
136	A	137	ASN	0	0.029	0.010	35.552	0.070	0.070	0.000	0.000	0.000	0.000
137	A	138	TYR	0	-0.052	-0.065	25.858	0.016	0.016	0.000	0.000	0.000	0.000
138	A	139	GLU	-1	-0.825	-0.896	30.905	0.677	0.677	0.000	0.000	0.000	0.000
139	A	140	GLU	-1	-0.755	-0.876	31.671	0.615	0.615	0.000	0.000	0.000	0.000
140	A	141	PHE	0	-0.001	-0.002	27.212	0.011	0.011	0.000	0.000	0.000	0.000
141	A	142	VAL	0	-0.015	-0.004	26.237	0.042	0.042	0.000	0.000	0.000	0.000
142	A	143	ARG	1	0.801	0.875	27.906	-0.588	-0.588	0.000	0.000	0.000	0.000
143	A	144	MET	0	0.032	0.035	29.727	0.006	0.006	0.000	0.000	0.000	0.000
144	A	145	MET	0	-0.071	-0.028	25.923	0.036	0.036	0.000	0.000	0.000	0.000
145	A	146	VAL	0	-0.098	-0.046	23.994	0.107	0.107	0.000	0.000	0.000	0.000
146	A	147	SER	-1	-1.023	-1.004	26.148	0.708	0.708	0.000	0.000	0.000	0.000

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