FMO DATABASE

FMODB ID: ML9MZ

Calculation Name: 2A11-A-Xray547

Preferred Name:

Target Type:

Ligand Name: calcium ion

Ligand 3-letter code: CA

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2A11

Chain ID: A

ChEMBL ID:

UniProt ID: P9WH03

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	154
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1366879.028934
FMO2-HF: Nuclear repulsion	1309527.096873
FMO2-HF: Total energy	-57351.932061
FMO2-MP2: Total energy	-57520.954697

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:ILE)

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

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.
-120.324	-115.356	12.107	-7.043	-10.03	-0.069

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.878 / q_NPA : 0.932

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	SER	0	0.051	0.037	3.204	8.864	9.876	0.139	-0.011	-1.139	-0.001
4	A	5	ARG	1	0.949	0.945	4.503	22.003	22.038	-0.001	-0.025	-0.009	0.000
93	A	94	GLU	-1	-0.865	-0.946	2.791	-68.007	-66.081	0.200	-1.058	-1.068	-0.010
97	A	98	VAL	0	-0.065	-0.021	1.999	-6.750	-8.853	10.281	-3.335	-4.843	-0.022
98	A	99	HIS	1	0.786	0.878	2.450	42.697	46.756	1.489	-2.607	-2.940	-0.036
99	A	100	VAL	0	0.008	0.023	4.956	3.392	3.431	-0.001	-0.007	-0.031	0.000
5	A	6	GLN	0	0.005	0.021	7.217	1.437	1.437	0.000	0.000	0.000	0.000
6	A	7	PRO	0	0.033	0.013	5.128	1.817	1.817	0.000	0.000	0.000	0.000
7	A	8	LEU	0	-0.032	-0.015	7.300	0.877	0.877	0.000	0.000	0.000	0.000
8	A	9	LEU	0	0.017	0.012	8.847	2.460	2.460	0.000	0.000	0.000	0.000
9	A	10	ASP	-1	-0.841	-0.922	11.112	-23.427	-23.427	0.000	0.000	0.000	0.000
10	A	11	ALA	0	-0.032	-0.005	11.112	1.735	1.735	0.000	0.000	0.000	0.000
11	A	12	LEU	0	-0.003	-0.007	12.531	1.837	1.837	0.000	0.000	0.000	0.000
12	A	13	GLY	0	-0.041	0.001	14.903	1.503	1.503	0.000	0.000	0.000	0.000
13	A	14	VAL	0	-0.068	-0.042	16.141	1.321	1.321	0.000	0.000	0.000	0.000
14	A	15	ASP	-1	-0.865	-0.929	15.677	-19.745	-19.745	0.000	0.000	0.000	0.000
15	A	16	LEU	0	-0.036	-0.031	14.350	0.823	0.823	0.000	0.000	0.000	0.000
16	A	17	PRO	0	0.058	0.045	15.155	-1.172	-1.172	0.000	0.000	0.000	0.000
17	A	18	ASP	-1	-0.847	-0.914	13.677	-21.851	-21.851	0.000	0.000	0.000	0.000
18	A	19	GLU	-1	-0.909	-0.950	13.771	-17.935	-17.935	0.000	0.000	0.000	0.000
19	A	20	LEU	0	-0.004	0.005	16.054	-0.117	-0.117	0.000	0.000	0.000	0.000
20	A	21	LEU	0	0.000	-0.005	10.551	-0.757	-0.757	0.000	0.000	0.000	0.000
21	A	22	SER	0	-0.025	-0.042	11.378	-2.252	-2.252	0.000	0.000	0.000	0.000
22	A	23	LEU	0	-0.033	0.015	12.447	-0.378	-0.378	0.000	0.000	0.000	0.000
23	A	24	ALA	0	-0.001	-0.009	13.700	0.105	0.105	0.000	0.000	0.000	0.000
24	A	25	LEU	0	-0.031	-0.015	7.883	-0.727	-0.727	0.000	0.000	0.000	0.000
25	A	26	THR	0	-0.044	-0.032	10.579	-1.458	-1.458	0.000	0.000	0.000	0.000
26	A	27	HIS	0	0.092	0.070	12.037	0.963	0.963	0.000	0.000	0.000	0.000
27	A	28	ARG	0	0.057	0.042	13.761	0.144	0.144	0.000	0.000	0.000	0.000
28	A	29	SER	0	-0.016	-0.021	13.400	0.019	0.019	0.000	0.000	0.000	0.000
29	A	30	TYR	0	0.005	0.003	10.188	0.296	0.296	0.000	0.000	0.000	0.000
30	A	31	ALA	0	0.017	0.017	13.696	0.407	0.407	0.000	0.000	0.000	0.000
31	A	32	TYR	0	-0.037	-0.048	16.526	0.656	0.656	0.000	0.000	0.000	0.000
32	A	33	GLU	-1	-0.857	-0.912	13.321	-18.540	-18.540	0.000	0.000	0.000	0.000
33	A	34	ASN	0	-0.101	-0.068	13.050	0.309	0.309	0.000	0.000	0.000	0.000
34	A	35	GLY	0	0.000	0.006	16.930	0.234	0.234	0.000	0.000	0.000	0.000
35	A	36	GLY	0	-0.042	-0.011	19.737	0.580	0.580	0.000	0.000	0.000	0.000
36	A	37	LEU	0	-0.036	-0.016	15.013	0.213	0.213	0.000	0.000	0.000	0.000
37	A	38	PRO	0	-0.023	-0.021	18.902	0.198	0.198	0.000	0.000	0.000	0.000
38	A	39	THR	0	-0.025	-0.049	17.236	-0.853	-0.853	0.000	0.000	0.000	0.000
39	A	40	ASN	0	-0.003	-0.003	14.812	0.977	0.977	0.000	0.000	0.000	0.000
40	A	41	GLU	-1	-0.742	-0.830	17.231	-13.661	-13.661	0.000	0.000	0.000	0.000
41	A	42	ARG	1	0.918	0.949	20.157	12.623	12.623	0.000	0.000	0.000	0.000
42	A	43	LEU	0	-0.043	-0.019	17.458	0.489	0.489	0.000	0.000	0.000	0.000
43	A	44	GLU	-1	-0.885	-0.941	18.716	-14.492	-14.492	0.000	0.000	0.000	0.000
44	A	45	PHE	0	0.006	0.004	20.225	0.444	0.444	0.000	0.000	0.000	0.000
45	A	46	LEU	0	-0.042	-0.011	23.132	0.419	0.419	0.000	0.000	0.000	0.000
46	A	47	GLY	0	0.031	-0.004	21.357	0.328	0.328	0.000	0.000	0.000	0.000
47	A	48	ASP	-1	-0.898	-0.900	22.428	-12.140	-12.140	0.000	0.000	0.000	0.000
48	A	49	ALA	0	0.023	0.017	24.323	0.363	0.363	0.000	0.000	0.000	0.000
49	A	50	VAL	0	-0.022	-0.009	24.489	0.366	0.366	0.000	0.000	0.000	0.000
50	A	51	LEU	0	0.014	0.019	21.847	0.255	0.255	0.000	0.000	0.000	0.000
51	A	52	GLY	0	0.047	0.021	25.282	0.307	0.307	0.000	0.000	0.000	0.000
52	A	53	LEU	0	-0.018	0.010	28.494	0.403	0.403	0.000	0.000	0.000	0.000
53	A	54	THR	0	-0.019	-0.024	26.651	0.338	0.338	0.000	0.000	0.000	0.000
54	A	55	ILE	0	0.000	-0.003	25.432	0.230	0.230	0.000	0.000	0.000	0.000
55	A	56	THR	0	-0.015	-0.020	29.200	0.368	0.368	0.000	0.000	0.000	0.000
56	A	57	ASP	-1	-0.862	-0.914	32.105	-9.173	-9.173	0.000	0.000	0.000	0.000
57	A	58	ALA	0	0.015	0.005	30.129	0.269	0.269	0.000	0.000	0.000	0.000
58	A	59	LEU	0	-0.016	-0.009	31.324	0.230	0.230	0.000	0.000	0.000	0.000
59	A	60	PHE	0	-0.004	-0.008	34.035	0.267	0.267	0.000	0.000	0.000	0.000
60	A	61	HIS	1	0.816	0.898	35.338	9.061	9.061	0.000	0.000	0.000	0.000
61	A	62	ARG	1	0.836	0.907	29.584	10.562	10.562	0.000	0.000	0.000	0.000
62	A	63	HIS	0	-0.035	-0.003	34.313	0.283	0.283	0.000	0.000	0.000	0.000
63	A	64	PRO	0	0.038	0.011	38.938	0.063	0.063	0.000	0.000	0.000	0.000
64	A	65	ASP	-1	-0.921	-0.950	42.174	-7.081	-7.081	0.000	0.000	0.000	0.000
65	A	66	ARG	1	0.880	0.949	38.526	8.384	8.384	0.000	0.000	0.000	0.000
66	A	67	SER	0	0.019	0.009	42.541	-0.024	-0.024	0.000	0.000	0.000	0.000
67	A	68	GLU	-1	-0.874	-0.941	40.012	-7.924	-7.924	0.000	0.000	0.000	0.000
68	A	69	GLY	0	0.018	0.001	38.982	-0.232	-0.232	0.000	0.000	0.000	0.000
69	A	70	ASP	-1	-0.885	-0.937	38.415	-8.111	-8.111	0.000	0.000	0.000	0.000
70	A	71	LEU	0	0.015	0.011	36.462	-0.302	-0.302	0.000	0.000	0.000	0.000
71	A	72	ALA	0	-0.021	-0.012	34.657	-0.353	-0.353	0.000	0.000	0.000	0.000
72	A	73	LYS	1	0.866	0.923	33.431	7.867	7.867	0.000	0.000	0.000	0.000
73	A	74	LEU	0	0.033	0.018	32.596	-0.266	-0.266	0.000	0.000	0.000	0.000
74	A	75	ARG	1	0.956	0.968	29.959	9.321	9.321	0.000	0.000	0.000	0.000
75	A	76	ALA	0	-0.015	0.005	28.838	-0.471	-0.471	0.000	0.000	0.000	0.000
76	A	77	SER	0	0.006	-0.005	27.865	-0.312	-0.312	0.000	0.000	0.000	0.000
77	A	78	VAL	0	-0.042	-0.026	25.330	-0.444	-0.444	0.000	0.000	0.000	0.000
78	A	79	VAL	0	0.006	-0.012	24.221	-0.584	-0.584	0.000	0.000	0.000	0.000
79	A	80	ASN	0	-0.019	0.004	23.928	-0.515	-0.515	0.000	0.000	0.000	0.000
80	A	81	THR	0	0.059	0.011	19.319	-0.275	-0.275	0.000	0.000	0.000	0.000
81	A	82	GLN	0	0.007	0.000	19.134	-1.039	-1.039	0.000	0.000	0.000	0.000
82	A	83	ALA	0	0.031	0.025	19.384	-0.793	-0.793	0.000	0.000	0.000	0.000
83	A	84	LEU	0	0.000	0.011	18.378	-0.821	-0.821	0.000	0.000	0.000	0.000
84	A	85	ALA	0	0.001	-0.001	15.289	-1.177	-1.177	0.000	0.000	0.000	0.000
85	A	86	ASP	-1	-0.852	-0.929	14.734	-18.531	-18.531	0.000	0.000	0.000	0.000
86	A	87	VAL	0	-0.027	-0.008	16.081	-0.866	-0.866	0.000	0.000	0.000	0.000
87	A	88	ALA	0	0.009	0.000	12.448	-1.385	-1.385	0.000	0.000	0.000	0.000
88	A	89	ARG	1	0.778	0.863	11.476	17.444	17.444	0.000	0.000	0.000	0.000
89	A	90	ARG	1	0.844	0.922	11.342	16.541	16.541	0.000	0.000	0.000	0.000
90	A	91	LEU	0	-0.005	0.031	10.964	0.351	0.351	0.000	0.000	0.000	0.000
91	A	92	CYS	0	-0.027	-0.030	6.093	0.258	0.258	0.000	0.000	0.000	0.000
92	A	93	ALA	0	0.001	0.007	7.312	0.100	0.100	0.000	0.000	0.000	0.000
94	A	95	GLY	0	0.046	0.042	5.621	-0.331	-0.331	0.000	0.000	0.000	0.000
95	A	96	LEU	0	-0.012	-0.022	6.680	-6.387	-6.387	0.000	0.000	0.000	0.000
96	A	97	GLY	0	0.064	0.028	7.028	-2.286	-2.286	0.000	0.000	0.000	0.000
100	A	101	LEU	0	-0.054	-0.010	6.189	-2.741	-2.741	0.000	0.000	0.000	0.000
101	A	102	LEU	0	-0.002	-0.013	8.145	2.285	2.285	0.000	0.000	0.000	0.000
102	A	103	GLY	0	0.062	0.032	10.047	-0.510	-0.510	0.000	0.000	0.000	0.000
103	A	104	ARG	1	0.851	0.901	10.754	20.041	20.041	0.000	0.000	0.000	0.000
104	A	105	GLY	0	0.011	0.016	12.649	-0.351	-0.351	0.000	0.000	0.000	0.000
105	A	106	GLU	-1	-0.850	-0.911	12.618	-17.523	-17.523	0.000	0.000	0.000	0.000
106	A	107	ALA	0	-0.026	-0.010	8.421	-0.828	-0.828	0.000	0.000	0.000	0.000
107	A	108	ASN	0	-0.051	-0.037	9.856	-0.499	-0.499	0.000	0.000	0.000	0.000
108	A	109	THR	0	-0.035	-0.040	11.921	0.542	0.542	0.000	0.000	0.000	0.000
109	A	110	GLY	0	0.024	0.021	10.507	0.637	0.637	0.000	0.000	0.000	0.000
110	A	111	GLY	0	0.022	0.003	11.304	-0.256	-0.256	0.000	0.000	0.000	0.000
111	A	112	ALA	0	-0.046	-0.036	6.260	-0.040	-0.040	0.000	0.000	0.000	0.000
112	A	113	ASP	-1	-0.838	-0.917	8.376	-23.995	-23.995	0.000	0.000	0.000	0.000
113	A	114	LYS	1	0.931	0.985	10.734	17.369	17.369	0.000	0.000	0.000	0.000
114	A	115	SER	0	0.020	-0.003	13.970	-0.351	-0.351	0.000	0.000	0.000	0.000
115	A	116	SER	0	0.020	-0.002	15.978	-0.135	-0.135	0.000	0.000	0.000	0.000
116	A	117	ILE	0	0.024	0.038	11.360	0.056	0.056	0.000	0.000	0.000	0.000
117	A	118	LEU	0	-0.031	-0.001	9.735	-0.847	-0.847	0.000	0.000	0.000	0.000
118	A	119	ALA	0	-0.007	-0.008	13.024	-0.265	-0.265	0.000	0.000	0.000	0.000
119	A	120	ASP	-1	-0.833	-0.917	16.023	-15.813	-15.813	0.000	0.000	0.000	0.000
120	A	121	GLY	0	-0.005	0.012	12.905	0.154	0.154	0.000	0.000	0.000	0.000
121	A	122	MET	0	-0.028	-0.014	13.938	-0.781	-0.781	0.000	0.000	0.000	0.000
122	A	123	GLU	0	-0.044	-0.067	15.528	0.321	0.321	0.000	0.000	0.000	0.000
123	A	124	SER	0	0.001	-0.023	15.256	0.570	0.570	0.000	0.000	0.000	0.000
124	A	125	LEU	0	-0.013	-0.009	11.247	0.205	0.205	0.000	0.000	0.000	0.000
125	A	126	LEU	0	-0.007	0.005	15.752	0.620	0.620	0.000	0.000	0.000	0.000
126	A	127	GLY	0	0.040	0.024	19.220	0.732	0.732	0.000	0.000	0.000	0.000
127	A	128	ALA	0	-0.026	-0.014	16.981	0.597	0.597	0.000	0.000	0.000	0.000
128	A	129	ILE	0	0.010	0.000	16.614	0.439	0.439	0.000	0.000	0.000	0.000
129	A	130	TYR	0	-0.002	-0.005	20.053	0.715	0.715	0.000	0.000	0.000	0.000
130	A	131	LEU	0	-0.058	-0.031	22.015	0.566	0.566	0.000	0.000	0.000	0.000
131	A	132	GLN	0	-0.034	-0.004	20.077	0.101	0.101	0.000	0.000	0.000	0.000
132	A	133	HIS	0	-0.038	-0.034	19.567	0.884	0.884	0.000	0.000	0.000	0.000
133	A	134	GLY	0	0.010	0.020	24.557	0.506	0.506	0.000	0.000	0.000	0.000
134	A	135	MET	0	-0.014	-0.017	25.997	-0.449	-0.449	0.000	0.000	0.000	0.000
135	A	136	GLU	-1	-0.787	-0.868	27.077	-10.581	-10.581	0.000	0.000	0.000	0.000
136	A	137	LYS	1	0.886	0.934	22.171	12.900	12.900	0.000	0.000	0.000	0.000
137	A	138	ALA	0	0.046	0.014	22.507	-0.575	-0.575	0.000	0.000	0.000	0.000
138	A	139	ARG	1	0.776	0.844	23.300	9.910	9.910	0.000	0.000	0.000	0.000
139	A	140	GLU	-1	-0.847	-0.908	23.973	-12.674	-12.674	0.000	0.000	0.000	0.000
140	A	141	VAL	0	-0.028	-0.003	18.378	-0.270	-0.270	0.000	0.000	0.000	0.000
141	A	142	ILE	0	0.008	0.007	20.789	-0.380	-0.380	0.000	0.000	0.000	0.000
142	A	143	LEU	0	-0.015	-0.022	22.654	0.004	0.004	0.000	0.000	0.000	0.000
143	A	144	ARG	1	0.835	0.916	16.640	17.155	17.155	0.000	0.000	0.000	0.000
144	A	145	LEU	0	-0.033	-0.019	15.962	-0.274	-0.274	0.000	0.000	0.000	0.000
145	A	146	PHE	0	0.018	-0.008	19.703	-0.166	-0.166	0.000	0.000	0.000	0.000
146	A	147	GLY	0	0.014	0.031	22.813	0.546	0.546	0.000	0.000	0.000	0.000
147	A	148	PRO	0	0.033	0.003	21.981	0.466	0.466	0.000	0.000	0.000	0.000
148	A	149	LEU	0	-0.017	0.000	22.771	0.312	0.312	0.000	0.000	0.000	0.000
149	A	150	LEU	0	-0.018	-0.018	25.441	0.488	0.488	0.000	0.000	0.000	0.000
150	A	151	ASP	-1	-0.879	-0.932	28.030	-10.629	-10.629	0.000	0.000	0.000	0.000
151	A	152	ALA	0	-0.044	-0.014	27.613	0.319	0.319	0.000	0.000	0.000	0.000
152	A	153	ALA	0	0.010	0.002	29.529	0.248	0.248	0.000	0.000	0.000	0.000
153	A	154	PRO	0	-0.111	-0.051	31.020	0.301	0.301	0.000	0.000	0.000	0.000
154	A	155	THR	-1	-0.984	-0.967	33.066	-9.236	-9.236	0.000	0.000	0.000	0.000

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