FMO DATABASE

FMODB ID: 8GR4Y

Calculation Name: 1OU9-A-Xray547

Preferred Name:

Target Type:

Ligand Name: calcium ion

Ligand 3-letter code: CA

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1OU9

Chain ID: A

ChEMBL ID:

UniProt ID: P45206

Base Structure: X-ray

Registration Date: 2025-10-03

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	121
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-995609.03641
FMO2-HF: Nuclear repulsion	947533.956274
FMO2-HF: Total energy	-48075.080136
FMO2-MP2: Total energy	-48216.057231

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:1:MET)

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

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.
-91.397	-85.799	4.613	-3.29	-6.921	-0.035

Interaction energy analysis for fragmet #1(A:1:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.810 / q_NPA : 0.895

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	3	TYR	0	-0.007	-0.016	2.668	-11.996	-6.516	4.613	-3.271	-6.822	-0.035
4	A	4	LYS	1	1.026	1.014	4.295	25.705	25.823	0.000	-0.019	-0.099	0.000
5	A	5	SER	0	-0.026	-0.018	7.279	0.589	0.589	0.000	0.000	0.000	0.000
6	A	6	SER	0	-0.017	0.000	10.218	0.609	0.609	0.000	0.000	0.000	0.000
7	A	7	PRO	0	0.028	0.020	13.987	-0.582	-0.582	0.000	0.000	0.000	0.000
8	A	8	LYS	1	0.938	0.948	15.440	18.562	18.562	0.000	0.000	0.000	0.000
9	A	9	ARG	1	0.835	0.933	18.301	13.345	13.345	0.000	0.000	0.000	0.000
10	A	10	PRO	0	-0.002	0.013	20.092	0.555	0.555	0.000	0.000	0.000	0.000
11	A	11	TYR	0	-0.014	-0.010	18.283	0.453	0.453	0.000	0.000	0.000	0.000
12	A	12	LEU	0	-0.012	0.002	21.297	0.356	0.356	0.000	0.000	0.000	0.000
13	A	13	LEU	0	0.017	0.011	23.945	0.518	0.518	0.000	0.000	0.000	0.000
14	A	14	ARG	1	0.812	0.898	21.668	13.005	13.005	0.000	0.000	0.000	0.000
15	A	15	ALA	0	0.030	0.021	25.240	0.350	0.350	0.000	0.000	0.000	0.000
16	A	16	TYR	0	0.003	-0.008	26.879	0.184	0.184	0.000	0.000	0.000	0.000
17	A	17	TYR	0	-0.062	-0.041	29.801	0.425	0.425	0.000	0.000	0.000	0.000
18	A	18	ASP	-1	-0.884	-0.949	29.369	-9.871	-9.871	0.000	0.000	0.000	0.000
19	A	19	TRP	0	0.002	0.010	31.415	0.301	0.301	0.000	0.000	0.000	0.000
20	A	20	LEU	0	-0.045	-0.015	33.137	0.333	0.333	0.000	0.000	0.000	0.000
21	A	21	VAL	0	-0.027	-0.013	35.331	0.316	0.316	0.000	0.000	0.000	0.000
22	A	22	ASP	-1	-0.916	-0.949	34.653	-8.623	-8.623	0.000	0.000	0.000	0.000
23	A	23	ASN	0	-0.150	-0.088	36.003	0.368	0.368	0.000	0.000	0.000	0.000
24	A	24	SER	0	-0.078	-0.035	39.160	0.257	0.257	0.000	0.000	0.000	0.000
25	A	25	PHE	0	-0.026	0.000	37.807	0.213	0.213	0.000	0.000	0.000	0.000
26	A	26	THR	0	-0.077	-0.081	39.925	0.006	0.006	0.000	0.000	0.000	0.000
27	A	27	PRO	0	-0.016	0.008	35.403	-0.016	-0.016	0.000	0.000	0.000	0.000
28	A	28	TYR	0	-0.025	-0.022	37.131	0.285	0.285	0.000	0.000	0.000	0.000
29	A	29	LEU	0	0.021	0.013	30.642	-0.228	-0.228	0.000	0.000	0.000	0.000
30	A	30	VAL	0	-0.017	-0.012	33.506	0.323	0.323	0.000	0.000	0.000	0.000
31	A	31	VAL	0	-0.001	-0.008	32.187	-0.367	-0.367	0.000	0.000	0.000	0.000
32	A	32	ASP	-1	-0.780	-0.875	31.163	-9.471	-9.471	0.000	0.000	0.000	0.000
33	A	33	ALA	0	-0.039	-0.041	32.999	-0.089	-0.089	0.000	0.000	0.000	0.000
34	A	34	THR	0	-0.108	-0.076	33.839	0.195	0.195	0.000	0.000	0.000	0.000
35	A	35	TYR	0	-0.047	-0.034	24.364	-0.065	-0.065	0.000	0.000	0.000	0.000
36	A	36	LEU	0	0.017	0.009	29.475	0.329	0.329	0.000	0.000	0.000	0.000
37	A	37	GLY	0	0.066	0.009	29.706	-0.280	-0.280	0.000	0.000	0.000	0.000
38	A	38	VAL	0	-0.087	-0.034	31.284	0.046	0.046	0.000	0.000	0.000	0.000
39	A	39	ASN	0	-0.023	0.004	33.144	0.373	0.373	0.000	0.000	0.000	0.000
40	A	40	VAL	0	0.046	-0.002	36.176	-0.002	-0.002	0.000	0.000	0.000	0.000
41	A	41	PRO	0	-0.059	-0.038	38.813	0.109	0.109	0.000	0.000	0.000	0.000
42	A	42	VAL	0	0.084	0.047	40.716	-0.012	-0.012	0.000	0.000	0.000	0.000
43	A	43	GLU	-1	-0.833	-0.906	42.779	-6.824	-6.824	0.000	0.000	0.000	0.000
44	A	44	TYR	0	-0.092	-0.061	43.437	0.245	0.245	0.000	0.000	0.000	0.000
45	A	45	VAL	0	-0.009	0.023	39.700	-0.107	-0.107	0.000	0.000	0.000	0.000
46	A	46	LYS	1	0.907	0.950	41.482	7.243	7.243	0.000	0.000	0.000	0.000
47	A	47	ASP	-1	-0.924	-0.969	40.861	-7.585	-7.585	0.000	0.000	0.000	0.000
48	A	48	GLY	0	0.013	0.017	38.136	-0.184	-0.184	0.000	0.000	0.000	0.000
49	A	49	GLN	0	0.020	0.010	35.268	-0.173	-0.173	0.000	0.000	0.000	0.000
50	A	50	ILE	0	0.014	0.002	36.812	0.311	0.311	0.000	0.000	0.000	0.000
51	A	51	VAL	0	-0.026	-0.009	36.975	-0.231	-0.231	0.000	0.000	0.000	0.000
52	A	52	LEU	0	-0.025	-0.009	35.772	0.254	0.254	0.000	0.000	0.000	0.000
53	A	53	ASN	0	0.023	0.022	37.718	-0.270	-0.270	0.000	0.000	0.000	0.000
54	A	54	LEU	0	0.055	0.025	33.124	0.066	0.066	0.000	0.000	0.000	0.000
55	A	55	SER	0	0.043	0.018	37.243	-0.011	-0.011	0.000	0.000	0.000	0.000
56	A	56	ALA	0	0.039	0.016	39.478	0.070	0.070	0.000	0.000	0.000	0.000
57	A	57	SER	0	-0.065	-0.023	40.622	0.183	0.183	0.000	0.000	0.000	0.000
58	A	58	ALA	0	-0.057	-0.028	41.902	0.173	0.173	0.000	0.000	0.000	0.000
59	A	59	THR	0	-0.060	-0.026	37.994	-0.040	-0.040	0.000	0.000	0.000	0.000
60	A	60	GLY	0	0.003	0.005	40.626	0.095	0.095	0.000	0.000	0.000	0.000
61	A	61	ASN	0	-0.055	-0.052	37.227	-0.103	-0.103	0.000	0.000	0.000	0.000
62	A	62	LEU	0	-0.002	0.018	33.352	-0.161	-0.161	0.000	0.000	0.000	0.000
63	A	63	GLN	0	0.008	0.013	30.207	-0.038	-0.038	0.000	0.000	0.000	0.000
64	A	64	LEU	0	0.034	0.013	28.199	-0.088	-0.088	0.000	0.000	0.000	0.000
65	A	65	THR	0	-0.025	-0.021	25.104	-0.469	-0.469	0.000	0.000	0.000	0.000
66	A	66	ASN	0	0.034	-0.013	18.797	0.290	0.290	0.000	0.000	0.000	0.000
67	A	67	ASP	-1	-0.866	-0.925	20.613	-13.768	-13.768	0.000	0.000	0.000	0.000
68	A	68	PHE	0	-0.002	0.003	23.173	0.181	0.181	0.000	0.000	0.000	0.000
69	A	69	ILE	0	-0.011	0.014	26.932	-0.028	-0.028	0.000	0.000	0.000	0.000
70	A	70	GLN	0	-0.001	-0.004	30.001	0.099	0.099	0.000	0.000	0.000	0.000
71	A	71	PHE	0	0.022	0.008	33.012	0.008	0.008	0.000	0.000	0.000	0.000
72	A	72	ASN	0	-0.017	0.001	36.525	0.110	0.110	0.000	0.000	0.000	0.000
73	A	73	ALA	0	0.088	0.037	40.293	-0.014	-0.014	0.000	0.000	0.000	0.000
74	A	74	ARG	1	0.873	0.931	42.521	6.500	6.500	0.000	0.000	0.000	0.000
75	A	75	PHE	0	0.054	0.035	41.407	0.045	0.045	0.000	0.000	0.000	0.000
76	A	76	LYS	1	0.923	0.948	47.347	6.264	6.264	0.000	0.000	0.000	0.000
77	A	77	GLY	0	0.035	0.025	50.056	0.121	0.121	0.000	0.000	0.000	0.000
78	A	78	VAL	0	-0.002	0.002	48.368	0.011	0.011	0.000	0.000	0.000	0.000
79	A	79	SER	0	-0.045	-0.018	45.508	-0.156	-0.156	0.000	0.000	0.000	0.000
80	A	80	ARG	1	0.870	0.911	43.083	6.969	6.969	0.000	0.000	0.000	0.000
81	A	81	GLU	-1	-0.881	-0.935	37.302	-7.986	-7.986	0.000	0.000	0.000	0.000
82	A	82	LEU	0	-0.046	-0.009	36.719	0.090	0.090	0.000	0.000	0.000	0.000
83	A	83	TYR	0	0.030	0.013	27.947	-0.108	-0.108	0.000	0.000	0.000	0.000
84	A	84	ILE	0	0.012	0.003	30.080	0.109	0.109	0.000	0.000	0.000	0.000
85	A	85	PRO	0	0.061	0.041	26.493	-0.279	-0.279	0.000	0.000	0.000	0.000
86	A	86	MET	0	-0.028	-0.016	23.272	0.176	0.176	0.000	0.000	0.000	0.000
87	A	87	GLY	0	0.009	-0.007	24.432	-0.124	-0.124	0.000	0.000	0.000	0.000
88	A	88	ALA	0	0.018	0.021	25.140	0.026	0.026	0.000	0.000	0.000	0.000
89	A	89	ALA	0	-0.034	-0.008	27.253	0.379	0.379	0.000	0.000	0.000	0.000
90	A	90	LEU	0	0.008	-0.002	27.590	-0.397	-0.397	0.000	0.000	0.000	0.000
91	A	91	ALA	0	0.002	-0.006	29.486	-0.225	-0.225	0.000	0.000	0.000	0.000
92	A	92	ILE	0	-0.037	-0.008	29.923	0.236	0.236	0.000	0.000	0.000	0.000
93	A	93	TYR	0	-0.006	0.001	32.371	-0.041	-0.041	0.000	0.000	0.000	0.000
94	A	94	ALA	0	0.067	0.041	35.271	0.132	0.132	0.000	0.000	0.000	0.000
95	A	95	ARG	1	0.838	0.917	38.466	7.238	7.238	0.000	0.000	0.000	0.000
96	A	96	GLU	-1	-0.806	-0.889	41.565	-7.342	-7.342	0.000	0.000	0.000	0.000
97	A	97	ASN	0	-0.024	-0.020	39.560	0.083	0.083	0.000	0.000	0.000	0.000
98	A	98	GLY	0	-0.018	0.005	39.216	-0.004	-0.004	0.000	0.000	0.000	0.000
99	A	99	ASP	-1	-0.905	-0.947	35.321	-9.293	-9.293	0.000	0.000	0.000	0.000
100	A	100	GLY	0	0.021	-0.006	32.885	0.095	0.095	0.000	0.000	0.000	0.000
101	A	101	VAL	0	-0.047	-0.012	26.792	-0.217	-0.217	0.000	0.000	0.000	0.000
102	A	102	MET	0	0.007	0.002	28.781	0.394	0.394	0.000	0.000	0.000	0.000
103	A	103	PHE	0	-0.041	-0.038	24.754	-0.368	-0.368	0.000	0.000	0.000	0.000
104	A	104	GLU	-1	-0.910	-0.950	21.981	-13.252	-13.252	0.000	0.000	0.000	0.000
105	A	105	PRO	0	0.019	0.008	22.118	0.001	0.001	0.000	0.000	0.000	0.000
106	A	106	GLU	-1	-0.780	-0.893	17.469	-17.529	-17.529	0.000	0.000	0.000	0.000
107	A	107	GLU	-1	-0.895	-0.937	16.487	-18.470	-18.470	0.000	0.000	0.000	0.000
108	A	108	ILE	0	0.005	0.009	14.378	0.470	0.470	0.000	0.000	0.000	0.000
109	A	109	TYR	0	-0.005	-0.017	17.943	0.543	0.543	0.000	0.000	0.000	0.000
110	A	110	ASP	-1	-0.879	-0.922	21.326	-12.812	-12.812	0.000	0.000	0.000	0.000
111	A	111	GLU	-1	-0.983	-0.999	16.586	-17.233	-17.233	0.000	0.000	0.000	0.000
112	A	112	LEU	0	-0.049	-0.033	19.181	0.301	0.301	0.000	0.000	0.000	0.000
113	A	113	ASN	0	-0.016	0.019	22.460	0.754	0.754	0.000	0.000	0.000	0.000
114	A	114	ILE	0	-0.033	-0.025	23.708	0.235	0.235	0.000	0.000	0.000	0.000
115	A	115	GLU	-1	-0.956	-0.976	27.372	-8.763	-8.763	0.000	0.000	0.000	0.000
116	A	116	PRO	0	-0.042	-0.016	28.359	-0.073	-0.073	0.000	0.000	0.000	0.000
117	A	117	ASP	-1	-0.919	-0.955	30.294	-8.911	-8.911	0.000	0.000	0.000	0.000
118	A	118	THR	0	-0.043	-0.028	33.244	-0.080	-0.080	0.000	0.000	0.000	0.000
119	A	119	GLU	-1	-0.971	-0.976	35.996	-7.227	-7.227	0.000	0.000	0.000	0.000
120	A	120	GLN	0	-0.086	-0.053	36.558	-0.136	-0.136	0.000	0.000	0.000	0.000
121	A	121	PRO	-1	-0.948	-0.962	35.758	-7.285	-7.285	0.000	0.000	0.000	0.000

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