FMO DATABASE

FMODB ID: GRQY1

Calculation Name: 2QT7-A-Xray547

Preferred Name:

Target Type:

Ligand Name: calcium ion

Ligand 3-letter code: CA

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2QT7

Chain ID: A

ChEMBL ID:

UniProt ID: Q16849

Base Structure: X-ray

Registration Date: 2025-10-04

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	89
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-595376.878547
FMO2-HF: Nuclear repulsion	562061.672382
FMO2-HF: Total energy	-33315.206165
FMO2-MP2: Total energy	-33414.114295

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:21:GLU)

Summations of interaction energy for fragment #1(A:21: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.
-38.16	-40.863	28.855	-13.757	-12.395	0.095

Interaction energy analysis for fragmet #1(A:21:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.062 / q_NPA : -0.007

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

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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	23	TYR	0	-0.055	-0.063	1.668	-23.882	-26.037	17.525	-8.547	-6.823	0.060
49	A	69	ARG	1	0.919	0.971	3.748	1.233	1.563	0.002	-0.050	-0.281	0.000
88	A	108	GLN	0	0.005	-0.023	1.829	-16.307	-17.516	11.329	-5.150	-4.970	0.035
89	A	109	ARG	0	-0.051	0.008	4.746	-0.409	-0.078	-0.001	-0.010	-0.321	0.000
4	A	24	GLY	0	0.024	0.019	5.935	-1.269	-1.269	0.000	0.000	0.000	0.000
5	A	25	TYR	0	-0.064	-0.068	7.678	1.604	1.604	0.000	0.000	0.000	0.000
6	A	26	ILE	0	0.018	0.004	11.876	-0.456	-0.456	0.000	0.000	0.000	0.000
7	A	27	VAL	0	-0.032	-0.011	14.921	0.461	0.461	0.000	0.000	0.000	0.000
8	A	28	THR	0	-0.003	-0.017	17.203	-0.191	-0.191	0.000	0.000	0.000	0.000
9	A	29	ASP	-1	-0.800	-0.900	20.613	0.648	0.648	0.000	0.000	0.000	0.000
10	A	30	GLN	0	-0.067	-0.023	21.616	0.099	0.099	0.000	0.000	0.000	0.000
11	A	31	LYS	1	0.927	0.970	21.823	-1.006	-1.006	0.000	0.000	0.000	0.000
12	A	32	PRO	0	-0.031	-0.024	19.561	-0.053	-0.053	0.000	0.000	0.000	0.000
13	A	33	LEU	0	0.061	0.016	16.910	-0.160	-0.160	0.000	0.000	0.000	0.000
14	A	34	SER	0	0.002	-0.001	19.077	0.273	0.273	0.000	0.000	0.000	0.000
15	A	35	LEU	0	0.059	0.016	15.652	-0.059	-0.059	0.000	0.000	0.000	0.000
16	A	36	ALA	0	-0.004	0.000	18.775	-0.065	-0.065	0.000	0.000	0.000	0.000
17	A	37	ALA	0	0.043	0.024	21.962	-0.129	-0.129	0.000	0.000	0.000	0.000
18	A	38	GLY	0	0.022	0.005	17.750	-0.132	-0.132	0.000	0.000	0.000	0.000
19	A	39	VAL	0	-0.002	-0.021	17.150	-0.111	-0.111	0.000	0.000	0.000	0.000
20	A	40	LYS	1	0.905	0.958	19.139	-0.726	-0.726	0.000	0.000	0.000	0.000
21	A	41	LEU	0	0.003	0.001	18.770	-0.145	-0.145	0.000	0.000	0.000	0.000
22	A	42	LEU	0	-0.035	-0.021	14.416	-0.131	-0.131	0.000	0.000	0.000	0.000
23	A	43	GLU	-1	-0.864	-0.907	18.597	0.393	0.393	0.000	0.000	0.000	0.000
24	A	44	ILE	0	0.037	0.025	21.987	-0.110	-0.110	0.000	0.000	0.000	0.000
25	A	45	LEU	0	-0.024	0.001	17.048	-0.124	-0.124	0.000	0.000	0.000	0.000
26	A	46	ALA	0	-0.044	-0.022	19.872	-0.176	-0.176	0.000	0.000	0.000	0.000
27	A	47	GLU	-1	-0.924	-0.960	21.258	-0.009	-0.009	0.000	0.000	0.000	0.000
28	A	48	HIS	0	-0.021	-0.010	22.678	-0.024	-0.024	0.000	0.000	0.000	0.000
29	A	49	VAL	0	-0.074	-0.048	18.941	-0.112	-0.112	0.000	0.000	0.000	0.000
30	A	50	HIS	0	0.002	0.019	22.230	-0.085	-0.085	0.000	0.000	0.000	0.000
31	A	51	MET	0	-0.060	-0.021	16.186	-0.161	-0.161	0.000	0.000	0.000	0.000
32	A	52	SER	0	0.021	0.013	20.743	0.166	0.166	0.000	0.000	0.000	0.000
33	A	53	SER	0	0.080	0.009	18.983	-0.057	-0.057	0.000	0.000	0.000	0.000
34	A	54	GLY	0	0.008	0.009	17.245	0.136	0.136	0.000	0.000	0.000	0.000
35	A	55	SER	0	-0.069	-0.053	15.828	0.115	0.115	0.000	0.000	0.000	0.000
36	A	56	PHE	0	0.013	0.006	12.962	-0.245	-0.245	0.000	0.000	0.000	0.000
37	A	57	ILE	0	-0.042	-0.026	9.327	0.447	0.447	0.000	0.000	0.000	0.000
38	A	58	ASN	0	-0.027	-0.033	6.717	-0.808	-0.808	0.000	0.000	0.000	0.000
39	A	59	ILE	0	0.060	0.044	8.362	1.464	1.464	0.000	0.000	0.000	0.000
40	A	60	SER	0	-0.034	-0.025	9.575	1.295	1.295	0.000	0.000	0.000	0.000
41	A	61	VAL	0	-0.011	0.018	11.431	-0.260	-0.260	0.000	0.000	0.000	0.000
42	A	62	VAL	0	0.016	0.004	10.350	0.430	0.430	0.000	0.000	0.000	0.000
43	A	63	GLY	0	0.020	0.013	13.831	-0.414	-0.414	0.000	0.000	0.000	0.000
44	A	64	PRO	0	0.033	0.028	17.143	-0.010	-0.010	0.000	0.000	0.000	0.000
45	A	65	ALA	0	-0.002	0.014	13.493	-0.329	-0.329	0.000	0.000	0.000	0.000
46	A	66	LEU	0	-0.004	0.010	13.521	0.560	0.560	0.000	0.000	0.000	0.000
47	A	67	THR	0	0.004	0.010	8.218	0.331	0.331	0.000	0.000	0.000	0.000
48	A	68	PHE	0	0.017	0.003	9.223	0.841	0.841	0.000	0.000	0.000	0.000
50	A	70	ILE	0	0.027	0.009	8.323	0.587	0.587	0.000	0.000	0.000	0.000
51	A	71	ARG	1	0.869	0.947	10.075	-1.113	-1.113	0.000	0.000	0.000	0.000
52	A	72	HIS	0	0.010	-0.002	12.643	-0.547	-0.547	0.000	0.000	0.000	0.000
53	A	73	ASN	0	-0.012	-0.017	14.597	0.483	0.483	0.000	0.000	0.000	0.000
54	A	74	GLU	-1	-0.867	-0.937	17.752	-1.307	-1.307	0.000	0.000	0.000	0.000
55	A	75	GLN	0	-0.057	-0.022	20.132	-0.048	-0.048	0.000	0.000	0.000	0.000
56	A	76	ASN	0	-0.076	-0.033	16.020	-0.268	-0.268	0.000	0.000	0.000	0.000
57	A	77	LEU	0	0.004	0.017	16.378	-0.316	-0.316	0.000	0.000	0.000	0.000
58	A	78	SER	0	-0.003	-0.041	11.831	-0.315	-0.315	0.000	0.000	0.000	0.000
59	A	79	LEU	0	-0.003	-0.022	6.680	0.633	0.633	0.000	0.000	0.000	0.000
60	A	80	ALA	0	0.029	0.030	11.266	0.575	0.575	0.000	0.000	0.000	0.000
61	A	81	ASP	-1	-0.804	-0.857	13.521	-2.386	-2.386	0.000	0.000	0.000	0.000
62	A	82	VAL	0	0.025	0.004	13.819	0.352	0.352	0.000	0.000	0.000	0.000
63	A	83	THR	0	-0.026	-0.029	12.337	0.335	0.335	0.000	0.000	0.000	0.000
64	A	84	GLN	0	-0.002	0.013	15.727	0.431	0.431	0.000	0.000	0.000	0.000
65	A	85	GLN	0	0.030	0.013	18.786	0.365	0.365	0.000	0.000	0.000	0.000
66	A	86	ALA	0	0.006	0.003	17.817	0.163	0.163	0.000	0.000	0.000	0.000
67	A	87	GLY	0	-0.005	-0.005	19.762	0.166	0.166	0.000	0.000	0.000	0.000
68	A	88	LEU	0	-0.067	-0.027	21.191	0.090	0.090	0.000	0.000	0.000	0.000
69	A	89	VAL	0	0.027	0.016	23.465	0.073	0.073	0.000	0.000	0.000	0.000
70	A	90	LYS	1	0.962	0.995	23.000	0.444	0.444	0.000	0.000	0.000	0.000
71	A	91	SER	0	0.006	-0.015	24.318	0.078	0.078	0.000	0.000	0.000	0.000
72	A	92	GLU	-1	-0.957	-0.966	27.025	-0.115	-0.115	0.000	0.000	0.000	0.000
73	A	93	LEU	0	0.006	0.004	20.909	0.083	0.083	0.000	0.000	0.000	0.000
74	A	94	GLU	-1	-0.806	-0.885	24.943	0.137	0.137	0.000	0.000	0.000	0.000
75	A	95	ALA	0	-0.005	-0.002	26.302	0.082	0.082	0.000	0.000	0.000	0.000
76	A	96	GLN	0	-0.031	-0.006	27.189	0.070	0.070	0.000	0.000	0.000	0.000
77	A	97	THR	0	-0.089	-0.081	23.084	0.097	0.097	0.000	0.000	0.000	0.000
78	A	98	GLY	0	-0.036	0.002	26.072	0.092	0.092	0.000	0.000	0.000	0.000
79	A	99	LEU	0	-0.063	-0.024	22.078	0.083	0.083	0.000	0.000	0.000	0.000
80	A	100	GLN	0	-0.013	-0.006	25.351	-0.073	-0.073	0.000	0.000	0.000	0.000
81	A	101	ILE	0	-0.022	-0.030	19.927	0.107	0.107	0.000	0.000	0.000	0.000
82	A	102	LEU	0	-0.062	-0.030	20.925	-0.136	-0.136	0.000	0.000	0.000	0.000
83	A	103	GLN	0	-0.036	-0.030	17.380	-0.013	-0.013	0.000	0.000	0.000	0.000
84	A	104	THR	0	-0.028	-0.016	15.797	0.233	0.233	0.000	0.000	0.000	0.000
85	A	105	GLY	0	0.024	0.016	13.621	-0.092	-0.092	0.000	0.000	0.000	0.000
86	A	106	VAL	0	0.000	-0.004	7.828	0.437	0.437	0.000	0.000	0.000	0.000
87	A	107	GLY	0	0.030	0.021	7.601	0.032	0.032	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:21:GLU)