FMO DATABASE

FMODB ID: NZR1Q

Calculation Name: 2I2R-K-Xray547

Preferred Name:

Target Type:

Ligand Name: calcium ion | zinc ion

Ligand 3-letter code: CA | ZN

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2I2R

Chain ID: K

ChEMBL ID:

UniProt ID: Q9NZI2

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	138
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1210774.812299
FMO2-HF: Nuclear repulsion	1153453.349218
FMO2-HF: Total energy	-57321.463082
FMO2-MP2: Total energy	-57486.607497

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:3:ALA)

Summations of interaction energy for fragment #1(A:3:ALA)

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.
-47.127	-41.815	0.39	-2.372	-3.328	-0.01

Interaction energy analysis for fragmet #1(A:3:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.936 / q_NPA : 0.950

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	5	VAL	0	0.028	0.018	2.873	7.132	9.656	0.062	-1.142	-1.443	-0.002
4	A	6	ALA	0	0.032	0.012	4.620	8.102	8.281	-0.001	-0.018	-0.159	0.000
54	A	56	THR	0	-0.083	-0.079	2.640	-7.513	-6.292	0.293	-0.644	-0.870	-0.004
55	A	57	THR	0	-0.123	-0.056	3.665	-13.535	-12.862	0.009	-0.301	-0.381	-0.002
56	A	58	LEU	0	0.063	0.027	4.429	0.591	0.589	-0.001	-0.009	0.012	0.000
58	A	60	ARG	1	0.790	0.912	3.724	47.134	47.868	0.029	-0.257	-0.507	-0.002
59	A	61	TYR	0	0.031	0.023	5.196	0.651	0.634	-0.001	-0.001	0.020	0.000
5	A	7	ALA	0	-0.003	-0.003	6.585	5.091	5.091	0.000	0.000	0.000	0.000
6	A	8	TRP	0	0.004	-0.002	7.937	4.075	4.075	0.000	0.000	0.000	0.000
7	A	9	LEU	0	0.000	0.016	9.603	2.312	2.312	0.000	0.000	0.000	0.000
8	A	10	PRO	0	-0.022	-0.018	11.225	2.230	2.230	0.000	0.000	0.000	0.000
9	A	11	PHE	0	0.010	0.007	13.644	1.621	1.621	0.000	0.000	0.000	0.000
10	A	12	ALA	0	0.004	0.008	14.274	1.160	1.160	0.000	0.000	0.000	0.000
11	A	13	ARG	1	0.754	0.828	12.692	22.787	22.787	0.000	0.000	0.000	0.000
12	A	14	ALA	0	-0.006	-0.012	17.146	0.983	0.983	0.000	0.000	0.000	0.000
13	A	15	ALA	0	-0.010	0.001	19.401	0.830	0.830	0.000	0.000	0.000	0.000
14	A	16	ALA	0	-0.011	0.004	20.389	0.502	0.502	0.000	0.000	0.000	0.000
15	A	17	ILE	0	-0.038	-0.017	21.527	0.577	0.577	0.000	0.000	0.000	0.000
16	A	18	GLY	0	0.015	0.010	24.346	0.280	0.280	0.000	0.000	0.000	0.000
17	A	19	TRP	0	-0.041	-0.020	26.297	0.521	0.521	0.000	0.000	0.000	0.000
18	A	20	MET	0	0.013	0.009	21.717	-0.277	-0.277	0.000	0.000	0.000	0.000
19	A	21	PRO	0	-0.015	0.007	25.136	0.035	0.035	0.000	0.000	0.000	0.000
20	A	22	VAL	0	0.038	-0.003	23.101	-0.424	-0.424	0.000	0.000	0.000	0.000
21	A	23	ALA	0	-0.034	-0.007	23.678	-0.233	-0.233	0.000	0.000	0.000	0.000
22	A	24	ASN	0	0.017	0.006	22.917	-0.295	-0.295	0.000	0.000	0.000	0.000
23	A	25	CYS	0	-0.010	0.000	18.614	-0.442	-0.442	0.000	0.000	0.000	0.000
24	A	26	PRO	0	0.051	0.017	16.574	-0.312	-0.312	0.000	0.000	0.000	0.000
25	A	27	MET	0	-0.043	-0.024	12.439	-1.022	-1.022	0.000	0.000	0.000	0.000
26	A	28	PRO	0	0.069	0.042	14.056	-1.017	-1.017	0.000	0.000	0.000	0.000
27	A	29	LEU	0	0.026	0.012	15.446	0.104	0.104	0.000	0.000	0.000	0.000
28	A	30	ALA	0	0.053	0.034	14.576	-0.606	-0.606	0.000	0.000	0.000	0.000
29	A	31	PRO	0	0.004	0.003	14.859	-0.742	-0.742	0.000	0.000	0.000	0.000
30	A	32	ALA	0	0.027	0.039	11.544	-0.402	-0.402	0.000	0.000	0.000	0.000
31	A	33	ASP	-1	-0.791	-0.880	10.298	-26.956	-26.956	0.000	0.000	0.000	0.000
32	A	34	LYS	1	0.845	0.910	9.522	24.731	24.731	0.000	0.000	0.000	0.000
33	A	35	ASN	0	-0.023	-0.007	9.982	-1.382	-1.382	0.000	0.000	0.000	0.000
34	A	36	LYS	1	0.890	0.942	7.177	36.441	36.441	0.000	0.000	0.000	0.000
35	A	37	ARG	1	0.863	0.913	12.313	20.183	20.183	0.000	0.000	0.000	0.000
36	A	38	GLN	0	0.043	0.024	8.973	-3.970	-3.970	0.000	0.000	0.000	0.000
37	A	39	ASP	-1	-0.775	-0.848	5.769	-41.028	-41.028	0.000	0.000	0.000	0.000
38	A	40	GLU	-1	-0.790	-0.876	8.681	-19.882	-19.882	0.000	0.000	0.000	0.000
39	A	41	LEU	0	-0.021	-0.012	9.828	-2.231	-2.231	0.000	0.000	0.000	0.000
40	A	42	ILE	0	0.007	0.003	10.346	1.357	1.357	0.000	0.000	0.000	0.000
41	A	43	VAL	0	0.010	-0.009	13.135	-0.475	-0.475	0.000	0.000	0.000	0.000
42	A	44	LEU	0	0.006	0.004	12.317	0.107	0.107	0.000	0.000	0.000	0.000
43	A	45	ASN	0	-0.042	-0.030	16.690	0.409	0.409	0.000	0.000	0.000	0.000
44	A	46	VAL	0	0.053	0.035	18.870	0.226	0.226	0.000	0.000	0.000	0.000
45	A	47	SER	0	-0.003	0.001	21.725	0.381	0.381	0.000	0.000	0.000	0.000
46	A	48	GLY	0	0.045	0.028	24.226	0.478	0.478	0.000	0.000	0.000	0.000
47	A	49	ARG	1	0.879	0.937	20.187	13.624	13.624	0.000	0.000	0.000	0.000
48	A	50	ARG	1	0.827	0.896	19.601	12.331	12.331	0.000	0.000	0.000	0.000
49	A	51	PHE	0	-0.022	0.002	14.973	-0.425	-0.425	0.000	0.000	0.000	0.000
50	A	52	GLN	0	-0.002	-0.004	13.567	-0.417	-0.417	0.000	0.000	0.000	0.000
51	A	53	THR	0	-0.022	-0.027	7.694	-0.956	-0.956	0.000	0.000	0.000	0.000
52	A	54	TRP	0	-0.018	0.016	5.513	1.366	1.366	0.000	0.000	0.000	0.000
53	A	55	ARG	1	0.863	0.900	6.997	28.793	28.793	0.000	0.000	0.000	0.000
57	A	59	GLU	-1	-0.810	-0.892	5.552	-39.059	-39.059	0.000	0.000	0.000	0.000
60	A	62	PRO	0	-0.001	0.009	8.416	2.075	2.075	0.000	0.000	0.000	0.000
61	A	63	ASP	-1	-0.945	-0.976	11.204	-19.921	-19.921	0.000	0.000	0.000	0.000
62	A	64	THR	0	0.075	0.060	12.171	0.870	0.870	0.000	0.000	0.000	0.000
63	A	65	LEU	0	0.013	0.032	14.393	-1.187	-1.187	0.000	0.000	0.000	0.000
64	A	66	LEU	0	0.001	-0.018	12.738	-0.166	-0.166	0.000	0.000	0.000	0.000
65	A	67	GLY	0	0.002	0.006	10.403	-1.306	-1.306	0.000	0.000	0.000	0.000
66	A	68	SER	0	-0.082	-0.037	11.075	-0.574	-0.574	0.000	0.000	0.000	0.000
67	A	69	THR	0	-0.012	-0.027	13.940	-0.415	-0.415	0.000	0.000	0.000	0.000
68	A	70	GLU	-1	-0.893	-0.933	16.829	-14.799	-14.799	0.000	0.000	0.000	0.000
69	A	71	LYS	1	0.857	0.922	12.643	23.599	23.599	0.000	0.000	0.000	0.000
70	A	72	GLU	-1	-0.846	-0.895	17.844	-17.025	-17.025	0.000	0.000	0.000	0.000
71	A	73	PHE	0	-0.071	-0.034	19.943	0.698	0.698	0.000	0.000	0.000	0.000
72	A	74	PHE	0	0.012	0.007	20.241	0.581	0.581	0.000	0.000	0.000	0.000
73	A	75	PHE	0	-0.029	-0.008	18.732	-0.259	-0.259	0.000	0.000	0.000	0.000
74	A	76	ASN	0	0.003	0.012	21.427	0.818	0.818	0.000	0.000	0.000	0.000
75	A	77	GLU	-1	-0.867	-0.940	23.447	-12.925	-12.925	0.000	0.000	0.000	0.000
76	A	78	ASP	-1	-0.966	-0.982	25.399	-10.657	-10.657	0.000	0.000	0.000	0.000
77	A	79	THR	0	-0.102	-0.088	24.186	-0.078	-0.078	0.000	0.000	0.000	0.000
78	A	80	LYS	1	0.839	0.938	20.790	12.573	12.573	0.000	0.000	0.000	0.000
79	A	81	GLU	-1	-0.754	-0.831	18.841	-14.174	-14.174	0.000	0.000	0.000	0.000
80	A	82	TYR	0	-0.054	-0.057	14.970	-0.258	-0.258	0.000	0.000	0.000	0.000
81	A	83	PHE	0	-0.046	-0.024	19.173	-0.104	-0.104	0.000	0.000	0.000	0.000
82	A	84	PHE	0	0.023	0.000	17.135	-0.095	-0.095	0.000	0.000	0.000	0.000
83	A	85	ASP	-1	-0.922	-0.960	22.468	-10.732	-10.732	0.000	0.000	0.000	0.000
84	A	86	ARG	1	0.828	0.909	22.594	12.837	12.837	0.000	0.000	0.000	0.000
85	A	87	ASP	-1	-0.751	-0.870	24.153	-12.258	-12.258	0.000	0.000	0.000	0.000
86	A	88	PRO	0	-0.060	-0.032	21.470	-0.750	-0.750	0.000	0.000	0.000	0.000
87	A	89	GLU	-1	-0.833	-0.911	20.798	-14.086	-14.086	0.000	0.000	0.000	0.000
88	A	90	VAL	0	0.055	0.012	20.740	-0.762	-0.762	0.000	0.000	0.000	0.000
89	A	91	PHE	0	0.019	0.015	15.375	-1.180	-1.180	0.000	0.000	0.000	0.000
90	A	92	ARG	1	0.823	0.900	16.286	13.274	13.274	0.000	0.000	0.000	0.000
91	A	93	CYS	0	-0.046	-0.003	15.439	-1.107	-1.107	0.000	0.000	0.000	0.000
92	A	94	VAL	0	0.061	0.042	14.715	-1.203	-1.203	0.000	0.000	0.000	0.000
93	A	95	LEU	0	-0.017	-0.009	10.657	-1.888	-1.888	0.000	0.000	0.000	0.000
94	A	96	ASN	0	-0.102	-0.091	10.646	-3.225	-3.225	0.000	0.000	0.000	0.000
95	A	97	PHE	0	0.075	0.058	10.919	-1.928	-1.928	0.000	0.000	0.000	0.000
96	A	98	TYR	0	0.023	-0.012	7.762	-2.327	-2.327	0.000	0.000	0.000	0.000
97	A	99	ARG	1	0.828	0.920	6.331	17.824	17.824	0.000	0.000	0.000	0.000
98	A	100	THR	0	-0.072	-0.039	6.725	-3.597	-3.597	0.000	0.000	0.000	0.000
99	A	101	GLY	0	0.043	0.017	9.364	1.121	1.121	0.000	0.000	0.000	0.000
100	A	102	LYS	1	0.927	0.971	10.588	20.653	20.653	0.000	0.000	0.000	0.000
101	A	103	LEU	0	0.026	0.031	14.221	-0.488	-0.488	0.000	0.000	0.000	0.000
102	A	104	HIS	0	-0.054	-0.090	15.896	-0.208	-0.208	0.000	0.000	0.000	0.000
103	A	105	TYR	0	0.039	0.011	18.896	-0.136	-0.136	0.000	0.000	0.000	0.000
104	A	106	PRO	0	-0.027	-0.014	21.292	0.208	0.208	0.000	0.000	0.000	0.000
105	A	107	ARG	1	0.942	0.957	23.632	12.175	12.175	0.000	0.000	0.000	0.000
106	A	108	TYR	0	-0.062	-0.023	23.807	0.282	0.282	0.000	0.000	0.000	0.000
107	A	109	GLU	-1	-0.848	-0.926	25.497	-10.749	-10.749	0.000	0.000	0.000	0.000
108	A	110	CYS	0	-0.087	-0.026	28.158	0.159	0.159	0.000	0.000	0.000	0.000
109	A	111	ILE	0	0.065	0.037	27.558	-0.342	-0.342	0.000	0.000	0.000	0.000
110	A	112	SER	0	0.029	0.010	27.787	-0.208	-0.208	0.000	0.000	0.000	0.000
111	A	113	ALA	0	0.011	0.006	28.290	-0.190	-0.190	0.000	0.000	0.000	0.000
112	A	114	TYR	0	-0.008	-0.029	20.207	-0.442	-0.442	0.000	0.000	0.000	0.000
113	A	115	ASP	-1	-0.751	-0.854	23.559	-12.418	-12.418	0.000	0.000	0.000	0.000
114	A	116	ASP	-1	-0.911	-0.953	24.805	-11.090	-11.090	0.000	0.000	0.000	0.000
115	A	117	GLU	-1	-0.860	-0.923	21.702	-13.436	-13.436	0.000	0.000	0.000	0.000
116	A	118	LEU	0	-0.039	-0.021	18.950	-0.767	-0.767	0.000	0.000	0.000	0.000
117	A	119	ALA	0	0.007	0.006	20.500	-0.592	-0.592	0.000	0.000	0.000	0.000
118	A	120	PHE	0	-0.024	-0.004	21.179	-0.207	-0.207	0.000	0.000	0.000	0.000
119	A	121	TYR	0	-0.032	-0.044	16.986	-0.464	-0.464	0.000	0.000	0.000	0.000
120	A	122	GLY	0	0.036	0.018	17.308	-1.198	-1.198	0.000	0.000	0.000	0.000
121	A	123	ILE	0	-0.066	-0.029	14.756	-0.856	-0.856	0.000	0.000	0.000	0.000
122	A	124	LEU	0	0.015	-0.003	17.987	0.966	0.966	0.000	0.000	0.000	0.000
123	A	125	PRO	0	0.016	-0.004	19.971	-0.457	-0.457	0.000	0.000	0.000	0.000
124	A	126	GLU	-1	-0.843	-0.913	21.907	-12.452	-12.452	0.000	0.000	0.000	0.000
125	A	127	ILE	0	-0.057	-0.017	14.937	-0.382	-0.382	0.000	0.000	0.000	0.000
126	A	128	ILE	0	-0.053	-0.015	17.358	-0.963	-0.963	0.000	0.000	0.000	0.000
127	A	129	GLY	0	0.010	0.012	18.770	0.190	0.190	0.000	0.000	0.000	0.000
128	A	130	ASP	-1	-0.856	-0.941	19.399	-14.022	-14.022	0.000	0.000	0.000	0.000
129	A	131	CYS	0	-0.117	-0.088	20.473	0.238	0.238	0.000	0.000	0.000	0.000
130	A	132	CYS	-1	-0.803	-0.817	21.476	-14.081	-14.081	0.000	0.000	0.000	0.000
131	A	133	TYR	0	-0.078	-0.049	23.235	0.610	0.610	0.000	0.000	0.000	0.000
132	A	134	GLU	-1	-0.905	-0.945	24.906	-10.378	-10.378	0.000	0.000	0.000	0.000
133	A	135	GLU	-1	-0.968	-1.002	27.052	-10.003	-10.003	0.000	0.000	0.000	0.000
134	A	136	TYR	0	-0.082	-0.074	25.348	0.269	0.269	0.000	0.000	0.000	0.000
135	A	137	LYS	1	0.854	0.938	27.499	9.640	9.640	0.000	0.000	0.000	0.000
136	A	138	ASP	-1	-0.887	-0.959	30.649	-9.018	-9.018	0.000	0.000	0.000	0.000
137	A	139	ARG	1	0.801	0.913	30.247	10.506	10.506	0.000	0.000	0.000	0.000
138	A	140	LYS	0	-0.101	-0.036	27.686	1.696	1.696	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

Interactive mode: IFIE and PIEDA for fragment #1(A:3:ALA)