FMO DATABASE

FMODB ID: 749NK

Calculation Name: 1S7Z-A-Xray549

Preferred Name:

Target Type:

Ligand Name: cesium ion

Ligand 3-letter code: CS

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1S7Z

Chain ID: A

ChEMBL ID:

UniProt ID: P03775

Base Structure: X-ray

Registration Date: 2025-10-11

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	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	106
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-840798.02449
FMO2-HF: Nuclear repulsion	796188.499679
FMO2-HF: Total energy	-44609.524811
FMO2-MP2: Total energy	-44737.304662

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:5:MET)

Summations of interaction energy for fragment #1(A:5: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.
-408.113	-396.507	14.977	-10.98	-15.601	-0.117

Interaction energy analysis for fragmet #1(A:5:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.741 / q_NPA : 0.877

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	7	TYR	0	0.029	-0.027	2.854	-6.999	-2.856	0.280	-2.231	-2.193	-0.018
4	A	8	ASN	0	0.027	0.010	5.181	4.016	4.199	-0.001	-0.007	-0.174	0.000
5	A	9	ASN	0	-0.037	-0.020	2.284	-8.894	-8.649	5.113	-2.062	-3.296	-0.027
6	A	10	VAL	0	-0.033	-0.019	2.632	0.570	1.786	0.490	-0.330	-1.376	-0.004
7	A	11	PHE	0	0.030	0.018	5.200	2.420	2.477	0.000	-0.012	-0.044	0.000
9	A	13	HIS	0	-0.080	-0.044	4.151	3.209	3.483	0.003	-0.037	-0.241	0.000
42	A	46	PRO	0	-0.027	-0.007	3.427	-0.273	0.041	0.005	-0.049	-0.269	0.000
47	A	51	ASP	-1	-0.856	-0.936	2.592	-78.735	-75.709	1.778	-1.960	-2.844	-0.020
48	A	52	ILE	0	0.024	0.020	3.534	-4.611	-4.081	0.011	-0.281	-0.259	-0.002
50	A	54	SER	0	-0.042	-0.023	1.974	-17.183	-16.617	6.118	-3.503	-3.181	-0.041
51	A	55	VAL	0	-0.002	0.015	2.462	-4.146	-3.235	1.181	-0.490	-1.602	-0.005
52	A	56	MET	0	0.025	0.024	4.811	4.003	4.144	-0.001	-0.018	-0.122	0.000
8	A	12	ASP	-1	-0.887	-0.947	6.832	-25.943	-25.943	0.000	0.000	0.000	0.000
10	A	14	ALA	0	0.028	0.011	8.726	1.733	1.733	0.000	0.000	0.000	0.000
11	A	15	TYR	0	0.000	0.008	11.106	1.575	1.575	0.000	0.000	0.000	0.000
12	A	16	GLU	-1	-0.936	-0.966	11.914	-15.181	-15.181	0.000	0.000	0.000	0.000
13	A	17	MET	0	-0.037	-0.021	11.707	0.964	0.964	0.000	0.000	0.000	0.000
14	A	18	LEU	0	0.011	0.014	14.456	0.984	0.984	0.000	0.000	0.000	0.000
15	A	19	LYS	1	0.881	0.924	16.152	15.431	15.431	0.000	0.000	0.000	0.000
16	A	20	GLU	-1	-0.909	-0.942	15.226	-15.061	-15.061	0.000	0.000	0.000	0.000
17	A	21	ASN	0	-0.051	-0.037	17.644	0.835	0.835	0.000	0.000	0.000	0.000
18	A	22	ILE	0	-0.005	0.000	20.480	0.591	0.591	0.000	0.000	0.000	0.000
19	A	23	ARG	1	0.792	0.877	22.050	12.171	12.171	0.000	0.000	0.000	0.000
20	A	24	TYR	0	-0.198	-0.119	18.795	0.742	0.742	0.000	0.000	0.000	0.000
21	A	25	ASP	-1	-0.928	-0.964	24.601	-10.826	-10.826	0.000	0.000	0.000	0.000
22	A	26	ASP	-1	-0.890	-0.892	26.613	-8.990	-8.990	0.000	0.000	0.000	0.000
23	A	27	ILE	0	-0.003	0.007	23.322	0.263	0.263	0.000	0.000	0.000	0.000
24	A	28	ARG	1	0.829	0.872	27.212	9.032	9.032	0.000	0.000	0.000	0.000
25	A	29	ASP	-1	-0.880	-0.926	29.092	-9.303	-9.303	0.000	0.000	0.000	0.000
26	A	30	THR	0	0.042	0.012	25.804	-0.252	-0.252	0.000	0.000	0.000	0.000
27	A	31	ASP	-1	-0.974	-0.995	26.705	-9.797	-9.797	0.000	0.000	0.000	0.000
28	A	32	ASP	-1	-0.973	-0.981	28.074	-9.572	-9.572	0.000	0.000	0.000	0.000
29	A	33	LEU	0	0.000	0.000	21.916	-0.305	-0.305	0.000	0.000	0.000	0.000
30	A	34	HIS	1	0.820	0.911	22.168	11.656	11.656	0.000	0.000	0.000	0.000
31	A	35	ASP	-1	-0.887	-0.939	21.246	-12.070	-12.070	0.000	0.000	0.000	0.000
32	A	36	ALA	0	0.045	0.029	20.106	-0.587	-0.587	0.000	0.000	0.000	0.000
33	A	37	ILE	0	0.055	0.031	17.256	-0.805	-0.805	0.000	0.000	0.000	0.000
34	A	38	HIS	0	-0.001	-0.002	16.274	-0.903	-0.903	0.000	0.000	0.000	0.000
35	A	39	MET	0	-0.021	-0.022	15.907	-0.555	-0.555	0.000	0.000	0.000	0.000
36	A	40	ALA	0	0.003	0.021	14.328	-0.666	-0.666	0.000	0.000	0.000	0.000
37	A	41	ALA	0	0.019	0.011	11.753	-1.503	-1.503	0.000	0.000	0.000	0.000
38	A	42	ASP	-1	-0.994	-1.006	11.041	-18.704	-18.704	0.000	0.000	0.000	0.000
39	A	43	ASN	0	-0.066	-0.041	11.739	-0.738	-0.738	0.000	0.000	0.000	0.000
40	A	44	ALA	0	0.001	0.017	8.161	-0.953	-0.953	0.000	0.000	0.000	0.000
41	A	45	VAL	0	-0.032	0.001	6.466	-3.870	-3.870	0.000	0.000	0.000	0.000
43	A	47	HIS	0	0.060	0.020	5.541	2.442	2.442	0.000	0.000	0.000	0.000
44	A	48	TYR	0	-0.066	-0.034	6.613	3.035	3.035	0.000	0.000	0.000	0.000
45	A	49	TYR	0	0.029	-0.002	6.994	-2.649	-2.649	0.000	0.000	0.000	0.000
46	A	50	ALA	0	-0.024	-0.008	6.681	-0.593	-0.593	0.000	0.000	0.000	0.000
49	A	53	PHE	0	-0.039	-0.036	6.241	1.514	1.514	0.000	0.000	0.000	0.000
53	A	57	ALA	0	-0.080	-0.025	6.517	3.608	3.608	0.000	0.000	0.000	0.000
54	A	58	SER	0	-0.098	-0.047	5.661	-1.291	-1.291	0.000	0.000	0.000	0.000
55	A	59	GLU	-1	-0.869	-0.950	7.777	-34.823	-34.823	0.000	0.000	0.000	0.000
56	A	60	GLY	0	0.016	-0.002	9.102	-1.490	-1.490	0.000	0.000	0.000	0.000
57	A	61	ILE	0	-0.036	0.005	8.293	0.846	0.846	0.000	0.000	0.000	0.000
58	A	62	ASP	-1	-0.883	-0.921	11.432	-20.207	-20.207	0.000	0.000	0.000	0.000
59	A	63	LEU	0	-0.075	-0.051	14.017	-0.605	-0.605	0.000	0.000	0.000	0.000
60	A	64	GLU	-1	-0.949	-0.987	15.580	-16.355	-16.355	0.000	0.000	0.000	0.000
61	A	65	PHE	0	-0.031	-0.023	16.349	-0.746	-0.746	0.000	0.000	0.000	0.000
62	A	66	GLU	-1	-0.937	-0.946	19.085	-12.870	-12.870	0.000	0.000	0.000	0.000
63	A	67	ASP	-1	-0.874	-0.945	20.973	-11.207	-11.207	0.000	0.000	0.000	0.000
64	A	68	SER	0	-0.057	-0.042	21.647	-0.412	-0.412	0.000	0.000	0.000	0.000
65	A	69	GLY	0	-0.067	-0.033	23.586	0.029	0.029	0.000	0.000	0.000	0.000
66	A	70	LEU	0	-0.007	-0.003	18.554	0.056	0.056	0.000	0.000	0.000	0.000
67	A	71	MET	0	-0.052	0.000	18.732	-0.948	-0.948	0.000	0.000	0.000	0.000
68	A	72	PRO	0	-0.067	-0.029	17.915	0.671	0.671	0.000	0.000	0.000	0.000
69	A	73	ASP	-1	-0.900	-0.948	21.015	-11.743	-11.743	0.000	0.000	0.000	0.000
70	A	74	THR	0	-0.010	-0.021	19.869	0.327	0.327	0.000	0.000	0.000	0.000
71	A	75	LYS	1	0.901	0.940	22.331	12.107	12.107	0.000	0.000	0.000	0.000
72	A	76	ASP	-1	-0.922	-0.956	17.959	-15.306	-15.306	0.000	0.000	0.000	0.000
73	A	77	VAL	0	0.031	0.001	14.996	-0.451	-0.451	0.000	0.000	0.000	0.000
74	A	78	ILE	0	0.000	0.001	10.218	-0.517	-0.517	0.000	0.000	0.000	0.000
75	A	79	ARG	1	0.934	0.973	12.893	16.026	16.026	0.000	0.000	0.000	0.000
76	A	80	ILE	0	0.018	0.022	14.896	-0.248	-0.248	0.000	0.000	0.000	0.000
77	A	81	LEU	0	0.013	0.002	10.827	-0.248	-0.248	0.000	0.000	0.000	0.000
78	A	82	GLN	0	-0.036	-0.024	9.326	0.589	0.589	0.000	0.000	0.000	0.000
79	A	83	ALA	0	0.001	0.003	11.106	-0.219	-0.219	0.000	0.000	0.000	0.000
80	A	84	ARG	1	0.804	0.898	12.735	19.405	19.405	0.000	0.000	0.000	0.000
81	A	85	ILE	0	0.006	-0.017	6.379	-0.777	-0.777	0.000	0.000	0.000	0.000
82	A	86	TYR	0	-0.041	-0.028	10.102	0.003	0.003	0.000	0.000	0.000	0.000
83	A	87	GLU	-1	-0.738	-0.864	12.257	-15.587	-15.587	0.000	0.000	0.000	0.000
84	A	88	GLN	0	-0.011	0.000	11.331	0.843	0.843	0.000	0.000	0.000	0.000
85	A	89	LEU	0	0.025	0.021	8.235	0.308	0.308	0.000	0.000	0.000	0.000
86	A	90	THR	0	-0.075	-0.056	12.236	1.241	1.241	0.000	0.000	0.000	0.000
87	A	91	ILE	0	-0.028	-0.008	15.720	0.930	0.930	0.000	0.000	0.000	0.000
88	A	92	ASP	-1	-0.720	-0.834	12.507	-20.144	-20.144	0.000	0.000	0.000	0.000
89	A	93	LEU	0	-0.014	-0.016	13.662	0.582	0.582	0.000	0.000	0.000	0.000
90	A	94	TRP	0	-0.070	-0.038	16.489	0.857	0.857	0.000	0.000	0.000	0.000
91	A	95	GLU	-1	-1.026	-0.998	18.605	-14.187	-14.187	0.000	0.000	0.000	0.000
92	A	96	ASP	-1	-0.838	-0.933	16.481	-15.985	-15.985	0.000	0.000	0.000	0.000
93	A	97	ALA	0	-0.061	-0.022	19.639	0.382	0.382	0.000	0.000	0.000	0.000
94	A	98	GLU	-1	-0.934	-0.976	21.949	-10.177	-10.177	0.000	0.000	0.000	0.000
95	A	99	ASP	-1	-0.935	-0.965	21.950	-12.007	-12.007	0.000	0.000	0.000	0.000
96	A	100	LEU	0	-0.024	-0.019	17.503	0.171	0.171	0.000	0.000	0.000	0.000
97	A	101	LEU	0	-0.021	0.001	21.979	0.201	0.201	0.000	0.000	0.000	0.000
98	A	102	ASN	0	-0.025	-0.013	25.453	0.565	0.565	0.000	0.000	0.000	0.000
99	A	103	GLU	-1	-0.877	-0.921	20.567	-13.207	-13.207	0.000	0.000	0.000	0.000
100	A	104	TYR	0	-0.071	-0.056	24.004	0.159	0.159	0.000	0.000	0.000	0.000
101	A	105	LEU	0	-0.056	-0.035	25.460	0.402	0.402	0.000	0.000	0.000	0.000
102	A	106	GLU	-1	-0.980	-0.987	28.058	-9.549	-9.549	0.000	0.000	0.000	0.000
103	A	107	GLU	-1	-0.870	-0.885	24.318	-11.191	-11.191	0.000	0.000	0.000	0.000
104	A	108	VAL	0	-0.103	-0.061	28.026	0.147	0.147	0.000	0.000	0.000	0.000
105	A	109	GLU	-1	-0.974	-0.988	31.680	-8.057	-8.057	0.000	0.000	0.000	0.000
106	A	110	GLU	-2	-2.004	-1.990	35.146	-14.533	-14.533	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:5:MET)