FMO DATABASE

FMODB ID: 978V2

Calculation Name: 3K1S-G-Xray547

Preferred Name:

Target Type:

Ligand Name: magnesium ion | chloride ion

Ligand 3-letter code: MG | CL

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3K1S

Chain ID: G

ChEMBL ID:

UniProt ID: A0A6H3A5D1

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	106
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-748426.89641
FMO2-HF: Nuclear repulsion	706223.36189
FMO2-HF: Total energy	-42203.534519
FMO2-MP2: Total energy	-42323.829098

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.
-90.315	-88.834	-0.018	-0.677	-0.785	-0.002

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 : 0.835 / q_NPA : 0.894

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	THR	0	0.000	-0.002	3.838	-2.388	-0.907	-0.018	-0.677	-0.785	-0.002
4	A	4	THR	0	0.033	-0.007	6.515	0.619	0.619	0.000	0.000	0.000	0.000
5	A	5	ALA	0	0.069	0.038	9.571	1.843	1.843	0.000	0.000	0.000	0.000
6	A	6	GLU	-1	-0.815	-0.905	6.191	-46.056	-46.056	0.000	0.000	0.000	0.000
7	A	7	GLN	0	-0.047	-0.035	7.320	2.733	2.733	0.000	0.000	0.000	0.000
8	A	8	ILE	0	0.035	0.038	10.131	1.799	1.799	0.000	0.000	0.000	0.000
9	A	9	PRO	0	0.004	-0.007	11.956	1.445	1.445	0.000	0.000	0.000	0.000
10	A	10	PHE	0	-0.006	-0.009	8.563	1.167	1.167	0.000	0.000	0.000	0.000
11	A	11	GLN	0	0.017	0.014	13.084	2.298	2.298	0.000	0.000	0.000	0.000
12	A	12	LEU	0	0.006	0.016	15.551	1.191	1.191	0.000	0.000	0.000	0.000
13	A	13	ILE	0	-0.008	0.011	15.658	1.091	1.091	0.000	0.000	0.000	0.000
14	A	14	LEU	0	-0.024	0.003	16.454	0.870	0.870	0.000	0.000	0.000	0.000
15	A	15	ASN	0	-0.020	-0.014	18.753	1.333	1.333	0.000	0.000	0.000	0.000
16	A	16	SER	0	0.019	-0.011	21.316	0.912	0.912	0.000	0.000	0.000	0.000
17	A	17	GLY	0	-0.033	-0.015	21.949	0.658	0.658	0.000	0.000	0.000	0.000
18	A	18	ASN	0	-0.008	0.006	21.618	0.722	0.722	0.000	0.000	0.000	0.000
19	A	19	ALA	0	0.026	0.013	24.871	0.538	0.538	0.000	0.000	0.000	0.000
20	A	20	ARG	1	0.958	0.975	24.748	12.046	12.046	0.000	0.000	0.000	0.000
21	A	21	SER	0	-0.057	-0.026	26.394	0.414	0.414	0.000	0.000	0.000	0.000
22	A	22	PHE	0	0.034	0.012	27.031	0.331	0.331	0.000	0.000	0.000	0.000
23	A	23	ALA	0	0.030	0.016	31.020	0.385	0.385	0.000	0.000	0.000	0.000
24	A	24	MET	0	-0.015	-0.010	32.165	0.415	0.415	0.000	0.000	0.000	0.000
25	A	25	GLU	-1	-0.915	-0.966	30.564	-9.748	-9.748	0.000	0.000	0.000	0.000
26	A	26	ALA	0	0.012	0.011	34.816	0.304	0.304	0.000	0.000	0.000	0.000
27	A	27	LEU	0	-0.019	0.002	36.789	0.282	0.282	0.000	0.000	0.000	0.000
28	A	28	GLN	0	-0.033	-0.018	36.715	0.483	0.483	0.000	0.000	0.000	0.000
29	A	29	PHE	0	-0.003	-0.007	36.111	0.213	0.213	0.000	0.000	0.000	0.000
30	A	30	ALA	0	0.055	0.013	40.793	0.207	0.207	0.000	0.000	0.000	0.000
31	A	31	LYS	1	0.826	0.919	40.642	7.821	7.821	0.000	0.000	0.000	0.000
32	A	32	GLN	0	-0.083	-0.040	40.421	0.180	0.180	0.000	0.000	0.000	0.000
33	A	33	GLY	0	0.116	0.069	45.237	0.097	0.097	0.000	0.000	0.000	0.000
34	A	34	LYS	1	0.791	0.912	41.941	7.472	7.472	0.000	0.000	0.000	0.000
35	A	35	MET	0	0.008	0.001	42.660	-0.301	-0.301	0.000	0.000	0.000	0.000
36	A	36	ALA	0	-0.001	0.015	42.855	-0.110	-0.110	0.000	0.000	0.000	0.000
37	A	37	GLU	-1	-0.813	-0.924	39.219	-7.605	-7.605	0.000	0.000	0.000	0.000
38	A	38	ALA	0	-0.007	0.001	38.128	-0.284	-0.284	0.000	0.000	0.000	0.000
39	A	39	ASP	-1	-0.832	-0.892	38.075	-7.782	-7.782	0.000	0.000	0.000	0.000
40	A	40	GLU	-1	-0.884	-0.938	36.059	-9.003	-9.003	0.000	0.000	0.000	0.000
41	A	41	ALA	0	-0.021	-0.009	34.061	-0.329	-0.329	0.000	0.000	0.000	0.000
42	A	42	MET	0	0.011	-0.001	33.350	-0.429	-0.429	0.000	0.000	0.000	0.000
43	A	43	VAL	0	-0.045	-0.014	33.748	-0.198	-0.198	0.000	0.000	0.000	0.000
44	A	44	LYS	1	0.849	0.922	30.279	9.088	9.088	0.000	0.000	0.000	0.000
45	A	45	ALA	0	0.022	0.004	29.259	-0.439	-0.439	0.000	0.000	0.000	0.000
46	A	46	LYS	1	0.901	0.952	29.428	9.074	9.074	0.000	0.000	0.000	0.000
47	A	47	GLU	-1	-0.862	-0.948	28.215	-11.003	-11.003	0.000	0.000	0.000	0.000
48	A	48	ALA	0	-0.015	0.014	25.126	-0.488	-0.488	0.000	0.000	0.000	0.000
49	A	49	ILE	0	0.001	-0.011	24.514	-0.523	-0.523	0.000	0.000	0.000	0.000
50	A	50	ASN	0	-0.063	-0.019	25.709	-0.260	-0.260	0.000	0.000	0.000	0.000
51	A	51	GLU	-1	-0.872	-0.948	21.149	-15.087	-15.087	0.000	0.000	0.000	0.000
52	A	52	ALA	0	-0.038	-0.021	21.027	-0.769	-0.769	0.000	0.000	0.000	0.000
53	A	53	HIS	0	0.040	-0.001	21.581	-0.794	-0.794	0.000	0.000	0.000	0.000
54	A	54	HIS	0	-0.034	0.021	17.945	-0.200	-0.200	0.000	0.000	0.000	0.000
55	A	55	PHE	0	0.009	-0.009	15.320	-0.769	-0.769	0.000	0.000	0.000	0.000
56	A	56	GLN	0	0.038	0.016	18.987	-1.070	-1.070	0.000	0.000	0.000	0.000
57	A	57	THR	0	-0.046	-0.039	21.342	0.292	0.292	0.000	0.000	0.000	0.000
58	A	58	GLU	-1	-0.798	-0.868	16.849	-17.583	-17.583	0.000	0.000	0.000	0.000
59	A	59	LEU	0	-0.030	-0.006	16.713	-0.427	-0.427	0.000	0.000	0.000	0.000
60	A	60	ILE	0	0.006	0.006	19.119	0.036	0.036	0.000	0.000	0.000	0.000
61	A	61	GLN	0	-0.008	-0.002	21.807	0.641	0.641	0.000	0.000	0.000	0.000
62	A	62	SER	0	-0.029	-0.026	17.334	-0.016	-0.016	0.000	0.000	0.000	0.000
63	A	63	GLU	-1	-0.948	-0.970	19.417	-14.329	-14.329	0.000	0.000	0.000	0.000
64	A	64	ALA	0	-0.042	-0.017	21.398	0.531	0.531	0.000	0.000	0.000	0.000
65	A	65	ARG	1	0.641	0.759	17.465	17.565	17.565	0.000	0.000	0.000	0.000
66	A	66	GLY	0	-0.016	0.005	22.318	0.181	0.181	0.000	0.000	0.000	0.000
67	A	67	GLU	-1	-0.887	-0.910	16.579	-18.611	-18.611	0.000	0.000	0.000	0.000
68	A	68	LYS	1	0.923	0.956	17.233	16.242	16.242	0.000	0.000	0.000	0.000
69	A	69	THR	0	0.044	0.026	14.664	-1.780	-1.780	0.000	0.000	0.000	0.000
70	A	70	GLU	-1	-0.932	-0.966	12.608	-17.831	-17.831	0.000	0.000	0.000	0.000
71	A	71	ILE	0	-0.032	-0.017	14.339	-0.383	-0.383	0.000	0.000	0.000	0.000
72	A	72	SER	0	0.032	0.005	12.860	-0.223	-0.223	0.000	0.000	0.000	0.000
73	A	73	VAL	0	0.039	0.006	14.932	0.496	0.496	0.000	0.000	0.000	0.000
74	A	74	LEU	0	-0.009	0.001	11.161	0.724	0.724	0.000	0.000	0.000	0.000
75	A	75	LEU	0	0.043	0.020	14.634	0.281	0.281	0.000	0.000	0.000	0.000
76	A	76	ILE	0	0.003	0.005	16.004	0.625	0.625	0.000	0.000	0.000	0.000
77	A	77	HIS	0	0.054	0.033	17.475	1.081	1.081	0.000	0.000	0.000	0.000
78	A	78	ALA	0	-0.027	-0.015	16.716	0.489	0.489	0.000	0.000	0.000	0.000
79	A	79	GLN	0	-0.003	0.010	18.844	0.805	0.805	0.000	0.000	0.000	0.000
80	A	80	ASP	-1	-0.882	-0.944	21.818	-12.227	-12.227	0.000	0.000	0.000	0.000
81	A	81	HIS	0	-0.070	-0.065	20.464	0.933	0.933	0.000	0.000	0.000	0.000
82	A	82	LEU	0	0.034	0.038	22.490	0.463	0.463	0.000	0.000	0.000	0.000
83	A	83	MET	0	0.018	0.002	24.247	0.453	0.453	0.000	0.000	0.000	0.000
84	A	84	ASN	0	-0.017	0.007	26.361	0.863	0.863	0.000	0.000	0.000	0.000
85	A	85	ALA	0	-0.020	-0.004	26.052	0.412	0.412	0.000	0.000	0.000	0.000
86	A	86	ILE	0	-0.002	-0.003	27.310	0.335	0.335	0.000	0.000	0.000	0.000
87	A	87	THR	0	0.015	-0.001	30.112	0.418	0.418	0.000	0.000	0.000	0.000
88	A	88	VAL	0	-0.044	-0.028	31.000	0.330	0.330	0.000	0.000	0.000	0.000
89	A	89	LYS	1	0.914	0.965	31.232	9.784	9.784	0.000	0.000	0.000	0.000
90	A	90	GLU	-1	-0.962	-0.976	33.341	-8.566	-8.566	0.000	0.000	0.000	0.000
91	A	91	LEU	0	0.032	0.001	36.003	0.272	0.272	0.000	0.000	0.000	0.000
92	A	92	ALA	0	-0.026	-0.012	35.699	0.237	0.237	0.000	0.000	0.000	0.000
93	A	93	ALA	0	-0.013	-0.001	37.579	0.180	0.180	0.000	0.000	0.000	0.000
94	A	94	GLU	-1	-0.874	-0.932	39.541	-7.284	-7.284	0.000	0.000	0.000	0.000
95	A	95	PHE	0	-0.058	-0.037	39.305	0.227	0.227	0.000	0.000	0.000	0.000
96	A	96	ILE	0	-0.017	-0.014	38.241	0.186	0.186	0.000	0.000	0.000	0.000
97	A	97	ASP	-1	-0.926	-0.955	42.650	-6.764	-6.764	0.000	0.000	0.000	0.000
98	A	98	LEU	0	-0.016	-0.009	45.348	0.228	0.228	0.000	0.000	0.000	0.000
99	A	99	TYR	0	-0.005	-0.023	43.031	0.110	0.110	0.000	0.000	0.000	0.000
100	A	100	LYS	1	0.891	0.920	43.502	7.428	7.428	0.000	0.000	0.000	0.000
101	A	101	LYS	1	0.933	0.966	48.582	6.240	6.240	0.000	0.000	0.000	0.000
102	A	102	LEU	0	-0.109	-0.056	49.181	0.169	0.169	0.000	0.000	0.000	0.000
103	A	103	GLU	-1	-0.856	-0.941	49.179	-6.392	-6.392	0.000	0.000	0.000	0.000
104	A	104	ALA	0	-0.084	-0.024	52.524	0.100	0.100	0.000	0.000	0.000	0.000
105	A	105	LYS	1	0.853	0.916	54.753	5.661	5.661	0.000	0.000	0.000	0.000
106	A	106	GLY	-1	-0.910	-0.932	56.874	-5.313	-5.313	0.000	0.000	0.000	0.000

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