FMO DATABASE

FMODB ID: MZKZZ

Calculation Name: 2ETS-A-Xray549

Preferred Name:

Target Type:

Ligand Name: phosphate ion | chloride ion

Ligand 3-letter code: PO4 | CL

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2ETS

Chain ID: A

ChEMBL ID:

UniProt ID: A0A0H3

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	115
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1045047.741623
FMO2-HF: Nuclear repulsion	996294.285595
FMO2-HF: Total energy	-48753.456027
FMO2-MP2: Total energy	-48895.980582

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:-4:HIS)

Summations of interaction energy for fragment #1(A:-4:HIS)

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.
-191.72	-192.279	28.351	-15.131	-12.66	-0.168

Interaction energy analysis for fragmet #1(A:-4:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 2 / q_Mulliken : 1.699 / q_NPA : 1.855

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	-2	HIS	0	0.068	0.027	3.889	-2.541	-0.720	-0.014	-0.779	-1.028	-0.002
6	A	1	MET	0	0.011	0.010	1.961	-20.960	-29.317	19.711	-6.568	-4.786	-0.071
57	A	52	HIS	1	0.741	0.850	3.647	72.276	73.097	0.008	-0.315	-0.514	-0.003
58	A	53	ARG	1	0.966	0.986	4.521	38.642	38.754	-0.001	-0.013	-0.098	0.000
60	A	55	PHE	0	0.009	-0.022	1.850	-37.827	-33.284	8.647	-7.135	-6.054	-0.090
61	A	56	ILE	0	0.036	0.019	3.820	6.311	6.812	0.000	-0.321	-0.180	-0.002
4	A	-1	HIS	1	0.904	0.965	5.878	57.307	57.307	0.000	0.000	0.000	0.000
5	A	0	HIS	0	0.043	0.032	6.522	-5.892	-5.892	0.000	0.000	0.000	0.000
7	A	2	ASN	0	-0.001	0.012	6.239	7.369	7.369	0.000	0.000	0.000	0.000
8	A	3	ASP	-1	-0.824	-0.913	9.117	-43.084	-43.084	0.000	0.000	0.000	0.000
9	A	4	LEU	0	-0.028	-0.017	7.508	2.617	2.617	0.000	0.000	0.000	0.000
10	A	5	VAL	0	0.005	0.008	8.849	3.348	3.348	0.000	0.000	0.000	0.000
11	A	6	GLU	0	0.016	0.007	11.426	4.283	4.283	0.000	0.000	0.000	0.000
12	A	7	SER	0	-0.029	-0.006	13.895	3.476	3.476	0.000	0.000	0.000	0.000
13	A	8	LEU	0	0.034	0.009	12.275	2.258	2.258	0.000	0.000	0.000	0.000
14	A	9	ILE	0	-0.002	0.004	14.851	2.191	2.191	0.000	0.000	0.000	0.000
15	A	10	TYR	0	-0.046	-0.014	17.526	2.224	2.224	0.000	0.000	0.000	0.000
16	A	11	GLU	-1	-0.717	-0.846	18.841	-24.753	-24.753	0.000	0.000	0.000	0.000
17	A	12	VAL	0	0.006	0.004	18.722	1.456	1.456	0.000	0.000	0.000	0.000
18	A	13	ASN	0	0.005	-0.005	21.239	1.674	1.674	0.000	0.000	0.000	0.000
19	A	14	ASN	0	-0.055	-0.024	23.240	2.098	2.098	0.000	0.000	0.000	0.000
20	A	15	MET	0	-0.010	0.007	20.483	1.221	1.221	0.000	0.000	0.000	0.000
21	A	16	GLN	0	0.012	-0.002	25.618	0.444	0.444	0.000	0.000	0.000	0.000
22	A	17	GLN	0	0.007	-0.007	27.646	1.013	1.013	0.000	0.000	0.000	0.000
23	A	18	ASN	0	-0.065	-0.034	27.742	1.178	1.178	0.000	0.000	0.000	0.000
24	A	19	PHE	0	0.049	0.023	29.778	0.879	0.879	0.000	0.000	0.000	0.000
25	A	20	GLU	-1	-0.764	-0.845	31.540	-17.143	-17.143	0.000	0.000	0.000	0.000
26	A	21	ASN	0	-0.016	0.020	33.290	0.850	0.850	0.000	0.000	0.000	0.000
27	A	22	VAL	0	0.001	0.013	33.595	0.566	0.566	0.000	0.000	0.000	0.000
28	A	23	LYS	1	0.775	0.882	35.425	17.049	17.049	0.000	0.000	0.000	0.000
29	A	24	SER	0	-0.057	-0.035	37.439	0.545	0.545	0.000	0.000	0.000	0.000
30	A	25	GLN	0	0.007	-0.010	37.622	0.124	0.124	0.000	0.000	0.000	0.000
31	A	26	GLN	0	-0.045	-0.017	40.288	0.429	0.429	0.000	0.000	0.000	0.000
32	A	27	GLN	0	-0.023	-0.017	39.832	0.463	0.463	0.000	0.000	0.000	0.000
33	A	28	ASP	-1	-0.755	-0.855	36.425	-16.375	-16.375	0.000	0.000	0.000	0.000
34	A	29	HIS	0	0.045	0.034	32.398	-0.135	-0.135	0.000	0.000	0.000	0.000
35	A	30	ASP	-1	-0.809	-0.905	35.093	-16.724	-16.724	0.000	0.000	0.000	0.000
36	A	31	PHE	0	0.005	-0.002	30.887	-0.570	-0.570	0.000	0.000	0.000	0.000
37	A	32	TYR	0	0.012	-0.003	31.992	-0.710	-0.710	0.000	0.000	0.000	0.000
38	A	33	GLN	0	-0.011	-0.012	32.428	-0.432	-0.432	0.000	0.000	0.000	0.000
39	A	34	THR	0	-0.024	-0.007	30.318	-0.227	-0.227	0.000	0.000	0.000	0.000
40	A	35	VAL	0	-0.032	-0.016	28.881	-0.739	-0.739	0.000	0.000	0.000	0.000
41	A	36	LYS	1	0.851	0.937	27.464	20.184	20.184	0.000	0.000	0.000	0.000
42	A	37	PRO	0	0.015	0.004	26.330	-0.808	-0.808	0.000	0.000	0.000	0.000
43	A	38	TYR	0	-0.038	-0.035	22.897	-0.715	-0.715	0.000	0.000	0.000	0.000
44	A	39	THR	0	-0.031	-0.034	23.066	-0.956	-0.956	0.000	0.000	0.000	0.000
45	A	40	GLU	-1	-0.788	-0.882	21.660	-23.468	-23.468	0.000	0.000	0.000	0.000
46	A	41	HIS	0	-0.067	-0.034	20.040	-1.477	-1.477	0.000	0.000	0.000	0.000
47	A	42	ILE	0	-0.013	-0.014	18.354	-1.810	-1.810	0.000	0.000	0.000	0.000
48	A	43	ASP	-1	-0.866	-0.947	17.030	-29.962	-29.962	0.000	0.000	0.000	0.000
49	A	44	SER	0	-0.055	-0.018	16.281	-2.375	-2.375	0.000	0.000	0.000	0.000
50	A	45	ILE	0	0.030	0.017	13.365	-2.814	-2.814	0.000	0.000	0.000	0.000
51	A	46	LEU	0	-0.008	-0.014	12.243	-4.016	-4.016	0.000	0.000	0.000	0.000
52	A	47	ASN	0	-0.009	-0.008	12.391	-2.828	-2.828	0.000	0.000	0.000	0.000
53	A	48	GLU	-1	-0.879	-0.941	9.739	-49.620	-49.620	0.000	0.000	0.000	0.000
54	A	49	ILE	0	-0.048	-0.023	7.835	-7.954	-7.954	0.000	0.000	0.000	0.000
55	A	50	LYS	1	0.901	0.959	7.832	30.065	30.065	0.000	0.000	0.000	0.000
56	A	51	LEU	0	-0.018	0.008	7.595	-2.976	-2.976	0.000	0.000	0.000	0.000
59	A	54	GLU	-1	-0.879	-0.940	5.595	-65.971	-65.971	0.000	0.000	0.000	0.000
62	A	57	ILE	0	-0.079	-0.043	6.528	7.711	7.711	0.000	0.000	0.000	0.000
63	A	58	GLU	-1	-0.907	-0.951	7.481	-48.360	-48.360	0.000	0.000	0.000	0.000
64	A	59	VAL	0	-0.038	0.011	7.237	1.276	1.276	0.000	0.000	0.000	0.000
65	A	60	PRO	0	0.042	0.000	9.848	3.631	3.631	0.000	0.000	0.000	0.000
66	A	61	TYR	0	-0.027	-0.015	13.379	0.152	0.152	0.000	0.000	0.000	0.000
67	A	62	MET	0	-0.060	0.003	10.998	2.107	2.107	0.000	0.000	0.000	0.000
68	A	63	ASN	0	0.073	0.027	12.821	1.893	1.893	0.000	0.000	0.000	0.000
69	A	64	SER	0	0.066	0.027	12.775	-0.548	-0.548	0.000	0.000	0.000	0.000
70	A	65	ARG	1	0.936	0.975	13.701	27.890	27.890	0.000	0.000	0.000	0.000
71	A	66	LYS	1	0.785	0.866	15.037	33.306	33.306	0.000	0.000	0.000	0.000
72	A	67	PHE	0	0.066	0.034	9.089	0.205	0.205	0.000	0.000	0.000	0.000
73	A	68	GLU	-1	-0.860	-0.945	13.341	-38.387	-38.387	0.000	0.000	0.000	0.000
74	A	69	LEU	0	-0.046	-0.027	15.964	1.746	1.746	0.000	0.000	0.000	0.000
75	A	70	LEU	0	0.002	0.015	12.957	1.514	1.514	0.000	0.000	0.000	0.000
76	A	71	ILE	0	0.001	-0.003	12.362	0.777	0.777	0.000	0.000	0.000	0.000
77	A	72	ALA	0	0.033	0.024	16.344	1.337	1.337	0.000	0.000	0.000	0.000
78	A	73	ASN	0	-0.032	-0.028	19.691	2.523	2.523	0.000	0.000	0.000	0.000
79	A	74	ILE	0	0.021	0.013	15.513	1.245	1.245	0.000	0.000	0.000	0.000
80	A	75	GLU	-1	-0.813	-0.904	18.357	-29.353	-29.353	0.000	0.000	0.000	0.000
81	A	76	GLN	0	-0.053	-0.018	21.088	0.785	0.785	0.000	0.000	0.000	0.000
82	A	77	LEU	0	-0.022	-0.015	21.526	1.210	1.210	0.000	0.000	0.000	0.000
83	A	78	SER	0	0.016	-0.010	22.045	1.039	1.039	0.000	0.000	0.000	0.000
84	A	79	VAL	0	0.038	0.012	24.171	0.892	0.892	0.000	0.000	0.000	0.000
85	A	80	GLU	-1	-0.819	-0.913	27.362	-20.319	-20.319	0.000	0.000	0.000	0.000
86	A	81	CYS	0	-0.100	-0.025	26.486	0.843	0.843	0.000	0.000	0.000	0.000
87	A	82	HIS	1	0.850	0.920	26.998	21.156	21.156	0.000	0.000	0.000	0.000
88	A	83	PHE	0	0.007	0.009	31.496	0.708	0.708	0.000	0.000	0.000	0.000
89	A	84	LYS	1	0.933	0.983	34.428	14.364	14.364	0.000	0.000	0.000	0.000
90	A	85	ARG	1	0.798	0.872	36.692	16.300	16.300	0.000	0.000	0.000	0.000
91	A	86	THR	0	-0.003	0.003	31.002	0.186	0.186	0.000	0.000	0.000	0.000
92	A	87	SER	0	0.011	-0.001	33.875	0.366	0.366	0.000	0.000	0.000	0.000
93	A	88	ARG	1	0.842	0.864	32.811	16.733	16.733	0.000	0.000	0.000	0.000
94	A	89	LYS	1	0.910	0.958	32.400	17.487	17.487	0.000	0.000	0.000	0.000
95	A	90	LEU	0	0.028	0.005	30.828	-0.362	-0.362	0.000	0.000	0.000	0.000
96	A	91	PHE	0	0.027	0.022	27.046	-0.645	-0.645	0.000	0.000	0.000	0.000
97	A	92	ILE	0	0.017	0.003	27.285	-0.747	-0.747	0.000	0.000	0.000	0.000
98	A	93	GLU	-1	-0.938	-0.966	27.215	-19.964	-19.964	0.000	0.000	0.000	0.000
99	A	94	LYS	1	0.857	0.924	23.680	21.550	21.550	0.000	0.000	0.000	0.000
100	A	95	LEU	0	0.011	0.013	23.085	-1.042	-1.042	0.000	0.000	0.000	0.000
101	A	96	LYS	1	0.932	0.968	22.514	20.216	20.216	0.000	0.000	0.000	0.000
102	A	97	SER	0	-0.037	-0.006	22.042	-1.192	-1.192	0.000	0.000	0.000	0.000
103	A	98	VAL	0	0.044	0.016	17.920	-1.203	-1.203	0.000	0.000	0.000	0.000
104	A	99	GLN	0	-0.006	-0.014	17.740	-1.077	-1.077	0.000	0.000	0.000	0.000
105	A	100	TYR	0	-0.021	0.004	18.239	-1.180	-1.180	0.000	0.000	0.000	0.000
106	A	101	ASP	-1	-0.759	-0.866	15.482	-33.633	-33.633	0.000	0.000	0.000	0.000
107	A	102	LEU	0	-0.016	-0.015	13.104	-2.768	-2.768	0.000	0.000	0.000	0.000
108	A	103	GLN	0	0.001	0.002	13.459	-1.757	-1.757	0.000	0.000	0.000	0.000
109	A	104	ASN	0	0.012	0.003	14.176	-1.051	-1.051	0.000	0.000	0.000	0.000
110	A	105	ILE	0	-0.033	-0.022	8.381	-2.718	-2.718	0.000	0.000	0.000	0.000
111	A	106	LEU	0	-0.030	-0.022	9.633	-4.187	-4.187	0.000	0.000	0.000	0.000
112	A	107	ASP	-1	-0.898	-0.954	10.917	-38.309	-38.309	0.000	0.000	0.000	0.000
113	A	108	GLY	0	-0.038	-0.013	9.955	-0.385	-0.385	0.000	0.000	0.000	0.000
114	A	109	VAL	0	-0.121	-0.070	5.757	-9.120	-9.120	0.000	0.000	0.000	0.000
115	A	110	THR	-1	-0.928	-0.943	7.407	-51.239	-51.239	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-4:HIS)