FMO DATABASE

FMODB ID: 97RY2

Calculation Name: 4EXR-A-Xray547

Preferred Name:

Target Type:

Ligand Name: phosphate ion

Ligand 3-letter code: PO4

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4EXR

Chain ID: A

ChEMBL ID:

UniProt ID: Q186H8

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	152
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1538188.497227
FMO2-HF: Nuclear repulsion	1475831.708153
FMO2-HF: Total energy	-62356.789074
FMO2-MP2: Total energy	-62538.972223

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:53:ASN)

Summations of interaction energy for fragment #1(A:53:ASN)

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.
-228.229	-221.04	14.705	-10.458	-11.433	-0.101

Interaction energy analysis for fragmet #1(A:53:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.766 / q_NPA : 0.878

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	55	ASN	0	0.053	0.046	2.753	5.328	10.756	0.754	-2.650	-3.531	-0.001
4	A	56	LEU	0	0.006	0.004	4.169	-7.929	-7.669	0.001	-0.033	-0.227	0.000
6	A	58	GLU	-1	-0.969	-0.979	1.817	-69.076	-72.689	12.356	-4.451	-4.292	-0.056
7	A	59	GLN	0	-0.050	-0.031	2.433	-41.192	-36.424	1.596	-3.244	-3.120	-0.044
36	A	88	ARG	1	0.837	0.921	4.782	44.011	44.132	-0.001	-0.018	-0.101	0.000
41	A	93	PHE	0	-0.001	-0.006	3.788	-3.359	-3.134	-0.001	-0.062	-0.162	0.000
5	A	57	MET	0	-0.011	-0.001	6.557	1.621	1.621	0.000	0.000	0.000	0.000
8	A	60	ASP	-1	-0.883	-0.936	5.711	-21.535	-21.535	0.000	0.000	0.000	0.000
9	A	61	PHE	0	-0.020	-0.015	7.603	-2.856	-2.856	0.000	0.000	0.000	0.000
10	A	62	LYS	1	0.884	0.942	11.447	27.722	27.722	0.000	0.000	0.000	0.000
11	A	63	VAL	0	-0.050	0.003	14.146	2.002	2.002	0.000	0.000	0.000	0.000
12	A	64	PRO	0	0.036	0.042	15.220	-1.177	-1.177	0.000	0.000	0.000	0.000
13	A	65	TYR	0	0.109	0.028	17.120	0.354	0.354	0.000	0.000	0.000	0.000
14	A	66	THR	0	0.024	0.012	18.445	0.478	0.478	0.000	0.000	0.000	0.000
15	A	67	ASP	-1	-0.852	-0.927	19.660	-14.553	-14.553	0.000	0.000	0.000	0.000
16	A	68	ALA	0	-0.009	0.004	18.438	0.533	0.533	0.000	0.000	0.000	0.000
17	A	69	ILE	0	0.025	0.012	20.586	0.641	0.641	0.000	0.000	0.000	0.000
18	A	70	ASN	0	-0.026	-0.025	23.708	0.857	0.857	0.000	0.000	0.000	0.000
19	A	71	ILE	0	-0.014	-0.009	21.140	0.506	0.506	0.000	0.000	0.000	0.000
20	A	72	PHE	0	0.027	0.023	24.235	0.459	0.459	0.000	0.000	0.000	0.000
21	A	73	LYS	1	0.986	0.989	25.951	11.739	11.739	0.000	0.000	0.000	0.000
22	A	74	ASP	-1	-0.966	-0.980	28.327	-10.040	-10.040	0.000	0.000	0.000	0.000
23	A	75	LYS	1	0.824	0.913	27.957	11.504	11.504	0.000	0.000	0.000	0.000
24	A	76	TYR	0	-0.047	-0.059	27.565	0.551	0.551	0.000	0.000	0.000	0.000
25	A	77	LYS	1	0.820	0.900	31.593	9.820	9.820	0.000	0.000	0.000	0.000
26	A	78	ASP	-1	-0.888	-0.922	33.935	-8.412	-8.412	0.000	0.000	0.000	0.000
27	A	79	ALA	0	-0.030	0.003	31.156	0.125	0.125	0.000	0.000	0.000	0.000
28	A	80	ASP	-1	-0.825	-0.907	31.651	-9.576	-9.576	0.000	0.000	0.000	0.000
29	A	81	ILE	0	-0.053	-0.038	25.176	-0.097	-0.097	0.000	0.000	0.000	0.000
30	A	82	VAL	0	-0.049	-0.027	27.560	0.273	0.273	0.000	0.000	0.000	0.000
31	A	83	ASP	-1	-0.796	-0.882	23.299	-12.730	-12.730	0.000	0.000	0.000	0.000
32	A	84	LEU	0	-0.071	-0.050	19.055	-0.107	-0.107	0.000	0.000	0.000	0.000
33	A	85	SER	0	0.027	0.017	16.597	0.009	0.009	0.000	0.000	0.000	0.000
34	A	86	LEU	0	-0.048	-0.021	10.992	-0.063	-0.063	0.000	0.000	0.000	0.000
35	A	87	GLU	-1	-0.829	-0.922	11.404	-21.579	-21.579	0.000	0.000	0.000	0.000
37	A	89	ASP	-1	-0.884	-0.931	8.803	-20.587	-20.587	0.000	0.000	0.000	0.000
38	A	90	LEU	0	0.012	-0.011	9.130	-1.025	-1.025	0.000	0.000	0.000	0.000
39	A	91	ASN	0	-0.073	-0.046	6.182	-8.860	-8.860	0.000	0.000	0.000	0.000
40	A	92	LYS	1	0.858	0.944	7.232	21.317	21.317	0.000	0.000	0.000	0.000
42	A	94	VAL	0	0.000	-0.002	9.257	1.906	1.906	0.000	0.000	0.000	0.000
43	A	95	TYR	0	-0.007	-0.020	12.970	-0.479	-0.479	0.000	0.000	0.000	0.000
44	A	96	THR	0	-0.007	0.004	15.795	0.628	0.628	0.000	0.000	0.000	0.000
45	A	97	VAL	0	-0.025	-0.017	18.549	0.045	0.045	0.000	0.000	0.000	0.000
46	A	98	GLU	-1	-0.838	-0.931	21.848	-13.543	-13.543	0.000	0.000	0.000	0.000
47	A	99	GLY	0	0.046	0.001	25.180	0.051	0.051	0.000	0.000	0.000	0.000
48	A	100	VAL	0	0.026	0.019	28.776	0.068	0.068	0.000	0.000	0.000	0.000
49	A	101	ASP	-1	-0.766	-0.852	32.484	-8.898	-8.898	0.000	0.000	0.000	0.000
50	A	102	ASP	-1	-0.857	-0.909	35.927	-8.087	-8.087	0.000	0.000	0.000	0.000
51	A	103	ASN	0	-0.110	-0.069	38.085	0.361	0.361	0.000	0.000	0.000	0.000
52	A	104	ASN	0	-0.029	-0.031	34.235	0.179	0.179	0.000	0.000	0.000	0.000
53	A	105	GLU	-1	-0.865	-0.923	29.808	-10.531	-10.531	0.000	0.000	0.000	0.000
54	A	106	TYR	0	-0.072	-0.079	28.872	0.112	0.112	0.000	0.000	0.000	0.000
55	A	107	LYS	1	0.919	0.973	22.063	13.563	13.563	0.000	0.000	0.000	0.000
56	A	108	MET	0	-0.082	-0.025	22.528	0.210	0.210	0.000	0.000	0.000	0.000
57	A	109	LYS	1	0.910	0.970	17.179	16.443	16.443	0.000	0.000	0.000	0.000
58	A	110	ILE	0	-0.002	-0.009	17.337	0.500	0.500	0.000	0.000	0.000	0.000
59	A	111	ASP	-1	-0.801	-0.884	12.549	-26.525	-26.525	0.000	0.000	0.000	0.000
60	A	112	ALA	0	0.030	-0.005	10.914	1.039	1.039	0.000	0.000	0.000	0.000
61	A	113	ASN	0	-0.071	-0.049	8.539	0.916	0.916	0.000	0.000	0.000	0.000
62	A	114	THR	0	-0.055	-0.074	12.434	0.823	0.823	0.000	0.000	0.000	0.000
63	A	115	LYS	1	0.849	0.934	15.291	17.601	17.601	0.000	0.000	0.000	0.000
64	A	116	ASP	-1	-0.868	-0.895	16.798	-17.257	-17.257	0.000	0.000	0.000	0.000
65	A	117	VAL	0	-0.004	-0.006	18.081	-0.602	-0.602	0.000	0.000	0.000	0.000
66	A	118	LEU	0	-0.068	-0.038	14.725	0.031	0.031	0.000	0.000	0.000	0.000
67	A	119	GLU	-1	-0.819	-0.919	19.274	-14.110	-14.110	0.000	0.000	0.000	0.000
68	A	120	ASP	-1	-0.803	-0.867	21.967	-12.074	-12.074	0.000	0.000	0.000	0.000
69	A	121	LYS	1	0.795	0.902	25.293	11.833	11.833	0.000	0.000	0.000	0.000
70	A	122	THR	0	0.007	-0.001	27.327	0.044	0.044	0.000	0.000	0.000	0.000
71	A	123	GLU	-1	-0.824	-0.901	29.564	-10.703	-10.703	0.000	0.000	0.000	0.000
72	A	124	LYS	1	0.872	0.956	32.712	8.111	8.111	0.000	0.000	0.000	0.000
73	A	125	LEU	0	0.035	0.023	33.949	-0.018	-0.018	0.000	0.000	0.000	0.000
74	A	126	ASP	-1	-0.873	-0.936	36.214	-8.498	-8.498	0.000	0.000	0.000	0.000
75	A	127	SER	0	-0.122	-0.109	38.469	0.015	0.015	0.000	0.000	0.000	0.000
76	A	128	GLU	-1	-0.924	-0.940	39.778	-7.345	-7.345	0.000	0.000	0.000	0.000
77	A	129	ASP	-1	-0.839	-0.924	35.660	-9.041	-9.041	0.000	0.000	0.000	0.000
78	A	130	LEU	0	-0.079	-0.021	38.563	-0.040	-0.040	0.000	0.000	0.000	0.000
79	A	131	ASN	0	-0.093	-0.059	40.742	0.131	0.131	0.000	0.000	0.000	0.000
80	A	132	GLY	0	0.051	0.025	39.523	0.144	0.144	0.000	0.000	0.000	0.000
81	A	133	VAL	0	-0.095	-0.030	38.818	-0.090	-0.090	0.000	0.000	0.000	0.000
82	A	134	ALA	0	0.139	0.062	34.269	-0.121	-0.121	0.000	0.000	0.000	0.000
83	A	135	ARG	1	0.725	0.831	34.308	8.426	8.426	0.000	0.000	0.000	0.000
84	A	136	LYS	1	0.848	0.927	35.333	8.074	8.074	0.000	0.000	0.000	0.000
85	A	137	GLU	-1	-0.825	-0.909	31.039	-10.029	-10.029	0.000	0.000	0.000	0.000
86	A	138	LYS	1	0.709	0.868	30.780	8.917	8.917	0.000	0.000	0.000	0.000
87	A	139	LEU	0	0.014	0.016	24.805	0.166	0.166	0.000	0.000	0.000	0.000
88	A	140	ASP	-1	-0.849	-0.921	28.925	-10.123	-10.123	0.000	0.000	0.000	0.000
89	A	141	LEU	0	-0.021	-0.022	24.221	-0.323	-0.323	0.000	0.000	0.000	0.000
90	A	142	ASN	0	-0.068	-0.031	26.969	-0.272	-0.272	0.000	0.000	0.000	0.000
91	A	143	ASP	-1	-0.956	-0.983	28.247	-10.218	-10.218	0.000	0.000	0.000	0.000
92	A	144	ILE	0	-0.046	-0.001	22.845	0.033	0.033	0.000	0.000	0.000	0.000
93	A	145	MET	0	-0.063	-0.005	20.620	-0.341	-0.341	0.000	0.000	0.000	0.000
94	A	146	THR	0	0.004	-0.016	17.702	-0.606	-0.606	0.000	0.000	0.000	0.000
95	A	147	PRO	0	0.058	0.018	14.789	0.053	0.053	0.000	0.000	0.000	0.000
96	A	148	GLN	0	-0.012	0.001	11.437	-1.601	-1.601	0.000	0.000	0.000	0.000
97	A	149	GLN	0	0.051	0.038	14.257	-0.083	-0.083	0.000	0.000	0.000	0.000
98	A	150	ALA	0	0.049	0.028	17.149	0.397	0.397	0.000	0.000	0.000	0.000
99	A	151	MET	0	-0.008	0.007	10.766	-0.417	-0.417	0.000	0.000	0.000	0.000
100	A	152	GLU	-1	-0.900	-0.955	13.455	-18.753	-18.753	0.000	0.000	0.000	0.000
101	A	153	ILE	0	-0.081	-0.040	14.514	0.620	0.620	0.000	0.000	0.000	0.000
102	A	154	ALA	0	0.028	0.015	15.038	0.480	0.480	0.000	0.000	0.000	0.000
103	A	155	LEU	0	0.002	0.004	9.449	0.288	0.288	0.000	0.000	0.000	0.000
104	A	156	LYS	1	0.842	0.916	13.916	14.367	14.367	0.000	0.000	0.000	0.000
105	A	157	GLU	-1	-0.936	-0.944	17.152	-12.040	-12.040	0.000	0.000	0.000	0.000
106	A	158	GLN	0	-0.062	-0.036	15.279	1.128	1.128	0.000	0.000	0.000	0.000
107	A	159	ASN	0	0.025	0.009	11.567	-1.952	-1.952	0.000	0.000	0.000	0.000
108	A	160	GLY	0	0.003	-0.020	10.865	1.242	1.242	0.000	0.000	0.000	0.000
109	A	161	ILE	0	-0.045	-0.010	4.882	-1.387	-1.387	0.000	0.000	0.000	0.000
110	A	162	VAL	0	0.036	0.017	7.462	1.482	1.482	0.000	0.000	0.000	0.000
111	A	163	LYS	1	0.868	0.946	6.151	26.586	26.586	0.000	0.000	0.000	0.000
112	A	164	GLU	-1	-0.878	-0.937	9.555	-21.026	-21.026	0.000	0.000	0.000	0.000
113	A	165	TRP	0	-0.050	-0.033	12.602	1.236	1.236	0.000	0.000	0.000	0.000
114	A	166	SER	0	0.074	0.010	15.064	-0.025	-0.025	0.000	0.000	0.000	0.000
115	A	167	LEU	0	-0.139	-0.068	18.561	0.133	0.133	0.000	0.000	0.000	0.000
116	A	168	ASP	-1	-0.771	-0.885	21.796	-12.475	-12.475	0.000	0.000	0.000	0.000
117	A	169	LYS	1	0.786	0.890	24.922	10.023	10.023	0.000	0.000	0.000	0.000
118	A	170	ASP	-1	-0.837	-0.904	28.552	-9.874	-9.874	0.000	0.000	0.000	0.000
119	A	171	LEU	0	-0.097	-0.062	30.785	0.099	0.099	0.000	0.000	0.000	0.000
120	A	172	ASP	-1	-0.941	-0.974	33.606	-8.958	-8.958	0.000	0.000	0.000	0.000
121	A	173	VAL	0	-0.056	-0.017	28.350	-0.073	-0.073	0.000	0.000	0.000	0.000
122	A	174	THR	0	0.056	0.032	25.923	-0.227	-0.227	0.000	0.000	0.000	0.000
123	A	175	PHE	0	-0.030	-0.022	22.954	0.017	0.017	0.000	0.000	0.000	0.000
124	A	176	TYR	0	0.018	-0.012	18.462	-0.491	-0.491	0.000	0.000	0.000	0.000
125	A	177	LYS	1	0.869	0.941	19.051	15.787	15.787	0.000	0.000	0.000	0.000
126	A	178	ILE	0	-0.021	-0.017	13.368	-0.976	-0.976	0.000	0.000	0.000	0.000
127	A	179	ARG	1	0.773	0.841	12.989	18.256	18.256	0.000	0.000	0.000	0.000
128	A	180	ILE	0	-0.047	-0.034	11.036	-2.150	-2.150	0.000	0.000	0.000	0.000
129	A	181	ASP	-1	-0.788	-0.903	10.141	-21.701	-21.701	0.000	0.000	0.000	0.000
130	A	182	LYS	1	0.845	0.902	11.299	16.207	16.207	0.000	0.000	0.000	0.000
131	A	183	ASP	-1	-0.851	-0.917	13.155	-14.224	-14.224	0.000	0.000	0.000	0.000
132	A	184	LYS	1	0.774	0.865	14.149	14.314	14.314	0.000	0.000	0.000	0.000
133	A	185	ASN	0	-0.029	0.001	16.004	0.811	0.811	0.000	0.000	0.000	0.000
134	A	186	GLU	-1	-0.786	-0.862	14.031	-20.073	-20.073	0.000	0.000	0.000	0.000
135	A	187	TYR	0	-0.029	-0.025	15.666	1.260	1.260	0.000	0.000	0.000	0.000
136	A	188	ASP	-1	-0.754	-0.847	16.318	-17.154	-17.154	0.000	0.000	0.000	0.000
137	A	189	ILE	0	-0.053	-0.028	16.735	0.956	0.956	0.000	0.000	0.000	0.000
138	A	190	LYS	1	0.932	0.980	19.140	11.936	11.936	0.000	0.000	0.000	0.000
139	A	191	VAL	0	-0.005	-0.007	19.359	0.432	0.432	0.000	0.000	0.000	0.000
140	A	192	ASP	-1	-0.770	-0.873	22.413	-10.997	-10.997	0.000	0.000	0.000	0.000
141	A	193	SER	0	-0.007	-0.020	23.465	-0.128	-0.128	0.000	0.000	0.000	0.000
142	A	194	LYS	1	0.865	0.922	24.502	10.355	10.355	0.000	0.000	0.000	0.000
143	A	195	LYS	1	0.811	0.888	26.984	10.119	10.119	0.000	0.000	0.000	0.000
144	A	196	GLY	0	0.015	0.002	23.077	0.050	0.050	0.000	0.000	0.000	0.000
145	A	197	THR	0	-0.057	-0.034	23.426	-0.107	-0.107	0.000	0.000	0.000	0.000
146	A	198	VAL	0	0.031	0.021	21.362	-0.191	-0.191	0.000	0.000	0.000	0.000
147	A	199	LEU	0	-0.045	-0.022	24.003	0.526	0.526	0.000	0.000	0.000	0.000
148	A	200	LYS	1	0.781	0.879	24.265	11.743	11.743	0.000	0.000	0.000	0.000
149	A	201	VAL	0	0.025	0.030	20.564	-0.614	-0.614	0.000	0.000	0.000	0.000
150	A	202	GLU	-1	-0.835	-0.911	21.553	-11.110	-11.110	0.000	0.000	0.000	0.000
151	A	203	LYS	1	0.767	0.874	19.911	12.959	12.959	0.000	0.000	0.000	0.000
152	A	204	GLU	-2	-1.662	-1.790	19.032	-28.877	-28.877	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:53:ASN)