FMO DATABASE

FMODB ID: KKQK3

Calculation Name: 1EAJ-A-Xray547

Preferred Name:

Target Type:

Ligand Name: sulfate ion

Ligand 3-letter code: SO4

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1EAJ

Chain ID: A

ChEMBL ID:

UniProt ID: P78310

Base Structure: X-ray

Registration Date: 2025-09-02

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	123
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1038952.025403
FMO2-HF: Nuclear repulsion	990861.48852
FMO2-HF: Total energy	-48090.536883
FMO2-MP2: Total energy	-48231.805955

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:16:PHE)

Summations of interaction energy for fragment #1(A:16:PHE)

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.
-84.044	-74.098	10.473	-6.942	-13.476	-0.056

Interaction energy analysis for fragmet #1(A:16:PHE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.821 / q_NPA : 0.908

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	18	ARG	1	0.947	0.948	2.924	23.956	26.424	0.232	-1.323	-1.377	-0.008
29	A	44	THR	0	-0.050	-0.035	3.403	-4.584	-4.215	0.034	-0.118	-0.285	-0.001
30	A	45	LEU	0	0.034	0.026	3.135	1.861	2.818	0.043	-0.288	-0.712	0.000
31	A	46	SER	0	-0.054	-0.037	2.201	-29.231	-25.928	6.823	-5.034	-5.092	-0.050
32	A	47	PRO	0	-0.006	-0.022	2.386	-1.466	1.612	3.283	-0.878	-5.482	0.002
33	A	48	GLU	-1	-0.800	-0.875	3.840	-31.770	-32.083	0.059	0.705	-0.451	0.001
34	A	49	ASP	-1	-0.775	-0.870	4.792	-33.980	-33.896	-0.001	-0.006	-0.077	0.000
4	A	19	SER	0	0.048	0.025	5.704	2.555	2.555	0.000	0.000	0.000	0.000
5	A	20	LEU	0	-0.009	0.020	6.274	-4.157	-4.157	0.000	0.000	0.000	0.000
6	A	21	SER	0	-0.070	-0.034	6.947	3.599	3.599	0.000	0.000	0.000	0.000
7	A	22	ILE	0	0.014	-0.011	8.631	-1.187	-1.187	0.000	0.000	0.000	0.000
8	A	23	THR	0	-0.036	-0.018	10.974	0.023	0.023	0.000	0.000	0.000	0.000
9	A	24	THR	0	0.000	-0.002	12.664	0.824	0.824	0.000	0.000	0.000	0.000
10	A	25	PRO	0	0.021	0.006	14.017	0.834	0.834	0.000	0.000	0.000	0.000
11	A	26	GLU	-1	-0.773	-0.864	16.555	-12.782	-12.782	0.000	0.000	0.000	0.000
12	A	27	GLU	-1	-0.852	-0.910	19.645	-16.037	-16.037	0.000	0.000	0.000	0.000
13	A	28	MET	0	-0.043	-0.011	22.536	0.264	0.264	0.000	0.000	0.000	0.000
14	A	29	ILE	0	-0.011	0.003	22.836	-0.210	-0.210	0.000	0.000	0.000	0.000
15	A	30	GLU	-1	-0.852	-0.945	26.674	-9.437	-9.437	0.000	0.000	0.000	0.000
16	A	31	LYS	1	0.782	0.894	29.190	10.007	10.007	0.000	0.000	0.000	0.000
17	A	32	ALA	0	0.062	0.038	32.397	0.163	0.163	0.000	0.000	0.000	0.000
18	A	33	LYS	1	0.987	0.979	35.430	7.437	7.437	0.000	0.000	0.000	0.000
19	A	34	GLY	0	-0.063	-0.024	37.235	0.124	0.124	0.000	0.000	0.000	0.000
20	A	35	GLU	-1	-0.845	-0.904	33.174	-9.641	-9.641	0.000	0.000	0.000	0.000
21	A	36	THR	0	-0.029	-0.028	28.581	0.018	0.018	0.000	0.000	0.000	0.000
22	A	37	ALA	0	0.011	0.020	27.469	-0.083	-0.083	0.000	0.000	0.000	0.000
23	A	38	TYR	0	-0.015	-0.024	18.900	-0.324	-0.324	0.000	0.000	0.000	0.000
24	A	39	LEU	0	0.033	0.015	22.180	0.014	0.014	0.000	0.000	0.000	0.000
25	A	40	PRO	0	0.024	0.013	17.455	-0.558	-0.558	0.000	0.000	0.000	0.000
26	A	41	CYS	0	-0.035	-0.001	15.302	-0.640	-0.640	0.000	0.000	0.000	0.000
27	A	42	LYS	1	0.869	0.939	11.712	18.928	18.928	0.000	0.000	0.000	0.000
28	A	43	PHE	0	0.037	0.021	8.219	-0.858	-0.858	0.000	0.000	0.000	0.000
35	A	50	GLN	0	-0.049	-0.042	5.946	1.406	1.406	0.000	0.000	0.000	0.000
36	A	51	GLY	0	-0.005	0.005	7.601	1.396	1.396	0.000	0.000	0.000	0.000
37	A	52	PRO	0	-0.010	-0.010	10.176	-1.391	-1.391	0.000	0.000	0.000	0.000
38	A	53	LEU	0	-0.026	-0.012	10.169	-0.621	-0.621	0.000	0.000	0.000	0.000
39	A	54	ASP	-1	-0.911	-0.930	12.283	-14.338	-14.338	0.000	0.000	0.000	0.000
40	A	55	ILE	0	0.002	-0.009	13.816	-1.052	-1.052	0.000	0.000	0.000	0.000
41	A	56	GLU	-1	-0.825	-0.912	16.840	-12.762	-12.762	0.000	0.000	0.000	0.000
42	A	57	TRP	0	-0.009	-0.017	18.756	-0.486	-0.486	0.000	0.000	0.000	0.000
43	A	58	LEU	0	-0.033	-0.010	22.080	0.528	0.528	0.000	0.000	0.000	0.000
44	A	59	ILE	0	-0.014	-0.005	24.956	-0.286	-0.286	0.000	0.000	0.000	0.000
45	A	60	SER	0	0.021	0.012	27.789	0.265	0.265	0.000	0.000	0.000	0.000
46	A	61	PRO	0	-0.025	-0.010	30.196	-0.122	-0.122	0.000	0.000	0.000	0.000
47	A	62	ALA	0	0.019	0.003	32.954	0.074	0.074	0.000	0.000	0.000	0.000
48	A	63	ASP	-1	-0.892	-0.935	35.154	-8.291	-8.291	0.000	0.000	0.000	0.000
49	A	64	ASN	0	-0.059	-0.042	35.917	0.193	0.193	0.000	0.000	0.000	0.000
50	A	65	GLN	0	0.003	-0.010	36.631	-0.009	-0.009	0.000	0.000	0.000	0.000
51	A	66	LYS	1	0.841	0.948	33.904	8.770	8.770	0.000	0.000	0.000	0.000
52	A	67	VAL	0	0.047	0.013	30.138	-0.126	-0.126	0.000	0.000	0.000	0.000
53	A	68	ASP	-1	-0.921	-0.970	26.490	-11.769	-11.769	0.000	0.000	0.000	0.000
54	A	69	GLN	0	-0.031	-0.019	28.034	0.240	0.240	0.000	0.000	0.000	0.000
55	A	70	VAL	0	0.007	-0.003	24.753	-0.289	-0.289	0.000	0.000	0.000	0.000
56	A	71	ILE	0	-0.021	-0.008	25.230	0.384	0.384	0.000	0.000	0.000	0.000
57	A	72	ILE	0	-0.028	-0.011	22.767	0.181	0.181	0.000	0.000	0.000	0.000
58	A	73	LEU	0	-0.026	0.003	20.690	-0.405	-0.405	0.000	0.000	0.000	0.000
59	A	74	TYR	0	-0.066	-0.062	14.811	-0.034	-0.034	0.000	0.000	0.000	0.000
60	A	75	SER	0	0.010	-0.021	18.312	-0.490	-0.490	0.000	0.000	0.000	0.000
61	A	76	GLY	0	0.002	-0.007	18.575	0.541	0.541	0.000	0.000	0.000	0.000
62	A	77	ASP	-1	-0.874	-0.918	17.396	-15.597	-15.597	0.000	0.000	0.000	0.000
63	A	78	LYS	1	0.925	0.976	18.830	11.776	11.776	0.000	0.000	0.000	0.000
64	A	79	ILE	0	0.037	0.012	21.205	-0.459	-0.459	0.000	0.000	0.000	0.000
65	A	80	TYR	0	-0.045	-0.018	22.937	0.767	0.767	0.000	0.000	0.000	0.000
66	A	81	ASP	-1	-0.738	-0.861	25.748	-11.549	-11.549	0.000	0.000	0.000	0.000
67	A	82	ASP	-1	-0.842	-0.930	27.726	-9.723	-9.723	0.000	0.000	0.000	0.000
68	A	83	TYR	0	-0.097	-0.037	29.553	0.335	0.335	0.000	0.000	0.000	0.000
69	A	84	TYR	0	-0.008	-0.001	25.656	0.303	0.303	0.000	0.000	0.000	0.000
70	A	85	PRO	0	-0.024	-0.017	31.222	0.090	0.090	0.000	0.000	0.000	0.000
71	A	86	ASP	-1	-0.885	-0.952	31.697	-9.134	-9.134	0.000	0.000	0.000	0.000
72	A	87	LEU	0	0.024	0.000	29.047	-0.294	-0.294	0.000	0.000	0.000	0.000
73	A	88	LYS	1	0.966	1.005	32.195	8.219	8.219	0.000	0.000	0.000	0.000
74	A	89	GLY	0	-0.018	-0.013	32.846	0.289	0.289	0.000	0.000	0.000	0.000
75	A	90	ARG	1	0.719	0.821	32.206	9.171	9.171	0.000	0.000	0.000	0.000
76	A	91	VAL	0	0.010	0.027	26.117	-0.237	-0.237	0.000	0.000	0.000	0.000
77	A	92	HIS	1	0.805	0.874	26.115	10.936	10.936	0.000	0.000	0.000	0.000
78	A	93	PHE	0	0.038	0.013	18.895	-0.250	-0.250	0.000	0.000	0.000	0.000
79	A	94	THR	0	0.005	-0.007	20.184	0.393	0.393	0.000	0.000	0.000	0.000
80	A	95	SER	0	-0.065	-0.016	16.784	0.446	0.446	0.000	0.000	0.000	0.000
81	A	96	ASN	0	0.001	-0.008	19.713	-0.131	-0.131	0.000	0.000	0.000	0.000
82	A	97	ASP	-1	-0.813	-0.916	14.617	-20.371	-20.371	0.000	0.000	0.000	0.000
83	A	98	LEU	0	0.005	0.019	15.254	-1.055	-1.055	0.000	0.000	0.000	0.000
84	A	99	LYS	1	0.831	0.907	11.191	16.488	16.488	0.000	0.000	0.000	0.000
85	A	100	SER	0	-0.067	-0.031	10.021	-2.664	-2.664	0.000	0.000	0.000	0.000
86	A	101	GLY	0	0.039	0.027	9.709	-2.627	-2.627	0.000	0.000	0.000	0.000
87	A	102	ASP	-1	-0.835	-0.870	10.385	-18.708	-18.708	0.000	0.000	0.000	0.000
88	A	103	ALA	0	0.052	0.011	13.949	0.960	0.960	0.000	0.000	0.000	0.000
89	A	104	SER	0	-0.054	-0.053	15.729	0.863	0.863	0.000	0.000	0.000	0.000
90	A	105	ILE	0	0.005	0.025	18.449	0.351	0.351	0.000	0.000	0.000	0.000
91	A	106	ASN	0	-0.035	-0.030	22.159	0.004	0.004	0.000	0.000	0.000	0.000
92	A	107	VAL	0	0.054	0.032	25.585	0.104	0.104	0.000	0.000	0.000	0.000
93	A	108	THR	0	0.008	-0.002	28.948	0.177	0.177	0.000	0.000	0.000	0.000
94	A	109	ASN	0	-0.002	-0.004	32.066	0.193	0.193	0.000	0.000	0.000	0.000
95	A	110	LEU	0	0.004	0.026	30.688	0.153	0.153	0.000	0.000	0.000	0.000
96	A	111	GLN	0	-0.022	-0.034	34.782	0.533	0.533	0.000	0.000	0.000	0.000
97	A	112	LEU	0	0.026	0.002	35.866	-0.186	-0.186	0.000	0.000	0.000	0.000
98	A	113	SER	0	0.025	0.017	36.563	0.004	0.004	0.000	0.000	0.000	0.000
99	A	114	ASP	-1	-0.778	-0.842	32.036	-9.467	-9.467	0.000	0.000	0.000	0.000
100	A	115	ILE	0	-0.002	0.023	31.494	-0.438	-0.438	0.000	0.000	0.000	0.000
101	A	116	GLY	0	0.043	0.020	30.989	0.233	0.233	0.000	0.000	0.000	0.000
102	A	117	THR	0	-0.067	-0.033	25.593	-0.208	-0.208	0.000	0.000	0.000	0.000
103	A	118	TYR	0	-0.026	-0.030	24.035	0.033	0.033	0.000	0.000	0.000	0.000
104	A	119	GLN	0	-0.021	-0.021	20.568	-0.851	-0.851	0.000	0.000	0.000	0.000
105	A	121	LYS	1	0.873	0.939	16.497	13.631	13.631	0.000	0.000	0.000	0.000
106	A	122	VAL	0	0.015	0.003	11.030	0.228	0.228	0.000	0.000	0.000	0.000
107	A	123	LYS	1	0.952	0.980	12.392	15.641	15.641	0.000	0.000	0.000	0.000
108	A	124	LYS	1	0.814	0.889	6.717	28.050	28.050	0.000	0.000	0.000	0.000
109	A	125	ALA	0	-0.007	0.026	9.288	-1.392	-1.392	0.000	0.000	0.000	0.000
110	A	126	PRO	0	0.010	-0.006	9.177	-0.439	-0.439	0.000	0.000	0.000	0.000
111	A	127	GLY	0	0.042	0.033	8.978	0.985	0.985	0.000	0.000	0.000	0.000
112	A	128	VAL	0	-0.023	-0.041	9.987	1.279	1.279	0.000	0.000	0.000	0.000
113	A	129	ALA	0	-0.021	0.007	10.936	-0.725	-0.725	0.000	0.000	0.000	0.000
114	A	130	ASN	0	0.014	-0.012	13.034	0.921	0.921	0.000	0.000	0.000	0.000
115	A	131	LYS	1	0.746	0.868	15.677	17.162	17.162	0.000	0.000	0.000	0.000
116	A	132	LYS	1	0.848	0.920	17.497	13.835	13.835	0.000	0.000	0.000	0.000
117	A	133	ILE	0	-0.015	-0.012	19.879	-0.432	-0.432	0.000	0.000	0.000	0.000
118	A	134	HIS	0	-0.044	-0.014	23.091	0.670	0.670	0.000	0.000	0.000	0.000
119	A	135	LEU	0	-0.015	0.000	26.824	-0.132	-0.132	0.000	0.000	0.000	0.000
120	A	136	VAL	0	0.020	-0.003	28.686	0.332	0.332	0.000	0.000	0.000	0.000
121	A	137	VAL	0	-0.011	-0.012	32.060	-0.136	-0.136	0.000	0.000	0.000	0.000
122	A	138	LEU	0	-0.019	-0.008	34.660	0.263	0.263	0.000	0.000	0.000	0.000
123	A	139	VAL	-1	-0.925	-0.968	37.517	-7.826	-7.826	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:16:PHE)