FMO DATABASE

FMODB ID: KKQY3

Calculation Name: 1G2I-A-Xray547

Preferred Name:

Target Type:

Ligand Name: sulfate ion

Ligand 3-letter code: SO4

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1G2I

Chain ID: A

ChEMBL ID:

UniProt ID: O59413

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	166
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1784521.767371
FMO2-HF: Nuclear repulsion	1719546.157828
FMO2-HF: Total energy	-64975.609542
FMO2-MP2: Total energy	-65166.523516

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.
-184.949	-183.334	25.471	-10.786	-16.303	-0.102

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 : 0.810 / q_NPA : 0.907

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	VAL	0	0.013	0.005	3.505	5.984	7.969	0.011	-0.748	-1.249	-0.002
4	A	4	LEU	0	-0.004	0.001	5.223	2.679	2.713	-0.001	-0.004	-0.028	0.000
28	A	28	HIS	0	-0.002	0.006	1.991	-53.025	-54.056	13.407	-5.950	-6.426	-0.081
29	A	29	GLU	-1	-0.883	-0.923	3.230	-36.607	-35.772	0.015	-0.149	-0.702	-0.001
30	A	30	VAL	0	-0.055	-0.027	5.235	-1.843	-1.921	-0.001	-0.018	0.097	0.000
63	A	63	ASP	-1	-0.785	-0.885	2.046	-56.822	-57.246	6.685	-2.545	-3.716	-0.015
64	A	64	ALA	0	0.026	0.011	3.522	2.751	3.749	0.232	-0.236	-0.995	0.000
65	A	65	LEU	0	-0.046	-0.019	4.942	-0.492	-0.489	-0.001	-0.013	0.011	0.000
95	A	95	PRO	0	0.022	0.017	3.999	1.466	1.883	0.027	-0.096	-0.348	0.000
165	A	165	LEU	0	-0.055	-0.039	2.694	-1.066	-2.708	5.087	-0.855	-2.590	-0.002
166	A	166	LYS	0	-0.019	0.031	3.679	-18.696	-18.178	0.010	-0.172	-0.357	-0.001
5	A	5	PHE	0	0.036	0.002	8.575	1.050	1.050	0.000	0.000	0.000	0.000
6	A	6	LEU	0	-0.006	0.007	11.858	0.900	0.900	0.000	0.000	0.000	0.000
7	A	7	THR	0	0.005	-0.001	14.841	0.973	0.973	0.000	0.000	0.000	0.000
8	A	8	ALA	0	0.044	0.027	17.924	0.289	0.289	0.000	0.000	0.000	0.000
9	A	9	ASN	0	0.065	0.032	21.504	-0.325	-0.325	0.000	0.000	0.000	0.000
10	A	10	GLU	-1	-0.814	-0.901	24.601	-10.507	-10.507	0.000	0.000	0.000	0.000
11	A	11	PHE	0	-0.043	-0.011	20.280	0.112	0.112	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.855	-0.942	21.619	-11.801	-11.801	0.000	0.000	0.000	0.000
13	A	13	ASP	-1	-0.776	-0.882	20.787	-13.352	-13.352	0.000	0.000	0.000	0.000
14	A	14	VAL	0	0.068	0.011	20.080	-0.860	-0.860	0.000	0.000	0.000	0.000
15	A	15	GLU	-1	-0.777	-0.915	18.071	-14.960	-14.960	0.000	0.000	0.000	0.000
16	A	16	LEU	0	-0.030	0.000	14.451	-0.962	-0.962	0.000	0.000	0.000	0.000
17	A	17	ILE	0	0.012	-0.006	14.930	-1.501	-1.501	0.000	0.000	0.000	0.000
18	A	18	TYR	0	0.029	0.023	15.491	-1.086	-1.086	0.000	0.000	0.000	0.000
19	A	19	PRO	0	0.022	0.008	11.391	-1.142	-1.142	0.000	0.000	0.000	0.000
20	A	20	TYR	0	-0.018	-0.003	10.542	-2.538	-2.538	0.000	0.000	0.000	0.000
21	A	21	HIS	0	-0.060	-0.045	10.473	-2.022	-2.022	0.000	0.000	0.000	0.000
22	A	22	ARG	1	0.827	0.889	10.259	24.532	24.532	0.000	0.000	0.000	0.000
23	A	23	LEU	0	0.018	0.008	6.066	-1.151	-1.151	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.942	0.971	6.221	21.998	21.998	0.000	0.000	0.000	0.000
25	A	25	GLU	-1	-0.964	-0.974	7.964	-24.047	-24.047	0.000	0.000	0.000	0.000
26	A	26	GLU	-1	-0.859	-0.906	5.841	-29.647	-29.647	0.000	0.000	0.000	0.000
27	A	27	GLY	0	-0.005	0.011	5.438	-4.387	-4.387	0.000	0.000	0.000	0.000
31	A	31	TYR	0	-0.057	-0.038	6.739	5.530	5.530	0.000	0.000	0.000	0.000
32	A	32	ILE	0	-0.030	-0.023	10.681	0.511	0.511	0.000	0.000	0.000	0.000
33	A	33	ALA	0	0.023	0.008	13.839	0.682	0.682	0.000	0.000	0.000	0.000
34	A	34	SER	0	-0.009	-0.047	15.320	0.680	0.680	0.000	0.000	0.000	0.000
35	A	35	PHE	0	-0.012	-0.013	18.953	-0.100	-0.100	0.000	0.000	0.000	0.000
36	A	36	GLU	-1	-0.914	-0.959	22.274	-11.154	-11.154	0.000	0.000	0.000	0.000
37	A	37	ARG	1	0.844	0.891	18.384	15.456	15.456	0.000	0.000	0.000	0.000
38	A	38	GLY	0	0.032	0.028	22.314	0.599	0.599	0.000	0.000	0.000	0.000
39	A	39	THR	0	-0.022	-0.020	22.114	-0.673	-0.673	0.000	0.000	0.000	0.000
40	A	40	ILE	0	-0.035	-0.001	18.812	0.552	0.552	0.000	0.000	0.000	0.000
41	A	41	THR	0	-0.020	-0.020	22.982	-0.309	-0.309	0.000	0.000	0.000	0.000
42	A	42	GLY	0	-0.001	0.012	24.042	0.091	0.091	0.000	0.000	0.000	0.000
43	A	43	LYS	1	0.889	0.945	24.596	11.950	11.950	0.000	0.000	0.000	0.000
44	A	44	HIS	0	-0.098	-0.056	26.155	0.755	0.755	0.000	0.000	0.000	0.000
45	A	45	GLY	0	0.004	0.009	27.821	0.184	0.184	0.000	0.000	0.000	0.000
46	A	46	TYR	0	-0.022	-0.014	22.780	-0.194	-0.194	0.000	0.000	0.000	0.000
47	A	47	SER	0	-0.013	0.000	23.887	-0.437	-0.437	0.000	0.000	0.000	0.000
48	A	48	VAL	0	0.004	-0.006	18.571	-0.449	-0.449	0.000	0.000	0.000	0.000
49	A	49	LYS	1	0.968	0.981	16.038	19.294	19.294	0.000	0.000	0.000	0.000
50	A	50	VAL	0	-0.010	0.001	17.556	-0.932	-0.932	0.000	0.000	0.000	0.000
51	A	51	ASP	-1	-0.819	-0.896	13.954	-21.361	-21.361	0.000	0.000	0.000	0.000
52	A	52	LEU	0	-0.086	-0.039	12.934	0.728	0.728	0.000	0.000	0.000	0.000
53	A	53	THR	0	0.052	0.027	17.015	-0.121	-0.121	0.000	0.000	0.000	0.000
54	A	54	PHE	0	0.037	0.018	16.653	-0.582	-0.582	0.000	0.000	0.000	0.000
55	A	55	ASP	-1	-0.898	-0.948	17.759	-13.567	-13.567	0.000	0.000	0.000	0.000
56	A	56	LYS	1	0.905	0.949	18.006	14.126	14.126	0.000	0.000	0.000	0.000
57	A	57	VAL	0	0.002	0.020	12.132	-0.792	-0.792	0.000	0.000	0.000	0.000
58	A	58	ASN	0	0.054	0.025	13.297	1.327	1.327	0.000	0.000	0.000	0.000
59	A	59	PRO	0	-0.014	-0.028	11.241	-1.455	-1.455	0.000	0.000	0.000	0.000
60	A	60	GLU	-1	-0.863	-0.900	9.823	-22.108	-22.108	0.000	0.000	0.000	0.000
61	A	61	GLU	-1	-0.938	-0.948	9.329	-23.013	-23.013	0.000	0.000	0.000	0.000
62	A	62	PHE	0	-0.047	-0.035	6.158	-3.442	-3.442	0.000	0.000	0.000	0.000
66	A	66	VAL	0	0.003	0.004	8.340	0.637	0.637	0.000	0.000	0.000	0.000
67	A	67	LEU	0	-0.027	-0.014	10.931	0.784	0.784	0.000	0.000	0.000	0.000
68	A	68	PRO	0	0.028	0.002	14.514	0.622	0.622	0.000	0.000	0.000	0.000
69	A	69	GLY	0	0.019	0.012	17.304	0.473	0.473	0.000	0.000	0.000	0.000
70	A	70	GLY	0	-0.032	-0.017	21.040	-0.127	-0.127	0.000	0.000	0.000	0.000
71	A	71	ARG	1	0.870	0.898	24.226	10.070	10.070	0.000	0.000	0.000	0.000
72	A	72	ALA	0	-0.019	0.020	21.352	0.119	0.119	0.000	0.000	0.000	0.000
73	A	73	PRO	0	0.031	0.009	19.992	0.112	0.112	0.000	0.000	0.000	0.000
74	A	74	GLU	-1	-0.871	-0.927	21.840	-10.299	-10.299	0.000	0.000	0.000	0.000
75	A	75	ARG	1	0.953	0.976	24.756	10.663	10.663	0.000	0.000	0.000	0.000
76	A	76	VAL	0	0.023	0.006	18.414	0.098	0.098	0.000	0.000	0.000	0.000
77	A	77	ARG	1	0.896	0.957	21.703	11.077	11.077	0.000	0.000	0.000	0.000
78	A	78	LEU	0	-0.003	0.004	22.799	0.296	0.296	0.000	0.000	0.000	0.000
79	A	79	ASN	0	-0.015	0.003	21.323	-0.191	-0.191	0.000	0.000	0.000	0.000
80	A	80	GLU	-1	-0.880	-0.949	21.781	-13.053	-13.053	0.000	0.000	0.000	0.000
81	A	81	LYS	1	0.929	0.978	17.144	15.334	15.334	0.000	0.000	0.000	0.000
82	A	82	ALA	0	0.026	0.011	17.236	-0.782	-0.782	0.000	0.000	0.000	0.000
83	A	83	VAL	0	-0.002	0.003	16.966	-0.755	-0.755	0.000	0.000	0.000	0.000
84	A	84	SER	0	-0.104	-0.058	18.438	-0.381	-0.381	0.000	0.000	0.000	0.000
85	A	85	ILE	0	-0.027	-0.009	12.503	-0.446	-0.446	0.000	0.000	0.000	0.000
86	A	86	ALA	0	0.026	0.011	13.553	-0.842	-0.842	0.000	0.000	0.000	0.000
87	A	87	ARG	1	0.913	0.958	14.542	12.599	12.599	0.000	0.000	0.000	0.000
88	A	88	LYS	1	0.947	0.996	14.264	15.402	15.402	0.000	0.000	0.000	0.000
89	A	89	MET	0	0.002	0.011	7.170	0.350	0.350	0.000	0.000	0.000	0.000
90	A	90	PHE	0	0.029	0.005	10.806	-0.570	-0.570	0.000	0.000	0.000	0.000
91	A	91	SER	0	-0.047	-0.046	12.842	0.239	0.239	0.000	0.000	0.000	0.000
92	A	92	GLU	0	-0.083	-0.082	11.001	-0.080	-0.080	0.000	0.000	0.000	0.000
93	A	93	GLY	0	0.007	0.015	10.616	-0.641	-0.641	0.000	0.000	0.000	0.000
94	A	94	LYS	1	0.844	0.942	6.713	24.233	24.233	0.000	0.000	0.000	0.000
96	A	96	VAL	0	-0.011	-0.010	7.016	-0.935	-0.935	0.000	0.000	0.000	0.000
97	A	97	ALA	0	0.024	0.031	9.978	1.189	1.189	0.000	0.000	0.000	0.000
98	A	98	SER	0	-0.032	-0.031	11.896	0.296	0.296	0.000	0.000	0.000	0.000
99	A	99	ILE	0	-0.007	0.014	15.583	0.439	0.439	0.000	0.000	0.000	0.000
100	A	100	CYS	0	0.039	0.032	18.651	0.531	0.531	0.000	0.000	0.000	0.000
101	A	101	HIS	1	0.880	0.925	22.104	11.758	11.758	0.000	0.000	0.000	0.000
102	A	102	GLY	0	0.052	0.047	18.146	0.214	0.214	0.000	0.000	0.000	0.000
103	A	103	PRO	0	-0.002	-0.016	18.781	-0.163	-0.163	0.000	0.000	0.000	0.000
104	A	104	GLN	0	0.006	-0.025	19.707	0.104	0.104	0.000	0.000	0.000	0.000
105	A	105	ILE	0	-0.018	-0.014	17.462	0.387	0.387	0.000	0.000	0.000	0.000
106	A	106	LEU	0	0.015	0.009	15.042	0.098	0.098	0.000	0.000	0.000	0.000
107	A	107	ILE	0	0.014	0.004	19.196	0.274	0.274	0.000	0.000	0.000	0.000
108	A	108	SER	0	-0.036	-0.016	22.529	0.351	0.351	0.000	0.000	0.000	0.000
109	A	109	ALA	0	-0.030	-0.008	18.713	0.149	0.149	0.000	0.000	0.000	0.000
110	A	110	GLY	0	0.002	0.006	20.753	0.050	0.050	0.000	0.000	0.000	0.000
111	A	111	VAL	0	-0.061	-0.029	16.936	0.262	0.262	0.000	0.000	0.000	0.000
112	A	112	LEU	0	0.007	0.003	18.555	-0.227	-0.227	0.000	0.000	0.000	0.000
113	A	113	ARG	1	0.913	0.972	21.055	10.255	10.255	0.000	0.000	0.000	0.000
114	A	114	GLY	0	-0.019	-0.010	23.063	-0.119	-0.119	0.000	0.000	0.000	0.000
115	A	115	ARG	1	0.770	0.893	14.206	15.257	15.257	0.000	0.000	0.000	0.000
116	A	116	LYS	1	0.881	0.916	19.670	11.905	11.905	0.000	0.000	0.000	0.000
117	A	117	GLY	0	0.015	-0.012	19.214	-0.727	-0.727	0.000	0.000	0.000	0.000
118	A	118	THR	0	-0.007	-0.010	20.263	0.666	0.666	0.000	0.000	0.000	0.000
119	A	119	SER	0	0.013	0.004	20.945	-0.446	-0.446	0.000	0.000	0.000	0.000
120	A	120	TYR	0	0.038	0.018	22.931	0.311	0.311	0.000	0.000	0.000	0.000
121	A	121	PRO	0	0.030	0.008	25.621	0.153	0.153	0.000	0.000	0.000	0.000
122	A	122	GLY	0	-0.030	-0.012	28.617	0.251	0.251	0.000	0.000	0.000	0.000
123	A	123	ILE	0	-0.026	-0.006	24.379	0.116	0.116	0.000	0.000	0.000	0.000
124	A	124	LYS	1	0.895	0.945	27.398	8.803	8.803	0.000	0.000	0.000	0.000
125	A	125	ASP	-1	-0.819	-0.906	28.463	-8.982	-8.982	0.000	0.000	0.000	0.000
126	A	126	ASP	-1	-0.914	-0.951	27.818	-9.738	-9.738	0.000	0.000	0.000	0.000
127	A	127	MET	0	-0.052	-0.025	20.938	-0.232	-0.232	0.000	0.000	0.000	0.000
128	A	128	ILE	0	0.018	0.020	25.977	-0.102	-0.102	0.000	0.000	0.000	0.000
129	A	129	ASN	0	-0.026	-0.009	28.598	0.195	0.195	0.000	0.000	0.000	0.000
130	A	130	ALA	0	-0.055	-0.033	24.748	0.077	0.077	0.000	0.000	0.000	0.000
131	A	131	GLY	0	-0.044	-0.026	25.723	-0.166	-0.166	0.000	0.000	0.000	0.000
132	A	132	VAL	0	-0.014	0.002	22.148	-0.164	-0.164	0.000	0.000	0.000	0.000
133	A	133	GLU	-1	-0.834	-0.899	23.925	-10.664	-10.664	0.000	0.000	0.000	0.000
134	A	134	TRP	0	-0.026	-0.038	24.420	-0.250	-0.250	0.000	0.000	0.000	0.000
135	A	135	VAL	0	-0.009	-0.008	24.044	0.412	0.412	0.000	0.000	0.000	0.000
136	A	136	ASP	-1	-0.876	-0.913	24.998	-10.817	-10.817	0.000	0.000	0.000	0.000
137	A	137	ALA	0	0.010	-0.006	23.335	0.197	0.197	0.000	0.000	0.000	0.000
138	A	138	GLU	-1	-0.825	-0.875	21.968	-13.366	-13.366	0.000	0.000	0.000	0.000
139	A	139	VAL	0	-0.030	-0.008	16.447	-0.646	-0.646	0.000	0.000	0.000	0.000
140	A	140	VAL	0	-0.034	0.011	18.523	0.548	0.548	0.000	0.000	0.000	0.000
141	A	141	VAL	0	-0.004	-0.006	13.344	-0.743	-0.743	0.000	0.000	0.000	0.000
142	A	142	ASP	-1	-0.767	-0.869	14.997	-13.636	-13.636	0.000	0.000	0.000	0.000
143	A	143	GLY	0	0.027	0.012	13.095	-0.338	-0.338	0.000	0.000	0.000	0.000
144	A	144	ASN	0	-0.023	-0.005	9.492	0.297	0.297	0.000	0.000	0.000	0.000
145	A	145	TRP	0	-0.040	-0.016	10.248	-0.884	-0.884	0.000	0.000	0.000	0.000
146	A	146	VAL	0	0.023	0.010	11.423	0.604	0.604	0.000	0.000	0.000	0.000
147	A	147	SER	0	-0.019	-0.002	13.756	0.026	0.026	0.000	0.000	0.000	0.000
148	A	148	SER	0	0.040	-0.026	17.045	-0.067	-0.067	0.000	0.000	0.000	0.000
149	A	149	ARG	1	0.782	0.863	19.647	11.702	11.702	0.000	0.000	0.000	0.000
150	A	150	VAL	0	-0.017	-0.024	23.062	0.275	0.275	0.000	0.000	0.000	0.000
151	A	151	PRO	0	0.057	0.014	21.734	-0.363	-0.363	0.000	0.000	0.000	0.000
152	A	152	ALA	0	-0.004	0.005	22.282	-0.289	-0.289	0.000	0.000	0.000	0.000
153	A	153	ASP	-1	-0.704	-0.833	20.811	-12.792	-12.792	0.000	0.000	0.000	0.000
154	A	154	LEU	0	-0.057	-0.020	17.205	-0.717	-0.717	0.000	0.000	0.000	0.000
155	A	155	TYR	0	-0.036	-0.058	16.743	-1.231	-1.231	0.000	0.000	0.000	0.000
156	A	156	ALA	0	0.009	0.014	17.430	-0.634	-0.634	0.000	0.000	0.000	0.000
157	A	157	TRP	0	0.001	-0.014	14.487	-1.225	-1.225	0.000	0.000	0.000	0.000
158	A	158	MET	0	-0.020	-0.005	11.076	-1.910	-1.910	0.000	0.000	0.000	0.000
159	A	159	ARG	1	0.841	0.936	12.070	14.028	14.028	0.000	0.000	0.000	0.000
160	A	160	GLU	-1	-0.776	-0.867	13.705	-17.730	-17.730	0.000	0.000	0.000	0.000
161	A	161	PHE	0	0.030	0.004	7.307	-1.251	-1.251	0.000	0.000	0.000	0.000
162	A	162	VAL	0	0.015	-0.005	8.122	-2.221	-2.221	0.000	0.000	0.000	0.000
163	A	163	LYS	1	0.748	0.855	8.528	16.367	16.367	0.000	0.000	0.000	0.000
164	A	164	LEU	0	-0.025	-0.007	6.390	-0.333	-0.333	0.000	0.000	0.000	0.000

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