FMO DATABASE

FMODB ID: MR7GZ

Calculation Name: 2H1C-A-Xray547

Preferred Name:

Target Type:

Ligand Name: sulfate ion | acetate ion | magnesium ion

Ligand 3-letter code: SO4 | ACT | MG

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2H1C

Chain ID: A

ChEMBL ID:

UniProt ID: Q5F881

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	139
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1195243.235013
FMO2-HF: Nuclear repulsion	1142867.034003
FMO2-HF: Total energy	-52376.201011
FMO2-MP2: Total energy	-52533.274704

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.
-138.965	-132.641	15.063	-7.572	-13.815	-0.098

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 : 0.812 / q_NPA : 0.928

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	LEU	0	-0.016	0.001	3.846	4.282	5.541	-0.018	-0.463	-0.778	-0.001
32	A	32	ASP	-1	-0.897	-0.962	2.581	-71.985	-69.319	7.323	-4.790	-5.199	-0.044
33	A	33	VAL	0	-0.037	-0.021	2.308	-17.404	-17.232	3.102	-0.199	-3.075	-0.039
34	A	34	TYR	0	-0.008	0.004	3.118	5.525	6.750	0.836	-0.574	-1.487	-0.001
115	A	115	SER	0	-0.013	0.009	4.775	-3.826	-3.610	-0.001	-0.012	-0.203	0.000
116	A	116	LEU	0	-0.056	-0.022	2.246	-11.810	-11.522	3.819	-1.410	-2.698	-0.013
117	A	117	THR	0	-0.015	-0.002	3.815	8.654	9.152	0.002	-0.124	-0.375	0.000
4	A	4	LEU	0	0.001	-0.005	6.843	1.110	1.110	0.000	0.000	0.000	0.000
5	A	5	ASP	-1	-0.765	-0.843	9.921	-18.496	-18.496	0.000	0.000	0.000	0.000
6	A	6	THR	0	0.000	-0.042	13.169	-0.220	-0.220	0.000	0.000	0.000	0.000
7	A	7	ASN	0	-0.032	-0.016	16.354	-0.098	-0.098	0.000	0.000	0.000	0.000
8	A	8	VAL	0	0.034	0.026	11.923	0.741	0.741	0.000	0.000	0.000	0.000
9	A	9	ILE	0	-0.009	0.000	13.165	0.297	0.297	0.000	0.000	0.000	0.000
10	A	10	SER	0	-0.026	-0.035	15.098	1.154	1.154	0.000	0.000	0.000	0.000
11	A	11	GLU	-1	-0.798	-0.873	17.980	-13.518	-13.518	0.000	0.000	0.000	0.000
12	A	12	PRO	0	0.011	-0.013	16.506	0.985	0.985	0.000	0.000	0.000	0.000
13	A	13	LEU	0	-0.043	-0.004	19.783	0.665	0.665	0.000	0.000	0.000	0.000
14	A	14	ARG	1	0.811	0.897	22.313	13.900	13.900	0.000	0.000	0.000	0.000
15	A	15	PRO	0	-0.042	-0.040	24.827	-0.002	-0.002	0.000	0.000	0.000	0.000
16	A	16	GLN	0	-0.028	-0.013	27.087	0.227	0.227	0.000	0.000	0.000	0.000
17	A	17	PRO	0	-0.032	0.020	21.552	-0.012	-0.012	0.000	0.000	0.000	0.000
18	A	18	ASN	0	0.022	-0.008	19.917	-0.506	-0.506	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.853	-0.941	19.676	-14.105	-14.105	0.000	0.000	0.000	0.000
20	A	20	ARG	1	0.846	0.931	16.540	15.429	15.429	0.000	0.000	0.000	0.000
21	A	21	VAL	0	0.014	0.004	14.865	-1.274	-1.274	0.000	0.000	0.000	0.000
22	A	22	VAL	0	-0.025	-0.009	14.806	-1.272	-1.272	0.000	0.000	0.000	0.000
23	A	23	ALA	0	0.044	0.018	15.537	-0.882	-0.882	0.000	0.000	0.000	0.000
24	A	24	TRP	0	0.017	0.012	7.335	-1.104	-1.104	0.000	0.000	0.000	0.000
25	A	25	LEU	0	-0.033	-0.016	10.715	-2.387	-2.387	0.000	0.000	0.000	0.000
26	A	26	ASP	-1	-0.912	-0.957	11.603	-19.943	-19.943	0.000	0.000	0.000	0.000
27	A	27	SER	0	-0.129	-0.071	10.749	-0.208	-0.208	0.000	0.000	0.000	0.000
28	A	28	LEU	0	-0.054	-0.022	6.268	-3.150	-3.150	0.000	0.000	0.000	0.000
29	A	29	ILE	0	0.014	0.016	5.479	3.193	3.193	0.000	0.000	0.000	0.000
30	A	30	LEU	0	0.019	0.011	6.471	-4.099	-4.099	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.882	-0.962	5.527	-29.303	-29.303	0.000	0.000	0.000	0.000
35	A	35	LEU	0	0.003	0.007	6.917	0.537	0.537	0.000	0.000	0.000	0.000
36	A	36	SER	0	0.035	0.023	10.190	0.594	0.594	0.000	0.000	0.000	0.000
37	A	37	ALA	0	0.024	-0.004	12.043	0.852	0.852	0.000	0.000	0.000	0.000
38	A	38	ILE	0	-0.018	-0.002	15.288	1.001	1.001	0.000	0.000	0.000	0.000
39	A	39	THR	0	0.056	0.026	13.947	0.459	0.459	0.000	0.000	0.000	0.000
40	A	40	VAL	0	0.002	0.000	14.545	0.747	0.747	0.000	0.000	0.000	0.000
41	A	41	ALA	0	-0.020	-0.008	17.186	0.879	0.879	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.864	-0.914	18.672	-15.254	-15.254	0.000	0.000	0.000	0.000
43	A	43	LEU	0	-0.001	0.003	16.416	0.717	0.717	0.000	0.000	0.000	0.000
44	A	44	ARG	1	0.808	0.862	20.249	14.574	14.574	0.000	0.000	0.000	0.000
45	A	45	LEU	0	-0.012	0.002	23.109	0.645	0.645	0.000	0.000	0.000	0.000
46	A	46	GLY	0	0.021	0.005	24.046	0.513	0.513	0.000	0.000	0.000	0.000
47	A	47	VAL	0	-0.005	-0.012	23.910	0.491	0.491	0.000	0.000	0.000	0.000
48	A	48	ALA	0	-0.028	-0.023	26.535	0.515	0.515	0.000	0.000	0.000	0.000
49	A	49	LEU	0	-0.021	-0.018	28.412	0.493	0.493	0.000	0.000	0.000	0.000
50	A	50	LEU	0	-0.049	-0.004	27.598	0.301	0.301	0.000	0.000	0.000	0.000
51	A	51	LEU	0	0.029	0.008	31.367	0.222	0.222	0.000	0.000	0.000	0.000
52	A	52	ASN	0	-0.022	0.002	33.906	0.210	0.210	0.000	0.000	0.000	0.000
53	A	53	GLY	0	0.081	0.024	33.610	-0.259	-0.259	0.000	0.000	0.000	0.000
54	A	54	LYS	1	0.949	0.976	34.157	7.971	7.971	0.000	0.000	0.000	0.000
55	A	55	LYS	1	0.986	0.984	29.382	9.954	9.954	0.000	0.000	0.000	0.000
56	A	56	LYS	1	0.960	1.002	29.644	9.121	9.121	0.000	0.000	0.000	0.000
57	A	57	ASN	0	0.004	-0.007	29.194	-0.353	-0.353	0.000	0.000	0.000	0.000
58	A	58	VAL	0	0.002	0.007	28.483	-0.167	-0.167	0.000	0.000	0.000	0.000
59	A	59	LEU	0	0.022	0.007	23.168	-0.253	-0.253	0.000	0.000	0.000	0.000
60	A	60	HIS	0	-0.004	0.007	24.662	-0.346	-0.346	0.000	0.000	0.000	0.000
61	A	61	GLU	-1	-0.888	-0.950	25.098	-11.231	-11.231	0.000	0.000	0.000	0.000
62	A	62	ARG	1	0.914	0.955	23.181	11.145	11.145	0.000	0.000	0.000	0.000
63	A	63	LEU	0	0.030	0.017	19.239	-0.636	-0.636	0.000	0.000	0.000	0.000
64	A	64	GLU	-1	-0.779	-0.866	20.273	-14.196	-14.196	0.000	0.000	0.000	0.000
65	A	65	GLN	0	0.002	0.004	21.616	-0.616	-0.616	0.000	0.000	0.000	0.000
66	A	66	SER	0	-0.097	-0.057	20.773	0.312	0.312	0.000	0.000	0.000	0.000
67	A	67	ILE	0	-0.010	0.012	16.266	-0.544	-0.544	0.000	0.000	0.000	0.000
68	A	68	LEU	0	0.011	-0.002	15.858	-1.165	-1.165	0.000	0.000	0.000	0.000
69	A	69	PRO	0	-0.012	-0.002	15.686	-0.927	-0.927	0.000	0.000	0.000	0.000
70	A	70	LEU	0	0.025	0.029	13.341	-0.419	-0.419	0.000	0.000	0.000	0.000
71	A	71	PHE	0	0.018	0.001	9.210	-1.515	-1.515	0.000	0.000	0.000	0.000
72	A	72	ALA	0	0.028	0.018	12.307	0.023	0.023	0.000	0.000	0.000	0.000
73	A	73	GLY	0	-0.030	-0.021	11.782	-0.990	-0.990	0.000	0.000	0.000	0.000
74	A	74	ARG	1	0.815	0.909	6.297	28.687	28.687	0.000	0.000	0.000	0.000
75	A	75	ILE	0	-0.004	0.004	9.156	-1.359	-1.359	0.000	0.000	0.000	0.000
76	A	76	LEU	0	-0.028	-0.013	6.503	0.853	0.853	0.000	0.000	0.000	0.000
77	A	77	PRO	0	-0.010	-0.008	11.193	0.718	0.718	0.000	0.000	0.000	0.000
78	A	78	PHE	0	0.008	0.004	13.563	-0.888	-0.888	0.000	0.000	0.000	0.000
79	A	79	ASP	-1	-0.851	-0.935	14.837	-17.250	-17.250	0.000	0.000	0.000	0.000
80	A	80	GLU	-1	-0.911	-0.965	17.530	-14.024	-14.024	0.000	0.000	0.000	0.000
81	A	81	PRO	0	0.049	0.021	15.137	-0.063	-0.063	0.000	0.000	0.000	0.000
82	A	82	VAL	0	-0.017	-0.006	12.533	-0.460	-0.460	0.000	0.000	0.000	0.000
83	A	83	ALA	0	-0.013	-0.005	15.295	0.096	0.096	0.000	0.000	0.000	0.000
84	A	84	ALA	0	0.008	0.005	18.744	0.417	0.417	0.000	0.000	0.000	0.000
85	A	85	ILE	0	0.021	0.006	13.013	0.215	0.215	0.000	0.000	0.000	0.000
86	A	86	TYR	0	-0.005	-0.001	16.782	0.233	0.233	0.000	0.000	0.000	0.000
87	A	87	ALA	0	-0.013	-0.002	18.148	0.409	0.409	0.000	0.000	0.000	0.000
88	A	88	GLN	0	-0.007	0.012	18.210	-0.163	-0.163	0.000	0.000	0.000	0.000
89	A	89	ILE	0	0.000	0.014	14.069	0.353	0.353	0.000	0.000	0.000	0.000
90	A	90	ARG	1	0.860	0.917	18.675	13.695	13.695	0.000	0.000	0.000	0.000
91	A	91	SER	0	-0.049	-0.033	21.728	0.565	0.565	0.000	0.000	0.000	0.000
92	A	92	TYR	0	0.028	0.034	20.686	0.479	0.479	0.000	0.000	0.000	0.000
93	A	93	ALA	0	0.049	0.016	21.026	0.397	0.397	0.000	0.000	0.000	0.000
94	A	94	LYS	1	0.933	0.966	22.946	11.393	11.393	0.000	0.000	0.000	0.000
95	A	95	THR	0	-0.045	-0.040	26.182	0.378	0.378	0.000	0.000	0.000	0.000
96	A	96	HIS	0	-0.057	-0.018	24.704	0.424	0.424	0.000	0.000	0.000	0.000
97	A	97	GLY	0	-0.014	-0.008	26.531	-0.185	-0.185	0.000	0.000	0.000	0.000
98	A	98	LYS	1	0.900	0.966	21.716	13.309	13.309	0.000	0.000	0.000	0.000
99	A	99	GLU	-1	-0.974	-0.975	24.037	-11.876	-11.876	0.000	0.000	0.000	0.000
100	A	100	ILE	0	0.037	0.004	18.501	-0.598	-0.598	0.000	0.000	0.000	0.000
101	A	101	ALA	0	0.000	0.017	21.591	0.708	0.708	0.000	0.000	0.000	0.000
102	A	102	ALA	0	-0.030	-0.024	21.037	-0.452	-0.452	0.000	0.000	0.000	0.000
103	A	103	ALA	0	0.068	0.028	19.399	-0.501	-0.501	0.000	0.000	0.000	0.000
104	A	104	ASP	-1	-0.780	-0.877	16.840	-16.589	-16.589	0.000	0.000	0.000	0.000
105	A	105	GLY	0	0.022	0.010	15.855	-1.162	-1.162	0.000	0.000	0.000	0.000
106	A	106	TYR	0	-0.019	-0.013	16.041	-0.480	-0.480	0.000	0.000	0.000	0.000
107	A	107	ILE	0	0.024	0.037	11.810	-1.121	-1.121	0.000	0.000	0.000	0.000
108	A	108	ALA	0	0.028	0.007	11.312	-2.130	-2.130	0.000	0.000	0.000	0.000
109	A	109	ALA	0	0.004	0.006	11.452	-1.490	-1.490	0.000	0.000	0.000	0.000
110	A	110	THR	0	-0.039	-0.033	9.065	-0.525	-0.525	0.000	0.000	0.000	0.000
111	A	111	ALA	0	0.021	0.010	7.202	-1.616	-1.616	0.000	0.000	0.000	0.000
112	A	112	LYS	1	0.859	0.930	7.078	18.405	18.405	0.000	0.000	0.000	0.000
113	A	113	GLN	0	-0.027	-0.016	9.260	-1.311	-1.311	0.000	0.000	0.000	0.000
114	A	114	HIS	1	0.863	0.928	5.686	27.789	27.789	0.000	0.000	0.000	0.000
118	A	118	VAL	0	-0.016	-0.014	5.906	-2.499	-2.499	0.000	0.000	0.000	0.000
119	A	119	ALA	0	0.010	0.013	8.313	1.210	1.210	0.000	0.000	0.000	0.000
120	A	120	THR	0	-0.031	-0.070	10.014	1.910	1.910	0.000	0.000	0.000	0.000
121	A	121	ARG	1	0.938	0.973	13.820	14.733	14.733	0.000	0.000	0.000	0.000
122	A	122	ASP	-1	-0.900	-0.945	17.170	-14.952	-14.952	0.000	0.000	0.000	0.000
123	A	123	THR	0	-0.004	-0.016	14.345	0.189	0.189	0.000	0.000	0.000	0.000
124	A	124	GLY	0	0.011	0.020	16.702	-0.301	-0.301	0.000	0.000	0.000	0.000
125	A	125	SER	0	0.003	-0.032	18.257	0.139	0.139	0.000	0.000	0.000	0.000
126	A	126	PHE	0	0.013	-0.008	13.253	-0.447	-0.447	0.000	0.000	0.000	0.000
127	A	127	PHE	0	0.015	-0.002	14.723	-0.807	-0.807	0.000	0.000	0.000	0.000
128	A	128	ALA	0	-0.021	-0.009	16.617	0.253	0.253	0.000	0.000	0.000	0.000
129	A	129	ALA	0	0.013	0.005	14.963	0.609	0.609	0.000	0.000	0.000	0.000
130	A	130	ASP	-1	-0.925	-0.958	15.212	-17.628	-17.628	0.000	0.000	0.000	0.000
131	A	131	VAL	0	-0.038	-0.022	9.438	-1.060	-1.060	0.000	0.000	0.000	0.000
132	A	132	ALA	0	0.021	0.026	7.469	1.096	1.096	0.000	0.000	0.000	0.000
133	A	133	VAL	0	-0.015	-0.017	9.088	-1.748	-1.748	0.000	0.000	0.000	0.000
134	A	134	PHE	0	0.003	0.005	8.939	-0.801	-0.801	0.000	0.000	0.000	0.000
135	A	135	ASN	0	0.036	0.022	10.693	0.518	0.518	0.000	0.000	0.000	0.000
136	A	136	PRO	0	0.028	0.022	12.252	0.801	0.801	0.000	0.000	0.000	0.000
137	A	137	TRP	0	-0.007	-0.010	13.963	0.986	0.986	0.000	0.000	0.000	0.000
138	A	138	HIS	0	-0.089	-0.034	15.977	1.428	1.428	0.000	0.000	0.000	0.000
139	A	139	LEU	-1	-0.895	-0.944	13.851	-21.837	-21.837	0.000	0.000	0.000	0.000

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