FMO DATABASE

FMODB ID: VY8Y1

Calculation Name: 1H7C-A-Xray547

Preferred Name:

Target Type:

Ligand Name: sulfate ion | acetic acid

Ligand 3-letter code: SO4 | ACY

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1H7C

Chain ID: A

ChEMBL ID:

UniProt ID: O75347

Base Structure: X-ray

Registration Date: 2025-10-05

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	103
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-775275.552819
FMO2-HF: Nuclear repulsion	731340.73543
FMO2-HF: Total energy	-43934.81739
FMO2-MP2: Total energy	-44061.140841

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:PRO)

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

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.
-41.684	-37.984	0.033	-1.508	-2.225	-0.007

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.875 / q_NPA : 0.912

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

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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	6	VAL	0	0.096	0.059	3.150	0.997	3.926	0.017	-1.275	-1.671	-0.007
4	A	7	ARG	1	0.936	0.971	3.509	47.066	47.837	0.016	-0.233	-0.554	0.000
5	A	8	GLN	0	0.002	0.010	5.198	7.675	7.675	0.000	0.000	0.000	0.000
6	A	9	ILE	0	0.070	0.048	7.085	3.857	3.857	0.000	0.000	0.000	0.000
7	A	10	LYS	1	0.976	1.003	8.163	26.807	26.807	0.000	0.000	0.000	0.000
8	A	11	ILE	0	-0.032	-0.023	8.673	2.885	2.885	0.000	0.000	0.000	0.000
9	A	12	LYS	0	0.043	0.030	10.839	2.401	2.401	0.000	0.000	0.000	0.000
10	A	13	THR	0	0.043	0.008	12.456	2.237	2.237	0.000	0.000	0.000	0.000
11	A	14	GLY	0	-0.046	-0.024	13.866	1.546	1.546	0.000	0.000	0.000	0.000
12	A	15	VAL	0	-0.038	-0.023	14.766	1.332	1.332	0.000	0.000	0.000	0.000
13	A	16	VAL	0	0.065	0.036	17.018	1.121	1.121	0.000	0.000	0.000	0.000
14	A	17	ARG	1	0.900	0.951	16.620	18.145	18.145	0.000	0.000	0.000	0.000
15	A	18	ARG	1	0.895	0.955	17.910	16.517	16.517	0.000	0.000	0.000	0.000
16	A	19	LEU	0	0.060	0.031	20.376	0.700	0.700	0.000	0.000	0.000	0.000
17	A	20	VAL	0	0.035	0.030	23.061	0.680	0.680	0.000	0.000	0.000	0.000
18	A	21	LYS	1	0.894	0.945	24.438	12.793	12.793	0.000	0.000	0.000	0.000
19	A	22	GLU	-1	-0.908	-0.960	23.586	-12.490	-12.490	0.000	0.000	0.000	0.000
20	A	23	ARG	1	0.905	0.947	27.188	11.126	11.126	0.000	0.000	0.000	0.000
21	A	24	VAL	0	-0.009	-0.005	28.954	0.420	0.420	0.000	0.000	0.000	0.000
22	A	25	MET	0	-0.041	-0.013	30.300	0.371	0.371	0.000	0.000	0.000	0.000
23	A	26	TYR	0	0.067	0.014	29.328	0.447	0.447	0.000	0.000	0.000	0.000
24	A	27	GLU	-1	-0.813	-0.905	32.568	-9.571	-9.571	0.000	0.000	0.000	0.000
25	A	28	LYS	1	0.916	0.963	34.787	8.823	8.823	0.000	0.000	0.000	0.000
26	A	29	GLU	-1	-0.879	-0.923	36.340	-8.275	-8.275	0.000	0.000	0.000	0.000
27	A	30	ALA	0	0.039	0.014	37.736	0.272	0.272	0.000	0.000	0.000	0.000
28	A	31	LYS	1	0.876	0.935	39.172	7.836	7.836	0.000	0.000	0.000	0.000
29	A	32	GLN	0	-0.037	-0.019	40.820	0.056	0.056	0.000	0.000	0.000	0.000
30	A	33	GLN	0	-0.041	-0.023	42.412	0.210	0.210	0.000	0.000	0.000	0.000
31	A	34	GLU	-1	-0.897	-0.957	43.626	-6.717	-6.717	0.000	0.000	0.000	0.000
32	A	35	GLU	-1	-0.819	-0.911	44.850	-6.922	-6.922	0.000	0.000	0.000	0.000
33	A	36	LYS	1	0.819	0.915	47.020	6.762	6.762	0.000	0.000	0.000	0.000
34	A	37	ILE	0	0.015	0.004	46.629	0.176	0.176	0.000	0.000	0.000	0.000
35	A	38	GLU	-1	-0.956	-0.982	47.426	-6.591	-6.591	0.000	0.000	0.000	0.000
36	A	39	LYS	1	0.851	0.935	48.775	6.687	6.687	0.000	0.000	0.000	0.000
37	A	40	MET	0	0.051	0.028	52.876	0.040	0.040	0.000	0.000	0.000	0.000
38	A	41	ARG	1	0.865	0.936	49.492	6.408	6.408	0.000	0.000	0.000	0.000
39	A	42	ALA	0	-0.045	-0.018	55.645	0.092	0.092	0.000	0.000	0.000	0.000
40	A	43	GLU	-1	-0.997	-0.986	56.663	-5.602	-5.602	0.000	0.000	0.000	0.000
41	A	44	ASP	-1	-0.915	-0.970	58.129	-5.425	-5.425	0.000	0.000	0.000	0.000
42	A	45	GLY	0	0.005	0.023	58.147	0.060	0.060	0.000	0.000	0.000	0.000
43	A	46	GLU	-1	-0.841	-0.925	54.049	-6.099	-6.099	0.000	0.000	0.000	0.000
44	A	47	ASN	0	0.002	-0.010	57.048	0.095	0.095	0.000	0.000	0.000	0.000
45	A	48	TYR	0	-0.009	0.002	56.167	-0.125	-0.125	0.000	0.000	0.000	0.000
46	A	49	ASP	-1	-0.851	-0.937	54.834	-5.781	-5.781	0.000	0.000	0.000	0.000
47	A	50	ILE	0	-0.007	-0.004	51.559	-0.165	-0.165	0.000	0.000	0.000	0.000
48	A	51	LYS	1	0.779	0.878	50.706	5.759	5.759	0.000	0.000	0.000	0.000
49	A	52	LYS	1	1.036	1.021	49.507	6.069	6.069	0.000	0.000	0.000	0.000
50	A	53	GLN	0	-0.002	0.006	48.140	-0.266	-0.266	0.000	0.000	0.000	0.000
51	A	54	ALA	0	0.070	0.028	46.410	-0.186	-0.186	0.000	0.000	0.000	0.000
52	A	55	GLU	-1	-0.964	-0.983	44.959	-6.714	-6.714	0.000	0.000	0.000	0.000
53	A	56	ILE	0	0.011	0.003	43.184	-0.152	-0.152	0.000	0.000	0.000	0.000
54	A	57	LEU	0	-0.044	-0.011	41.795	-0.217	-0.217	0.000	0.000	0.000	0.000
55	A	58	GLN	0	-0.068	-0.041	40.665	-0.117	-0.117	0.000	0.000	0.000	0.000
56	A	59	GLU	-1	-0.913	-0.944	38.478	-7.998	-7.998	0.000	0.000	0.000	0.000
57	A	60	SER	0	0.003	-0.013	35.693	-0.257	-0.257	0.000	0.000	0.000	0.000
58	A	61	ARG	1	0.940	0.959	35.611	7.455	7.455	0.000	0.000	0.000	0.000
59	A	62	MET	0	-0.055	-0.028	35.729	-0.018	-0.018	0.000	0.000	0.000	0.000
60	A	63	MET	0	0.018	0.020	30.693	-0.142	-0.142	0.000	0.000	0.000	0.000
61	A	64	ILE	0	0.005	0.020	31.437	-0.380	-0.380	0.000	0.000	0.000	0.000
62	A	65	PRO	0	0.002	-0.002	31.419	-0.321	-0.321	0.000	0.000	0.000	0.000
63	A	66	ASP	-1	-0.807	-0.867	28.149	-11.412	-11.412	0.000	0.000	0.000	0.000
64	A	67	CYS	0	-0.023	-0.014	27.077	-0.500	-0.500	0.000	0.000	0.000	0.000
65	A	68	GLN	0	-0.020	-0.019	26.586	-0.398	-0.398	0.000	0.000	0.000	0.000
66	A	69	ARG	1	0.903	0.951	27.065	9.668	9.668	0.000	0.000	0.000	0.000
67	A	70	ARG	1	0.825	0.887	23.145	11.525	11.525	0.000	0.000	0.000	0.000
68	A	71	LEU	0	-0.023	-0.010	22.299	-0.678	-0.678	0.000	0.000	0.000	0.000
69	A	72	GLU	-1	-0.855	-0.929	22.557	-12.845	-12.845	0.000	0.000	0.000	0.000
70	A	73	ALA	0	-0.009	-0.006	21.465	-0.474	-0.474	0.000	0.000	0.000	0.000
71	A	74	ALA	0	-0.015	-0.017	18.254	-0.804	-0.804	0.000	0.000	0.000	0.000
72	A	75	TYR	0	-0.013	-0.008	17.978	-1.175	-1.175	0.000	0.000	0.000	0.000
73	A	76	LEU	0	0.039	0.014	19.369	-0.686	-0.686	0.000	0.000	0.000	0.000
74	A	77	ASP	-1	-0.883	-0.922	14.459	-21.114	-21.114	0.000	0.000	0.000	0.000
75	A	78	LEU	0	0.011	-0.012	13.374	-1.329	-1.329	0.000	0.000	0.000	0.000
76	A	79	GLN	0	-0.043	-0.026	15.210	-0.767	-0.767	0.000	0.000	0.000	0.000
77	A	80	ARG	1	0.863	0.922	13.003	19.829	19.829	0.000	0.000	0.000	0.000
78	A	81	ILE	0	-0.067	-0.035	10.360	-0.902	-0.902	0.000	0.000	0.000	0.000
79	A	82	LEU	0	-0.019	-0.011	12.262	-1.239	-1.239	0.000	0.000	0.000	0.000
80	A	83	GLU	-1	-0.899	-0.936	13.748	-15.792	-15.792	0.000	0.000	0.000	0.000
81	A	84	ASN	0	-0.053	-0.019	11.551	1.606	1.606	0.000	0.000	0.000	0.000
82	A	85	GLU	-1	-0.877	-0.938	7.259	-39.944	-39.944	0.000	0.000	0.000	0.000
83	A	86	LYS	1	0.926	0.945	10.636	15.822	15.822	0.000	0.000	0.000	0.000
84	A	87	ASP	-1	-0.791	-0.854	8.606	-30.442	-30.442	0.000	0.000	0.000	0.000
85	A	88	LEU	0	-0.066	-0.042	5.677	-2.425	-2.425	0.000	0.000	0.000	0.000
86	A	89	GLU	-1	-0.844	-0.911	9.740	-18.025	-18.025	0.000	0.000	0.000	0.000
87	A	90	GLU	-1	-0.839	-0.917	13.035	-17.109	-17.109	0.000	0.000	0.000	0.000
88	A	91	ALA	0	-0.063	-0.018	9.172	0.368	0.368	0.000	0.000	0.000	0.000
89	A	92	GLU	-1	-0.877	-0.932	11.186	-17.909	-17.909	0.000	0.000	0.000	0.000
90	A	93	GLU	-1	-0.935	-0.999	7.864	-31.005	-31.005	0.000	0.000	0.000	0.000
91	A	94	TYR	0	-0.034	-0.019	10.757	0.879	0.879	0.000	0.000	0.000	0.000
92	A	95	LYS	1	0.842	0.910	12.139	20.420	20.420	0.000	0.000	0.000	0.000
93	A	96	GLU	-1	-0.917	-0.964	13.986	-17.288	-17.288	0.000	0.000	0.000	0.000
94	A	97	ALA	0	-0.025	-0.013	12.982	0.955	0.955	0.000	0.000	0.000	0.000
95	A	98	ARG	1	0.820	0.897	15.043	15.890	15.890	0.000	0.000	0.000	0.000
96	A	99	LEU	0	0.047	0.036	17.740	0.757	0.757	0.000	0.000	0.000	0.000
97	A	100	VAL	0	-0.066	-0.030	17.628	0.766	0.766	0.000	0.000	0.000	0.000
98	A	101	LEU	0	-0.015	0.002	17.139	0.681	0.681	0.000	0.000	0.000	0.000
99	A	102	ASP	-1	-0.831	-0.936	20.497	-13.367	-13.367	0.000	0.000	0.000	0.000
100	A	103	SER	0	-0.050	-0.041	22.831	0.722	0.722	0.000	0.000	0.000	0.000
101	A	104	VAL	0	-0.083	-0.046	22.453	0.350	0.350	0.000	0.000	0.000	0.000
102	A	105	LYS	0	-0.074	-0.006	22.224	0.334	0.334	0.000	0.000	0.000	0.000
103	A	106	LEU	-1	-0.963	-0.952	27.141	-10.019	-10.019	0.000	0.000	0.000	0.000

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