FMO DATABASE

FMODB ID: 24Q1R

Calculation Name: 1VIP-A-Xray547

Preferred Name:

Target Type:

Ligand Name: sulfate ion

Ligand 3-letter code: SO4

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1VIP

Chain ID: A

ChEMBL ID:

UniProt ID: P81458

Base Structure: X-ray

Registration Date: 2025-10-03

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	114
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1011585.552842
FMO2-HF: Nuclear repulsion	960061.36209
FMO2-HF: Total energy	-51524.190752
FMO2-MP2: Total energy	-51661.526453

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:ASN)

Summations of interaction energy for fragment #1(A:1: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.
-59.034	-47.855	36.483	-21.052	-26.606	-0.133

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.794 / q_NPA : 0.901

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	PHE	0	0.009	0.023	2.365	1.621	4.809	3.357	-2.529	-4.016	0.021
4	A	4	GLN	0	0.038	0.020	1.979	-39.577	-38.722	12.887	-6.014	-7.727	-0.028
5	A	5	PHE	0	0.029	0.015	3.944	5.472	6.007	0.010	-0.195	-0.349	0.001
50	A	52	TYR	0	-0.019	-0.063	4.666	-2.586	-2.500	-0.001	-0.006	-0.078	0.000
59	A	69	LYS	1	1.035	1.013	2.871	15.726	17.962	0.241	-1.052	-1.425	-0.011
60	A	70	LEU	0	-0.018	-0.028	2.443	-13.780	-11.543	2.587	-2.173	-2.651	-0.027
61	A	71	SER	0	-0.026	0.000	3.087	-4.838	-2.994	0.377	-0.918	-1.303	-0.008
62	A	72	LEU	0	-0.007	0.011	1.779	-41.284	-42.382	11.213	-5.072	-5.043	-0.053
63	A	73	TYR	0	-0.028	-0.039	2.204	6.465	7.041	5.810	-2.705	-3.682	-0.025
64	A	74	SER	0	0.003	0.004	5.090	-0.197	-0.187	-0.001	-0.001	-0.008	0.000
83	A	95	VAL	0	0.003	0.001	3.913	0.291	0.424	0.000	-0.030	-0.102	0.000
85	A	99	ASP	-1	-0.749	-0.832	3.461	-62.717	-62.140	0.003	-0.357	-0.222	-0.003
6	A	6	ALA	0	0.013	0.004	5.621	5.477	5.477	0.000	0.000	0.000	0.000
7	A	7	GLU	-1	-0.843	-0.900	6.420	-32.701	-32.701	0.000	0.000	0.000	0.000
8	A	8	MET	0	-0.037	-0.020	5.784	3.806	3.806	0.000	0.000	0.000	0.000
9	A	9	ILE	0	0.031	0.021	9.616	2.762	2.762	0.000	0.000	0.000	0.000
10	A	10	VAL	0	-0.008	0.020	11.375	2.030	2.030	0.000	0.000	0.000	0.000
11	A	11	LYS	1	0.897	0.953	12.444	19.212	19.212	0.000	0.000	0.000	0.000
12	A	12	MET	0	-0.052	-0.018	12.926	1.292	1.292	0.000	0.000	0.000	0.000
13	A	13	THR	0	-0.016	-0.036	14.959	1.279	1.279	0.000	0.000	0.000	0.000
14	A	14	GLY	0	-0.005	0.011	16.881	0.949	0.949	0.000	0.000	0.000	0.000
15	A	16	LYS	1	0.888	0.961	16.964	15.144	15.144	0.000	0.000	0.000	0.000
16	A	17	ASN	0	0.038	0.008	14.270	-2.191	-2.191	0.000	0.000	0.000	0.000
17	A	18	PRO	0	0.060	0.020	10.389	0.771	0.771	0.000	0.000	0.000	0.000
18	A	19	LEU	0	-0.012	0.011	13.322	0.277	0.277	0.000	0.000	0.000	0.000
19	A	20	SER	0	-0.008	-0.012	14.711	0.449	0.449	0.000	0.000	0.000	0.000
20	A	21	SER	0	-0.051	-0.015	16.696	1.123	1.123	0.000	0.000	0.000	0.000
21	A	22	TYR	0	0.049	0.008	13.941	0.499	0.499	0.000	0.000	0.000	0.000
22	A	23	SER	0	-0.021	-0.011	13.957	-1.508	-1.508	0.000	0.000	0.000	0.000
23	A	24	ASP	-1	-0.812	-0.908	15.353	-14.187	-14.187	0.000	0.000	0.000	0.000
24	A	25	TYR	0	-0.052	-0.062	18.709	0.402	0.402	0.000	0.000	0.000	0.000
25	A	26	GLY	0	-0.021	0.000	19.582	-0.470	-0.470	0.000	0.000	0.000	0.000
26	A	27	CYS	0	-0.055	-0.008	21.518	0.326	0.326	0.000	0.000	0.000	0.000
27	A	28	TYR	0	-0.048	-0.040	16.750	-0.223	-0.223	0.000	0.000	0.000	0.000
28	A	29	CYS	0	-0.125	-0.018	13.887	-2.970	-2.970	0.000	0.000	0.000	0.000
29	A	30	GLY	0	0.050	0.022	13.447	0.579	0.579	0.000	0.000	0.000	0.000
30	A	31	TRP	0	-0.069	-0.026	14.496	-0.547	-0.547	0.000	0.000	0.000	0.000
31	A	32	GLY	0	0.019	0.017	16.758	1.024	1.024	0.000	0.000	0.000	0.000
32	A	33	GLY	0	-0.017	-0.017	17.988	-0.259	-0.259	0.000	0.000	0.000	0.000
33	A	34	LYS	1	0.909	0.956	18.570	12.065	12.065	0.000	0.000	0.000	0.000
34	A	35	GLY	0	0.030	0.028	22.403	0.041	0.041	0.000	0.000	0.000	0.000
35	A	36	LYS	1	0.871	0.940	24.067	10.668	10.668	0.000	0.000	0.000	0.000
36	A	37	PRO	0	-0.020	-0.011	21.237	0.099	0.099	0.000	0.000	0.000	0.000
37	A	38	GLN	0	-0.005	0.002	23.148	0.831	0.831	0.000	0.000	0.000	0.000
38	A	39	ASP	-1	-0.774	-0.860	22.475	-13.160	-13.160	0.000	0.000	0.000	0.000
39	A	40	ALA	0	0.017	0.004	22.286	-0.418	-0.418	0.000	0.000	0.000	0.000
40	A	41	THR	0	0.007	0.002	18.262	-0.924	-0.924	0.000	0.000	0.000	0.000
41	A	42	ASP	-1	-0.710	-0.873	17.805	-16.000	-16.000	0.000	0.000	0.000	0.000
42	A	43	ARG	1	0.837	0.910	18.517	12.637	12.637	0.000	0.000	0.000	0.000
43	A	44	CYS	0	0.016	0.033	14.907	1.134	1.134	0.000	0.000	0.000	0.000
44	A	46	PHE	0	0.064	0.034	14.411	-1.096	-1.096	0.000	0.000	0.000	0.000
45	A	47	VAL	0	0.009	0.000	14.718	-0.491	-0.491	0.000	0.000	0.000	0.000
46	A	48	HIS	1	0.787	0.891	6.963	32.268	32.268	0.000	0.000	0.000	0.000
47	A	49	ASP	-1	-0.853	-0.921	11.280	-25.636	-25.636	0.000	0.000	0.000	0.000
48	A	133	CYS	-1	-0.910	-0.947	12.858	-14.704	-14.704	0.000	0.000	0.000	0.000
49	A	51	CYS	0	-0.099	-0.028	7.710	2.388	2.388	0.000	0.000	0.000	0.000
51	A	53	GLU	-1	-0.901	-0.946	10.325	-22.689	-22.689	0.000	0.000	0.000	0.000
52	A	54	LYS	1	0.910	0.970	13.439	20.632	20.632	0.000	0.000	0.000	0.000
53	A	55	VAL	0	-0.051	-0.038	8.881	0.465	0.465	0.000	0.000	0.000	0.000
54	A	56	LYS	1	1.016	1.008	10.387	16.615	16.615	0.000	0.000	0.000	0.000
55	A	59	SER	0	0.009	0.000	11.202	-0.584	-0.584	0.000	0.000	0.000	0.000
56	A	61	CYS	0	-0.092	-0.039	8.073	0.516	0.516	0.000	0.000	0.000	0.000
57	A	67	LYS	1	0.988	0.990	7.360	22.091	22.091	0.000	0.000	0.000	0.000
58	A	68	PRO	0	0.041	0.032	5.222	-6.930	-6.930	0.000	0.000	0.000	0.000
65	A	75	TYR	0	-0.075	-0.089	5.971	0.971	0.971	0.000	0.000	0.000	0.000
66	A	76	SER	0	0.017	0.037	9.110	1.680	1.680	0.000	0.000	0.000	0.000
67	A	77	PHE	0	0.037	0.006	10.387	-0.045	-0.045	0.000	0.000	0.000	0.000
68	A	78	GLN	0	-0.013	-0.025	14.025	1.704	1.704	0.000	0.000	0.000	0.000
69	A	79	ASN	0	-0.003	-0.002	17.502	-0.170	-0.170	0.000	0.000	0.000	0.000
70	A	80	GLY	0	0.039	0.032	19.286	0.372	0.372	0.000	0.000	0.000	0.000
71	A	81	GLY	0	0.002	-0.006	16.032	0.057	0.057	0.000	0.000	0.000	0.000
72	A	82	ILE	0	0.002	-0.002	9.710	-0.344	-0.344	0.000	0.000	0.000	0.000
73	A	83	VAL	0	0.007	0.009	12.784	0.736	0.736	0.000	0.000	0.000	0.000
74	A	84	CYS	0	-0.024	0.005	5.154	-2.538	-2.538	0.000	0.000	0.000	0.000
75	A	85	GLY	0	0.012	0.002	10.647	2.300	2.300	0.000	0.000	0.000	0.000
76	A	87	ASP	-1	-0.814	-0.921	8.283	-33.352	-33.352	0.000	0.000	0.000	0.000
77	A	88	ASN	0	-0.021	-0.011	11.389	1.641	1.641	0.000	0.000	0.000	0.000
78	A	89	HIS	0	0.039	0.025	10.454	-0.772	-0.772	0.000	0.000	0.000	0.000
79	A	90	SER	0	0.054	0.018	10.757	-2.723	-2.723	0.000	0.000	0.000	0.000
80	A	92	LYS	1	0.932	0.970	6.216	37.220	37.220	0.000	0.000	0.000	0.000
81	A	93	ARG	1	0.863	0.920	6.647	19.204	19.204	0.000	0.000	0.000	0.000
82	A	94	ALA	0	-0.002	0.006	9.203	-0.095	-0.095	0.000	0.000	0.000	0.000
84	A	97	GLU	-1	-0.751	-0.870	6.052	-21.372	-21.372	0.000	0.000	0.000	0.000
86	A	100	ARG	1	0.861	0.899	7.032	25.916	25.916	0.000	0.000	0.000	0.000
87	A	101	VAL	0	-0.023	-0.008	9.611	2.317	2.317	0.000	0.000	0.000	0.000
88	A	102	ALA	0	0.015	0.023	10.074	1.625	1.625	0.000	0.000	0.000	0.000
89	A	103	ALA	0	0.005	-0.004	9.884	1.493	1.493	0.000	0.000	0.000	0.000
90	A	104	THR	0	-0.059	-0.038	11.866	1.737	1.737	0.000	0.000	0.000	0.000
91	A	106	PHE	0	0.002	-0.013	11.575	0.927	0.927	0.000	0.000	0.000	0.000
92	A	107	ARG	1	0.817	0.898	16.327	16.798	16.798	0.000	0.000	0.000	0.000
93	A	108	ASP	-1	-0.846	-0.910	18.146	-14.796	-14.796	0.000	0.000	0.000	0.000
94	A	109	ASN	0	-0.025	-0.022	19.583	1.327	1.327	0.000	0.000	0.000	0.000
95	A	110	LEU	0	-0.018	-0.011	19.585	0.316	0.316	0.000	0.000	0.000	0.000
96	A	111	ASN	0	-0.026	-0.009	22.403	-0.036	-0.036	0.000	0.000	0.000	0.000
97	A	112	THR	0	-0.021	-0.014	24.542	0.604	0.604	0.000	0.000	0.000	0.000
98	A	113	TYR	0	-0.090	-0.047	19.188	0.173	0.173	0.000	0.000	0.000	0.000
99	A	114	ASP	-1	-0.801	-0.912	23.797	-10.459	-10.459	0.000	0.000	0.000	0.000
100	A	115	LYS	1	0.921	0.944	24.104	11.958	11.958	0.000	0.000	0.000	0.000
101	A	116	LYS	1	0.884	0.963	26.549	10.314	10.314	0.000	0.000	0.000	0.000
102	A	117	TYR	0	-0.009	-0.006	23.652	0.291	0.291	0.000	0.000	0.000	0.000
103	A	118	HIS	0	-0.028	-0.010	20.801	-0.044	-0.044	0.000	0.000	0.000	0.000
104	A	119	ASN	0	-0.060	-0.027	22.813	0.294	0.294	0.000	0.000	0.000	0.000
105	A	120	TYR	0	-0.020	-0.008	23.575	0.788	0.788	0.000	0.000	0.000	0.000
106	A	121	PRO	0	0.035	0.009	25.406	-0.115	-0.115	0.000	0.000	0.000	0.000
107	A	122	PRO	0	0.051	0.010	25.159	0.092	0.092	0.000	0.000	0.000	0.000
108	A	124	SER	0	-0.041	-0.024	26.979	-0.053	-0.053	0.000	0.000	0.000	0.000
109	A	125	GLN	0	0.006	0.010	28.028	0.378	0.378	0.000	0.000	0.000	0.000
110	A	127	THR	0	-0.006	-0.014	26.519	-0.043	-0.043	0.000	0.000	0.000	0.000
111	A	128	GLY	0	0.008	0.002	28.342	-0.190	-0.190	0.000	0.000	0.000	0.000
112	A	129	THR	0	-0.053	-0.048	24.936	-0.345	-0.345	0.000	0.000	0.000	0.000
113	A	130	GLU	-1	-0.791	-0.868	23.005	-11.547	-11.547	0.000	0.000	0.000	0.000
114	A	131	GLN	0	-0.039	-0.019	23.207	0.013	0.013	0.000	0.000	0.000	0.000

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