FMO DATABASE

FMODB ID: ZZ64N

Calculation Name: 1VHS-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1VHS

Chain ID: A

ChEMBL ID:

UniProt ID: P71043

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	165
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1661007.038885
FMO2-HF: Nuclear repulsion	1596016.925688
FMO2-HF: Total energy	-64990.113198
FMO2-MP2: Total energy	-65180.219899

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:0:SER)

Summations of interaction energy for fragment #1(A:0:SER)

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.
-215.829	-215.003	23.033	-13.613	-10.248	-0.149

Interaction energy analysis for fragmet #1(A:0:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.731 / q_NPA : 0.846

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	2	THR	0	0.024	0.024	3.862	5.572	7.816	-0.023	-1.147	-1.075	-0.004
58	A	57	ASP	-1	-0.773	-0.879	3.638	-51.688	-51.381	0.000	-0.094	-0.212	0.000
59	A	58	GLU	-1	-0.852	-0.932	1.831	-146.829	-148.790	23.054	-12.308	-8.786	-0.145
60	A	59	ASN	0	-0.112	-0.061	4.099	8.615	8.851	0.002	-0.064	-0.175	0.000
4	A	3	LEU	0	-0.032	-0.011	6.166	1.307	1.307	0.000	0.000	0.000	0.000
5	A	4	ARG	1	0.761	0.843	9.736	23.474	23.474	0.000	0.000	0.000	0.000
6	A	5	LEU	0	0.015	-0.002	12.891	-0.010	-0.010	0.000	0.000	0.000	0.000
7	A	6	ALA	0	-0.016	0.000	15.935	-0.701	-0.701	0.000	0.000	0.000	0.000
8	A	7	GLU	-1	-0.906	-0.966	17.440	-16.554	-16.554	0.000	0.000	0.000	0.000
9	A	8	HIS	0	-0.021	-0.017	19.488	-0.501	-0.501	0.000	0.000	0.000	0.000
10	A	9	ARG	1	0.942	0.967	15.574	18.271	18.271	0.000	0.000	0.000	0.000
11	A	10	ASP	-1	-0.732	-0.830	15.906	-20.380	-20.380	0.000	0.000	0.000	0.000
12	A	11	LEU	0	-0.040	-0.009	17.818	-0.517	-0.517	0.000	0.000	0.000	0.000
13	A	12	GLU	-1	-0.880	-0.956	17.775	-17.868	-17.868	0.000	0.000	0.000	0.000
14	A	13	ALA	0	0.074	0.053	14.289	0.026	0.026	0.000	0.000	0.000	0.000
15	A	14	VAL	0	-0.034	-0.026	16.073	-0.580	-0.580	0.000	0.000	0.000	0.000
16	A	15	VAL	0	0.020	0.016	17.403	0.018	0.018	0.000	0.000	0.000	0.000
17	A	16	ALA	0	0.010	0.014	16.953	0.333	0.333	0.000	0.000	0.000	0.000
18	A	17	ILE	0	-0.034	-0.014	12.331	0.071	0.071	0.000	0.000	0.000	0.000
19	A	18	TYR	0	-0.086	-0.052	16.181	0.018	0.018	0.000	0.000	0.000	0.000
20	A	19	ASN	0	0.056	0.003	19.385	0.579	0.579	0.000	0.000	0.000	0.000
21	A	20	SER	0	-0.085	-0.045	16.399	0.096	0.096	0.000	0.000	0.000	0.000
22	A	21	THR	0	-0.045	-0.039	17.052	0.464	0.464	0.000	0.000	0.000	0.000
23	A	22	ILE	0	-0.001	0.027	19.486	0.392	0.392	0.000	0.000	0.000	0.000
24	A	23	ALA	0	-0.013	-0.004	21.962	0.588	0.588	0.000	0.000	0.000	0.000
25	A	24	SER	0	-0.074	-0.049	20.471	0.384	0.384	0.000	0.000	0.000	0.000
26	A	25	ARG	1	0.843	0.898	22.607	11.422	11.422	0.000	0.000	0.000	0.000
27	A	26	MET	0	-0.029	0.000	20.842	0.633	0.633	0.000	0.000	0.000	0.000
28	A	27	VAL	0	-0.023	-0.030	18.992	-0.059	-0.059	0.000	0.000	0.000	0.000
29	A	28	THR	0	0.042	0.049	22.359	0.428	0.428	0.000	0.000	0.000	0.000
30	A	29	ALA	0	-0.007	-0.017	24.053	0.235	0.235	0.000	0.000	0.000	0.000
31	A	30	ASP	-1	-0.845	-0.871	26.201	-11.198	-11.198	0.000	0.000	0.000	0.000
32	A	31	THR	0	0.009	-0.023	26.891	-0.270	-0.270	0.000	0.000	0.000	0.000
33	A	32	GLU	-1	-0.945	-0.978	28.596	-10.462	-10.462	0.000	0.000	0.000	0.000
34	A	33	PRO	0	-0.069	-0.028	25.034	-0.238	-0.238	0.000	0.000	0.000	0.000
35	A	34	VAL	0	0.019	0.017	24.978	0.414	0.414	0.000	0.000	0.000	0.000
36	A	35	THR	0	-0.012	-0.036	25.395	-0.533	-0.533	0.000	0.000	0.000	0.000
37	A	36	PRO	0	0.001	-0.019	23.541	-0.151	-0.151	0.000	0.000	0.000	0.000
38	A	37	GLU	-1	-0.875	-0.951	25.365	-11.520	-11.520	0.000	0.000	0.000	0.000
39	A	38	ASP	-1	-0.838	-0.883	28.335	-10.481	-10.481	0.000	0.000	0.000	0.000
40	A	39	ARG	1	0.892	0.952	23.899	12.812	12.812	0.000	0.000	0.000	0.000
41	A	40	MET	0	0.020	0.028	26.077	-0.497	-0.497	0.000	0.000	0.000	0.000
42	A	41	GLU	-1	-0.897	-0.948	27.522	-10.011	-10.011	0.000	0.000	0.000	0.000
43	A	42	TRP	0	-0.078	-0.048	20.538	-0.187	-0.187	0.000	0.000	0.000	0.000
44	A	43	PHE	0	-0.026	-0.019	19.806	-0.262	-0.262	0.000	0.000	0.000	0.000
45	A	44	SER	0	0.006	-0.019	24.723	-0.266	-0.266	0.000	0.000	0.000	0.000
46	A	45	GLY	0	-0.020	0.005	27.313	0.205	0.205	0.000	0.000	0.000	0.000
47	A	46	HIS	1	0.770	0.899	22.735	13.661	13.661	0.000	0.000	0.000	0.000
48	A	47	THR	0	-0.015	-0.013	25.719	0.099	0.099	0.000	0.000	0.000	0.000
49	A	48	GLU	-1	-0.924	-0.969	23.988	-12.079	-12.079	0.000	0.000	0.000	0.000
50	A	49	SER	0	0.000	0.003	23.443	-0.440	-0.440	0.000	0.000	0.000	0.000
51	A	50	ARG	1	0.752	0.860	24.164	11.439	11.439	0.000	0.000	0.000	0.000
52	A	51	PRO	0	0.089	0.063	19.951	0.116	0.116	0.000	0.000	0.000	0.000
53	A	52	LEU	0	0.015	0.003	18.080	-0.145	-0.145	0.000	0.000	0.000	0.000
54	A	53	TYR	0	-0.017	-0.012	13.999	0.115	0.115	0.000	0.000	0.000	0.000
55	A	54	VAL	0	0.031	0.009	12.423	-0.024	-0.024	0.000	0.000	0.000	0.000
56	A	55	ALA	0	-0.032	-0.021	7.769	-0.379	-0.379	0.000	0.000	0.000	0.000
57	A	56	GLU	-1	-0.814	-0.898	7.600	-28.266	-28.266	0.000	0.000	0.000	0.000
61	A	60	GLY	0	0.012	0.021	6.967	4.627	4.627	0.000	0.000	0.000	0.000
62	A	61	ASN	0	-0.074	-0.047	8.034	6.350	6.350	0.000	0.000	0.000	0.000
63	A	62	VAL	0	-0.009	-0.002	8.172	-4.105	-4.105	0.000	0.000	0.000	0.000
64	A	63	ALA	0	0.044	0.022	7.208	1.113	1.113	0.000	0.000	0.000	0.000
65	A	64	ALA	0	-0.052	-0.045	9.257	1.301	1.301	0.000	0.000	0.000	0.000
66	A	65	TRP	0	-0.015	-0.002	11.191	-0.215	-0.215	0.000	0.000	0.000	0.000
67	A	66	ILE	0	-0.043	-0.014	12.250	0.283	0.283	0.000	0.000	0.000	0.000
68	A	67	SER	0	-0.041	-0.033	15.843	0.342	0.342	0.000	0.000	0.000	0.000
69	A	68	PHE	0	0.004	-0.006	17.683	0.176	0.176	0.000	0.000	0.000	0.000
70	A	69	GLU	-1	-0.751	-0.833	22.116	-13.102	-13.102	0.000	0.000	0.000	0.000
71	A	70	THR	0	-0.016	-0.023	25.634	0.134	0.134	0.000	0.000	0.000	0.000
72	A	71	PHE	0	0.002	0.024	29.237	0.218	0.218	0.000	0.000	0.000	0.000
73	A	72	TYR	0	-0.006	-0.019	30.996	0.366	0.366	0.000	0.000	0.000	0.000
74	A	73	GLY	0	0.046	0.041	34.442	-0.064	-0.064	0.000	0.000	0.000	0.000
75	A	74	ARG	1	0.938	0.958	36.018	7.971	7.971	0.000	0.000	0.000	0.000
76	A	75	PRO	0	0.048	0.009	36.940	-0.140	-0.140	0.000	0.000	0.000	0.000
77	A	76	ALA	0	-0.060	-0.023	36.973	-0.109	-0.109	0.000	0.000	0.000	0.000
78	A	77	TYR	0	0.026	-0.001	33.819	0.078	0.078	0.000	0.000	0.000	0.000
79	A	78	ASN	0	0.037	0.032	32.595	-0.336	-0.336	0.000	0.000	0.000	0.000
80	A	79	LYS	1	0.941	0.979	30.405	8.765	8.765	0.000	0.000	0.000	0.000
81	A	80	THR	0	-0.013	-0.003	29.840	-0.152	-0.152	0.000	0.000	0.000	0.000
82	A	81	ALA	0	-0.011	-0.003	25.813	0.129	0.129	0.000	0.000	0.000	0.000
83	A	82	GLU	-1	-0.864	-0.937	25.094	-11.219	-11.219	0.000	0.000	0.000	0.000
84	A	83	VAL	0	-0.018	-0.018	18.362	-0.336	-0.336	0.000	0.000	0.000	0.000
85	A	84	SER	0	-0.021	-0.008	20.348	-0.082	-0.082	0.000	0.000	0.000	0.000
86	A	85	ILE	0	-0.012	-0.018	13.931	-0.595	-0.595	0.000	0.000	0.000	0.000
87	A	86	TYR	0	0.021	0.018	15.484	0.653	0.653	0.000	0.000	0.000	0.000
88	A	87	ILE	0	-0.012	-0.019	9.898	-1.658	-1.658	0.000	0.000	0.000	0.000
89	A	88	ASP	-1	-0.757	-0.871	10.865	-22.586	-22.586	0.000	0.000	0.000	0.000
90	A	89	GLU	-1	-0.824	-0.898	12.096	-19.543	-19.543	0.000	0.000	0.000	0.000
91	A	90	ALA	0	-0.007	0.005	12.023	-0.158	-0.158	0.000	0.000	0.000	0.000
92	A	91	CYS	0	-0.039	-0.022	6.978	-2.504	-2.504	0.000	0.000	0.000	0.000
93	A	92	ARG	1	0.795	0.891	9.105	18.963	18.963	0.000	0.000	0.000	0.000
94	A	93	GLY	0	-0.016	-0.016	11.277	-0.449	-0.449	0.000	0.000	0.000	0.000
95	A	94	LYS	1	0.869	0.927	6.661	31.207	31.207	0.000	0.000	0.000	0.000
96	A	95	GLY	0	0.005	0.003	6.986	-3.963	-3.963	0.000	0.000	0.000	0.000
97	A	96	VAL	0	0.038	0.017	5.883	1.685	1.685	0.000	0.000	0.000	0.000
98	A	97	GLY	0	0.039	0.010	8.209	0.879	0.879	0.000	0.000	0.000	0.000
99	A	98	SER	0	-0.041	-0.014	10.774	1.899	1.899	0.000	0.000	0.000	0.000
100	A	99	TYR	0	0.011	0.012	5.918	2.249	2.249	0.000	0.000	0.000	0.000
101	A	100	LEU	0	0.048	0.015	8.965	1.273	1.273	0.000	0.000	0.000	0.000
102	A	101	LEU	0	0.000	0.012	11.206	1.477	1.477	0.000	0.000	0.000	0.000
103	A	102	GLN	0	-0.032	-0.019	11.020	1.549	1.549	0.000	0.000	0.000	0.000
104	A	103	GLU	-1	-0.787	-0.880	9.791	-21.731	-21.731	0.000	0.000	0.000	0.000
105	A	104	ALA	0	0.000	0.003	13.190	1.126	1.126	0.000	0.000	0.000	0.000
106	A	105	LEU	0	-0.036	-0.031	16.149	1.190	1.190	0.000	0.000	0.000	0.000
107	A	106	ARG	1	0.826	0.904	12.148	20.830	20.830	0.000	0.000	0.000	0.000
108	A	107	ILE	0	-0.020	-0.006	13.955	0.624	0.624	0.000	0.000	0.000	0.000
109	A	108	ALA	0	0.017	0.005	18.008	0.757	0.757	0.000	0.000	0.000	0.000
110	A	109	PRO	0	0.027	0.004	20.628	0.632	0.632	0.000	0.000	0.000	0.000
111	A	110	ASN	0	-0.033	-0.013	20.538	0.196	0.196	0.000	0.000	0.000	0.000
112	A	111	LEU	0	-0.029	0.016	20.425	0.275	0.275	0.000	0.000	0.000	0.000
113	A	112	GLY	0	0.003	0.011	23.851	0.442	0.442	0.000	0.000	0.000	0.000
114	A	113	ILE	0	-0.091	-0.041	23.172	0.429	0.429	0.000	0.000	0.000	0.000
115	A	114	ARG	1	0.938	0.988	26.561	9.090	9.090	0.000	0.000	0.000	0.000
116	A	115	SER	0	-0.003	-0.008	28.313	-0.052	-0.052	0.000	0.000	0.000	0.000
117	A	116	LEU	0	0.007	0.008	21.047	-0.013	-0.013	0.000	0.000	0.000	0.000
118	A	117	MET	0	-0.026	-0.020	25.746	0.237	0.237	0.000	0.000	0.000	0.000
119	A	118	ALA	0	0.044	0.024	22.032	-0.473	-0.473	0.000	0.000	0.000	0.000
120	A	119	PHE	0	0.013	0.010	23.893	0.469	0.469	0.000	0.000	0.000	0.000
121	A	120	ILE	0	0.008	0.000	21.702	-0.538	-0.538	0.000	0.000	0.000	0.000
122	A	121	PHE	0	0.043	0.025	24.920	0.577	0.577	0.000	0.000	0.000	0.000
123	A	122	GLY	0	0.003	0.001	26.245	-0.291	-0.291	0.000	0.000	0.000	0.000
124	A	123	HIS	0	-0.006	-0.017	26.179	0.299	0.299	0.000	0.000	0.000	0.000
125	A	124	ASN	0	0.051	0.036	20.100	-0.545	-0.545	0.000	0.000	0.000	0.000
126	A	125	LYS	1	0.890	0.929	23.036	10.741	10.741	0.000	0.000	0.000	0.000
127	A	126	PRO	0	-0.008	-0.007	18.489	0.008	0.008	0.000	0.000	0.000	0.000
128	A	127	SER	0	0.021	0.002	18.911	-0.746	-0.746	0.000	0.000	0.000	0.000
129	A	128	LEU	0	0.005	0.010	19.864	0.025	0.025	0.000	0.000	0.000	0.000
130	A	129	LYS	1	0.843	0.890	21.642	11.885	11.885	0.000	0.000	0.000	0.000
131	A	130	LEU	0	-0.044	-0.006	14.967	-0.039	-0.039	0.000	0.000	0.000	0.000
132	A	131	PHE	0	0.081	0.028	18.142	-0.258	-0.258	0.000	0.000	0.000	0.000
133	A	132	GLU	-1	-0.821	-0.888	20.815	-11.520	-11.520	0.000	0.000	0.000	0.000
134	A	133	LYS	1	0.884	0.942	19.072	15.579	15.579	0.000	0.000	0.000	0.000
135	A	134	HIS	0	-0.037	-0.011	15.678	-0.604	-0.604	0.000	0.000	0.000	0.000
136	A	135	GLY	0	0.001	0.004	20.602	0.111	0.111	0.000	0.000	0.000	0.000
137	A	136	PHE	0	-0.039	-0.016	20.623	0.255	0.255	0.000	0.000	0.000	0.000
138	A	137	ALA	0	0.004	-0.001	25.245	0.048	0.048	0.000	0.000	0.000	0.000
139	A	138	GLU	-1	-0.825	-0.901	28.681	-10.175	-10.175	0.000	0.000	0.000	0.000
140	A	139	TRP	0	-0.001	-0.006	30.011	0.295	0.295	0.000	0.000	0.000	0.000
141	A	140	GLY	0	0.011	0.005	32.019	0.344	0.344	0.000	0.000	0.000	0.000
142	A	141	LEU	0	-0.044	-0.001	32.117	-0.380	-0.380	0.000	0.000	0.000	0.000
143	A	142	PHE	0	-0.001	-0.004	33.367	0.343	0.343	0.000	0.000	0.000	0.000
144	A	143	PRO	0	0.013	0.000	34.640	-0.223	-0.223	0.000	0.000	0.000	0.000
145	A	144	GLY	0	0.016	-0.009	35.531	0.197	0.197	0.000	0.000	0.000	0.000
146	A	145	ILE	0	-0.039	-0.012	33.416	0.186	0.186	0.000	0.000	0.000	0.000
147	A	146	ALA	0	0.024	0.035	31.492	0.018	0.018	0.000	0.000	0.000	0.000
148	A	147	GLU	-1	-0.953	-0.991	33.486	-8.195	-8.195	0.000	0.000	0.000	0.000
149	A	148	MET	0	0.017	0.013	27.732	-0.243	-0.243	0.000	0.000	0.000	0.000
150	A	149	ASP	-1	-0.807	-0.878	31.293	-10.137	-10.137	0.000	0.000	0.000	0.000
151	A	150	GLY	0	0.015	0.021	34.637	0.170	0.170	0.000	0.000	0.000	0.000
152	A	151	LYS	1	0.854	0.930	33.921	9.111	9.111	0.000	0.000	0.000	0.000
153	A	152	ARG	1	0.926	0.951	34.804	7.988	7.988	0.000	0.000	0.000	0.000
154	A	153	TYR	0	-0.021	-0.012	29.756	-0.126	-0.126	0.000	0.000	0.000	0.000
155	A	154	ASP	-1	-0.870	-0.927	31.866	-9.122	-9.122	0.000	0.000	0.000	0.000
156	A	155	LEU	0	-0.008	0.001	27.887	-0.425	-0.425	0.000	0.000	0.000	0.000
157	A	156	LYS	1	0.805	0.879	28.227	10.619	10.619	0.000	0.000	0.000	0.000
158	A	157	ILE	0	0.000	0.013	28.088	-0.402	-0.402	0.000	0.000	0.000	0.000
159	A	158	LEU	0	-0.002	-0.001	24.257	0.271	0.271	0.000	0.000	0.000	0.000
160	A	159	GLY	0	0.038	0.002	26.162	-0.316	-0.316	0.000	0.000	0.000	0.000
161	A	160	ARG	1	0.893	0.949	21.444	13.047	13.047	0.000	0.000	0.000	0.000
162	A	161	GLU	-1	-0.915	-0.956	26.824	-9.554	-9.554	0.000	0.000	0.000	0.000
163	A	162	LEU	0	-0.081	-0.058	23.049	-0.282	-0.282	0.000	0.000	0.000	0.000
164	A	163	SER	0	-0.077	-0.047	26.462	-0.109	-0.109	0.000	0.000	0.000	0.000
165	A	164	GLU	-2	-1.867	-1.913	29.264	-18.806	-18.806	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:SER)