FMO DATABASE

FMODB ID: VV481

Calculation Name: 2HQN-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2HQN

Chain ID: A

ChEMBL ID:

UniProt ID: Q9ZM42

Base Structure: SolutionNMR

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	109
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-863155.098623
FMO2-HF: Nuclear repulsion	819312.581517
FMO2-HF: Total energy	-43842.517105
FMO2-MP2: Total energy	-43969.813393

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:115:GLY)

Summations of interaction energy for fragment #1(A:115:GLY)

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.
-67.152	-65.999	-0.014	-0.526	-0.613	-0.003

Interaction energy analysis for fragmet #1(A:115:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.840 / q_NPA : 0.905

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	117	GLY	0	0.017	0.019	3.854	1.310	2.463	-0.014	-0.526	-0.613	-0.003
4	A	118	SER	0	0.067	0.026	6.985	0.931	0.931	0.000	0.000	0.000	0.000
5	A	119	ASN	0	-0.062	-0.019	9.239	-0.957	-0.957	0.000	0.000	0.000	0.000
6	A	120	VAL	0	0.024	0.011	9.486	1.042	1.042	0.000	0.000	0.000	0.000
7	A	121	ILE	0	-0.040	-0.018	12.312	-0.230	-0.230	0.000	0.000	0.000	0.000
8	A	122	GLU	-1	-0.932	-0.966	15.206	-18.484	-18.484	0.000	0.000	0.000	0.000
9	A	123	ILE	0	-0.005	0.008	17.696	0.407	0.407	0.000	0.000	0.000	0.000
10	A	124	GLY	0	-0.003	0.002	21.387	0.397	0.397	0.000	0.000	0.000	0.000
11	A	125	ASP	-1	-0.874	-0.955	21.518	-12.936	-12.936	0.000	0.000	0.000	0.000
12	A	126	LEU	0	-0.074	-0.028	21.086	0.220	0.220	0.000	0.000	0.000	0.000
13	A	127	THR	0	0.038	0.025	14.448	-0.077	-0.077	0.000	0.000	0.000	0.000
14	A	128	ILE	0	-0.033	-0.024	17.128	0.537	0.537	0.000	0.000	0.000	0.000
15	A	129	SER	0	0.025	0.001	14.434	-1.189	-1.189	0.000	0.000	0.000	0.000
16	A	130	PRO	0	-0.025	-0.012	15.237	0.527	0.527	0.000	0.000	0.000	0.000
17	A	131	ASP	-1	-0.898	-0.960	13.139	-22.190	-22.190	0.000	0.000	0.000	0.000
18	A	132	GLU	-1	-0.927	-0.963	14.188	-21.406	-21.406	0.000	0.000	0.000	0.000
19	A	133	GLU	-1	-0.884	-0.958	17.134	-12.902	-12.902	0.000	0.000	0.000	0.000
20	A	134	LYS	1	0.847	0.931	16.443	19.353	19.353	0.000	0.000	0.000	0.000
21	A	135	ILE	0	-0.032	-0.024	18.756	-0.473	-0.473	0.000	0.000	0.000	0.000
22	A	136	ILE	0	0.018	0.015	16.858	0.371	0.371	0.000	0.000	0.000	0.000
23	A	137	TYR	0	-0.002	-0.045	20.050	0.210	0.210	0.000	0.000	0.000	0.000
24	A	138	LYS	1	0.860	0.930	22.998	12.677	12.677	0.000	0.000	0.000	0.000
25	A	139	GLY	0	0.020	0.014	21.153	0.366	0.366	0.000	0.000	0.000	0.000
26	A	140	ARG	1	0.900	0.964	22.231	10.926	10.926	0.000	0.000	0.000	0.000
27	A	141	GLU	-1	-0.793	-0.895	18.203	-17.231	-17.231	0.000	0.000	0.000	0.000
28	A	142	VAL	0	-0.049	-0.029	22.079	0.693	0.693	0.000	0.000	0.000	0.000
29	A	143	GLU	-1	-0.777	-0.873	22.356	-13.124	-13.124	0.000	0.000	0.000	0.000
30	A	144	VAL	0	-0.066	-0.025	23.486	0.742	0.742	0.000	0.000	0.000	0.000
31	A	145	LYS	1	0.849	0.930	23.828	12.434	12.434	0.000	0.000	0.000	0.000
32	A	146	GLY	0	-0.067	-0.037	26.618	0.596	0.596	0.000	0.000	0.000	0.000
33	A	147	LYS	1	0.999	0.990	27.641	9.266	9.266	0.000	0.000	0.000	0.000
34	A	148	PRO	0	0.049	0.022	28.546	-0.178	-0.178	0.000	0.000	0.000	0.000
35	A	149	PHE	0	0.016	0.001	20.910	0.159	0.159	0.000	0.000	0.000	0.000
36	A	150	GLU	-1	-0.867	-0.905	22.157	-14.376	-14.376	0.000	0.000	0.000	0.000
37	A	151	VAL	0	-0.005	0.000	25.042	-0.160	-0.160	0.000	0.000	0.000	0.000
38	A	152	LEU	0	-0.070	-0.035	26.946	0.117	0.117	0.000	0.000	0.000	0.000
39	A	153	THR	0	-0.001	-0.010	20.353	-0.190	-0.190	0.000	0.000	0.000	0.000
40	A	154	HIS	0	0.006	-0.003	21.029	-0.764	-0.764	0.000	0.000	0.000	0.000
41	A	155	LEU	0	-0.021	-0.023	22.877	0.013	0.013	0.000	0.000	0.000	0.000
42	A	156	ALA	0	-0.021	-0.014	22.303	0.144	0.144	0.000	0.000	0.000	0.000
43	A	157	ARG	1	0.943	0.984	17.611	15.515	15.515	0.000	0.000	0.000	0.000
44	A	158	HIS	0	-0.019	0.002	20.746	-0.726	-0.726	0.000	0.000	0.000	0.000
45	A	159	ARG	1	0.840	0.912	23.450	11.540	11.540	0.000	0.000	0.000	0.000
46	A	160	ASP	-1	-0.855	-0.925	23.492	-12.479	-12.479	0.000	0.000	0.000	0.000
47	A	161	GLN	0	0.031	0.022	26.025	0.449	0.449	0.000	0.000	0.000	0.000
48	A	162	ILE	0	-0.107	-0.053	29.722	0.161	0.161	0.000	0.000	0.000	0.000
49	A	163	VAL	0	0.024	0.016	31.306	-0.104	-0.104	0.000	0.000	0.000	0.000
50	A	164	SER	0	-0.013	-0.021	33.661	0.161	0.161	0.000	0.000	0.000	0.000
51	A	165	LYS	1	0.866	0.937	35.532	7.495	7.495	0.000	0.000	0.000	0.000
52	A	166	GLU	-1	-0.909	-0.956	36.588	-7.754	-7.754	0.000	0.000	0.000	0.000
53	A	167	GLN	0	-0.011	-0.013	33.328	-0.327	-0.327	0.000	0.000	0.000	0.000
54	A	168	LEU	0	-0.015	-0.005	30.527	-0.210	-0.210	0.000	0.000	0.000	0.000
55	A	169	LEU	0	-0.037	-0.016	31.917	-0.196	-0.196	0.000	0.000	0.000	0.000
56	A	170	ASP	-1	-0.926	-0.964	33.596	-9.314	-9.314	0.000	0.000	0.000	0.000
57	A	171	ALA	0	-0.052	-0.022	28.763	-0.208	-0.208	0.000	0.000	0.000	0.000
58	A	172	ILE	0	-0.068	-0.032	26.123	-0.483	-0.483	0.000	0.000	0.000	0.000
59	A	173	TRP	0	-0.036	-0.014	29.271	-0.031	-0.031	0.000	0.000	0.000	0.000
60	A	174	GLU	-1	-0.815	-0.908	28.224	-10.980	-10.980	0.000	0.000	0.000	0.000
61	A	175	GLU	-1	-0.976	-0.992	30.850	-9.506	-9.506	0.000	0.000	0.000	0.000
62	A	176	PRO	0	0.019	0.011	34.287	0.073	0.073	0.000	0.000	0.000	0.000
63	A	177	GLU	-1	-0.871	-0.953	36.852	-7.495	-7.495	0.000	0.000	0.000	0.000
64	A	178	MET	0	-0.056	-0.036	40.130	0.191	0.191	0.000	0.000	0.000	0.000
65	A	179	VAL	0	-0.011	0.021	35.492	0.068	0.068	0.000	0.000	0.000	0.000
66	A	180	THR	0	-0.011	-0.010	38.284	0.151	0.151	0.000	0.000	0.000	0.000
67	A	181	PRO	0	0.058	0.009	39.160	-0.190	-0.190	0.000	0.000	0.000	0.000
68	A	182	ASN	0	-0.029	-0.033	39.742	-0.061	-0.061	0.000	0.000	0.000	0.000
69	A	183	VAL	0	0.048	0.036	34.622	-0.042	-0.042	0.000	0.000	0.000	0.000
70	A	184	ILE	0	0.016	0.013	34.148	-0.195	-0.195	0.000	0.000	0.000	0.000
71	A	185	GLU	-1	-0.893	-0.939	35.622	-7.654	-7.654	0.000	0.000	0.000	0.000
72	A	186	VAL	0	-0.005	0.005	36.279	-0.075	-0.075	0.000	0.000	0.000	0.000
73	A	187	ALA	0	0.012	0.002	31.964	-0.127	-0.127	0.000	0.000	0.000	0.000
74	A	188	ILE	0	0.010	0.001	32.323	-0.209	-0.209	0.000	0.000	0.000	0.000
75	A	189	ASN	0	-0.006	-0.010	34.260	-0.125	-0.125	0.000	0.000	0.000	0.000
76	A	190	GLN	0	-0.028	-0.012	33.379	-0.035	-0.035	0.000	0.000	0.000	0.000
77	A	191	ILE	0	0.023	0.008	27.995	-0.116	-0.116	0.000	0.000	0.000	0.000
78	A	192	ARG	1	0.886	0.947	31.278	8.488	8.488	0.000	0.000	0.000	0.000
79	A	193	GLN	0	-0.009	-0.035	33.493	0.008	0.008	0.000	0.000	0.000	0.000
80	A	194	LYS	1	0.910	0.961	30.018	9.701	9.701	0.000	0.000	0.000	0.000
81	A	195	MET	0	-0.001	0.012	25.052	-0.378	-0.378	0.000	0.000	0.000	0.000
82	A	196	ASP	-1	-0.800	-0.874	30.054	-8.828	-8.828	0.000	0.000	0.000	0.000
83	A	197	LYS	1	0.831	0.909	32.719	8.681	8.681	0.000	0.000	0.000	0.000
84	A	198	PRO	0	-0.026	0.002	30.302	0.101	0.101	0.000	0.000	0.000	0.000
85	A	199	LEU	0	-0.035	-0.021	26.347	-0.143	-0.143	0.000	0.000	0.000	0.000
86	A	200	GLY	0	-0.027	0.001	30.351	-0.009	-0.009	0.000	0.000	0.000	0.000
87	A	201	ILE	0	-0.062	-0.022	28.875	0.045	0.045	0.000	0.000	0.000	0.000
88	A	202	SER	0	0.004	-0.024	32.257	0.048	0.048	0.000	0.000	0.000	0.000
89	A	203	THR	0	0.009	-0.006	28.143	-0.202	-0.202	0.000	0.000	0.000	0.000
90	A	204	VAL	0	0.022	0.005	30.071	-0.072	-0.072	0.000	0.000	0.000	0.000
91	A	205	GLU	-1	-0.750	-0.821	32.356	-8.663	-8.663	0.000	0.000	0.000	0.000
92	A	206	THR	0	-0.054	-0.025	35.661	0.035	0.035	0.000	0.000	0.000	0.000
93	A	207	VAL	0	0.022	-0.005	37.667	0.184	0.184	0.000	0.000	0.000	0.000
94	A	208	ARG	1	0.997	0.982	40.399	6.602	6.602	0.000	0.000	0.000	0.000
95	A	209	ARG	1	0.944	0.988	41.227	7.176	7.176	0.000	0.000	0.000	0.000
96	A	210	ARG	1	0.899	0.940	37.530	7.872	7.872	0.000	0.000	0.000	0.000
97	A	211	GLY	0	0.091	0.045	38.099	0.016	0.016	0.000	0.000	0.000	0.000
98	A	212	TYR	0	0.023	0.011	34.165	0.164	0.164	0.000	0.000	0.000	0.000
99	A	213	ARG	1	0.848	0.907	32.702	8.618	8.618	0.000	0.000	0.000	0.000
100	A	214	PHE	0	0.045	0.026	25.593	0.097	0.097	0.000	0.000	0.000	0.000
101	A	215	CYS	0	-0.016	-0.016	28.099	-0.126	-0.126	0.000	0.000	0.000	0.000
102	A	216	TYR	0	0.080	0.038	25.295	0.257	0.257	0.000	0.000	0.000	0.000
103	A	217	PRO	0	0.030	0.044	26.930	-0.208	-0.208	0.000	0.000	0.000	0.000
104	A	218	LYS	1	0.853	0.934	24.053	12.003	12.003	0.000	0.000	0.000	0.000
105	A	219	PRO	0	-0.029	-0.028	28.093	-0.031	-0.031	0.000	0.000	0.000	0.000
106	A	220	ALA	0	-0.010	0.004	31.224	0.190	0.190	0.000	0.000	0.000	0.000
107	A	221	CYS	0	-0.047	-0.012	33.657	0.275	0.275	0.000	0.000	0.000	0.000
108	A	222	GLU	-1	-0.965	-0.985	36.227	-8.400	-8.400	0.000	0.000	0.000	0.000
109	A	223	GLU	-2	-1.930	-1.953	39.115	-14.386	-14.386	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:115:GLY)