FMO DATABASE

FMODB ID: VRJ71

Calculation Name: 2HNG-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2HNG

Chain ID: A

ChEMBL ID:

UniProt ID: A0A0H2

Base Structure: X-ray

Registration Date: 2023-06-19

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	125
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1038072.732765
FMO2-HF: Nuclear repulsion	987139.188226
FMO2-HF: Total energy	-50933.544539
FMO2-MP2: Total energy	-51081.960741

3D Structure

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:ALA)

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

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.
0.167	2.06	-0.004	-0.895	-0.993	0.004

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.043 / q_NPA : 0.021

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	ASN	0	-0.033	-0.010	3.864	0.007	1.900	-0.004	-0.895	-0.993	0.004
4	A	7	LEU	0	0.003	0.009	5.698	0.411	0.411	0.000	0.000	0.000	0.000
5	A	8	LYS	1	0.800	0.877	8.013	1.120	1.120	0.000	0.000	0.000	0.000
6	A	9	ARG	1	0.803	0.879	8.039	0.411	0.411	0.000	0.000	0.000	0.000
7	A	10	GLU	-1	-0.849	-0.904	13.362	-0.258	-0.258	0.000	0.000	0.000	0.000
8	A	11	GLN	0	-0.037	-0.026	16.489	0.007	0.007	0.000	0.000	0.000	0.000
9	A	12	GLU	-1	-0.880	-0.943	16.725	-0.131	-0.131	0.000	0.000	0.000	0.000
10	A	13	PHE	0	-0.020	-0.010	19.320	0.021	0.021	0.000	0.000	0.000	0.000
11	A	14	VAL	0	0.024	0.002	22.890	-0.005	-0.005	0.000	0.000	0.000	0.000
12	A	15	SER	0	-0.046	-0.016	25.223	0.000	0.000	0.000	0.000	0.000	0.000
13	A	16	GLN	0	-0.014	-0.013	27.193	0.004	0.004	0.000	0.000	0.000	0.000
14	A	17	TYR	0	0.000	-0.018	26.595	-0.003	-0.003	0.000	0.000	0.000	0.000
15	A	18	HIS	0	-0.050	-0.008	29.715	-0.001	-0.001	0.000	0.000	0.000	0.000
16	A	19	PHE	0	0.028	0.008	32.161	0.002	0.002	0.000	0.000	0.000	0.000
17	A	20	ASP	-1	-0.857	-0.920	34.662	-0.028	-0.028	0.000	0.000	0.000	0.000
18	A	21	ALA	0	0.002	-0.014	37.447	0.003	0.003	0.000	0.000	0.000	0.000
19	A	22	ARG	1	0.766	0.842	37.811	0.002	0.002	0.000	0.000	0.000	0.000
20	A	23	ASN	0	0.020	0.011	41.220	0.003	0.003	0.000	0.000	0.000	0.000
21	A	24	PHE	0	0.029	-0.014	41.694	-0.001	-0.001	0.000	0.000	0.000	0.000
22	A	25	GLU	-1	-0.908	-0.935	45.749	-0.009	-0.009	0.000	0.000	0.000	0.000
23	A	26	TRP	0	-0.030	-0.018	40.438	-0.001	-0.001	0.000	0.000	0.000	0.000
24	A	27	GLU	-1	-0.766	-0.864	40.937	-0.010	-0.010	0.000	0.000	0.000	0.000
25	A	28	ASN	0	-0.113	-0.036	44.476	0.002	0.002	0.000	0.000	0.000	0.000
26	A	29	GLU	-1	-0.922	-0.956	47.869	-0.015	-0.015	0.000	0.000	0.000	0.000
27	A	30	ASN	0	-0.125	-0.071	43.313	-0.003	-0.003	0.000	0.000	0.000	0.000
28	A	31	GLY	0	0.005	0.022	42.412	-0.002	-0.002	0.000	0.000	0.000	0.000
29	A	32	ALA	0	-0.022	-0.020	39.478	-0.001	-0.001	0.000	0.000	0.000	0.000
30	A	33	PRO	0	-0.016	0.001	35.584	-0.002	-0.002	0.000	0.000	0.000	0.000
31	A	34	GLU	-1	-0.939	-0.978	31.909	-0.018	-0.018	0.000	0.000	0.000	0.000
32	A	35	THR	0	-0.031	-0.018	27.889	-0.005	-0.005	0.000	0.000	0.000	0.000
33	A	36	LYS	1	0.892	0.945	25.925	0.084	0.084	0.000	0.000	0.000	0.000
34	A	37	VAL	0	-0.007	-0.007	21.715	-0.002	-0.002	0.000	0.000	0.000	0.000
35	A	38	ASP	-1	-0.865	-0.919	22.016	-0.122	-0.122	0.000	0.000	0.000	0.000
36	A	39	VAL	0	-0.001	0.005	15.789	0.001	0.001	0.000	0.000	0.000	0.000
37	A	40	ASN	0	-0.031	-0.021	19.185	-0.019	-0.019	0.000	0.000	0.000	0.000
38	A	41	PHE	0	0.026	-0.001	14.181	-0.026	-0.026	0.000	0.000	0.000	0.000
39	A	42	GLN	0	0.002	0.013	19.404	0.027	0.027	0.000	0.000	0.000	0.000
40	A	43	LEU	0	0.006	0.006	18.283	-0.020	-0.020	0.000	0.000	0.000	0.000
41	A	44	LEU	0	-0.059	-0.023	20.049	0.035	0.035	0.000	0.000	0.000	0.000
42	A	45	GLN	0	0.007	-0.003	20.554	0.006	0.006	0.000	0.000	0.000	0.000
43	A	46	HIS	0	0.014	0.036	18.549	-0.064	-0.064	0.000	0.000	0.000	0.000
44	A	47	ASP	-1	-0.808	-0.877	18.558	-0.356	-0.356	0.000	0.000	0.000	0.000
45	A	48	GLN	0	0.000	-0.028	18.526	-0.059	-0.059	0.000	0.000	0.000	0.000
46	A	49	GLU	-1	-1.001	-0.984	19.759	-0.276	-0.276	0.000	0.000	0.000	0.000
47	A	50	ASN	0	-0.092	-0.070	16.751	0.005	0.005	0.000	0.000	0.000	0.000
48	A	51	GLN	0	-0.034	-0.005	13.684	-0.128	-0.128	0.000	0.000	0.000	0.000
49	A	52	VAL	0	0.001	-0.002	13.868	-0.136	-0.136	0.000	0.000	0.000	0.000
50	A	53	THR	0	-0.028	-0.015	13.689	0.108	0.108	0.000	0.000	0.000	0.000
51	A	54	SER	0	-0.005	-0.014	14.890	-0.085	-0.085	0.000	0.000	0.000	0.000
52	A	55	LEU	0	0.029	0.002	14.200	0.039	0.039	0.000	0.000	0.000	0.000
53	A	56	ILE	0	0.010	0.008	17.272	-0.007	-0.007	0.000	0.000	0.000	0.000
54	A	57	VAL	0	0.016	0.012	13.747	-0.011	-0.011	0.000	0.000	0.000	0.000
55	A	58	ILE	0	0.001	-0.017	17.199	0.032	0.032	0.000	0.000	0.000	0.000
56	A	59	LEU	0	-0.007	0.017	18.813	-0.003	-0.003	0.000	0.000	0.000	0.000
57	A	60	SER	0	-0.023	-0.011	20.892	0.012	0.012	0.000	0.000	0.000	0.000
58	A	61	PHE	0	0.005	-0.016	23.994	0.004	0.004	0.000	0.000	0.000	0.000
59	A	62	MET	0	0.020	0.016	26.473	0.000	0.000	0.000	0.000	0.000	0.000
60	A	63	ILE	0	-0.005	-0.003	25.854	0.002	0.002	0.000	0.000	0.000	0.000
61	A	64	VAL	0	-0.015	0.003	29.924	0.001	0.001	0.000	0.000	0.000	0.000
62	A	65	PHE	0	0.046	0.026	29.474	0.005	0.005	0.000	0.000	0.000	0.000
63	A	66	ASP	-1	-0.881	-0.936	35.132	0.014	0.014	0.000	0.000	0.000	0.000
64	A	67	LYS	1	0.808	0.887	38.505	-0.007	-0.007	0.000	0.000	0.000	0.000
65	A	68	PHE	0	0.034	0.020	32.899	-0.002	-0.002	0.000	0.000	0.000	0.000
66	A	69	VAL	0	0.023	0.010	33.144	0.002	0.002	0.000	0.000	0.000	0.000
67	A	70	ILE	0	0.001	0.025	28.418	0.000	0.000	0.000	0.000	0.000	0.000
68	A	71	SER	0	-0.024	-0.025	30.151	-0.004	-0.004	0.000	0.000	0.000	0.000
69	A	72	GLY	0	0.055	0.021	28.637	0.002	0.002	0.000	0.000	0.000	0.000
70	A	73	THR	0	-0.063	-0.053	24.283	-0.009	-0.009	0.000	0.000	0.000	0.000
71	A	74	ILE	0	-0.021	0.003	20.306	0.004	0.004	0.000	0.000	0.000	0.000
72	A	75	SER	0	-0.007	-0.002	20.000	-0.015	-0.015	0.000	0.000	0.000	0.000
73	A	76	GLN	0	0.075	0.027	13.967	-0.028	-0.028	0.000	0.000	0.000	0.000
74	A	77	VAL	0	0.002	0.030	16.981	-0.036	-0.036	0.000	0.000	0.000	0.000
75	A	78	ASN	0	-0.057	-0.043	12.038	-0.052	-0.052	0.000	0.000	0.000	0.000
76	A	79	HIS	1	0.819	0.878	12.618	0.489	0.489	0.000	0.000	0.000	0.000
77	A	80	ILE	0	0.024	0.019	8.756	-0.118	-0.118	0.000	0.000	0.000	0.000
78	A	81	ASP	-1	-0.808	-0.889	9.699	-0.798	-0.798	0.000	0.000	0.000	0.000
79	A	82	GLY	0	0.050	0.031	9.182	-0.374	-0.374	0.000	0.000	0.000	0.000
80	A	83	ARG	1	0.775	0.849	8.000	1.267	1.267	0.000	0.000	0.000	0.000
81	A	84	ILE	0	-0.002	0.011	11.959	0.037	0.037	0.000	0.000	0.000	0.000
82	A	85	VAL	0	-0.023	-0.013	12.950	-0.063	-0.063	0.000	0.000	0.000	0.000
83	A	86	ASN	0	-0.107	-0.064	15.802	0.050	0.050	0.000	0.000	0.000	0.000
84	A	87	GLU	-1	-0.804	-0.877	18.549	-0.244	-0.244	0.000	0.000	0.000	0.000
85	A	88	PRO	0	-0.009	-0.007	16.502	-0.034	-0.034	0.000	0.000	0.000	0.000
86	A	89	SER	0	-0.050	-0.054	15.961	-0.028	-0.028	0.000	0.000	0.000	0.000
87	A	90	GLU	-1	-0.850	-0.922	15.197	-0.443	-0.443	0.000	0.000	0.000	0.000
88	A	91	LEU	0	-0.094	-0.034	10.741	-0.106	-0.106	0.000	0.000	0.000	0.000
89	A	92	ASN	0	0.024	0.011	8.270	0.252	0.252	0.000	0.000	0.000	0.000
90	A	93	GLN	0	0.035	-0.005	11.371	-0.015	-0.015	0.000	0.000	0.000	0.000
91	A	94	GLU	-1	-0.900	-0.938	5.574	0.659	0.659	0.000	0.000	0.000	0.000
92	A	95	GLU	-1	-0.792	-0.875	6.864	-1.293	-1.293	0.000	0.000	0.000	0.000
93	A	96	VAL	0	0.009	-0.002	8.466	-0.020	-0.020	0.000	0.000	0.000	0.000
94	A	97	GLU	-1	-0.832	-0.903	10.901	0.128	0.128	0.000	0.000	0.000	0.000
95	A	98	THR	0	-0.023	-0.023	5.341	0.083	0.083	0.000	0.000	0.000	0.000
96	A	99	LEU	0	-0.044	-0.018	8.626	-0.011	-0.011	0.000	0.000	0.000	0.000
97	A	100	ALA	0	0.051	0.023	10.872	0.049	0.049	0.000	0.000	0.000	0.000
98	A	101	ARG	1	0.800	0.874	10.566	-0.049	-0.049	0.000	0.000	0.000	0.000
99	A	102	PRO	0	-0.015	-0.004	11.412	0.047	0.047	0.000	0.000	0.000	0.000
100	A	103	CYS	0	0.008	0.012	14.383	0.023	0.023	0.000	0.000	0.000	0.000
101	A	104	LEU	0	0.029	0.017	14.712	0.018	0.018	0.000	0.000	0.000	0.000
102	A	105	ASN	0	0.003	0.007	14.122	0.029	0.029	0.000	0.000	0.000	0.000
103	A	106	MET	0	-0.005	0.004	17.705	0.016	0.016	0.000	0.000	0.000	0.000
104	A	107	LEU	0	0.012	0.009	20.361	0.008	0.008	0.000	0.000	0.000	0.000
105	A	108	ASN	0	0.003	-0.005	18.737	0.001	0.001	0.000	0.000	0.000	0.000
106	A	109	ARG	1	0.769	0.867	21.517	-0.033	-0.033	0.000	0.000	0.000	0.000
107	A	110	LEU	0	0.012	-0.006	23.363	0.002	0.002	0.000	0.000	0.000	0.000
108	A	111	THR	0	0.045	0.018	25.624	-0.001	-0.001	0.000	0.000	0.000	0.000
109	A	112	TYR	0	-0.099	-0.020	26.221	0.004	0.004	0.000	0.000	0.000	0.000
110	A	113	GLU	-1	-0.792	-0.876	27.724	0.030	0.030	0.000	0.000	0.000	0.000
111	A	114	VAL	0	-0.021	-0.008	29.948	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	115	THR	0	-0.028	-0.039	30.481	0.001	0.001	0.000	0.000	0.000	0.000
113	A	116	GLU	-1	-0.775	-0.868	32.203	0.043	0.043	0.000	0.000	0.000	0.000
114	A	117	ILE	0	-0.062	-0.037	33.353	-0.001	-0.001	0.000	0.000	0.000	0.000
115	A	118	ALA	0	-0.057	-0.023	35.618	-0.001	-0.001	0.000	0.000	0.000	0.000
116	A	119	LEU	0	-0.081	-0.045	35.158	-0.002	-0.002	0.000	0.000	0.000	0.000
117	A	120	ASP	-1	-0.955	-0.959	38.569	0.022	0.022	0.000	0.000	0.000	0.000
118	A	121	LEU	0	-0.047	-0.022	37.179	0.003	0.003	0.000	0.000	0.000	0.000
119	A	122	PRO	0	-0.042	-0.028	33.337	-0.001	-0.001	0.000	0.000	0.000	0.000
120	A	123	GLY	0	0.009	0.020	30.585	-0.002	-0.002	0.000	0.000	0.000	0.000
121	A	124	ILE	0	-0.032	-0.031	28.560	0.007	0.007	0.000	0.000	0.000	0.000
122	A	125	ASN	0	-0.044	-0.032	23.413	-0.010	-0.010	0.000	0.000	0.000	0.000
123	A	126	LEU	0	-0.016	-0.008	23.595	0.003	0.003	0.000	0.000	0.000	0.000
124	A	127	GLU	-1	-0.936	-0.946	21.080	0.123	0.123	0.000	0.000	0.000	0.000
125	A	128	PHE	0	0.007	0.026	17.657	0.005	0.005	0.000	0.000	0.000	0.000

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