FMO DATABASE

FMODB ID: YYJL2

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	OptHSide
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	-1038417.493962
FMO2-HF: Nuclear repulsion	987484.21606
FMO2-HF: Total energy	-50933.277901
FMO2-MP2: Total energy	-51081.746289

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.
0.202	2.068	-0.01	-0.887	-0.968	0.005

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 : 0.034 / q_NPA : 0.019

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	-0.021	0.006	3.841	-0.119	1.747	-0.010	-0.887	-0.968	0.005
4	A	7	LEU	0	0.005	0.007	5.860	0.380	0.380	0.000	0.000	0.000	0.000
5	A	8	LYS	1	0.795	0.875	8.144	1.051	1.051	0.000	0.000	0.000	0.000
6	A	9	ARG	1	0.822	0.901	8.563	0.363	0.363	0.000	0.000	0.000	0.000
7	A	10	GLU	-1	-0.839	-0.898	13.292	-0.244	-0.244	0.000	0.000	0.000	0.000
8	A	11	GLN	0	-0.043	-0.032	16.683	0.011	0.011	0.000	0.000	0.000	0.000
9	A	12	GLU	-1	-0.883	-0.942	17.216	-0.119	-0.119	0.000	0.000	0.000	0.000
10	A	13	PHE	0	-0.027	-0.015	19.450	0.020	0.020	0.000	0.000	0.000	0.000
11	A	14	VAL	0	0.013	0.003	23.085	-0.004	-0.004	0.000	0.000	0.000	0.000
12	A	15	SER	0	-0.063	-0.022	25.727	-0.003	-0.003	0.000	0.000	0.000	0.000
13	A	16	GLN	0	-0.024	-0.019	27.929	0.007	0.007	0.000	0.000	0.000	0.000
14	A	17	TYR	0	0.009	-0.007	27.097	-0.003	-0.003	0.000	0.000	0.000	0.000
15	A	18	HIS	0	-0.038	-0.011	30.081	0.000	0.000	0.000	0.000	0.000	0.000
16	A	19	PHE	0	0.027	0.015	32.626	0.001	0.001	0.000	0.000	0.000	0.000
17	A	20	ASP	-1	-0.896	-0.946	34.789	-0.025	-0.025	0.000	0.000	0.000	0.000
18	A	21	ALA	0	-0.003	-0.012	37.773	0.002	0.002	0.000	0.000	0.000	0.000
19	A	22	ARG	1	0.775	0.846	37.675	-0.001	-0.001	0.000	0.000	0.000	0.000
20	A	23	ASN	0	0.007	0.012	41.022	0.003	0.003	0.000	0.000	0.000	0.000
21	A	24	PHE	0	0.040	-0.015	41.789	-0.001	-0.001	0.000	0.000	0.000	0.000
22	A	25	GLU	-1	-0.909	-0.934	45.782	-0.008	-0.008	0.000	0.000	0.000	0.000
23	A	26	TRP	0	-0.003	-0.009	40.746	0.000	0.000	0.000	0.000	0.000	0.000
24	A	27	GLU	-1	-0.764	-0.866	40.817	-0.008	-0.008	0.000	0.000	0.000	0.000
25	A	28	ASN	0	-0.075	-0.016	44.454	0.001	0.001	0.000	0.000	0.000	0.000
26	A	29	GLU	-1	-0.979	-0.982	47.737	-0.015	-0.015	0.000	0.000	0.000	0.000
27	A	30	ASN	0	-0.121	-0.070	43.618	-0.003	-0.003	0.000	0.000	0.000	0.000
28	A	31	GLY	0	-0.008	0.013	42.457	-0.002	-0.002	0.000	0.000	0.000	0.000
29	A	32	ALA	0	-0.029	-0.023	39.483	-0.001	-0.001	0.000	0.000	0.000	0.000
30	A	33	PRO	0	-0.010	0.003	35.402	-0.002	-0.002	0.000	0.000	0.000	0.000
31	A	34	GLU	-1	-0.938	-0.978	32.024	-0.013	-0.013	0.000	0.000	0.000	0.000
32	A	35	THR	0	-0.024	-0.019	27.735	-0.005	-0.005	0.000	0.000	0.000	0.000
33	A	36	LYS	1	0.889	0.939	26.183	0.079	0.079	0.000	0.000	0.000	0.000
34	A	37	VAL	0	-0.017	-0.010	21.621	-0.002	-0.002	0.000	0.000	0.000	0.000
35	A	38	ASP	-1	-0.870	-0.929	21.903	-0.114	-0.114	0.000	0.000	0.000	0.000
36	A	39	VAL	0	0.000	0.004	15.928	0.000	0.000	0.000	0.000	0.000	0.000
37	A	40	ASN	0	-0.038	-0.007	19.349	-0.012	-0.012	0.000	0.000	0.000	0.000
38	A	41	PHE	0	0.043	0.006	14.166	-0.022	-0.022	0.000	0.000	0.000	0.000
39	A	42	GLN	0	-0.001	0.013	19.245	0.022	0.022	0.000	0.000	0.000	0.000
40	A	43	LEU	0	0.013	0.011	18.477	-0.024	-0.024	0.000	0.000	0.000	0.000
41	A	44	LEU	0	-0.060	-0.026	19.953	0.032	0.032	0.000	0.000	0.000	0.000
42	A	45	GLN	0	-0.024	-0.026	20.384	0.008	0.008	0.000	0.000	0.000	0.000
43	A	46	HIS	0	0.010	0.027	18.602	-0.068	-0.068	0.000	0.000	0.000	0.000
44	A	47	ASP	-1	-0.840	-0.892	18.567	-0.349	-0.349	0.000	0.000	0.000	0.000
45	A	48	GLN	0	0.023	-0.023	18.667	-0.064	-0.064	0.000	0.000	0.000	0.000
46	A	49	GLU	-1	-0.995	-0.984	19.450	-0.289	-0.289	0.000	0.000	0.000	0.000
47	A	50	ASN	0	-0.074	-0.063	16.907	-0.004	-0.004	0.000	0.000	0.000	0.000
48	A	51	GLN	0	-0.037	0.002	13.701	-0.108	-0.108	0.000	0.000	0.000	0.000
49	A	52	VAL	0	0.020	0.004	13.798	-0.138	-0.138	0.000	0.000	0.000	0.000
50	A	53	THR	0	-0.015	0.002	13.626	0.105	0.105	0.000	0.000	0.000	0.000
51	A	54	SER	0	0.008	0.013	14.654	-0.074	-0.074	0.000	0.000	0.000	0.000
52	A	55	LEU	0	0.038	0.006	14.022	0.038	0.038	0.000	0.000	0.000	0.000
53	A	56	ILE	0	0.009	0.002	17.486	-0.006	-0.006	0.000	0.000	0.000	0.000
54	A	57	VAL	0	-0.008	0.002	14.027	-0.005	-0.005	0.000	0.000	0.000	0.000
55	A	58	ILE	0	0.008	-0.015	17.418	0.030	0.030	0.000	0.000	0.000	0.000
56	A	59	LEU	0	-0.006	0.010	19.022	0.000	0.000	0.000	0.000	0.000	0.000
57	A	60	SER	0	-0.029	-0.015	20.953	0.011	0.011	0.000	0.000	0.000	0.000
58	A	61	PHE	0	0.013	-0.008	23.998	0.004	0.004	0.000	0.000	0.000	0.000
59	A	62	MET	0	0.034	0.016	26.272	0.000	0.000	0.000	0.000	0.000	0.000
60	A	63	ILE	0	-0.010	-0.004	25.614	0.002	0.002	0.000	0.000	0.000	0.000
61	A	64	VAL	0	-0.003	0.006	29.800	0.000	0.000	0.000	0.000	0.000	0.000
62	A	65	PHE	0	0.023	0.018	29.255	0.005	0.005	0.000	0.000	0.000	0.000
63	A	66	ASP	-1	-0.894	-0.947	34.713	0.017	0.017	0.000	0.000	0.000	0.000
64	A	67	LYS	1	0.857	0.910	38.175	-0.009	-0.009	0.000	0.000	0.000	0.000
65	A	68	PHE	0	0.035	0.024	32.729	-0.002	-0.002	0.000	0.000	0.000	0.000
66	A	69	VAL	0	0.018	0.010	33.224	0.002	0.002	0.000	0.000	0.000	0.000
67	A	70	ILE	0	-0.011	0.016	28.638	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	71	SER	0	-0.016	-0.017	29.514	-0.003	-0.003	0.000	0.000	0.000	0.000
69	A	72	GLY	0	0.059	0.029	28.688	0.002	0.002	0.000	0.000	0.000	0.000
70	A	73	THR	0	-0.061	-0.048	24.462	-0.008	-0.008	0.000	0.000	0.000	0.000
71	A	74	ILE	0	0.003	0.012	20.758	0.004	0.004	0.000	0.000	0.000	0.000
72	A	75	SER	0	-0.008	-0.008	20.124	-0.013	-0.013	0.000	0.000	0.000	0.000
73	A	76	GLN	0	0.080	0.030	14.262	-0.026	-0.026	0.000	0.000	0.000	0.000
74	A	77	VAL	0	0.012	0.033	17.216	-0.035	-0.035	0.000	0.000	0.000	0.000
75	A	78	ASN	0	-0.048	-0.031	12.140	-0.049	-0.049	0.000	0.000	0.000	0.000
76	A	79	HIS	1	0.804	0.866	12.881	0.464	0.464	0.000	0.000	0.000	0.000
77	A	80	ILE	0	0.019	0.007	8.812	-0.116	-0.116	0.000	0.000	0.000	0.000
78	A	81	ASP	-1	-0.826	-0.899	9.655	-0.823	-0.823	0.000	0.000	0.000	0.000
79	A	82	GLY	0	0.051	0.019	9.135	-0.395	-0.395	0.000	0.000	0.000	0.000
80	A	83	ARG	1	0.777	0.848	7.847	1.340	1.340	0.000	0.000	0.000	0.000
81	A	84	ILE	0	-0.001	0.011	11.998	0.061	0.061	0.000	0.000	0.000	0.000
82	A	85	VAL	0	-0.019	-0.008	12.645	-0.020	-0.020	0.000	0.000	0.000	0.000
83	A	86	ASN	0	-0.026	-0.021	15.434	0.047	0.047	0.000	0.000	0.000	0.000
84	A	87	GLU	-1	-0.806	-0.865	18.181	-0.241	-0.241	0.000	0.000	0.000	0.000
85	A	88	PRO	0	0.018	-0.002	16.367	-0.034	-0.034	0.000	0.000	0.000	0.000
86	A	89	SER	0	-0.070	-0.064	16.180	-0.019	-0.019	0.000	0.000	0.000	0.000
87	A	90	GLU	-1	-0.955	-0.983	15.218	-0.414	-0.414	0.000	0.000	0.000	0.000
88	A	91	LEU	0	-0.105	-0.037	10.763	-0.091	-0.091	0.000	0.000	0.000	0.000
89	A	92	ASN	0	0.028	0.016	8.220	0.217	0.217	0.000	0.000	0.000	0.000
90	A	93	GLN	0	0.040	-0.006	11.883	-0.004	-0.004	0.000	0.000	0.000	0.000
91	A	94	GLU	-1	-0.894	-0.932	6.160	0.819	0.819	0.000	0.000	0.000	0.000
92	A	95	GLU	-1	-0.776	-0.883	7.082	-1.344	-1.344	0.000	0.000	0.000	0.000
93	A	96	VAL	0	0.000	0.000	8.628	-0.018	-0.018	0.000	0.000	0.000	0.000
94	A	97	GLU	-1	-0.848	-0.905	10.772	0.169	0.169	0.000	0.000	0.000	0.000
95	A	98	THR	0	-0.013	-0.017	5.459	0.093	0.093	0.000	0.000	0.000	0.000
96	A	99	LEU	0	-0.044	-0.027	8.684	0.006	0.006	0.000	0.000	0.000	0.000
97	A	100	ALA	0	0.030	0.017	10.894	0.037	0.037	0.000	0.000	0.000	0.000
98	A	101	ARG	1	0.793	0.877	11.121	-0.067	-0.067	0.000	0.000	0.000	0.000
99	A	102	PRO	0	-0.005	-0.008	12.029	0.039	0.039	0.000	0.000	0.000	0.000
100	A	103	CYS	0	-0.005	0.009	15.094	0.016	0.016	0.000	0.000	0.000	0.000
101	A	104	LEU	0	0.022	0.010	14.771	0.020	0.020	0.000	0.000	0.000	0.000
102	A	105	ASN	0	0.009	0.005	14.929	0.027	0.027	0.000	0.000	0.000	0.000
103	A	106	MET	0	0.001	0.011	18.514	0.014	0.014	0.000	0.000	0.000	0.000
104	A	107	LEU	0	0.003	0.004	21.040	0.007	0.007	0.000	0.000	0.000	0.000
105	A	108	ASN	0	0.017	0.000	19.424	-0.005	-0.005	0.000	0.000	0.000	0.000
106	A	109	ARG	1	0.830	0.900	22.424	-0.037	-0.037	0.000	0.000	0.000	0.000
107	A	110	LEU	0	-0.003	-0.001	24.270	0.000	0.000	0.000	0.000	0.000	0.000
108	A	111	THR	0	0.033	0.009	26.051	-0.002	-0.002	0.000	0.000	0.000	0.000
109	A	112	TYR	0	-0.097	-0.025	26.672	0.004	0.004	0.000	0.000	0.000	0.000
110	A	113	GLU	-1	-0.803	-0.893	28.182	0.035	0.035	0.000	0.000	0.000	0.000
111	A	114	VAL	0	-0.024	-0.011	30.464	-0.002	-0.002	0.000	0.000	0.000	0.000
112	A	115	THR	0	-0.039	-0.041	30.994	0.001	0.001	0.000	0.000	0.000	0.000
113	A	116	GLU	-1	-0.782	-0.869	32.769	0.046	0.046	0.000	0.000	0.000	0.000
114	A	117	ILE	0	-0.047	-0.021	33.947	-0.001	-0.001	0.000	0.000	0.000	0.000
115	A	118	ALA	0	-0.067	-0.034	36.256	-0.001	-0.001	0.000	0.000	0.000	0.000
116	A	119	LEU	0	-0.084	-0.053	35.550	-0.002	-0.002	0.000	0.000	0.000	0.000
117	A	120	ASP	-1	-0.960	-0.956	38.709	0.024	0.024	0.000	0.000	0.000	0.000
118	A	121	LEU	0	-0.053	-0.025	37.312	0.002	0.002	0.000	0.000	0.000	0.000
119	A	122	PRO	0	-0.037	-0.026	33.858	-0.001	-0.001	0.000	0.000	0.000	0.000
120	A	123	GLY	0	0.007	0.018	31.090	-0.002	-0.002	0.000	0.000	0.000	0.000
121	A	124	ILE	0	-0.046	-0.032	28.849	0.007	0.007	0.000	0.000	0.000	0.000
122	A	125	ASN	0	-0.017	-0.018	23.499	-0.009	-0.009	0.000	0.000	0.000	0.000
123	A	126	LEU	0	-0.017	-0.012	23.668	0.004	0.004	0.000	0.000	0.000	0.000
124	A	127	GLU	-1	-0.984	-0.979	21.138	0.131	0.131	0.000	0.000	0.000	0.000
125	A	128	PHE	0	0.041	0.055	17.186	0.021	0.021	0.000	0.000	0.000	0.000

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