FMO DATABASE

FMODB ID: 59K7Z

Calculation Name: 2HNG-A-Xray311

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: 2021-09-06

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 1.20200116

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	126
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1041324.162376
FMO2-HF: Nuclear repulsion	990240.5317
FMO2-HF: Total energy	-51083.630676
FMO2-MP2: Total energy	-51232.58183

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:3:ACE )

Summations of interaction energy for fragment #1(A:3:ACE )

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.
0.151	0.854	-0.005	-0.311	-0.386	0

Interaction energy analysis for fragmet #1(A:3:ACE )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.004 / q_NPA : -0.012

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].
3	A	5	MET	0	0.001	0.031	3.854	1.275	1.978	-0.005	-0.311	-0.386
4	A	6	ASN	0	0.004	0.017	6.825	-0.004	-0.004	0.000	0.000	0.000
5	A	7	LEU	0	0.012	0.011	9.470	0.144	0.144	0.000	0.000	0.000
6	A	8	LYS	1	0.787	0.872	12.427	0.241	0.241	0.000	0.000	0.000
7	A	9	ARG	1	0.810	0.903	13.083	0.471	0.471	0.000	0.000	0.000
8	A	10	GLU	-1	-0.847	-0.905	18.169	-0.117	-0.117	0.000	0.000	0.000
9	A	11	GLN	0	-0.028	-0.019	21.592	-0.025	-0.025	0.000	0.000	0.000
10	A	12	GLU	-1	-0.904	-0.947	22.291	-0.196	-0.196	0.000	0.000	0.000
11	A	13	PHE	0	-0.038	-0.019	24.092	0.013	0.013	0.000	0.000	0.000
12	A	14	VAL	0	0.019	0.004	27.390	-0.003	-0.003	0.000	0.000	0.000
13	A	15	SER	0	-0.053	-0.018	29.833	0.007	0.007	0.000	0.000	0.000
14	A	16	GLN	0	-0.036	-0.024	31.627	0.007	0.007	0.000	0.000	0.000
15	A	17	TYR	0	0.009	-0.007	30.892	-0.004	-0.004	0.000	0.000	0.000
16	A	18	HIS	0	-0.039	-0.010	33.834	0.003	0.003	0.000	0.000	0.000
17	A	19	PHE	0	0.025	0.012	36.159	-0.002	-0.002	0.000	0.000	0.000
18	A	20	ASP	-1	-0.893	-0.948	38.385	-0.051	-0.051	0.000	0.000	0.000
19	A	21	ALA	0	-0.007	-0.011	41.082	-0.001	-0.001	0.000	0.000	0.000
20	A	22	ARG	1	0.768	0.853	40.647	0.046	0.046	0.000	0.000	0.000
21	A	23	ASN	0	0.006	0.021	44.098	0.003	0.003	0.000	0.000	0.000
22	A	24	PHE	0	0.017	-0.022	44.577	0.001	0.001	0.000	0.000	0.000
23	A	25	GLU	-1	-0.937	-0.948	48.593	-0.025	-0.025	0.000	0.000	0.000
24	A	26	TRP	0	0.005	-0.015	43.480	0.001	0.001	0.000	0.000	0.000
25	A	27	GLU	-1	-0.775	-0.890	43.532	-0.040	-0.040	0.000	0.000	0.000
26	A	28	ASN	0	-0.070	-0.014	47.039	0.001	0.001	0.000	0.000	0.000
27	A	29	GLU	-1	-0.989	-0.985	50.186	-0.022	-0.022	0.000	0.000	0.000
28	A	30	ASN	0	-0.092	-0.046	46.043	0.002	0.002	0.000	0.000	0.000
29	A	31	GLY	0	-0.012	0.009	44.640	0.000	0.000	0.000	0.000	0.000
30	A	32	ALA	0	-0.036	-0.027	41.830	-0.001	-0.001	0.000	0.000	0.000
31	A	33	PRO	0	-0.015	0.004	38.070	0.000	0.000	0.000	0.000	0.000
32	A	34	GLU	-1	-0.932	-0.977	34.233	-0.046	-0.046	0.000	0.000	0.000
33	A	35	THR	0	-0.027	-0.018	30.121	-0.002	-0.002	0.000	0.000	0.000
34	A	36	LYS	1	0.962	0.984	29.163	0.063	0.063	0.000	0.000	0.000
35	A	37	VAL	0	-0.003	-0.004	24.225	-0.001	-0.001	0.000	0.000	0.000
36	A	38	ASP	-1	-0.886	-0.944	24.147	-0.087	-0.087	0.000	0.000	0.000
37	A	39	VAL	0	-0.019	-0.005	18.654	-0.008	-0.008	0.000	0.000	0.000
38	A	40	ASN	0	-0.051	-0.013	21.709	0.014	0.014	0.000	0.000	0.000
39	A	41	PHE	0	0.037	0.004	16.486	-0.014	-0.014	0.000	0.000	0.000
40	A	42	GLN	0	-0.011	0.007	21.540	0.013	0.013	0.000	0.000	0.000
41	A	43	LEU	0	0.008	0.004	19.814	-0.011	-0.011	0.000	0.000	0.000
42	A	44	LEU	0	-0.067	-0.028	22.419	0.005	0.005	0.000	0.000	0.000
43	A	45	GLN	0	-0.026	-0.029	22.494	0.005	0.005	0.000	0.000	0.000
44	A	46	HIS	0	0.026	0.024	19.880	-0.010	-0.010	0.000	0.000	0.000
45	A	47	ASP	-1	-0.830	-0.898	20.466	-0.024	-0.024	0.000	0.000	0.000
46	A	48	GLN	0	0.011	-0.030	20.234	0.010	0.010	0.000	0.000	0.000
47	A	49	GLU	-1	-0.998	-0.983	20.826	0.004	0.004	0.000	0.000	0.000
48	A	50	ASN	0	-0.069	-0.048	19.127	0.015	0.015	0.000	0.000	0.000
49	A	51	GLN	0	-0.044	0.003	14.568	0.001	0.001	0.000	0.000	0.000
50	A	52	VAL	0	0.019	0.008	15.477	-0.016	-0.016	0.000	0.000	0.000
51	A	53	THR	0	-0.034	0.016	15.607	0.007	0.007	0.000	0.000	0.000
52	A	54	SER	0	0.023	0.022	16.972	-0.038	-0.038	0.000	0.000	0.000
53	A	55	LEU	0	0.039	0.016	16.365	0.019	0.019	0.000	0.000	0.000
54	A	56	ILE	0	-0.001	-0.004	20.431	-0.016	-0.016	0.000	0.000	0.000
55	A	57	VAL	0	0.003	0.007	17.327	0.009	0.009	0.000	0.000	0.000
56	A	58	ILE	0	0.014	-0.011	20.526	0.001	0.001	0.000	0.000	0.000
57	A	59	LEU	0	0.008	0.020	22.285	0.002	0.002	0.000	0.000	0.000
58	A	60	SER	0	-0.046	-0.028	24.132	0.010	0.010	0.000	0.000	0.000
59	A	61	PHE	0	0.016	-0.003	27.164	-0.003	-0.003	0.000	0.000	0.000
60	A	62	MET	0	0.022	0.008	29.276	0.006	0.006	0.000	0.000	0.000
61	A	63	ILE	0	0.004	0.003	28.828	-0.001	-0.001	0.000	0.000	0.000
62	A	64	VAL	0	-0.007	0.004	32.704	0.002	0.002	0.000	0.000	0.000
63	A	65	PHE	0	0.026	0.019	32.508	-0.001	-0.001	0.000	0.000	0.000
64	A	66	ASP	-1	-0.890	-0.947	37.583	-0.045	-0.045	0.000	0.000	0.000
65	A	67	LYS	1	0.887	0.921	41.101	0.042	0.042	0.000	0.000	0.000
66	A	68	PHE	0	0.030	0.020	36.163	0.002	0.002	0.000	0.000	0.000
67	A	69	VAL	0	0.020	0.014	36.137	-0.001	-0.001	0.000	0.000	0.000
68	A	70	ILE	0	-0.003	0.017	32.036	0.001	0.001	0.000	0.000	0.000
69	A	71	SER	0	-0.016	-0.017	32.780	-0.001	-0.001	0.000	0.000	0.000
70	A	72	GLY	0	0.049	0.024	32.050	0.001	0.001	0.000	0.000	0.000
71	A	73	THR	0	-0.060	-0.045	27.846	0.000	0.000	0.000	0.000	0.000
72	A	74	ILE	0	0.005	0.014	24.577	0.004	0.004	0.000	0.000	0.000
73	A	75	SER	0	-0.014	-0.009	23.697	-0.001	-0.001	0.000	0.000	0.000
74	A	76	GLN	0	0.067	0.009	18.751	-0.022	-0.022	0.000	0.000	0.000
75	A	77	VAL	0	0.010	0.031	20.729	-0.007	-0.007	0.000	0.000	0.000
76	A	78	ASN	0	-0.013	-0.009	15.740	-0.066	-0.066	0.000	0.000	0.000
77	A	79	HIS	1	0.794	0.847	16.733	0.178	0.178	0.000	0.000	0.000
78	A	80	ILE	0	0.031	0.013	10.969	-0.056	-0.056	0.000	0.000	0.000
79	A	81	ASP	-1	-0.846	-0.906	12.341	-0.070	-0.070	0.000	0.000	0.000
80	A	82	GLY	0	0.050	0.022	11.134	-0.026	-0.026	0.000	0.000	0.000
81	A	83	ARG	1	0.820	0.890	9.083	0.097	0.097	0.000	0.000	0.000
82	A	84	ILE	0	0.010	0.004	13.013	-0.031	-0.031	0.000	0.000	0.000
83	A	85	VAL	0	-0.034	-0.018	13.758	0.018	0.018	0.000	0.000	0.000
84	A	86	ASN	0	0.014	-0.008	16.416	-0.019	-0.019	0.000	0.000	0.000
85	A	87	GLU	-1	-0.846	-0.921	18.986	-0.040	-0.040	0.000	0.000	0.000
86	A	88	PRO	0	0.002	-0.008	17.507	0.002	0.002	0.000	0.000	0.000
87	A	89	SER	0	-0.037	-0.018	17.182	-0.011	-0.011	0.000	0.000	0.000
88	A	90	GLU	-1	-0.978	-0.989	15.717	0.038	0.038	0.000	0.000	0.000
89	A	91	LEU	0	-0.106	-0.032	12.044	0.010	0.010	0.000	0.000	0.000
90	A	92	ASN	0	0.024	0.005	8.455	-0.071	-0.071	0.000	0.000	0.000
91	A	93	GLN	0	0.036	-0.012	12.733	-0.049	-0.049	0.000	0.000	0.000
92	A	94	GLU	-1	-0.890	-0.927	7.104	-0.827	-0.827	0.000	0.000	0.000
93	A	95	GLU	-1	-0.815	-0.917	8.317	-0.265	-0.265	0.000	0.000	0.000
94	A	96	VAL	0	-0.006	-0.003	10.401	-0.016	-0.016	0.000	0.000	0.000
95	A	97	GLU	-1	-0.858	-0.917	13.193	-0.350	-0.350	0.000	0.000	0.000
96	A	98	THR	0	-0.019	-0.024	9.333	-0.064	-0.064	0.000	0.000	0.000
97	A	99	LEU	0	-0.051	-0.036	12.094	0.029	0.029	0.000	0.000	0.000
98	A	100	ALA	0	0.023	0.013	14.261	0.030	0.030	0.000	0.000	0.000
99	A	101	ARG	1	0.751	0.871	14.932	0.336	0.336	0.000	0.000	0.000
100	A	102	PRO	0	-0.015	-0.018	16.099	0.030	0.030	0.000	0.000	0.000
101	A	103	CYS	0	-0.003	0.014	19.361	0.033	0.033	0.000	0.000	0.000
102	A	104	LEU	0	0.022	0.013	18.086	0.023	0.023	0.000	0.000	0.000
103	A	105	ASN	0	0.018	0.010	18.682	0.017	0.017	0.000	0.000	0.000
104	A	106	MET	0	-0.018	0.000	22.334	0.021	0.021	0.000	0.000	0.000
105	A	107	LEU	0	-0.006	0.001	24.873	0.014	0.014	0.000	0.000	0.000
106	A	108	ASN	0	0.012	-0.009	22.645	0.024	0.024	0.000	0.000	0.000
107	A	109	ARG	1	0.918	0.961	26.462	0.129	0.129	0.000	0.000	0.000
108	A	110	LEU	0	-0.011	-0.005	28.193	0.010	0.010	0.000	0.000	0.000
109	A	111	THR	0	0.033	0.016	29.770	0.011	0.011	0.000	0.000	0.000
110	A	112	TYR	0	-0.050	0.011	30.114	0.005	0.005	0.000	0.000	0.000
111	A	113	GLU	-1	-0.867	-0.951	32.048	-0.088	-0.088	0.000	0.000	0.000
112	A	114	VAL	0	-0.033	-0.011	34.300	0.007	0.007	0.000	0.000	0.000
113	A	115	THR	0	-0.048	-0.044	34.508	0.006	0.006	0.000	0.000	0.000
114	A	116	GLU	-1	-0.851	-0.924	36.324	-0.073	-0.073	0.000	0.000	0.000
115	A	117	ILE	0	-0.052	-0.022	38.039	0.005	0.005	0.000	0.000	0.000
116	A	118	ALA	0	-0.070	-0.036	39.954	0.004	0.004	0.000	0.000	0.000
117	A	119	LEU	0	-0.082	-0.054	38.989	0.004	0.004	0.000	0.000	0.000
118	A	120	ASP	-1	-0.967	-0.959	42.196	-0.047	-0.047	0.000	0.000	0.000
119	A	121	LEU	0	-0.058	-0.032	40.319	0.002	0.002	0.000	0.000	0.000
120	A	122	PRO	0	-0.039	-0.027	36.616	-0.002	-0.002	0.000	0.000	0.000
121	A	123	GLY	0	0.024	0.040	34.378	0.001	0.001	0.000	0.000	0.000
122	A	124	ILE	0	-0.035	-0.030	31.727	-0.001	-0.001	0.000	0.000	0.000
123	A	125	ASN	0	-0.029	-0.024	26.121	-0.010	-0.010	0.000	0.000	0.000
124	A	126	LEU	0	-0.033	-0.023	26.896	0.003	0.003	0.000	0.000	0.000
125	A	127	GLU	-1	-1.016	-0.995	23.775	-0.128	-0.128	0.000	0.000	0.000
126	A	128	PHE	-1	-0.759	-0.847	20.148	-0.231	-0.231	0.000	0.000	0.000

Top

Graph

Manual

About

Interactive mode: IFIE and PIEDA for fragment #1(A:3:ACE )