FMO DATABASE

FMODB ID: Q83MY

Calculation Name: 1HEK-A-Xray309

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1HEK

Chain ID: A

ChEMBL ID:

UniProt ID: P69732

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:

Apendix: None

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	117
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-978147.392916
FMO2-HF: Nuclear repulsion	932121.541041
FMO2-HF: Total energy	-46025.851875
FMO2-MP2: Total energy	-46160.886772

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:-6:ALA )

Summations of interaction energy for fragment #1(A:-6: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.
-49.046	-48.142	-0.008	-0.483	-0.412	0

Interaction energy analysis for fragmet #1(A:-6:ALA )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.861 / q_NPA : 0.916

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	-4	ALA	0	0.059	0.018	3.871	-3.890	-2.986	-0.008	-0.483	-0.412
4	A	-3	ASP	-1	-0.910	-0.933	6.921	-29.432	-29.432	0.000	0.000	0.000
5	A	-2	ILE	0	-0.045	-0.049	9.774	3.112	3.112	0.000	0.000	0.000
6	A	-1	GLY	0	0.026	0.034	12.382	1.228	1.228	0.000	0.000	0.000
7	A	0	SER	0	0.010	-0.002	13.452	-0.064	-0.064	0.000	0.000	0.000
8	A	1	MET	0	-0.070	-0.030	15.865	1.091	1.091	0.000	0.000	0.000
9	A	2	GLY	0	-0.043	-0.031	18.078	0.229	0.229	0.000	0.000	0.000
10	A	3	ASP	-1	-0.755	-0.887	18.797	-16.623	-16.623	0.000	0.000	0.000
11	A	4	PRO	0	-0.082	-0.008	21.059	0.520	0.520	0.000	0.000	0.000
12	A	5	LEU	0	-0.034	-0.036	24.627	0.457	0.457	0.000	0.000	0.000
13	A	6	THR	0	0.008	0.012	25.630	-0.012	-0.012	0.000	0.000	0.000
14	A	7	TRP	0	0.067	0.028	25.594	0.463	0.463	0.000	0.000	0.000
15	A	8	SER	0	0.071	0.030	27.147	0.277	0.277	0.000	0.000	0.000
16	A	9	LYS	1	0.936	0.970	29.633	10.135	10.135	0.000	0.000	0.000
17	A	10	ALA	0	0.022	0.011	27.452	0.311	0.311	0.000	0.000	0.000
18	A	11	LEU	0	0.073	0.033	29.532	0.292	0.292	0.000	0.000	0.000
19	A	12	LYS	1	0.971	1.008	31.629	8.581	8.581	0.000	0.000	0.000
20	A	13	LYS	1	0.862	0.900	32.152	9.819	9.819	0.000	0.000	0.000
21	A	14	LEU	0	-0.005	0.002	28.659	0.147	0.147	0.000	0.000	0.000
22	A	15	GLU	-1	-0.914	-0.948	32.679	-8.280	-8.280	0.000	0.000	0.000
23	A	16	LYS	1	0.781	0.907	36.021	8.675	8.675	0.000	0.000	0.000
24	A	17	VAL	0	0.033	0.050	32.490	0.234	0.234	0.000	0.000	0.000
25	A	18	THR	0	0.001	-0.005	35.760	0.030	0.030	0.000	0.000	0.000
26	A	19	VAL	0	0.029	0.024	35.645	-0.260	-0.260	0.000	0.000	0.000
27	A	20	GLN	0	-0.011	-0.032	35.799	-0.066	-0.066	0.000	0.000	0.000
28	A	21	GLY	0	0.001	0.029	38.257	0.106	0.106	0.000	0.000	0.000
29	A	22	SER	0	0.027	0.004	42.050	0.064	0.064	0.000	0.000	0.000
30	A	23	GLN	0	-0.012	-0.006	40.382	0.298	0.298	0.000	0.000	0.000
31	A	24	LYS	1	0.844	0.917	39.108	7.791	7.791	0.000	0.000	0.000
32	A	25	LEU	0	0.050	0.038	32.042	0.022	0.022	0.000	0.000	0.000
33	A	26	THR	0	0.022	0.005	36.674	0.029	0.029	0.000	0.000	0.000
34	A	27	THR	0	0.083	0.032	34.824	-0.332	-0.332	0.000	0.000	0.000
35	A	28	GLY	0	0.094	0.019	33.872	-0.278	-0.278	0.000	0.000	0.000
36	A	29	ASN	0	-0.037	-0.012	33.989	-0.050	-0.050	0.000	0.000	0.000
37	A	30	CYS	0	0.000	0.007	30.097	-0.295	-0.295	0.000	0.000	0.000
38	A	31	ASN	0	-0.005	-0.003	30.026	0.076	0.076	0.000	0.000	0.000
39	A	32	TRP	0	-0.011	0.047	30.318	-0.296	-0.296	0.000	0.000	0.000
40	A	33	ALA	0	0.071	0.043	27.796	-0.186	-0.186	0.000	0.000	0.000
41	A	34	LEU	0	-0.038	0.015	23.829	-0.379	-0.379	0.000	0.000	0.000
42	A	35	SER	0	0.034	-0.041	25.826	-0.379	-0.379	0.000	0.000	0.000
43	A	36	LEU	0	-0.080	-0.036	27.468	-0.125	-0.125	0.000	0.000	0.000
44	A	37	VAL	0	0.019	0.008	21.688	-0.093	-0.093	0.000	0.000	0.000
45	A	38	ASP	-1	-0.830	-0.914	23.108	-13.359	-13.359	0.000	0.000	0.000
46	A	39	LEU	0	0.010	0.009	24.143	-0.040	-0.040	0.000	0.000	0.000
47	A	40	PHE	0	-0.026	-0.009	21.818	0.113	0.113	0.000	0.000	0.000
48	A	41	HIS	0	-0.045	-0.015	19.681	-0.246	-0.246	0.000	0.000	0.000
49	A	42	ASP	-1	-0.944	-0.965	20.902	-13.279	-13.279	0.000	0.000	0.000
50	A	43	THR	0	-0.090	-0.010	18.655	-0.418	-0.418	0.000	0.000	0.000
51	A	44	ASN	0	0.044	-0.043	21.524	0.936	0.936	0.000	0.000	0.000
52	A	45	PHE	0	0.021	-0.001	17.570	0.324	0.324	0.000	0.000	0.000
53	A	46	VAL	0	-0.049	-0.038	23.160	0.415	0.415	0.000	0.000	0.000
54	A	47	LYS	1	0.868	0.969	25.801	12.262	12.262	0.000	0.000	0.000
55	A	48	GLU	-1	-0.996	-1.001	21.459	-13.376	-13.376	0.000	0.000	0.000
56	A	49	LYS	1	0.875	0.938	24.769	10.802	10.802	0.000	0.000	0.000
57	A	50	ASP	-1	-0.831	-0.938	23.781	-12.788	-12.788	0.000	0.000	0.000
58	A	51	TRP	0	0.019	-0.003	19.707	-0.358	-0.358	0.000	0.000	0.000
59	A	52	GLN	0	0.032	0.011	16.641	0.961	0.961	0.000	0.000	0.000
60	A	53	LEU	0	0.003	0.021	17.517	-0.449	-0.449	0.000	0.000	0.000
61	A	54	ARG	1	0.963	0.987	11.275	23.032	23.032	0.000	0.000	0.000
62	A	55	ASP	-1	-0.912	-0.952	13.589	-22.375	-22.375	0.000	0.000	0.000
63	A	56	VAL	0	0.010	0.003	14.876	-0.042	-0.042	0.000	0.000	0.000
64	A	57	ILE	0	-0.105	-0.069	15.864	0.391	0.391	0.000	0.000	0.000
65	A	58	PRO	0	0.012	-0.002	12.446	0.638	0.638	0.000	0.000	0.000
66	A	59	LEU	0	-0.014	0.012	15.111	0.188	0.188	0.000	0.000	0.000
67	A	60	LEU	0	-0.042	-0.031	17.857	0.848	0.848	0.000	0.000	0.000
68	A	61	GLU	-1	-0.900	-0.944	18.111	-13.750	-13.750	0.000	0.000	0.000
69	A	62	ASP	-1	-0.849	-0.916	18.467	-15.931	-15.931	0.000	0.000	0.000
70	A	63	VAL	0	0.005	0.015	21.331	0.776	0.776	0.000	0.000	0.000
71	A	64	THR	0	-0.070	-0.037	23.816	0.613	0.613	0.000	0.000	0.000
72	A	65	GLN	0	0.013	0.009	23.430	1.110	1.110	0.000	0.000	0.000
73	A	66	THR	0	-0.038	-0.032	25.236	0.416	0.416	0.000	0.000	0.000
74	A	67	LEU	0	-0.050	-0.033	27.677	0.519	0.519	0.000	0.000	0.000
75	A	68	SER	0	0.043	0.014	30.370	-0.063	-0.063	0.000	0.000	0.000
76	A	69	GLY	0	0.006	0.007	32.771	0.072	0.072	0.000	0.000	0.000
77	A	70	GLN	0	0.107	0.036	33.854	-0.268	-0.268	0.000	0.000	0.000
78	A	71	GLU	-1	-0.922	-0.954	33.415	-8.972	-8.972	0.000	0.000	0.000
79	A	72	ARG	1	0.865	0.951	28.546	10.673	10.673	0.000	0.000	0.000
80	A	73	GLU	-1	-0.922	-0.982	29.993	-9.220	-9.220	0.000	0.000	0.000
81	A	74	ALA	0	-0.033	-0.012	31.062	-0.130	-0.130	0.000	0.000	0.000
82	A	75	PHE	0	0.052	0.025	23.977	-0.096	-0.096	0.000	0.000	0.000
83	A	76	GLU	-1	-0.931	-0.947	26.237	-11.208	-11.208	0.000	0.000	0.000
84	A	77	ARG	1	0.937	0.982	27.168	9.289	9.289	0.000	0.000	0.000
85	A	78	THR	0	-0.042	-0.027	28.886	0.115	0.115	0.000	0.000	0.000
86	A	79	TRP	0	0.054	-0.052	23.118	-0.293	-0.293	0.000	0.000	0.000
87	A	80	TRP	0	0.046	0.040	25.002	0.205	0.205	0.000	0.000	0.000
88	A	81	ALA	0	0.019	0.016	25.903	-0.152	-0.152	0.000	0.000	0.000
89	A	82	ILE	0	-0.005	0.035	25.062	-0.191	-0.191	0.000	0.000	0.000
90	A	83	SER	0	-0.053	-0.034	21.801	-0.383	-0.383	0.000	0.000	0.000
91	A	84	ALA	0	0.025	0.012	23.445	-0.159	-0.159	0.000	0.000	0.000
92	A	85	VAL	0	-0.086	-0.038	25.291	0.006	0.006	0.000	0.000	0.000
93	A	86	LYS	1	0.830	0.926	21.817	13.601	13.601	0.000	0.000	0.000
94	A	87	MET	0	-0.024	-0.029	19.069	-0.259	-0.259	0.000	0.000	0.000
95	A	88	GLY	0	-0.070	-0.038	23.642	0.115	0.115	0.000	0.000	0.000
96	A	89	LEU	0	-0.012	0.004	25.594	0.319	0.319	0.000	0.000	0.000
97	A	90	GLN	0	-0.101	-0.068	27.887	0.412	0.412	0.000	0.000	0.000
98	A	91	ILE	0	0.020	0.059	30.539	0.160	0.160	0.000	0.000	0.000
99	A	92	ASN	0	-0.026	-0.041	32.559	-0.010	-0.010	0.000	0.000	0.000
100	A	93	ASN	0	0.013	-0.047	34.116	0.086	0.086	0.000	0.000	0.000
101	A	94	VAL	0	0.039	0.038	31.556	-0.231	-0.231	0.000	0.000	0.000
102	A	95	VAL	0	0.037	-0.007	31.277	-0.208	-0.208	0.000	0.000	0.000
103	A	96	ASP	-1	-0.916	-0.937	30.518	-9.226	-9.226	0.000	0.000	0.000
104	A	97	GLY	0	0.103	0.031	28.213	-0.041	-0.041	0.000	0.000	0.000
105	A	98	LYS	1	0.945	0.987	26.280	10.038	10.038	0.000	0.000	0.000
106	A	99	ALA	0	-0.041	-0.020	24.723	-0.521	-0.521	0.000	0.000	0.000
107	A	100	SER	0	0.055	0.004	23.338	-0.347	-0.347	0.000	0.000	0.000
108	A	101	PHE	0	0.006	0.029	21.331	-0.622	-0.622	0.000	0.000	0.000
109	A	102	GLN	0	0.015	-0.016	20.089	-0.504	-0.504	0.000	0.000	0.000
110	A	103	LEU	0	-0.070	-0.023	17.842	-0.722	-0.722	0.000	0.000	0.000
111	A	104	LEU	0	-0.005	-0.031	17.097	-0.924	-0.924	0.000	0.000	0.000
112	A	105	ARG	1	0.910	1.006	16.027	14.826	14.826	0.000	0.000	0.000
113	A	106	ALA	0	0.020	-0.008	14.272	-1.184	-1.184	0.000	0.000	0.000
114	A	107	LYS	1	0.892	0.970	12.612	17.232	17.232	0.000	0.000	0.000
115	A	108	TYR	0	-0.048	-0.035	11.298	-1.663	-1.663	0.000	0.000	0.000
116	A	109	GLU	-1	-0.880	-0.944	11.479	-19.305	-19.305	0.000	0.000	0.000
117	A	110	NME	0	-0.013	0.009	8.103	-0.173	-0.173	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-6:ALA )