FMO DATABASE

FMODB ID: V5GN1

Calculation Name: 2H7W-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2H7W

Chain ID: A

ChEMBL ID:

UniProt ID: Q966X9

Base Structure: X-ray

Registration Date: 2023-09-19

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	108
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-806700.536454
FMO2-HF: Nuclear repulsion	765575.843235
FMO2-HF: Total energy	-41124.693219
FMO2-MP2: Total energy	-41246.471897

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:HIS)

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

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.
-7.366	-2.191	2.713	-3.01	-4.878	-0.003

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.044 / q_NPA : 0.020

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	5	VAL	0	-0.015	0.008	3.448	-1.727	0.225	-0.011	-0.861	-1.080	0.002
4	A	6	THR	0	0.014	0.002	5.906	-0.680	-0.680	0.000	0.000	0.000	0.000
5	A	7	LYS	1	0.873	0.899	9.700	-0.543	-0.543	0.000	0.000	0.000	0.000
6	A	8	ALA	0	-0.018	-0.004	11.317	-0.082	-0.082	0.000	0.000	0.000	0.000
7	A	9	HIS	0	0.033	0.019	7.099	-0.300	-0.300	0.000	0.000	0.000	0.000
8	A	10	ASN	0	0.010	0.006	9.962	-0.029	-0.029	0.000	0.000	0.000	0.000
9	A	11	GLY	0	-0.016	-0.012	12.459	-0.037	-0.037	0.000	0.000	0.000	0.000
10	A	12	ALA	0	-0.030	-0.004	8.671	-0.062	-0.062	0.000	0.000	0.000	0.000
11	A	13	THR	0	-0.018	-0.017	9.281	-0.145	-0.145	0.000	0.000	0.000	0.000
12	A	14	LEU	0	-0.007	-0.002	2.147	-0.130	-0.449	2.553	-0.907	-1.327	-0.001
13	A	15	THR	0	-0.051	-0.025	6.102	-0.398	-0.398	0.000	0.000	0.000	0.000
14	A	16	VAL	0	0.004	0.003	4.164	-0.233	-0.083	-0.001	-0.013	-0.136	0.000
15	A	17	ALA	0	0.015	0.002	6.644	0.155	0.155	0.000	0.000	0.000	0.000
16	A	18	VAL	0	-0.014	-0.025	9.010	0.029	0.029	0.000	0.000	0.000	0.000
17	A	19	GLY	0	-0.045	-0.025	10.930	-0.048	-0.048	0.000	0.000	0.000	0.000
18	A	20	GLU	-1	-0.912	-0.947	3.630	-2.221	-1.656	0.002	-0.184	-0.384	-0.001
19	A	21	LEU	0	-0.032	-0.017	5.235	-0.115	-0.115	0.000	0.000	0.000	0.000
20	A	22	VAL	0	0.015	0.003	2.785	-0.751	1.055	0.166	-0.636	-1.335	-0.004
21	A	23	GLU	-1	-0.834	-0.901	3.575	-0.252	0.769	0.004	-0.409	-0.616	0.001
22	A	24	ILE	0	0.006	-0.001	5.632	0.345	0.345	0.000	0.000	0.000	0.000
23	A	25	GLN	0	0.007	0.009	7.921	-0.144	-0.144	0.000	0.000	0.000	0.000
24	A	26	LEU	0	-0.002	-0.004	10.726	0.060	0.060	0.000	0.000	0.000	0.000
25	A	27	PRO	0	-0.006	0.001	13.802	-0.082	-0.082	0.000	0.000	0.000	0.000
26	A	28	SER	0	0.003	-0.017	17.316	-0.006	-0.006	0.000	0.000	0.000	0.000
27	A	29	ASN	0	0.077	0.041	19.648	-0.040	-0.040	0.000	0.000	0.000	0.000
28	A	30	PRO	0	0.081	0.065	21.545	-0.004	-0.004	0.000	0.000	0.000	0.000
29	A	31	THR	0	-0.049	-0.031	24.336	-0.014	-0.014	0.000	0.000	0.000	0.000
30	A	32	THR	0	-0.004	-0.017	25.476	-0.003	-0.003	0.000	0.000	0.000	0.000
31	A	33	GLY	0	0.004	-0.001	27.329	-0.004	-0.004	0.000	0.000	0.000	0.000
32	A	34	PHE	0	-0.085	-0.044	23.513	-0.003	-0.003	0.000	0.000	0.000	0.000
33	A	35	ALA	0	-0.024	-0.010	20.680	-0.005	-0.005	0.000	0.000	0.000	0.000
34	A	36	TRP	0	-0.040	-0.034	16.297	0.023	0.023	0.000	0.000	0.000	0.000
35	A	37	TYR	0	-0.033	-0.005	18.398	-0.018	-0.018	0.000	0.000	0.000	0.000
36	A	38	PHE	0	0.071	0.032	13.271	0.043	0.043	0.000	0.000	0.000	0.000
37	A	39	GLU	-1	-0.925	-0.976	18.776	0.217	0.217	0.000	0.000	0.000	0.000
38	A	40	GLY	0	-0.002	0.001	22.009	-0.006	-0.006	0.000	0.000	0.000	0.000
39	A	41	GLY	0	-0.066	-0.022	23.029	-0.015	-0.015	0.000	0.000	0.000	0.000
40	A	42	THR	0	0.020	0.012	21.215	-0.018	-0.018	0.000	0.000	0.000	0.000
41	A	43	LYS	1	0.819	0.896	17.799	-0.273	-0.273	0.000	0.000	0.000	0.000
42	A	44	GLU	-1	-0.867	-0.940	17.040	0.240	0.240	0.000	0.000	0.000	0.000
43	A	45	SER	0	-0.007	-0.019	15.850	0.025	0.025	0.000	0.000	0.000	0.000
44	A	46	PRO	0	-0.016	-0.004	16.516	-0.029	-0.029	0.000	0.000	0.000	0.000
45	A	47	ASN	0	0.001	-0.009	17.922	-0.037	-0.037	0.000	0.000	0.000	0.000
46	A	48	GLU	-1	-0.738	-0.857	17.363	0.226	0.226	0.000	0.000	0.000	0.000
47	A	49	SER	0	-0.026	-0.014	17.513	-0.011	-0.011	0.000	0.000	0.000	0.000
48	A	50	MET	0	-0.096	-0.026	15.636	-0.008	-0.008	0.000	0.000	0.000	0.000
49	A	51	PHE	0	0.021	-0.007	11.728	0.013	0.013	0.000	0.000	0.000	0.000
50	A	52	THR	0	0.004	0.007	12.865	-0.018	-0.018	0.000	0.000	0.000	0.000
51	A	53	VAL	0	-0.051	-0.028	12.030	0.090	0.090	0.000	0.000	0.000	0.000
52	A	54	GLU	-1	-0.851	-0.897	11.254	0.135	0.135	0.000	0.000	0.000	0.000
53	A	55	ASN	0	-0.044	-0.037	12.678	0.061	0.061	0.000	0.000	0.000	0.000
54	A	56	LYS	1	0.872	0.953	12.949	-0.107	-0.107	0.000	0.000	0.000	0.000
55	A	57	TYR	0	0.050	0.035	14.388	0.051	0.051	0.000	0.000	0.000	0.000
56	A	58	PHE	0	-0.013	-0.023	11.344	-0.085	-0.085	0.000	0.000	0.000	0.000
57	A	59	PRO	0	0.051	0.020	16.018	0.036	0.036	0.000	0.000	0.000	0.000
58	A	60	PRO	0	0.046	0.028	18.241	-0.018	-0.018	0.000	0.000	0.000	0.000
59	A	61	ASP	-1	-0.850	-0.940	16.726	-0.104	-0.104	0.000	0.000	0.000	0.000
60	A	62	SER	0	-0.028	-0.017	19.967	-0.015	-0.015	0.000	0.000	0.000	0.000
61	A	63	LYS	1	0.810	0.911	19.387	0.031	0.031	0.000	0.000	0.000	0.000
62	A	64	LEU	0	-0.005	0.013	24.597	0.000	0.000	0.000	0.000	0.000	0.000
63	A	65	LEU	0	0.049	0.009	26.408	0.013	0.013	0.000	0.000	0.000	0.000
64	A	66	GLY	0	0.011	0.009	28.009	0.002	0.002	0.000	0.000	0.000	0.000
65	A	67	ALA	0	-0.016	0.012	24.105	0.019	0.019	0.000	0.000	0.000	0.000
66	A	68	GLY	0	-0.010	-0.010	22.091	-0.001	-0.001	0.000	0.000	0.000	0.000
67	A	69	GLY	0	-0.010	-0.009	18.718	-0.023	-0.023	0.000	0.000	0.000	0.000
68	A	70	THR	0	-0.077	-0.046	12.697	0.066	0.066	0.000	0.000	0.000	0.000
69	A	71	GLU	-1	-0.748	-0.837	14.877	0.296	0.296	0.000	0.000	0.000	0.000
70	A	72	HIS	0	0.021	0.002	8.434	0.198	0.198	0.000	0.000	0.000	0.000
71	A	73	PHE	0	0.018	-0.005	10.598	-0.159	-0.159	0.000	0.000	0.000	0.000
72	A	74	HIS	1	0.780	0.876	6.914	-0.193	-0.193	0.000	0.000	0.000	0.000
73	A	75	VAL	0	0.057	0.023	7.670	-0.194	-0.194	0.000	0.000	0.000	0.000
74	A	76	THR	0	-0.013	0.000	7.449	0.075	0.075	0.000	0.000	0.000	0.000
75	A	77	VAL	0	0.021	0.016	8.379	-0.046	-0.046	0.000	0.000	0.000	0.000
76	A	78	LYS	1	0.900	0.960	10.994	-0.198	-0.198	0.000	0.000	0.000	0.000
77	A	79	ALA	0	0.041	0.027	14.358	-0.030	-0.030	0.000	0.000	0.000	0.000
78	A	80	ALA	0	0.023	0.012	14.154	0.020	0.020	0.000	0.000	0.000	0.000
79	A	81	GLY	0	0.005	0.005	14.529	-0.001	-0.001	0.000	0.000	0.000	0.000
80	A	82	THR	0	-0.029	-0.023	12.472	0.010	0.010	0.000	0.000	0.000	0.000
81	A	83	HIS	0	-0.012	-0.013	11.537	0.005	0.005	0.000	0.000	0.000	0.000
82	A	84	ALA	0	0.018	0.012	11.455	0.069	0.069	0.000	0.000	0.000	0.000
83	A	85	VAL	0	-0.013	-0.001	9.395	-0.048	-0.048	0.000	0.000	0.000	0.000
84	A	86	ASN	0	0.002	-0.008	12.344	0.093	0.093	0.000	0.000	0.000	0.000
85	A	87	LEU	0	0.014	0.008	12.741	-0.035	-0.035	0.000	0.000	0.000	0.000
86	A	88	THR	0	-0.031	-0.030	16.286	0.000	0.000	0.000	0.000	0.000	0.000
87	A	89	TYR	0	0.013	0.022	19.429	-0.011	-0.011	0.000	0.000	0.000	0.000
88	A	90	MET	0	-0.002	-0.011	20.778	-0.024	-0.024	0.000	0.000	0.000	0.000
89	A	91	ARG	1	0.927	0.970	24.097	-0.159	-0.159	0.000	0.000	0.000	0.000
90	A	92	PRO	0	0.014	0.023	25.367	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	93	TRP	0	0.008	-0.009	26.860	-0.002	-0.002	0.000	0.000	0.000	0.000
92	A	94	THR	0	-0.083	-0.033	29.265	-0.008	-0.008	0.000	0.000	0.000	0.000
93	A	95	GLY	0	0.042	0.025	26.853	-0.004	-0.004	0.000	0.000	0.000	0.000
94	A	96	PRO	0	-0.025	-0.024	24.269	0.005	0.005	0.000	0.000	0.000	0.000
95	A	97	SER	0	-0.015	-0.018	26.196	-0.016	-0.016	0.000	0.000	0.000	0.000
96	A	98	HIS	0	-0.048	-0.032	26.564	0.019	0.019	0.000	0.000	0.000	0.000
97	A	99	ASP	-1	-0.841	-0.912	27.057	0.223	0.223	0.000	0.000	0.000	0.000
98	A	100	SER	0	-0.087	-0.036	23.436	0.004	0.004	0.000	0.000	0.000	0.000
99	A	101	GLU	-1	-0.756	-0.851	18.923	0.507	0.507	0.000	0.000	0.000	0.000
100	A	102	ARG	1	0.941	0.959	18.543	-0.329	-0.329	0.000	0.000	0.000	0.000
101	A	103	PHE	0	-0.016	-0.012	9.212	0.025	0.025	0.000	0.000	0.000	0.000
102	A	104	ILE	0	0.015	0.018	13.097	-0.050	-0.050	0.000	0.000	0.000	0.000
103	A	105	VAL	0	0.010	0.030	6.674	0.125	0.125	0.000	0.000	0.000	0.000
104	A	106	TYR	0	0.005	-0.003	9.818	-0.167	-0.167	0.000	0.000	0.000	0.000
105	A	107	LEU	0	0.008	0.011	5.529	0.158	0.158	0.000	0.000	0.000	0.000
106	A	108	LYS	1	0.916	0.958	8.493	-0.513	-0.513	0.000	0.000	0.000	0.000
107	A	109	ALA	0	0.024	0.012	9.626	-0.034	-0.034	0.000	0.000	0.000	0.000
108	A	110	ASN	0	0.003	0.016	11.170	-0.012	-0.012	0.000	0.000	0.000	0.000

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