FMO DATABASE

FMODB ID: 17LYZ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-802514.059133
FMO2-HF: Nuclear repulsion	761389.063976
FMO2-HF: Total energy	-41124.995156
FMO2-MP2: Total energy	-41246.65845

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.
-12.218	-4.642	2.398	-3.894	-6.079	-0.015

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 : 0.056 / q_NPA : 0.029

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	-0.003	0.007	3.874	-1.329	0.398	-0.013	-0.827	-0.887	0.002
4	A	6	THR	0	0.000	-0.011	6.439	-0.613	-0.613	0.000	0.000	0.000	0.000
5	A	7	LYS	1	0.866	0.898	10.283	-0.473	-0.473	0.000	0.000	0.000	0.000
6	A	8	ALA	0	-0.010	-0.001	12.544	-0.071	-0.071	0.000	0.000	0.000	0.000
7	A	9	HIS	0	0.015	0.019	7.023	-0.364	-0.364	0.000	0.000	0.000	0.000
8	A	10	ASN	0	-0.008	-0.009	10.875	0.051	0.051	0.000	0.000	0.000	0.000
9	A	11	GLY	0	0.021	0.015	13.132	-0.064	-0.064	0.000	0.000	0.000	0.000
10	A	12	ALA	0	-0.035	-0.007	9.592	-0.047	-0.047	0.000	0.000	0.000	0.000
11	A	13	THR	0	-0.012	-0.021	9.630	-0.109	-0.109	0.000	0.000	0.000	0.000
12	A	14	LEU	0	0.004	0.016	2.448	-0.455	-0.030	1.049	-0.532	-0.942	0.002
13	A	15	THR	0	-0.050	-0.029	6.554	-0.576	-0.576	0.000	0.000	0.000	0.000
14	A	16	VAL	0	0.001	0.018	3.857	-0.009	0.174	0.000	-0.022	-0.161	0.000
15	A	17	ALA	0	0.044	0.016	6.214	0.207	0.207	0.000	0.000	0.000	0.000
16	A	18	VAL	0	-0.032	-0.023	8.351	0.008	0.008	0.000	0.000	0.000	0.000
17	A	19	GLY	0	-0.009	-0.001	10.680	-0.039	-0.039	0.000	0.000	0.000	0.000
18	A	20	GLU	-1	-0.916	-0.955	2.586	-7.030	-4.838	0.471	-1.186	-1.478	-0.015
19	A	21	LEU	0	-0.024	-0.008	5.465	-0.105	-0.105	0.000	0.000	0.000	0.000
20	A	22	VAL	0	-0.011	-0.013	2.401	-1.417	0.973	0.889	-1.114	-2.164	-0.005
21	A	23	GLU	-1	-0.839	-0.902	3.784	0.101	0.760	0.002	-0.213	-0.447	0.001
22	A	24	ILE	0	0.002	-0.001	5.911	0.454	0.454	0.000	0.000	0.000	0.000
23	A	25	GLN	0	0.004	0.015	8.129	-0.197	-0.197	0.000	0.000	0.000	0.000
24	A	26	LEU	0	0.016	0.004	11.046	0.022	0.022	0.000	0.000	0.000	0.000
25	A	27	PRO	0	-0.019	-0.012	14.108	-0.083	-0.083	0.000	0.000	0.000	0.000
26	A	28	SER	0	-0.002	-0.018	17.575	-0.004	-0.004	0.000	0.000	0.000	0.000
27	A	29	ASN	0	0.051	0.021	20.019	-0.037	-0.037	0.000	0.000	0.000	0.000
28	A	30	PRO	0	0.080	0.068	22.151	-0.007	-0.007	0.000	0.000	0.000	0.000
29	A	31	THR	0	-0.046	-0.032	25.038	-0.014	-0.014	0.000	0.000	0.000	0.000
30	A	32	THR	0	0.006	-0.008	26.148	-0.004	-0.004	0.000	0.000	0.000	0.000
31	A	33	GLY	0	0.001	-0.009	28.108	-0.003	-0.003	0.000	0.000	0.000	0.000
32	A	34	PHE	0	-0.069	-0.029	24.119	-0.001	-0.001	0.000	0.000	0.000	0.000
33	A	35	ALA	0	-0.034	-0.016	20.926	-0.007	-0.007	0.000	0.000	0.000	0.000
34	A	36	TRP	0	-0.044	-0.036	16.586	0.023	0.023	0.000	0.000	0.000	0.000
35	A	37	TYR	0	-0.018	-0.005	18.674	-0.018	-0.018	0.000	0.000	0.000	0.000
36	A	38	PHE	0	0.071	0.024	13.270	0.041	0.041	0.000	0.000	0.000	0.000
37	A	39	GLU	-1	-0.948	-0.984	18.935	0.229	0.229	0.000	0.000	0.000	0.000
38	A	40	GLY	0	0.000	0.005	22.156	-0.006	-0.006	0.000	0.000	0.000	0.000
39	A	41	GLY	0	-0.044	-0.012	23.121	-0.017	-0.017	0.000	0.000	0.000	0.000
40	A	42	THR	0	0.011	0.010	20.592	-0.010	-0.010	0.000	0.000	0.000	0.000
41	A	43	LYS	1	0.808	0.887	17.581	-0.279	-0.279	0.000	0.000	0.000	0.000
42	A	44	GLU	-1	-0.848	-0.925	16.459	0.279	0.279	0.000	0.000	0.000	0.000
43	A	45	SER	0	-0.010	-0.017	15.256	0.017	0.017	0.000	0.000	0.000	0.000
44	A	46	PRO	0	-0.005	-0.002	16.098	-0.030	-0.030	0.000	0.000	0.000	0.000
45	A	47	ASN	0	0.006	0.008	17.411	-0.035	-0.035	0.000	0.000	0.000	0.000
46	A	48	GLU	-1	-0.725	-0.849	16.607	0.271	0.271	0.000	0.000	0.000	0.000
47	A	49	SER	0	-0.039	-0.035	16.466	-0.005	-0.005	0.000	0.000	0.000	0.000
48	A	50	MET	0	-0.069	-0.012	15.230	-0.009	-0.009	0.000	0.000	0.000	0.000
49	A	51	PHE	0	0.020	-0.014	11.167	0.008	0.008	0.000	0.000	0.000	0.000
50	A	52	THR	0	-0.010	-0.002	12.831	-0.008	-0.008	0.000	0.000	0.000	0.000
51	A	53	VAL	0	-0.075	-0.036	11.793	0.083	0.083	0.000	0.000	0.000	0.000
52	A	54	GLU	-1	-0.832	-0.889	11.672	0.286	0.286	0.000	0.000	0.000	0.000
53	A	55	ASN	0	-0.066	-0.057	12.843	0.055	0.055	0.000	0.000	0.000	0.000
54	A	56	LYS	1	0.878	0.950	13.422	-0.151	-0.151	0.000	0.000	0.000	0.000
55	A	57	TYR	0	0.051	0.030	14.630	0.035	0.035	0.000	0.000	0.000	0.000
56	A	58	PHE	0	0.018	0.001	11.765	-0.074	-0.074	0.000	0.000	0.000	0.000
57	A	59	PRO	0	0.045	0.026	16.693	0.026	0.026	0.000	0.000	0.000	0.000
58	A	60	PRO	0	0.075	0.034	19.222	-0.026	-0.026	0.000	0.000	0.000	0.000
59	A	61	ASP	-1	-0.867	-0.941	17.147	-0.090	-0.090	0.000	0.000	0.000	0.000
60	A	62	SER	0	-0.021	-0.004	20.524	-0.013	-0.013	0.000	0.000	0.000	0.000
61	A	63	LYS	1	0.772	0.877	19.515	0.026	0.026	0.000	0.000	0.000	0.000
62	A	64	LEU	0	0.014	0.018	24.875	0.002	0.002	0.000	0.000	0.000	0.000
63	A	65	LEU	0	0.034	0.007	26.889	0.013	0.013	0.000	0.000	0.000	0.000
64	A	66	GLY	0	0.016	0.012	28.484	0.000	0.000	0.000	0.000	0.000	0.000
65	A	67	ALA	0	-0.019	0.008	24.850	0.016	0.016	0.000	0.000	0.000	0.000
66	A	68	GLY	0	-0.009	-0.003	22.798	0.003	0.003	0.000	0.000	0.000	0.000
67	A	69	GLY	0	-0.001	-0.002	19.194	-0.027	-0.027	0.000	0.000	0.000	0.000
68	A	70	THR	0	-0.071	-0.033	12.994	0.058	0.058	0.000	0.000	0.000	0.000
69	A	71	GLU	-1	-0.749	-0.842	15.347	0.297	0.297	0.000	0.000	0.000	0.000
70	A	72	HIS	0	0.014	0.008	8.915	0.181	0.181	0.000	0.000	0.000	0.000
71	A	73	PHE	0	0.024	0.002	10.528	-0.128	-0.128	0.000	0.000	0.000	0.000
72	A	74	HIS	1	0.779	0.856	7.701	-0.362	-0.362	0.000	0.000	0.000	0.000
73	A	75	VAL	0	0.063	0.041	7.189	-0.167	-0.167	0.000	0.000	0.000	0.000
74	A	76	THR	0	-0.008	-0.011	7.329	0.097	0.097	0.000	0.000	0.000	0.000
75	A	77	VAL	0	0.011	0.003	7.713	-0.040	-0.040	0.000	0.000	0.000	0.000
76	A	78	LYS	1	0.874	0.947	10.425	-0.257	-0.257	0.000	0.000	0.000	0.000
77	A	79	ALA	0	0.043	0.032	13.936	-0.028	-0.028	0.000	0.000	0.000	0.000
78	A	80	ALA	0	0.029	0.014	13.552	0.017	0.017	0.000	0.000	0.000	0.000
79	A	81	GLY	0	0.002	0.003	13.902	-0.004	-0.004	0.000	0.000	0.000	0.000
80	A	82	THR	0	-0.037	-0.030	12.583	0.025	0.025	0.000	0.000	0.000	0.000
81	A	83	HIS	0	-0.005	-0.009	10.871	0.017	0.017	0.000	0.000	0.000	0.000
82	A	84	ALA	0	0.035	0.014	11.170	0.094	0.094	0.000	0.000	0.000	0.000
83	A	85	VAL	0	-0.005	0.003	9.047	-0.062	-0.062	0.000	0.000	0.000	0.000
84	A	86	ASN	0	-0.029	-0.017	12.157	0.093	0.093	0.000	0.000	0.000	0.000
85	A	87	LEU	0	0.024	0.017	12.762	-0.034	-0.034	0.000	0.000	0.000	0.000
86	A	88	THR	0	-0.038	-0.039	16.441	-0.009	-0.009	0.000	0.000	0.000	0.000
87	A	89	TYR	0	0.003	0.024	19.605	-0.013	-0.013	0.000	0.000	0.000	0.000
88	A	90	MET	0	-0.002	-0.009	21.151	-0.026	-0.026	0.000	0.000	0.000	0.000
89	A	91	ARG	1	0.928	0.972	24.399	-0.152	-0.152	0.000	0.000	0.000	0.000
90	A	92	PRO	0	0.018	0.018	25.551	-0.002	-0.002	0.000	0.000	0.000	0.000
91	A	93	TRP	0	0.006	-0.002	27.079	-0.002	-0.002	0.000	0.000	0.000	0.000
92	A	94	THR	0	-0.096	-0.056	29.502	-0.010	-0.010	0.000	0.000	0.000	0.000
93	A	95	GLY	0	0.038	0.036	27.252	-0.004	-0.004	0.000	0.000	0.000	0.000
94	A	96	PRO	0	-0.015	-0.011	24.377	0.005	0.005	0.000	0.000	0.000	0.000
95	A	97	SER	0	-0.001	0.000	26.323	-0.009	-0.009	0.000	0.000	0.000	0.000
96	A	98	HIS	0	-0.018	-0.023	26.588	0.023	0.023	0.000	0.000	0.000	0.000
97	A	99	ASP	-1	-0.850	-0.920	26.999	0.209	0.209	0.000	0.000	0.000	0.000
98	A	100	SER	0	-0.079	-0.030	24.002	0.005	0.005	0.000	0.000	0.000	0.000
99	A	101	GLU	-1	-0.766	-0.864	19.420	0.466	0.466	0.000	0.000	0.000	0.000
100	A	102	ARG	1	0.915	0.941	18.993	-0.314	-0.314	0.000	0.000	0.000	0.000
101	A	103	PHE	0	-0.009	-0.003	9.862	0.017	0.017	0.000	0.000	0.000	0.000
102	A	104	ILE	0	0.017	0.021	13.313	-0.043	-0.043	0.000	0.000	0.000	0.000
103	A	105	VAL	0	0.004	0.015	7.215	0.119	0.119	0.000	0.000	0.000	0.000
104	A	106	TYR	0	0.001	0.003	10.133	-0.160	-0.160	0.000	0.000	0.000	0.000
105	A	107	LEU	0	0.008	-0.003	5.058	0.227	0.227	0.000	0.000	0.000	0.000
106	A	108	LYS	1	0.916	0.951	8.211	-0.698	-0.698	0.000	0.000	0.000	0.000
107	A	109	ALA	0	0.018	0.012	9.416	-0.020	-0.020	0.000	0.000	0.000	0.000
108	A	110	ASN	0	-0.020	-0.007	10.358	-0.024	-0.024	0.000	0.000	0.000	0.000

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