FMO DATABASE

FMODB ID: YZG12

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	OptH
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	-807574.67055
FMO2-HF: Nuclear repulsion	766450.466067
FMO2-HF: Total energy	-41124.204483
FMO2-MP2: Total energy	-41246.019596

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.
-7.516	-1.609	0.396	-2.307	-3.993	0.001

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 : 0.026

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	-0.022	0.008	3.475	-1.827	0.103	-0.006	-0.840	-1.084	0.003
4	A	6	THR	0	0.000	-0.010	5.938	-0.723	-0.723	0.000	0.000	0.000	0.000
5	A	7	LYS	1	0.913	0.920	9.732	-0.486	-0.486	0.000	0.000	0.000	0.000
6	A	8	ALA	0	-0.025	-0.003	11.311	-0.076	-0.076	0.000	0.000	0.000	0.000
7	A	9	HIS	0	0.038	0.025	7.751	-0.078	-0.078	0.000	0.000	0.000	0.000
8	A	10	ASN	0	0.035	0.024	9.992	-0.005	-0.005	0.000	0.000	0.000	0.000
9	A	11	GLY	0	-0.022	-0.016	12.518	-0.035	-0.035	0.000	0.000	0.000	0.000
10	A	12	ALA	0	-0.036	-0.004	8.676	-0.056	-0.056	0.000	0.000	0.000	0.000
11	A	13	THR	0	-0.005	-0.014	9.242	-0.138	-0.138	0.000	0.000	0.000	0.000
12	A	14	LEU	0	-0.024	-0.010	2.617	-0.498	0.084	0.292	-0.259	-0.615	0.000
13	A	15	THR	0	-0.038	-0.023	6.101	-0.397	-0.397	0.000	0.000	0.000	0.000
14	A	16	VAL	0	-0.010	-0.002	4.164	-0.233	-0.084	-0.001	-0.013	-0.134	0.000
15	A	17	ALA	0	0.021	0.001	6.664	0.122	0.122	0.000	0.000	0.000	0.000
16	A	18	VAL	0	-0.013	-0.024	9.035	0.038	0.038	0.000	0.000	0.000	0.000
17	A	19	GLY	0	-0.052	-0.028	10.942	-0.046	-0.046	0.000	0.000	0.000	0.000
18	A	20	GLU	-1	-0.902	-0.939	3.713	-1.721	-1.199	0.001	-0.161	-0.362	-0.001
19	A	21	LEU	0	-0.031	-0.022	4.970	-0.174	-0.174	0.000	0.000	0.000	0.000
20	A	22	VAL	0	0.010	0.004	3.080	-0.570	1.122	0.106	-0.590	-1.208	-0.003
21	A	23	GLU	-1	-0.822	-0.902	3.579	-0.791	0.270	0.005	-0.433	-0.632	0.002
22	A	24	ILE	0	0.017	0.005	5.646	0.394	0.365	-0.001	-0.011	0.042	0.000
23	A	25	GLN	0	-0.036	-0.030	7.659	-0.276	-0.276	0.000	0.000	0.000	0.000
24	A	26	LEU	0	0.021	0.001	10.726	0.070	0.070	0.000	0.000	0.000	0.000
25	A	27	PRO	0	-0.004	0.008	13.829	-0.081	-0.081	0.000	0.000	0.000	0.000
26	A	28	SER	0	0.005	-0.013	17.344	0.001	0.001	0.000	0.000	0.000	0.000
27	A	29	ASN	0	0.067	0.030	19.524	-0.043	-0.043	0.000	0.000	0.000	0.000
28	A	30	PRO	0	0.081	0.067	21.349	-0.001	-0.001	0.000	0.000	0.000	0.000
29	A	31	THR	0	-0.050	-0.030	24.154	-0.010	-0.010	0.000	0.000	0.000	0.000
30	A	32	THR	0	0.000	-0.003	25.435	-0.002	-0.002	0.000	0.000	0.000	0.000
31	A	33	GLY	0	0.003	-0.008	27.143	-0.002	-0.002	0.000	0.000	0.000	0.000
32	A	34	PHE	0	-0.072	-0.043	23.485	-0.001	-0.001	0.000	0.000	0.000	0.000
33	A	35	ALA	0	-0.031	-0.017	20.661	-0.007	-0.007	0.000	0.000	0.000	0.000
34	A	36	TRP	0	-0.045	-0.043	16.302	0.023	0.023	0.000	0.000	0.000	0.000
35	A	37	TYR	0	-0.035	-0.017	18.415	-0.018	-0.018	0.000	0.000	0.000	0.000
36	A	38	PHE	0	0.073	0.031	13.371	0.047	0.047	0.000	0.000	0.000	0.000
37	A	39	GLU	-1	-0.917	-0.973	18.784	0.213	0.213	0.000	0.000	0.000	0.000
38	A	40	GLY	0	-0.005	-0.002	22.016	-0.006	-0.006	0.000	0.000	0.000	0.000
39	A	41	GLY	0	-0.067	-0.030	23.042	-0.015	-0.015	0.000	0.000	0.000	0.000
40	A	42	THR	0	-0.011	0.000	21.876	-0.012	-0.012	0.000	0.000	0.000	0.000
41	A	43	LYS	1	0.829	0.902	17.543	-0.255	-0.255	0.000	0.000	0.000	0.000
42	A	44	GLU	-1	-0.847	-0.926	17.041	0.236	0.236	0.000	0.000	0.000	0.000
43	A	45	SER	0	-0.034	-0.023	15.559	0.022	0.022	0.000	0.000	0.000	0.000
44	A	46	PRO	0	0.001	0.002	16.512	-0.028	-0.028	0.000	0.000	0.000	0.000
45	A	47	ASN	0	-0.005	-0.023	17.929	-0.038	-0.038	0.000	0.000	0.000	0.000
46	A	48	GLU	-1	-0.805	-0.908	17.349	0.230	0.230	0.000	0.000	0.000	0.000
47	A	49	SER	0	-0.032	-0.009	17.535	-0.008	-0.008	0.000	0.000	0.000	0.000
48	A	50	MET	0	-0.087	-0.019	15.534	-0.004	-0.004	0.000	0.000	0.000	0.000
49	A	51	PHE	0	0.014	-0.013	11.674	0.022	0.022	0.000	0.000	0.000	0.000
50	A	52	THR	0	0.032	0.041	12.879	-0.025	-0.025	0.000	0.000	0.000	0.000
51	A	53	VAL	0	-0.044	-0.025	12.049	0.095	0.095	0.000	0.000	0.000	0.000
52	A	54	GLU	-1	-0.923	-0.935	12.201	0.065	0.065	0.000	0.000	0.000	0.000
53	A	55	ASN	0	-0.020	-0.037	12.685	0.060	0.060	0.000	0.000	0.000	0.000
54	A	56	LYS	1	0.908	0.979	12.832	-0.021	-0.021	0.000	0.000	0.000	0.000
55	A	57	TYR	0	0.034	0.024	14.224	0.043	0.043	0.000	0.000	0.000	0.000
56	A	58	PHE	0	-0.033	-0.030	11.024	-0.089	-0.089	0.000	0.000	0.000	0.000
57	A	59	PRO	0	0.046	0.013	15.844	0.035	0.035	0.000	0.000	0.000	0.000
58	A	60	PRO	0	0.048	0.030	18.064	-0.027	-0.027	0.000	0.000	0.000	0.000
59	A	61	ASP	-1	-0.886	-0.954	16.889	-0.188	-0.188	0.000	0.000	0.000	0.000
60	A	62	SER	0	-0.023	-0.018	19.798	-0.010	-0.010	0.000	0.000	0.000	0.000
61	A	63	LYS	1	0.843	0.926	19.470	0.090	0.090	0.000	0.000	0.000	0.000
62	A	64	LEU	0	-0.009	0.009	24.424	0.004	0.004	0.000	0.000	0.000	0.000
63	A	65	LEU	0	0.054	0.010	26.223	0.012	0.012	0.000	0.000	0.000	0.000
64	A	66	GLY	0	0.007	0.009	27.824	0.002	0.002	0.000	0.000	0.000	0.000
65	A	67	ALA	0	-0.014	0.015	23.775	0.019	0.019	0.000	0.000	0.000	0.000
66	A	68	GLY	0	-0.015	-0.013	21.897	-0.001	-0.001	0.000	0.000	0.000	0.000
67	A	69	GLY	0	-0.017	-0.013	18.528	-0.026	-0.026	0.000	0.000	0.000	0.000
68	A	70	THR	0	-0.050	-0.030	12.504	0.062	0.062	0.000	0.000	0.000	0.000
69	A	71	GLU	-1	-0.741	-0.833	14.697	0.268	0.268	0.000	0.000	0.000	0.000
70	A	72	HIS	0	0.014	0.003	8.222	0.225	0.225	0.000	0.000	0.000	0.000
71	A	73	PHE	0	0.028	-0.001	10.586	-0.145	-0.145	0.000	0.000	0.000	0.000
72	A	74	HIS	1	0.792	0.877	6.760	-0.160	-0.160	0.000	0.000	0.000	0.000
73	A	75	VAL	0	0.065	0.030	7.687	-0.195	-0.195	0.000	0.000	0.000	0.000
74	A	76	THR	0	-0.004	0.003	7.469	0.115	0.115	0.000	0.000	0.000	0.000
75	A	77	VAL	0	0.026	0.021	8.616	-0.060	-0.060	0.000	0.000	0.000	0.000
76	A	78	LYS	1	0.908	0.959	10.970	-0.224	-0.224	0.000	0.000	0.000	0.000
77	A	79	ALA	0	0.046	0.030	14.346	-0.032	-0.032	0.000	0.000	0.000	0.000
78	A	80	ALA	0	0.019	0.019	14.130	0.025	0.025	0.000	0.000	0.000	0.000
79	A	81	GLY	0	0.014	0.006	14.504	-0.006	-0.006	0.000	0.000	0.000	0.000
80	A	82	THR	0	-0.039	-0.025	12.368	0.027	0.027	0.000	0.000	0.000	0.000
81	A	83	HIS	0	-0.019	-0.028	11.516	-0.006	-0.006	0.000	0.000	0.000	0.000
82	A	84	ALA	0	0.018	0.015	11.451	0.070	0.070	0.000	0.000	0.000	0.000
83	A	85	VAL	0	-0.011	0.002	9.482	-0.048	-0.048	0.000	0.000	0.000	0.000
84	A	86	ASN	0	0.022	-0.001	12.348	0.097	0.097	0.000	0.000	0.000	0.000
85	A	87	LEU	0	-0.015	-0.006	12.587	-0.036	-0.036	0.000	0.000	0.000	0.000
86	A	88	THR	0	-0.021	-0.028	16.300	0.007	0.007	0.000	0.000	0.000	0.000
87	A	89	TYR	0	0.013	0.026	19.447	-0.016	-0.016	0.000	0.000	0.000	0.000
88	A	90	MET	0	-0.021	-0.013	20.799	-0.022	-0.022	0.000	0.000	0.000	0.000
89	A	91	ARG	1	0.927	0.966	24.114	-0.147	-0.147	0.000	0.000	0.000	0.000
90	A	92	PRO	0	0.017	0.022	25.417	0.000	0.000	0.000	0.000	0.000	0.000
91	A	93	TRP	0	0.013	-0.001	26.873	-0.001	-0.001	0.000	0.000	0.000	0.000
92	A	94	THR	0	-0.098	-0.037	29.292	-0.009	-0.009	0.000	0.000	0.000	0.000
93	A	95	GLY	0	0.035	0.019	26.868	-0.003	-0.003	0.000	0.000	0.000	0.000
94	A	96	PRO	0	-0.030	-0.027	24.297	0.004	0.004	0.000	0.000	0.000	0.000
95	A	97	SER	0	-0.004	-0.017	26.212	-0.018	-0.018	0.000	0.000	0.000	0.000
96	A	98	HIS	0	-0.027	-0.016	26.584	0.019	0.019	0.000	0.000	0.000	0.000
97	A	99	ASP	-1	-0.858	-0.921	27.027	0.215	0.215	0.000	0.000	0.000	0.000
98	A	100	SER	0	-0.081	-0.033	23.423	0.001	0.001	0.000	0.000	0.000	0.000
99	A	101	GLU	-1	-0.788	-0.868	18.593	0.465	0.465	0.000	0.000	0.000	0.000
100	A	102	ARG	1	0.938	0.960	18.552	-0.328	-0.328	0.000	0.000	0.000	0.000
101	A	103	PHE	0	-0.025	-0.019	9.149	0.020	0.020	0.000	0.000	0.000	0.000
102	A	104	ILE	0	0.014	0.019	13.140	-0.046	-0.046	0.000	0.000	0.000	0.000
103	A	105	VAL	0	0.002	0.026	6.710	0.124	0.124	0.000	0.000	0.000	0.000
104	A	106	TYR	0	0.018	0.004	9.818	-0.153	-0.153	0.000	0.000	0.000	0.000
105	A	107	LEU	0	0.007	0.008	5.498	0.157	0.157	0.000	0.000	0.000	0.000
106	A	108	LYS	1	0.938	0.974	8.484	-0.506	-0.506	0.000	0.000	0.000	0.000
107	A	109	ALA	0	0.033	0.014	9.646	-0.024	-0.024	0.000	0.000	0.000	0.000
108	A	110	ASN	0	-0.005	0.011	11.194	-0.027	-0.027	0.000	0.000	0.000	0.000

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