FMO DATABASE

FMODB ID: 2N9ZR

Calculation Name: 1U7I-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1U7I

Chain ID: A

ChEMBL ID:

UniProt ID: Q9I3Y6

Base Structure: X-ray

Registration Date: 2023-09-23

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	134
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1124199.084436
FMO2-HF: Nuclear repulsion	1071515.907433
FMO2-HF: Total energy	-52683.177002
FMO2-MP2: Total energy	-52835.333454

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:0:HIS)

Summations of interaction energy for fragment #1(A:0: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.
-3.372	-1.993	-0.025	-0.594	-0.76	0.002

Interaction energy analysis for fragmet #1(A:0:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.016 / 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	2	SER	0	0.039	0.019	3.805	-2.868	-1.489	-0.025	-0.594	-0.760	0.002
4	A	3	ALA	0	0.042	0.022	6.986	0.451	0.451	0.000	0.000	0.000	0.000
5	A	4	ARG	1	0.911	0.972	8.800	-0.430	-0.430	0.000	0.000	0.000	0.000
6	A	5	VAL	0	0.039	0.024	9.418	0.064	0.064	0.000	0.000	0.000	0.000
7	A	6	ARG	1	0.855	0.917	12.355	0.070	0.070	0.000	0.000	0.000	0.000
8	A	7	PRO	0	0.081	0.057	16.083	0.002	0.002	0.000	0.000	0.000	0.000
9	A	8	PHE	0	-0.027	-0.035	18.645	0.053	0.053	0.000	0.000	0.000	0.000
10	A	9	LEU	0	0.028	0.030	20.778	-0.024	-0.024	0.000	0.000	0.000	0.000
11	A	10	MET	0	-0.014	-0.010	24.364	0.032	0.032	0.000	0.000	0.000	0.000
12	A	11	PHE	0	0.046	0.033	25.983	-0.014	-0.014	0.000	0.000	0.000	0.000
13	A	12	GLN	0	0.044	0.017	29.744	0.021	0.021	0.000	0.000	0.000	0.000
14	A	13	GLY	0	-0.050	-0.020	32.090	-0.004	-0.004	0.000	0.000	0.000	0.000
15	A	14	VAL	0	0.002	-0.005	33.811	0.006	0.006	0.000	0.000	0.000	0.000
16	A	15	GLN	0	-0.063	-0.051	33.155	-0.008	-0.008	0.000	0.000	0.000	0.000
17	A	16	ALA	0	0.030	0.021	29.792	-0.004	-0.004	0.000	0.000	0.000	0.000
18	A	17	GLU	-1	-0.792	-0.879	31.601	0.031	0.031	0.000	0.000	0.000	0.000
19	A	18	ALA	0	-0.035	-0.019	33.769	-0.002	-0.002	0.000	0.000	0.000	0.000
20	A	19	ALA	0	0.015	0.011	31.507	-0.004	-0.004	0.000	0.000	0.000	0.000
21	A	20	MET	0	-0.012	0.000	29.237	-0.001	-0.001	0.000	0.000	0.000	0.000
22	A	21	ASN	0	0.014	-0.002	31.741	0.000	0.000	0.000	0.000	0.000	0.000
23	A	22	PHE	0	-0.024	-0.003	34.476	-0.001	-0.001	0.000	0.000	0.000	0.000
24	A	23	TYR	0	-0.026	-0.036	29.188	-0.004	-0.004	0.000	0.000	0.000	0.000
25	A	24	LEU	0	-0.006	-0.007	30.631	-0.004	-0.004	0.000	0.000	0.000	0.000
26	A	25	SER	0	-0.101	-0.046	33.551	0.000	0.000	0.000	0.000	0.000	0.000
27	A	26	LEU	0	-0.046	-0.018	33.361	-0.003	-0.003	0.000	0.000	0.000	0.000
28	A	27	PHE	0	-0.028	-0.030	30.887	-0.010	-0.010	0.000	0.000	0.000	0.000
29	A	28	ASP	-1	-0.909	-0.942	33.763	-0.020	-0.020	0.000	0.000	0.000	0.000
30	A	29	ASP	-1	-0.822	-0.895	29.375	-0.017	-0.017	0.000	0.000	0.000	0.000
31	A	30	ALA	0	-0.005	-0.013	29.822	-0.009	-0.009	0.000	0.000	0.000	0.000
32	A	31	GLU	-1	-0.858	-0.925	29.099	0.053	0.053	0.000	0.000	0.000	0.000
33	A	32	ILE	0	0.011	-0.008	28.930	-0.004	-0.004	0.000	0.000	0.000	0.000
34	A	33	LEU	0	-0.030	-0.008	24.189	0.011	0.011	0.000	0.000	0.000	0.000
35	A	34	GLN	0	-0.051	-0.039	22.851	0.015	0.015	0.000	0.000	0.000	0.000
36	A	35	ILE	0	0.014	0.001	27.648	-0.014	-0.014	0.000	0.000	0.000	0.000
37	A	36	GLN	0	-0.003	0.016	28.459	0.018	0.018	0.000	0.000	0.000	0.000
38	A	37	ARG	1	0.818	0.883	30.611	-0.063	-0.063	0.000	0.000	0.000	0.000
39	A	38	TYR	0	-0.036	-0.002	29.865	0.016	0.016	0.000	0.000	0.000	0.000
40	A	39	GLY	0	0.063	0.038	34.552	-0.007	-0.007	0.000	0.000	0.000	0.000
41	A	40	ALA	0	0.023	-0.007	37.631	-0.005	-0.005	0.000	0.000	0.000	0.000
42	A	41	GLU	-1	-0.932	-0.968	34.172	0.106	0.106	0.000	0.000	0.000	0.000
43	A	42	GLY	0	-0.004	0.044	35.910	0.000	0.000	0.000	0.000	0.000	0.000
44	A	43	PRO	0	-0.039	-0.052	31.344	0.011	0.011	0.000	0.000	0.000	0.000
45	A	44	GLY	0	-0.009	-0.004	33.512	-0.011	-0.011	0.000	0.000	0.000	0.000
46	A	45	PRO	0	-0.008	-0.017	34.496	0.005	0.005	0.000	0.000	0.000	0.000
47	A	46	GLU	-1	-0.864	-0.919	36.667	0.065	0.065	0.000	0.000	0.000	0.000
48	A	47	GLY	0	-0.056	-0.025	37.377	-0.007	-0.007	0.000	0.000	0.000	0.000
49	A	48	SER	0	-0.084	-0.047	34.330	-0.004	-0.004	0.000	0.000	0.000	0.000
50	A	49	VAL	0	0.000	-0.016	28.802	0.012	0.012	0.000	0.000	0.000	0.000
51	A	50	LEU	0	-0.004	0.011	27.109	-0.004	-0.004	0.000	0.000	0.000	0.000
52	A	51	LYS	1	0.793	0.873	21.450	-0.107	-0.107	0.000	0.000	0.000	0.000
53	A	52	ALA	0	0.035	0.021	25.831	0.006	0.006	0.000	0.000	0.000	0.000
54	A	53	LEU	0	-0.078	-0.031	20.915	-0.002	-0.002	0.000	0.000	0.000	0.000
55	A	54	PHE	0	0.054	0.029	24.654	0.010	0.010	0.000	0.000	0.000	0.000
56	A	55	ARG	1	0.741	0.856	24.534	-0.006	-0.006	0.000	0.000	0.000	0.000
57	A	56	LEU	0	-0.002	0.010	25.532	0.007	0.007	0.000	0.000	0.000	0.000
58	A	57	GLY	0	0.070	0.042	25.913	-0.019	-0.019	0.000	0.000	0.000	0.000
59	A	58	ASP	-1	-0.943	-0.965	22.801	-0.118	-0.118	0.000	0.000	0.000	0.000
60	A	59	GLN	0	-0.038	-0.019	18.578	-0.029	-0.029	0.000	0.000	0.000	0.000
61	A	60	SER	0	-0.011	-0.022	19.818	0.024	0.024	0.000	0.000	0.000	0.000
62	A	61	VAL	0	-0.005	-0.005	20.456	-0.032	-0.032	0.000	0.000	0.000	0.000
63	A	62	HIS	0	0.001	0.013	17.103	0.048	0.048	0.000	0.000	0.000	0.000
64	A	63	CYS	0	-0.019	-0.003	22.287	-0.026	-0.026	0.000	0.000	0.000	0.000
65	A	64	ILE	0	0.018	0.000	24.483	0.024	0.024	0.000	0.000	0.000	0.000
66	A	65	ASP	-1	-0.676	-0.823	27.183	-0.013	-0.013	0.000	0.000	0.000	0.000
67	A	66	SER	0	-0.050	-0.035	28.344	0.018	0.018	0.000	0.000	0.000	0.000
68	A	67	HIS	0	0.061	0.011	30.148	-0.016	-0.016	0.000	0.000	0.000	0.000
69	A	68	VAL	0	-0.045	-0.008	30.057	-0.003	-0.003	0.000	0.000	0.000	0.000
70	A	69	ARG	1	0.934	0.974	31.213	0.018	0.018	0.000	0.000	0.000	0.000
71	A	70	HIS	0	0.012	-0.002	28.055	-0.005	-0.005	0.000	0.000	0.000	0.000
72	A	71	ALA	0	-0.004	-0.006	31.738	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	72	PHE	0	-0.050	-0.013	26.496	-0.006	-0.006	0.000	0.000	0.000	0.000
74	A	73	ASP	-1	-0.841	-0.920	29.888	-0.102	-0.102	0.000	0.000	0.000	0.000
75	A	74	PHE	0	-0.040	-0.022	25.859	-0.021	-0.021	0.000	0.000	0.000	0.000
76	A	75	THR	0	-0.002	-0.005	26.514	-0.008	-0.008	0.000	0.000	0.000	0.000
77	A	76	PRO	0	-0.008	-0.023	27.270	-0.006	-0.006	0.000	0.000	0.000	0.000
78	A	77	ALA	0	-0.012	0.009	23.629	-0.015	-0.015	0.000	0.000	0.000	0.000
79	A	78	PHE	0	-0.028	-0.012	17.808	-0.045	-0.045	0.000	0.000	0.000	0.000
80	A	79	SER	0	-0.037	-0.008	23.073	0.031	0.031	0.000	0.000	0.000	0.000
81	A	80	PHE	0	-0.010	0.004	22.862	-0.019	-0.019	0.000	0.000	0.000	0.000
82	A	81	PHE	0	-0.017	-0.011	24.520	0.003	0.003	0.000	0.000	0.000	0.000
83	A	82	VAL	0	0.014	0.004	25.727	0.002	0.002	0.000	0.000	0.000	0.000
84	A	83	ASP	-1	-0.892	-0.945	26.161	-0.249	-0.249	0.000	0.000	0.000	0.000
85	A	84	CYS	0	-0.096	-0.051	29.342	0.017	0.017	0.000	0.000	0.000	0.000
86	A	85	GLU	-1	-0.896	-0.950	32.923	-0.095	-0.095	0.000	0.000	0.000	0.000
87	A	86	SER	0	-0.024	-0.025	35.029	0.004	0.004	0.000	0.000	0.000	0.000
88	A	87	ASN	0	-0.024	-0.043	38.276	-0.009	-0.009	0.000	0.000	0.000	0.000
89	A	88	ALA	0	0.027	0.016	40.772	0.000	0.000	0.000	0.000	0.000	0.000
90	A	89	GLN	0	0.029	0.026	33.912	-0.004	-0.004	0.000	0.000	0.000	0.000
91	A	90	ILE	0	0.022	0.000	35.203	0.001	0.001	0.000	0.000	0.000	0.000
92	A	91	GLU	-1	-0.895	-0.932	37.569	-0.092	-0.092	0.000	0.000	0.000	0.000
93	A	92	ARG	1	0.914	0.960	36.937	0.072	0.072	0.000	0.000	0.000	0.000
94	A	93	LEU	0	-0.017	-0.011	33.415	0.003	0.003	0.000	0.000	0.000	0.000
95	A	94	ALA	0	0.016	0.001	37.171	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	95	GLU	-1	-0.962	-0.958	38.254	-0.069	-0.069	0.000	0.000	0.000	0.000
97	A	96	ALA	0	0.008	-0.005	38.134	0.003	0.003	0.000	0.000	0.000	0.000
98	A	97	LEU	0	-0.050	-0.037	33.135	0.002	0.002	0.000	0.000	0.000	0.000
99	A	98	SER	0	-0.071	-0.046	36.837	-0.001	-0.001	0.000	0.000	0.000	0.000
100	A	99	ASP	-1	-0.912	-0.931	39.192	-0.060	-0.060	0.000	0.000	0.000	0.000
101	A	100	GLY	0	-0.023	-0.017	40.456	0.003	0.003	0.000	0.000	0.000	0.000
102	A	101	GLY	0	-0.017	-0.004	38.063	0.000	0.000	0.000	0.000	0.000	0.000
103	A	102	LYS	1	0.879	0.935	37.351	0.134	0.134	0.000	0.000	0.000	0.000
104	A	103	ALA	0	0.067	0.025	37.210	-0.007	-0.007	0.000	0.000	0.000	0.000
105	A	104	LEU	0	-0.096	-0.048	33.071	0.001	0.001	0.000	0.000	0.000	0.000
106	A	105	MET	0	-0.006	0.009	33.987	-0.009	-0.009	0.000	0.000	0.000	0.000
107	A	106	PRO	0	0.013	0.010	37.230	0.001	0.001	0.000	0.000	0.000	0.000
108	A	107	LEU	0	0.045	0.037	38.163	-0.007	-0.007	0.000	0.000	0.000	0.000
109	A	108	GLY	0	-0.005	0.002	39.102	0.008	0.008	0.000	0.000	0.000	0.000
110	A	109	ASP	-1	-0.896	-0.943	38.867	-0.164	-0.164	0.000	0.000	0.000	0.000
111	A	110	TYR	0	-0.073	-0.070	35.940	0.000	0.000	0.000	0.000	0.000	0.000
112	A	111	GLY	0	-0.001	0.005	36.935	-0.010	-0.010	0.000	0.000	0.000	0.000
113	A	112	PHE	0	-0.058	-0.023	32.091	-0.004	-0.004	0.000	0.000	0.000	0.000
114	A	113	SER	0	-0.065	-0.056	33.140	-0.007	-0.007	0.000	0.000	0.000	0.000
115	A	114	GLN	0	0.017	0.044	35.176	0.004	0.004	0.000	0.000	0.000	0.000
116	A	115	ARG	1	0.882	0.932	36.707	0.135	0.135	0.000	0.000	0.000	0.000
117	A	116	PHE	0	-0.003	0.006	30.227	-0.007	-0.007	0.000	0.000	0.000	0.000
118	A	117	ALA	0	0.041	0.016	34.325	0.011	0.011	0.000	0.000	0.000	0.000
119	A	118	TRP	0	-0.004	-0.006	27.367	-0.013	-0.013	0.000	0.000	0.000	0.000
120	A	119	LEU	0	-0.017	-0.010	33.196	0.008	0.008	0.000	0.000	0.000	0.000
121	A	120	ALA	0	-0.031	-0.010	32.622	-0.012	-0.012	0.000	0.000	0.000	0.000
122	A	121	ASP	-1	-0.656	-0.818	32.174	-0.095	-0.095	0.000	0.000	0.000	0.000
123	A	122	ARG	1	0.975	0.986	34.876	0.049	0.049	0.000	0.000	0.000	0.000
124	A	123	PHE	0	-0.107	-0.056	32.581	0.010	0.010	0.000	0.000	0.000	0.000
125	A	124	GLY	0	0.025	0.021	32.789	0.000	0.000	0.000	0.000	0.000	0.000
126	A	125	VAL	0	-0.046	-0.012	27.414	-0.017	-0.017	0.000	0.000	0.000	0.000
127	A	126	SER	0	-0.002	0.002	28.086	0.001	0.001	0.000	0.000	0.000	0.000
128	A	127	TRP	0	-0.016	-0.020	28.030	-0.015	-0.015	0.000	0.000	0.000	0.000
129	A	128	GLN	0	-0.022	-0.019	26.039	0.006	0.006	0.000	0.000	0.000	0.000
130	A	129	LEU	0	-0.009	0.003	29.689	0.002	0.002	0.000	0.000	0.000	0.000
131	A	130	ASN	0	0.086	0.032	30.423	0.003	0.003	0.000	0.000	0.000	0.000
132	A	131	LEU	0	-0.001	0.022	32.321	0.006	0.006	0.000	0.000	0.000	0.000
133	A	132	ALA	0	0.029	-0.010	31.707	-0.003	-0.003	0.000	0.000	0.000	0.000
134	A	133	GLY	0	-0.003	0.017	32.872	0.006	0.006	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:HIS)