FMO DATABASE

FMODB ID: N9G9Q

Calculation Name: 1QU1-A-Xray372

Preferred Name: Hemagglutinin

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 1QU1

Chain ID: A

ChEMBL ID: CHEMBL1932897

UniProt ID: P03437

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	132
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-929944.507108
FMO2-HF: Nuclear repulsion	875284.333886
FMO2-HF: Total energy	-54660.173221
FMO2-MP2: Total energy	-54820.314459

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:34:GLN)

Summations of interaction energy for fragment #1(A:34:GLN)

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.
-0.959	0.663	-0.009	-0.869	-0.745	0.004

Interaction energy analysis for fragmet #1(A:34:GLN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.026 / q_NPA : 0.004

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	36	ALA	0	0.057	0.046	3.836	-2.716	-1.094	-0.009	-0.869	-0.745	0.004
4	A	37	ASP	-1	-0.779	-0.912	6.358	-0.284	-0.284	0.000	0.000	0.000	0.000
5	A	38	LEU	0	0.056	0.043	9.602	0.228	0.228	0.000	0.000	0.000	0.000
6	A	39	LYS	1	0.971	0.981	12.462	0.557	0.557	0.000	0.000	0.000	0.000
7	A	40	SER	0	-0.011	-0.005	11.505	0.043	0.043	0.000	0.000	0.000	0.000
8	A	41	THR	0	-0.009	-0.029	10.363	0.109	0.109	0.000	0.000	0.000	0.000
9	A	42	GLN	0	-0.055	-0.025	12.618	0.149	0.149	0.000	0.000	0.000	0.000
10	A	43	ALA	0	0.017	0.018	16.096	0.022	0.022	0.000	0.000	0.000	0.000
11	A	44	ALA	0	-0.021	-0.003	14.281	0.016	0.016	0.000	0.000	0.000	0.000
12	A	45	ILE	0	0.019	0.005	15.194	0.033	0.033	0.000	0.000	0.000	0.000
13	A	46	ASP	-1	-0.845	-0.927	17.656	0.151	0.151	0.000	0.000	0.000	0.000
14	A	47	GLN	0	-0.082	-0.027	19.392	0.019	0.019	0.000	0.000	0.000	0.000
15	A	48	ILE	0	-0.016	-0.013	17.998	0.000	0.000	0.000	0.000	0.000	0.000
16	A	49	ASN	0	0.034	0.007	21.100	0.002	0.002	0.000	0.000	0.000	0.000
17	A	50	GLY	0	0.023	0.030	23.384	-0.012	-0.012	0.000	0.000	0.000	0.000
18	A	51	LYS	1	0.802	0.888	24.545	-0.128	-0.128	0.000	0.000	0.000	0.000
19	A	52	LEU	0	0.022	0.012	24.731	-0.005	-0.005	0.000	0.000	0.000	0.000
20	A	53	ASN	0	0.005	-0.017	26.793	-0.011	-0.011	0.000	0.000	0.000	0.000
21	A	54	ARG	1	0.879	0.921	29.122	-0.106	-0.106	0.000	0.000	0.000	0.000
22	A	55	VAL	0	-0.016	-0.002	29.151	-0.009	-0.009	0.000	0.000	0.000	0.000
23	A	56	ILE	0	0.008	0.018	29.045	-0.004	-0.004	0.000	0.000	0.000	0.000
24	A	57	GLU	-1	-0.951	-0.962	32.713	0.097	0.097	0.000	0.000	0.000	0.000
25	A	58	LYS	1	0.840	0.903	33.930	-0.107	-0.107	0.000	0.000	0.000	0.000
26	A	59	THR	0	-0.049	-0.035	34.412	-0.003	-0.003	0.000	0.000	0.000	0.000
27	A	60	ASN	0	-0.060	-0.031	35.771	-0.006	-0.006	0.000	0.000	0.000	0.000
28	A	61	GLU	-1	-0.965	-0.982	38.545	0.081	0.081	0.000	0.000	0.000	0.000
29	A	62	LYS	1	0.896	0.939	39.831	-0.088	-0.088	0.000	0.000	0.000	0.000
30	A	63	PHE	0	-0.009	-0.020	37.463	-0.003	-0.003	0.000	0.000	0.000	0.000
31	A	64	HIS	1	0.836	0.900	41.808	-0.111	-0.111	0.000	0.000	0.000	0.000
32	A	65	GLN	0	-0.001	0.008	44.666	-0.006	-0.006	0.000	0.000	0.000	0.000
33	A	66	ILE	0	-0.016	-0.012	42.894	-0.003	-0.003	0.000	0.000	0.000	0.000
34	A	67	GLU	-1	-0.820	-0.887	45.047	0.101	0.101	0.000	0.000	0.000	0.000
35	A	68	LYS	1	0.826	0.917	48.597	-0.069	-0.069	0.000	0.000	0.000	0.000
36	A	69	GLU	-1	-0.839	-0.916	49.307	0.067	0.067	0.000	0.000	0.000	0.000
37	A	70	PHE	0	-0.015	-0.009	47.955	-0.002	-0.002	0.000	0.000	0.000	0.000
38	A	71	SER	0	0.012	0.012	52.458	-0.002	-0.002	0.000	0.000	0.000	0.000
39	A	72	GLH	0	-0.094	-0.078	54.702	-0.003	-0.003	0.000	0.000	0.000	0.000
40	A	73	VAL	0	-0.001	-0.003	54.435	-0.003	-0.003	0.000	0.000	0.000	0.000
41	A	74	GLU	-1	-0.907	-0.964	54.351	0.074	0.074	0.000	0.000	0.000	0.000
42	A	75	GLY	0	-0.012	-0.005	58.360	-0.002	-0.002	0.000	0.000	0.000	0.000
43	A	76	ARG	1	0.833	0.923	59.464	-0.051	-0.051	0.000	0.000	0.000	0.000
44	A	77	ILE	0	0.012	0.009	58.880	-0.002	-0.002	0.000	0.000	0.000	0.000
45	A	78	GLN	0	-0.036	-0.021	62.047	0.000	0.000	0.000	0.000	0.000	0.000
46	A	79	ASP	-1	-0.844	-0.927	64.543	0.046	0.046	0.000	0.000	0.000	0.000
47	A	80	LEU	0	-0.011	-0.010	65.281	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	81	GLU	-1	-0.893	-0.944	65.406	0.052	0.052	0.000	0.000	0.000	0.000
49	A	82	LYS	1	0.835	0.914	66.836	-0.049	-0.049	0.000	0.000	0.000	0.000
50	A	83	TYR	0	0.050	0.018	70.275	-0.002	-0.002	0.000	0.000	0.000	0.000
51	A	84	VAL	0	-0.024	0.001	70.157	-0.002	-0.002	0.000	0.000	0.000	0.000
52	A	85	GLU	-1	-0.795	-0.895	72.770	0.039	0.039	0.000	0.000	0.000	0.000
53	A	86	ASP	-1	-0.758	-0.875	74.754	0.037	0.037	0.000	0.000	0.000	0.000
54	A	87	THR	0	-0.054	-0.026	75.144	-0.002	-0.002	0.000	0.000	0.000	0.000
55	A	88	LYS	1	0.826	0.906	76.361	-0.041	-0.041	0.000	0.000	0.000	0.000
56	A	89	ILE	0	-0.012	-0.014	78.656	-0.001	-0.001	0.000	0.000	0.000	0.000
57	A	90	ASP	-1	-0.811	-0.873	80.517	0.031	0.031	0.000	0.000	0.000	0.000
58	A	91	LEU	0	-0.035	-0.007	80.196	-0.001	-0.001	0.000	0.000	0.000	0.000
59	A	92	TRP	0	-0.025	-0.024	81.160	-0.001	-0.001	0.000	0.000	0.000	0.000
60	A	93	SER	0	-0.026	-0.033	84.187	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	94	TYR	0	0.015	0.015	86.338	-0.001	-0.001	0.000	0.000	0.000	0.000
62	A	95	ASN	0	-0.031	-0.021	86.083	-0.001	-0.001	0.000	0.000	0.000	0.000
63	A	96	ALA	0	-0.010	-0.014	88.996	-0.001	-0.001	0.000	0.000	0.000	0.000
64	A	97	GLU	-1	-0.927	-0.957	90.675	0.025	0.025	0.000	0.000	0.000	0.000
65	A	98	LEU	0	-0.013	0.000	92.293	-0.001	-0.001	0.000	0.000	0.000	0.000
66	A	99	LEU	0	-0.027	-0.016	92.317	-0.001	-0.001	0.000	0.000	0.000	0.000
67	A	100	VAL	0	0.056	0.019	94.908	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	101	ALA	0	-0.013	0.009	96.661	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	102	LEU	0	0.004	-0.011	97.133	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	103	GLU	-1	-0.840	-0.923	99.668	0.023	0.023	0.000	0.000	0.000	0.000
71	A	104	ASN	0	-0.055	-0.028	100.081	-0.001	-0.001	0.000	0.000	0.000	0.000
72	A	105	GLN	0	-0.138	-0.056	102.634	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	106	HIS	0	-0.043	-0.033	104.843	0.000	0.000	0.000	0.000	0.000	0.000
74	A	107	THR	0	-0.065	-0.020	102.724	0.000	0.000	0.000	0.000	0.000	0.000
75	A	108	ILE	0	-0.050	-0.033	98.158	0.000	0.000	0.000	0.000	0.000	0.000
76	A	109	ASP	-1	-0.728	-0.824	102.510	0.023	0.023	0.000	0.000	0.000	0.000
77	A	110	LEU	0	-0.046	-0.034	96.122	0.000	0.000	0.000	0.000	0.000	0.000
78	A	111	THR	0	-0.098	-0.072	98.244	0.001	0.001	0.000	0.000	0.000	0.000
79	A	112	ASP	-1	-0.858	-0.915	100.621	0.023	0.023	0.000	0.000	0.000	0.000
80	A	113	SER	0	-0.048	-0.043	98.958	0.001	0.001	0.000	0.000	0.000	0.000
81	A	114	GLU	-1	-0.868	-0.925	96.259	0.026	0.026	0.000	0.000	0.000	0.000
82	A	115	MET	0	0.061	0.030	95.837	0.001	0.001	0.000	0.000	0.000	0.000
83	A	116	ASN	0	-0.031	-0.010	95.542	0.001	0.001	0.000	0.000	0.000	0.000
84	A	117	LYS	1	0.817	0.896	92.336	-0.026	-0.026	0.000	0.000	0.000	0.000
85	A	118	LEU	0	-0.041	-0.018	91.189	0.001	0.001	0.000	0.000	0.000	0.000
86	A	119	PHE	0	0.083	0.035	90.734	0.001	0.001	0.000	0.000	0.000	0.000
87	A	120	GLU	-1	-0.742	-0.850	90.155	0.032	0.032	0.000	0.000	0.000	0.000
88	A	121	LYS	1	0.887	0.944	86.606	-0.030	-0.030	0.000	0.000	0.000	0.000
89	A	122	THR	0	-0.034	-0.022	86.088	0.001	0.001	0.000	0.000	0.000	0.000
90	A	123	ARG	1	0.897	0.942	86.431	-0.030	-0.030	0.000	0.000	0.000	0.000
91	A	124	ARG	1	0.800	0.881	84.276	-0.032	-0.032	0.000	0.000	0.000	0.000
92	A	125	GLN	0	-0.058	-0.013	80.435	0.002	0.002	0.000	0.000	0.000	0.000
93	A	126	LEU	0	-0.070	-0.013	81.689	0.001	0.001	0.000	0.000	0.000	0.000
94	A	136	GLY	0	0.000	-0.020	87.620	0.000	0.000	0.000	0.000	0.000	0.000
95	A	137	SER	0	-0.041	-0.005	89.321	0.000	0.000	0.000	0.000	0.000	0.000
96	A	138	PHE	0	0.022	-0.006	88.927	0.000	0.000	0.000	0.000	0.000	0.000
97	A	139	LYS	1	0.984	1.003	84.237	-0.028	-0.028	0.000	0.000	0.000	0.000
98	A	140	ILE	0	0.027	0.016	80.667	0.000	0.000	0.000	0.000	0.000	0.000
99	A	141	TYR	0	-0.060	-0.035	80.224	0.000	0.000	0.000	0.000	0.000	0.000
100	A	142	HIS	0	-0.059	-0.048	76.447	0.001	0.001	0.000	0.000	0.000	0.000
101	A	143	LYS	1	0.869	0.922	73.008	-0.038	-0.038	0.000	0.000	0.000	0.000
102	A	144	CYS	0	-0.085	-0.004	67.698	0.002	0.002	0.000	0.000	0.000	0.000
103	A	145	ASP	-1	-0.817	-0.903	70.877	0.038	0.038	0.000	0.000	0.000	0.000
104	A	146	ASN	0	0.016	-0.013	72.214	0.001	0.001	0.000	0.000	0.000	0.000
105	A	147	ALA	0	0.014	0.018	67.980	0.000	0.000	0.000	0.000	0.000	0.000
106	A	149	ILE	0	0.004	-0.024	68.144	0.000	0.000	0.000	0.000	0.000	0.000
107	A	150	GLU	-1	-0.900	-0.931	67.254	0.034	0.034	0.000	0.000	0.000	0.000
108	A	151	SER	0	-0.016	-0.011	63.907	0.000	0.000	0.000	0.000	0.000	0.000
109	A	152	ILE	0	-0.025	-0.027	64.419	0.001	0.001	0.000	0.000	0.000	0.000
110	A	153	ARG	1	0.850	0.945	66.004	-0.033	-0.033	0.000	0.000	0.000	0.000
111	A	154	ASN	0	-0.054	-0.051	65.270	0.000	0.000	0.000	0.000	0.000	0.000
112	A	155	GLY	0	0.010	0.020	62.700	0.000	0.000	0.000	0.000	0.000	0.000
113	A	156	THR	0	-0.012	0.005	58.062	0.000	0.000	0.000	0.000	0.000	0.000
114	A	157	TYR	0	0.007	-0.013	54.445	0.001	0.001	0.000	0.000	0.000	0.000
115	A	158	ASP	-1	-0.843	-0.865	51.510	0.055	0.055	0.000	0.000	0.000	0.000
116	A	159	HIS	0	-0.089	-0.062	49.249	0.002	0.002	0.000	0.000	0.000	0.000
117	A	160	ASP	-1	-0.813	-0.881	44.006	0.075	0.075	0.000	0.000	0.000	0.000
118	A	161	VAL	0	-0.002	-0.001	43.819	0.003	0.003	0.000	0.000	0.000	0.000
119	A	162	TYR	0	0.009	-0.002	34.677	0.000	0.000	0.000	0.000	0.000	0.000
120	A	163	ARG	1	0.983	0.994	38.408	-0.057	-0.057	0.000	0.000	0.000	0.000
121	A	164	ASP	-1	-0.837	-0.928	35.344	0.093	0.093	0.000	0.000	0.000	0.000
122	A	165	GLU	-1	-0.826	-0.875	30.224	0.094	0.094	0.000	0.000	0.000	0.000
123	A	166	ALA	0	0.008	0.010	29.730	0.003	0.003	0.000	0.000	0.000	0.000
124	A	167	LEU	0	0.069	0.022	26.157	0.012	0.012	0.000	0.000	0.000	0.000
125	A	168	ASN	0	-0.019	-0.019	20.796	-0.035	-0.035	0.000	0.000	0.000	0.000
126	A	169	ASN	0	-0.002	-0.001	21.857	0.020	0.020	0.000	0.000	0.000	0.000
127	A	170	ARG	1	0.935	0.963	12.264	-0.161	-0.161	0.000	0.000	0.000	0.000
128	A	171	PHE	0	0.042	0.023	14.050	-0.046	-0.046	0.000	0.000	0.000	0.000
129	A	172	GLN	0	0.025	0.022	12.064	0.155	0.155	0.000	0.000	0.000	0.000
130	A	173	ILE	0	-0.013	-0.012	8.836	-0.089	-0.089	0.000	0.000	0.000	0.000
131	A	174	LYS	1	0.923	0.960	9.328	0.451	0.451	0.000	0.000	0.000	0.000
132	A	175	GLY	0	-0.049	-0.011	5.627	0.337	0.337	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

Interactive mode: IFIE and PIEDA for fragment #1(A:34:GLN)