FMO DATABASE

FMODB ID: 85V5Y

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:

Apendix: None

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	132
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-929094.402746
FMO2-HF: Nuclear repulsion	874435.170652
FMO2-HF: Total energy	-54659.232095
FMO2-MP2: Total energy	-54819.377802

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.
-0.479	0.802	-0.005	-0.666	-0.611	0.002

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 : 0.016 / q_NPA : -0.011

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	0.051	0.015	3.836	-2.086	-0.805	-0.005	-0.666	-0.611	0.002
4	A	37	ASP	-1	-0.828	-0.940	6.358	-0.467	-0.467	0.000	0.000	0.000	0.000
5	A	38	LEU	0	0.056	0.033	9.602	0.250	0.250	0.000	0.000	0.000	0.000
6	A	39	LYS	1	0.970	0.978	12.462	0.673	0.673	0.000	0.000	0.000	0.000
7	A	40	SER	0	-0.007	0.002	11.568	0.040	0.040	0.000	0.000	0.000	0.000
8	A	41	THR	0	0.026	0.004	10.061	0.134	0.134	0.000	0.000	0.000	0.000
9	A	42	GLN	0	-0.049	-0.020	12.615	0.171	0.171	0.000	0.000	0.000	0.000
10	A	43	ALA	0	0.008	0.015	16.102	0.033	0.033	0.000	0.000	0.000	0.000
11	A	44	ALA	0	-0.012	-0.001	14.217	0.023	0.023	0.000	0.000	0.000	0.000
12	A	45	ILE	0	0.024	0.016	15.312	0.047	0.047	0.000	0.000	0.000	0.000
13	A	46	ASP	-1	-0.855	-0.939	17.645	0.097	0.097	0.000	0.000	0.000	0.000
14	A	47	GLN	0	-0.078	-0.022	18.952	0.023	0.023	0.000	0.000	0.000	0.000
15	A	48	ILE	0	-0.044	-0.025	18.094	0.007	0.007	0.000	0.000	0.000	0.000
16	A	49	ASN	0	0.017	0.000	21.092	0.020	0.020	0.000	0.000	0.000	0.000
17	A	50	GLY	0	0.013	0.017	23.371	-0.009	-0.009	0.000	0.000	0.000	0.000
18	A	51	LYS	1	0.864	0.936	24.651	-0.092	-0.092	0.000	0.000	0.000	0.000
19	A	52	LEU	0	0.024	0.016	24.630	-0.002	-0.002	0.000	0.000	0.000	0.000
20	A	53	ASN	0	0.056	0.012	26.781	0.005	0.005	0.000	0.000	0.000	0.000
21	A	54	ARG	1	0.817	0.876	29.111	-0.081	-0.081	0.000	0.000	0.000	0.000
22	A	55	VAL	0	-0.010	0.003	29.166	-0.008	-0.008	0.000	0.000	0.000	0.000
23	A	56	ILE	0	0.011	0.031	29.584	-0.002	-0.002	0.000	0.000	0.000	0.000
24	A	57	GLU	-1	-0.973	-0.981	32.697	0.080	0.080	0.000	0.000	0.000	0.000
25	A	58	LYS	1	0.844	0.916	34.182	-0.087	-0.087	0.000	0.000	0.000	0.000
26	A	59	THR	0	-0.046	-0.047	34.360	-0.002	-0.002	0.000	0.000	0.000	0.000
27	A	60	ASN	0	-0.002	0.007	36.223	0.001	0.001	0.000	0.000	0.000	0.000
28	A	61	GLU	-1	-0.986	-0.991	38.528	0.068	0.068	0.000	0.000	0.000	0.000
29	A	62	LYS	1	0.925	0.964	39.885	-0.082	-0.082	0.000	0.000	0.000	0.000
30	A	63	PHE	0	0.001	-0.013	37.408	-0.002	-0.002	0.000	0.000	0.000	0.000
31	A	64	HIS	1	0.840	0.918	42.207	-0.104	-0.104	0.000	0.000	0.000	0.000
32	A	65	GLN	0	0.003	0.016	44.554	-0.005	-0.005	0.000	0.000	0.000	0.000
33	A	66	ILE	0	-0.008	-0.007	42.924	-0.003	-0.003	0.000	0.000	0.000	0.000
34	A	67	GLU	-1	-0.826	-0.908	44.965	0.100	0.100	0.000	0.000	0.000	0.000
35	A	68	LYS	1	0.903	0.967	48.580	-0.063	-0.063	0.000	0.000	0.000	0.000
36	A	69	GLU	-1	-0.823	-0.903	49.755	0.061	0.061	0.000	0.000	0.000	0.000
37	A	70	PHE	0	-0.002	-0.012	47.715	-0.001	-0.001	0.000	0.000	0.000	0.000
38	A	71	SER	0	0.026	0.020	52.442	-0.002	-0.002	0.000	0.000	0.000	0.000
39	A	72	GLH	0	-0.113	-0.087	54.686	-0.003	-0.003	0.000	0.000	0.000	0.000
40	A	73	VAL	0	0.007	0.003	54.431	-0.003	-0.003	0.000	0.000	0.000	0.000
41	A	74	GLU	-1	-0.926	-0.974	54.380	0.074	0.074	0.000	0.000	0.000	0.000
42	A	75	GLY	0	-0.014	-0.005	58.343	-0.002	-0.002	0.000	0.000	0.000	0.000
43	A	76	ARG	1	0.854	0.939	59.731	-0.048	-0.048	0.000	0.000	0.000	0.000
44	A	77	ILE	0	0.013	0.012	59.007	-0.002	-0.002	0.000	0.000	0.000	0.000
45	A	78	GLN	0	-0.026	-0.007	61.973	0.000	0.000	0.000	0.000	0.000	0.000
46	A	79	ASP	-1	-0.901	-0.964	64.531	0.043	0.043	0.000	0.000	0.000	0.000
47	A	80	LEU	0	-0.037	-0.022	65.083	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	81	GLU	-1	-0.905	-0.964	65.108	0.053	0.053	0.000	0.000	0.000	0.000
49	A	82	LYS	1	0.916	0.958	67.781	-0.047	-0.047	0.000	0.000	0.000	0.000
50	A	83	TYR	0	0.035	0.016	70.262	-0.002	-0.002	0.000	0.000	0.000	0.000
51	A	84	VAL	0	-0.029	-0.002	70.046	-0.002	-0.002	0.000	0.000	0.000	0.000
52	A	85	GLU	-1	-0.924	-0.967	72.751	0.040	0.040	0.000	0.000	0.000	0.000
53	A	86	ASP	-1	-0.738	-0.873	74.746	0.036	0.036	0.000	0.000	0.000	0.000
54	A	87	THR	0	-0.043	-0.022	75.187	-0.002	-0.002	0.000	0.000	0.000	0.000
55	A	88	LYS	1	0.900	0.955	76.829	-0.041	-0.041	0.000	0.000	0.000	0.000
56	A	89	ILE	0	-0.011	-0.018	78.494	-0.001	-0.001	0.000	0.000	0.000	0.000
57	A	90	ASP	-1	-0.807	-0.879	80.504	0.030	0.030	0.000	0.000	0.000	0.000
58	A	91	LEU	0	-0.026	-0.009	80.175	-0.001	-0.001	0.000	0.000	0.000	0.000
59	A	92	TRP	0	-0.032	-0.026	81.183	-0.001	-0.001	0.000	0.000	0.000	0.000
60	A	93	SER	0	-0.025	-0.022	84.250	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	94	TYR	0	0.013	0.015	86.323	-0.001	-0.001	0.000	0.000	0.000	0.000
62	A	95	ASN	0	-0.036	-0.021	86.168	-0.001	-0.001	0.000	0.000	0.000	0.000
63	A	96	ALA	0	-0.014	-0.015	88.981	-0.001	-0.001	0.000	0.000	0.000	0.000
64	A	97	GLU	-1	-0.935	-0.959	90.656	0.024	0.024	0.000	0.000	0.000	0.000
65	A	98	LEU	0	-0.009	0.001	92.276	-0.001	-0.001	0.000	0.000	0.000	0.000
66	A	99	LEU	0	-0.030	-0.015	92.473	-0.001	-0.001	0.000	0.000	0.000	0.000
67	A	100	VAL	0	0.058	0.021	94.871	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	101	ALA	0	-0.018	0.001	96.644	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	102	LEU	0	-0.005	-0.017	97.107	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	103	GLU	-1	-0.859	-0.933	99.653	0.024	0.024	0.000	0.000	0.000	0.000
71	A	104	ASN	0	-0.045	-0.021	100.046	-0.001	-0.001	0.000	0.000	0.000	0.000
72	A	105	GLN	0	-0.140	-0.056	102.636	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	106	HIS	0	-0.043	-0.032	104.831	0.000	0.000	0.000	0.000	0.000	0.000
74	A	107	THR	0	-0.068	-0.018	102.617	0.000	0.000	0.000	0.000	0.000	0.000
75	A	108	ILE	0	-0.047	-0.031	98.160	0.000	0.000	0.000	0.000	0.000	0.000
76	A	109	ASP	-1	-0.716	-0.818	102.524	0.023	0.023	0.000	0.000	0.000	0.000
77	A	110	LEU	0	-0.058	-0.035	96.280	0.001	0.001	0.000	0.000	0.000	0.000
78	A	111	THR	0	-0.109	-0.088	98.224	0.001	0.001	0.000	0.000	0.000	0.000
79	A	112	ASP	-1	-0.849	-0.908	100.600	0.023	0.023	0.000	0.000	0.000	0.000
80	A	113	SER	0	-0.049	-0.047	98.947	0.001	0.001	0.000	0.000	0.000	0.000
81	A	114	GLU	-1	-0.987	-0.995	96.482	0.026	0.026	0.000	0.000	0.000	0.000
82	A	115	MET	0	0.076	0.031	95.818	0.001	0.001	0.000	0.000	0.000	0.000
83	A	116	ASN	0	-0.014	0.008	95.523	0.001	0.001	0.000	0.000	0.000	0.000
84	A	117	LYS	1	0.929	0.962	92.399	-0.028	-0.028	0.000	0.000	0.000	0.000
85	A	118	LEU	0	-0.025	-0.008	91.177	0.001	0.001	0.000	0.000	0.000	0.000
86	A	119	PHE	0	0.084	0.033	90.715	0.001	0.001	0.000	0.000	0.000	0.000
87	A	120	GLU	-1	-0.811	-0.891	90.250	0.032	0.032	0.000	0.000	0.000	0.000
88	A	121	LYS	1	0.873	0.939	85.876	-0.032	-0.032	0.000	0.000	0.000	0.000
89	A	122	THR	0	-0.032	-0.023	86.068	0.001	0.001	0.000	0.000	0.000	0.000
90	A	123	ARG	1	0.855	0.910	86.411	-0.031	-0.031	0.000	0.000	0.000	0.000
91	A	124	ARG	1	0.867	0.931	84.230	-0.034	-0.034	0.000	0.000	0.000	0.000
92	A	125	GLN	0	-0.023	0.000	80.347	0.002	0.002	0.000	0.000	0.000	0.000
93	A	126	LEU	0	-0.037	0.006	81.669	0.001	0.001	0.000	0.000	0.000	0.000
94	A	136	GLY	0	0.008	-0.022	87.564	0.000	0.000	0.000	0.000	0.000	0.000
95	A	137	SER	0	-0.049	-0.005	89.304	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	138	PHE	0	0.033	-0.007	88.906	0.000	0.000	0.000	0.000	0.000	0.000
97	A	139	LYS	1	0.987	1.015	84.553	-0.027	-0.027	0.000	0.000	0.000	0.000
98	A	140	ILE	0	0.027	0.015	80.523	0.000	0.000	0.000	0.000	0.000	0.000
99	A	141	TYR	0	-0.081	-0.048	80.157	-0.001	-0.001	0.000	0.000	0.000	0.000
100	A	142	HIS	0	-0.056	-0.040	76.310	0.001	0.001	0.000	0.000	0.000	0.000
101	A	143	LYS	1	0.892	0.941	72.913	-0.039	-0.039	0.000	0.000	0.000	0.000
102	A	144	CYS	0	-0.066	0.006	67.689	0.002	0.002	0.000	0.000	0.000	0.000
103	A	145	ASP	-1	-0.839	-0.912	70.831	0.036	0.036	0.000	0.000	0.000	0.000
104	A	146	ASN	0	0.011	-0.014	72.201	0.001	0.001	0.000	0.000	0.000	0.000
105	A	147	ALA	0	0.021	0.017	67.936	0.000	0.000	0.000	0.000	0.000	0.000
106	A	149	ILE	0	-0.001	-0.026	68.133	0.000	0.000	0.000	0.000	0.000	0.000
107	A	150	GLU	-1	-0.910	-0.943	66.996	0.030	0.030	0.000	0.000	0.000	0.000
108	A	151	SER	0	-0.017	-0.014	63.630	0.000	0.000	0.000	0.000	0.000	0.000
109	A	152	ILE	0	-0.020	-0.023	64.410	0.001	0.001	0.000	0.000	0.000	0.000
110	A	153	ARG	1	0.856	0.945	65.995	-0.030	-0.030	0.000	0.000	0.000	0.000
111	A	154	ASN	0	-0.059	-0.049	65.248	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	155	GLY	0	0.006	0.025	62.687	0.000	0.000	0.000	0.000	0.000	0.000
113	A	156	THR	0	-0.042	-0.013	58.058	0.001	0.001	0.000	0.000	0.000	0.000
114	A	157	TYR	0	0.034	-0.004	54.408	0.001	0.001	0.000	0.000	0.000	0.000
115	A	158	ASP	-1	-0.877	-0.894	51.697	0.047	0.047	0.000	0.000	0.000	0.000
116	A	159	HIS	0	-0.098	-0.065	49.751	0.003	0.003	0.000	0.000	0.000	0.000
117	A	160	ASP	-1	-0.872	-0.939	43.795	0.065	0.065	0.000	0.000	0.000	0.000
118	A	161	VAL	0	-0.021	-0.006	43.732	0.004	0.004	0.000	0.000	0.000	0.000
119	A	162	TYR	0	-0.003	-0.010	34.694	0.000	0.000	0.000	0.000	0.000	0.000
120	A	163	ARG	1	0.989	0.995	38.201	-0.041	-0.041	0.000	0.000	0.000	0.000
121	A	164	ASP	-1	-0.846	-0.930	35.291	0.080	0.080	0.000	0.000	0.000	0.000
122	A	165	GLU	-1	-0.829	-0.878	30.178	0.073	0.073	0.000	0.000	0.000	0.000
123	A	166	ALA	0	-0.009	-0.003	29.708	0.004	0.004	0.000	0.000	0.000	0.000
124	A	167	LEU	0	0.060	0.008	26.224	0.011	0.011	0.000	0.000	0.000	0.000
125	A	168	ASN	0	-0.017	-0.012	20.814	-0.043	-0.043	0.000	0.000	0.000	0.000
126	A	169	ASN	0	0.003	0.007	21.810	0.026	0.026	0.000	0.000	0.000	0.000
127	A	170	ARG	1	0.940	0.959	12.249	-0.062	-0.062	0.000	0.000	0.000	0.000
128	A	171	PHE	0	0.023	0.017	13.728	-0.056	-0.056	0.000	0.000	0.000	0.000
129	A	172	GLN	0	0.005	0.006	12.093	0.121	0.121	0.000	0.000	0.000	0.000
130	A	173	ILE	0	0.008	-0.008	9.293	-0.089	-0.089	0.000	0.000	0.000	0.000
131	A	174	LYS	1	0.925	0.962	9.351	0.613	0.613	0.000	0.000	0.000	0.000
132	A	175	GLY	0	0.006	0.046	6.136	-0.090	-0.090	0.000	0.000	0.000	0.000

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