FMO DATABASE

FMODB ID: JL9L9

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

Total energy (hartree)

FMO2-HF: Electronic energy	-930324.884923
FMO2-HF: Nuclear repulsion	875664.305278
FMO2-HF: Total energy	-54660.579646
FMO2-MP2: Total energy	-54820.642721

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.
-0.243	1.109	-0.004	-0.669	-0.68	0.003

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 : 0.039 / q_NPA : 0.012

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	0.058	0.047	3.917	-2.068	-0.716	-0.004	-0.669	-0.680	0.003
4	A	37	ASP	-1	-0.771	-0.876	6.276	-0.134	-0.134	0.000	0.000	0.000	0.000
5	A	38	LEU	0	0.063	0.041	9.527	0.162	0.162	0.000	0.000	0.000	0.000
6	A	39	LYS	1	0.894	0.939	12.229	0.470	0.470	0.000	0.000	0.000	0.000
7	A	40	SER	0	-0.008	-0.014	11.381	0.012	0.012	0.000	0.000	0.000	0.000
8	A	41	THR	0	-0.026	-0.029	10.374	0.065	0.065	0.000	0.000	0.000	0.000
9	A	42	GLN	0	-0.026	-0.024	12.528	0.121	0.121	0.000	0.000	0.000	0.000
10	A	43	ALA	0	0.003	0.010	16.079	0.011	0.011	0.000	0.000	0.000	0.000
11	A	44	ALA	0	-0.014	0.000	14.078	0.001	0.001	0.000	0.000	0.000	0.000
12	A	45	ILE	0	0.009	0.000	14.753	0.027	0.027	0.000	0.000	0.000	0.000
13	A	46	ASP	-1	-0.823	-0.917	17.463	0.169	0.169	0.000	0.000	0.000	0.000
14	A	47	GLN	0	-0.046	-0.006	19.329	0.011	0.011	0.000	0.000	0.000	0.000
15	A	48	ILE	0	-0.007	-0.003	17.805	-0.003	-0.003	0.000	0.000	0.000	0.000
16	A	49	ASN	0	0.029	0.012	20.914	0.001	0.001	0.000	0.000	0.000	0.000
17	A	50	GLY	0	0.027	0.025	23.087	-0.008	-0.008	0.000	0.000	0.000	0.000
18	A	51	LYS	1	0.771	0.869	24.006	-0.087	-0.087	0.000	0.000	0.000	0.000
19	A	52	LEU	0	0.015	0.001	24.266	-0.006	-0.006	0.000	0.000	0.000	0.000
20	A	53	ASN	0	-0.018	-0.026	26.418	-0.011	-0.011	0.000	0.000	0.000	0.000
21	A	54	ARG	1	0.820	0.879	28.828	-0.081	-0.081	0.000	0.000	0.000	0.000
22	A	55	VAL	0	-0.019	0.002	28.816	-0.009	-0.009	0.000	0.000	0.000	0.000
23	A	56	ILE	0	0.016	0.024	28.956	-0.005	-0.005	0.000	0.000	0.000	0.000
24	A	57	GLU	-1	-0.888	-0.926	32.547	0.077	0.077	0.000	0.000	0.000	0.000
25	A	58	LYS	1	0.853	0.919	33.847	-0.074	-0.074	0.000	0.000	0.000	0.000
26	A	59	THR	0	-0.040	-0.031	34.186	-0.002	-0.002	0.000	0.000	0.000	0.000
27	A	60	ASN	0	-0.063	-0.035	35.666	-0.005	-0.005	0.000	0.000	0.000	0.000
28	A	61	GLU	-1	-0.959	-0.975	38.575	0.063	0.063	0.000	0.000	0.000	0.000
29	A	62	LYS	1	0.893	0.933	39.632	-0.064	-0.064	0.000	0.000	0.000	0.000
30	A	63	PHE	0	-0.032	-0.022	37.258	-0.002	-0.002	0.000	0.000	0.000	0.000
31	A	64	HIS	1	0.862	0.905	41.726	-0.095	-0.095	0.000	0.000	0.000	0.000
32	A	65	GLN	0	-0.005	0.004	44.425	-0.004	-0.004	0.000	0.000	0.000	0.000
33	A	66	ILE	0	0.002	0.001	42.744	-0.003	-0.003	0.000	0.000	0.000	0.000
34	A	67	GLU	-1	-0.821	-0.894	44.697	0.084	0.084	0.000	0.000	0.000	0.000
35	A	68	LYS	1	0.810	0.913	48.448	-0.055	-0.055	0.000	0.000	0.000	0.000
36	A	69	GLU	-1	-0.861	-0.927	48.506	0.049	0.049	0.000	0.000	0.000	0.000
37	A	70	PHE	0	-0.026	-0.018	47.929	-0.002	-0.002	0.000	0.000	0.000	0.000
38	A	71	SER	0	0.003	-0.006	52.160	-0.002	-0.002	0.000	0.000	0.000	0.000
39	A	72	GLH	0	-0.086	-0.070	54.375	-0.003	-0.003	0.000	0.000	0.000	0.000
40	A	73	VAL	0	-0.012	0.000	54.202	-0.003	-0.003	0.000	0.000	0.000	0.000
41	A	74	GLU	-1	-0.910	-0.969	53.839	0.058	0.058	0.000	0.000	0.000	0.000
42	A	75	GLY	0	0.000	-0.003	57.945	-0.001	-0.001	0.000	0.000	0.000	0.000
43	A	76	ARG	1	0.814	0.896	59.265	-0.038	-0.038	0.000	0.000	0.000	0.000
44	A	77	ILE	0	0.008	0.012	58.588	-0.002	-0.002	0.000	0.000	0.000	0.000
45	A	78	GLN	0	-0.022	-0.025	61.788	-0.001	-0.001	0.000	0.000	0.000	0.000
46	A	79	ASP	-1	-0.828	-0.905	64.164	0.036	0.036	0.000	0.000	0.000	0.000
47	A	80	LEU	0	-0.007	-0.011	65.252	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	81	GLU	-1	-0.888	-0.943	65.591	0.040	0.040	0.000	0.000	0.000	0.000
49	A	82	LYS	1	0.822	0.910	66.557	-0.038	-0.038	0.000	0.000	0.000	0.000
50	A	83	TYR	0	0.073	0.031	70.279	-0.002	-0.002	0.000	0.000	0.000	0.000
51	A	84	VAL	0	-0.017	0.006	69.897	-0.001	-0.001	0.000	0.000	0.000	0.000
52	A	85	GLU	-1	-0.784	-0.885	72.609	0.030	0.030	0.000	0.000	0.000	0.000
53	A	86	ASP	-1	-0.773	-0.886	74.577	0.028	0.028	0.000	0.000	0.000	0.000
54	A	87	THR	0	-0.054	-0.030	74.967	-0.001	-0.001	0.000	0.000	0.000	0.000
55	A	88	LYS	1	0.820	0.900	76.235	-0.031	-0.031	0.000	0.000	0.000	0.000
56	A	89	ILE	0	-0.013	-0.003	78.466	-0.001	-0.001	0.000	0.000	0.000	0.000
57	A	90	ASP	-1	-0.807	-0.877	80.488	0.023	0.023	0.000	0.000	0.000	0.000
58	A	91	LEU	0	-0.035	-0.009	80.059	-0.001	-0.001	0.000	0.000	0.000	0.000
59	A	92	TRP	0	-0.009	-0.014	81.119	-0.001	-0.001	0.000	0.000	0.000	0.000
60	A	93	SER	0	-0.022	-0.023	84.073	0.000	0.000	0.000	0.000	0.000	0.000
61	A	94	TYR	0	0.034	0.020	86.339	-0.001	-0.001	0.000	0.000	0.000	0.000
62	A	95	ASN	0	-0.030	-0.024	85.893	-0.001	-0.001	0.000	0.000	0.000	0.000
63	A	96	ALA	0	-0.007	-0.009	88.900	0.000	0.000	0.000	0.000	0.000	0.000
64	A	97	GLU	-1	-0.924	-0.959	90.582	0.019	0.019	0.000	0.000	0.000	0.000
65	A	98	LEU	0	-0.016	-0.006	92.127	-0.001	-0.001	0.000	0.000	0.000	0.000
66	A	99	LEU	0	-0.022	-0.009	92.066	0.000	0.000	0.000	0.000	0.000	0.000
67	A	100	VAL	0	0.069	0.024	94.715	0.000	0.000	0.000	0.000	0.000	0.000
68	A	101	ALA	0	-0.018	0.006	96.433	0.000	0.000	0.000	0.000	0.000	0.000
69	A	102	LEU	0	-0.009	-0.019	96.868	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	103	GLU	-1	-0.849	-0.924	99.364	0.018	0.018	0.000	0.000	0.000	0.000
71	A	104	ASN	0	-0.066	-0.041	99.994	0.000	0.000	0.000	0.000	0.000	0.000
72	A	105	GLN	0	-0.121	-0.053	102.073	0.000	0.000	0.000	0.000	0.000	0.000
73	A	106	HIS	0	-0.031	-0.022	104.591	0.000	0.000	0.000	0.000	0.000	0.000
74	A	107	THR	0	-0.048	-0.011	102.658	0.000	0.000	0.000	0.000	0.000	0.000
75	A	108	ILE	0	-0.061	-0.031	97.866	0.000	0.000	0.000	0.000	0.000	0.000
76	A	109	ASP	-1	-0.761	-0.847	101.773	0.017	0.017	0.000	0.000	0.000	0.000
77	A	110	LEU	0	-0.028	-0.027	95.558	0.000	0.000	0.000	0.000	0.000	0.000
78	A	111	THR	0	-0.101	-0.076	97.740	0.001	0.001	0.000	0.000	0.000	0.000
79	A	112	ASP	-1	-0.857	-0.923	100.248	0.017	0.017	0.000	0.000	0.000	0.000
80	A	113	SER	0	-0.032	-0.016	99.164	0.000	0.000	0.000	0.000	0.000	0.000
81	A	114	GLU	-1	-0.848	-0.918	95.574	0.019	0.019	0.000	0.000	0.000	0.000
82	A	115	MET	0	0.045	0.025	95.681	0.001	0.001	0.000	0.000	0.000	0.000
83	A	116	ASN	0	-0.048	-0.019	95.193	0.001	0.001	0.000	0.000	0.000	0.000
84	A	117	LYS	1	0.800	0.882	92.051	-0.019	-0.019	0.000	0.000	0.000	0.000
85	A	118	LEU	0	-0.043	-0.016	90.813	0.001	0.001	0.000	0.000	0.000	0.000
86	A	119	PHE	0	0.083	0.040	90.438	0.001	0.001	0.000	0.000	0.000	0.000
87	A	120	GLU	-1	-0.734	-0.842	89.784	0.025	0.025	0.000	0.000	0.000	0.000
88	A	121	LYS	1	0.891	0.950	86.562	-0.022	-0.022	0.000	0.000	0.000	0.000
89	A	122	THR	0	-0.026	-0.019	85.781	0.001	0.001	0.000	0.000	0.000	0.000
90	A	123	ARG	1	0.898	0.937	86.082	-0.023	-0.023	0.000	0.000	0.000	0.000
91	A	124	ARG	1	0.794	0.878	84.048	-0.025	-0.025	0.000	0.000	0.000	0.000
92	A	125	GLN	0	-0.039	-0.004	80.155	0.001	0.001	0.000	0.000	0.000	0.000
93	A	126	LEU	0	-0.087	-0.029	81.375	0.001	0.001	0.000	0.000	0.000	0.000
94	A	136	GLY	0	-0.008	-0.016	87.126	0.000	0.000	0.000	0.000	0.000	0.000
95	A	137	SER	0	-0.046	-0.019	88.881	0.000	0.000	0.000	0.000	0.000	0.000
96	A	138	PHE	0	0.018	0.006	88.773	0.000	0.000	0.000	0.000	0.000	0.000
97	A	139	LYS	1	0.994	1.003	83.754	-0.022	-0.022	0.000	0.000	0.000	0.000
98	A	140	ILE	0	0.010	0.010	80.395	0.000	0.000	0.000	0.000	0.000	0.000
99	A	141	TYR	0	-0.058	-0.035	79.940	-0.001	-0.001	0.000	0.000	0.000	0.000
100	A	142	HIS	0	-0.068	-0.045	76.260	0.001	0.001	0.000	0.000	0.000	0.000
101	A	143	LYS	1	0.864	0.914	72.721	-0.029	-0.029	0.000	0.000	0.000	0.000
102	A	144	CYS	0	-0.075	0.000	67.324	0.002	0.002	0.000	0.000	0.000	0.000
103	A	145	ASP	-1	-0.795	-0.890	70.227	0.031	0.031	0.000	0.000	0.000	0.000
104	A	146	ASN	0	0.005	-0.019	71.854	0.000	0.000	0.000	0.000	0.000	0.000
105	A	147	ALA	0	-0.006	0.005	67.510	-0.001	-0.001	0.000	0.000	0.000	0.000
106	A	149	ILE	0	-0.007	-0.025	68.017	0.000	0.000	0.000	0.000	0.000	0.000
107	A	150	GLU	-1	-0.872	-0.915	66.968	0.024	0.024	0.000	0.000	0.000	0.000
108	A	151	SER	0	-0.059	-0.038	63.793	0.000	0.000	0.000	0.000	0.000	0.000
109	A	152	ILE	0	-0.031	-0.029	64.057	0.000	0.000	0.000	0.000	0.000	0.000
110	A	153	ARG	1	0.841	0.939	65.925	-0.025	-0.025	0.000	0.000	0.000	0.000
111	A	154	ASN	0	-0.039	-0.045	64.978	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	155	GLY	0	-0.015	0.016	62.512	0.000	0.000	0.000	0.000	0.000	0.000
113	A	156	THR	0	0.004	0.014	57.563	0.000	0.000	0.000	0.000	0.000	0.000
114	A	157	TYR	0	0.036	0.005	54.250	0.001	0.001	0.000	0.000	0.000	0.000
115	A	158	ASP	-1	-0.828	-0.866	50.862	0.043	0.043	0.000	0.000	0.000	0.000
116	A	159	HIS	0	-0.090	-0.052	48.877	0.001	0.001	0.000	0.000	0.000	0.000
117	A	160	ASP	-1	-0.801	-0.871	44.122	0.053	0.053	0.000	0.000	0.000	0.000
118	A	161	VAL	0	-0.018	-0.011	43.883	0.003	0.003	0.000	0.000	0.000	0.000
119	A	162	TYR	0	0.027	0.011	34.755	0.001	0.001	0.000	0.000	0.000	0.000
120	A	163	ARG	1	0.962	0.986	38.432	-0.037	-0.037	0.000	0.000	0.000	0.000
121	A	164	ASP	-1	-0.817	-0.909	34.954	0.060	0.060	0.000	0.000	0.000	0.000
122	A	165	GLU	-1	-0.830	-0.895	29.950	0.064	0.064	0.000	0.000	0.000	0.000
123	A	166	ALA	0	-0.002	0.011	29.179	0.002	0.002	0.000	0.000	0.000	0.000
124	A	167	LEU	0	0.071	0.022	25.897	0.010	0.010	0.000	0.000	0.000	0.000
125	A	168	ASN	0	-0.017	-0.019	20.271	-0.018	-0.018	0.000	0.000	0.000	0.000
126	A	169	ASN	0	0.002	0.002	21.706	0.013	0.013	0.000	0.000	0.000	0.000
127	A	170	ARG	1	0.920	0.955	12.321	0.061	0.061	0.000	0.000	0.000	0.000
128	A	171	PHE	0	0.035	0.019	13.958	-0.045	-0.045	0.000	0.000	0.000	0.000
129	A	172	GLN	0	0.034	0.027	11.927	0.122	0.122	0.000	0.000	0.000	0.000
130	A	173	ILE	0	-0.031	-0.016	8.445	-0.077	-0.077	0.000	0.000	0.000	0.000
131	A	174	LYS	1	0.929	0.962	8.854	0.382	0.382	0.000	0.000	0.000	0.000
132	A	175	GLY	0	-0.016	-0.005	5.778	0.417	0.417	0.000	0.000	0.000	0.000

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