FMO DATABASE

FMODB ID: 6NQ3Z

Calculation Name: 2QJX-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2QJX

Chain ID: A

ChEMBL ID:

UniProt ID: P40013

Base Structure: X-ray

Registration Date: 2023-09-20

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	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	117
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1111274.593101
FMO2-HF: Nuclear repulsion	1061526.571508
FMO2-HF: Total energy	-49748.021593
FMO2-MP2: Total energy	-49891.769555

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:8:SER)

Summations of interaction energy for fragment #1(A:8:SER)

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.
-55.45	-57.472	29.514	-15.657	-11.833	-0.088

Interaction energy analysis for fragmet #1(A:8:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.012 / q_NPA : -0.034

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	10	THR	0	0.078	0.039	2.729	-4.470	-1.026	0.512	-1.755	-2.201	0.012
4	A	11	GLU	-1	-0.791	-0.852	1.616	-47.510	-53.957	28.993	-13.579	-8.967	-0.101
5	A	12	LEU	0	-0.081	-0.041	3.997	-0.290	0.570	0.009	-0.294	-0.574	0.001
6	A	13	LEU	0	0.027	0.009	5.867	-0.358	-0.358	0.000	0.000	0.000	0.000
7	A	14	THR	0	-0.012	-0.012	6.968	-0.230	-0.230	0.000	0.000	0.000	0.000
8	A	15	TRP	0	-0.012	-0.012	7.921	0.019	0.019	0.000	0.000	0.000	0.000
9	A	16	LEU	0	0.005	0.005	9.607	-0.018	-0.018	0.000	0.000	0.000	0.000
10	A	17	ASN	0	-0.025	-0.019	11.723	-0.047	-0.047	0.000	0.000	0.000	0.000
11	A	18	GLY	0	0.043	0.034	12.744	-0.042	-0.042	0.000	0.000	0.000	0.000
12	A	19	LEU	0	-0.017	-0.010	13.647	-0.001	-0.001	0.000	0.000	0.000	0.000
13	A	20	LEU	0	-0.043	-0.028	15.413	-0.007	-0.007	0.000	0.000	0.000	0.000
14	A	21	ASN	0	-0.008	-0.002	17.343	0.003	0.003	0.000	0.000	0.000	0.000
15	A	22	LEU	0	-0.038	-0.010	15.788	0.022	0.022	0.000	0.000	0.000	0.000
16	A	23	ASN	0	0.073	0.022	15.914	0.000	0.000	0.000	0.000	0.000	0.000
17	A	24	TYR	0	0.015	0.025	13.027	0.017	0.017	0.000	0.000	0.000	0.000
18	A	25	LYS	1	0.807	0.872	11.980	-0.466	-0.466	0.000	0.000	0.000	0.000
19	A	26	LYS	1	0.850	0.914	10.324	-0.539	-0.539	0.000	0.000	0.000	0.000
20	A	27	ILE	0	-0.005	0.003	6.564	-0.024	-0.024	0.000	0.000	0.000	0.000
21	A	28	GLU	-1	-0.796	-0.903	10.330	0.915	0.915	0.000	0.000	0.000	0.000
22	A	29	GLU	-1	-0.751	-0.864	13.744	0.569	0.569	0.000	0.000	0.000	0.000
23	A	30	CYS	0	-0.018	0.000	12.247	-0.057	-0.057	0.000	0.000	0.000	0.000
24	A	31	GLY	0	0.035	0.021	14.698	-0.048	-0.048	0.000	0.000	0.000	0.000
25	A	32	THR	0	0.026	0.014	16.642	-0.062	-0.062	0.000	0.000	0.000	0.000
26	A	33	GLY	0	-0.009	-0.004	18.199	-0.051	-0.051	0.000	0.000	0.000	0.000
27	A	34	ALA	0	0.003	0.009	19.516	-0.015	-0.015	0.000	0.000	0.000	0.000
28	A	35	ALA	0	0.061	0.024	15.648	-0.023	-0.023	0.000	0.000	0.000	0.000
29	A	36	TYR	0	-0.032	-0.047	12.860	0.018	0.018	0.000	0.000	0.000	0.000
30	A	37	CYS	0	-0.041	-0.011	17.468	-0.036	-0.036	0.000	0.000	0.000	0.000
31	A	38	GLN	0	0.024	-0.001	19.560	-0.005	-0.005	0.000	0.000	0.000	0.000
32	A	39	ILE	0	-0.018	0.008	13.462	-0.019	-0.019	0.000	0.000	0.000	0.000
33	A	40	MET	0	0.009	0.012	17.540	-0.027	-0.027	0.000	0.000	0.000	0.000
34	A	41	ASP	-1	-0.764	-0.850	20.280	0.123	0.123	0.000	0.000	0.000	0.000
35	A	42	SER	0	-0.044	-0.034	18.627	-0.025	-0.025	0.000	0.000	0.000	0.000
36	A	43	ILE	0	-0.037	-0.008	17.176	-0.014	-0.014	0.000	0.000	0.000	0.000
37	A	44	TYR	0	-0.022	-0.034	21.217	-0.023	-0.023	0.000	0.000	0.000	0.000
38	A	45	GLY	0	0.045	0.038	24.722	-0.011	-0.011	0.000	0.000	0.000	0.000
39	A	46	ASP	-1	-0.781	-0.851	26.699	0.136	0.136	0.000	0.000	0.000	0.000
40	A	47	LEU	0	0.017	0.009	23.806	0.004	0.004	0.000	0.000	0.000	0.000
41	A	48	PRO	0	-0.014	0.004	27.298	-0.012	-0.012	0.000	0.000	0.000	0.000
42	A	49	MET	0	0.045	0.007	23.368	0.011	0.011	0.000	0.000	0.000	0.000
43	A	50	ASN	0	-0.018	-0.007	27.820	0.002	0.002	0.000	0.000	0.000	0.000
44	A	51	ARG	1	0.953	0.971	30.560	-0.131	-0.131	0.000	0.000	0.000	0.000
45	A	52	VAL	0	-0.002	0.019	23.765	0.006	0.006	0.000	0.000	0.000	0.000
46	A	53	LYS	1	0.866	0.932	26.355	-0.193	-0.193	0.000	0.000	0.000	0.000
47	A	54	PHE	0	0.005	-0.019	19.458	0.019	0.019	0.000	0.000	0.000	0.000
48	A	55	ASN	0	-0.009	-0.008	22.381	0.039	0.039	0.000	0.000	0.000	0.000
49	A	56	ALA	0	-0.017	0.003	23.690	-0.012	-0.012	0.000	0.000	0.000	0.000
50	A	57	THR	0	-0.018	-0.014	23.993	0.019	0.019	0.000	0.000	0.000	0.000
51	A	58	ALA	0	0.007	0.013	25.965	0.003	0.003	0.000	0.000	0.000	0.000
52	A	59	GLU	-1	-0.874	-0.946	24.494	0.274	0.274	0.000	0.000	0.000	0.000
53	A	60	TYR	0	0.060	0.010	26.415	0.005	0.005	0.000	0.000	0.000	0.000
54	A	61	GLU	-1	-0.780	-0.870	26.735	0.207	0.207	0.000	0.000	0.000	0.000
55	A	62	PHE	0	0.070	0.031	22.258	0.005	0.005	0.000	0.000	0.000	0.000
56	A	63	GLN	0	-0.010	-0.010	24.061	0.001	0.001	0.000	0.000	0.000	0.000
57	A	64	THR	0	-0.051	-0.025	26.210	-0.014	-0.014	0.000	0.000	0.000	0.000
58	A	65	ASN	0	-0.025	-0.027	22.731	-0.030	-0.030	0.000	0.000	0.000	0.000
59	A	66	TYR	0	0.008	-0.029	18.181	0.010	0.010	0.000	0.000	0.000	0.000
60	A	67	LYS	1	0.950	0.994	23.496	-0.207	-0.207	0.000	0.000	0.000	0.000
61	A	68	ILE	0	-0.004	0.017	25.540	-0.014	-0.014	0.000	0.000	0.000	0.000
62	A	69	LEU	0	0.010	0.001	19.002	-0.008	-0.008	0.000	0.000	0.000	0.000
63	A	70	GLN	0	-0.011	-0.013	23.544	-0.017	-0.017	0.000	0.000	0.000	0.000
64	A	71	SER	0	-0.019	-0.020	25.190	-0.018	-0.018	0.000	0.000	0.000	0.000
65	A	72	CYS	0	-0.103	-0.039	23.889	-0.018	-0.018	0.000	0.000	0.000	0.000
66	A	73	PHE	0	0.032	-0.007	18.553	-0.001	-0.001	0.000	0.000	0.000	0.000
67	A	74	SER	0	-0.001	0.012	24.777	-0.016	-0.016	0.000	0.000	0.000	0.000
68	A	75	ARG	1	0.844	0.906	27.459	-0.162	-0.162	0.000	0.000	0.000	0.000
69	A	76	HIS	1	0.784	0.874	25.174	-0.157	-0.157	0.000	0.000	0.000	0.000
70	A	77	GLY	0	0.062	0.048	26.693	-0.002	-0.002	0.000	0.000	0.000	0.000
71	A	78	ILE	0	-0.069	-0.031	21.059	0.005	0.005	0.000	0.000	0.000	0.000
72	A	79	GLU	-1	-0.890	-0.950	23.930	0.168	0.168	0.000	0.000	0.000	0.000
73	A	80	LYS	1	0.795	0.920	15.795	-0.460	-0.460	0.000	0.000	0.000	0.000
74	A	81	THR	0	0.058	0.016	19.667	0.017	0.017	0.000	0.000	0.000	0.000
75	A	82	VAL	0	0.025	0.008	18.961	0.052	0.052	0.000	0.000	0.000	0.000
76	A	83	TYR	0	0.039	0.027	17.536	-0.027	-0.027	0.000	0.000	0.000	0.000
77	A	84	VAL	0	0.057	0.017	19.779	0.030	0.030	0.000	0.000	0.000	0.000
78	A	85	ASP	-1	-0.806	-0.889	21.064	0.330	0.330	0.000	0.000	0.000	0.000
79	A	86	LYS	1	0.797	0.888	17.489	-0.329	-0.329	0.000	0.000	0.000	0.000
80	A	87	LEU	0	-0.043	-0.014	14.933	0.027	0.027	0.000	0.000	0.000	0.000
81	A	88	ILE	0	0.029	0.020	17.439	0.029	0.029	0.000	0.000	0.000	0.000
82	A	89	ARG	1	0.937	0.976	19.735	-0.313	-0.313	0.000	0.000	0.000	0.000
83	A	90	CYS	0	-0.048	-0.003	16.480	0.003	0.003	0.000	0.000	0.000	0.000
84	A	91	LYS	1	0.870	0.930	15.075	-0.505	-0.505	0.000	0.000	0.000	0.000
85	A	92	PHE	0	0.045	0.015	6.170	0.085	0.085	0.000	0.000	0.000	0.000
86	A	93	GLN	0	-0.024	-0.029	8.238	0.218	0.218	0.000	0.000	0.000	0.000
87	A	94	ASP	-1	-0.744	-0.867	10.230	0.733	0.733	0.000	0.000	0.000	0.000
88	A	95	ASN	0	0.010	0.000	11.919	-0.032	-0.032	0.000	0.000	0.000	0.000
89	A	96	LEU	0	-0.038	0.001	4.009	0.031	0.152	0.000	-0.029	-0.091	0.000
90	A	97	GLU	-1	-0.846	-0.916	7.828	1.150	1.150	0.000	0.000	0.000	0.000
91	A	98	PHE	0	-0.026	-0.008	9.654	-0.048	-0.048	0.000	0.000	0.000	0.000
92	A	99	LEU	0	0.042	0.017	8.305	-0.074	-0.074	0.000	0.000	0.000	0.000
93	A	100	GLN	0	-0.010	-0.010	5.034	-0.152	-0.152	0.000	0.000	0.000	0.000
94	A	101	TRP	0	0.004	-0.002	8.446	-0.185	-0.185	0.000	0.000	0.000	0.000
95	A	102	LEU	0	0.028	0.010	11.976	-0.130	-0.130	0.000	0.000	0.000	0.000
96	A	103	LYS	1	0.901	0.976	5.559	-0.343	-0.343	0.000	0.000	0.000	0.000
97	A	104	LYS	1	0.901	0.949	7.242	-1.826	-1.826	0.000	0.000	0.000	0.000
98	A	105	HIS	0	-0.040	-0.004	12.182	-0.155	-0.155	0.000	0.000	0.000	0.000
99	A	106	TRP	0	0.061	-0.002	13.731	-0.060	-0.060	0.000	0.000	0.000	0.000
100	A	107	ILE	0	-0.019	-0.007	10.336	-0.050	-0.050	0.000	0.000	0.000	0.000
101	A	108	ARG	1	0.919	0.969	14.847	-0.139	-0.139	0.000	0.000	0.000	0.000
102	A	109	HIS	1	0.872	0.926	17.760	-0.168	-0.168	0.000	0.000	0.000	0.000
103	A	110	LYS	1	0.757	0.887	18.262	-0.050	-0.050	0.000	0.000	0.000	0.000
104	A	111	ASP	-1	-0.719	-0.806	20.046	0.028	0.028	0.000	0.000	0.000	0.000
105	A	112	GLU	-1	-0.877	-0.944	22.571	-0.021	-0.021	0.000	0.000	0.000	0.000
106	A	113	SER	0	-0.110	-0.065	24.782	-0.003	-0.003	0.000	0.000	0.000	0.000
107	A	114	VAL	0	0.008	0.002	23.623	0.004	0.004	0.000	0.000	0.000	0.000
108	A	115	TYR	0	-0.021	-0.044	21.071	0.022	0.022	0.000	0.000	0.000	0.000
109	A	116	ASP	-1	-0.776	-0.878	22.582	0.073	0.073	0.000	0.000	0.000	0.000
110	A	117	PRO	0	0.006	-0.008	20.159	0.011	0.011	0.000	0.000	0.000	0.000
111	A	118	ASP	-1	-0.758	-0.848	22.680	0.153	0.153	0.000	0.000	0.000	0.000
112	A	119	ALA	0	0.019	0.012	25.209	0.004	0.004	0.000	0.000	0.000	0.000
113	A	120	ARG	1	0.767	0.852	24.943	-0.118	-0.118	0.000	0.000	0.000	0.000
114	A	121	ARG	1	0.749	0.858	20.143	-0.191	-0.191	0.000	0.000	0.000	0.000
115	A	122	LYS	1	0.864	0.936	26.547	-0.104	-0.104	0.000	0.000	0.000	0.000
116	A	123	TYR	0	0.019	0.000	27.404	0.001	0.001	0.000	0.000	0.000	0.000
117	A	124	ARG	1	0.793	0.901	25.204	-0.138	-0.138	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:8:SER)