FMO DATABASE

FMODB ID: M343Z

Calculation Name: 2Q00-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2Q00

Chain ID: A

ChEMBL ID:

UniProt ID: P95883

Base Structure: X-ray

Registration Date: 2023-06-19

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	122
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1093898.255206
FMO2-HF: Nuclear repulsion	1045390.024302
FMO2-HF: Total energy	-48508.230904
FMO2-MP2: Total energy	-48653.378917

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:2:SER)

Summations of interaction energy for fragment #1(A:2: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.
-6.318	-4.16	-0.012	-0.96	-1.186	0

Interaction energy analysis for fragmet #1(A:2:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.000 / q_NPA : -0.007

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

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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	4	SER	0	0.001	0.008	3.799	0.064	1.576	-0.018	-0.651	-0.842	0.002
4	A	5	THR	0	-0.008	-0.035	6.476	-0.360	-0.360	0.000	0.000	0.000	0.000
5	A	6	SER	0	-0.027	-0.061	8.456	-0.075	-0.075	0.000	0.000	0.000	0.000
6	A	7	ALA	0	-0.006	-0.010	11.875	-0.059	-0.059	0.000	0.000	0.000	0.000
7	A	8	GLU	-1	-0.775	-0.868	7.443	1.442	1.442	0.000	0.000	0.000	0.000
8	A	9	VAL	0	0.006	0.012	10.640	-0.083	-0.083	0.000	0.000	0.000	0.000
9	A	10	TYR	0	-0.031	-0.012	12.952	-0.067	-0.067	0.000	0.000	0.000	0.000
10	A	11	TYR	0	-0.028	-0.046	14.436	-0.051	-0.051	0.000	0.000	0.000	0.000
11	A	12	GLU	-1	-0.868	-0.931	12.947	0.150	0.150	0.000	0.000	0.000	0.000
12	A	13	GLU	-1	-0.841	-0.919	15.569	0.160	0.160	0.000	0.000	0.000	0.000
13	A	14	ALA	0	-0.035	-0.028	18.349	-0.023	-0.023	0.000	0.000	0.000	0.000
14	A	15	GLU	-1	-0.720	-0.818	17.428	0.063	0.063	0.000	0.000	0.000	0.000
15	A	16	GLU	-1	-0.882	-0.906	18.519	0.088	0.088	0.000	0.000	0.000	0.000
16	A	17	PHE	0	-0.035	-0.030	21.113	-0.011	-0.011	0.000	0.000	0.000	0.000
17	A	18	LEU	0	-0.002	0.010	23.482	-0.012	-0.012	0.000	0.000	0.000	0.000
18	A	19	SER	0	-0.067	-0.036	22.404	-0.012	-0.012	0.000	0.000	0.000	0.000
19	A	20	LYS	1	0.771	0.875	22.371	-0.087	-0.087	0.000	0.000	0.000	0.000
20	A	21	GLY	0	-0.003	0.002	27.429	-0.002	-0.002	0.000	0.000	0.000	0.000
21	A	22	ASP	-1	-0.887	-0.942	27.360	0.071	0.071	0.000	0.000	0.000	0.000
22	A	23	LEU	0	0.023	-0.020	27.483	0.006	0.006	0.000	0.000	0.000	0.000
23	A	24	VAL	0	0.060	0.045	28.324	0.004	0.004	0.000	0.000	0.000	0.000
24	A	25	GLN	0	-0.001	0.005	25.684	0.007	0.007	0.000	0.000	0.000	0.000
25	A	26	ALA	0	-0.011	-0.001	23.657	0.011	0.011	0.000	0.000	0.000	0.000
26	A	27	CYS	0	-0.048	-0.020	23.488	0.007	0.007	0.000	0.000	0.000	0.000
27	A	28	GLU	-1	-0.738	-0.869	24.603	0.112	0.112	0.000	0.000	0.000	0.000
28	A	29	LYS	1	0.778	0.887	20.159	-0.151	-0.151	0.000	0.000	0.000	0.000
29	A	30	TYR	0	0.006	-0.038	19.830	0.017	0.017	0.000	0.000	0.000	0.000
30	A	31	TYR	0	-0.012	-0.002	20.489	0.003	0.003	0.000	0.000	0.000	0.000
31	A	32	LYS	1	0.871	0.935	19.662	-0.139	-0.139	0.000	0.000	0.000	0.000
32	A	33	ALA	0	0.020	0.008	16.298	0.016	0.016	0.000	0.000	0.000	0.000
33	A	34	ALA	0	0.005	0.001	16.716	0.011	0.011	0.000	0.000	0.000	0.000
34	A	35	GLU	-1	-0.833	-0.910	18.965	0.122	0.122	0.000	0.000	0.000	0.000
35	A	36	GLU	-1	-0.822	-0.883	14.532	0.238	0.238	0.000	0.000	0.000	0.000
36	A	37	ALA	0	0.029	0.028	14.526	0.007	0.007	0.000	0.000	0.000	0.000
37	A	38	ILE	0	-0.027	-0.011	15.601	-0.029	-0.029	0.000	0.000	0.000	0.000
38	A	39	LYS	1	0.780	0.875	16.659	-0.186	-0.186	0.000	0.000	0.000	0.000
39	A	40	LEU	0	0.030	0.019	9.905	-0.014	-0.014	0.000	0.000	0.000	0.000
40	A	41	LEU	0	0.051	0.031	14.200	-0.043	-0.043	0.000	0.000	0.000	0.000
41	A	42	VAL	0	-0.065	-0.034	16.201	-0.029	-0.029	0.000	0.000	0.000	0.000
42	A	43	ILE	0	-0.060	-0.039	14.470	-0.013	-0.013	0.000	0.000	0.000	0.000
43	A	44	GLU	-1	-0.852	-0.922	12.211	-0.132	-0.132	0.000	0.000	0.000	0.000
44	A	45	ASN	0	-0.129	-0.065	15.282	-0.034	-0.034	0.000	0.000	0.000	0.000
45	A	46	ASN	0	-0.015	-0.002	18.306	0.015	0.015	0.000	0.000	0.000	0.000
46	A	47	LEU	0	0.032	0.029	20.075	0.000	0.000	0.000	0.000	0.000	0.000
47	A	48	LYS	1	0.913	0.942	22.978	-0.011	-0.011	0.000	0.000	0.000	0.000
48	A	49	GLU	-1	-0.858	-0.934	24.995	0.005	0.005	0.000	0.000	0.000	0.000
49	A	50	ILE	0	-0.009	-0.006	23.446	0.005	0.005	0.000	0.000	0.000	0.000
50	A	51	THR	0	0.011	-0.006	21.028	0.007	0.007	0.000	0.000	0.000	0.000
51	A	52	ASN	0	0.000	0.008	24.295	0.009	0.009	0.000	0.000	0.000	0.000
52	A	53	ASN	0	-0.084	-0.028	27.701	-0.001	-0.001	0.000	0.000	0.000	0.000
53	A	54	VAL	0	-0.003	0.014	23.500	0.002	0.002	0.000	0.000	0.000	0.000
54	A	55	LYS	1	0.982	0.998	26.877	-0.055	-0.055	0.000	0.000	0.000	0.000
55	A	56	ASN	0	-0.071	-0.056	28.086	0.002	0.002	0.000	0.000	0.000	0.000
56	A	57	LYS	1	1.033	1.016	25.449	-0.098	-0.098	0.000	0.000	0.000	0.000
57	A	58	GLY	0	-0.003	0.011	22.652	-0.003	-0.003	0.000	0.000	0.000	0.000
58	A	59	ARG	1	0.823	0.903	22.245	-0.113	-0.113	0.000	0.000	0.000	0.000
59	A	60	TRP	0	0.001	-0.004	20.195	-0.011	-0.011	0.000	0.000	0.000	0.000
60	A	61	LYS	1	0.868	0.928	25.137	-0.048	-0.048	0.000	0.000	0.000	0.000
61	A	62	SER	0	0.123	0.050	27.468	-0.001	-0.001	0.000	0.000	0.000	0.000
62	A	63	GLU	-1	-0.795	-0.896	28.196	0.044	0.044	0.000	0.000	0.000	0.000
63	A	64	ASN	0	-0.044	-0.014	26.028	-0.011	-0.011	0.000	0.000	0.000	0.000
64	A	65	LEU	0	0.098	0.071	21.915	-0.006	-0.006	0.000	0.000	0.000	0.000
65	A	66	PHE	0	0.009	0.016	25.036	-0.007	-0.007	0.000	0.000	0.000	0.000
66	A	67	LYS	1	0.797	0.898	27.707	-0.039	-0.039	0.000	0.000	0.000	0.000
67	A	68	ALA	0	0.055	0.017	22.628	-0.007	-0.007	0.000	0.000	0.000	0.000
68	A	69	SER	0	-0.016	-0.014	23.631	-0.009	-0.009	0.000	0.000	0.000	0.000
69	A	70	LYS	1	0.898	0.946	24.638	-0.026	-0.026	0.000	0.000	0.000	0.000
70	A	71	LEU	0	-0.009	-0.008	25.753	-0.006	-0.006	0.000	0.000	0.000	0.000
71	A	72	LEU	0	0.045	0.033	20.029	-0.008	-0.008	0.000	0.000	0.000	0.000
72	A	73	ARG	1	0.864	0.933	23.339	0.011	0.011	0.000	0.000	0.000	0.000
73	A	74	SER	0	-0.038	-0.026	25.544	-0.003	-0.003	0.000	0.000	0.000	0.000
74	A	75	ASN	0	-0.038	0.002	18.040	0.000	0.000	0.000	0.000	0.000	0.000
75	A	76	ASN	0	0.077	0.029	19.341	-0.003	-0.003	0.000	0.000	0.000	0.000
76	A	77	THR	0	0.024	-0.003	22.474	0.011	0.011	0.000	0.000	0.000	0.000
77	A	78	GLU	-1	-0.820	-0.905	22.749	-0.022	-0.022	0.000	0.000	0.000	0.000
78	A	79	ILE	0	0.067	0.048	19.737	0.010	0.010	0.000	0.000	0.000	0.000
79	A	80	PRO	0	-0.013	-0.007	22.898	0.010	0.010	0.000	0.000	0.000	0.000
80	A	81	ILE	0	-0.069	-0.060	26.241	0.006	0.006	0.000	0.000	0.000	0.000
81	A	82	LEU	0	0.061	0.053	20.495	0.002	0.002	0.000	0.000	0.000	0.000
82	A	83	TRP	0	0.031	-0.004	21.910	0.009	0.009	0.000	0.000	0.000	0.000
83	A	84	LYS	1	0.828	0.919	24.606	-0.011	-0.011	0.000	0.000	0.000	0.000
84	A	85	SER	0	0.027	-0.004	25.353	0.001	0.001	0.000	0.000	0.000	0.000
85	A	86	ALA	0	0.021	0.021	23.025	0.005	0.005	0.000	0.000	0.000	0.000
86	A	87	TRP	0	-0.051	-0.028	24.900	0.005	0.005	0.000	0.000	0.000	0.000
87	A	88	THR	0	-0.011	-0.022	28.048	0.001	0.001	0.000	0.000	0.000	0.000
88	A	89	LEU	0	-0.021	-0.012	24.356	0.001	0.001	0.000	0.000	0.000	0.000
89	A	90	HIS	0	-0.018	-0.010	26.887	0.004	0.004	0.000	0.000	0.000	0.000
90	A	91	VAL	0	-0.023	-0.024	28.451	0.000	0.000	0.000	0.000	0.000	0.000
91	A	92	GLU	-1	-0.811	-0.901	32.218	0.033	0.033	0.000	0.000	0.000	0.000
92	A	93	GLY	0	0.008	0.007	30.312	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	94	PHE	0	-0.088	-0.044	28.621	0.001	0.001	0.000	0.000	0.000	0.000
94	A	95	HIS	0	-0.062	-0.043	30.550	-0.003	-0.003	0.000	0.000	0.000	0.000
95	A	96	GLU	-1	-0.955	-0.982	33.840	0.033	0.033	0.000	0.000	0.000	0.000
96	A	97	LEU	0	-0.093	-0.020	33.693	-0.003	-0.003	0.000	0.000	0.000	0.000
97	A	98	SER	0	-0.017	-0.006	35.253	-0.002	-0.002	0.000	0.000	0.000	0.000
98	A	99	LEU	0	-0.011	0.008	30.743	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	100	ASN	0	-0.006	-0.003	33.661	0.002	0.002	0.000	0.000	0.000	0.000
100	A	101	GLU	-1	-0.763	-0.871	29.391	0.028	0.028	0.000	0.000	0.000	0.000
101	A	102	LYS	1	0.884	0.921	29.802	-0.020	-0.020	0.000	0.000	0.000	0.000
102	A	103	GLU	-1	-0.866	-0.946	30.445	0.022	0.022	0.000	0.000	0.000	0.000
103	A	104	VAL	0	0.059	0.029	26.336	0.002	0.002	0.000	0.000	0.000	0.000
104	A	105	LYS	1	0.851	0.916	25.658	-0.026	-0.026	0.000	0.000	0.000	0.000
105	A	106	LYS	1	0.935	0.963	25.379	-0.014	-0.014	0.000	0.000	0.000	0.000
106	A	107	LEU	0	0.021	0.028	26.368	-0.001	-0.001	0.000	0.000	0.000	0.000
107	A	108	LYS	1	0.826	0.915	20.323	-0.060	-0.060	0.000	0.000	0.000	0.000
108	A	109	GLU	-1	-0.881	-0.934	20.512	0.051	0.051	0.000	0.000	0.000	0.000
109	A	110	ASP	-1	-0.850	-0.902	21.139	0.022	0.022	0.000	0.000	0.000	0.000
110	A	111	VAL	0	-0.046	-0.034	18.294	0.002	0.002	0.000	0.000	0.000	0.000
111	A	112	ARG	1	0.950	0.998	14.127	-0.068	-0.068	0.000	0.000	0.000	0.000
112	A	113	LYS	1	0.832	0.901	16.013	0.037	0.037	0.000	0.000	0.000	0.000
113	A	114	LEU	0	-0.004	-0.004	16.921	-0.011	-0.011	0.000	0.000	0.000	0.000
114	A	115	VAL	0	-0.006	-0.018	12.354	0.003	0.003	0.000	0.000	0.000	0.000
115	A	116	ILE	0	0.000	0.001	11.809	0.037	0.037	0.000	0.000	0.000	0.000
116	A	117	PHE	0	-0.027	-0.008	12.151	-0.040	-0.040	0.000	0.000	0.000	0.000
117	A	118	ALA	0	-0.007	0.002	12.914	-0.042	-0.042	0.000	0.000	0.000	0.000
118	A	119	VAL	0	0.040	0.027	6.922	-0.084	-0.084	0.000	0.000	0.000	0.000
119	A	120	ASN	0	-0.019	-0.014	8.363	-0.104	-0.104	0.000	0.000	0.000	0.000
120	A	121	SER	0	-0.136	-0.070	10.567	-0.095	-0.095	0.000	0.000	0.000	0.000
121	A	122	LEU	0	-0.004	0.015	6.666	0.030	0.030	0.000	0.000	0.000	0.000
122	A	123	GLU	-1	-1.022	-1.000	3.625	-6.698	-6.052	0.006	-0.309	-0.344	-0.002

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:SER)