FMO DATABASE

FMODB ID: 9GZG2

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1093747.059123
FMO2-HF: Nuclear repulsion	1045239.824085
FMO2-HF: Total energy	-48507.235037
FMO2-MP2: Total energy	-48652.441687

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.
-8.436	-6.143	-0.008	-1.047	-1.239	-0.002

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 : -0.002 / q_NPA : -0.006

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	4	SER	0	-0.004	0.003	3.799	-0.932	0.559	-0.017	-0.647	-0.828	0.001
4	A	5	THR	0	-0.014	-0.023	5.837	0.774	0.774	0.000	0.000	0.000	0.000
5	A	6	SER	0	-0.018	-0.049	7.977	-0.068	-0.068	0.000	0.000	0.000	0.000
6	A	7	ALA	0	0.003	-0.006	11.102	-0.019	-0.019	0.000	0.000	0.000	0.000
7	A	8	GLU	-1	-0.793	-0.895	6.277	-1.949	-1.949	0.000	0.000	0.000	0.000
8	A	9	VAL	0	0.023	0.025	10.029	0.015	0.015	0.000	0.000	0.000	0.000
9	A	10	TYR	0	-0.028	-0.009	12.194	0.059	0.059	0.000	0.000	0.000	0.000
10	A	11	TYR	0	0.017	0.003	13.548	0.050	0.050	0.000	0.000	0.000	0.000
11	A	12	GLU	-1	-0.869	-0.929	12.568	-0.677	-0.677	0.000	0.000	0.000	0.000
12	A	13	GLU	-1	-0.917	-0.973	15.000	-0.083	-0.083	0.000	0.000	0.000	0.000
13	A	14	ALA	0	-0.052	-0.039	17.780	0.037	0.037	0.000	0.000	0.000	0.000
14	A	15	GLU	-1	-0.813	-0.882	16.552	-0.351	-0.351	0.000	0.000	0.000	0.000
15	A	16	GLU	-1	-0.982	-0.982	18.244	-0.189	-0.189	0.000	0.000	0.000	0.000
16	A	17	PHE	0	-0.017	-0.025	20.891	0.029	0.029	0.000	0.000	0.000	0.000
17	A	18	LEU	0	-0.015	0.003	22.866	0.018	0.018	0.000	0.000	0.000	0.000
18	A	19	SER	0	-0.048	-0.018	22.305	0.013	0.013	0.000	0.000	0.000	0.000
19	A	20	LYS	1	0.873	0.942	23.657	0.150	0.150	0.000	0.000	0.000	0.000
20	A	21	GLY	0	0.003	0.005	27.301	0.014	0.014	0.000	0.000	0.000	0.000
21	A	22	ASP	-1	-0.897	-0.946	26.688	-0.088	-0.088	0.000	0.000	0.000	0.000
22	A	23	LEU	0	0.026	-0.020	26.778	-0.010	-0.010	0.000	0.000	0.000	0.000
23	A	24	VAL	0	0.068	0.050	27.423	-0.008	-0.008	0.000	0.000	0.000	0.000
24	A	25	GLN	0	-0.021	-0.003	24.977	0.005	0.005	0.000	0.000	0.000	0.000
25	A	26	ALA	0	-0.007	-0.001	22.788	-0.007	-0.007	0.000	0.000	0.000	0.000
26	A	27	CYS	0	-0.044	-0.020	22.590	-0.018	-0.018	0.000	0.000	0.000	0.000
27	A	28	GLU	-1	-0.801	-0.905	23.706	-0.104	-0.104	0.000	0.000	0.000	0.000
28	A	29	LYS	1	0.867	0.946	19.353	0.118	0.118	0.000	0.000	0.000	0.000
29	A	30	TYR	0	-0.003	-0.049	18.874	-0.006	-0.006	0.000	0.000	0.000	0.000
30	A	31	TYR	0	-0.022	-0.004	19.575	-0.011	-0.011	0.000	0.000	0.000	0.000
31	A	32	LYS	1	0.882	0.940	19.016	0.064	0.064	0.000	0.000	0.000	0.000
32	A	33	ALA	0	0.028	0.014	15.411	0.007	0.007	0.000	0.000	0.000	0.000
33	A	34	ALA	0	-0.001	-0.001	15.863	-0.024	-0.024	0.000	0.000	0.000	0.000
34	A	35	GLU	-1	-0.872	-0.960	18.243	-0.051	-0.051	0.000	0.000	0.000	0.000
35	A	36	GLU	-1	-0.866	-0.932	14.121	-0.021	-0.021	0.000	0.000	0.000	0.000
36	A	37	ALA	0	0.027	0.028	13.885	0.002	0.002	0.000	0.000	0.000	0.000
37	A	38	ILE	0	-0.030	-0.009	14.947	0.005	0.005	0.000	0.000	0.000	0.000
38	A	39	LYS	1	0.828	0.916	16.537	0.036	0.036	0.000	0.000	0.000	0.000
39	A	40	LEU	0	0.046	0.027	9.566	0.038	0.038	0.000	0.000	0.000	0.000
40	A	41	LEU	0	0.041	0.027	14.109	0.014	0.014	0.000	0.000	0.000	0.000
41	A	42	VAL	0	-0.077	-0.038	15.989	0.019	0.019	0.000	0.000	0.000	0.000
42	A	43	ILE	0	-0.068	-0.044	15.065	0.020	0.020	0.000	0.000	0.000	0.000
43	A	44	GLU	-1	-0.869	-0.933	12.426	-0.055	-0.055	0.000	0.000	0.000	0.000
44	A	45	ASN	0	-0.105	-0.049	15.566	0.016	0.016	0.000	0.000	0.000	0.000
45	A	46	ASN	0	-0.024	-0.005	18.611	0.018	0.018	0.000	0.000	0.000	0.000
46	A	47	LEU	0	0.046	0.032	20.475	0.000	0.000	0.000	0.000	0.000	0.000
47	A	48	LYS	1	0.950	0.951	23.293	-0.038	-0.038	0.000	0.000	0.000	0.000
48	A	49	GLU	-1	-0.901	-0.950	25.439	-0.038	-0.038	0.000	0.000	0.000	0.000
49	A	50	ILE	0	-0.004	-0.003	23.558	0.006	0.006	0.000	0.000	0.000	0.000
50	A	51	THR	0	-0.010	-0.009	21.574	0.007	0.007	0.000	0.000	0.000	0.000
51	A	52	ASN	0	-0.001	-0.002	24.632	0.022	0.022	0.000	0.000	0.000	0.000
52	A	53	ASN	0	-0.119	-0.049	28.140	-0.001	-0.001	0.000	0.000	0.000	0.000
53	A	54	VAL	0	-0.011	0.021	23.817	-0.005	-0.005	0.000	0.000	0.000	0.000
54	A	55	LYS	1	0.992	1.003	27.153	-0.015	-0.015	0.000	0.000	0.000	0.000
55	A	56	ASN	0	-0.088	-0.060	28.365	0.001	0.001	0.000	0.000	0.000	0.000
56	A	57	LYS	1	1.038	1.011	25.769	-0.076	-0.076	0.000	0.000	0.000	0.000
57	A	58	GLY	0	0.005	0.018	22.840	-0.009	-0.009	0.000	0.000	0.000	0.000
58	A	59	ARG	1	0.906	0.962	22.112	0.051	0.051	0.000	0.000	0.000	0.000
59	A	60	TRP	0	0.007	0.013	20.229	-0.001	-0.001	0.000	0.000	0.000	0.000
60	A	61	LYS	1	0.936	0.972	25.033	0.009	0.009	0.000	0.000	0.000	0.000
61	A	62	SER	0	0.159	0.058	27.062	-0.004	-0.004	0.000	0.000	0.000	0.000
62	A	63	GLU	-1	-0.855	-0.935	27.750	-0.049	-0.049	0.000	0.000	0.000	0.000
63	A	64	ASN	0	-0.087	-0.044	25.710	-0.002	-0.002	0.000	0.000	0.000	0.000
64	A	65	LEU	0	0.101	0.076	21.662	-0.003	-0.003	0.000	0.000	0.000	0.000
65	A	66	PHE	0	0.014	0.019	24.642	-0.013	-0.013	0.000	0.000	0.000	0.000
66	A	67	LYS	1	0.845	0.938	27.222	0.031	0.031	0.000	0.000	0.000	0.000
67	A	68	ALA	0	0.064	0.018	22.465	-0.003	-0.003	0.000	0.000	0.000	0.000
68	A	69	SER	0	-0.006	-0.011	23.079	-0.011	-0.011	0.000	0.000	0.000	0.000
69	A	70	LYS	1	0.897	0.943	24.095	0.080	0.080	0.000	0.000	0.000	0.000
70	A	71	LEU	0	-0.009	-0.012	25.579	-0.007	-0.007	0.000	0.000	0.000	0.000
71	A	72	LEU	0	0.053	0.039	19.626	-0.001	-0.001	0.000	0.000	0.000	0.000
72	A	73	ARG	1	0.857	0.929	22.893	0.125	0.125	0.000	0.000	0.000	0.000
73	A	74	SER	0	-0.038	-0.028	25.311	-0.005	-0.005	0.000	0.000	0.000	0.000
74	A	75	ASN	0	-0.039	0.010	18.067	-0.025	-0.025	0.000	0.000	0.000	0.000
75	A	76	ASN	0	0.076	0.028	19.615	-0.002	-0.002	0.000	0.000	0.000	0.000
76	A	77	THR	0	0.025	-0.007	22.111	0.003	0.003	0.000	0.000	0.000	0.000
77	A	78	GLU	-1	-0.809	-0.908	22.156	-0.268	-0.268	0.000	0.000	0.000	0.000
78	A	79	ILE	0	0.062	0.047	19.550	0.009	0.009	0.000	0.000	0.000	0.000
79	A	80	PRO	0	-0.044	-0.020	22.162	0.013	0.013	0.000	0.000	0.000	0.000
80	A	81	ILE	0	-0.064	-0.064	25.451	0.018	0.018	0.000	0.000	0.000	0.000
81	A	82	LEU	0	0.057	0.047	19.552	0.007	0.007	0.000	0.000	0.000	0.000
82	A	83	TRP	0	0.033	0.001	21.144	0.003	0.003	0.000	0.000	0.000	0.000
83	A	84	LYS	1	0.857	0.936	23.721	0.144	0.144	0.000	0.000	0.000	0.000
84	A	85	SER	0	0.011	-0.015	24.279	0.017	0.017	0.000	0.000	0.000	0.000
85	A	86	ALA	0	0.034	0.028	22.162	0.003	0.003	0.000	0.000	0.000	0.000
86	A	87	TRP	0	-0.034	-0.026	23.973	0.014	0.014	0.000	0.000	0.000	0.000
87	A	88	THR	0	0.000	-0.003	27.157	0.010	0.010	0.000	0.000	0.000	0.000
88	A	89	LEU	0	-0.013	-0.009	23.358	0.005	0.005	0.000	0.000	0.000	0.000
89	A	90	HIS	0	-0.032	-0.015	26.147	0.015	0.015	0.000	0.000	0.000	0.000
90	A	91	VAL	0	-0.033	-0.027	27.573	0.009	0.009	0.000	0.000	0.000	0.000
91	A	92	GLU	-1	-0.859	-0.940	31.338	-0.097	-0.097	0.000	0.000	0.000	0.000
92	A	93	GLY	0	-0.010	-0.002	29.386	0.001	0.001	0.000	0.000	0.000	0.000
93	A	94	PHE	0	-0.092	-0.044	27.780	0.008	0.008	0.000	0.000	0.000	0.000
94	A	95	HIS	0	-0.062	-0.038	29.859	0.011	0.011	0.000	0.000	0.000	0.000
95	A	96	GLU	-1	-0.946	-0.976	32.996	-0.068	-0.068	0.000	0.000	0.000	0.000
96	A	97	LEU	0	-0.093	-0.016	33.119	0.003	0.003	0.000	0.000	0.000	0.000
97	A	98	SER	0	-0.008	-0.002	34.356	0.000	0.000	0.000	0.000	0.000	0.000
98	A	99	LEU	0	0.017	0.017	29.496	-0.005	-0.005	0.000	0.000	0.000	0.000
99	A	100	ASN	0	0.009	0.009	32.703	-0.005	-0.005	0.000	0.000	0.000	0.000
100	A	101	GLU	-1	-0.821	-0.918	28.685	-0.173	-0.173	0.000	0.000	0.000	0.000
101	A	102	LYS	1	0.884	0.920	28.940	0.128	0.128	0.000	0.000	0.000	0.000
102	A	103	GLU	-1	-0.903	-0.969	29.442	-0.130	-0.130	0.000	0.000	0.000	0.000
103	A	104	VAL	0	0.059	0.029	25.280	-0.010	-0.010	0.000	0.000	0.000	0.000
104	A	105	LYS	1	0.896	0.951	24.718	0.182	0.182	0.000	0.000	0.000	0.000
105	A	106	LYS	1	0.951	0.970	24.367	0.137	0.137	0.000	0.000	0.000	0.000
106	A	107	LEU	0	0.028	0.027	25.355	-0.011	-0.011	0.000	0.000	0.000	0.000
107	A	108	LYS	1	0.924	0.977	20.147	0.318	0.318	0.000	0.000	0.000	0.000
108	A	109	GLU	-1	-0.958	-0.974	19.929	-0.416	-0.416	0.000	0.000	0.000	0.000
109	A	110	ASP	-1	-0.846	-0.898	20.144	-0.266	-0.266	0.000	0.000	0.000	0.000
110	A	111	VAL	0	-0.046	-0.030	17.277	-0.014	-0.014	0.000	0.000	0.000	0.000
111	A	112	ARG	1	0.957	0.999	12.878	0.623	0.623	0.000	0.000	0.000	0.000
112	A	113	LYS	1	0.871	0.924	15.031	0.254	0.254	0.000	0.000	0.000	0.000
113	A	114	LEU	0	-0.005	-0.004	16.131	-0.020	-0.020	0.000	0.000	0.000	0.000
114	A	115	VAL	0	-0.003	-0.016	11.322	-0.010	-0.010	0.000	0.000	0.000	0.000
115	A	116	ILE	0	-0.009	-0.004	10.968	-0.061	-0.061	0.000	0.000	0.000	0.000
116	A	117	PHE	0	-0.026	-0.003	11.545	-0.051	-0.051	0.000	0.000	0.000	0.000
117	A	118	ALA	0	-0.007	-0.007	11.865	-0.002	-0.002	0.000	0.000	0.000	0.000
118	A	119	VAL	0	0.025	0.023	6.204	0.077	0.077	0.000	0.000	0.000	0.000
119	A	120	ASN	0	-0.023	-0.017	8.004	-0.279	-0.279	0.000	0.000	0.000	0.000
120	A	121	SER	0	-0.145	-0.077	10.347	0.075	0.075	0.000	0.000	0.000	0.000
121	A	122	LEU	0	-0.015	0.012	6.843	0.110	0.110	0.000	0.000	0.000	0.000
122	A	123	GLU	-1	-0.990	-0.985	3.487	-5.621	-4.819	0.009	-0.400	-0.411	-0.003

Top

Graph

Manual

About

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