FMO DATABASE

FMODB ID: 7GQGK

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1095464.717191
FMO2-HF: Nuclear repulsion	1046955.976774
FMO2-HF: Total energy	-48508.740417
FMO2-MP2: Total energy	-48653.755205

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.
-16.705	-11.891	0.991	-2.96	-2.844	-0.027

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 : -0.005

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	-0.036	-0.014	3.870	-0.132	1.261	-0.013	-0.650	-0.729	0.001
4	A	5	THR	0	-0.024	-0.045	6.460	-0.550	-0.550	0.000	0.000	0.000	0.000
5	A	6	SER	0	-0.031	-0.060	8.498	-0.074	-0.074	0.000	0.000	0.000	0.000
6	A	7	ALA	0	0.004	-0.001	11.808	-0.063	-0.063	0.000	0.000	0.000	0.000
7	A	8	GLU	-1	-0.728	-0.827	7.253	1.776	1.776	0.000	0.000	0.000	0.000
8	A	9	VAL	0	-0.005	0.008	10.785	-0.100	-0.100	0.000	0.000	0.000	0.000
9	A	10	TYR	0	-0.027	-0.023	13.076	-0.073	-0.073	0.000	0.000	0.000	0.000
10	A	11	TYR	0	-0.047	-0.055	14.240	-0.060	-0.060	0.000	0.000	0.000	0.000
11	A	12	GLU	-1	-0.878	-0.952	13.289	0.208	0.208	0.000	0.000	0.000	0.000
12	A	13	GLU	-1	-0.830	-0.916	15.677	0.177	0.177	0.000	0.000	0.000	0.000
13	A	14	ALA	0	-0.022	-0.007	18.445	-0.027	-0.027	0.000	0.000	0.000	0.000
14	A	15	GLU	-1	-0.693	-0.799	17.565	0.085	0.085	0.000	0.000	0.000	0.000
15	A	16	GLU	-1	-0.825	-0.877	18.744	0.112	0.112	0.000	0.000	0.000	0.000
16	A	17	PHE	0	-0.052	-0.038	21.023	-0.015	-0.015	0.000	0.000	0.000	0.000
17	A	18	LEU	0	-0.005	-0.003	23.630	-0.014	-0.014	0.000	0.000	0.000	0.000
18	A	19	SER	0	-0.068	-0.050	22.377	-0.014	-0.014	0.000	0.000	0.000	0.000
19	A	20	LYS	1	0.749	0.865	22.521	-0.124	-0.124	0.000	0.000	0.000	0.000
20	A	21	GLY	0	-0.007	0.005	27.334	-0.004	-0.004	0.000	0.000	0.000	0.000
21	A	22	ASP	-1	-0.863	-0.928	27.485	0.084	0.084	0.000	0.000	0.000	0.000
22	A	23	LEU	0	0.030	-0.017	27.315	0.008	0.008	0.000	0.000	0.000	0.000
23	A	24	VAL	0	0.048	0.050	28.179	0.003	0.003	0.000	0.000	0.000	0.000
24	A	25	GLN	0	0.014	-0.007	25.331	0.011	0.011	0.000	0.000	0.000	0.000
25	A	26	ALA	0	-0.019	0.000	23.523	0.012	0.012	0.000	0.000	0.000	0.000
26	A	27	CYS	0	-0.059	-0.007	23.433	0.006	0.006	0.000	0.000	0.000	0.000
27	A	28	GLU	-1	-0.723	-0.853	24.489	0.120	0.120	0.000	0.000	0.000	0.000
28	A	29	LYS	1	0.724	0.873	20.095	-0.167	-0.167	0.000	0.000	0.000	0.000
29	A	30	TYR	0	0.029	-0.025	19.694	0.017	0.017	0.000	0.000	0.000	0.000
30	A	31	TYR	0	-0.022	-0.008	20.407	0.000	0.000	0.000	0.000	0.000	0.000
31	A	32	LYS	1	0.881	0.937	19.306	-0.159	-0.159	0.000	0.000	0.000	0.000
32	A	33	ALA	0	0.018	0.018	16.223	0.015	0.015	0.000	0.000	0.000	0.000
33	A	34	ALA	0	0.027	0.009	16.380	0.008	0.008	0.000	0.000	0.000	0.000
34	A	35	GLU	-1	-0.815	-0.900	18.753	0.119	0.119	0.000	0.000	0.000	0.000
35	A	36	GLU	-1	-0.826	-0.881	14.294	0.238	0.238	0.000	0.000	0.000	0.000
36	A	37	ALA	0	0.028	0.025	14.152	0.000	0.000	0.000	0.000	0.000	0.000
37	A	38	ILE	0	-0.045	-0.023	15.219	-0.042	-0.042	0.000	0.000	0.000	0.000
38	A	39	LYS	1	0.770	0.861	16.424	-0.187	-0.187	0.000	0.000	0.000	0.000
39	A	40	LEU	0	0.029	0.021	9.492	-0.009	-0.009	0.000	0.000	0.000	0.000
40	A	41	LEU	0	0.024	0.018	13.850	-0.056	-0.056	0.000	0.000	0.000	0.000
41	A	42	VAL	0	-0.038	-0.028	15.809	-0.033	-0.033	0.000	0.000	0.000	0.000
42	A	43	ILE	0	-0.050	-0.018	14.071	-0.007	-0.007	0.000	0.000	0.000	0.000
43	A	44	GLU	-1	-0.831	-0.920	11.382	-0.261	-0.261	0.000	0.000	0.000	0.000
44	A	45	ASN	0	-0.096	-0.052	14.510	-0.040	-0.040	0.000	0.000	0.000	0.000
45	A	46	ASN	0	-0.035	-0.017	17.728	0.027	0.027	0.000	0.000	0.000	0.000
46	A	47	LEU	0	0.024	0.024	19.568	0.007	0.007	0.000	0.000	0.000	0.000
47	A	48	LYS	1	0.903	0.949	22.461	0.024	0.024	0.000	0.000	0.000	0.000
48	A	49	GLU	-1	-0.864	-0.943	24.599	-0.022	-0.022	0.000	0.000	0.000	0.000
49	A	50	ILE	0	-0.017	-0.010	22.836	0.008	0.008	0.000	0.000	0.000	0.000
50	A	51	THR	0	0.003	-0.011	20.536	0.009	0.009	0.000	0.000	0.000	0.000
51	A	52	ASN	0	0.002	0.006	23.887	0.009	0.009	0.000	0.000	0.000	0.000
52	A	53	ASN	0	-0.056	-0.013	27.223	-0.001	-0.001	0.000	0.000	0.000	0.000
53	A	54	VAL	0	-0.005	0.011	23.077	0.004	0.004	0.000	0.000	0.000	0.000
54	A	55	LYS	1	0.953	0.968	26.433	-0.050	-0.050	0.000	0.000	0.000	0.000
55	A	56	ASN	0	-0.024	-0.011	27.817	0.000	0.000	0.000	0.000	0.000	0.000
56	A	57	LYS	1	1.003	0.997	24.878	-0.095	-0.095	0.000	0.000	0.000	0.000
57	A	58	GLY	0	0.001	0.010	22.681	-0.003	-0.003	0.000	0.000	0.000	0.000
58	A	59	ARG	1	0.796	0.879	22.013	-0.118	-0.118	0.000	0.000	0.000	0.000
59	A	60	TRP	0	0.005	0.004	19.654	-0.010	-0.010	0.000	0.000	0.000	0.000
60	A	61	LYS	1	0.868	0.918	24.560	-0.042	-0.042	0.000	0.000	0.000	0.000
61	A	62	SER	0	0.097	0.045	27.054	-0.003	-0.003	0.000	0.000	0.000	0.000
62	A	63	GLU	-1	-0.793	-0.894	27.838	0.038	0.038	0.000	0.000	0.000	0.000
63	A	64	ASN	0	-0.034	-0.013	25.864	-0.012	-0.012	0.000	0.000	0.000	0.000
64	A	65	LEU	0	0.070	0.052	21.531	-0.008	-0.008	0.000	0.000	0.000	0.000
65	A	66	PHE	0	0.008	0.018	24.678	-0.009	-0.009	0.000	0.000	0.000	0.000
66	A	67	LYS	1	0.815	0.919	27.274	-0.028	-0.028	0.000	0.000	0.000	0.000
67	A	68	ALA	0	0.062	0.029	21.903	-0.008	-0.008	0.000	0.000	0.000	0.000
68	A	69	SER	0	0.023	0.003	23.200	-0.013	-0.013	0.000	0.000	0.000	0.000
69	A	70	LYS	1	0.857	0.923	24.166	-0.013	-0.013	0.000	0.000	0.000	0.000
70	A	71	LEU	0	-0.019	-0.012	25.416	-0.006	-0.006	0.000	0.000	0.000	0.000
71	A	72	LEU	0	0.040	0.018	19.410	-0.010	-0.010	0.000	0.000	0.000	0.000
72	A	73	ARG	1	0.888	0.957	22.605	0.028	0.028	0.000	0.000	0.000	0.000
73	A	74	SER	0	-0.030	-0.022	24.979	-0.003	-0.003	0.000	0.000	0.000	0.000
74	A	75	ASN	0	-0.045	-0.005	17.187	0.004	0.004	0.000	0.000	0.000	0.000
75	A	76	ASN	0	0.071	0.027	18.631	0.001	0.001	0.000	0.000	0.000	0.000
76	A	77	THR	0	0.024	0.002	21.679	0.013	0.013	0.000	0.000	0.000	0.000
77	A	78	GLU	-1	-0.828	-0.912	22.138	-0.041	-0.041	0.000	0.000	0.000	0.000
78	A	79	ILE	0	0.063	0.047	19.109	0.014	0.014	0.000	0.000	0.000	0.000
79	A	80	PRO	0	-0.025	-0.013	22.305	0.013	0.013	0.000	0.000	0.000	0.000
80	A	81	ILE	0	-0.087	-0.047	25.520	0.005	0.005	0.000	0.000	0.000	0.000
81	A	82	LEU	0	0.079	0.038	20.115	0.004	0.004	0.000	0.000	0.000	0.000
82	A	83	TRP	0	0.029	0.003	21.833	0.012	0.012	0.000	0.000	0.000	0.000
83	A	84	LYS	1	0.816	0.903	24.203	0.000	0.000	0.000	0.000	0.000	0.000
84	A	85	SER	0	0.014	-0.014	24.968	0.002	0.002	0.000	0.000	0.000	0.000
85	A	86	ALA	0	0.033	0.020	22.744	0.006	0.006	0.000	0.000	0.000	0.000
86	A	87	TRP	0	-0.049	-0.027	24.704	0.006	0.006	0.000	0.000	0.000	0.000
87	A	88	THR	0	-0.016	-0.023	27.884	0.001	0.001	0.000	0.000	0.000	0.000
88	A	89	LEU	0	-0.016	-0.012	24.173	0.002	0.002	0.000	0.000	0.000	0.000
89	A	90	HIS	0	-0.005	0.003	26.910	0.006	0.006	0.000	0.000	0.000	0.000
90	A	91	VAL	0	-0.020	-0.016	28.447	0.000	0.000	0.000	0.000	0.000	0.000
91	A	92	GLU	-1	-0.790	-0.880	32.223	0.034	0.034	0.000	0.000	0.000	0.000
92	A	93	GLY	0	-0.010	-0.020	30.020	0.000	0.000	0.000	0.000	0.000	0.000
93	A	94	PHE	0	-0.079	-0.044	28.629	0.003	0.003	0.000	0.000	0.000	0.000
94	A	95	HIS	0	-0.069	-0.043	30.509	-0.002	-0.002	0.000	0.000	0.000	0.000
95	A	96	GLU	-1	-0.925	-0.951	33.866	0.034	0.034	0.000	0.000	0.000	0.000
96	A	97	LEU	0	-0.081	-0.025	33.472	-0.002	-0.002	0.000	0.000	0.000	0.000
97	A	98	SER	0	-0.018	-0.020	35.274	-0.002	-0.002	0.000	0.000	0.000	0.000
98	A	99	LEU	0	-0.035	-0.002	30.592	-0.003	-0.003	0.000	0.000	0.000	0.000
99	A	100	ASN	0	0.035	0.012	33.818	0.003	0.003	0.000	0.000	0.000	0.000
100	A	101	GLU	-1	-0.757	-0.870	29.352	0.039	0.039	0.000	0.000	0.000	0.000
101	A	102	LYS	1	0.854	0.913	29.607	-0.028	-0.028	0.000	0.000	0.000	0.000
102	A	103	GLU	-1	-0.861	-0.929	30.339	0.024	0.024	0.000	0.000	0.000	0.000
103	A	104	VAL	0	0.056	0.020	26.350	0.001	0.001	0.000	0.000	0.000	0.000
104	A	105	LYS	1	0.895	0.930	25.504	-0.041	-0.041	0.000	0.000	0.000	0.000
105	A	106	LYS	1	0.837	0.914	25.266	-0.020	-0.020	0.000	0.000	0.000	0.000
106	A	107	LEU	0	0.003	0.012	26.118	-0.003	-0.003	0.000	0.000	0.000	0.000
107	A	108	LYS	1	0.816	0.899	20.087	-0.076	-0.076	0.000	0.000	0.000	0.000
108	A	109	GLU	-1	-0.832	-0.901	20.183	0.067	0.067	0.000	0.000	0.000	0.000
109	A	110	ASP	-1	-0.862	-0.896	20.556	0.019	0.019	0.000	0.000	0.000	0.000
110	A	111	VAL	0	-0.017	-0.017	18.312	0.001	0.001	0.000	0.000	0.000	0.000
111	A	112	ARG	1	0.935	0.981	13.699	-0.111	-0.111	0.000	0.000	0.000	0.000
112	A	113	LYS	1	0.821	0.900	15.709	0.055	0.055	0.000	0.000	0.000	0.000
113	A	114	LEU	0	-0.018	-0.014	16.408	-0.016	-0.016	0.000	0.000	0.000	0.000
114	A	115	VAL	0	0.022	0.005	12.095	-0.004	-0.004	0.000	0.000	0.000	0.000
115	A	116	ILE	0	-0.004	0.002	11.450	0.041	0.041	0.000	0.000	0.000	0.000
116	A	117	PHE	0	-0.044	-0.019	11.750	-0.062	-0.062	0.000	0.000	0.000	0.000
117	A	118	ALA	0	-0.006	0.003	12.694	-0.057	-0.057	0.000	0.000	0.000	0.000
118	A	119	VAL	0	0.030	0.028	6.404	-0.090	-0.090	0.000	0.000	0.000	0.000
119	A	120	ASN	0	-0.025	-0.027	8.002	-0.197	-0.197	0.000	0.000	0.000	0.000
120	A	121	SER	0	-0.105	-0.056	9.903	-0.106	-0.106	0.000	0.000	0.000	0.000
121	A	122	LEU	0	0.011	0.029	6.115	0.032	0.032	0.000	0.000	0.000	0.000
122	A	123	GLU	-1	-1.018	-1.006	2.494	-16.774	-13.353	1.004	-2.310	-2.115	-0.028

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