FMO DATABASE

FMODB ID: 7G75K

Calculation Name: 2R39-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2R39

Chain ID: A

ChEMBL ID:

UniProt ID: Q87KC5

Base Structure: X-ray

Registration Date: 2023-06-20

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	111
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-864279.747817
FMO2-HF: Nuclear repulsion	820713.852623
FMO2-HF: Total energy	-43565.895194
FMO2-MP2: Total energy	-43694.26291

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:377:VAL)

Summations of interaction energy for fragment #1(A:377:VAL)

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.
-4.636	-0.788	0.521	-1.775	-2.595	-0.003

Interaction energy analysis for fragmet #1(A:377:VAL)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.008 / q_NPA : -0.010

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	379	PRO	0	0.013	0.022	2.817	-2.492	0.405	0.363	-1.560	-1.700	-0.004
4	A	380	ALA	0	0.044	0.027	5.092	0.697	0.790	-0.001	-0.002	-0.090	0.000
5	A	381	GLY	0	0.011	-0.019	6.128	-0.187	-0.187	0.000	0.000	0.000	0.000
6	A	382	MET	0	-0.028	-0.001	8.320	0.059	0.059	0.000	0.000	0.000	0.000
7	A	383	SER	0	-0.046	-0.013	11.893	0.076	0.076	0.000	0.000	0.000	0.000
8	A	384	VAL	0	0.029	0.004	14.328	-0.023	-0.023	0.000	0.000	0.000	0.000
9	A	385	ILE	0	-0.019	0.000	18.166	0.030	0.030	0.000	0.000	0.000	0.000
10	A	386	ARG	1	0.904	0.954	20.953	0.030	0.030	0.000	0.000	0.000	0.000
11	A	387	ASP	-1	-0.850	-0.886	24.206	-0.026	-0.026	0.000	0.000	0.000	0.000
12	A	388	ARG	1	0.971	0.970	26.872	-0.031	-0.031	0.000	0.000	0.000	0.000
13	A	389	ASN	0	-0.044	-0.025	29.298	0.001	0.001	0.000	0.000	0.000	0.000
14	A	390	GLN	0	-0.021	-0.009	28.336	-0.009	-0.009	0.000	0.000	0.000	0.000
15	A	391	LEU	0	0.015	0.003	32.691	0.002	0.002	0.000	0.000	0.000	0.000
16	A	392	PHE	0	-0.035	-0.026	34.625	0.001	0.001	0.000	0.000	0.000	0.000
17	A	393	ARG	1	0.925	0.976	35.710	0.048	0.048	0.000	0.000	0.000	0.000
18	A	394	VAL	0	0.010	-0.004	37.449	-0.004	-0.004	0.000	0.000	0.000	0.000
19	A	395	ASN	0	-0.038	0.006	34.921	-0.001	-0.001	0.000	0.000	0.000	0.000
20	A	396	SER	0	-0.037	-0.026	37.065	0.001	0.001	0.000	0.000	0.000	0.000
21	A	397	ALA	0	0.009	0.018	38.248	0.001	0.001	0.000	0.000	0.000	0.000
22	A	398	GLY	0	0.013	-0.007	40.259	0.004	0.004	0.000	0.000	0.000	0.000
23	A	399	GLU	-1	-0.808	-0.852	35.486	-0.085	-0.085	0.000	0.000	0.000	0.000
24	A	400	VAL	0	-0.032	-0.017	35.592	0.005	0.005	0.000	0.000	0.000	0.000
25	A	401	GLU	-1	-0.791	-0.897	32.282	-0.071	-0.071	0.000	0.000	0.000	0.000
26	A	402	ASN	0	-0.074	-0.034	29.015	0.010	0.010	0.000	0.000	0.000	0.000
27	A	403	THR	0	-0.014	-0.037	28.351	-0.008	-0.008	0.000	0.000	0.000	0.000
28	A	404	TYR	0	-0.003	-0.039	22.971	0.006	0.006	0.000	0.000	0.000	0.000
29	A	405	THR	0	0.012	0.011	20.216	-0.005	-0.005	0.000	0.000	0.000	0.000
30	A	406	LEU	0	0.018	0.021	17.736	0.011	0.011	0.000	0.000	0.000	0.000
31	A	407	LYS	1	0.907	0.955	14.046	0.012	0.012	0.000	0.000	0.000	0.000
32	A	408	VAL	0	0.020	0.005	12.114	-0.006	-0.006	0.000	0.000	0.000	0.000
33	A	409	ILE	0	-0.032	-0.006	7.709	0.095	0.095	0.000	0.000	0.000	0.000
34	A	410	ASN	0	0.037	0.030	8.523	-0.391	-0.391	0.000	0.000	0.000	0.000
35	A	411	LYS	1	0.745	0.852	2.709	0.970	1.727	0.160	-0.198	-0.719	0.001
36	A	412	THR	0	0.002	0.008	4.417	-0.612	-0.511	-0.001	-0.015	-0.086	0.000
37	A	413	GLN	0	-0.024	-0.030	7.138	0.198	0.198	0.000	0.000	0.000	0.000
38	A	414	GLN	0	-0.016	-0.010	10.422	0.052	0.052	0.000	0.000	0.000	0.000
39	A	415	VAL	0	0.032	0.028	11.730	-0.071	-0.071	0.000	0.000	0.000	0.000
40	A	416	GLN	0	-0.014	0.003	9.890	-0.020	-0.020	0.000	0.000	0.000	0.000
41	A	417	GLU	-1	-0.849	-0.921	13.393	-0.303	-0.303	0.000	0.000	0.000	0.000
42	A	418	TYR	0	-0.012	-0.011	9.264	-0.006	-0.006	0.000	0.000	0.000	0.000
43	A	419	ASN	0	-0.010	-0.008	15.534	0.070	0.070	0.000	0.000	0.000	0.000
44	A	420	LEU	0	-0.048	-0.027	15.958	-0.042	-0.042	0.000	0.000	0.000	0.000
45	A	421	ASP	-1	-0.783	-0.870	19.147	-0.274	-0.274	0.000	0.000	0.000	0.000
46	A	422	VAL	0	-0.012	-0.025	20.959	0.000	0.000	0.000	0.000	0.000	0.000
47	A	423	LYS	1	0.826	0.929	19.196	0.297	0.297	0.000	0.000	0.000	0.000
48	A	424	GLY	0	0.025	-0.009	24.552	0.007	0.007	0.000	0.000	0.000	0.000
49	A	425	LEU	0	-0.032	-0.015	27.106	0.015	0.015	0.000	0.000	0.000	0.000
50	A	426	ASN	0	-0.033	-0.025	30.300	-0.012	-0.012	0.000	0.000	0.000	0.000
51	A	427	ASP	-1	-0.866	-0.932	33.319	-0.089	-0.089	0.000	0.000	0.000	0.000
52	A	428	VAL	0	-0.029	-0.030	28.910	0.002	0.002	0.000	0.000	0.000	0.000
53	A	429	SER	0	-0.017	-0.004	32.108	-0.008	-0.008	0.000	0.000	0.000	0.000
54	A	430	TRP	0	-0.009	-0.027	21.618	0.006	0.006	0.000	0.000	0.000	0.000
55	A	431	TYR	0	-0.063	-0.053	28.451	-0.002	-0.002	0.000	0.000	0.000	0.000
56	A	432	GLY	0	0.062	0.010	25.373	0.009	0.009	0.000	0.000	0.000	0.000
57	A	433	LYS	1	0.909	0.957	21.671	0.201	0.201	0.000	0.000	0.000	0.000
58	A	434	GLN	0	-0.003	0.012	22.348	0.015	0.015	0.000	0.000	0.000	0.000
59	A	435	THR	0	0.022	-0.002	20.000	-0.015	-0.015	0.000	0.000	0.000	0.000
60	A	436	ILE	0	-0.107	-0.052	15.523	0.046	0.046	0.000	0.000	0.000	0.000
61	A	437	GLN	0	-0.031	-0.022	16.851	-0.025	-0.025	0.000	0.000	0.000	0.000
62	A	438	VAL	0	-0.023	-0.009	12.621	0.043	0.043	0.000	0.000	0.000	0.000
63	A	439	GLU	-1	-0.823	-0.925	13.717	-0.401	-0.401	0.000	0.000	0.000	0.000
64	A	440	PRO	0	-0.027	-0.015	11.047	-0.049	-0.049	0.000	0.000	0.000	0.000
65	A	441	GLY	0	-0.022	0.002	9.158	0.095	0.095	0.000	0.000	0.000	0.000
66	A	442	GLU	-1	-0.902	-0.938	10.172	-0.175	-0.175	0.000	0.000	0.000	0.000
67	A	443	VAL	0	-0.026	-0.028	11.517	-0.048	-0.048	0.000	0.000	0.000	0.000
68	A	444	LEU	0	0.005	0.015	13.696	0.034	0.034	0.000	0.000	0.000	0.000
69	A	445	ASN	0	-0.032	-0.041	16.109	0.015	0.015	0.000	0.000	0.000	0.000
70	A	446	LEU	0	-0.005	-0.006	17.932	0.006	0.006	0.000	0.000	0.000	0.000
71	A	447	PRO	0	-0.020	0.003	21.125	-0.001	-0.001	0.000	0.000	0.000	0.000
72	A	448	MET	0	-0.039	-0.010	23.335	-0.015	-0.015	0.000	0.000	0.000	0.000
73	A	449	SER	0	-0.059	-0.057	26.074	0.011	0.011	0.000	0.000	0.000	0.000
74	A	450	LEU	0	-0.006	0.015	25.650	-0.011	-0.011	0.000	0.000	0.000	0.000
75	A	451	GLY	0	0.019	0.014	29.466	0.012	0.012	0.000	0.000	0.000	0.000
76	A	452	ALA	0	0.035	0.014	32.792	-0.008	-0.008	0.000	0.000	0.000	0.000
77	A	453	ASP	-1	-0.757	-0.873	34.951	-0.056	-0.056	0.000	0.000	0.000	0.000
78	A	454	PRO	0	-0.011	-0.018	38.103	0.000	0.000	0.000	0.000	0.000	0.000
79	A	455	ASP	-1	-0.900	-0.940	39.653	-0.045	-0.045	0.000	0.000	0.000	0.000
80	A	456	LYS	1	0.800	0.895	37.829	0.068	0.068	0.000	0.000	0.000	0.000
81	A	457	LEU	0	-0.040	-0.006	33.499	-0.003	-0.003	0.000	0.000	0.000	0.000
82	A	458	ASN	0	0.023	0.006	33.080	0.008	0.008	0.000	0.000	0.000	0.000
83	A	459	SER	0	-0.004	-0.001	34.535	0.008	0.008	0.000	0.000	0.000	0.000
84	A	460	ALA	0	0.002	0.000	36.367	-0.003	-0.003	0.000	0.000	0.000	0.000
85	A	461	ILE	0	0.003	0.008	30.606	-0.001	-0.001	0.000	0.000	0.000	0.000
86	A	462	THR	0	-0.022	-0.010	29.133	-0.002	-0.002	0.000	0.000	0.000	0.000
87	A	463	THR	0	-0.013	-0.005	24.302	0.004	0.004	0.000	0.000	0.000	0.000
88	A	464	ILE	0	0.003	0.017	23.755	-0.005	-0.005	0.000	0.000	0.000	0.000
89	A	465	GLN	0	0.024	-0.001	19.360	-0.014	-0.014	0.000	0.000	0.000	0.000
90	A	466	PHE	0	0.046	0.023	18.905	-0.004	-0.004	0.000	0.000	0.000	0.000
91	A	467	ILE	0	-0.006	-0.015	16.935	-0.002	-0.002	0.000	0.000	0.000	0.000
92	A	468	LEU	0	-0.012	0.003	11.217	0.031	0.031	0.000	0.000	0.000	0.000
93	A	469	THR	0	0.027	0.000	14.582	-0.057	-0.057	0.000	0.000	0.000	0.000
94	A	470	ASP	-1	-0.811	-0.890	9.964	-1.234	-1.234	0.000	0.000	0.000	0.000
95	A	471	LYS	1	0.942	0.949	13.219	0.371	0.371	0.000	0.000	0.000	0.000
96	A	472	SER	0	-0.039	-0.025	13.179	0.069	0.069	0.000	0.000	0.000	0.000
97	A	473	ASN	0	-0.115	-0.074	9.656	-0.102	-0.102	0.000	0.000	0.000	0.000
98	A	474	GLU	-1	-0.985	-0.974	11.336	-0.863	-0.863	0.000	0.000	0.000	0.000
99	A	475	PHE	0	0.003	-0.001	7.483	-0.239	-0.239	0.000	0.000	0.000	0.000
100	A	476	THR	0	-0.020	-0.023	11.775	0.115	0.115	0.000	0.000	0.000	0.000
101	A	477	ILE	0	-0.035	-0.007	8.901	-0.097	-0.097	0.000	0.000	0.000	0.000
102	A	478	GLU	-1	-0.794	-0.881	12.414	-0.374	-0.374	0.000	0.000	0.000	0.000
103	A	479	VAL	0	-0.046	-0.018	14.020	0.029	0.029	0.000	0.000	0.000	0.000
104	A	480	GLU	-1	-0.861	-0.905	16.393	-0.061	-0.061	0.000	0.000	0.000	0.000
105	A	481	SER	0	0.023	0.005	19.629	0.023	0.023	0.000	0.000	0.000	0.000
106	A	482	ARG	1	0.786	0.862	22.581	0.048	0.048	0.000	0.000	0.000	0.000
107	A	483	PHE	0	0.054	0.052	26.436	0.000	0.000	0.000	0.000	0.000	0.000
108	A	484	ILE	0	-0.041	-0.038	29.354	0.006	0.006	0.000	0.000	0.000	0.000
109	A	485	LYS	1	0.885	0.962	32.586	0.047	0.047	0.000	0.000	0.000	0.000
110	A	486	LYS	1	0.942	0.968	36.174	0.027	0.027	0.000	0.000	0.000	0.000
111	A	487	LEU	0	0.012	0.017	38.390	0.005	0.005	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:377:VAL)