FMO DATABASE

FMODB ID: 2NQ6R

Calculation Name: 4GMQ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4GMQ

Chain ID: A

ChEMBL ID:

UniProt ID: G0RYD6

Base Structure: X-ray

Registration Date: 2023-09-23

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	92
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-600804.247032
FMO2-HF: Nuclear repulsion	567361.684138
FMO2-HF: Total energy	-33442.562894
FMO2-MP2: Total energy	-33542.958959

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:355:ASN)

Summations of interaction energy for fragment #1(A:355:ASN)

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.
-41.693	-38.491	12.332	-5.867	-9.668	0.049

Interaction energy analysis for fragmet #1(A:355:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.041 / 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

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	357	VAL	0	0.111	0.061	2.464	0.464	2.567	2.734	-1.689	-3.149	0.011
4	A	358	LYS	1	0.914	0.961	2.052	-23.668	-23.331	9.576	-3.975	-5.938	0.037
5	A	359	LYS	1	0.944	0.957	3.870	-8.097	-7.335	0.022	-0.203	-0.581	0.001
6	A	360	ASN	0	0.062	0.034	5.920	-1.011	-1.011	0.000	0.000	0.000	0.000
7	A	361	LYS	1	0.990	1.001	5.668	-3.773	-3.773	0.000	0.000	0.000	0.000
8	A	362	ARG	1	0.895	0.952	7.210	-4.907	-4.907	0.000	0.000	0.000	0.000
9	A	363	VAL	0	0.026	0.028	9.951	-0.375	-0.375	0.000	0.000	0.000	0.000
10	A	364	LEU	0	0.011	0.021	11.216	-0.237	-0.237	0.000	0.000	0.000	0.000
11	A	365	ARG	1	0.828	0.883	10.478	-1.798	-1.798	0.000	0.000	0.000	0.000
12	A	366	GLY	0	-0.010	-0.002	13.872	-0.161	-0.161	0.000	0.000	0.000	0.000
13	A	367	SER	0	0.010	0.004	15.648	-0.189	-0.189	0.000	0.000	0.000	0.000
14	A	368	VAL	0	0.050	0.018	17.971	-0.105	-0.105	0.000	0.000	0.000	0.000
15	A	369	LYS	1	0.917	0.968	18.982	-0.931	-0.931	0.000	0.000	0.000	0.000
16	A	370	GLU	-1	-0.936	-0.961	19.739	0.749	0.749	0.000	0.000	0.000	0.000
17	A	371	ALA	0	-0.025	-0.007	21.535	-0.068	-0.068	0.000	0.000	0.000	0.000
18	A	372	ASN	0	-0.049	-0.033	23.899	-0.026	-0.026	0.000	0.000	0.000	0.000
19	A	373	TYR	0	-0.020	-0.037	20.414	-0.027	-0.027	0.000	0.000	0.000	0.000
20	A	374	PHE	0	-0.036	-0.032	22.129	-0.030	-0.030	0.000	0.000	0.000	0.000
21	A	375	VAL	0	-0.030	0.001	27.409	-0.040	-0.040	0.000	0.000	0.000	0.000
22	A	376	GLU	-1	-0.876	-0.931	30.204	0.352	0.352	0.000	0.000	0.000	0.000
23	A	377	GLY	0	-0.039	-0.018	32.888	-0.006	-0.006	0.000	0.000	0.000	0.000
24	A	378	GLU	-1	-0.954	-0.972	30.266	0.409	0.409	0.000	0.000	0.000	0.000
25	A	379	ALA	0	0.010	0.012	27.091	-0.018	-0.018	0.000	0.000	0.000	0.000
26	A	380	SER	0	0.031	0.010	28.955	0.006	0.006	0.000	0.000	0.000	0.000
27	A	381	ALA	0	0.062	0.007	27.316	0.027	0.027	0.000	0.000	0.000	0.000
28	A	382	ALA	0	0.015	0.011	27.062	0.021	0.021	0.000	0.000	0.000	0.000
29	A	383	THR	0	0.010	0.010	27.192	-0.002	-0.002	0.000	0.000	0.000	0.000
30	A	384	ILE	0	0.016	0.005	22.448	0.028	0.028	0.000	0.000	0.000	0.000
31	A	385	ASP	-1	-0.894	-0.941	22.928	0.470	0.470	0.000	0.000	0.000	0.000
32	A	386	ALA	0	-0.003	-0.007	23.147	0.014	0.014	0.000	0.000	0.000	0.000
33	A	387	VAL	0	0.005	-0.003	21.363	0.005	0.005	0.000	0.000	0.000	0.000
34	A	388	LEU	0	0.000	-0.009	17.456	0.059	0.059	0.000	0.000	0.000	0.000
35	A	389	ASN	0	-0.042	-0.014	18.513	0.066	0.066	0.000	0.000	0.000	0.000
36	A	390	ASP	-1	-0.769	-0.860	19.839	0.370	0.370	0.000	0.000	0.000	0.000
37	A	391	VAL	0	-0.014	-0.011	15.167	0.012	0.012	0.000	0.000	0.000	0.000
38	A	392	ASP	-1	-0.810	-0.889	14.953	1.171	1.171	0.000	0.000	0.000	0.000
39	A	393	LEU	0	-0.010	0.008	15.579	-0.036	-0.036	0.000	0.000	0.000	0.000
40	A	394	VAL	0	0.056	0.027	16.006	-0.064	-0.064	0.000	0.000	0.000	0.000
41	A	395	ILE	0	-0.029	-0.020	10.739	0.051	0.051	0.000	0.000	0.000	0.000
42	A	396	THR	0	-0.127	-0.069	12.574	-0.100	-0.100	0.000	0.000	0.000	0.000
43	A	397	LYS	1	0.900	0.964	14.209	-0.262	-0.262	0.000	0.000	0.000	0.000
44	A	398	ILE	0	-0.050	-0.011	12.386	-0.076	-0.076	0.000	0.000	0.000	0.000
45	A	399	ASP	-1	-0.823	-0.904	10.403	-0.282	-0.282	0.000	0.000	0.000	0.000
46	A	400	ALA	0	-0.044	-0.055	6.434	0.320	0.320	0.000	0.000	0.000	0.000
47	A	401	ASP	-1	-0.885	-0.934	8.214	-0.359	-0.359	0.000	0.000	0.000	0.000
48	A	402	GLU	-1	-0.744	-0.865	11.314	0.226	0.226	0.000	0.000	0.000	0.000
49	A	403	ILE	0	-0.037	-0.023	7.858	0.394	0.394	0.000	0.000	0.000	0.000
50	A	404	ALA	0	-0.034	-0.025	9.222	0.264	0.264	0.000	0.000	0.000	0.000
51	A	405	ALA	0	0.011	0.009	10.560	0.028	0.028	0.000	0.000	0.000	0.000
52	A	406	LEU	0	-0.018	0.000	13.720	0.010	0.010	0.000	0.000	0.000	0.000
53	A	407	ALA	0	0.017	-0.010	11.096	0.036	0.036	0.000	0.000	0.000	0.000
54	A	408	GLY	0	-0.033	-0.020	13.118	-0.011	-0.011	0.000	0.000	0.000	0.000
55	A	409	LYS	1	0.909	0.957	15.218	-0.472	-0.472	0.000	0.000	0.000	0.000
56	A	410	LEU	0	0.018	0.011	15.463	-0.020	-0.020	0.000	0.000	0.000	0.000
57	A	411	ASN	0	-0.082	-0.046	13.463	0.006	0.006	0.000	0.000	0.000	0.000
58	A	412	GLY	0	0.009	0.011	16.786	-0.094	-0.094	0.000	0.000	0.000	0.000
59	A	413	LEU	0	-0.018	0.014	19.646	-0.063	-0.063	0.000	0.000	0.000	0.000
60	A	414	THR	0	0.022	-0.003	21.645	0.041	0.041	0.000	0.000	0.000	0.000
61	A	415	VAL	0	0.008	0.021	24.356	-0.011	-0.011	0.000	0.000	0.000	0.000
62	A	416	ALA	0	0.074	0.028	25.389	0.017	0.017	0.000	0.000	0.000	0.000
63	A	417	ASP	-1	-0.864	-0.942	25.829	0.359	0.359	0.000	0.000	0.000	0.000
64	A	418	GLU	-1	-0.986	-0.989	24.894	0.408	0.408	0.000	0.000	0.000	0.000
65	A	419	ILE	0	0.000	-0.007	20.471	0.009	0.009	0.000	0.000	0.000	0.000
66	A	420	LYS	1	0.851	0.932	22.313	-0.367	-0.367	0.000	0.000	0.000	0.000
67	A	421	ASN	0	-0.027	-0.025	24.461	-0.022	-0.022	0.000	0.000	0.000	0.000
68	A	422	VAL	0	0.011	0.022	19.386	-0.026	-0.026	0.000	0.000	0.000	0.000
69	A	423	TRP	0	0.004	-0.020	15.119	-0.004	-0.004	0.000	0.000	0.000	0.000
70	A	424	LYS	1	0.913	0.966	21.332	-0.341	-0.341	0.000	0.000	0.000	0.000
71	A	425	GLU	-1	-0.930	-0.939	22.828	0.187	0.187	0.000	0.000	0.000	0.000
72	A	426	GLU	-1	-0.795	-0.873	16.990	0.341	0.341	0.000	0.000	0.000	0.000
73	A	427	VAL	0	-0.006	-0.016	20.904	-0.039	-0.039	0.000	0.000	0.000	0.000
74	A	428	SER	0	-0.011	-0.009	22.705	-0.046	-0.046	0.000	0.000	0.000	0.000
75	A	429	ARG	1	0.725	0.828	17.045	-0.226	-0.226	0.000	0.000	0.000	0.000
76	A	430	LEU	0	-0.028	-0.027	18.081	-0.047	-0.047	0.000	0.000	0.000	0.000
77	A	431	VAL	0	-0.006	-0.003	22.181	-0.037	-0.037	0.000	0.000	0.000	0.000
78	A	432	GLY	0	0.002	0.009	25.672	-0.026	-0.026	0.000	0.000	0.000	0.000
79	A	433	ALA	0	-0.055	-0.019	22.434	-0.026	-0.026	0.000	0.000	0.000	0.000
80	A	434	GLY	0	-0.005	0.004	24.229	-0.032	-0.032	0.000	0.000	0.000	0.000
81	A	435	LYS	1	0.775	0.880	16.420	0.022	0.022	0.000	0.000	0.000	0.000
82	A	436	LEU	0	-0.043	-0.018	20.609	0.019	0.019	0.000	0.000	0.000	0.000
83	A	437	LYS	1	0.882	0.927	23.823	-0.038	-0.038	0.000	0.000	0.000	0.000
84	A	438	GLU	-1	-0.915	-0.960	27.300	0.119	0.119	0.000	0.000	0.000	0.000
85	A	439	GLY	0	-0.009	-0.003	28.927	0.018	0.018	0.000	0.000	0.000	0.000
86	A	440	ASP	-1	-0.895	-0.935	24.344	0.148	0.148	0.000	0.000	0.000	0.000
87	A	441	ILE	0	-0.072	-0.029	21.304	0.035	0.035	0.000	0.000	0.000	0.000
88	A	442	LYS	1	0.895	0.943	24.686	-0.379	-0.379	0.000	0.000	0.000	0.000
89	A	443	ALA	0	-0.002	-0.011	25.926	-0.003	-0.003	0.000	0.000	0.000	0.000
90	A	444	LEU	0	-0.035	-0.025	20.061	0.001	0.001	0.000	0.000	0.000	0.000
91	A	445	VAL	0	0.029	0.005	24.462	0.015	0.015	0.000	0.000	0.000	0.000
92	A	446	ALA	0	-0.012	0.012	26.859	-0.012	-0.012	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:355:ASN)