FMO DATABASE

FMODB ID: R9G48

Calculation Name: 2Q9V-A-Xray372

Preferred Name: Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 2Q9V

Chain ID: A

ChEMBL ID: CHEMBL4295927

UniProt ID: Q96QZ7

Base Structure: X-ray

Registration Date: 2023-09-19

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	90
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-607641.823823
FMO2-HF: Nuclear repulsion	573279.509766
FMO2-HF: Total energy	-34362.314056
FMO2-MP2: Total energy	-34463.453384

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:837:SER)

Summations of interaction energy for fragment #1(A:837: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.
-33.929	-26.248	10.483	-8.086	-10.079	-0.006

Interaction energy analysis for fragmet #1(A:837:SER)

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 : 0.001

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	839	GLU	-1	-0.819	-0.885	3.801	-1.908	0.298	-0.012	-1.137	-1.057	-0.001
4	A	840	GLN	0	-0.035	-0.022	6.191	0.284	0.284	0.000	0.000	0.000	0.000
5	A	841	ASP	-1	-0.786	-0.864	8.491	-0.309	-0.309	0.000	0.000	0.000	0.000
6	A	842	ILE	0	-0.047	-0.027	9.869	0.042	0.042	0.000	0.000	0.000	0.000
7	A	843	PHE	0	0.029	0.023	13.673	-0.010	-0.010	0.000	0.000	0.000	0.000
8	A	844	LEU	0	-0.036	-0.013	16.042	-0.001	-0.001	0.000	0.000	0.000	0.000
9	A	845	TRP	0	0.054	0.018	19.401	0.007	0.007	0.000	0.000	0.000	0.000
10	A	846	ARG	1	0.789	0.906	22.747	0.162	0.162	0.000	0.000	0.000	0.000
11	A	847	LYS	1	0.869	0.930	23.648	0.219	0.219	0.000	0.000	0.000	0.000
12	A	848	GLU	-1	-0.876	-0.937	26.535	-0.130	-0.130	0.000	0.000	0.000	0.000
13	A	849	THR	0	-0.009	-0.014	26.684	-0.004	-0.004	0.000	0.000	0.000	0.000
14	A	850	GLY	0	-0.014	-0.001	24.924	-0.016	-0.016	0.000	0.000	0.000	0.000
15	A	851	PHE	0	0.031	-0.008	19.554	-0.001	-0.001	0.000	0.000	0.000	0.000
16	A	852	GLY	0	-0.011	0.008	19.895	-0.017	-0.017	0.000	0.000	0.000	0.000
17	A	853	PHE	0	0.031	0.029	16.240	-0.021	-0.021	0.000	0.000	0.000	0.000
18	A	854	ARG	1	0.855	0.929	17.704	0.399	0.399	0.000	0.000	0.000	0.000
19	A	855	ILE	0	0.017	0.016	14.529	-0.053	-0.053	0.000	0.000	0.000	0.000
20	A	856	LEU	0	-0.001	-0.003	14.366	0.072	0.072	0.000	0.000	0.000	0.000
21	A	857	GLY	0	0.055	0.041	14.141	-0.096	-0.096	0.000	0.000	0.000	0.000
22	A	858	GLY	0	0.032	0.023	14.898	0.050	0.050	0.000	0.000	0.000	0.000
23	A	859	ASN	0	-0.110	-0.083	16.372	0.094	0.094	0.000	0.000	0.000	0.000
24	A	860	GLU	-1	-0.935	-0.964	18.772	-0.254	-0.254	0.000	0.000	0.000	0.000
25	A	861	PRO	0	-0.070	-0.052	18.026	-0.043	-0.043	0.000	0.000	0.000	0.000
26	A	862	GLY	0	0.042	0.027	15.846	0.041	0.041	0.000	0.000	0.000	0.000
27	A	863	GLU	-1	-0.866	-0.898	14.236	-0.607	-0.607	0.000	0.000	0.000	0.000
28	A	864	PRO	0	-0.032	-0.015	9.196	0.045	0.045	0.000	0.000	0.000	0.000
29	A	865	ILE	0	0.009	0.007	10.489	0.083	0.083	0.000	0.000	0.000	0.000
30	A	866	TYR	0	-0.022	-0.025	6.635	-0.044	-0.044	0.000	0.000	0.000	0.000
31	A	867	ILE	0	-0.020	-0.003	10.330	0.246	0.246	0.000	0.000	0.000	0.000
32	A	868	GLY	0	0.054	0.020	12.399	-0.070	-0.070	0.000	0.000	0.000	0.000
33	A	869	HIS	0	-0.008	-0.005	15.144	0.003	0.003	0.000	0.000	0.000	0.000
34	A	870	ILE	0	0.038	0.026	13.465	0.019	0.019	0.000	0.000	0.000	0.000
35	A	871	VAL	0	-0.050	-0.027	17.744	0.024	0.024	0.000	0.000	0.000	0.000
36	A	872	PRO	0	0.037	0.012	21.482	0.006	0.006	0.000	0.000	0.000	0.000
37	A	873	LEU	0	-0.002	0.001	22.793	0.016	0.016	0.000	0.000	0.000	0.000
38	A	874	GLY	0	0.013	0.010	22.286	0.017	0.017	0.000	0.000	0.000	0.000
39	A	875	ALA	0	-0.039	-0.015	20.955	0.007	0.007	0.000	0.000	0.000	0.000
40	A	876	ALA	0	0.032	0.007	15.943	0.008	0.008	0.000	0.000	0.000	0.000
41	A	877	ASP	-1	-0.847	-0.922	16.980	-0.295	-0.295	0.000	0.000	0.000	0.000
42	A	878	THR	0	-0.050	-0.034	18.890	0.018	0.018	0.000	0.000	0.000	0.000
43	A	879	ASP	-1	-0.805	-0.870	15.650	-0.302	-0.302	0.000	0.000	0.000	0.000
44	A	880	GLY	0	0.006	0.012	16.177	0.020	0.020	0.000	0.000	0.000	0.000
45	A	881	ARG	1	0.767	0.869	11.986	0.262	0.262	0.000	0.000	0.000	0.000
46	A	882	LEU	0	-0.002	0.010	10.601	-0.140	-0.140	0.000	0.000	0.000	0.000
47	A	883	ARG	1	0.887	0.908	6.190	1.779	1.779	0.000	0.000	0.000	0.000
48	A	884	SER	0	-0.049	-0.052	10.402	-0.114	-0.114	0.000	0.000	0.000	0.000
49	A	885	GLY	0	-0.013	-0.004	9.285	0.026	0.026	0.000	0.000	0.000	0.000
50	A	886	ASP	-1	-0.767	-0.851	6.107	-2.490	-2.490	0.000	0.000	0.000	0.000
51	A	887	GLU	-1	-0.866	-0.932	5.329	-2.108	-2.108	0.000	0.000	0.000	0.000
52	A	888	LEU	0	-0.033	-0.016	7.162	0.195	0.195	0.000	0.000	0.000	0.000
53	A	889	ILE	0	-0.003	-0.009	7.534	0.080	0.080	0.000	0.000	0.000	0.000
54	A	890	SER	0	-0.067	-0.064	10.507	0.135	0.135	0.000	0.000	0.000	0.000
55	A	891	VAL	0	0.043	0.024	13.526	-0.063	-0.063	0.000	0.000	0.000	0.000
56	A	892	ASP	-1	-0.809	-0.906	16.383	-0.193	-0.193	0.000	0.000	0.000	0.000
57	A	893	GLY	0	0.004	0.016	16.924	0.030	0.030	0.000	0.000	0.000	0.000
58	A	894	THR	0	-0.023	-0.005	17.823	0.034	0.034	0.000	0.000	0.000	0.000
59	A	895	PRO	0	0.009	-0.016	14.721	-0.049	-0.049	0.000	0.000	0.000	0.000
60	A	896	VAL	0	0.005	0.011	13.081	0.024	0.024	0.000	0.000	0.000	0.000
61	A	897	ILE	0	0.039	0.021	10.270	-0.043	-0.043	0.000	0.000	0.000	0.000
62	A	898	GLY	0	0.020	0.020	12.758	0.079	0.079	0.000	0.000	0.000	0.000
63	A	899	LYS	1	0.799	0.900	14.755	0.307	0.307	0.000	0.000	0.000	0.000
64	A	900	SER	0	0.041	0.005	17.126	-0.046	-0.046	0.000	0.000	0.000	0.000
65	A	901	HIS	0	0.064	0.018	18.356	0.003	0.003	0.000	0.000	0.000	0.000
66	A	902	GLN	0	0.019	0.024	19.264	0.006	0.006	0.000	0.000	0.000	0.000
67	A	903	LEU	0	-0.007	0.007	18.533	0.021	0.021	0.000	0.000	0.000	0.000
68	A	904	VAL	0	0.046	0.020	16.263	0.013	0.013	0.000	0.000	0.000	0.000
69	A	905	VAL	0	-0.016	-0.003	19.269	0.013	0.013	0.000	0.000	0.000	0.000
70	A	906	GLN	0	-0.001	-0.008	22.687	0.019	0.019	0.000	0.000	0.000	0.000
71	A	907	LEU	0	-0.002	0.006	18.922	0.016	0.016	0.000	0.000	0.000	0.000
72	A	908	MET	0	0.010	0.006	18.891	0.003	0.003	0.000	0.000	0.000	0.000
73	A	909	GLN	0	0.006	0.006	21.844	0.012	0.012	0.000	0.000	0.000	0.000
74	A	910	GLN	0	-0.029	-0.020	24.528	0.021	0.021	0.000	0.000	0.000	0.000
75	A	911	ALA	0	0.049	0.017	21.717	0.013	0.013	0.000	0.000	0.000	0.000
76	A	912	ALA	0	-0.076	-0.042	23.783	0.010	0.010	0.000	0.000	0.000	0.000
77	A	913	LYS	1	0.847	0.925	26.142	0.158	0.158	0.000	0.000	0.000	0.000
78	A	914	GLN	0	-0.056	-0.021	23.166	0.025	0.025	0.000	0.000	0.000	0.000
79	A	915	GLY	0	0.016	0.015	26.924	0.008	0.008	0.000	0.000	0.000	0.000
80	A	916	HIS	0	-0.034	-0.018	22.868	-0.012	-0.012	0.000	0.000	0.000	0.000
81	A	917	VAL	0	0.046	0.022	17.850	-0.003	-0.003	0.000	0.000	0.000	0.000
82	A	918	ASN	0	-0.042	-0.039	15.724	-0.012	-0.012	0.000	0.000	0.000	0.000
83	A	919	LEU	0	-0.004	-0.001	12.807	0.000	0.000	0.000	0.000	0.000	0.000
84	A	920	THR	0	0.028	0.021	9.802	-0.025	-0.025	0.000	0.000	0.000	0.000
85	A	921	VAL	0	-0.002	-0.014	7.161	-0.044	-0.044	0.000	0.000	0.000	0.000
86	A	922	ARG	1	0.817	0.905	2.357	-7.622	-4.925	1.793	-1.739	-2.750	0.017
87	A	923	GLN	0	-0.033	-0.034	3.183	-1.707	-0.744	0.146	-0.408	-0.701	-0.004
88	A	924	THR	0	-0.018	-0.027	2.444	-5.614	-3.449	4.038	-3.204	-2.999	-0.035
89	A	925	ARG	1	0.906	0.961	2.241	-14.604	-14.980	4.519	-1.595	-2.549	0.017
90	A	926	LEU	0	0.025	0.019	5.136	-0.033	-0.007	-0.001	-0.003	-0.023	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:837:SER)