FMO DATABASE

FMODB ID: 6NV5Z

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

Total energy (hartree)

FMO2-HF: Electronic energy	-606236.011718
FMO2-HF: Nuclear repulsion	571874.10418
FMO2-HF: Total energy	-34361.907538
FMO2-MP2: Total energy	-34463.083512

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.
-28.158	-21.857	13.401	-8.963	-10.736	-0.02

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 : -0.027 / q_NPA : -0.020

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	-0.868	-0.931	3.814	-2.372	0.146	-0.022	-1.278	-1.219	-0.002
4	A	840	GLN	0	-0.032	-0.013	6.294	0.135	0.135	0.000	0.000	0.000	0.000
5	A	841	ASP	-1	-0.791	-0.887	8.432	-0.240	-0.240	0.000	0.000	0.000	0.000
6	A	842	ILE	0	-0.082	-0.046	9.737	0.014	0.014	0.000	0.000	0.000	0.000
7	A	843	PHE	0	0.008	0.008	13.331	-0.004	-0.004	0.000	0.000	0.000	0.000
8	A	844	LEU	0	-0.035	-0.019	15.988	-0.001	-0.001	0.000	0.000	0.000	0.000
9	A	845	TRP	0	0.048	0.022	19.067	0.008	0.008	0.000	0.000	0.000	0.000
10	A	846	ARG	1	0.868	0.954	22.667	0.166	0.166	0.000	0.000	0.000	0.000
11	A	847	LYS	1	0.923	0.970	23.372	0.205	0.205	0.000	0.000	0.000	0.000
12	A	848	GLU	-1	-0.912	-0.961	26.342	-0.120	-0.120	0.000	0.000	0.000	0.000
13	A	849	THR	0	-0.025	-0.017	25.888	-0.002	-0.002	0.000	0.000	0.000	0.000
14	A	850	GLY	0	-0.042	-0.015	24.688	-0.014	-0.014	0.000	0.000	0.000	0.000
15	A	851	PHE	0	0.032	-0.001	19.206	0.002	0.002	0.000	0.000	0.000	0.000
16	A	852	GLY	0	-0.007	-0.004	19.656	-0.014	-0.014	0.000	0.000	0.000	0.000
17	A	853	PHE	0	0.036	0.021	15.346	-0.017	-0.017	0.000	0.000	0.000	0.000
18	A	854	ARG	1	0.900	0.952	17.237	0.374	0.374	0.000	0.000	0.000	0.000
19	A	855	ILE	0	0.006	0.015	14.120	-0.061	-0.061	0.000	0.000	0.000	0.000
20	A	856	LEU	0	-0.022	-0.012	13.917	0.073	0.073	0.000	0.000	0.000	0.000
21	A	857	GLY	0	0.053	0.036	14.104	-0.076	-0.076	0.000	0.000	0.000	0.000
22	A	858	GLY	0	0.054	0.023	14.978	0.039	0.039	0.000	0.000	0.000	0.000
23	A	859	ASN	0	-0.128	-0.066	16.362	0.076	0.076	0.000	0.000	0.000	0.000
24	A	860	GLU	-1	-0.941	-0.961	18.782	-0.228	-0.228	0.000	0.000	0.000	0.000
25	A	861	PRO	0	-0.044	-0.037	17.968	-0.037	-0.037	0.000	0.000	0.000	0.000
26	A	862	GLY	0	0.005	0.008	15.476	0.025	0.025	0.000	0.000	0.000	0.000
27	A	863	GLU	-1	-0.850	-0.914	14.155	-0.503	-0.503	0.000	0.000	0.000	0.000
28	A	864	PRO	0	-0.007	-0.007	9.328	0.032	0.032	0.000	0.000	0.000	0.000
29	A	865	ILE	0	0.011	0.021	10.880	0.045	0.045	0.000	0.000	0.000	0.000
30	A	866	TYR	0	0.003	-0.002	6.633	0.015	0.015	0.000	0.000	0.000	0.000
31	A	867	ILE	0	-0.005	0.007	9.941	0.263	0.263	0.000	0.000	0.000	0.000
32	A	868	GLY	0	0.032	0.013	12.031	-0.081	-0.081	0.000	0.000	0.000	0.000
33	A	869	HIS	0	-0.011	-0.010	14.615	-0.002	-0.002	0.000	0.000	0.000	0.000
34	A	870	ILE	0	0.055	0.032	12.910	0.009	0.009	0.000	0.000	0.000	0.000
35	A	871	VAL	0	-0.059	-0.031	17.295	0.028	0.028	0.000	0.000	0.000	0.000
36	A	872	PRO	0	0.028	0.010	20.884	0.003	0.003	0.000	0.000	0.000	0.000
37	A	873	LEU	0	-0.009	-0.017	22.087	0.018	0.018	0.000	0.000	0.000	0.000
38	A	874	GLY	0	-0.012	0.001	22.122	0.018	0.018	0.000	0.000	0.000	0.000
39	A	875	ALA	0	-0.065	-0.043	20.650	-0.001	-0.001	0.000	0.000	0.000	0.000
40	A	876	ALA	0	0.040	0.016	15.537	0.006	0.006	0.000	0.000	0.000	0.000
41	A	877	ASP	-1	-0.822	-0.903	16.500	-0.304	-0.304	0.000	0.000	0.000	0.000
42	A	878	THR	0	-0.076	-0.044	18.150	0.021	0.021	0.000	0.000	0.000	0.000
43	A	879	ASP	-1	-0.826	-0.890	15.376	-0.283	-0.283	0.000	0.000	0.000	0.000
44	A	880	GLY	0	0.014	0.019	15.735	0.022	0.022	0.000	0.000	0.000	0.000
45	A	881	ARG	1	0.796	0.887	11.328	0.245	0.245	0.000	0.000	0.000	0.000
46	A	882	LEU	0	-0.012	0.009	9.898	-0.136	-0.136	0.000	0.000	0.000	0.000
47	A	883	ARG	1	0.975	0.976	6.816	1.361	1.361	0.000	0.000	0.000	0.000
48	A	884	SER	0	-0.035	-0.043	9.628	-0.133	-0.133	0.000	0.000	0.000	0.000
49	A	885	GLY	0	-0.046	-0.029	8.879	-0.007	-0.007	0.000	0.000	0.000	0.000
50	A	886	ASP	-1	-0.787	-0.883	5.700	-2.604	-2.604	0.000	0.000	0.000	0.000
51	A	887	GLU	-1	-0.934	-0.975	5.186	-1.498	-1.498	0.000	0.000	0.000	0.000
52	A	888	LEU	0	-0.035	-0.019	6.824	0.200	0.200	0.000	0.000	0.000	0.000
53	A	889	ILE	0	-0.030	-0.011	7.248	0.049	0.049	0.000	0.000	0.000	0.000
54	A	890	SER	0	-0.013	-0.014	10.200	0.108	0.108	0.000	0.000	0.000	0.000
55	A	891	VAL	0	0.033	0.021	13.515	-0.059	-0.059	0.000	0.000	0.000	0.000
56	A	892	ASP	-1	-0.799	-0.906	16.333	-0.171	-0.171	0.000	0.000	0.000	0.000
57	A	893	GLY	0	-0.004	0.006	17.118	0.024	0.024	0.000	0.000	0.000	0.000
58	A	894	THR	0	-0.026	-0.008	18.296	0.032	0.032	0.000	0.000	0.000	0.000
59	A	895	PRO	0	-0.009	-0.017	14.665	-0.042	-0.042	0.000	0.000	0.000	0.000
60	A	896	VAL	0	-0.028	-0.032	12.811	0.015	0.015	0.000	0.000	0.000	0.000
61	A	897	ILE	0	0.064	0.035	9.746	-0.043	-0.043	0.000	0.000	0.000	0.000
62	A	898	GLY	0	-0.021	-0.009	12.758	0.066	0.066	0.000	0.000	0.000	0.000
63	A	899	LYS	1	0.872	0.948	15.053	0.210	0.210	0.000	0.000	0.000	0.000
64	A	900	SER	0	0.058	0.038	16.757	-0.044	-0.044	0.000	0.000	0.000	0.000
65	A	901	HIS	0	0.090	0.027	18.001	-0.006	-0.006	0.000	0.000	0.000	0.000
66	A	902	GLN	0	-0.008	-0.019	18.891	0.014	0.014	0.000	0.000	0.000	0.000
67	A	903	LEU	0	-0.017	0.007	18.573	0.021	0.021	0.000	0.000	0.000	0.000
68	A	904	VAL	0	0.070	0.028	15.957	0.015	0.015	0.000	0.000	0.000	0.000
69	A	905	VAL	0	-0.029	-0.009	19.111	0.011	0.011	0.000	0.000	0.000	0.000
70	A	906	GLN	0	-0.030	-0.019	22.436	0.020	0.020	0.000	0.000	0.000	0.000
71	A	907	LEU	0	0.009	0.004	18.455	0.013	0.013	0.000	0.000	0.000	0.000
72	A	908	MET	0	0.009	0.001	18.886	0.003	0.003	0.000	0.000	0.000	0.000
73	A	909	GLN	0	-0.021	0.002	21.781	0.005	0.005	0.000	0.000	0.000	0.000
74	A	910	GLN	0	-0.051	-0.035	24.470	0.016	0.016	0.000	0.000	0.000	0.000
75	A	911	ALA	0	0.056	0.031	21.277	0.011	0.011	0.000	0.000	0.000	0.000
76	A	912	ALA	0	-0.077	-0.057	23.296	0.007	0.007	0.000	0.000	0.000	0.000
77	A	913	LYS	1	0.894	0.959	25.692	0.137	0.137	0.000	0.000	0.000	0.000
78	A	914	GLN	0	-0.064	-0.028	22.699	0.025	0.025	0.000	0.000	0.000	0.000
79	A	915	GLY	0	0.003	0.009	26.246	0.007	0.007	0.000	0.000	0.000	0.000
80	A	916	HIS	0	-0.033	-0.026	22.275	-0.009	-0.009	0.000	0.000	0.000	0.000
81	A	917	VAL	0	0.028	0.020	17.222	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	918	ASN	0	-0.029	-0.012	15.859	-0.022	-0.022	0.000	0.000	0.000	0.000
83	A	919	LEU	0	-0.021	-0.006	12.291	0.009	0.009	0.000	0.000	0.000	0.000
84	A	920	THR	0	0.029	0.032	9.223	-0.005	-0.005	0.000	0.000	0.000	0.000
85	A	921	VAL	0	0.008	-0.009	6.831	-0.060	-0.060	0.000	0.000	0.000	0.000
86	A	922	ARG	1	0.900	0.962	2.060	-9.184	-8.567	6.093	-2.685	-4.024	0.026
87	A	923	GLN	0	-0.034	-0.044	2.835	-3.146	-1.907	0.645	-0.568	-1.315	-0.007
88	A	924	THR	0	-0.028	-0.026	2.326	-3.971	-3.297	6.566	-3.955	-3.284	-0.039
89	A	925	ARG	1	0.944	0.976	3.194	-6.999	-5.765	0.120	-0.471	-0.882	0.002
90	A	926	LEU	0	0.024	0.024	4.900	0.122	0.141	-0.001	-0.006	-0.012	0.000

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