FMO DATABASE

FMODB ID: Z659N

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

Total energy (hartree)

FMO2-HF: Electronic energy	-606783.34188
FMO2-HF: Nuclear repulsion	572421.225582
FMO2-HF: Total energy	-34362.116298
FMO2-MP2: Total energy	-34463.290481

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.
-30.353	-21.063	9.419	-8.423	-10.287	-0.022

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 : -0.017 / q_NPA : -0.015

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	-0.833	-0.887	3.814	-2.274	0.252	-0.021	-1.315	-1.190	-0.002
4	A	840	GLN	0	-0.025	-0.012	6.181	0.234	0.234	0.000	0.000	0.000	0.000
5	A	841	ASP	-1	-0.762	-0.857	8.376	-0.285	-0.285	0.000	0.000	0.000	0.000
6	A	842	ILE	0	-0.081	-0.044	9.696	0.015	0.015	0.000	0.000	0.000	0.000
7	A	843	PHE	0	0.009	0.013	13.313	-0.003	-0.003	0.000	0.000	0.000	0.000
8	A	844	LEU	0	-0.031	-0.018	15.807	-0.002	-0.002	0.000	0.000	0.000	0.000
9	A	845	TRP	0	0.049	0.020	19.067	0.009	0.009	0.000	0.000	0.000	0.000
10	A	846	ARG	1	0.844	0.941	22.681	0.171	0.171	0.000	0.000	0.000	0.000
11	A	847	LYS	1	0.884	0.947	23.442	0.222	0.222	0.000	0.000	0.000	0.000
12	A	848	GLU	-1	-0.902	-0.959	26.367	-0.130	-0.130	0.000	0.000	0.000	0.000
13	A	849	THR	0	-0.010	-0.013	26.150	-0.002	-0.002	0.000	0.000	0.000	0.000
14	A	850	GLY	0	-0.045	-0.016	24.706	-0.014	-0.014	0.000	0.000	0.000	0.000
15	A	851	PHE	0	0.032	0.000	19.229	0.001	0.001	0.000	0.000	0.000	0.000
16	A	852	GLY	0	-0.008	-0.003	19.692	-0.015	-0.015	0.000	0.000	0.000	0.000
17	A	853	PHE	0	0.056	0.030	15.666	-0.024	-0.024	0.000	0.000	0.000	0.000
18	A	854	ARG	1	0.852	0.925	17.289	0.405	0.405	0.000	0.000	0.000	0.000
19	A	855	ILE	0	0.018	0.017	14.124	-0.064	-0.064	0.000	0.000	0.000	0.000
20	A	856	LEU	0	-0.015	-0.009	13.861	0.072	0.072	0.000	0.000	0.000	0.000
21	A	857	GLY	0	0.058	0.039	14.100	-0.075	-0.075	0.000	0.000	0.000	0.000
22	A	858	GLY	0	0.054	0.025	14.979	0.039	0.039	0.000	0.000	0.000	0.000
23	A	859	ASN	0	-0.132	-0.080	16.390	0.078	0.078	0.000	0.000	0.000	0.000
24	A	860	GLU	-1	-0.938	-0.963	18.765	-0.217	-0.217	0.000	0.000	0.000	0.000
25	A	861	PRO	0	-0.038	-0.031	17.982	-0.037	-0.037	0.000	0.000	0.000	0.000
26	A	862	GLY	0	0.002	0.007	15.511	0.024	0.024	0.000	0.000	0.000	0.000
27	A	863	GLU	-1	-0.839	-0.897	14.138	-0.523	-0.523	0.000	0.000	0.000	0.000
28	A	864	PRO	0	-0.019	-0.013	9.291	0.030	0.030	0.000	0.000	0.000	0.000
29	A	865	ILE	0	0.001	0.019	10.953	0.031	0.031	0.000	0.000	0.000	0.000
30	A	866	TYR	0	0.011	0.001	6.513	-0.006	-0.006	0.000	0.000	0.000	0.000
31	A	867	ILE	0	-0.010	0.004	9.875	0.261	0.261	0.000	0.000	0.000	0.000
32	A	868	GLY	0	0.038	0.020	12.059	-0.090	-0.090	0.000	0.000	0.000	0.000
33	A	869	HIS	0	-0.007	-0.007	14.683	-0.004	-0.004	0.000	0.000	0.000	0.000
34	A	870	ILE	0	0.048	0.028	12.865	0.012	0.012	0.000	0.000	0.000	0.000
35	A	871	VAL	0	-0.040	-0.021	17.371	0.027	0.027	0.000	0.000	0.000	0.000
36	A	872	PRO	0	0.034	0.013	20.963	0.003	0.003	0.000	0.000	0.000	0.000
37	A	873	LEU	0	0.000	-0.002	22.174	0.020	0.020	0.000	0.000	0.000	0.000
38	A	874	GLY	0	0.001	0.005	22.182	0.021	0.021	0.000	0.000	0.000	0.000
39	A	875	ALA	0	-0.056	-0.037	20.721	-0.002	-0.002	0.000	0.000	0.000	0.000
40	A	876	ALA	0	0.032	0.015	15.642	0.004	0.004	0.000	0.000	0.000	0.000
41	A	877	ASP	-1	-0.838	-0.916	16.567	-0.332	-0.332	0.000	0.000	0.000	0.000
42	A	878	THR	0	-0.045	-0.027	18.232	0.021	0.021	0.000	0.000	0.000	0.000
43	A	879	ASP	-1	-0.820	-0.876	15.278	-0.326	-0.326	0.000	0.000	0.000	0.000
44	A	880	GLY	0	0.014	0.019	15.821	0.023	0.023	0.000	0.000	0.000	0.000
45	A	881	ARG	1	0.772	0.868	11.404	0.273	0.273	0.000	0.000	0.000	0.000
46	A	882	LEU	0	-0.005	0.007	10.179	-0.156	-0.156	0.000	0.000	0.000	0.000
47	A	883	ARG	1	0.925	0.942	6.299	1.912	1.912	0.000	0.000	0.000	0.000
48	A	884	SER	0	-0.035	-0.041	9.705	-0.135	-0.135	0.000	0.000	0.000	0.000
49	A	885	GLY	0	-0.039	-0.025	8.787	-0.026	-0.026	0.000	0.000	0.000	0.000
50	A	886	ASP	-1	-0.778	-0.867	5.767	-2.842	-2.842	0.000	0.000	0.000	0.000
51	A	887	GLU	-1	-0.906	-0.960	5.230	-1.291	-1.291	0.000	0.000	0.000	0.000
52	A	888	LEU	0	-0.025	-0.014	6.919	0.194	0.194	0.000	0.000	0.000	0.000
53	A	889	ILE	0	0.002	-0.005	7.606	0.076	0.076	0.000	0.000	0.000	0.000
54	A	890	SER	0	-0.043	-0.026	10.468	0.117	0.117	0.000	0.000	0.000	0.000
55	A	891	VAL	0	0.041	0.020	13.431	-0.065	-0.065	0.000	0.000	0.000	0.000
56	A	892	ASP	-1	-0.796	-0.898	16.251	-0.186	-0.186	0.000	0.000	0.000	0.000
57	A	893	GLY	0	0.001	0.010	17.015	0.026	0.026	0.000	0.000	0.000	0.000
58	A	894	THR	0	-0.024	-0.006	18.200	0.034	0.034	0.000	0.000	0.000	0.000
59	A	895	PRO	0	-0.011	-0.017	14.935	-0.043	-0.043	0.000	0.000	0.000	0.000
60	A	896	VAL	0	-0.020	-0.029	13.088	0.015	0.015	0.000	0.000	0.000	0.000
61	A	897	ILE	0	0.062	0.034	10.274	-0.042	-0.042	0.000	0.000	0.000	0.000
62	A	898	GLY	0	-0.011	-0.007	12.949	0.068	0.068	0.000	0.000	0.000	0.000
63	A	899	LYS	1	0.840	0.935	15.170	0.207	0.207	0.000	0.000	0.000	0.000
64	A	900	SER	0	0.046	0.011	16.859	-0.045	-0.045	0.000	0.000	0.000	0.000
65	A	901	HIS	0	0.086	0.023	18.102	-0.005	-0.005	0.000	0.000	0.000	0.000
66	A	902	GLN	0	0.010	0.011	18.988	0.009	0.009	0.000	0.000	0.000	0.000
67	A	903	LEU	0	-0.018	0.006	18.608	0.020	0.020	0.000	0.000	0.000	0.000
68	A	904	VAL	0	0.058	0.023	16.202	0.014	0.014	0.000	0.000	0.000	0.000
69	A	905	VAL	0	-0.025	-0.008	19.290	0.010	0.010	0.000	0.000	0.000	0.000
70	A	906	GLN	0	-0.018	-0.013	22.591	0.017	0.017	0.000	0.000	0.000	0.000
71	A	907	LEU	0	0.006	0.004	18.804	0.013	0.013	0.000	0.000	0.000	0.000
72	A	908	MET	0	0.006	0.000	18.735	0.000	0.000	0.000	0.000	0.000	0.000
73	A	909	GLN	0	-0.014	0.004	21.738	0.005	0.005	0.000	0.000	0.000	0.000
74	A	910	GLN	0	-0.057	-0.043	24.448	0.017	0.017	0.000	0.000	0.000	0.000
75	A	911	ALA	0	0.059	0.035	21.256	0.011	0.011	0.000	0.000	0.000	0.000
76	A	912	ALA	0	-0.078	-0.055	23.252	0.007	0.007	0.000	0.000	0.000	0.000
77	A	913	LYS	1	0.901	0.959	25.667	0.142	0.142	0.000	0.000	0.000	0.000
78	A	914	GLN	0	-0.067	-0.023	22.650	0.026	0.026	0.000	0.000	0.000	0.000
79	A	915	GLY	0	0.011	0.011	26.233	0.007	0.007	0.000	0.000	0.000	0.000
80	A	916	HIS	0	-0.037	-0.027	22.299	-0.011	-0.011	0.000	0.000	0.000	0.000
81	A	917	VAL	0	0.032	0.019	17.268	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	918	ASN	0	-0.048	-0.036	15.511	-0.015	-0.015	0.000	0.000	0.000	0.000
83	A	919	LEU	0	-0.016	-0.003	12.289	0.011	0.011	0.000	0.000	0.000	0.000
84	A	920	THR	0	0.025	0.021	9.215	-0.003	-0.003	0.000	0.000	0.000	0.000
85	A	921	VAL	0	-0.003	-0.017	6.798	-0.041	-0.041	0.000	0.000	0.000	0.000
86	A	922	ARG	1	0.845	0.924	2.379	-8.660	-5.842	1.994	-1.855	-2.956	0.020
87	A	923	GLN	0	-0.051	-0.058	2.832	-2.870	-1.665	0.707	-0.612	-1.301	-0.008
88	A	924	THR	0	-0.016	-0.021	2.343	-4.436	-3.255	5.911	-3.861	-3.231	-0.038
89	A	925	ARG	1	0.914	0.964	2.763	-10.105	-8.563	0.829	-0.774	-1.597	0.006
90	A	926	LEU	0	0.024	0.023	4.894	0.097	0.115	-0.001	-0.006	-0.012	0.000

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