FMO DATABASE

FMODB ID: G6NN1

Calculation Name: 2VW9-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2VW9

Chain ID: A

ChEMBL ID:

UniProt ID: O25841

Base Structure: X-ray

Registration Date: 2023-06-21

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	108
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-767229.034017
FMO2-HF: Nuclear repulsion	724372.674281
FMO2-HF: Total energy	-42856.359736
FMO2-MP2: Total energy	-42979.595212

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:1001:MET)

Summations of interaction energy for fragment #1(A:1001:MET)

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.
0.674	2.695	-0.006	-0.951	-1.064	0.005

Interaction energy analysis for fragmet #1(A:1001:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.043 / q_NPA : 0.016

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	1003	ASN	0	-0.008	-0.015	3.860	-0.764	1.257	-0.006	-0.951	-1.064	0.005
4	A	1004	LYS	1	0.772	0.889	5.964	1.442	1.442	0.000	0.000	0.000	0.000
5	A	1005	VAL	0	0.008	0.006	9.653	0.128	0.128	0.000	0.000	0.000	0.000
6	A	1006	ILE	0	0.036	0.006	12.852	0.003	0.003	0.000	0.000	0.000	0.000
7	A	1007	MET	0	-0.027	-0.011	16.315	0.028	0.028	0.000	0.000	0.000	0.000
8	A	1008	VAL	0	0.035	0.027	19.400	0.010	0.010	0.000	0.000	0.000	0.000
9	A	1009	GLY	0	0.023	0.027	23.153	0.006	0.006	0.000	0.000	0.000	0.000
10	A	1010	ARG	1	0.842	0.921	25.123	0.173	0.173	0.000	0.000	0.000	0.000
11	A	1011	LEU	0	0.004	0.021	25.945	0.000	0.000	0.000	0.000	0.000	0.000
12	A	1012	THR	0	0.004	-0.003	27.398	0.015	0.015	0.000	0.000	0.000	0.000
13	A	1013	ARG	1	0.718	0.795	24.693	0.148	0.148	0.000	0.000	0.000	0.000
14	A	1014	ASN	0	0.054	0.015	30.098	-0.015	-0.015	0.000	0.000	0.000	0.000
15	A	1015	VAL	0	0.004	0.015	26.612	0.000	0.000	0.000	0.000	0.000	0.000
16	A	1016	GLU	-1	-0.800	-0.860	26.233	-0.116	-0.116	0.000	0.000	0.000	0.000
17	A	1017	LEU	0	-0.067	-0.025	27.150	-0.005	-0.005	0.000	0.000	0.000	0.000
18	A	1018	LYS	1	0.890	0.942	26.127	0.103	0.103	0.000	0.000	0.000	0.000
19	A	1019	TYR	0	0.037	-0.002	27.330	-0.011	-0.011	0.000	0.000	0.000	0.000
20	A	1020	LEU	0	-0.030	-0.013	22.059	0.011	0.011	0.000	0.000	0.000	0.000
21	A	1021	PRO	0	0.034	0.000	26.351	-0.002	-0.002	0.000	0.000	0.000	0.000
22	A	1022	SER	0	0.008	0.006	23.994	0.007	0.007	0.000	0.000	0.000	0.000
23	A	1023	GLY	0	0.042	0.029	26.641	-0.004	-0.004	0.000	0.000	0.000	0.000
24	A	1024	SER	0	-0.041	-0.015	22.917	-0.007	-0.007	0.000	0.000	0.000	0.000
25	A	1025	ALA	0	0.037	0.027	25.060	0.009	0.009	0.000	0.000	0.000	0.000
26	A	1026	ALA	0	-0.038	-0.025	22.543	-0.022	-0.022	0.000	0.000	0.000	0.000
27	A	1027	ALA	0	0.041	0.026	22.891	0.019	0.019	0.000	0.000	0.000	0.000
28	A	1028	THR	0	-0.080	-0.027	21.774	-0.014	-0.014	0.000	0.000	0.000	0.000
29	A	1029	ILE	0	0.050	0.038	22.189	0.016	0.016	0.000	0.000	0.000	0.000
30	A	1030	GLY	0	0.062	0.032	22.831	-0.014	-0.014	0.000	0.000	0.000	0.000
31	A	1031	LEU	0	-0.038	-0.012	21.122	0.006	0.006	0.000	0.000	0.000	0.000
32	A	1032	ALA	0	0.003	-0.003	24.224	0.015	0.015	0.000	0.000	0.000	0.000
33	A	1033	THR	0	-0.003	-0.028	22.005	-0.005	-0.005	0.000	0.000	0.000	0.000
34	A	1034	SER	0	-0.112	-0.060	24.461	0.000	0.000	0.000	0.000	0.000	0.000
35	A	1035	ARG	1	0.838	0.892	22.554	0.183	0.183	0.000	0.000	0.000	0.000
36	A	1036	ARG	1	0.898	0.923	26.206	0.163	0.163	0.000	0.000	0.000	0.000
37	A	1037	PHE	0	-0.033	-0.005	27.167	-0.010	-0.010	0.000	0.000	0.000	0.000
38	A	1038	LYS	1	0.847	0.919	29.272	0.099	0.099	0.000	0.000	0.000	0.000
39	A	1039	LYS	1	0.924	0.962	30.894	0.082	0.082	0.000	0.000	0.000	0.000
40	A	1040	GLN	0	0.031	0.017	32.677	-0.002	-0.002	0.000	0.000	0.000	0.000
41	A	1041	ASP	-1	-0.721	-0.848	33.626	-0.073	-0.073	0.000	0.000	0.000	0.000
42	A	1042	GLY	0	-0.055	-0.042	36.938	-0.002	-0.002	0.000	0.000	0.000	0.000
43	A	1043	THR	0	-0.043	-0.026	36.509	-0.003	-0.003	0.000	0.000	0.000	0.000
44	A	1044	LEU	0	0.033	0.020	32.782	-0.004	-0.004	0.000	0.000	0.000	0.000
45	A	1045	GLY	0	-0.028	-0.021	32.115	0.010	0.010	0.000	0.000	0.000	0.000
46	A	1046	GLU	-1	-0.791	-0.873	28.801	-0.144	-0.144	0.000	0.000	0.000	0.000
47	A	1047	GLU	-1	-0.783	-0.835	23.932	-0.161	-0.161	0.000	0.000	0.000	0.000
48	A	1048	VAL	0	0.004	-0.021	26.173	-0.013	-0.013	0.000	0.000	0.000	0.000
49	A	1049	CYS	0	0.001	0.009	20.219	0.005	0.005	0.000	0.000	0.000	0.000
50	A	1050	PHE	0	-0.014	-0.010	22.859	-0.014	-0.014	0.000	0.000	0.000	0.000
51	A	1051	ILE	0	0.009	0.001	16.551	0.006	0.006	0.000	0.000	0.000	0.000
52	A	1052	ASP	-1	-0.741	-0.826	20.504	-0.149	-0.149	0.000	0.000	0.000	0.000
53	A	1053	ALA	0	0.008	0.005	18.077	-0.025	-0.025	0.000	0.000	0.000	0.000
54	A	1054	ARG	1	0.776	0.844	16.998	0.179	0.179	0.000	0.000	0.000	0.000
55	A	1055	LEU	0	0.027	0.008	17.944	-0.061	-0.061	0.000	0.000	0.000	0.000
56	A	1056	PHE	0	0.040	0.002	16.893	0.041	0.041	0.000	0.000	0.000	0.000
57	A	1057	GLY	0	0.040	0.018	20.540	-0.022	-0.022	0.000	0.000	0.000	0.000
58	A	1058	ARG	1	0.928	0.935	22.725	0.199	0.199	0.000	0.000	0.000	0.000
59	A	1059	THR	0	0.045	0.021	19.794	0.023	0.023	0.000	0.000	0.000	0.000
60	A	1060	ALA	0	-0.015	0.005	22.739	0.006	0.006	0.000	0.000	0.000	0.000
61	A	1061	GLU	-1	-0.784	-0.874	24.242	-0.154	-0.154	0.000	0.000	0.000	0.000
62	A	1062	ILE	0	-0.027	-0.011	25.127	0.012	0.012	0.000	0.000	0.000	0.000
63	A	1063	ALA	0	0.020	0.000	24.996	0.007	0.007	0.000	0.000	0.000	0.000
64	A	1064	ASN	0	-0.009	-0.027	27.043	0.012	0.012	0.000	0.000	0.000	0.000
65	A	1065	GLN	0	-0.047	-0.002	29.951	0.005	0.005	0.000	0.000	0.000	0.000
66	A	1066	TYR	0	-0.041	-0.023	29.828	0.011	0.011	0.000	0.000	0.000	0.000
67	A	1067	LEU	0	-0.032	0.002	26.360	-0.007	-0.007	0.000	0.000	0.000	0.000
68	A	1068	SER	0	0.022	0.009	30.708	0.012	0.012	0.000	0.000	0.000	0.000
69	A	1069	LYS	1	0.926	0.949	31.494	0.100	0.100	0.000	0.000	0.000	0.000
70	A	1070	GLY	0	-0.004	0.012	31.612	0.006	0.006	0.000	0.000	0.000	0.000
71	A	1071	SER	0	0.003	-0.007	30.433	0.001	0.001	0.000	0.000	0.000	0.000
72	A	1072	SER	0	-0.049	-0.040	28.897	-0.005	-0.005	0.000	0.000	0.000	0.000
73	A	1073	VAL	0	-0.048	-0.031	23.942	0.002	0.002	0.000	0.000	0.000	0.000
74	A	1074	LEU	0	0.036	0.026	20.155	0.001	0.001	0.000	0.000	0.000	0.000
75	A	1075	ILE	0	-0.029	-0.013	17.164	0.005	0.005	0.000	0.000	0.000	0.000
76	A	1076	GLU	-1	-0.799	-0.891	14.449	-0.896	-0.896	0.000	0.000	0.000	0.000
77	A	1077	GLY	0	0.003	0.002	13.756	0.063	0.063	0.000	0.000	0.000	0.000
78	A	1078	ARG	1	0.855	0.919	8.437	0.917	0.917	0.000	0.000	0.000	0.000
79	A	1079	LEU	0	0.038	0.012	9.362	0.216	0.216	0.000	0.000	0.000	0.000
80	A	1080	THR	0	-0.031	-0.025	9.084	-0.125	-0.125	0.000	0.000	0.000	0.000
81	A	1081	TYR	0	0.038	0.018	11.164	0.046	0.046	0.000	0.000	0.000	0.000
82	A	1082	GLU	-1	-0.757	-0.817	12.743	-0.068	-0.068	0.000	0.000	0.000	0.000
83	A	1083	SER	0	-0.009	-0.025	15.798	0.030	0.030	0.000	0.000	0.000	0.000
84	A	1084	TRP	0	-0.023	-0.008	17.675	0.002	0.002	0.000	0.000	0.000	0.000
85	A	1085	MET	0	0.051	0.055	20.961	0.012	0.012	0.000	0.000	0.000	0.000
86	A	1086	ASP	-1	-0.771	-0.854	24.591	0.046	0.046	0.000	0.000	0.000	0.000
87	A	1087	GLN	0	0.046	-0.004	27.014	0.005	0.005	0.000	0.000	0.000	0.000
88	A	1088	THR	0	-0.043	-0.027	30.389	-0.003	-0.003	0.000	0.000	0.000	0.000
89	A	1089	GLY	0	0.025	0.024	29.363	0.004	0.004	0.000	0.000	0.000	0.000
90	A	1090	LYS	1	0.829	0.911	26.876	-0.046	-0.046	0.000	0.000	0.000	0.000
91	A	1091	LYS	1	0.889	0.914	22.287	-0.158	-0.158	0.000	0.000	0.000	0.000
92	A	1092	ASN	0	-0.036	-0.022	22.354	-0.014	-0.014	0.000	0.000	0.000	0.000
93	A	1093	SER	0	0.007	0.001	17.308	0.016	0.016	0.000	0.000	0.000	0.000
94	A	1094	ARG	1	0.834	0.911	17.512	0.076	0.076	0.000	0.000	0.000	0.000
95	A	1095	HIS	0	0.040	0.026	12.072	-0.025	-0.025	0.000	0.000	0.000	0.000
96	A	1096	THR	0	-0.081	-0.057	14.677	-0.011	-0.011	0.000	0.000	0.000	0.000
97	A	1097	ILE	0	0.060	0.025	13.913	-0.042	-0.042	0.000	0.000	0.000	0.000
98	A	1098	THR	0	-0.062	-0.020	12.697	0.091	0.091	0.000	0.000	0.000	0.000
99	A	1099	ALA	0	0.014	0.007	13.723	-0.127	-0.127	0.000	0.000	0.000	0.000
100	A	1100	ASP	-1	-0.836	-0.900	12.442	-1.092	-1.092	0.000	0.000	0.000	0.000
101	A	1101	SER	0	-0.053	-0.031	15.692	0.076	0.076	0.000	0.000	0.000	0.000
102	A	1102	LEU	0	0.012	-0.006	19.085	-0.002	-0.002	0.000	0.000	0.000	0.000
103	A	1103	GLN	0	0.024	0.019	22.260	0.019	0.019	0.000	0.000	0.000	0.000
104	A	1104	PHE	0	0.021	0.006	24.889	0.004	0.004	0.000	0.000	0.000	0.000
105	A	1105	MET	0	-0.005	-0.002	26.569	-0.002	-0.002	0.000	0.000	0.000	0.000
106	A	1106	ASP	-1	-0.747	-0.848	29.919	-0.165	-0.165	0.000	0.000	0.000	0.000
107	A	1107	LYS	1	0.945	0.989	33.246	0.172	0.172	0.000	0.000	0.000	0.000
108	A	1108	LYS	1	0.896	0.942	32.514	0.174	0.174	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:1001:MET)