FMO DATABASE

FMODB ID: N13ZQ

Calculation Name: 4NJ6-A-Xray322

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4NJ6

Chain ID: A

ChEMBL ID:

UniProt ID: P93022

Base Structure: X-ray

Registration Date: 2021-09-07

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

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. 1.20200129

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	90
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-628270.373581
FMO2-HF: Nuclear repulsion	592534.764821
FMO2-HF: Total energy	-35735.60876
FMO2-MP2: Total energy	-35839.476345

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:1038:ACE )

Summations of interaction energy for fragment #1(A:1038:ACE )

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.
-1.378	0.218	-0.002	-0.79	-0.804	-0.002

Interaction energy analysis for fragmet #1(A:1038:ACE )

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 : -0.020

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	1040	TYR	0	-0.009	0.016	3.724	0.006	1.629	-0.002	-0.786	-0.835	-0.002
4	A	1041	THR	0	0.042	0.029	5.129	-0.085	-0.112	0.000	-0.004	0.031	0.000
5	A	1042	ALA	0	-0.035	-0.013	7.537	0.172	0.172	0.000	0.000	0.000	0.000
6	A	1043	VAL	0	0.055	0.027	8.890	-0.071	-0.071	0.000	0.000	0.000	0.000
7	A	1044	GLN	0	-0.034	-0.032	11.277	0.018	0.018	0.000	0.000	0.000	0.000
8	A	1045	LYS	1	1.009	1.012	14.981	-0.062	-0.062	0.000	0.000	0.000	0.000
9	A	1046	ARG	1	0.968	0.990	18.691	-0.022	-0.022	0.000	0.000	0.000	0.000
10	A	1047	GLY	0	-0.027	-0.015	21.016	-0.007	-0.007	0.000	0.000	0.000	0.000
11	A	1048	SER	0	-0.038	-0.010	19.212	-0.006	-0.006	0.000	0.000	0.000	0.000
12	A	1049	VAL	0	-0.015	0.001	15.251	0.012	0.012	0.000	0.000	0.000	0.000
13	A	1050	GLY	0	0.009	0.011	13.042	-0.020	-0.020	0.000	0.000	0.000	0.000
14	A	1051	ARG	1	0.931	0.959	12.200	-0.091	-0.091	0.000	0.000	0.000	0.000
15	A	1052	SER	0	-0.001	-0.010	6.782	-0.078	-0.078	0.000	0.000	0.000	0.000
16	A	1053	ILE	0	0.018	0.012	9.346	0.020	0.020	0.000	0.000	0.000	0.000
17	A	1054	ASP	-1	-0.824	-0.909	9.356	-0.606	-0.606	0.000	0.000	0.000	0.000
18	A	1055	VAL	0	0.050	-0.004	10.630	0.079	0.079	0.000	0.000	0.000	0.000
19	A	1056	ASN	0	0.017	0.006	11.696	0.100	0.100	0.000	0.000	0.000	0.000
20	A	1057	ARG	1	0.855	0.938	12.703	0.205	0.205	0.000	0.000	0.000	0.000
21	A	1058	TYR	0	-0.115	-0.108	14.507	0.030	0.030	0.000	0.000	0.000	0.000
22	A	1059	ARG	1	0.935	0.958	18.480	0.073	0.073	0.000	0.000	0.000	0.000
23	A	1060	GLY	0	0.036	0.012	21.189	-0.001	-0.001	0.000	0.000	0.000	0.000
24	A	1061	TYR	0	-0.024	-0.052	19.618	0.002	0.002	0.000	0.000	0.000	0.000
25	A	1062	ASP	-1	-0.892	-0.931	22.231	-0.061	-0.061	0.000	0.000	0.000	0.000
26	A	1063	GLU	-1	-0.900	-0.932	21.085	-0.091	-0.091	0.000	0.000	0.000	0.000
27	A	1064	LEU	0	0.024	0.015	15.853	0.009	0.009	0.000	0.000	0.000	0.000
28	A	1065	ARG	1	0.936	0.966	19.417	0.085	0.085	0.000	0.000	0.000	0.000
29	A	1066	HIS	0	0.011	-0.004	21.744	0.016	0.016	0.000	0.000	0.000	0.000
30	A	1067	ASP	-1	-0.819	-0.846	17.955	-0.024	-0.024	0.000	0.000	0.000	0.000
31	A	1068	LEU	0	-0.013	-0.015	15.300	0.018	0.018	0.000	0.000	0.000	0.000
32	A	1069	ALA	0	0.017	0.012	19.178	0.016	0.016	0.000	0.000	0.000	0.000
33	A	1070	ARG	1	0.909	0.958	21.576	0.026	0.026	0.000	0.000	0.000	0.000
34	A	1071	MET	0	-0.096	-0.043	14.826	0.018	0.018	0.000	0.000	0.000	0.000
35	A	1072	PHE	0	-0.086	-0.045	15.188	0.021	0.021	0.000	0.000	0.000	0.000
36	A	1073	GLY	0	-0.012	0.004	20.837	0.001	0.001	0.000	0.000	0.000	0.000
37	A	1074	ILE	0	-0.077	-0.033	23.226	0.000	0.000	0.000	0.000	0.000	0.000
38	A	1075	GLU	-1	-0.924	-0.980	25.467	0.004	0.004	0.000	0.000	0.000	0.000
39	A	1076	GLY	0	-0.020	-0.003	26.993	0.002	0.002	0.000	0.000	0.000	0.000
40	A	1077	GLN	0	-0.024	-0.012	27.011	-0.002	-0.002	0.000	0.000	0.000	0.000
41	A	1078	LEU	0	-0.014	-0.028	21.432	-0.001	-0.001	0.000	0.000	0.000	0.000
42	A	1079	GLU	-1	-0.840	-0.918	25.620	-0.027	-0.027	0.000	0.000	0.000	0.000
43	A	1080	ASP	-1	-0.834	-0.911	27.091	-0.036	-0.036	0.000	0.000	0.000	0.000
44	A	1081	PRO	0	-0.050	-0.028	26.705	0.004	0.004	0.000	0.000	0.000	0.000
45	A	1082	GLN	0	-0.077	-0.031	28.602	0.001	0.001	0.000	0.000	0.000	0.000
46	A	1083	THR	0	-0.012	-0.021	31.651	0.003	0.003	0.000	0.000	0.000	0.000
47	A	1084	SER	0	-0.070	-0.017	27.783	0.003	0.003	0.000	0.000	0.000	0.000
48	A	1085	ASP	-1	-0.907	-0.953	29.690	-0.006	-0.006	0.000	0.000	0.000	0.000
49	A	1086	TRP	0	-0.104	-0.055	24.251	0.004	0.004	0.000	0.000	0.000	0.000
50	A	1087	LYS	1	0.971	0.987	24.375	0.022	0.022	0.000	0.000	0.000	0.000
51	A	1088	LEU	0	-0.001	0.008	18.293	0.005	0.005	0.000	0.000	0.000	0.000
52	A	1089	VAL	0	0.010	0.000	18.363	-0.008	-0.008	0.000	0.000	0.000	0.000
53	A	1090	TYR	0	0.002	-0.016	15.015	0.007	0.007	0.000	0.000	0.000	0.000
54	A	1091	VAL	0	-0.027	-0.009	12.925	0.016	0.016	0.000	0.000	0.000	0.000
55	A	1092	ALA	0	0.084	0.047	13.912	-0.056	-0.056	0.000	0.000	0.000	0.000
56	A	1093	HIS	0	0.009	-0.002	13.432	0.020	0.020	0.000	0.000	0.000	0.000
57	A	1094	GLU	-1	-0.926	-0.965	16.670	-0.110	-0.110	0.000	0.000	0.000	0.000
58	A	1095	ASN	0	-0.099	-0.052	15.227	0.024	0.024	0.000	0.000	0.000	0.000
59	A	1096	ALA	0	0.013	0.020	17.202	0.024	0.024	0.000	0.000	0.000	0.000
60	A	1097	ILE	0	-0.018	-0.021	18.181	-0.015	-0.015	0.000	0.000	0.000	0.000
61	A	1098	LEU	0	0.006	0.013	19.282	0.011	0.011	0.000	0.000	0.000	0.000
62	A	1099	LEU	0	0.003	-0.003	20.327	0.002	0.002	0.000	0.000	0.000	0.000
63	A	1100	VAL	0	-0.015	-0.011	18.238	-0.012	-0.012	0.000	0.000	0.000	0.000
64	A	1101	GLY	0	-0.053	-0.048	21.010	0.014	0.014	0.000	0.000	0.000	0.000
65	A	1102	ASP	-1	-0.924	-0.941	23.411	-0.079	-0.079	0.000	0.000	0.000	0.000
66	A	1103	ASP	-1	-0.905	-0.938	21.236	-0.153	-0.153	0.000	0.000	0.000	0.000
67	A	1104	PRO	0	-0.007	0.022	23.514	0.004	0.004	0.000	0.000	0.000	0.000
68	A	1105	TRP	0	0.018	-0.003	17.458	-0.010	-0.010	0.000	0.000	0.000	0.000
69	A	1106	GLU	-1	-0.902	-0.958	19.103	-0.192	-0.192	0.000	0.000	0.000	0.000
70	A	1107	GLU	-1	-0.907	-0.964	18.430	-0.196	-0.196	0.000	0.000	0.000	0.000
71	A	1108	PHE	0	0.016	0.014	15.777	-0.034	-0.034	0.000	0.000	0.000	0.000
72	A	1109	VAL	0	-0.019	-0.017	14.190	-0.045	-0.045	0.000	0.000	0.000	0.000
73	A	1110	ASN	0	-0.045	-0.023	13.503	-0.120	-0.120	0.000	0.000	0.000	0.000
74	A	1111	CYS	0	-0.044	-0.006	14.309	-0.027	-0.027	0.000	0.000	0.000	0.000
75	A	1112	VAL	0	-0.036	0.018	11.765	-0.002	-0.002	0.000	0.000	0.000	0.000
76	A	1113	GLN	0	-0.062	-0.051	9.516	-0.174	-0.174	0.000	0.000	0.000	0.000
77	A	1114	SER	0	-0.104	-0.056	8.694	0.010	0.010	0.000	0.000	0.000	0.000
78	A	1115	ILE	0	0.071	0.038	10.928	0.006	0.006	0.000	0.000	0.000	0.000
79	A	1116	LYS	1	0.916	0.955	14.019	0.015	0.015	0.000	0.000	0.000	0.000
80	A	1117	ILE	0	0.021	0.023	16.780	-0.013	-0.013	0.000	0.000	0.000	0.000
81	A	1118	LEU	0	-0.036	-0.012	19.980	0.013	0.013	0.000	0.000	0.000	0.000
82	A	1119	SER	0	0.024	0.003	22.689	-0.004	-0.004	0.000	0.000	0.000	0.000
83	A	1120	SER	0	0.085	0.015	26.069	-0.003	-0.003	0.000	0.000	0.000	0.000
84	A	1121	ALA	0	0.007	0.007	28.875	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	1122	GLU	-1	-0.910	-0.965	21.927	0.031	0.031	0.000	0.000	0.000	0.000
86	A	1123	VAL	0	0.027	0.009	25.527	-0.002	-0.002	0.000	0.000	0.000	0.000
87	A	1124	GLN	0	-0.038	-0.028	26.900	0.001	0.001	0.000	0.000	0.000	0.000
88	A	1125	GLN	0	-0.038	-0.024	27.395	0.002	0.002	0.000	0.000	0.000	0.000
89	A	1126	MET	0	-0.049	-0.003	23.129	0.002	0.002	0.000	0.000	0.000	0.000
90	A	1127	NME	0	-0.010	0.015	26.836	-0.002	-0.002	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:1038:ACE )