FMO DATABASE

FMODB ID: 94JY2

Calculation Name: 1FTF-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1FTF

Chain ID: A

ChEMBL ID:

UniProt ID: P0A2W6

Base Structure: X-ray

Registration Date: 2023-09-20

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

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
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	116
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-937200.658564
FMO2-HF: Nuclear repulsion	892166.033216
FMO2-HF: Total energy	-45034.625349
FMO2-MP2: Total energy	-45167.026025

3D Structure Molmil

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:1003:MET)

Summations of interaction energy for fragment #1(A:1003: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.
-6.521	-3.8	11.163	-5.186	-8.698	-0.022

Interaction energy analysis for fragmet #1(A:1003:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.012 / 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	1005	VAL	0	-0.036	-0.025	2.768	-3.835	-0.281	0.771	-1.658	-2.668	-0.005
4	A	1006	GLY	0	0.056	0.031	4.640	0.636	0.803	-0.001	-0.018	-0.147	0.000
5	A	1007	HIS	0	-0.094	-0.061	8.172	0.067	0.067	0.000	0.000	0.000	0.000
6	A	1008	GLY	0	0.041	0.034	11.110	0.046	0.046	0.000	0.000	0.000	0.000
7	A	1009	ILE	0	-0.029	-0.011	14.745	0.015	0.015	0.000	0.000	0.000	0.000
8	A	1010	ASP	-1	-0.863	-0.949	18.062	-0.176	-0.176	0.000	0.000	0.000	0.000
9	A	1011	ILE	0	-0.012	0.001	21.643	0.011	0.011	0.000	0.000	0.000	0.000
10	A	1012	GLU	-1	-0.850	-0.924	25.130	-0.114	-0.114	0.000	0.000	0.000	0.000
11	A	1013	GLU	-1	-0.956	-0.973	28.203	-0.051	-0.051	0.000	0.000	0.000	0.000
12	A	1014	LEU	0	-0.006	-0.012	30.967	-0.006	-0.006	0.000	0.000	0.000	0.000
13	A	1015	ALA	0	0.060	0.038	33.497	-0.002	-0.002	0.000	0.000	0.000	0.000
14	A	1016	SER	0	0.023	0.022	32.866	0.003	0.003	0.000	0.000	0.000	0.000
15	A	1017	ILE	0	0.015	0.011	30.000	-0.003	-0.003	0.000	0.000	0.000	0.000
16	A	1018	GLU	-1	-0.949	-0.984	33.917	-0.064	-0.064	0.000	0.000	0.000	0.000
17	A	1019	SER	0	-0.050	-0.041	37.371	0.004	0.004	0.000	0.000	0.000	0.000
18	A	1020	ALA	0	-0.070	-0.038	35.103	0.002	0.002	0.000	0.000	0.000	0.000
19	A	1021	VAL	0	-0.032	-0.020	35.793	-0.002	-0.002	0.000	0.000	0.000	0.000
20	A	1022	THR	0	-0.038	-0.016	38.174	0.003	0.003	0.000	0.000	0.000	0.000
21	A	1023	ARG	1	0.865	0.958	38.488	0.077	0.077	0.000	0.000	0.000	0.000
22	A	1024	HIS	0	0.023	0.008	36.852	0.005	0.005	0.000	0.000	0.000	0.000
23	A	1025	GLU	-1	-0.880	-0.945	39.016	-0.097	-0.097	0.000	0.000	0.000	0.000
24	A	1026	GLY	0	-0.016	-0.013	37.769	-0.005	-0.005	0.000	0.000	0.000	0.000
25	A	1027	PHE	0	-0.011	-0.008	31.107	-0.009	-0.009	0.000	0.000	0.000	0.000
26	A	1028	ALA	0	0.080	0.035	33.037	-0.010	-0.010	0.000	0.000	0.000	0.000
27	A	1029	LYS	1	0.999	0.989	32.335	0.125	0.125	0.000	0.000	0.000	0.000
28	A	1030	ARG	1	0.900	0.963	29.781	0.142	0.142	0.000	0.000	0.000	0.000
29	A	1031	VAL	0	-0.018	0.002	27.378	-0.014	-0.014	0.000	0.000	0.000	0.000
30	A	1032	LEU	0	-0.023	-0.007	27.511	-0.017	-0.017	0.000	0.000	0.000	0.000
31	A	1033	THR	0	0.044	0.016	25.826	0.012	0.012	0.000	0.000	0.000	0.000
32	A	1034	ALA	0	-0.017	-0.021	29.049	0.013	0.013	0.000	0.000	0.000	0.000
33	A	1035	LEU	0	0.062	0.039	26.814	0.012	0.012	0.000	0.000	0.000	0.000
34	A	1036	GLU	-1	-0.730	-0.842	25.027	-0.225	-0.225	0.000	0.000	0.000	0.000
35	A	1037	MET	0	-0.047	-0.023	29.313	0.014	0.014	0.000	0.000	0.000	0.000
36	A	1038	GLU	-1	-0.901	-0.933	32.581	-0.129	-0.129	0.000	0.000	0.000	0.000
37	A	1039	ARG	1	0.946	0.988	29.347	0.122	0.122	0.000	0.000	0.000	0.000
38	A	1040	PHE	0	0.015	-0.005	32.364	0.010	0.010	0.000	0.000	0.000	0.000
39	A	1041	THR	0	-0.057	-0.042	33.730	0.011	0.011	0.000	0.000	0.000	0.000
40	A	1042	SER	0	-0.015	0.004	35.629	0.008	0.008	0.000	0.000	0.000	0.000
41	A	1043	LEU	0	-0.128	-0.042	32.370	0.007	0.007	0.000	0.000	0.000	0.000
42	A	1044	LYS	1	0.989	0.979	37.042	0.064	0.064	0.000	0.000	0.000	0.000
43	A	1045	GLY	0	0.016	0.004	38.410	0.000	0.000	0.000	0.000	0.000	0.000
44	A	1046	ARG	1	1.033	1.010	37.060	0.041	0.041	0.000	0.000	0.000	0.000
45	A	1047	ARG	1	0.985	0.995	33.910	0.056	0.056	0.000	0.000	0.000	0.000
46	A	1048	GLN	0	-0.032	-0.006	33.439	-0.001	-0.001	0.000	0.000	0.000	0.000
47	A	1049	ILE	0	0.041	0.015	33.829	-0.009	-0.009	0.000	0.000	0.000	0.000
48	A	1050	GLU	-1	-0.850	-0.940	28.636	-0.105	-0.105	0.000	0.000	0.000	0.000
49	A	1051	TYR	0	-0.039	-0.017	27.490	-0.010	-0.010	0.000	0.000	0.000	0.000
50	A	1052	LEU	0	-0.009	-0.008	28.538	-0.014	-0.014	0.000	0.000	0.000	0.000
51	A	1053	ALA	0	0.035	0.020	28.672	-0.014	-0.014	0.000	0.000	0.000	0.000
52	A	1054	GLY	0	0.044	0.024	25.883	-0.010	-0.010	0.000	0.000	0.000	0.000
53	A	1055	ARG	1	0.803	0.890	24.229	0.166	0.166	0.000	0.000	0.000	0.000
54	A	1056	TRP	0	-0.018	-0.004	24.094	-0.029	-0.029	0.000	0.000	0.000	0.000
55	A	1057	SER	0	-0.001	-0.011	23.622	-0.020	-0.020	0.000	0.000	0.000	0.000
56	A	1058	ALA	0	0.007	-0.009	20.169	-0.020	-0.020	0.000	0.000	0.000	0.000
57	A	1059	LYS	1	0.775	0.877	19.184	0.209	0.209	0.000	0.000	0.000	0.000
58	A	1060	GLU	-1	-0.868	-0.935	19.690	-0.261	-0.261	0.000	0.000	0.000	0.000
59	A	1061	ALA	0	-0.044	-0.027	17.387	-0.022	-0.022	0.000	0.000	0.000	0.000
60	A	1062	PHE	0	0.049	0.004	13.640	-0.049	-0.049	0.000	0.000	0.000	0.000
61	A	1063	SER	0	0.003	-0.003	14.752	-0.084	-0.084	0.000	0.000	0.000	0.000
62	A	1064	LYS	1	0.915	0.966	15.842	0.182	0.182	0.000	0.000	0.000	0.000
63	A	1065	ALA	0	-0.039	0.003	11.432	-0.010	-0.010	0.000	0.000	0.000	0.000
64	A	1066	MET	0	-0.029	-0.014	10.813	-0.113	-0.113	0.000	0.000	0.000	0.000
65	A	1067	GLY	0	-0.010	0.018	12.550	0.025	0.025	0.000	0.000	0.000	0.000
66	A	1068	THR	0	-0.083	-0.043	14.172	0.081	0.081	0.000	0.000	0.000	0.000
67	A	1069	GLY	0	0.044	0.016	17.689	0.004	0.004	0.000	0.000	0.000	0.000
68	A	1070	ILE	0	0.094	0.036	20.766	-0.021	-0.021	0.000	0.000	0.000	0.000
69	A	1071	SER	0	-0.087	-0.041	22.159	-0.005	-0.005	0.000	0.000	0.000	0.000
70	A	1072	LYS	1	0.878	0.949	17.669	0.366	0.366	0.000	0.000	0.000	0.000
71	A	1073	LEU	0	-0.032	-0.015	16.707	-0.007	-0.007	0.000	0.000	0.000	0.000
72	A	1074	GLY	0	0.060	0.039	20.676	0.009	0.009	0.000	0.000	0.000	0.000
73	A	1075	PHE	0	-0.007	-0.026	22.813	-0.018	-0.018	0.000	0.000	0.000	0.000
74	A	1076	GLN	0	-0.073	-0.060	24.384	-0.017	-0.017	0.000	0.000	0.000	0.000
75	A	1077	ASP	-1	-0.949	-0.950	20.287	-0.393	-0.393	0.000	0.000	0.000	0.000
76	A	1078	LEU	0	-0.041	-0.015	17.794	-0.044	-0.044	0.000	0.000	0.000	0.000
77	A	1079	GLU	-1	-0.802	-0.874	21.003	-0.217	-0.217	0.000	0.000	0.000	0.000
78	A	1080	VAL	0	-0.003	-0.001	20.500	-0.027	-0.027	0.000	0.000	0.000	0.000
79	A	1081	LEU	0	0.012	0.026	21.941	0.038	0.038	0.000	0.000	0.000	0.000
80	A	1082	ASN	0	-0.038	-0.043	22.454	-0.010	-0.010	0.000	0.000	0.000	0.000
81	A	1083	ASN	0	0.085	0.045	18.887	0.024	0.024	0.000	0.000	0.000	0.000
82	A	1084	GLU	-1	-0.875	-0.941	22.491	-0.122	-0.122	0.000	0.000	0.000	0.000
83	A	1085	ARG	1	0.837	0.928	21.518	0.073	0.073	0.000	0.000	0.000	0.000
84	A	1086	GLY	0	0.023	0.003	23.941	0.015	0.015	0.000	0.000	0.000	0.000
85	A	1087	ALA	0	-0.025	-0.001	20.225	0.003	0.003	0.000	0.000	0.000	0.000
86	A	1088	PRO	0	-0.030	-0.013	20.386	-0.014	-0.014	0.000	0.000	0.000	0.000
87	A	1089	TYR	0	0.002	-0.005	17.175	-0.001	-0.001	0.000	0.000	0.000	0.000
88	A	1090	PHE	0	0.035	-0.003	15.955	0.017	0.017	0.000	0.000	0.000	0.000
89	A	1091	SER	0	-0.074	-0.055	17.360	-0.038	-0.038	0.000	0.000	0.000	0.000
90	A	1092	GLN	0	-0.006	-0.001	19.763	-0.033	-0.033	0.000	0.000	0.000	0.000
91	A	1093	ALA	0	0.065	0.009	15.607	0.018	0.018	0.000	0.000	0.000	0.000
92	A	1094	PRO	0	-0.009	0.025	14.944	-0.048	-0.048	0.000	0.000	0.000	0.000
93	A	1095	PHE	0	-0.029	-0.035	6.658	0.001	0.001	0.000	0.000	0.000	0.000
94	A	1096	SER	0	-0.007	-0.007	9.721	0.160	0.160	0.000	0.000	0.000	0.000
95	A	1097	GLY	0	0.063	0.051	7.534	0.086	0.086	0.000	0.000	0.000	0.000
96	A	1098	LYS	1	0.843	0.925	4.530	2.225	2.324	-0.001	-0.005	-0.093	0.000
97	A	1099	ILE	0	0.003	0.008	8.386	-0.216	-0.216	0.000	0.000	0.000	0.000
98	A	1100	TRP	0	-0.087	-0.040	7.250	0.152	0.152	0.000	0.000	0.000	0.000
99	A	1101	LEU	0	0.010	0.000	11.939	-0.026	-0.026	0.000	0.000	0.000	0.000
100	A	1102	SER	0	-0.057	-0.024	15.550	0.047	0.047	0.000	0.000	0.000	0.000
101	A	1103	ILE	0	0.010	0.000	18.409	-0.017	-0.017	0.000	0.000	0.000	0.000
102	A	1104	SER	0	-0.045	-0.015	21.932	0.016	0.016	0.000	0.000	0.000	0.000
103	A	1105	HIS	0	-0.004	0.008	24.900	-0.002	-0.002	0.000	0.000	0.000	0.000
104	A	1106	THR	0	0.023	0.019	28.433	0.007	0.007	0.000	0.000	0.000	0.000
105	A	1107	ASP	-1	-0.908	-0.967	31.861	-0.044	-0.044	0.000	0.000	0.000	0.000
106	A	1108	GLN	0	-0.068	-0.045	33.740	0.001	0.001	0.000	0.000	0.000	0.000
107	A	1109	PHE	0	0.007	0.005	29.196	-0.002	-0.002	0.000	0.000	0.000	0.000
108	A	1110	VAL	0	0.028	0.023	25.779	0.004	0.004	0.000	0.000	0.000	0.000
109	A	1111	THR	0	-0.054	-0.027	22.990	0.002	0.002	0.000	0.000	0.000	0.000
110	A	1112	ALA	0	0.034	0.012	20.144	0.000	0.000	0.000	0.000	0.000	0.000
111	A	1113	SER	0	-0.043	-0.023	15.614	-0.017	-0.017	0.000	0.000	0.000	0.000
112	A	1114	VAL	0	0.058	0.015	12.484	0.005	0.005	0.000	0.000	0.000	0.000
113	A	1115	ILE	0	-0.048	-0.014	7.855	0.001	0.001	0.000	0.000	0.000	0.000
114	A	1116	LEU	0	0.017	0.022	7.710	0.103	0.103	0.000	0.000	0.000	0.000
115	A	1117	GLU	-1	-0.880	-0.939	3.003	0.639	1.662	0.101	-0.325	-0.799	0.001
116	A	1118	GLU	-1	-0.931	-0.972	1.938	-5.837	-7.959	10.293	-3.180	-4.991	-0.018

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Interactive mode: IFIE and PIEDA for fragment #1(A:1003:MET)