FMO DATABASE

FMODB ID: K9GK3

Calculation Name: 1F2K-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1F2K

Chain ID: A

ChEMBL ID:

UniProt ID: P19984

Base Structure: X-ray

Registration Date: 2023-06-22

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	125
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-966842.67093
FMO2-HF: Nuclear repulsion	922440.482289
FMO2-HF: Total energy	-44402.188641
FMO2-MP2: Total energy	-44535.544412

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:SER)

Summations of interaction energy for fragment #1(A:1001: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.
-7.99	-2.308	2.323	-3.119	-4.884	-0.007

Interaction energy analysis for fragmet #1(A:1001: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 : 0.002

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	1003	GLN	0	0.002	-0.025	3.199	-3.589	-1.179	0.108	-1.145	-1.372	0.005
4	A	1004	THR	0	0.031	0.021	2.333	-3.732	-1.695	2.123	-1.507	-2.652	-0.013
5	A	1005	TYR	0	-0.025	-0.005	3.508	-0.790	0.445	0.092	-0.467	-0.860	0.001
6	A	1006	VAL	0	0.005	0.007	5.976	0.132	0.132	0.000	0.000	0.000	0.000
7	A	1007	ASP	-1	-0.806	-0.916	6.858	0.136	0.136	0.000	0.000	0.000	0.000
8	A	1008	THR	0	-0.066	-0.031	7.401	0.016	0.016	0.000	0.000	0.000	0.000
9	A	1009	ASN	0	-0.006	-0.014	7.359	-0.017	-0.017	0.000	0.000	0.000	0.000
10	A	1010	LEU	0	-0.015	0.007	10.001	0.059	0.059	0.000	0.000	0.000	0.000
11	A	1011	VAL	0	0.017	0.002	11.597	-0.011	-0.011	0.000	0.000	0.000	0.000
12	A	1012	GLY	0	-0.012	-0.002	11.604	0.001	0.001	0.000	0.000	0.000	0.000
13	A	1013	THR	0	-0.092	-0.049	13.035	0.005	0.005	0.000	0.000	0.000	0.000
14	A	1014	GLY	0	0.019	0.015	15.543	0.001	0.001	0.000	0.000	0.000	0.000
15	A	1015	ALA	0	-0.042	-0.022	17.495	0.009	0.009	0.000	0.000	0.000	0.000
16	A	1016	VAL	0	-0.023	-0.007	15.111	0.014	0.014	0.000	0.000	0.000	0.000
17	A	1017	THR	0	-0.027	-0.032	17.110	-0.014	-0.014	0.000	0.000	0.000	0.000
18	A	1018	GLN	0	-0.027	-0.021	15.592	-0.007	-0.007	0.000	0.000	0.000	0.000
19	A	1019	ALA	0	0.002	0.001	12.475	-0.012	-0.012	0.000	0.000	0.000	0.000
20	A	1020	ALA	0	-0.001	0.007	11.723	0.029	0.029	0.000	0.000	0.000	0.000
21	A	1021	ILE	0	-0.002	0.008	7.389	-0.037	-0.037	0.000	0.000	0.000	0.000
22	A	1022	ILE	0	-0.006	0.010	11.001	0.083	0.083	0.000	0.000	0.000	0.000
23	A	1023	GLY	0	0.121	0.074	12.827	0.012	0.012	0.000	0.000	0.000	0.000
24	A	1024	HIS	0	-0.086	-0.055	13.605	-0.060	-0.060	0.000	0.000	0.000	0.000
25	A	1025	ASP	-1	-0.836	-0.907	15.860	0.281	0.281	0.000	0.000	0.000	0.000
26	A	1026	GLY	0	-0.041	-0.032	17.112	-0.016	-0.016	0.000	0.000	0.000	0.000
27	A	1027	ASN	0	-0.042	-0.034	15.026	0.007	0.007	0.000	0.000	0.000	0.000
28	A	1028	THR	0	-0.023	-0.030	11.833	0.016	0.016	0.000	0.000	0.000	0.000
29	A	1029	TRP	0	-0.040	-0.013	7.398	-0.001	-0.001	0.000	0.000	0.000	0.000
30	A	1030	ALA	0	-0.001	0.005	6.626	0.362	0.362	0.000	0.000	0.000	0.000
31	A	1031	THR	0	-0.036	-0.046	8.725	-0.227	-0.227	0.000	0.000	0.000	0.000
32	A	1032	SER	0	0.058	0.057	10.163	0.017	0.017	0.000	0.000	0.000	0.000
33	A	1033	ALA	0	0.023	-0.017	11.772	0.016	0.016	0.000	0.000	0.000	0.000
34	A	1034	GLY	0	-0.003	0.001	13.677	-0.031	-0.031	0.000	0.000	0.000	0.000
35	A	1035	PHE	0	-0.050	0.008	14.701	-0.032	-0.032	0.000	0.000	0.000	0.000
36	A	1036	ALA	0	0.028	0.011	15.414	0.052	0.052	0.000	0.000	0.000	0.000
37	A	1037	VAL	0	-0.007	0.001	16.400	-0.039	-0.039	0.000	0.000	0.000	0.000
38	A	1038	SER	0	-0.017	-0.018	18.209	0.025	0.025	0.000	0.000	0.000	0.000
39	A	1039	PRO	0	0.113	0.040	18.817	-0.001	-0.001	0.000	0.000	0.000	0.000
40	A	1040	ALA	0	-0.009	0.010	20.114	-0.009	-0.009	0.000	0.000	0.000	0.000
41	A	1041	ASN	0	-0.005	-0.006	22.017	0.001	0.001	0.000	0.000	0.000	0.000
42	A	1042	GLY	0	0.043	0.031	19.077	-0.006	-0.006	0.000	0.000	0.000	0.000
43	A	1043	ALA	0	0.039	0.029	19.930	-0.002	-0.002	0.000	0.000	0.000	0.000
44	A	1044	ALA	0	-0.004	0.012	21.724	-0.011	-0.011	0.000	0.000	0.000	0.000
45	A	1045	LEU	0	-0.010	-0.007	19.161	-0.010	-0.010	0.000	0.000	0.000	0.000
46	A	1046	ALA	0	0.026	-0.002	19.451	-0.007	-0.007	0.000	0.000	0.000	0.000
47	A	1047	ASN	0	-0.073	-0.049	21.028	-0.015	-0.015	0.000	0.000	0.000	0.000
48	A	1048	ALA	0	0.016	0.017	24.362	-0.012	-0.012	0.000	0.000	0.000	0.000
49	A	1049	PHE	0	-0.004	0.001	19.526	-0.007	-0.007	0.000	0.000	0.000	0.000
50	A	1050	LYS	1	0.797	0.899	23.789	-0.104	-0.104	0.000	0.000	0.000	0.000
51	A	1051	ASP	-1	-0.793	-0.892	25.992	0.071	0.071	0.000	0.000	0.000	0.000
52	A	1052	ALA	0	0.026	0.019	28.515	0.003	0.003	0.000	0.000	0.000	0.000
53	A	1053	THR	0	-0.038	-0.036	29.519	-0.003	-0.003	0.000	0.000	0.000	0.000
54	A	1054	ALA	0	0.026	0.008	30.353	-0.003	-0.003	0.000	0.000	0.000	0.000
55	A	1055	ILE	0	0.043	0.012	26.391	-0.002	-0.002	0.000	0.000	0.000	0.000
56	A	1056	ARG	1	0.845	0.941	30.224	-0.081	-0.081	0.000	0.000	0.000	0.000
57	A	1057	SER	0	-0.017	0.006	32.802	-0.003	-0.003	0.000	0.000	0.000	0.000
58	A	1058	ASN	0	-0.040	-0.012	33.096	-0.005	-0.005	0.000	0.000	0.000	0.000
59	A	1059	GLY	0	0.021	0.010	30.467	0.002	0.002	0.000	0.000	0.000	0.000
60	A	1060	PHE	0	-0.013	-0.025	23.266	0.004	0.004	0.000	0.000	0.000	0.000
61	A	1061	GLU	-1	-0.855	-0.919	26.282	0.111	0.111	0.000	0.000	0.000	0.000
62	A	1062	LEU	0	-0.014	-0.022	19.774	0.014	0.014	0.000	0.000	0.000	0.000
63	A	1063	ALA	0	0.026	0.028	20.194	-0.008	-0.008	0.000	0.000	0.000	0.000
64	A	1064	GLY	0	0.009	0.017	22.311	-0.011	-0.011	0.000	0.000	0.000	0.000
65	A	1065	THR	0	-0.048	-0.013	25.145	-0.017	-0.017	0.000	0.000	0.000	0.000
66	A	1066	ARG	1	0.839	0.905	26.497	-0.087	-0.087	0.000	0.000	0.000	0.000
67	A	1067	TYR	0	-0.032	-0.025	22.977	-0.009	-0.009	0.000	0.000	0.000	0.000
68	A	1068	VAL	0	0.038	0.018	28.577	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	1069	THR	0	0.008	-0.014	28.289	0.005	0.005	0.000	0.000	0.000	0.000
70	A	1070	ILE	0	-0.069	-0.017	27.604	-0.008	-0.008	0.000	0.000	0.000	0.000
71	A	1071	ARG	1	0.825	0.889	24.405	-0.105	-0.105	0.000	0.000	0.000	0.000
72	A	1072	ALA	0	0.003	-0.017	26.282	0.007	0.007	0.000	0.000	0.000	0.000
73	A	1073	ASP	-1	-0.775	-0.862	24.550	0.096	0.096	0.000	0.000	0.000	0.000
74	A	1074	ASP	-1	-0.932	-0.956	24.404	0.104	0.104	0.000	0.000	0.000	0.000
75	A	1075	ARG	1	0.770	0.857	18.377	-0.136	-0.136	0.000	0.000	0.000	0.000
76	A	1076	SER	0	-0.050	-0.068	19.935	0.027	0.027	0.000	0.000	0.000	0.000
77	A	1077	VAL	0	0.019	0.022	21.659	-0.015	-0.015	0.000	0.000	0.000	0.000
78	A	1078	TYR	0	-0.076	-0.041	21.539	0.004	0.004	0.000	0.000	0.000	0.000
79	A	1079	GLY	0	0.065	0.032	24.606	-0.007	-0.007	0.000	0.000	0.000	0.000
80	A	1080	LYS	1	0.936	0.961	26.101	-0.064	-0.064	0.000	0.000	0.000	0.000
81	A	1081	LYS	1	0.956	0.969	28.408	-0.088	-0.088	0.000	0.000	0.000	0.000
82	A	1082	GLY	0	0.006	0.011	29.940	-0.001	-0.001	0.000	0.000	0.000	0.000
83	A	1083	SER	0	-0.021	-0.022	29.933	0.001	0.001	0.000	0.000	0.000	0.000
84	A	1084	ALA	0	-0.001	0.020	25.854	0.000	0.000	0.000	0.000	0.000	0.000
85	A	1085	GLY	0	-0.006	-0.020	24.948	-0.004	-0.004	0.000	0.000	0.000	0.000
86	A	1086	VAL	0	-0.029	-0.001	19.779	0.005	0.005	0.000	0.000	0.000	0.000
87	A	1087	ILE	0	-0.002	0.004	19.270	-0.008	-0.008	0.000	0.000	0.000	0.000
88	A	1088	THR	0	-0.046	-0.042	17.973	0.023	0.023	0.000	0.000	0.000	0.000
89	A	1089	VAL	0	0.031	0.004	16.136	-0.021	-0.021	0.000	0.000	0.000	0.000
90	A	1090	LYS	1	0.944	1.000	15.759	-0.124	-0.124	0.000	0.000	0.000	0.000
91	A	1091	THR	0	0.010	-0.008	11.500	-0.017	-0.017	0.000	0.000	0.000	0.000
92	A	1092	SER	0	-0.031	-0.028	13.433	-0.026	-0.026	0.000	0.000	0.000	0.000
93	A	1093	LYS	1	0.889	0.928	10.502	-0.143	-0.143	0.000	0.000	0.000	0.000
94	A	1094	ALA	0	0.022	0.019	10.533	0.018	0.018	0.000	0.000	0.000	0.000
95	A	1095	ILE	0	-0.018	-0.001	12.533	-0.067	-0.067	0.000	0.000	0.000	0.000
96	A	1096	LEU	0	-0.028	-0.006	10.488	0.067	0.067	0.000	0.000	0.000	0.000
97	A	1097	ILE	0	0.013	-0.006	13.679	-0.061	-0.061	0.000	0.000	0.000	0.000
98	A	1098	GLY	0	0.059	0.032	14.910	0.016	0.016	0.000	0.000	0.000	0.000
99	A	1099	VAL	0	-0.016	0.001	16.849	-0.016	-0.016	0.000	0.000	0.000	0.000
100	A	1100	TYR	0	0.032	0.036	19.223	-0.005	-0.005	0.000	0.000	0.000	0.000
101	A	1101	ASN	0	0.028	-0.002	21.796	-0.003	-0.003	0.000	0.000	0.000	0.000
102	A	1102	GLU	-1	-0.794	-0.926	24.741	0.043	0.043	0.000	0.000	0.000	0.000
103	A	1103	LYS	1	0.851	0.927	25.642	-0.044	-0.044	0.000	0.000	0.000	0.000
104	A	1104	ILE	0	-0.028	0.007	21.007	-0.004	-0.004	0.000	0.000	0.000	0.000
105	A	1105	GLN	0	0.033	0.024	25.106	0.006	0.006	0.000	0.000	0.000	0.000
106	A	1106	PRO	0	0.053	0.031	24.516	0.003	0.003	0.000	0.000	0.000	0.000
107	A	1107	GLY	0	0.038	0.008	23.752	0.007	0.007	0.000	0.000	0.000	0.000
108	A	1108	THR	0	-0.020	-0.024	21.272	0.001	0.001	0.000	0.000	0.000	0.000
109	A	1109	ALA	0	0.035	0.022	19.663	0.002	0.002	0.000	0.000	0.000	0.000
110	A	1110	ALA	0	-0.038	-0.019	18.963	0.015	0.015	0.000	0.000	0.000	0.000
111	A	1111	ASN	0	0.002	-0.001	19.623	0.015	0.015	0.000	0.000	0.000	0.000
112	A	1112	VAL	0	-0.019	0.003	14.516	0.012	0.012	0.000	0.000	0.000	0.000
113	A	1113	VAL	0	0.026	0.002	14.775	0.022	0.022	0.000	0.000	0.000	0.000
114	A	1114	GLU	-1	-0.714	-0.803	15.052	0.178	0.178	0.000	0.000	0.000	0.000
115	A	1115	LYS	1	0.960	0.995	15.103	-0.059	-0.059	0.000	0.000	0.000	0.000
116	A	1116	LEU	0	-0.032	-0.016	8.438	0.008	0.008	0.000	0.000	0.000	0.000
117	A	1117	ALA	0	0.016	0.001	11.248	0.096	0.096	0.000	0.000	0.000	0.000
118	A	1118	ASP	-1	-0.793	-0.870	13.238	0.158	0.158	0.000	0.000	0.000	0.000
119	A	1119	TYR	0	-0.046	-0.011	6.556	-0.204	-0.204	0.000	0.000	0.000	0.000
120	A	1120	LEU	0	0.009	-0.001	6.339	0.036	0.036	0.000	0.000	0.000	0.000
121	A	1121	ILE	0	-0.036	-0.022	9.819	-0.062	-0.062	0.000	0.000	0.000	0.000
122	A	1122	GLY	0	-0.012	0.005	13.058	-0.043	-0.043	0.000	0.000	0.000	0.000
123	A	1123	GLN	0	-0.047	-0.023	7.540	-0.081	-0.081	0.000	0.000	0.000	0.000
124	A	1124	GLY	0	-0.002	0.009	9.482	-0.075	-0.075	0.000	0.000	0.000	0.000
125	A	1125	PHE	0	0.008	0.023	6.569	0.076	0.076	0.000	0.000	0.000	0.000

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