FMO DATABASE

FMODB ID: QYVKY

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	OptH
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
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-967151.813932
FMO2-HF: Nuclear repulsion	922750.398154
FMO2-HF: Total energy	-44401.415778
FMO2-MP2: Total energy	-44534.880976

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.
-11.488	-6.07	2.272	-2.987	-4.702	0.011

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 : 0.016 / q_NPA : 0.008

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	-0.011	-0.025	3.193	-2.998	-0.421	0.126	-1.259	-1.444	0.007
4	A	1004	THR	0	0.041	0.022	2.294	-5.405	-3.756	2.053	-1.257	-2.445	0.003
5	A	1005	TYR	0	-0.026	-0.001	3.414	-2.510	-1.318	0.093	-0.471	-0.813	0.001
6	A	1006	VAL	0	-0.012	-0.003	5.951	-0.313	-0.313	0.000	0.000	0.000	0.000
7	A	1007	ASP	-1	-0.820	-0.920	7.621	1.459	1.459	0.000	0.000	0.000	0.000
8	A	1008	THR	0	-0.058	-0.028	7.591	-0.348	-0.348	0.000	0.000	0.000	0.000
9	A	1009	ASN	0	0.006	-0.006	7.090	0.014	0.014	0.000	0.000	0.000	0.000
10	A	1010	LEU	0	-0.008	0.011	9.980	-0.117	-0.117	0.000	0.000	0.000	0.000
11	A	1011	VAL	0	0.011	0.002	11.918	-0.100	-0.100	0.000	0.000	0.000	0.000
12	A	1012	GLY	0	-0.021	-0.006	12.041	-0.086	-0.086	0.000	0.000	0.000	0.000
13	A	1013	THR	0	-0.090	-0.043	13.283	-0.097	-0.097	0.000	0.000	0.000	0.000
14	A	1014	GLY	0	0.021	0.014	15.527	-0.050	-0.050	0.000	0.000	0.000	0.000
15	A	1015	ALA	0	-0.035	-0.020	17.511	-0.032	-0.032	0.000	0.000	0.000	0.000
16	A	1016	VAL	0	-0.023	-0.011	15.067	-0.021	-0.021	0.000	0.000	0.000	0.000
17	A	1017	THR	0	-0.098	-0.044	17.521	0.013	0.013	0.000	0.000	0.000	0.000
18	A	1018	GLN	0	0.022	-0.008	16.252	-0.005	-0.005	0.000	0.000	0.000	0.000
19	A	1019	ALA	0	0.006	-0.004	12.820	-0.037	-0.037	0.000	0.000	0.000	0.000
20	A	1020	ALA	0	0.002	0.010	11.830	0.074	0.074	0.000	0.000	0.000	0.000
21	A	1021	ILE	0	0.003	0.010	7.335	-0.024	-0.024	0.000	0.000	0.000	0.000
22	A	1022	ILE	0	-0.023	0.012	10.987	0.005	0.005	0.000	0.000	0.000	0.000
23	A	1023	GLY	0	0.125	0.070	12.716	0.007	0.007	0.000	0.000	0.000	0.000
24	A	1024	HIS	0	-0.085	-0.054	13.596	-0.024	-0.024	0.000	0.000	0.000	0.000
25	A	1025	ASP	-1	-0.835	-0.907	16.040	0.096	0.096	0.000	0.000	0.000	0.000
26	A	1026	GLY	0	-0.045	-0.025	17.108	-0.006	-0.006	0.000	0.000	0.000	0.000
27	A	1027	ASN	0	-0.030	-0.034	14.990	0.044	0.044	0.000	0.000	0.000	0.000
28	A	1028	THR	0	-0.006	-0.026	11.446	-0.006	-0.006	0.000	0.000	0.000	0.000
29	A	1029	TRP	0	-0.062	-0.025	7.157	-0.087	-0.087	0.000	0.000	0.000	0.000
30	A	1030	ALA	0	-0.008	-0.003	6.456	0.112	0.112	0.000	0.000	0.000	0.000
31	A	1031	THR	0	-0.038	-0.033	8.565	-0.170	-0.170	0.000	0.000	0.000	0.000
32	A	1032	SER	0	0.073	0.055	10.613	0.106	0.106	0.000	0.000	0.000	0.000
33	A	1033	ALA	0	0.017	-0.018	12.355	-0.097	-0.097	0.000	0.000	0.000	0.000
34	A	1034	GLY	0	-0.003	0.001	14.315	-0.049	-0.049	0.000	0.000	0.000	0.000
35	A	1035	PHE	0	-0.052	0.006	14.917	-0.065	-0.065	0.000	0.000	0.000	0.000
36	A	1036	ALA	0	0.039	0.008	15.753	0.050	0.050	0.000	0.000	0.000	0.000
37	A	1037	VAL	0	0.007	0.008	16.452	-0.037	-0.037	0.000	0.000	0.000	0.000
38	A	1038	SER	0	-0.040	-0.002	18.117	-0.001	-0.001	0.000	0.000	0.000	0.000
39	A	1039	PRO	0	0.122	0.040	18.631	0.007	0.007	0.000	0.000	0.000	0.000
40	A	1040	ALA	0	-0.001	0.013	20.099	-0.010	-0.010	0.000	0.000	0.000	0.000
41	A	1041	ASN	0	-0.001	-0.029	22.103	0.008	0.008	0.000	0.000	0.000	0.000
42	A	1042	GLY	0	0.036	0.029	19.064	0.000	0.000	0.000	0.000	0.000	0.000
43	A	1043	ALA	0	0.053	0.035	19.917	-0.001	-0.001	0.000	0.000	0.000	0.000
44	A	1044	ALA	0	-0.009	0.007	21.713	-0.009	-0.009	0.000	0.000	0.000	0.000
45	A	1045	LEU	0	-0.009	-0.004	19.108	-0.008	-0.008	0.000	0.000	0.000	0.000
46	A	1046	ALA	0	0.022	-0.002	19.507	-0.005	-0.005	0.000	0.000	0.000	0.000
47	A	1047	ASN	0	-0.068	-0.048	20.918	-0.011	-0.011	0.000	0.000	0.000	0.000
48	A	1048	ALA	0	0.025	0.021	24.222	-0.011	-0.011	0.000	0.000	0.000	0.000
49	A	1049	PHE	0	-0.023	-0.009	19.703	-0.007	-0.007	0.000	0.000	0.000	0.000
50	A	1050	LYS	1	0.814	0.912	23.685	-0.072	-0.072	0.000	0.000	0.000	0.000
51	A	1051	ASP	-1	-0.809	-0.904	25.891	0.060	0.060	0.000	0.000	0.000	0.000
52	A	1052	ALA	0	0.028	0.014	28.508	0.005	0.005	0.000	0.000	0.000	0.000
53	A	1053	THR	0	-0.025	-0.026	29.412	0.003	0.003	0.000	0.000	0.000	0.000
54	A	1054	ALA	0	0.020	0.005	30.223	0.000	0.000	0.000	0.000	0.000	0.000
55	A	1055	ILE	0	0.035	0.011	26.514	0.001	0.001	0.000	0.000	0.000	0.000
56	A	1056	ARG	1	0.850	0.951	30.188	-0.091	-0.091	0.000	0.000	0.000	0.000
57	A	1057	SER	0	-0.033	0.003	32.694	-0.001	-0.001	0.000	0.000	0.000	0.000
58	A	1058	ASN	0	-0.013	0.000	33.019	-0.003	-0.003	0.000	0.000	0.000	0.000
59	A	1059	GLY	0	0.015	0.000	30.403	0.005	0.005	0.000	0.000	0.000	0.000
60	A	1060	PHE	0	-0.027	-0.028	23.650	-0.002	-0.002	0.000	0.000	0.000	0.000
61	A	1061	GLU	-1	-0.939	-0.982	26.282	0.145	0.145	0.000	0.000	0.000	0.000
62	A	1062	LEU	0	-0.002	-0.010	20.199	0.009	0.009	0.000	0.000	0.000	0.000
63	A	1063	ALA	0	0.018	0.024	20.485	0.004	0.004	0.000	0.000	0.000	0.000
64	A	1064	GLY	0	0.003	0.013	22.563	-0.001	-0.001	0.000	0.000	0.000	0.000
65	A	1065	THR	0	-0.047	-0.008	25.498	-0.021	-0.021	0.000	0.000	0.000	0.000
66	A	1066	ARG	1	0.923	0.965	26.621	-0.117	-0.117	0.000	0.000	0.000	0.000
67	A	1067	TYR	0	-0.053	-0.031	23.334	0.000	0.000	0.000	0.000	0.000	0.000
68	A	1068	VAL	0	0.034	0.018	28.577	-0.008	-0.008	0.000	0.000	0.000	0.000
69	A	1069	THR	0	0.009	-0.017	28.017	0.012	0.012	0.000	0.000	0.000	0.000
70	A	1070	ILE	0	-0.062	-0.003	27.995	-0.011	-0.011	0.000	0.000	0.000	0.000
71	A	1071	ARG	1	0.924	0.954	24.760	-0.162	-0.162	0.000	0.000	0.000	0.000
72	A	1072	ALA	0	-0.013	-0.023	26.183	0.008	0.008	0.000	0.000	0.000	0.000
73	A	1073	ASP	-1	-0.798	-0.876	24.249	0.127	0.127	0.000	0.000	0.000	0.000
74	A	1074	ASP	-1	-0.926	-0.955	24.224	0.097	0.097	0.000	0.000	0.000	0.000
75	A	1075	ARG	1	0.800	0.879	18.008	-0.198	-0.198	0.000	0.000	0.000	0.000
76	A	1076	SER	0	-0.084	-0.075	19.841	0.027	0.027	0.000	0.000	0.000	0.000
77	A	1077	VAL	0	0.025	0.024	21.560	-0.022	-0.022	0.000	0.000	0.000	0.000
78	A	1078	TYR	0	-0.098	-0.036	21.327	0.019	0.019	0.000	0.000	0.000	0.000
79	A	1079	GLY	0	0.061	0.026	24.547	-0.019	-0.019	0.000	0.000	0.000	0.000
80	A	1080	LYS	1	0.937	0.961	26.101	-0.120	-0.120	0.000	0.000	0.000	0.000
81	A	1081	LYS	1	0.990	0.984	28.485	-0.167	-0.167	0.000	0.000	0.000	0.000
82	A	1082	GLY	0	-0.001	0.006	30.142	0.004	0.004	0.000	0.000	0.000	0.000
83	A	1083	SER	0	0.014	0.000	30.289	0.001	0.001	0.000	0.000	0.000	0.000
84	A	1084	ALA	0	-0.005	0.018	26.118	0.009	0.009	0.000	0.000	0.000	0.000
85	A	1085	GLY	0	-0.016	-0.031	25.108	-0.017	-0.017	0.000	0.000	0.000	0.000
86	A	1086	VAL	0	-0.011	0.011	19.843	0.021	0.021	0.000	0.000	0.000	0.000
87	A	1087	ILE	0	0.000	0.003	19.178	-0.029	-0.029	0.000	0.000	0.000	0.000
88	A	1088	THR	0	-0.043	-0.048	17.874	0.036	0.036	0.000	0.000	0.000	0.000
89	A	1089	VAL	0	0.039	0.006	15.900	-0.030	-0.030	0.000	0.000	0.000	0.000
90	A	1090	LYS	1	0.954	1.005	15.658	-0.072	-0.072	0.000	0.000	0.000	0.000
91	A	1091	THR	0	0.013	0.000	11.332	-0.026	-0.026	0.000	0.000	0.000	0.000
92	A	1092	SER	0	-0.019	-0.031	13.305	-0.026	-0.026	0.000	0.000	0.000	0.000
93	A	1093	LYS	1	0.915	0.950	10.476	0.060	0.060	0.000	0.000	0.000	0.000
94	A	1094	ALA	0	0.021	0.018	10.497	-0.005	-0.005	0.000	0.000	0.000	0.000
95	A	1095	ILE	0	-0.034	-0.009	12.429	-0.043	-0.043	0.000	0.000	0.000	0.000
96	A	1096	LEU	0	-0.028	-0.007	10.426	0.078	0.078	0.000	0.000	0.000	0.000
97	A	1097	ILE	0	0.032	0.003	13.574	-0.088	-0.088	0.000	0.000	0.000	0.000
98	A	1098	GLY	0	0.052	0.029	14.910	0.070	0.070	0.000	0.000	0.000	0.000
99	A	1099	VAL	0	-0.010	0.015	16.849	-0.053	-0.053	0.000	0.000	0.000	0.000
100	A	1100	TYR	0	0.036	0.024	19.529	0.026	0.026	0.000	0.000	0.000	0.000
101	A	1101	ASN	0	0.033	-0.007	22.069	-0.019	-0.019	0.000	0.000	0.000	0.000
102	A	1102	GLU	-1	-0.860	-0.966	25.214	0.143	0.143	0.000	0.000	0.000	0.000
103	A	1103	LYS	1	0.901	0.955	25.940	-0.187	-0.187	0.000	0.000	0.000	0.000
104	A	1104	ILE	0	-0.034	0.010	20.955	-0.001	-0.001	0.000	0.000	0.000	0.000
105	A	1105	GLN	0	0.035	0.026	25.194	-0.010	-0.010	0.000	0.000	0.000	0.000
106	A	1106	PRO	0	0.054	0.027	24.491	0.013	0.013	0.000	0.000	0.000	0.000
107	A	1107	GLY	0	0.041	0.009	23.725	0.014	0.014	0.000	0.000	0.000	0.000
108	A	1108	THR	0	-0.039	-0.022	21.284	0.000	0.000	0.000	0.000	0.000	0.000
109	A	1109	ALA	0	0.043	0.017	19.634	0.021	0.021	0.000	0.000	0.000	0.000
110	A	1110	ALA	0	-0.032	-0.016	18.934	0.029	0.029	0.000	0.000	0.000	0.000
111	A	1111	ASN	0	0.003	-0.002	19.593	0.007	0.007	0.000	0.000	0.000	0.000
112	A	1112	VAL	0	-0.029	-0.001	14.674	0.011	0.011	0.000	0.000	0.000	0.000
113	A	1113	VAL	0	0.023	0.003	14.752	0.040	0.040	0.000	0.000	0.000	0.000
114	A	1114	GLU	-1	-0.738	-0.860	14.978	0.258	0.258	0.000	0.000	0.000	0.000
115	A	1115	LYS	1	0.953	0.997	15.187	-0.260	-0.260	0.000	0.000	0.000	0.000
116	A	1116	LEU	0	-0.036	-0.017	8.534	0.002	0.002	0.000	0.000	0.000	0.000
117	A	1117	ALA	0	0.024	-0.006	11.189	0.067	0.067	0.000	0.000	0.000	0.000
118	A	1118	ASP	-1	-0.833	-0.891	13.176	0.189	0.189	0.000	0.000	0.000	0.000
119	A	1119	TYR	0	-0.043	-0.015	6.890	-0.148	-0.148	0.000	0.000	0.000	0.000
120	A	1120	LEU	0	0.003	-0.005	6.555	-0.023	-0.023	0.000	0.000	0.000	0.000
121	A	1121	ILE	0	-0.012	-0.014	9.768	-0.122	-0.122	0.000	0.000	0.000	0.000
122	A	1122	GLY	0	-0.022	0.000	12.996	-0.064	-0.064	0.000	0.000	0.000	0.000
123	A	1123	GLN	0	-0.046	-0.018	7.556	-0.022	-0.022	0.000	0.000	0.000	0.000
124	A	1124	GLY	0	-0.020	-0.002	9.448	-0.133	-0.133	0.000	0.000	0.000	0.000
125	A	1125	PHE	0	-0.031	-0.001	6.039	0.036	0.036	0.000	0.000	0.000	0.000

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