FMO DATABASE

FMODB ID: 49JQN

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

Total energy (hartree)

FMO2-HF: Electronic energy	-966473.357259
FMO2-HF: Nuclear repulsion	922070.649724
FMO2-HF: Total energy	-44402.707535
FMO2-MP2: Total energy	-44535.96088

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.
-9.229	-5.711	4.705	-3.207	-5.015	-0.018

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	0.028	-0.021	3.900	-2.088	-0.589	0.001	-0.657	-0.842	0.002
4	A	1004	THR	0	0.015	0.010	2.140	-4.885	-4.668	4.295	-1.741	-2.772	-0.022
5	A	1005	TYR	0	-0.007	-0.006	2.967	-2.260	-0.458	0.409	-0.809	-1.401	0.002
6	A	1006	VAL	0	-0.008	0.001	5.912	0.200	0.200	0.000	0.000	0.000	0.000
7	A	1007	ASP	-1	-0.772	-0.899	7.376	0.133	0.133	0.000	0.000	0.000	0.000
8	A	1008	THR	0	-0.059	-0.021	7.543	0.027	0.027	0.000	0.000	0.000	0.000
9	A	1009	ASN	0	-0.033	-0.031	7.438	-0.053	-0.053	0.000	0.000	0.000	0.000
10	A	1010	LEU	0	-0.006	0.015	9.930	0.082	0.082	0.000	0.000	0.000	0.000
11	A	1011	VAL	0	0.002	0.009	11.805	-0.008	-0.008	0.000	0.000	0.000	0.000
12	A	1012	GLY	0	0.012	0.012	11.958	0.006	0.006	0.000	0.000	0.000	0.000
13	A	1013	THR	0	-0.060	-0.037	13.314	0.008	0.008	0.000	0.000	0.000	0.000
14	A	1014	GLY	0	-0.007	0.003	15.674	0.006	0.006	0.000	0.000	0.000	0.000
15	A	1015	ALA	0	-0.046	-0.026	17.357	0.009	0.009	0.000	0.000	0.000	0.000
16	A	1016	VAL	0	-0.024	-0.020	15.323	0.016	0.016	0.000	0.000	0.000	0.000
17	A	1017	THR	0	0.001	-0.003	16.921	-0.014	-0.014	0.000	0.000	0.000	0.000
18	A	1018	GLN	0	-0.030	-0.011	15.620	-0.007	-0.007	0.000	0.000	0.000	0.000
19	A	1019	ALA	0	0.016	0.005	12.513	-0.007	-0.007	0.000	0.000	0.000	0.000
20	A	1020	ALA	0	-0.010	-0.004	11.499	0.012	0.012	0.000	0.000	0.000	0.000
21	A	1021	ILE	0	-0.017	0.000	6.944	0.000	0.000	0.000	0.000	0.000	0.000
22	A	1022	ILE	0	0.002	0.009	10.545	0.048	0.048	0.000	0.000	0.000	0.000
23	A	1023	GLY	0	0.080	0.042	12.406	0.005	0.005	0.000	0.000	0.000	0.000
24	A	1024	HIS	0	-0.077	-0.054	13.186	-0.046	-0.046	0.000	0.000	0.000	0.000
25	A	1025	ASP	-1	-0.830	-0.900	15.426	0.206	0.206	0.000	0.000	0.000	0.000
26	A	1026	GLY	0	-0.001	0.000	16.711	-0.015	-0.015	0.000	0.000	0.000	0.000
27	A	1027	ASN	0	-0.070	-0.056	14.522	0.011	0.011	0.000	0.000	0.000	0.000
28	A	1028	THR	0	-0.015	-0.020	11.838	0.022	0.022	0.000	0.000	0.000	0.000
29	A	1029	TRP	0	-0.028	-0.002	6.947	-0.022	-0.022	0.000	0.000	0.000	0.000
30	A	1030	ALA	0	-0.004	0.001	6.712	0.297	0.297	0.000	0.000	0.000	0.000
31	A	1031	THR	0	-0.035	-0.048	8.830	-0.162	-0.162	0.000	0.000	0.000	0.000
32	A	1032	SER	0	0.048	0.059	10.990	0.015	0.015	0.000	0.000	0.000	0.000
33	A	1033	ALA	0	0.033	-0.002	12.151	0.016	0.016	0.000	0.000	0.000	0.000
34	A	1034	GLY	0	-0.004	0.001	14.271	-0.024	-0.024	0.000	0.000	0.000	0.000
35	A	1035	PHE	0	-0.053	-0.008	15.044	-0.024	-0.024	0.000	0.000	0.000	0.000
36	A	1036	ALA	0	0.029	0.021	15.873	0.040	0.040	0.000	0.000	0.000	0.000
37	A	1037	VAL	0	-0.015	-0.012	16.418	-0.030	-0.030	0.000	0.000	0.000	0.000
38	A	1038	SER	0	0.002	-0.005	18.196	0.017	0.017	0.000	0.000	0.000	0.000
39	A	1039	PRO	0	0.090	0.027	18.319	-0.001	-0.001	0.000	0.000	0.000	0.000
40	A	1040	ALA	0	0.023	0.025	19.794	-0.006	-0.006	0.000	0.000	0.000	0.000
41	A	1041	ASN	0	-0.017	0.009	21.390	-0.001	-0.001	0.000	0.000	0.000	0.000
42	A	1042	GLY	0	0.035	0.026	18.498	-0.003	-0.003	0.000	0.000	0.000	0.000
43	A	1043	ALA	0	0.028	0.011	19.350	0.000	0.000	0.000	0.000	0.000	0.000
44	A	1044	ALA	0	-0.019	-0.007	21.448	-0.009	-0.009	0.000	0.000	0.000	0.000
45	A	1045	LEU	0	-0.016	-0.008	18.430	-0.008	-0.008	0.000	0.000	0.000	0.000
46	A	1046	ALA	0	0.013	-0.008	18.799	-0.003	-0.003	0.000	0.000	0.000	0.000
47	A	1047	ASN	0	-0.050	-0.022	20.342	-0.010	-0.010	0.000	0.000	0.000	0.000
48	A	1048	ALA	0	0.046	0.030	23.687	-0.009	-0.009	0.000	0.000	0.000	0.000
49	A	1049	PHE	0	-0.030	-0.006	18.781	-0.005	-0.005	0.000	0.000	0.000	0.000
50	A	1050	LYS	1	0.799	0.877	23.031	-0.082	-0.082	0.000	0.000	0.000	0.000
51	A	1051	ASP	-1	-0.781	-0.871	25.461	0.057	0.057	0.000	0.000	0.000	0.000
52	A	1052	ALA	0	0.029	0.025	27.681	0.002	0.002	0.000	0.000	0.000	0.000
53	A	1053	THR	0	-0.049	-0.038	28.765	-0.002	-0.002	0.000	0.000	0.000	0.000
54	A	1054	ALA	0	0.017	0.014	29.260	-0.003	-0.003	0.000	0.000	0.000	0.000
55	A	1055	ILE	0	0.032	0.013	25.752	0.000	0.000	0.000	0.000	0.000	0.000
56	A	1056	ARG	1	0.835	0.914	29.452	-0.070	-0.070	0.000	0.000	0.000	0.000
57	A	1057	SER	0	-0.016	0.005	32.383	-0.003	-0.003	0.000	0.000	0.000	0.000
58	A	1058	ASN	0	-0.020	-0.006	32.615	-0.003	-0.003	0.000	0.000	0.000	0.000
59	A	1059	GLY	0	0.009	0.021	30.199	0.000	0.000	0.000	0.000	0.000	0.000
60	A	1060	PHE	0	0.001	-0.010	22.898	0.002	0.002	0.000	0.000	0.000	0.000
61	A	1061	GLU	-1	-0.863	-0.922	25.901	0.087	0.087	0.000	0.000	0.000	0.000
62	A	1062	LEU	0	0.008	-0.011	19.373	0.012	0.012	0.000	0.000	0.000	0.000
63	A	1063	ALA	0	0.017	0.018	20.468	-0.011	-0.011	0.000	0.000	0.000	0.000
64	A	1064	GLY	0	0.014	0.017	22.405	-0.009	-0.009	0.000	0.000	0.000	0.000
65	A	1065	THR	0	-0.040	-0.007	25.410	-0.015	-0.015	0.000	0.000	0.000	0.000
66	A	1066	ARG	1	0.831	0.898	26.367	-0.068	-0.068	0.000	0.000	0.000	0.000
67	A	1067	TYR	0	-0.032	-0.019	23.181	-0.006	-0.006	0.000	0.000	0.000	0.000
68	A	1068	VAL	0	0.017	0.002	28.387	0.000	0.000	0.000	0.000	0.000	0.000
69	A	1069	THR	0	0.002	-0.029	27.587	0.004	0.004	0.000	0.000	0.000	0.000
70	A	1070	ILE	0	-0.076	-0.023	27.165	-0.007	-0.007	0.000	0.000	0.000	0.000
71	A	1071	ARG	1	0.824	0.892	23.586	-0.102	-0.102	0.000	0.000	0.000	0.000
72	A	1072	ALA	0	0.015	0.000	25.443	0.007	0.007	0.000	0.000	0.000	0.000
73	A	1073	ASP	-1	-0.804	-0.873	23.953	0.088	0.088	0.000	0.000	0.000	0.000
74	A	1074	ASP	-1	-0.899	-0.949	23.336	0.100	0.100	0.000	0.000	0.000	0.000
75	A	1075	ARG	1	0.763	0.852	18.051	-0.140	-0.140	0.000	0.000	0.000	0.000
76	A	1076	SER	0	-0.040	-0.060	19.188	0.028	0.028	0.000	0.000	0.000	0.000
77	A	1077	VAL	0	0.012	0.009	20.945	-0.017	-0.017	0.000	0.000	0.000	0.000
78	A	1078	TYR	0	-0.048	-0.036	21.076	0.004	0.004	0.000	0.000	0.000	0.000
79	A	1079	GLY	0	0.049	0.009	24.092	-0.006	-0.006	0.000	0.000	0.000	0.000
80	A	1080	LYS	1	0.924	0.965	25.858	-0.055	-0.055	0.000	0.000	0.000	0.000
81	A	1081	LYS	1	0.956	0.963	28.298	-0.073	-0.073	0.000	0.000	0.000	0.000
82	A	1082	GLY	0	0.014	0.015	30.205	-0.002	-0.002	0.000	0.000	0.000	0.000
83	A	1083	SER	0	-0.024	-0.039	30.746	0.002	0.002	0.000	0.000	0.000	0.000
84	A	1084	ALA	0	-0.010	0.005	26.319	0.000	0.000	0.000	0.000	0.000	0.000
85	A	1085	GLY	0	-0.023	-0.027	25.192	-0.002	-0.002	0.000	0.000	0.000	0.000
86	A	1086	VAL	0	-0.042	-0.002	19.955	0.004	0.004	0.000	0.000	0.000	0.000
87	A	1087	ILE	0	0.008	0.014	18.830	-0.008	-0.008	0.000	0.000	0.000	0.000
88	A	1088	THR	0	-0.036	-0.034	17.361	0.019	0.019	0.000	0.000	0.000	0.000
89	A	1089	VAL	0	0.035	0.011	15.691	-0.022	-0.022	0.000	0.000	0.000	0.000
90	A	1090	LYS	1	0.898	0.981	14.941	-0.101	-0.101	0.000	0.000	0.000	0.000
91	A	1091	THR	0	0.035	-0.005	10.731	-0.004	-0.004	0.000	0.000	0.000	0.000
92	A	1092	SER	0	-0.004	-0.006	12.563	-0.039	-0.039	0.000	0.000	0.000	0.000
93	A	1093	LYS	1	0.844	0.917	10.061	-0.125	-0.125	0.000	0.000	0.000	0.000
94	A	1094	ALA	0	0.028	0.029	9.692	0.001	0.001	0.000	0.000	0.000	0.000
95	A	1095	ILE	0	-0.017	0.002	11.744	-0.051	-0.051	0.000	0.000	0.000	0.000
96	A	1096	LEU	0	-0.005	0.014	9.823	0.064	0.064	0.000	0.000	0.000	0.000
97	A	1097	ILE	0	0.023	-0.006	12.958	-0.061	-0.061	0.000	0.000	0.000	0.000
98	A	1098	GLY	0	0.044	0.017	14.375	0.014	0.014	0.000	0.000	0.000	0.000
99	A	1099	VAL	0	-0.019	-0.002	16.651	-0.010	-0.010	0.000	0.000	0.000	0.000
100	A	1100	TYR	0	0.033	0.013	19.518	-0.007	-0.007	0.000	0.000	0.000	0.000
101	A	1101	ASN	0	0.024	-0.005	22.185	-0.003	-0.003	0.000	0.000	0.000	0.000
102	A	1102	GLU	-1	-0.737	-0.862	25.331	0.035	0.035	0.000	0.000	0.000	0.000
103	A	1103	LYS	1	0.805	0.912	26.087	-0.035	-0.035	0.000	0.000	0.000	0.000
104	A	1104	ILE	0	-0.015	0.008	20.928	-0.004	-0.004	0.000	0.000	0.000	0.000
105	A	1105	GLN	0	0.040	0.019	25.098	0.007	0.007	0.000	0.000	0.000	0.000
106	A	1106	PRO	0	0.036	0.016	24.276	0.004	0.004	0.000	0.000	0.000	0.000
107	A	1107	GLY	0	0.033	0.021	23.839	0.008	0.008	0.000	0.000	0.000	0.000
108	A	1108	THR	0	0.007	-0.001	20.803	0.005	0.005	0.000	0.000	0.000	0.000
109	A	1109	ALA	0	0.048	0.030	19.569	0.004	0.004	0.000	0.000	0.000	0.000
110	A	1110	ALA	0	-0.030	-0.017	18.926	0.015	0.015	0.000	0.000	0.000	0.000
111	A	1111	ASN	0	-0.045	-0.039	19.373	0.015	0.015	0.000	0.000	0.000	0.000
112	A	1112	VAL	0	-0.010	0.006	14.284	0.014	0.014	0.000	0.000	0.000	0.000
113	A	1113	VAL	0	0.019	0.007	14.459	0.029	0.029	0.000	0.000	0.000	0.000
114	A	1114	GLU	-1	-0.717	-0.795	14.744	0.182	0.182	0.000	0.000	0.000	0.000
115	A	1115	LYS	1	0.972	0.991	14.867	-0.066	-0.066	0.000	0.000	0.000	0.000
116	A	1116	LEU	0	-0.015	-0.006	8.113	0.016	0.016	0.000	0.000	0.000	0.000
117	A	1117	ALA	0	0.029	0.008	10.962	0.120	0.120	0.000	0.000	0.000	0.000
118	A	1118	ASP	-1	-0.795	-0.869	12.799	0.177	0.177	0.000	0.000	0.000	0.000
119	A	1119	TYR	0	-0.039	-0.011	6.206	-0.284	-0.284	0.000	0.000	0.000	0.000
120	A	1120	LEU	0	0.008	-0.007	5.871	0.079	0.079	0.000	0.000	0.000	0.000
121	A	1121	ILE	0	-0.044	-0.007	9.533	-0.069	-0.069	0.000	0.000	0.000	0.000
122	A	1122	GLY	0	-0.009	0.002	12.776	-0.049	-0.049	0.000	0.000	0.000	0.000
123	A	1123	GLN	0	-0.050	-0.016	7.806	-0.175	-0.175	0.000	0.000	0.000	0.000
124	A	1124	GLY	0	0.017	0.016	9.092	-0.070	-0.070	0.000	0.000	0.000	0.000
125	A	1125	PHE	0	-0.042	-0.036	5.960	-0.051	-0.051	0.000	0.000	0.000	0.000

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