FMO DATABASE

FMODB ID: VQ621

Calculation Name: 1K8F-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1K8F

Chain ID: A

ChEMBL ID:

UniProt ID: Q01518

Base Structure: X-ray

Registration Date: 2023-09-23

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	157
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1456476.257099
FMO2-HF: Nuclear repulsion	1395342.9702
FMO2-HF: Total energy	-61133.286899
FMO2-MP2: Total energy	-61310.520954

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:319:PRO)

Summations of interaction energy for fragment #1(A:319:PRO)

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.
-2.628	0.552	0.07	-1.368	-1.883	-0.001

Interaction energy analysis for fragmet #1(A:319:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.018 / 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

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	321	VAL	0	-0.014	0.002	3.702	-1.746	0.213	0.000	-0.839	-1.121	0.003
4	A	322	LEU	0	0.018	-0.015	5.819	0.623	0.623	0.000	0.000	0.000	0.000
5	A	323	GLU	-1	-0.907	-0.930	8.361	-1.578	-1.578	0.000	0.000	0.000	0.000
6	A	324	LEU	0	-0.009	0.005	11.256	-0.019	-0.019	0.000	0.000	0.000	0.000
7	A	325	GLU	-1	-0.799	-0.887	11.405	-0.872	-0.872	0.000	0.000	0.000	0.000
8	A	326	GLY	0	-0.001	-0.002	14.385	0.044	0.044	0.000	0.000	0.000	0.000
9	A	327	LYS	1	0.858	0.907	18.062	0.323	0.323	0.000	0.000	0.000	0.000
10	A	328	LYS	1	0.862	0.920	13.245	0.687	0.687	0.000	0.000	0.000	0.000
11	A	329	TRP	0	0.050	0.028	13.583	-0.102	-0.102	0.000	0.000	0.000	0.000
12	A	330	ARG	1	0.704	0.826	6.652	1.892	1.892	0.000	0.000	0.000	0.000
13	A	331	VAL	0	0.019	0.019	9.928	-0.125	-0.125	0.000	0.000	0.000	0.000
14	A	332	GLU	-1	-0.831	-0.926	5.844	-1.774	-1.774	0.000	0.000	0.000	0.000
15	A	333	ASN	0	-0.039	-0.020	2.926	-0.623	0.598	0.070	-0.529	-0.762	-0.004
16	A	334	GLN	0	-0.011	-0.015	5.598	0.629	0.629	0.000	0.000	0.000	0.000
17	A	335	GLU	-1	-0.881	-0.966	7.436	0.948	0.948	0.000	0.000	0.000	0.000
18	A	336	ASN	0	-0.070	-0.018	9.271	0.016	0.016	0.000	0.000	0.000	0.000
19	A	337	VAL	0	0.024	0.040	9.650	0.025	0.025	0.000	0.000	0.000	0.000
20	A	338	SER	0	-0.007	-0.028	12.705	0.004	0.004	0.000	0.000	0.000	0.000
21	A	339	ASN	0	-0.004	-0.011	15.129	0.008	0.008	0.000	0.000	0.000	0.000
22	A	340	LEU	0	0.006	0.018	11.345	-0.001	-0.001	0.000	0.000	0.000	0.000
23	A	341	VAL	0	0.002	-0.012	15.313	0.042	0.042	0.000	0.000	0.000	0.000
24	A	342	ILE	0	-0.045	-0.010	14.827	-0.042	-0.042	0.000	0.000	0.000	0.000
25	A	343	GLU	-1	-0.815	-0.903	18.013	-0.217	-0.217	0.000	0.000	0.000	0.000
26	A	344	ASP	-1	-0.901	-0.935	18.981	-0.391	-0.391	0.000	0.000	0.000	0.000
27	A	345	THR	0	0.050	0.018	21.137	-0.021	-0.021	0.000	0.000	0.000	0.000
28	A	346	GLU	-1	-0.856	-0.910	22.712	-0.271	-0.271	0.000	0.000	0.000	0.000
29	A	347	LEU	0	0.045	0.019	24.414	-0.013	-0.013	0.000	0.000	0.000	0.000
30	A	348	LYS	1	0.794	0.890	24.034	0.288	0.288	0.000	0.000	0.000	0.000
31	A	349	GLN	0	-0.009	-0.006	20.370	-0.014	-0.014	0.000	0.000	0.000	0.000
32	A	350	VAL	0	0.010	0.010	18.187	0.032	0.032	0.000	0.000	0.000	0.000
33	A	351	ALA	0	0.025	0.021	16.562	-0.048	-0.048	0.000	0.000	0.000	0.000
34	A	352	TYR	0	-0.069	-0.059	12.529	0.076	0.076	0.000	0.000	0.000	0.000
35	A	353	ILE	0	0.012	0.006	12.410	-0.134	-0.134	0.000	0.000	0.000	0.000
36	A	354	TYR	0	0.053	0.015	8.313	0.206	0.206	0.000	0.000	0.000	0.000
37	A	355	LYS	1	0.905	0.944	7.936	0.012	0.012	0.000	0.000	0.000	0.000
38	A	356	CYS	0	-0.042	0.005	8.283	-0.139	-0.139	0.000	0.000	0.000	0.000
39	A	357	VAL	0	0.021	-0.013	10.500	0.102	0.102	0.000	0.000	0.000	0.000
40	A	358	ASN	0	-0.076	-0.048	12.285	-0.014	-0.014	0.000	0.000	0.000	0.000
41	A	359	THR	0	-0.006	0.006	11.765	-0.045	-0.045	0.000	0.000	0.000	0.000
42	A	360	THR	0	-0.041	-0.020	14.085	0.036	0.036	0.000	0.000	0.000	0.000
43	A	361	LEU	0	-0.036	-0.015	14.830	-0.029	-0.029	0.000	0.000	0.000	0.000
44	A	362	GLN	0	0.020	0.006	17.042	0.045	0.045	0.000	0.000	0.000	0.000
45	A	363	ILE	0	-0.019	-0.019	18.247	-0.037	-0.037	0.000	0.000	0.000	0.000
46	A	364	LYS	1	0.841	0.918	20.869	0.259	0.259	0.000	0.000	0.000	0.000
47	A	365	GLY	0	0.025	0.004	23.494	-0.013	-0.013	0.000	0.000	0.000	0.000
48	A	366	LYS	1	0.814	0.904	25.564	0.170	0.170	0.000	0.000	0.000	0.000
49	A	367	ILE	0	0.012	0.014	21.052	-0.001	-0.001	0.000	0.000	0.000	0.000
50	A	368	ASN	0	-0.005	-0.016	24.132	0.014	0.014	0.000	0.000	0.000	0.000
51	A	369	SER	0	0.013	-0.007	23.053	0.015	0.015	0.000	0.000	0.000	0.000
52	A	370	ILE	0	0.009	0.016	18.550	-0.037	-0.037	0.000	0.000	0.000	0.000
53	A	371	THR	0	-0.012	-0.007	17.386	0.035	0.035	0.000	0.000	0.000	0.000
54	A	372	VAL	0	0.004	0.006	15.915	-0.065	-0.065	0.000	0.000	0.000	0.000
55	A	373	ASP	-1	-0.764	-0.873	14.570	-0.282	-0.282	0.000	0.000	0.000	0.000
56	A	374	ASN	0	-0.056	-0.021	12.514	-0.059	-0.059	0.000	0.000	0.000	0.000
57	A	375	CYS	0	-0.020	0.039	12.563	-0.056	-0.056	0.000	0.000	0.000	0.000
58	A	376	LYS	1	0.904	0.930	14.114	0.047	0.047	0.000	0.000	0.000	0.000
59	A	377	LYS	1	0.856	0.930	15.412	0.002	0.002	0.000	0.000	0.000	0.000
60	A	378	LEU	0	0.017	0.022	13.841	-0.013	-0.013	0.000	0.000	0.000	0.000
61	A	379	GLY	0	0.019	0.009	17.082	0.027	0.027	0.000	0.000	0.000	0.000
62	A	380	LEU	0	-0.021	-0.015	18.472	-0.037	-0.037	0.000	0.000	0.000	0.000
63	A	381	VAL	0	-0.035	-0.022	20.258	0.033	0.033	0.000	0.000	0.000	0.000
64	A	382	PHE	0	0.040	0.009	22.372	-0.029	-0.029	0.000	0.000	0.000	0.000
65	A	383	ASP	-1	-0.784	-0.881	24.179	-0.183	-0.183	0.000	0.000	0.000	0.000
66	A	384	ASP	-1	-0.823	-0.917	27.135	-0.144	-0.144	0.000	0.000	0.000	0.000
67	A	385	VAL	0	-0.027	-0.004	24.555	-0.021	-0.021	0.000	0.000	0.000	0.000
68	A	386	VAL	0	-0.113	-0.059	27.371	0.018	0.018	0.000	0.000	0.000	0.000
69	A	387	GLY	0	-0.012	-0.005	27.695	0.014	0.014	0.000	0.000	0.000	0.000
70	A	388	ILE	0	0.015	0.012	24.767	0.011	0.011	0.000	0.000	0.000	0.000
71	A	389	VAL	0	0.010	0.004	22.199	-0.025	-0.025	0.000	0.000	0.000	0.000
72	A	390	GLU	-1	-0.946	-0.969	21.331	-0.196	-0.196	0.000	0.000	0.000	0.000
73	A	391	ILE	0	0.001	0.013	19.883	-0.035	-0.035	0.000	0.000	0.000	0.000
74	A	392	ILE	0	-0.006	-0.006	18.299	0.039	0.039	0.000	0.000	0.000	0.000
75	A	393	ASN	0	-0.022	-0.010	17.293	0.009	0.009	0.000	0.000	0.000	0.000
76	A	394	SER	0	0.019	0.007	17.294	-0.018	-0.018	0.000	0.000	0.000	0.000
77	A	395	LYS	1	0.791	0.877	18.195	0.087	0.087	0.000	0.000	0.000	0.000
78	A	396	ASP	-1	-0.771	-0.869	19.093	-0.031	-0.031	0.000	0.000	0.000	0.000
79	A	397	VAL	0	0.010	0.012	18.434	-0.013	-0.013	0.000	0.000	0.000	0.000
80	A	398	LYS	1	0.916	0.972	20.856	0.164	0.164	0.000	0.000	0.000	0.000
81	A	399	VAL	0	-0.001	-0.002	21.746	-0.027	-0.027	0.000	0.000	0.000	0.000
82	A	400	GLN	0	0.012	0.011	23.876	0.019	0.019	0.000	0.000	0.000	0.000
83	A	401	VAL	0	0.012	0.025	25.782	-0.020	-0.020	0.000	0.000	0.000	0.000
84	A	402	MET	0	-0.021	0.001	27.636	0.016	0.016	0.000	0.000	0.000	0.000
85	A	403	GLY	0	0.010	0.013	29.915	0.014	0.014	0.000	0.000	0.000	0.000
86	A	404	LYS	1	0.816	0.895	31.558	0.122	0.122	0.000	0.000	0.000	0.000
87	A	405	VAL	0	0.022	-0.013	27.375	-0.014	-0.014	0.000	0.000	0.000	0.000
88	A	406	PRO	0	-0.023	0.006	30.028	0.010	0.010	0.000	0.000	0.000	0.000
89	A	407	THR	0	-0.008	-0.007	29.323	0.006	0.006	0.000	0.000	0.000	0.000
90	A	408	ILE	0	0.026	0.007	25.638	-0.017	-0.017	0.000	0.000	0.000	0.000
91	A	409	SER	0	-0.027	-0.006	25.832	0.018	0.018	0.000	0.000	0.000	0.000
92	A	410	ILE	0	0.017	-0.002	24.504	-0.018	-0.018	0.000	0.000	0.000	0.000
93	A	411	ASN	0	0.023	-0.013	23.620	0.028	0.028	0.000	0.000	0.000	0.000
94	A	412	LYS	1	0.835	0.909	21.301	0.117	0.117	0.000	0.000	0.000	0.000
95	A	413	THR	0	0.000	-0.005	21.543	-0.006	-0.006	0.000	0.000	0.000	0.000
96	A	414	ASP	-1	-0.826	-0.863	22.599	-0.035	-0.035	0.000	0.000	0.000	0.000
97	A	415	GLY	0	0.103	0.053	23.344	0.001	0.001	0.000	0.000	0.000	0.000
98	A	416	CYS	0	-0.111	-0.066	23.494	-0.021	-0.021	0.000	0.000	0.000	0.000
99	A	417	HIS	0	-0.017	0.007	25.191	0.010	0.010	0.000	0.000	0.000	0.000
100	A	418	ALA	0	0.021	0.004	26.282	-0.015	-0.015	0.000	0.000	0.000	0.000
101	A	419	TYR	0	-0.003	0.001	27.551	0.010	0.010	0.000	0.000	0.000	0.000
102	A	420	LEU	0	0.024	0.011	29.528	-0.013	-0.013	0.000	0.000	0.000	0.000
103	A	421	SER	0	0.032	-0.018	32.136	0.007	0.007	0.000	0.000	0.000	0.000
104	A	422	LYS	1	0.869	0.895	34.245	0.073	0.073	0.000	0.000	0.000	0.000
105	A	423	ASN	0	-0.052	-0.016	35.201	0.009	0.009	0.000	0.000	0.000	0.000
106	A	424	SER	0	-0.016	-0.015	32.812	-0.004	-0.004	0.000	0.000	0.000	0.000
107	A	425	LEU	0	0.002	0.007	34.625	-0.001	-0.001	0.000	0.000	0.000	0.000
108	A	426	ASP	-1	-0.884	-0.936	36.887	-0.102	-0.102	0.000	0.000	0.000	0.000
109	A	427	CYS	0	-0.067	-0.001	31.447	-0.003	-0.003	0.000	0.000	0.000	0.000
110	A	428	GLU	-1	-0.896	-0.945	33.276	-0.103	-0.103	0.000	0.000	0.000	0.000
111	A	429	ILE	0	0.003	-0.018	29.820	-0.010	-0.010	0.000	0.000	0.000	0.000
112	A	430	VAL	0	0.004	0.024	29.708	0.010	0.010	0.000	0.000	0.000	0.000
113	A	431	SER	0	0.040	0.021	28.951	-0.005	-0.005	0.000	0.000	0.000	0.000
114	A	432	ALA	0	0.011	0.001	28.320	0.007	0.007	0.000	0.000	0.000	0.000
115	A	433	LYS	1	0.871	0.931	26.200	0.041	0.041	0.000	0.000	0.000	0.000
116	A	434	SER	0	0.017	-0.001	26.291	-0.004	-0.004	0.000	0.000	0.000	0.000
117	A	435	SER	0	-0.007	-0.019	27.130	0.006	0.006	0.000	0.000	0.000	0.000
118	A	436	GLU	-1	-0.934	-0.965	27.636	-0.031	-0.031	0.000	0.000	0.000	0.000
119	A	437	MET	0	-0.033	-0.004	27.666	-0.012	-0.012	0.000	0.000	0.000	0.000
120	A	438	ASN	0	0.007	0.001	29.451	0.011	0.011	0.000	0.000	0.000	0.000
121	A	439	VAL	0	0.015	0.006	30.179	-0.011	-0.011	0.000	0.000	0.000	0.000
122	A	440	LEU	0	-0.037	-0.025	30.421	0.007	0.007	0.000	0.000	0.000	0.000
123	A	441	ILE	0	-0.008	-0.014	33.315	-0.008	-0.008	0.000	0.000	0.000	0.000
124	A	442	PRO	0	-0.023	0.010	35.025	0.004	0.004	0.000	0.000	0.000	0.000
125	A	443	THR	0	-0.063	-0.060	36.960	0.002	0.002	0.000	0.000	0.000	0.000
126	A	444	GLU	-1	-0.884	-0.946	39.719	-0.065	-0.065	0.000	0.000	0.000	0.000
127	A	445	GLY	0	0.015	0.018	40.109	0.004	0.004	0.000	0.000	0.000	0.000
128	A	446	GLY	0	-0.057	-0.014	36.170	0.001	0.001	0.000	0.000	0.000	0.000
129	A	447	ASP	-1	-0.850	-0.892	35.400	-0.056	-0.056	0.000	0.000	0.000	0.000
130	A	448	PHE	0	-0.023	-0.035	32.326	-0.006	-0.006	0.000	0.000	0.000	0.000
131	A	449	ASN	0	-0.045	-0.004	36.114	0.009	0.009	0.000	0.000	0.000	0.000
132	A	450	GLU	-1	-0.848	-0.938	31.923	-0.062	-0.062	0.000	0.000	0.000	0.000
133	A	451	PHE	0	-0.017	-0.009	35.165	0.006	0.006	0.000	0.000	0.000	0.000
134	A	452	PRO	0	0.032	0.036	34.116	-0.006	-0.006	0.000	0.000	0.000	0.000
135	A	453	VAL	0	-0.023	-0.018	32.063	0.001	0.001	0.000	0.000	0.000	0.000
136	A	454	PRO	0	-0.056	-0.042	34.038	0.002	0.002	0.000	0.000	0.000	0.000
137	A	455	GLU	-1	-0.798	-0.894	32.185	-0.041	-0.041	0.000	0.000	0.000	0.000
138	A	456	GLN	0	-0.047	-0.015	34.277	0.003	0.003	0.000	0.000	0.000	0.000
139	A	457	PHE	0	0.011	-0.001	34.742	-0.001	-0.001	0.000	0.000	0.000	0.000
140	A	458	LYS	1	0.892	0.969	39.973	0.031	0.031	0.000	0.000	0.000	0.000
141	A	459	THR	0	-0.017	-0.030	42.467	-0.002	-0.002	0.000	0.000	0.000	0.000
142	A	460	LEU	0	0.018	0.001	44.627	0.003	0.003	0.000	0.000	0.000	0.000
143	A	461	TRP	0	0.024	0.029	48.268	-0.003	-0.003	0.000	0.000	0.000	0.000
144	A	462	ASN	0	-0.046	-0.035	50.375	0.000	0.000	0.000	0.000	0.000	0.000
145	A	463	GLY	0	0.047	0.046	52.927	0.001	0.001	0.000	0.000	0.000	0.000
146	A	464	GLN	0	-0.074	-0.045	53.508	-0.001	-0.001	0.000	0.000	0.000	0.000
147	A	465	LYS	1	0.949	0.962	47.130	0.036	0.036	0.000	0.000	0.000	0.000
148	A	466	LEU	0	0.065	0.032	44.062	0.002	0.002	0.000	0.000	0.000	0.000
149	A	467	VAL	0	-0.016	-0.009	46.707	-0.003	-0.003	0.000	0.000	0.000	0.000
150	A	468	THR	0	0.016	-0.002	40.743	0.004	0.004	0.000	0.000	0.000	0.000
151	A	469	THR	0	0.011	0.017	44.015	-0.001	-0.001	0.000	0.000	0.000	0.000
152	A	470	VAL	0	0.025	0.004	39.122	0.001	0.001	0.000	0.000	0.000	0.000
153	A	471	THR	0	-0.021	-0.009	39.865	0.002	0.002	0.000	0.000	0.000	0.000
154	A	472	GLU	-1	-0.905	-0.958	39.848	-0.031	-0.031	0.000	0.000	0.000	0.000
155	A	473	ILE	0	0.010	0.019	35.972	0.004	0.004	0.000	0.000	0.000	0.000
156	A	474	ALA	0	0.029	0.015	39.187	-0.002	-0.002	0.000	0.000	0.000	0.000
157	A	475	GLY	0	-0.031	-0.014	37.966	0.005	0.005	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:319:PRO)