FMO DATABASE

FMODB ID: N94GQ

Calculation Name: 5K22-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5K22

Chain ID: A

ChEMBL ID:

UniProt ID: Q8NE01

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:

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	156
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1610548.179697
FMO2-HF: Nuclear repulsion	1548322.583483
FMO2-HF: Total energy	-62225.596214
FMO2-MP2: Total energy	-62407.217503

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:1:MET)

Summations of interaction energy for fragment #1(A:1: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.
-11.93	-9.101	3.434	-2.342	-3.92	0.015

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.013 / q_NPA : 0.001

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	3	ARG	1	0.910	0.961	2.444	-10.664	-8.171	3.432	-2.277	-3.647	0.015
4	A	4	PRO	0	0.017	0.021	4.724	-1.573	-1.436	0.000	-0.031	-0.106	0.000
5	A	5	ALA	0	0.040	0.008	7.832	0.113	0.113	0.000	0.000	0.000	0.000
6	A	6	PRO	0	-0.007	-0.014	9.296	0.174	0.174	0.000	0.000	0.000	0.000
7	A	7	VAL	0	-0.033	-0.001	12.100	-0.071	-0.071	0.000	0.000	0.000	0.000
8	A	8	GLU	-1	-0.865	-0.938	15.150	-0.036	-0.036	0.000	0.000	0.000	0.000
9	A	9	ILE	0	-0.091	-0.048	18.592	0.003	0.003	0.000	0.000	0.000	0.000
10	A	10	SER	0	0.028	0.007	21.293	0.007	0.007	0.000	0.000	0.000	0.000
11	A	11	TYR	0	-0.053	-0.046	24.785	-0.004	-0.004	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.903	-0.939	27.903	0.024	0.024	0.000	0.000	0.000	0.000
13	A	13	ASN	0	-0.042	-0.026	30.155	-0.001	-0.001	0.000	0.000	0.000	0.000
14	A	14	MET	0	-0.016	0.020	27.184	0.003	0.003	0.000	0.000	0.000	0.000
15	A	15	ARG	1	0.829	0.904	21.794	0.040	0.040	0.000	0.000	0.000	0.000
16	A	16	PHE	0	0.019	0.009	20.373	0.013	0.013	0.000	0.000	0.000	0.000
17	A	17	LEU	0	0.015	0.006	14.333	-0.027	-0.027	0.000	0.000	0.000	0.000
18	A	18	ILE	0	-0.024	0.016	13.771	0.055	0.055	0.000	0.000	0.000	0.000
19	A	19	THR	0	0.031	-0.001	10.154	-0.086	-0.086	0.000	0.000	0.000	0.000
20	A	20	HIS	0	-0.053	-0.038	5.650	0.517	0.517	0.000	0.000	0.000	0.000
21	A	21	ASN	0	0.059	0.010	7.495	-0.422	-0.422	0.000	0.000	0.000	0.000
22	A	22	PRO	0	-0.025	0.020	6.149	0.385	0.385	0.000	0.000	0.000	0.000
23	A	23	THR	0	0.008	-0.003	6.518	0.113	0.113	0.000	0.000	0.000	0.000
24	A	24	ASN	0	0.098	0.011	8.609	-0.118	-0.118	0.000	0.000	0.000	0.000
25	A	25	ALA	0	-0.001	0.011	7.734	-0.062	-0.062	0.000	0.000	0.000	0.000
26	A	26	THR	0	-0.024	-0.014	3.851	-0.229	-0.030	0.002	-0.034	-0.167	0.000
27	A	27	LEU	0	-0.007	0.010	6.509	-0.166	-0.166	0.000	0.000	0.000	0.000
28	A	28	ASN	0	0.062	0.025	9.783	0.012	0.012	0.000	0.000	0.000	0.000
29	A	29	LYS	1	0.911	0.973	6.616	1.032	1.032	0.000	0.000	0.000	0.000
30	A	30	PHE	0	0.001	-0.002	8.653	0.017	0.017	0.000	0.000	0.000	0.000
31	A	31	THR	0	0.033	-0.013	10.032	0.084	0.084	0.000	0.000	0.000	0.000
32	A	32	GLU	-1	-0.885	-0.950	12.338	-0.237	-0.237	0.000	0.000	0.000	0.000
33	A	33	GLU	-1	-0.918	-0.968	8.316	-0.696	-0.696	0.000	0.000	0.000	0.000
34	A	34	LEU	0	-0.015	0.001	13.029	0.034	0.034	0.000	0.000	0.000	0.000
35	A	35	LYS	1	0.980	1.000	15.699	0.177	0.177	0.000	0.000	0.000	0.000
36	A	36	LYS	1	0.924	0.982	15.676	0.288	0.288	0.000	0.000	0.000	0.000
37	A	37	TYR	0	-0.063	-0.039	13.937	0.008	0.008	0.000	0.000	0.000	0.000
38	A	38	GLY	0	0.037	0.043	18.669	0.022	0.022	0.000	0.000	0.000	0.000
39	A	39	VAL	0	-0.076	-0.045	17.969	0.018	0.018	0.000	0.000	0.000	0.000
40	A	40	THR	0	0.122	0.064	20.777	-0.004	-0.004	0.000	0.000	0.000	0.000
41	A	41	THR	0	-0.028	-0.015	21.732	0.007	0.007	0.000	0.000	0.000	0.000
42	A	42	LEU	0	-0.016	-0.015	14.778	0.004	0.004	0.000	0.000	0.000	0.000
43	A	43	VAL	0	0.001	0.014	18.426	-0.001	-0.001	0.000	0.000	0.000	0.000
44	A	44	ARG	1	0.818	0.899	14.253	-0.231	-0.231	0.000	0.000	0.000	0.000
45	A	45	VAL	0	0.038	0.015	15.826	-0.021	-0.021	0.000	0.000	0.000	0.000
46	A	46	CYS	0	-0.155	-0.076	12.701	0.062	0.062	0.000	0.000	0.000	0.000
47	A	47	ASP	-1	-0.853	-0.923	15.124	0.334	0.334	0.000	0.000	0.000	0.000
48	A	48	ALA	0	-0.026	-0.015	14.007	0.060	0.060	0.000	0.000	0.000	0.000
49	A	49	THR	0	-0.024	-0.014	9.561	-0.003	-0.003	0.000	0.000	0.000	0.000
50	A	50	TYR	0	-0.038	-0.029	11.476	-0.062	-0.062	0.000	0.000	0.000	0.000
51	A	51	ASP	-1	-0.809	-0.916	13.713	0.111	0.111	0.000	0.000	0.000	0.000
52	A	52	LYS	1	0.953	0.974	16.395	-0.154	-0.154	0.000	0.000	0.000	0.000
53	A	53	ALA	0	0.056	0.038	18.264	-0.020	-0.020	0.000	0.000	0.000	0.000
54	A	54	PRO	0	-0.025	-0.016	16.171	-0.016	-0.016	0.000	0.000	0.000	0.000
55	A	55	VAL	0	-0.012	-0.012	15.102	-0.020	-0.020	0.000	0.000	0.000	0.000
56	A	56	GLU	-1	-0.866	-0.954	17.726	0.071	0.071	0.000	0.000	0.000	0.000
57	A	57	LYS	1	0.806	0.898	19.858	0.050	0.050	0.000	0.000	0.000	0.000
58	A	58	GLU	-1	-0.912	-0.949	17.710	-0.109	-0.109	0.000	0.000	0.000	0.000
59	A	59	GLY	0	-0.014	0.017	20.998	-0.008	-0.008	0.000	0.000	0.000	0.000
60	A	60	ILE	0	-0.051	-0.013	17.952	0.001	0.001	0.000	0.000	0.000	0.000
61	A	61	HIS	0	0.028	0.002	21.817	0.010	0.010	0.000	0.000	0.000	0.000
62	A	62	VAL	0	-0.007	-0.006	18.107	0.013	0.013	0.000	0.000	0.000	0.000
63	A	63	LEU	0	-0.053	-0.021	20.489	-0.002	-0.002	0.000	0.000	0.000	0.000
64	A	64	ASP	-1	-0.864	-0.936	18.385	0.259	0.259	0.000	0.000	0.000	0.000
65	A	65	TRP	0	0.002	-0.009	20.123	-0.017	-0.017	0.000	0.000	0.000	0.000
66	A	66	PRO	0	0.012	0.011	18.806	0.021	0.021	0.000	0.000	0.000	0.000
67	A	67	PHE	0	-0.001	-0.013	19.543	-0.028	-0.028	0.000	0.000	0.000	0.000
68	A	68	ASP	-1	-0.863	-0.932	19.313	0.301	0.301	0.000	0.000	0.000	0.000
69	A	69	ASP	-1	-0.900	-0.965	15.414	0.647	0.647	0.000	0.000	0.000	0.000
70	A	70	GLY	0	-0.042	-0.014	17.884	-0.026	-0.026	0.000	0.000	0.000	0.000
71	A	71	ALA	0	0.011	-0.003	19.168	-0.037	-0.037	0.000	0.000	0.000	0.000
72	A	72	PRO	0	-0.019	-0.025	21.639	0.020	0.020	0.000	0.000	0.000	0.000
73	A	73	PRO	0	0.016	0.021	22.953	0.008	0.008	0.000	0.000	0.000	0.000
74	A	74	PRO	0	0.038	0.025	24.388	-0.018	-0.018	0.000	0.000	0.000	0.000
75	A	75	ASN	0	0.015	-0.014	27.584	0.005	0.005	0.000	0.000	0.000	0.000
76	A	76	GLN	0	0.094	0.042	29.077	-0.010	-0.010	0.000	0.000	0.000	0.000
77	A	77	ILE	0	0.016	0.038	23.159	-0.003	-0.003	0.000	0.000	0.000	0.000
78	A	78	VAL	0	-0.042	-0.026	26.161	0.001	0.001	0.000	0.000	0.000	0.000
79	A	79	ASP	-1	-0.916	-0.960	27.499	0.090	0.090	0.000	0.000	0.000	0.000
80	A	80	ASP	-1	-0.922	-0.973	27.546	0.110	0.110	0.000	0.000	0.000	0.000
81	A	81	TRP	0	-0.020	-0.019	21.583	-0.003	-0.003	0.000	0.000	0.000	0.000
82	A	82	LEU	0	0.012	-0.003	26.559	-0.010	-0.010	0.000	0.000	0.000	0.000
83	A	83	ASN	0	-0.049	-0.037	29.462	-0.018	-0.018	0.000	0.000	0.000	0.000
84	A	84	LEU	0	0.015	0.026	24.123	-0.009	-0.009	0.000	0.000	0.000	0.000
85	A	85	LEU	0	0.030	0.014	24.720	-0.011	-0.011	0.000	0.000	0.000	0.000
86	A	86	LYS	1	0.873	0.944	28.364	-0.077	-0.077	0.000	0.000	0.000	0.000
87	A	87	THR	0	-0.087	-0.050	30.045	-0.006	-0.006	0.000	0.000	0.000	0.000
88	A	88	LYS	1	0.911	0.957	26.110	-0.058	-0.058	0.000	0.000	0.000	0.000
89	A	89	PHE	0	-0.027	0.002	25.675	-0.006	-0.006	0.000	0.000	0.000	0.000
90	A	90	ARG	1	0.898	0.946	30.678	-0.043	-0.043	0.000	0.000	0.000	0.000
91	A	91	GLU	-1	-0.949	-0.959	28.325	0.027	0.027	0.000	0.000	0.000	0.000
92	A	92	GLU	-1	-0.879	-0.947	27.296	-0.026	-0.026	0.000	0.000	0.000	0.000
93	A	93	PRO	0	-0.030	-0.018	29.559	0.005	0.005	0.000	0.000	0.000	0.000
94	A	94	GLY	0	-0.014	-0.005	28.189	-0.006	-0.006	0.000	0.000	0.000	0.000
95	A	95	ALA	0	0.073	0.061	24.950	-0.011	-0.011	0.000	0.000	0.000	0.000
96	A	96	ALA	0	-0.052	-0.038	20.624	0.005	0.005	0.000	0.000	0.000	0.000
97	A	97	VAL	0	0.001	-0.001	21.091	0.002	0.002	0.000	0.000	0.000	0.000
98	A	98	ALA	0	0.007	-0.002	16.028	0.009	0.009	0.000	0.000	0.000	0.000
99	A	99	VAL	0	0.019	0.013	16.698	0.011	0.011	0.000	0.000	0.000	0.000
100	A	100	HIS	0	-0.034	0.004	11.278	-0.064	-0.064	0.000	0.000	0.000	0.000
101	A	101	CYS	0	0.003	0.019	12.227	-0.083	-0.083	0.000	0.000	0.000	0.000
102	A	102	VAL	0	0.060	0.012	8.617	0.079	0.079	0.000	0.000	0.000	0.000
103	A	103	ALA	0	0.034	0.005	6.656	0.584	0.584	0.000	0.000	0.000	0.000
104	A	104	GLY	0	0.033	0.018	8.471	-0.259	-0.259	0.000	0.000	0.000	0.000
105	A	105	LEU	0	-0.088	-0.057	10.066	-0.128	-0.128	0.000	0.000	0.000	0.000
106	A	106	GLY	0	0.116	0.056	13.133	0.028	0.028	0.000	0.000	0.000	0.000
107	A	107	ARG	1	0.904	0.945	14.694	-0.573	-0.573	0.000	0.000	0.000	0.000
108	A	108	ALA	0	0.028	0.017	14.733	-0.034	-0.034	0.000	0.000	0.000	0.000
109	A	109	PRO	0	-0.001	0.000	15.168	-0.050	-0.050	0.000	0.000	0.000	0.000
110	A	110	VAL	0	-0.014	0.011	18.209	-0.045	-0.045	0.000	0.000	0.000	0.000
111	A	111	LEU	0	0.064	0.033	20.576	-0.027	-0.027	0.000	0.000	0.000	0.000
112	A	112	VAL	0	0.026	0.027	19.407	-0.025	-0.025	0.000	0.000	0.000	0.000
113	A	113	ALA	0	0.002	-0.021	22.069	-0.024	-0.024	0.000	0.000	0.000	0.000
114	A	114	LEU	0	-0.015	-0.011	23.887	-0.017	-0.017	0.000	0.000	0.000	0.000
115	A	115	ALA	0	-0.015	0.003	25.341	-0.013	-0.013	0.000	0.000	0.000	0.000
116	A	116	LEU	0	-0.021	-0.002	23.708	-0.013	-0.013	0.000	0.000	0.000	0.000
117	A	117	ILE	0	0.000	0.001	27.417	-0.010	-0.010	0.000	0.000	0.000	0.000
118	A	118	GLU	-1	-0.817	-0.900	30.038	0.076	0.076	0.000	0.000	0.000	0.000
119	A	119	ALA	0	0.006	0.002	30.597	-0.006	-0.006	0.000	0.000	0.000	0.000
120	A	120	GLY	0	0.020	0.016	32.409	-0.007	-0.007	0.000	0.000	0.000	0.000
121	A	121	MET	0	-0.020	0.015	26.887	-0.004	-0.004	0.000	0.000	0.000	0.000
122	A	122	LYS	1	0.945	0.985	31.554	-0.059	-0.059	0.000	0.000	0.000	0.000
123	A	123	TYR	0	0.042	-0.006	27.446	-0.002	-0.002	0.000	0.000	0.000	0.000
124	A	124	GLU	-1	-0.897	-0.966	27.878	0.085	0.085	0.000	0.000	0.000	0.000
125	A	125	ASP	-1	-0.873	-0.943	27.588	0.054	0.054	0.000	0.000	0.000	0.000
126	A	126	ALA	0	0.004	0.002	25.975	0.000	0.000	0.000	0.000	0.000	0.000
127	A	127	VAL	0	-0.005	-0.005	22.672	0.015	0.015	0.000	0.000	0.000	0.000
128	A	128	GLN	0	-0.007	-0.010	22.355	0.030	0.030	0.000	0.000	0.000	0.000
129	A	129	PHE	0	0.036	0.026	23.172	-0.011	-0.011	0.000	0.000	0.000	0.000
130	A	130	ILE	0	0.006	0.001	17.946	-0.004	-0.004	0.000	0.000	0.000	0.000
131	A	131	ARG	1	0.859	0.909	18.416	-0.201	-0.201	0.000	0.000	0.000	0.000
132	A	132	GLN	0	-0.059	-0.013	18.927	-0.013	-0.013	0.000	0.000	0.000	0.000
133	A	133	LYS	1	0.924	0.984	17.242	-0.018	-0.018	0.000	0.000	0.000	0.000
134	A	134	ARG	1	0.854	0.943	9.658	-0.596	-0.596	0.000	0.000	0.000	0.000
135	A	135	ARG	1	0.989	1.001	14.349	-0.058	-0.058	0.000	0.000	0.000	0.000
136	A	136	GLY	0	-0.028	-0.020	14.160	0.079	0.079	0.000	0.000	0.000	0.000
137	A	137	ALA	0	0.001	0.013	15.334	0.055	0.055	0.000	0.000	0.000	0.000
138	A	138	PHE	0	0.049	0.028	16.256	0.052	0.052	0.000	0.000	0.000	0.000
139	A	139	ASN	0	0.047	0.015	18.354	-0.048	-0.048	0.000	0.000	0.000	0.000
140	A	140	SER	0	0.042	0.011	20.224	-0.015	-0.015	0.000	0.000	0.000	0.000
141	A	141	LYS	1	0.991	0.997	22.372	-0.277	-0.277	0.000	0.000	0.000	0.000
142	A	142	GLN	0	-0.027	-0.026	18.798	0.017	0.017	0.000	0.000	0.000	0.000
143	A	143	LEU	0	0.028	0.011	23.066	-0.011	-0.011	0.000	0.000	0.000	0.000
144	A	144	LEU	0	0.026	0.027	25.046	-0.018	-0.018	0.000	0.000	0.000	0.000
145	A	145	TYR	0	-0.003	-0.019	25.869	-0.012	-0.012	0.000	0.000	0.000	0.000
146	A	146	LEU	0	-0.029	-0.027	23.547	-0.010	-0.010	0.000	0.000	0.000	0.000
147	A	147	GLU	-1	-0.981	-0.979	27.665	0.094	0.094	0.000	0.000	0.000	0.000
148	A	148	LYS	1	0.915	0.959	30.597	-0.115	-0.115	0.000	0.000	0.000	0.000
149	A	149	TYR	0	-0.064	-0.032	29.901	-0.004	-0.004	0.000	0.000	0.000	0.000
150	A	150	ARG	1	0.947	0.971	32.034	-0.070	-0.070	0.000	0.000	0.000	0.000
151	A	151	PRO	0	0.016	0.020	33.363	0.002	0.002	0.000	0.000	0.000	0.000
152	A	152	LYS	1	0.840	0.904	35.063	-0.062	-0.062	0.000	0.000	0.000	0.000
153	A	153	MET	0	0.016	0.031	35.502	-0.004	-0.004	0.000	0.000	0.000	0.000
154	A	154	ARG	1	0.914	0.969	33.903	-0.085	-0.085	0.000	0.000	0.000	0.000
155	A	155	LEU	0	0.021	-0.013	29.740	0.004	0.004	0.000	0.000	0.000	0.000
156	A	156	ARG	1	0.977	1.011	34.270	-0.026	-0.026	0.000	0.000	0.000	0.000

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Support

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