FMO DATABASE

FMODB ID: 2JY8R

Calculation Name: 5CWK-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5CWK

Chain ID: A

ChEMBL ID:

UniProt ID:

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	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	172
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1685167.206551
FMO2-HF: Nuclear repulsion	1619919.850055
FMO2-HF: Total energy	-65247.356497
FMO2-MP2: Total energy	-65443.118649

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:2:SER)

Summations of interaction energy for fragment #1(A:2: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.
-7.71	-3.526	1.623	-2.124	-3.683	0.011

Interaction energy analysis for fragmet #1(A:2:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.028 / q_NPA : 0.003

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	4	ASP	-1	-0.791	-0.883	3.130	0.466	2.444	0.031	-0.865	-1.144	0.001
4	A	5	GLU	-1	-0.835	-0.913	2.720	-4.168	-2.357	1.589	-1.158	-2.242	0.010
5	A	6	LYS	1	0.884	0.947	4.126	-2.488	-2.093	0.003	-0.101	-0.297	0.000
6	A	7	GLU	-1	-0.831	-0.908	6.034	0.211	0.211	0.000	0.000	0.000	0.000
7	A	8	LYS	1	0.928	0.954	7.137	-1.005	-1.005	0.000	0.000	0.000	0.000
8	A	9	LEU	0	0.030	0.008	7.000	-0.175	-0.175	0.000	0.000	0.000	0.000
9	A	10	LYS	1	0.757	0.855	9.909	-0.342	-0.342	0.000	0.000	0.000	0.000
10	A	11	GLU	-1	-0.939	-0.967	11.755	0.262	0.262	0.000	0.000	0.000	0.000
11	A	12	LEU	0	0.014	0.015	11.794	-0.030	-0.030	0.000	0.000	0.000	0.000
12	A	13	LEU	0	0.016	0.009	14.084	-0.019	-0.019	0.000	0.000	0.000	0.000
13	A	14	LYS	1	0.852	0.919	15.882	-0.119	-0.119	0.000	0.000	0.000	0.000
14	A	15	ARG	1	0.857	0.911	17.429	-0.094	-0.094	0.000	0.000	0.000	0.000
15	A	16	ALA	0	0.056	0.033	18.555	-0.009	-0.009	0.000	0.000	0.000	0.000
16	A	17	GLU	-1	-0.796	-0.899	20.028	0.047	0.047	0.000	0.000	0.000	0.000
17	A	18	GLU	-1	-0.869	-0.893	21.555	0.083	0.083	0.000	0.000	0.000	0.000
18	A	19	LEU	0	0.029	0.020	22.155	-0.003	-0.003	0.000	0.000	0.000	0.000
19	A	20	ALA	0	-0.009	-0.004	24.377	-0.005	-0.005	0.000	0.000	0.000	0.000
20	A	21	LYS	1	0.753	0.866	24.619	-0.051	-0.051	0.000	0.000	0.000	0.000
21	A	22	SER	0	-0.042	-0.039	28.620	0.000	0.000	0.000	0.000	0.000	0.000
22	A	23	PRO	0	-0.027	-0.023	30.490	-0.002	-0.002	0.000	0.000	0.000	0.000
23	A	24	ASP	-1	-0.851	-0.920	31.306	0.006	0.006	0.000	0.000	0.000	0.000
24	A	25	PRO	0	0.021	-0.007	31.087	0.000	0.000	0.000	0.000	0.000	0.000
25	A	26	GLU	-1	-0.833	-0.921	29.373	-0.009	-0.009	0.000	0.000	0.000	0.000
26	A	27	ASP	-1	-0.835	-0.874	26.948	0.023	0.023	0.000	0.000	0.000	0.000
27	A	28	LEU	0	-0.035	-0.016	26.004	0.000	0.000	0.000	0.000	0.000	0.000
28	A	29	LYS	1	0.807	0.883	26.164	0.007	0.007	0.000	0.000	0.000	0.000
29	A	30	GLU	-1	-0.866	-0.924	21.603	-0.007	-0.007	0.000	0.000	0.000	0.000
30	A	31	ALA	0	-0.041	-0.023	21.813	0.000	0.000	0.000	0.000	0.000	0.000
31	A	32	VAL	0	-0.031	-0.014	21.266	-0.001	-0.001	0.000	0.000	0.000	0.000
32	A	33	ARG	1	0.878	0.942	20.533	0.010	0.010	0.000	0.000	0.000	0.000
33	A	34	LEU	0	0.017	0.003	17.365	-0.009	-0.009	0.000	0.000	0.000	0.000
34	A	35	ALA	0	-0.012	-0.008	16.138	-0.001	-0.001	0.000	0.000	0.000	0.000
35	A	36	GLU	-1	-0.915	-0.988	16.559	-0.084	-0.084	0.000	0.000	0.000	0.000
36	A	37	GLU	-1	-0.819	-0.878	13.410	-0.094	-0.094	0.000	0.000	0.000	0.000
37	A	38	VAL	0	-0.045	-0.020	11.835	-0.057	-0.057	0.000	0.000	0.000	0.000
38	A	39	VAL	0	-0.118	-0.066	12.324	-0.043	-0.043	0.000	0.000	0.000	0.000
39	A	40	ARG	1	0.752	0.860	13.722	0.144	0.144	0.000	0.000	0.000	0.000
40	A	41	GLU	-1	-0.794	-0.885	8.429	-0.460	-0.460	0.000	0.000	0.000	0.000
41	A	42	ARG	1	0.864	0.934	5.214	0.127	0.127	0.000	0.000	0.000	0.000
42	A	43	PRO	0	0.111	0.074	9.768	0.147	0.147	0.000	0.000	0.000	0.000
43	A	44	GLY	0	0.006	0.012	12.572	0.002	0.002	0.000	0.000	0.000	0.000
44	A	45	SER	0	-0.052	-0.038	10.219	0.089	0.089	0.000	0.000	0.000	0.000
45	A	46	ASN	0	0.014	-0.023	12.191	-0.026	-0.026	0.000	0.000	0.000	0.000
46	A	47	LEU	0	0.010	0.015	9.222	0.004	0.004	0.000	0.000	0.000	0.000
47	A	48	ALA	0	0.064	0.051	12.865	0.003	0.003	0.000	0.000	0.000	0.000
48	A	49	LYS	1	0.877	0.928	14.540	-0.019	-0.019	0.000	0.000	0.000	0.000
49	A	50	LYS	1	0.816	0.905	16.353	-0.056	-0.056	0.000	0.000	0.000	0.000
50	A	51	ALA	0	0.035	0.009	15.849	0.003	0.003	0.000	0.000	0.000	0.000
51	A	52	LEU	0	0.013	0.003	17.858	0.001	0.001	0.000	0.000	0.000	0.000
52	A	53	GLU	-1	-0.814	-0.879	20.612	0.046	0.046	0.000	0.000	0.000	0.000
53	A	54	ILE	0	-0.053	-0.016	19.810	0.001	0.001	0.000	0.000	0.000	0.000
54	A	55	ILE	0	0.029	0.020	19.490	0.000	0.000	0.000	0.000	0.000	0.000
55	A	56	LEU	0	-0.008	0.002	23.419	0.000	0.000	0.000	0.000	0.000	0.000
56	A	57	ARG	1	0.798	0.859	22.880	-0.036	-0.036	0.000	0.000	0.000	0.000
57	A	58	ALA	0	0.049	0.027	25.722	0.000	0.000	0.000	0.000	0.000	0.000
58	A	59	ALA	0	-0.001	-0.001	27.459	-0.001	-0.001	0.000	0.000	0.000	0.000
59	A	60	GLU	-1	-0.852	-0.921	29.269	0.007	0.007	0.000	0.000	0.000	0.000
60	A	61	GLU	-1	-0.815	-0.891	31.235	0.011	0.011	0.000	0.000	0.000	0.000
61	A	62	LEU	0	-0.005	0.002	28.651	-0.001	-0.001	0.000	0.000	0.000	0.000
62	A	63	ALA	0	-0.015	-0.011	32.793	-0.001	-0.001	0.000	0.000	0.000	0.000
63	A	64	LYS	1	0.713	0.836	34.900	-0.009	-0.009	0.000	0.000	0.000	0.000
64	A	65	LEU	0	0.012	0.018	34.457	0.001	0.001	0.000	0.000	0.000	0.000
65	A	66	PRO	0	-0.018	-0.022	38.247	-0.002	-0.002	0.000	0.000	0.000	0.000
66	A	67	ASP	-1	-0.802	-0.882	35.207	-0.011	-0.011	0.000	0.000	0.000	0.000
67	A	68	PRO	0	0.040	0.000	36.935	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	69	GLU	-1	-0.846	-0.928	31.733	-0.030	-0.030	0.000	0.000	0.000	0.000
69	A	70	ALA	0	0.016	0.009	32.334	-0.002	-0.002	0.000	0.000	0.000	0.000
70	A	71	LEU	0	-0.032	0.001	32.492	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	72	LYS	1	0.886	0.951	32.535	0.024	0.024	0.000	0.000	0.000	0.000
72	A	73	GLU	-1	-0.834	-0.916	27.199	-0.034	-0.034	0.000	0.000	0.000	0.000
73	A	74	ALA	0	0.023	0.012	28.478	-0.003	-0.003	0.000	0.000	0.000	0.000
74	A	75	VAL	0	-0.021	-0.022	29.903	-0.002	-0.002	0.000	0.000	0.000	0.000
75	A	76	LYS	1	0.785	0.885	27.010	0.032	0.032	0.000	0.000	0.000	0.000
76	A	77	ALA	0	0.027	0.013	25.154	-0.005	-0.005	0.000	0.000	0.000	0.000
77	A	78	ALA	0	0.008	-0.006	25.496	-0.003	-0.003	0.000	0.000	0.000	0.000
78	A	79	GLU	-1	-0.765	-0.848	27.454	-0.042	-0.042	0.000	0.000	0.000	0.000
79	A	80	LYS	1	0.822	0.898	19.142	0.092	0.092	0.000	0.000	0.000	0.000
80	A	81	VAL	0	0.011	0.010	23.421	-0.002	-0.002	0.000	0.000	0.000	0.000
81	A	82	VAL	0	-0.041	-0.023	24.646	0.003	0.003	0.000	0.000	0.000	0.000
82	A	83	ARG	1	0.828	0.903	21.973	0.088	0.088	0.000	0.000	0.000	0.000
83	A	84	GLU	-1	-0.790	-0.870	20.205	-0.105	-0.105	0.000	0.000	0.000	0.000
84	A	85	GLN	0	-0.042	-0.016	21.140	0.002	0.002	0.000	0.000	0.000	0.000
85	A	86	PRO	0	0.043	0.017	23.553	0.008	0.008	0.000	0.000	0.000	0.000
86	A	87	GLY	0	-0.034	-0.008	25.670	0.004	0.004	0.000	0.000	0.000	0.000
87	A	88	SER	0	0.000	-0.012	25.305	0.007	0.007	0.000	0.000	0.000	0.000
88	A	89	ASN	0	0.017	0.001	27.372	-0.006	-0.006	0.000	0.000	0.000	0.000
89	A	90	LEU	0	-0.003	0.005	23.405	-0.001	-0.001	0.000	0.000	0.000	0.000
90	A	91	ALA	0	0.060	0.047	27.279	-0.002	-0.002	0.000	0.000	0.000	0.000
91	A	92	LYS	1	0.886	0.947	28.554	0.002	0.002	0.000	0.000	0.000	0.000
92	A	93	LYS	1	0.875	0.926	30.095	-0.006	-0.006	0.000	0.000	0.000	0.000
93	A	94	ALA	0	0.023	0.010	28.204	0.000	0.000	0.000	0.000	0.000	0.000
94	A	95	LEU	0	-0.012	-0.002	30.317	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	96	GLU	-1	-0.912	-0.969	33.448	0.000	0.000	0.000	0.000	0.000	0.000
96	A	97	ILE	0	-0.022	-0.002	30.515	0.001	0.001	0.000	0.000	0.000	0.000
97	A	98	ILE	0	-0.008	0.001	30.814	0.000	0.000	0.000	0.000	0.000	0.000
98	A	99	LEU	0	-0.003	-0.005	34.551	0.000	0.000	0.000	0.000	0.000	0.000
99	A	100	ARG	1	0.808	0.885	36.632	0.003	0.003	0.000	0.000	0.000	0.000
100	A	101	ALA	0	0.058	0.027	35.255	0.001	0.001	0.000	0.000	0.000	0.000
101	A	102	ALA	0	0.000	0.005	37.381	0.000	0.000	0.000	0.000	0.000	0.000
102	A	103	GLU	-1	-0.792	-0.890	39.792	-0.005	-0.005	0.000	0.000	0.000	0.000
103	A	104	GLU	-1	-0.791	-0.867	39.777	-0.002	-0.002	0.000	0.000	0.000	0.000
104	A	105	LEU	0	0.015	0.003	37.216	0.000	0.000	0.000	0.000	0.000	0.000
105	A	106	ALA	0	-0.048	-0.028	41.542	0.000	0.000	0.000	0.000	0.000	0.000
106	A	107	LYS	1	0.781	0.895	43.938	0.005	0.005	0.000	0.000	0.000	0.000
107	A	108	LEU	0	-0.004	0.014	40.913	0.001	0.001	0.000	0.000	0.000	0.000
108	A	109	PRO	0	-0.022	-0.003	45.525	-0.001	-0.001	0.000	0.000	0.000	0.000
109	A	110	ASP	-1	-0.828	-0.928	43.832	-0.017	-0.017	0.000	0.000	0.000	0.000
110	A	111	PRO	0	0.040	0.018	45.771	0.000	0.000	0.000	0.000	0.000	0.000
111	A	112	GLU	-1	-0.805	-0.904	39.270	-0.027	-0.027	0.000	0.000	0.000	0.000
112	A	113	ALA	0	0.028	0.014	41.054	-0.001	-0.001	0.000	0.000	0.000	0.000
113	A	114	LEU	0	0.027	0.018	42.021	0.000	0.000	0.000	0.000	0.000	0.000
114	A	115	LYS	1	0.812	0.876	42.452	0.023	0.023	0.000	0.000	0.000	0.000
115	A	116	GLU	-1	-0.865	-0.931	35.985	-0.031	-0.031	0.000	0.000	0.000	0.000
116	A	117	ALA	0	0.007	0.009	39.057	-0.001	-0.001	0.000	0.000	0.000	0.000
117	A	118	VAL	0	-0.025	-0.011	41.104	0.000	0.000	0.000	0.000	0.000	0.000
118	A	119	LYS	1	0.794	0.884	37.209	0.029	0.029	0.000	0.000	0.000	0.000
119	A	120	ALA	0	-0.008	0.001	36.236	-0.002	-0.002	0.000	0.000	0.000	0.000
120	A	121	ALA	0	0.021	0.003	37.203	0.000	0.000	0.000	0.000	0.000	0.000
121	A	122	GLU	-1	-0.823	-0.927	39.658	-0.023	-0.023	0.000	0.000	0.000	0.000
122	A	123	LYS	1	0.817	0.919	31.178	0.037	0.037	0.000	0.000	0.000	0.000
123	A	124	VAL	0	0.020	0.009	35.913	0.000	0.000	0.000	0.000	0.000	0.000
124	A	125	VAL	0	-0.052	-0.027	37.327	0.001	0.001	0.000	0.000	0.000	0.000
125	A	126	ARG	1	0.805	0.887	36.851	0.026	0.026	0.000	0.000	0.000	0.000
126	A	127	GLH	0	-0.059	-0.055	30.946	0.000	0.000	0.000	0.000	0.000	0.000
127	A	128	GLN	0	-0.005	-0.003	34.285	0.005	0.005	0.000	0.000	0.000	0.000
128	A	129	PRO	0	0.073	0.060	37.491	0.002	0.002	0.000	0.000	0.000	0.000
129	A	130	GLY	0	-0.011	-0.007	40.768	0.001	0.001	0.000	0.000	0.000	0.000
130	A	131	SER	0	-0.053	-0.038	40.258	0.002	0.002	0.000	0.000	0.000	0.000
131	A	132	GLU	-1	-0.776	-0.886	42.479	-0.005	-0.005	0.000	0.000	0.000	0.000
132	A	133	LEU	0	0.002	0.010	36.823	0.000	0.000	0.000	0.000	0.000	0.000
133	A	134	ALA	0	0.023	0.027	40.858	-0.001	-0.001	0.000	0.000	0.000	0.000
134	A	135	LYS	1	0.825	0.879	42.095	0.005	0.005	0.000	0.000	0.000	0.000
135	A	136	LYS	1	0.859	0.933	43.094	0.005	0.005	0.000	0.000	0.000	0.000
136	A	137	ALA	0	0.017	0.000	41.021	0.000	0.000	0.000	0.000	0.000	0.000
137	A	138	LEU	0	0.001	-0.008	43.089	-0.001	-0.001	0.000	0.000	0.000	0.000
138	A	139	GLU	-1	-0.872	-0.914	46.266	-0.006	-0.006	0.000	0.000	0.000	0.000
139	A	140	ILE	0	-0.040	-0.007	42.432	0.000	0.000	0.000	0.000	0.000	0.000
140	A	141	ILE	0	0.014	0.013	42.912	0.000	0.000	0.000	0.000	0.000	0.000
141	A	142	GLU	-1	-0.760	-0.850	46.203	-0.010	-0.010	0.000	0.000	0.000	0.000
142	A	143	ARG	1	0.790	0.867	46.339	0.007	0.007	0.000	0.000	0.000	0.000
143	A	144	ALA	0	0.058	0.027	45.973	0.000	0.000	0.000	0.000	0.000	0.000
144	A	145	ALA	0	0.001	0.006	48.031	0.000	0.000	0.000	0.000	0.000	0.000
145	A	146	GLU	-1	-0.876	-0.936	50.284	-0.010	-0.010	0.000	0.000	0.000	0.000
146	A	147	GLU	-1	-0.862	-0.899	50.001	-0.008	-0.008	0.000	0.000	0.000	0.000
147	A	148	LEU	0	-0.019	-0.013	46.530	0.000	0.000	0.000	0.000	0.000	0.000
148	A	149	LYS	1	0.721	0.841	51.012	0.011	0.011	0.000	0.000	0.000	0.000
149	A	150	LYS	1	0.790	0.872	54.318	0.009	0.009	0.000	0.000	0.000	0.000
150	A	151	SER	0	-0.038	-0.030	52.135	0.000	0.000	0.000	0.000	0.000	0.000
151	A	152	PRO	0	-0.040	-0.026	54.212	0.000	0.000	0.000	0.000	0.000	0.000
152	A	153	ASP	-1	-0.844	-0.893	52.131	-0.015	-0.015	0.000	0.000	0.000	0.000
153	A	154	PRO	0	0.003	-0.014	53.702	0.000	0.000	0.000	0.000	0.000	0.000
154	A	155	GLU	-1	-0.960	-0.971	49.588	-0.022	-0.022	0.000	0.000	0.000	0.000
155	A	156	ALA	0	0.079	0.042	49.410	0.000	0.000	0.000	0.000	0.000	0.000
156	A	157	GLN	0	0.023	0.015	50.429	0.000	0.000	0.000	0.000	0.000	0.000
157	A	158	LYS	1	0.921	0.962	51.766	0.020	0.020	0.000	0.000	0.000	0.000
158	A	159	GLU	-1	-0.822	-0.900	45.247	-0.023	-0.023	0.000	0.000	0.000	0.000
159	A	160	ALA	0	0.018	0.019	49.257	0.000	0.000	0.000	0.000	0.000	0.000
160	A	161	LYS	1	0.880	0.911	50.950	0.013	0.013	0.000	0.000	0.000	0.000
161	A	162	LYS	1	0.854	0.924	48.911	0.020	0.020	0.000	0.000	0.000	0.000
162	A	163	ALA	0	0.050	0.021	47.510	0.000	0.000	0.000	0.000	0.000	0.000
163	A	164	GLU	-1	-0.761	-0.849	48.799	-0.012	-0.012	0.000	0.000	0.000	0.000
164	A	165	GLN	0	-0.101	-0.044	52.025	0.000	0.000	0.000	0.000	0.000	0.000
165	A	166	LYS	1	0.830	0.902	43.992	0.021	0.021	0.000	0.000	0.000	0.000
166	A	167	VAL	0	-0.018	-0.010	47.497	0.000	0.000	0.000	0.000	0.000	0.000
167	A	168	ARG	1	0.754	0.848	49.428	0.012	0.012	0.000	0.000	0.000	0.000
168	A	169	GLU	-1	-0.876	-0.924	50.347	-0.018	-0.018	0.000	0.000	0.000	0.000
169	A	170	GLU	-1	-0.800	-0.876	44.623	-0.021	-0.021	0.000	0.000	0.000	0.000
170	A	171	ARG	1	0.768	0.869	48.303	0.011	0.011	0.000	0.000	0.000	0.000
171	A	172	PRO	0	0.007	0.016	50.709	0.000	0.000	0.000	0.000	0.000	0.000
172	A	173	GLY	0	-0.034	-0.021	53.352	0.001	0.001	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:SER)