FMO DATABASE

FMODB ID: 7295K

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1676577.760646
FMO2-HF: Nuclear repulsion	1611330.716298
FMO2-HF: Total energy	-65247.044348
FMO2-MP2: Total energy	-65442.742498

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.
-10.926	-6.468	1.832	-2.518	-3.773	0.006

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 : 0.035 / q_NPA : 0.010

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	-0.790	-0.890	2.978	-4.769	-2.190	0.058	-1.248	-1.390	0.003
4	A	5	GLU	-1	-0.866	-0.928	2.283	-3.891	-2.360	1.774	-1.181	-2.124	0.003
5	A	6	LYS	1	0.895	0.941	4.234	-1.817	-1.469	0.000	-0.089	-0.259	0.000
6	A	7	GLU	-1	-0.803	-0.896	6.215	0.400	0.400	0.000	0.000	0.000	0.000
7	A	8	LYS	1	0.941	0.984	7.125	2.126	2.126	0.000	0.000	0.000	0.000
8	A	9	LEU	0	0.015	0.006	7.690	0.263	0.263	0.000	0.000	0.000	0.000
9	A	10	LYS	1	0.750	0.842	10.128	-0.145	-0.145	0.000	0.000	0.000	0.000
10	A	11	GLU	-1	-0.943	-0.962	12.034	-0.540	-0.540	0.000	0.000	0.000	0.000
11	A	12	LEU	0	0.017	0.017	11.728	0.063	0.063	0.000	0.000	0.000	0.000
12	A	13	LEU	0	-0.011	-0.001	14.437	0.054	0.054	0.000	0.000	0.000	0.000
13	A	14	LYS	1	0.875	0.928	16.299	0.112	0.112	0.000	0.000	0.000	0.000
14	A	15	ARG	1	0.874	0.929	17.782	0.218	0.218	0.000	0.000	0.000	0.000
15	A	16	ALA	0	0.040	0.019	18.726	0.014	0.014	0.000	0.000	0.000	0.000
16	A	17	GLU	-1	-0.822	-0.923	20.395	0.065	0.065	0.000	0.000	0.000	0.000
17	A	18	GLU	-1	-0.872	-0.901	21.937	-0.108	-0.108	0.000	0.000	0.000	0.000
18	A	19	LEU	0	0.036	0.023	22.022	0.007	0.007	0.000	0.000	0.000	0.000
19	A	20	ALA	0	-0.005	-0.001	24.713	0.005	0.005	0.000	0.000	0.000	0.000
20	A	21	LYS	1	0.744	0.860	24.809	0.016	0.016	0.000	0.000	0.000	0.000
21	A	22	SER	0	-0.049	-0.037	28.920	0.008	0.008	0.000	0.000	0.000	0.000
22	A	23	PRO	0	-0.015	-0.017	30.822	0.002	0.002	0.000	0.000	0.000	0.000
23	A	24	ASP	-1	-0.859	-0.921	31.345	-0.086	-0.086	0.000	0.000	0.000	0.000
24	A	25	PRO	0	0.035	-0.002	30.944	-0.002	-0.002	0.000	0.000	0.000	0.000
25	A	26	GLU	-1	-0.860	-0.934	29.501	-0.116	-0.116	0.000	0.000	0.000	0.000
26	A	27	ASP	-1	-0.843	-0.883	26.983	-0.120	-0.120	0.000	0.000	0.000	0.000
27	A	28	LEU	0	-0.050	-0.023	25.940	-0.005	-0.005	0.000	0.000	0.000	0.000
28	A	29	LYS	1	0.858	0.915	25.959	0.090	0.090	0.000	0.000	0.000	0.000
29	A	30	GLU	-1	-0.849	-0.908	21.161	-0.239	-0.239	0.000	0.000	0.000	0.000
30	A	31	ALA	0	-0.033	-0.017	21.569	-0.018	-0.018	0.000	0.000	0.000	0.000
31	A	32	VAL	0	-0.037	-0.020	21.117	0.007	0.007	0.000	0.000	0.000	0.000
32	A	33	ARG	1	0.923	0.959	20.320	0.166	0.166	0.000	0.000	0.000	0.000
33	A	34	LEU	0	0.026	0.014	17.005	-0.020	-0.020	0.000	0.000	0.000	0.000
34	A	35	ALA	0	-0.025	-0.019	16.045	-0.010	-0.010	0.000	0.000	0.000	0.000
35	A	36	GLU	-1	-0.910	-0.981	16.594	-0.058	-0.058	0.000	0.000	0.000	0.000
36	A	37	GLU	-1	-0.940	-0.962	13.265	-0.441	-0.441	0.000	0.000	0.000	0.000
37	A	38	VAL	0	-0.031	-0.010	11.759	-0.010	-0.010	0.000	0.000	0.000	0.000
38	A	39	VAL	0	-0.117	-0.066	12.409	0.088	0.088	0.000	0.000	0.000	0.000
39	A	40	ARG	1	0.884	0.943	13.535	0.408	0.408	0.000	0.000	0.000	0.000
40	A	41	GLU	-1	-0.821	-0.891	8.391	-0.554	-0.554	0.000	0.000	0.000	0.000
41	A	42	ARG	1	0.874	0.936	5.328	-1.341	-1.341	0.000	0.000	0.000	0.000
42	A	43	PRO	0	0.107	0.060	10.172	0.085	0.085	0.000	0.000	0.000	0.000
43	A	44	GLY	0	0.004	0.009	12.948	0.090	0.090	0.000	0.000	0.000	0.000
44	A	45	SER	0	-0.048	-0.024	10.568	0.075	0.075	0.000	0.000	0.000	0.000
45	A	46	ASN	0	0.027	-0.015	12.548	-0.111	-0.111	0.000	0.000	0.000	0.000
46	A	47	LEU	0	-0.007	0.002	9.308	-0.033	-0.033	0.000	0.000	0.000	0.000
47	A	48	ALA	0	0.045	0.036	13.099	-0.085	-0.085	0.000	0.000	0.000	0.000
48	A	49	LYS	1	0.908	0.944	14.626	-0.469	-0.469	0.000	0.000	0.000	0.000
49	A	50	LYS	1	0.825	0.908	16.702	-0.185	-0.185	0.000	0.000	0.000	0.000
50	A	51	ALA	0	0.044	0.015	16.181	-0.034	-0.034	0.000	0.000	0.000	0.000
51	A	52	LEU	0	0.009	0.008	18.207	-0.028	-0.028	0.000	0.000	0.000	0.000
52	A	53	GLU	-1	-0.819	-0.882	20.970	0.128	0.128	0.000	0.000	0.000	0.000
53	A	54	ILE	0	-0.061	-0.025	20.156	-0.011	-0.011	0.000	0.000	0.000	0.000
54	A	55	ILE	0	0.030	0.014	19.724	-0.010	-0.010	0.000	0.000	0.000	0.000
55	A	56	LEU	0	-0.008	0.000	23.695	-0.008	-0.008	0.000	0.000	0.000	0.000
56	A	57	ARG	1	0.823	0.891	23.306	-0.064	-0.064	0.000	0.000	0.000	0.000
57	A	58	ALA	0	0.064	0.034	26.076	-0.004	-0.004	0.000	0.000	0.000	0.000
58	A	59	ALA	0	0.004	0.003	27.803	-0.005	-0.005	0.000	0.000	0.000	0.000
59	A	60	GLU	-1	-0.858	-0.939	29.507	0.026	0.026	0.000	0.000	0.000	0.000
60	A	61	GLU	-1	-0.819	-0.890	31.455	-0.007	-0.007	0.000	0.000	0.000	0.000
61	A	62	LEU	0	-0.014	-0.006	28.695	-0.003	-0.003	0.000	0.000	0.000	0.000
62	A	63	ALA	0	-0.027	-0.013	32.944	-0.002	-0.002	0.000	0.000	0.000	0.000
63	A	64	LYS	1	0.722	0.838	35.319	0.006	0.006	0.000	0.000	0.000	0.000
64	A	65	LEU	0	0.024	0.026	34.446	0.000	0.000	0.000	0.000	0.000	0.000
65	A	66	PRO	0	-0.011	-0.011	38.326	0.000	0.000	0.000	0.000	0.000	0.000
66	A	67	ASP	-1	-0.826	-0.921	35.421	-0.068	-0.068	0.000	0.000	0.000	0.000
67	A	68	PRO	0	0.027	-0.004	37.048	0.001	0.001	0.000	0.000	0.000	0.000
68	A	69	GLU	-1	-0.924	-0.964	31.737	-0.085	-0.085	0.000	0.000	0.000	0.000
69	A	70	ALA	0	0.005	0.004	32.388	-0.003	-0.003	0.000	0.000	0.000	0.000
70	A	71	LEU	0	-0.027	0.001	32.489	0.003	0.003	0.000	0.000	0.000	0.000
71	A	72	LYS	1	0.891	0.948	32.838	0.065	0.065	0.000	0.000	0.000	0.000
72	A	73	GLU	-1	-0.861	-0.930	26.944	-0.104	-0.104	0.000	0.000	0.000	0.000
73	A	74	ALA	0	0.008	0.004	28.724	0.004	0.004	0.000	0.000	0.000	0.000
74	A	75	VAL	0	-0.020	-0.016	30.262	0.010	0.010	0.000	0.000	0.000	0.000
75	A	76	LYS	1	0.823	0.909	27.350	0.100	0.100	0.000	0.000	0.000	0.000
76	A	77	ALA	0	0.050	0.035	25.431	0.005	0.005	0.000	0.000	0.000	0.000
77	A	78	ALA	0	0.006	-0.003	25.849	0.014	0.014	0.000	0.000	0.000	0.000
78	A	79	GLU	-1	-0.842	-0.909	28.083	0.023	0.023	0.000	0.000	0.000	0.000
79	A	80	LYS	1	0.837	0.916	19.707	0.017	0.017	0.000	0.000	0.000	0.000
80	A	81	VAL	0	0.011	0.004	23.706	0.019	0.019	0.000	0.000	0.000	0.000
81	A	82	VAL	0	-0.043	-0.014	24.899	0.020	0.020	0.000	0.000	0.000	0.000
82	A	83	ARG	1	0.824	0.907	22.026	-0.012	-0.012	0.000	0.000	0.000	0.000
83	A	84	GLU	-1	-0.800	-0.884	20.384	0.051	0.051	0.000	0.000	0.000	0.000
84	A	85	GLN	0	-0.053	-0.025	21.172	0.052	0.052	0.000	0.000	0.000	0.000
85	A	86	PRO	0	0.050	0.024	24.127	-0.004	-0.004	0.000	0.000	0.000	0.000
86	A	87	GLY	0	-0.028	-0.003	26.042	-0.005	-0.005	0.000	0.000	0.000	0.000
87	A	88	SER	0	-0.015	-0.010	25.219	0.007	0.007	0.000	0.000	0.000	0.000
88	A	89	ASN	0	0.032	0.004	27.364	-0.014	-0.014	0.000	0.000	0.000	0.000
89	A	90	LEU	0	0.009	0.003	24.057	-0.010	-0.010	0.000	0.000	0.000	0.000
90	A	91	ALA	0	0.040	0.030	27.946	-0.013	-0.013	0.000	0.000	0.000	0.000
91	A	92	LYS	1	0.929	0.963	29.143	-0.069	-0.069	0.000	0.000	0.000	0.000
92	A	93	LYS	1	0.883	0.947	30.551	-0.041	-0.041	0.000	0.000	0.000	0.000
93	A	94	ALA	0	0.014	0.003	28.627	-0.009	-0.009	0.000	0.000	0.000	0.000
94	A	95	LEU	0	0.003	0.000	30.729	-0.009	-0.009	0.000	0.000	0.000	0.000
95	A	96	GLU	-1	-0.939	-0.976	33.839	0.039	0.039	0.000	0.000	0.000	0.000
96	A	97	ILE	0	-0.036	-0.014	30.877	-0.005	-0.005	0.000	0.000	0.000	0.000
97	A	98	ILE	0	-0.005	0.003	31.244	-0.007	-0.007	0.000	0.000	0.000	0.000
98	A	99	LEU	0	-0.004	-0.001	34.908	-0.005	-0.005	0.000	0.000	0.000	0.000
99	A	100	ARG	1	0.810	0.887	37.088	0.005	0.005	0.000	0.000	0.000	0.000
100	A	101	ALA	0	0.070	0.027	35.379	-0.003	-0.003	0.000	0.000	0.000	0.000
101	A	102	ALA	0	0.011	0.013	37.506	-0.004	-0.004	0.000	0.000	0.000	0.000
102	A	103	GLU	-1	-0.811	-0.909	39.848	0.002	0.002	0.000	0.000	0.000	0.000
103	A	104	GLU	-1	-0.791	-0.857	39.851	-0.017	-0.017	0.000	0.000	0.000	0.000
104	A	105	LEU	0	0.006	0.000	37.284	-0.002	-0.002	0.000	0.000	0.000	0.000
105	A	106	ALA	0	-0.053	-0.028	41.613	-0.001	-0.001	0.000	0.000	0.000	0.000
106	A	107	LYS	1	0.780	0.881	44.011	0.015	0.015	0.000	0.000	0.000	0.000
107	A	108	LEU	0	-0.018	0.009	40.900	-0.001	-0.001	0.000	0.000	0.000	0.000
108	A	109	PRO	0	-0.014	-0.001	45.529	0.001	0.001	0.000	0.000	0.000	0.000
109	A	110	ASP	-1	-0.822	-0.932	44.167	-0.045	-0.045	0.000	0.000	0.000	0.000
110	A	111	PRO	0	0.036	0.015	45.866	0.002	0.002	0.000	0.000	0.000	0.000
111	A	112	GLU	-1	-0.871	-0.938	39.557	-0.050	-0.050	0.000	0.000	0.000	0.000
112	A	113	ALA	0	0.012	0.016	41.196	0.000	0.000	0.000	0.000	0.000	0.000
113	A	114	LEU	0	0.015	0.011	42.009	0.003	0.003	0.000	0.000	0.000	0.000
114	A	115	LYS	1	0.814	0.879	42.594	0.038	0.038	0.000	0.000	0.000	0.000
115	A	116	GLU	-1	-0.845	-0.916	36.087	-0.041	-0.041	0.000	0.000	0.000	0.000
116	A	117	ALA	0	0.006	0.010	38.970	0.003	0.003	0.000	0.000	0.000	0.000
117	A	118	VAL	0	-0.017	-0.010	41.048	0.004	0.004	0.000	0.000	0.000	0.000
118	A	119	LYS	1	0.873	0.929	36.672	0.044	0.044	0.000	0.000	0.000	0.000
119	A	120	ALA	0	-0.001	-0.003	36.440	0.003	0.003	0.000	0.000	0.000	0.000
120	A	121	ALA	0	0.015	0.001	37.424	0.006	0.006	0.000	0.000	0.000	0.000
121	A	122	GLU	-1	-0.841	-0.933	40.167	-0.001	-0.001	0.000	0.000	0.000	0.000
122	A	123	LYS	1	0.891	0.964	31.307	0.020	0.020	0.000	0.000	0.000	0.000
123	A	124	VAL	0	-0.002	-0.001	36.216	0.006	0.006	0.000	0.000	0.000	0.000
124	A	125	VAL	0	-0.042	-0.017	37.563	0.006	0.006	0.000	0.000	0.000	0.000
125	A	126	ARG	1	0.815	0.889	37.408	-0.009	-0.009	0.000	0.000	0.000	0.000
126	A	127	GLH	0	-0.067	-0.054	31.238	0.006	0.006	0.000	0.000	0.000	0.000
127	A	128	GLN	0	-0.029	-0.018	34.771	0.010	0.010	0.000	0.000	0.000	0.000
128	A	129	PRO	0	0.052	0.049	37.887	-0.002	-0.002	0.000	0.000	0.000	0.000
129	A	130	GLY	0	0.007	-0.001	41.184	0.004	0.004	0.000	0.000	0.000	0.000
130	A	131	SER	0	-0.036	-0.022	40.639	0.001	0.001	0.000	0.000	0.000	0.000
131	A	132	GLU	-1	-0.770	-0.886	42.856	0.024	0.024	0.000	0.000	0.000	0.000
132	A	133	LEU	0	0.016	0.012	37.233	-0.003	-0.003	0.000	0.000	0.000	0.000
133	A	134	ALA	0	0.008	0.017	41.378	-0.004	-0.004	0.000	0.000	0.000	0.000
134	A	135	LYS	1	0.833	0.883	42.539	-0.029	-0.029	0.000	0.000	0.000	0.000
135	A	136	LYS	1	0.897	0.948	43.561	-0.012	-0.012	0.000	0.000	0.000	0.000
136	A	137	ALA	0	0.006	-0.002	41.365	-0.003	-0.003	0.000	0.000	0.000	0.000
137	A	138	LEU	0	0.004	-0.003	43.374	-0.004	-0.004	0.000	0.000	0.000	0.000
138	A	139	GLU	-1	-0.946	-0.967	46.464	0.008	0.008	0.000	0.000	0.000	0.000
139	A	140	ILE	0	-0.063	-0.019	42.809	-0.002	-0.002	0.000	0.000	0.000	0.000
140	A	141	ILE	0	0.005	0.010	43.034	-0.003	-0.003	0.000	0.000	0.000	0.000
141	A	142	GLU	-1	-0.791	-0.877	46.425	0.000	0.000	0.000	0.000	0.000	0.000
142	A	143	ARG	1	0.855	0.918	46.850	0.000	0.000	0.000	0.000	0.000	0.000
143	A	144	ALA	0	0.060	0.023	46.105	-0.002	-0.002	0.000	0.000	0.000	0.000
144	A	145	ALA	0	0.004	0.007	48.121	-0.002	-0.002	0.000	0.000	0.000	0.000
145	A	146	GLU	-1	-0.892	-0.949	50.091	-0.009	-0.009	0.000	0.000	0.000	0.000
146	A	147	GLU	-1	-0.886	-0.912	50.031	-0.015	-0.015	0.000	0.000	0.000	0.000
147	A	148	LEU	0	-0.040	-0.022	46.660	-0.002	-0.002	0.000	0.000	0.000	0.000
148	A	149	LYS	1	0.715	0.838	51.110	0.009	0.009	0.000	0.000	0.000	0.000
149	A	150	LYS	1	0.807	0.883	54.683	0.013	0.013	0.000	0.000	0.000	0.000
150	A	151	SER	0	-0.030	-0.016	52.267	-0.001	-0.001	0.000	0.000	0.000	0.000
151	A	152	PRO	0	-0.005	-0.009	54.403	0.001	0.001	0.000	0.000	0.000	0.000
152	A	153	ASP	-1	-0.868	-0.910	52.085	-0.031	-0.031	0.000	0.000	0.000	0.000
153	A	154	PRO	0	0.013	-0.012	54.092	0.001	0.001	0.000	0.000	0.000	0.000
154	A	155	GLU	-1	-0.966	-0.979	49.664	-0.034	-0.034	0.000	0.000	0.000	0.000
155	A	156	ALA	0	0.073	0.039	49.669	0.001	0.001	0.000	0.000	0.000	0.000
156	A	157	GLN	0	0.022	0.012	50.702	0.003	0.003	0.000	0.000	0.000	0.000
157	A	158	LYS	1	0.907	0.955	51.609	0.020	0.020	0.000	0.000	0.000	0.000
158	A	159	GLU	-1	-0.818	-0.904	45.321	-0.027	-0.027	0.000	0.000	0.000	0.000
159	A	160	ALA	0	0.012	0.018	49.208	0.002	0.002	0.000	0.000	0.000	0.000
160	A	161	LYS	1	0.880	0.914	51.124	0.010	0.010	0.000	0.000	0.000	0.000
161	A	162	LYS	1	0.861	0.916	49.095	0.009	0.009	0.000	0.000	0.000	0.000
162	A	163	ALA	0	0.048	0.027	47.636	0.002	0.002	0.000	0.000	0.000	0.000
163	A	164	GLU	-1	-0.759	-0.847	48.838	-0.004	-0.004	0.000	0.000	0.000	0.000
164	A	165	GLN	0	-0.102	-0.043	51.909	0.000	0.000	0.000	0.000	0.000	0.000
165	A	166	LYS	1	0.872	0.939	44.129	0.001	0.001	0.000	0.000	0.000	0.000
166	A	167	VAL	0	0.006	0.008	48.057	0.003	0.003	0.000	0.000	0.000	0.000
167	A	168	ARG	1	0.799	0.872	49.804	0.002	0.002	0.000	0.000	0.000	0.000
168	A	169	GLU	-1	-0.887	-0.929	50.924	0.004	0.004	0.000	0.000	0.000	0.000
169	A	170	GLU	-1	-0.831	-0.899	45.047	0.011	0.011	0.000	0.000	0.000	0.000
170	A	171	ARG	1	0.791	0.896	48.934	-0.005	-0.005	0.000	0.000	0.000	0.000
171	A	172	PRO	0	0.005	0.009	51.282	0.000	0.000	0.000	0.000	0.000	0.000
172	A	173	GLY	0	-0.021	-0.011	53.834	-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)