FMO DATABASE

FMODB ID: MV5JZ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1673935.322234
FMO2-HF: Nuclear repulsion	1608690.158704
FMO2-HF: Total energy	-65245.16353
FMO2-MP2: Total energy	-65440.739877

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.
-2.289	-0.526	7.683	-4.223	-5.223	-0.008

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 : 0.006 / 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	-0.861	-0.929	3.065	-4.336	-1.664	0.031	-1.265	-1.438	0.003
4	A	5	GLU	-1	-0.860	-0.923	1.732	-2.621	-3.928	7.647	-3.000	-3.341	-0.011
5	A	6	LYS	1	0.869	0.932	3.311	2.214	2.481	0.006	0.048	-0.321	0.000
6	A	7	GLU	-1	-0.832	-0.939	5.381	-0.078	0.053	-0.001	-0.006	-0.123	0.000
7	A	8	LYS	1	1.029	1.035	6.589	1.384	1.384	0.000	0.000	0.000	0.000
8	A	9	LEU	0	0.018	0.008	6.860	0.406	0.406	0.000	0.000	0.000	0.000
9	A	10	LYS	1	0.817	0.897	9.171	1.000	1.000	0.000	0.000	0.000	0.000
10	A	11	GLU	-1	-0.957	-0.965	10.937	-0.581	-0.581	0.000	0.000	0.000	0.000
11	A	12	LEU	0	0.014	0.014	11.035	0.101	0.101	0.000	0.000	0.000	0.000
12	A	13	LEU	0	-0.019	-0.004	13.356	0.085	0.085	0.000	0.000	0.000	0.000
13	A	14	LYS	1	0.957	0.985	15.088	0.352	0.352	0.000	0.000	0.000	0.000
14	A	15	ARG	1	0.953	0.979	16.738	0.324	0.324	0.000	0.000	0.000	0.000
15	A	16	ALA	0	0.030	0.017	17.768	0.036	0.036	0.000	0.000	0.000	0.000
16	A	17	GLU	-1	-0.986	-1.014	18.596	-0.178	-0.178	0.000	0.000	0.000	0.000
17	A	18	GLU	-1	-1.002	-1.010	21.196	-0.212	-0.212	0.000	0.000	0.000	0.000
18	A	19	LEU	0	0.025	0.015	21.396	0.015	0.015	0.000	0.000	0.000	0.000
19	A	20	ALA	0	-0.002	0.001	23.741	0.015	0.015	0.000	0.000	0.000	0.000
20	A	21	LYS	1	0.836	0.924	24.670	0.152	0.152	0.000	0.000	0.000	0.000
21	A	22	SER	0	-0.062	-0.024	27.980	0.011	0.011	0.000	0.000	0.000	0.000
22	A	23	PRO	0	-0.011	-0.014	29.900	0.002	0.002	0.000	0.000	0.000	0.000
23	A	24	ASP	-1	-0.860	-0.930	30.627	-0.084	-0.084	0.000	0.000	0.000	0.000
24	A	25	PRO	0	0.025	-0.005	30.278	-0.005	-0.005	0.000	0.000	0.000	0.000
25	A	26	GLU	-1	-0.925	-0.970	29.137	-0.093	-0.093	0.000	0.000	0.000	0.000
26	A	27	ASP	-1	-0.821	-0.892	26.387	-0.132	-0.132	0.000	0.000	0.000	0.000
27	A	28	LEU	0	-0.043	-0.021	25.291	-0.012	-0.012	0.000	0.000	0.000	0.000
28	A	29	LYS	1	0.911	0.951	25.338	0.070	0.070	0.000	0.000	0.000	0.000
29	A	30	GLU	-1	-0.866	-0.934	20.568	-0.189	-0.189	0.000	0.000	0.000	0.000
30	A	31	ALA	0	-0.028	-0.014	21.059	-0.022	-0.022	0.000	0.000	0.000	0.000
31	A	32	VAL	0	-0.036	-0.015	20.425	-0.015	-0.015	0.000	0.000	0.000	0.000
32	A	33	ARG	1	0.947	0.979	20.095	0.114	0.114	0.000	0.000	0.000	0.000
33	A	34	LEU	0	0.026	0.016	16.378	-0.019	-0.019	0.000	0.000	0.000	0.000
34	A	35	ALA	0	-0.015	-0.012	15.467	-0.040	-0.040	0.000	0.000	0.000	0.000
35	A	36	GLU	-1	-0.939	-0.997	15.932	-0.104	-0.104	0.000	0.000	0.000	0.000
36	A	37	GLU	-1	-0.950	-0.975	13.070	-0.270	-0.270	0.000	0.000	0.000	0.000
37	A	38	VAL	0	-0.018	-0.001	11.151	-0.021	-0.021	0.000	0.000	0.000	0.000
38	A	39	VAL	0	-0.117	-0.063	11.844	0.015	0.015	0.000	0.000	0.000	0.000
39	A	40	ARG	1	0.912	0.964	13.879	0.163	0.163	0.000	0.000	0.000	0.000
40	A	41	GLU	-1	-0.872	-0.923	8.285	-0.027	-0.027	0.000	0.000	0.000	0.000
41	A	42	ARG	1	0.879	0.947	4.956	0.179	0.179	0.000	0.000	0.000	0.000
42	A	43	PRO	0	0.094	0.065	10.174	0.004	0.004	0.000	0.000	0.000	0.000
43	A	44	GLY	0	-0.008	0.004	12.942	0.046	0.046	0.000	0.000	0.000	0.000
44	A	45	SER	0	-0.072	-0.054	10.538	0.007	0.007	0.000	0.000	0.000	0.000
45	A	46	ASN	0	0.019	-0.020	12.569	-0.035	-0.035	0.000	0.000	0.000	0.000
46	A	47	LEU	0	-0.014	-0.002	9.198	-0.003	-0.003	0.000	0.000	0.000	0.000
47	A	48	ALA	0	0.056	0.042	13.127	-0.014	-0.014	0.000	0.000	0.000	0.000
48	A	49	LYS	1	0.946	0.966	14.561	-0.055	-0.055	0.000	0.000	0.000	0.000
49	A	50	LYS	1	0.923	0.977	16.454	0.121	0.121	0.000	0.000	0.000	0.000
50	A	51	ALA	0	0.051	0.018	15.602	0.002	0.002	0.000	0.000	0.000	0.000
51	A	52	LEU	0	-0.013	-0.002	17.687	0.008	0.008	0.000	0.000	0.000	0.000
52	A	53	GLU	-1	-0.945	-0.974	20.631	-0.053	-0.053	0.000	0.000	0.000	0.000
53	A	54	ILE	0	-0.056	-0.028	19.543	0.007	0.007	0.000	0.000	0.000	0.000
54	A	55	ILE	0	0.026	0.014	19.210	0.006	0.006	0.000	0.000	0.000	0.000
55	A	56	LEU	0	0.000	0.000	22.910	0.008	0.008	0.000	0.000	0.000	0.000
56	A	57	ARG	1	0.938	0.971	23.513	0.100	0.100	0.000	0.000	0.000	0.000
57	A	58	ALA	0	0.075	0.042	25.289	0.004	0.004	0.000	0.000	0.000	0.000
58	A	59	ALA	0	0.000	0.002	27.012	0.005	0.005	0.000	0.000	0.000	0.000
59	A	60	GLU	-1	-0.963	-1.008	28.789	-0.043	-0.043	0.000	0.000	0.000	0.000
60	A	61	GLU	-1	-0.888	-0.940	30.629	-0.056	-0.056	0.000	0.000	0.000	0.000
61	A	62	LEU	0	-0.027	-0.009	28.172	0.003	0.003	0.000	0.000	0.000	0.000
62	A	63	ALA	0	-0.024	-0.012	32.295	0.004	0.004	0.000	0.000	0.000	0.000
63	A	64	LYS	1	0.793	0.890	34.669	0.055	0.055	0.000	0.000	0.000	0.000
64	A	65	LEU	0	0.018	0.025	33.976	0.002	0.002	0.000	0.000	0.000	0.000
65	A	66	PRO	0	0.030	0.011	37.719	0.001	0.001	0.000	0.000	0.000	0.000
66	A	67	ASP	-1	-0.843	-0.937	35.255	-0.053	-0.053	0.000	0.000	0.000	0.000
67	A	68	PRO	0	0.021	0.000	36.679	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	69	GLU	-1	-0.963	-0.980	31.342	-0.055	-0.055	0.000	0.000	0.000	0.000
69	A	70	ALA	0	0.014	0.007	32.008	-0.003	-0.003	0.000	0.000	0.000	0.000
70	A	71	LEU	0	-0.011	0.008	32.069	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	72	LYS	1	0.954	0.977	32.755	0.039	0.039	0.000	0.000	0.000	0.000
72	A	73	GLU	-1	-0.936	-0.964	26.402	-0.076	-0.076	0.000	0.000	0.000	0.000
73	A	74	ALA	0	0.023	0.011	28.338	-0.002	-0.002	0.000	0.000	0.000	0.000
74	A	75	VAL	0	-0.024	-0.014	29.753	0.003	0.003	0.000	0.000	0.000	0.000
75	A	76	LYS	1	0.903	0.942	27.222	0.056	0.056	0.000	0.000	0.000	0.000
76	A	77	ALA	0	0.070	0.048	25.029	0.002	0.002	0.000	0.000	0.000	0.000
77	A	78	ALA	0	-0.001	-0.006	25.334	0.001	0.001	0.000	0.000	0.000	0.000
78	A	79	GLU	-1	-0.841	-0.917	27.741	-0.006	-0.006	0.000	0.000	0.000	0.000
79	A	80	LYS	1	0.870	0.946	19.796	0.076	0.076	0.000	0.000	0.000	0.000
80	A	81	VAL	0	-0.007	-0.001	23.427	0.005	0.005	0.000	0.000	0.000	0.000
81	A	82	VAL	0	-0.035	-0.010	24.714	0.009	0.009	0.000	0.000	0.000	0.000
82	A	83	ARG	1	0.911	0.953	22.130	0.009	0.009	0.000	0.000	0.000	0.000
83	A	84	GLU	-1	-0.876	-0.943	19.730	-0.026	-0.026	0.000	0.000	0.000	0.000
84	A	85	GLN	0	-0.044	-0.019	21.210	0.019	0.019	0.000	0.000	0.000	0.000
85	A	86	PRO	0	0.049	0.024	24.140	-0.003	-0.003	0.000	0.000	0.000	0.000
86	A	87	GLY	0	-0.029	-0.007	26.052	0.000	0.000	0.000	0.000	0.000	0.000
87	A	88	SER	0	-0.013	-0.009	25.334	0.000	0.000	0.000	0.000	0.000	0.000
88	A	89	ASN	0	0.031	0.005	27.387	0.000	0.000	0.000	0.000	0.000	0.000
89	A	90	LEU	0	0.012	0.001	24.047	-0.002	-0.002	0.000	0.000	0.000	0.000
90	A	91	ALA	0	0.038	0.033	28.000	-0.005	-0.005	0.000	0.000	0.000	0.000
91	A	92	LYS	1	0.974	0.980	29.163	0.001	0.001	0.000	0.000	0.000	0.000
92	A	93	LYS	1	0.958	0.996	30.416	0.031	0.031	0.000	0.000	0.000	0.000
93	A	94	ALA	0	0.020	0.008	28.439	-0.003	-0.003	0.000	0.000	0.000	0.000
94	A	95	LEU	0	0.005	0.000	30.467	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	96	GLU	-1	-0.952	-0.982	33.635	-0.018	-0.018	0.000	0.000	0.000	0.000
96	A	97	ILE	0	-0.035	-0.008	30.064	0.000	0.000	0.000	0.000	0.000	0.000
97	A	98	ILE	0	-0.011	0.000	30.993	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	99	LEU	0	0.001	-0.006	34.371	0.000	0.000	0.000	0.000	0.000	0.000
99	A	100	ARG	1	0.792	0.888	36.468	0.033	0.033	0.000	0.000	0.000	0.000
100	A	101	ALA	0	0.070	0.023	34.832	0.000	0.000	0.000	0.000	0.000	0.000
101	A	102	ALA	0	0.004	0.008	36.965	0.000	0.000	0.000	0.000	0.000	0.000
102	A	103	GLU	-1	-0.919	-0.978	39.401	-0.019	-0.019	0.000	0.000	0.000	0.000
103	A	104	GLU	-1	-0.829	-0.902	39.292	-0.032	-0.032	0.000	0.000	0.000	0.000
104	A	105	LEU	0	-0.015	-0.009	36.993	0.000	0.000	0.000	0.000	0.000	0.000
105	A	106	ALA	0	-0.045	-0.027	41.237	0.001	0.001	0.000	0.000	0.000	0.000
106	A	107	LYS	1	0.859	0.942	43.829	0.028	0.028	0.000	0.000	0.000	0.000
107	A	108	LEU	0	-0.019	0.007	40.573	0.000	0.000	0.000	0.000	0.000	0.000
108	A	109	PRO	0	-0.011	0.003	45.193	0.001	0.001	0.000	0.000	0.000	0.000
109	A	110	ASP	-1	-0.816	-0.932	44.459	-0.026	-0.026	0.000	0.000	0.000	0.000
110	A	111	PRO	0	0.029	0.015	45.718	0.000	0.000	0.000	0.000	0.000	0.000
111	A	112	GLU	-1	-0.940	-0.983	40.694	-0.024	-0.024	0.000	0.000	0.000	0.000
112	A	113	ALA	0	-0.017	0.009	41.042	-0.001	-0.001	0.000	0.000	0.000	0.000
113	A	114	LEU	0	0.023	0.017	41.806	0.001	0.001	0.000	0.000	0.000	0.000
114	A	115	LYS	1	0.862	0.925	42.443	0.018	0.018	0.000	0.000	0.000	0.000
115	A	116	GLU	-1	-0.967	-0.987	36.108	-0.026	-0.026	0.000	0.000	0.000	0.000
116	A	117	ALA	0	0.030	0.024	38.762	0.000	0.000	0.000	0.000	0.000	0.000
117	A	118	VAL	0	-0.025	-0.010	40.748	0.001	0.001	0.000	0.000	0.000	0.000
118	A	119	LYS	1	0.968	0.986	36.949	0.020	0.020	0.000	0.000	0.000	0.000
119	A	120	ALA	0	0.002	0.000	36.179	0.001	0.001	0.000	0.000	0.000	0.000
120	A	121	ALA	0	0.023	0.004	37.113	0.001	0.001	0.000	0.000	0.000	0.000
121	A	122	GLU	-1	-0.916	-0.983	39.800	-0.005	-0.005	0.000	0.000	0.000	0.000
122	A	123	LYS	1	0.889	0.956	31.112	0.025	0.025	0.000	0.000	0.000	0.000
123	A	124	VAL	0	0.014	0.009	36.003	0.003	0.003	0.000	0.000	0.000	0.000
124	A	125	VAL	0	-0.038	-0.011	37.385	0.002	0.002	0.000	0.000	0.000	0.000
125	A	126	ARG	1	0.918	0.955	37.302	-0.002	-0.002	0.000	0.000	0.000	0.000
126	A	127	GLH	0	-0.059	-0.044	30.912	0.002	0.002	0.000	0.000	0.000	0.000
127	A	128	GLN	0	-0.062	-0.031	34.839	0.001	0.001	0.000	0.000	0.000	0.000
128	A	129	PRO	0	0.052	0.052	37.893	-0.001	-0.001	0.000	0.000	0.000	0.000
129	A	130	GLY	0	-0.003	-0.004	41.186	0.001	0.001	0.000	0.000	0.000	0.000
130	A	131	SER	0	-0.045	-0.032	40.619	-0.001	-0.001	0.000	0.000	0.000	0.000
131	A	132	GLU	-1	-0.879	-0.962	42.869	-0.004	-0.004	0.000	0.000	0.000	0.000
132	A	133	LEU	0	0.021	0.011	37.139	-0.001	-0.001	0.000	0.000	0.000	0.000
133	A	134	ALA	0	-0.001	0.015	41.327	-0.001	-0.001	0.000	0.000	0.000	0.000
134	A	135	LYS	1	0.960	0.972	42.512	-0.001	-0.001	0.000	0.000	0.000	0.000
135	A	136	LYS	1	0.947	0.979	43.306	0.014	0.014	0.000	0.000	0.000	0.000
136	A	137	ALA	0	-0.002	-0.004	41.153	-0.001	-0.001	0.000	0.000	0.000	0.000
137	A	138	LEU	0	-0.012	-0.011	43.074	-0.001	-0.001	0.000	0.000	0.000	0.000
138	A	139	GLU	-1	-0.958	-0.976	46.192	-0.009	-0.009	0.000	0.000	0.000	0.000
139	A	140	ILE	0	-0.065	-0.018	42.183	-0.001	-0.001	0.000	0.000	0.000	0.000
140	A	141	ILE	0	-0.024	-0.003	42.789	-0.001	-0.001	0.000	0.000	0.000	0.000
141	A	142	GLU	-1	-0.908	-0.964	46.100	-0.007	-0.007	0.000	0.000	0.000	0.000
142	A	143	ARG	1	0.951	0.974	47.284	0.015	0.015	0.000	0.000	0.000	0.000
143	A	144	ALA	0	0.041	0.018	45.774	0.000	0.000	0.000	0.000	0.000	0.000
144	A	145	ALA	0	-0.011	-0.001	47.820	0.000	0.000	0.000	0.000	0.000	0.000
145	A	146	GLU	-1	-0.936	-0.988	49.882	-0.009	-0.009	0.000	0.000	0.000	0.000
146	A	147	GLU	-1	-0.967	-0.980	49.739	-0.016	-0.016	0.000	0.000	0.000	0.000
147	A	148	LEU	0	-0.054	-0.032	46.685	0.000	0.000	0.000	0.000	0.000	0.000
148	A	149	LYS	1	0.835	0.926	50.983	0.008	0.008	0.000	0.000	0.000	0.000
149	A	150	LYS	1	0.863	0.936	54.541	0.014	0.014	0.000	0.000	0.000	0.000
150	A	151	SER	0	-0.028	0.010	51.799	0.000	0.000	0.000	0.000	0.000	0.000
151	A	152	PRO	0	0.019	-0.001	54.361	0.001	0.001	0.000	0.000	0.000	0.000
152	A	153	ASP	-1	-0.896	-0.936	51.442	-0.015	-0.015	0.000	0.000	0.000	0.000
153	A	154	PRO	0	-0.011	-0.027	54.196	0.000	0.000	0.000	0.000	0.000	0.000
154	A	155	GLU	-1	-0.954	-0.980	49.766	-0.011	-0.011	0.000	0.000	0.000	0.000
155	A	156	ALA	0	0.079	0.048	49.741	0.000	0.000	0.000	0.000	0.000	0.000
156	A	157	GLN	0	0.020	0.015	50.773	0.001	0.001	0.000	0.000	0.000	0.000
157	A	158	LYS	1	0.880	0.941	51.455	0.006	0.006	0.000	0.000	0.000	0.000
158	A	159	GLU	-1	-0.846	-0.951	46.045	-0.012	-0.012	0.000	0.000	0.000	0.000
159	A	160	ALA	0	0.026	0.026	49.187	0.001	0.001	0.000	0.000	0.000	0.000
160	A	161	LYS	1	0.931	0.959	51.057	0.006	0.006	0.000	0.000	0.000	0.000
161	A	162	LYS	1	0.926	0.959	49.014	0.002	0.002	0.000	0.000	0.000	0.000
162	A	163	ALA	0	0.033	0.024	47.575	0.001	0.001	0.000	0.000	0.000	0.000
163	A	164	GLU	-1	-0.809	-0.922	48.735	-0.006	-0.006	0.000	0.000	0.000	0.000
164	A	165	GLN	0	-0.123	-0.051	51.769	0.000	0.000	0.000	0.000	0.000	0.000
165	A	166	LYS	1	0.951	0.984	44.048	0.005	0.005	0.000	0.000	0.000	0.000
166	A	167	VAL	0	0.012	0.014	47.840	0.001	0.001	0.000	0.000	0.000	0.000
167	A	168	ARG	1	0.892	0.940	49.593	0.004	0.004	0.000	0.000	0.000	0.000
168	A	169	GLU	-1	-0.969	-0.981	50.883	0.003	0.003	0.000	0.000	0.000	0.000
169	A	170	GLU	-1	-0.941	-0.966	45.246	0.001	0.001	0.000	0.000	0.000	0.000
170	A	171	ARG	1	0.877	0.955	48.933	0.004	0.004	0.000	0.000	0.000	0.000
171	A	172	PRO	0	-0.022	-0.004	51.283	0.001	0.001	0.000	0.000	0.000	0.000
172	A	173	GLY	0	0.005	0.003	53.835	-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)