FMO DATABASE

FMODB ID: J3VQ9

Calculation Name: 3CWX-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3CWX

Chain ID: A

ChEMBL ID:

UniProt ID: P94837

Base Structure: X-ray

Registration Date: 2023-03-14

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	129
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1198710.760706
FMO2-HF: Nuclear repulsion	1144879.498733
FMO2-HF: Total energy	-53831.261973
FMO2-MP2: Total energy	-53987.055561

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:47:GLU)

Summations of interaction energy for fragment #1(A:47:GLU)

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.
26.92	30.355	0.214	-1.315	-2.336	-0.003

Interaction energy analysis for fragmet #1(A:47:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.957 / q_NPA : -0.992

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	49	ASN	0	-0.007	-0.029	3.861	-5.646	-4.165	-0.009	-0.627	-0.846	0.002
4	A	50	PRO	0	-0.052	-0.002	6.292	-1.740	-1.740	0.000	0.000	0.000	0.000
5	A	51	ASP	-1	-0.743	-0.873	9.190	15.759	15.759	0.000	0.000	0.000	0.000
6	A	52	ILE	0	-0.042	-0.010	11.022	-1.244	-1.244	0.000	0.000	0.000	0.000
7	A	53	ILE	0	0.046	0.013	12.767	0.385	0.385	0.000	0.000	0.000	0.000
8	A	54	LYS	1	0.767	0.860	15.366	-16.254	-16.254	0.000	0.000	0.000	0.000
9	A	55	ASP	-1	-0.876	-0.931	17.954	13.249	13.249	0.000	0.000	0.000	0.000
10	A	56	GLU	-1	-0.814	-0.895	12.824	18.372	18.372	0.000	0.000	0.000	0.000
11	A	57	VAL	0	-0.055	-0.029	16.967	-0.263	-0.263	0.000	0.000	0.000	0.000
12	A	58	PHE	0	0.046	0.025	10.927	0.331	0.331	0.000	0.000	0.000	0.000
13	A	59	ASP	-1	-0.859	-0.927	16.119	12.955	12.955	0.000	0.000	0.000	0.000
14	A	60	PHE	0	-0.019	-0.011	10.666	-0.613	-0.613	0.000	0.000	0.000	0.000
15	A	61	VAL	0	0.019	0.007	15.706	-0.126	-0.126	0.000	0.000	0.000	0.000
16	A	62	ILE	0	-0.004	-0.002	14.003	-0.518	-0.518	0.000	0.000	0.000	0.000
17	A	63	VAL	0	0.049	0.029	13.991	-0.233	-0.233	0.000	0.000	0.000	0.000
18	A	64	ASN	0	-0.019	-0.017	16.757	-0.287	-0.287	0.000	0.000	0.000	0.000
19	A	65	ARG	1	0.830	0.922	20.039	-11.000	-11.000	0.000	0.000	0.000	0.000
20	A	66	VAL	0	-0.018	-0.014	19.109	-0.424	-0.424	0.000	0.000	0.000	0.000
21	A	67	LEU	0	0.055	0.026	13.984	-0.291	-0.291	0.000	0.000	0.000	0.000
22	A	68	LYS	1	0.836	0.925	17.895	-13.420	-13.420	0.000	0.000	0.000	0.000
23	A	69	LYS	1	0.886	0.958	20.447	-10.539	-10.539	0.000	0.000	0.000	0.000
24	A	70	ILE	0	0.005	0.012	19.672	-0.411	-0.411	0.000	0.000	0.000	0.000
25	A	71	LYS	1	0.807	0.890	22.957	-9.449	-9.449	0.000	0.000	0.000	0.000
26	A	72	ASP	-1	-0.836	-0.931	22.454	12.237	12.237	0.000	0.000	0.000	0.000
27	A	73	LEU	0	0.004	0.000	16.208	0.087	0.087	0.000	0.000	0.000	0.000
28	A	74	LYS	1	0.865	0.907	15.427	-15.618	-15.618	0.000	0.000	0.000	0.000
29	A	75	HIS	0	0.044	0.042	19.684	0.324	0.324	0.000	0.000	0.000	0.000
30	A	76	TYR	0	-0.055	-0.040	19.683	-0.210	-0.210	0.000	0.000	0.000	0.000
31	A	77	ASP	-1	-0.903	-0.951	16.742	15.104	15.104	0.000	0.000	0.000	0.000
32	A	78	PRO	0	-0.086	-0.026	14.277	0.710	0.710	0.000	0.000	0.000	0.000
33	A	79	MET	0	-0.019	-0.001	6.822	0.956	0.956	0.000	0.000	0.000	0.000
34	A	80	ILE	0	-0.004	-0.019	8.614	-0.802	-0.802	0.000	0.000	0.000	0.000
35	A	81	GLU	-1	-0.790	-0.880	3.142	35.564	36.219	0.019	-0.138	-0.537	0.000
36	A	82	LYS	1	0.776	0.881	4.544	-23.933	-23.770	-0.001	-0.015	-0.147	0.000
37	A	83	ILE	0	-0.029	-0.007	2.887	4.175	5.081	0.206	-0.494	-0.618	-0.005
38	A	84	PHE	0	0.018	-0.030	3.969	-4.195	-3.965	-0.001	-0.041	-0.188	0.000
39	A	85	ASP	-1	-0.832	-0.887	5.864	29.440	29.440	0.000	0.000	0.000	0.000
40	A	86	GLU	-1	-0.832	-0.927	8.297	21.322	21.322	0.000	0.000	0.000	0.000
41	A	87	LYS	1	0.959	0.968	10.787	-18.482	-18.482	0.000	0.000	0.000	0.000
42	A	88	GLY	0	-0.016	0.000	13.500	-1.267	-1.267	0.000	0.000	0.000	0.000
43	A	89	LYS	1	0.737	0.862	11.274	-23.658	-23.658	0.000	0.000	0.000	0.000
44	A	90	GLU	-1	-0.856	-0.907	7.248	23.786	23.786	0.000	0.000	0.000	0.000
45	A	91	MET	0	-0.030	0.004	8.433	-1.712	-1.712	0.000	0.000	0.000	0.000
46	A	92	GLY	0	0.006	-0.034	8.567	-1.494	-1.494	0.000	0.000	0.000	0.000
47	A	93	LEU	0	-0.005	0.003	7.174	1.166	1.166	0.000	0.000	0.000	0.000
48	A	94	ASN	0	-0.038	-0.024	5.568	-3.877	-3.877	0.000	0.000	0.000	0.000
49	A	95	VAL	0	-0.007	-0.001	7.508	0.088	0.088	0.000	0.000	0.000	0.000
50	A	96	GLU	-1	-0.824	-0.898	10.359	18.651	18.651	0.000	0.000	0.000	0.000
51	A	97	ILE	0	-0.018	-0.005	12.773	-0.078	-0.078	0.000	0.000	0.000	0.000
52	A	98	GLN	0	0.025	0.005	14.922	-1.120	-1.120	0.000	0.000	0.000	0.000
53	A	99	ILE	0	-0.061	-0.042	18.407	-0.450	-0.450	0.000	0.000	0.000	0.000
54	A	100	ASN	0	-0.104	-0.060	21.840	-0.576	-0.576	0.000	0.000	0.000	0.000
55	A	101	PRO	0	0.040	0.040	20.725	0.145	0.145	0.000	0.000	0.000	0.000
56	A	102	GLU	-1	-0.863	-0.927	21.817	11.172	11.172	0.000	0.000	0.000	0.000
57	A	103	VAL	0	-0.072	-0.036	23.837	-0.188	-0.188	0.000	0.000	0.000	0.000
58	A	104	LYS	1	0.918	0.937	14.157	-17.700	-17.700	0.000	0.000	0.000	0.000
59	A	105	ASP	-1	-0.826	-0.903	16.132	17.119	17.119	0.000	0.000	0.000	0.000
60	A	106	PHE	0	-0.047	-0.001	18.772	-0.313	-0.313	0.000	0.000	0.000	0.000
61	A	107	PHE	0	0.000	-0.024	21.500	-0.371	-0.371	0.000	0.000	0.000	0.000
62	A	108	THR	0	0.001	0.020	16.571	0.415	0.415	0.000	0.000	0.000	0.000
63	A	109	PHE	0	0.045	0.006	15.963	-0.392	-0.392	0.000	0.000	0.000	0.000
64	A	110	LYS	1	0.873	0.911	11.988	-17.163	-17.163	0.000	0.000	0.000	0.000
65	A	111	SER	0	-0.038	-0.004	12.425	-1.377	-1.377	0.000	0.000	0.000	0.000
66	A	112	ILE	0	0.024	0.027	9.145	1.005	1.005	0.000	0.000	0.000	0.000
67	A	113	SER	0	-0.021	-0.025	10.275	-1.784	-1.784	0.000	0.000	0.000	0.000
68	A	114	THR	0	-0.022	-0.024	9.899	1.253	1.253	0.000	0.000	0.000	0.000
69	A	115	THR	0	0.036	0.007	11.937	-0.945	-0.945	0.000	0.000	0.000	0.000
70	A	116	ASN	0	-0.027	-0.005	14.313	-0.816	-0.816	0.000	0.000	0.000	0.000
71	A	117	LYS	1	0.933	0.975	15.645	-14.793	-14.793	0.000	0.000	0.000	0.000
72	A	118	GLN	0	0.050	0.029	14.496	0.145	0.145	0.000	0.000	0.000	0.000
73	A	119	ARG	1	0.782	0.851	14.632	-15.993	-15.993	0.000	0.000	0.000	0.000
74	A	120	CYS	0	-0.018	0.004	14.932	0.727	0.727	0.000	0.000	0.000	0.000
75	A	121	PHE	0	0.032	0.009	14.305	-0.425	-0.425	0.000	0.000	0.000	0.000
76	A	122	LEU	0	0.010	0.015	18.098	0.105	0.105	0.000	0.000	0.000	0.000
77	A	123	SER	0	-0.035	-0.033	18.044	-0.004	-0.004	0.000	0.000	0.000	0.000
78	A	124	LEU	0	0.008	0.011	20.003	-0.039	-0.039	0.000	0.000	0.000	0.000
79	A	125	ARG	1	0.921	0.949	22.794	-10.797	-10.797	0.000	0.000	0.000	0.000
80	A	126	GLY	0	0.053	0.043	19.476	-0.043	-0.043	0.000	0.000	0.000	0.000
81	A	127	GLU	-1	-0.854	-0.899	19.990	11.424	11.424	0.000	0.000	0.000	0.000
82	A	128	THR	0	-0.018	-0.011	16.857	0.212	0.212	0.000	0.000	0.000	0.000
83	A	129	ARG	1	0.785	0.895	20.265	-10.819	-10.819	0.000	0.000	0.000	0.000
84	A	130	GLU	-1	-0.790	-0.855	18.665	14.445	14.445	0.000	0.000	0.000	0.000
85	A	131	ILE	0	0.005	-0.009	20.660	-0.632	-0.632	0.000	0.000	0.000	0.000
86	A	132	LEU	0	-0.004	-0.004	21.232	0.373	0.373	0.000	0.000	0.000	0.000
87	A	134	ASP	-1	-0.785	-0.900	21.311	9.703	9.703	0.000	0.000	0.000	0.000
88	A	135	ASN	0	0.036	0.017	24.487	0.258	0.258	0.000	0.000	0.000	0.000
89	A	136	LYS	1	0.914	0.965	26.676	-9.281	-9.281	0.000	0.000	0.000	0.000
90	A	137	LEU	0	0.039	0.034	20.810	-0.054	-0.054	0.000	0.000	0.000	0.000
91	A	138	TYR	0	-0.003	-0.029	19.030	-0.125	-0.125	0.000	0.000	0.000	0.000
92	A	139	ASN	0	-0.004	-0.017	23.482	0.108	0.108	0.000	0.000	0.000	0.000
93	A	140	MET	0	-0.007	0.011	26.375	-0.182	-0.182	0.000	0.000	0.000	0.000
94	A	141	LEU	0	0.012	0.007	19.791	-0.040	-0.040	0.000	0.000	0.000	0.000
95	A	142	LEU	0	-0.041	-0.008	23.483	-0.042	-0.042	0.000	0.000	0.000	0.000
96	A	143	ALA	0	-0.015	-0.006	25.155	-0.138	-0.138	0.000	0.000	0.000	0.000
97	A	144	VAL	0	0.011	0.017	25.028	-0.210	-0.210	0.000	0.000	0.000	0.000
98	A	145	PHE	0	0.050	0.014	19.944	-0.101	-0.101	0.000	0.000	0.000	0.000
99	A	146	ASN	0	-0.057	-0.016	24.603	-0.082	-0.082	0.000	0.000	0.000	0.000
100	A	147	SER	0	0.015	-0.006	27.514	-0.289	-0.289	0.000	0.000	0.000	0.000
101	A	148	TYR	0	-0.006	0.013	27.751	-0.352	-0.352	0.000	0.000	0.000	0.000
102	A	149	ASP	-1	-0.782	-0.886	29.643	8.358	8.358	0.000	0.000	0.000	0.000
103	A	150	PRO	0	-0.009	-0.016	31.687	-0.125	-0.125	0.000	0.000	0.000	0.000
104	A	151	ASN	0	-0.082	-0.048	34.234	-0.308	-0.308	0.000	0.000	0.000	0.000
105	A	152	ASP	-1	-0.856	-0.915	35.972	7.540	7.540	0.000	0.000	0.000	0.000
106	A	153	LEU	0	0.040	0.034	31.818	0.122	0.122	0.000	0.000	0.000	0.000
107	A	154	LEU	0	0.014	0.011	33.659	0.172	0.172	0.000	0.000	0.000	0.000
108	A	155	LYS	1	0.849	0.908	34.455	-7.702	-7.702	0.000	0.000	0.000	0.000
109	A	156	HIS	0	0.008	0.012	26.366	0.270	0.270	0.000	0.000	0.000	0.000
110	A	157	ILE	0	0.032	0.017	30.538	0.187	0.187	0.000	0.000	0.000	0.000
111	A	158	SER	0	-0.033	-0.024	32.017	0.008	0.008	0.000	0.000	0.000	0.000
112	A	159	THR	0	-0.064	-0.041	29.772	0.066	0.066	0.000	0.000	0.000	0.000
113	A	160	VAL	0	0.041	0.019	26.543	0.194	0.194	0.000	0.000	0.000	0.000
114	A	161	GLU	-1	-0.826	-0.904	28.485	9.507	9.507	0.000	0.000	0.000	0.000
115	A	162	SER	0	-0.064	-0.028	30.975	-0.062	-0.062	0.000	0.000	0.000	0.000
116	A	163	LEU	0	0.026	0.008	23.255	0.015	0.015	0.000	0.000	0.000	0.000
117	A	164	LYS	1	0.883	0.934	27.093	-9.582	-9.582	0.000	0.000	0.000	0.000
118	A	165	LYS	1	0.941	0.973	28.322	-8.097	-8.097	0.000	0.000	0.000	0.000
119	A	166	ILE	0	-0.026	-0.018	26.436	-0.067	-0.067	0.000	0.000	0.000	0.000
120	A	167	PHE	0	0.017	-0.003	22.589	0.010	0.010	0.000	0.000	0.000	0.000
121	A	168	TYR	0	0.009	-0.020	26.594	0.108	0.108	0.000	0.000	0.000	0.000
122	A	169	THR	0	-0.063	-0.026	29.602	-0.246	-0.246	0.000	0.000	0.000	0.000
123	A	170	ILE	0	-0.071	-0.012	24.151	-0.128	-0.128	0.000	0.000	0.000	0.000
124	A	171	THR	0	-0.044	-0.027	28.459	0.039	0.039	0.000	0.000	0.000	0.000
125	A	172	CYS	0	-0.040	-0.036	26.110	0.345	0.345	0.000	0.000	0.000	0.000
126	A	173	GLU	-1	-0.884	-0.911	28.439	8.558	8.558	0.000	0.000	0.000	0.000
127	A	174	ALA	0	-0.004	-0.010	30.369	0.205	0.205	0.000	0.000	0.000	0.000
128	A	175	VAL	0	-0.021	-0.008	32.413	-0.213	-0.213	0.000	0.000	0.000	0.000
129	A	176	TYR	0	0.000	0.009	33.260	-0.104	-0.104	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:47:GLU)