FMO DATABASE

FMODB ID: 82Q9Y

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1197359.219375
FMO2-HF: Nuclear repulsion	1143530.382819
FMO2-HF: Total energy	-53828.836556
FMO2-MP2: Total energy	-53984.786521

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.
30.111	33.873	0.518	-1.62	-2.663	-0.008

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 : -0.971 / q_NPA : -0.999

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	0.013	-0.015	3.791	-6.181	-4.585	-0.017	-0.662	-0.917	0.003
4	A	50	PRO	0	-0.061	-0.012	6.132	-1.854	-1.854	0.000	0.000	0.000	0.000
5	A	51	ASP	-1	-0.871	-0.951	8.924	17.024	17.024	0.000	0.000	0.000	0.000
6	A	52	ILE	0	-0.040	-0.003	11.794	-1.072	-1.072	0.000	0.000	0.000	0.000
7	A	53	ILE	0	0.004	-0.010	13.009	0.174	0.174	0.000	0.000	0.000	0.000
8	A	54	LYS	1	0.877	0.919	15.463	-15.084	-15.084	0.000	0.000	0.000	0.000
9	A	55	ASP	-1	-0.957	-0.959	17.962	13.203	13.203	0.000	0.000	0.000	0.000
10	A	56	GLU	-1	-0.865	-0.927	13.485	17.430	17.430	0.000	0.000	0.000	0.000
11	A	57	VAL	0	-0.060	-0.044	17.313	-0.445	-0.445	0.000	0.000	0.000	0.000
12	A	58	PHE	0	0.072	0.029	11.336	0.227	0.227	0.000	0.000	0.000	0.000
13	A	59	ASP	-1	-0.823	-0.890	16.548	12.364	12.364	0.000	0.000	0.000	0.000
14	A	60	PHE	0	-0.050	-0.029	11.006	-0.652	-0.652	0.000	0.000	0.000	0.000
15	A	61	VAL	0	0.051	0.009	16.268	-0.226	-0.226	0.000	0.000	0.000	0.000
16	A	62	ILE	0	-0.014	-0.005	14.584	-0.338	-0.338	0.000	0.000	0.000	0.000
17	A	63	VAL	0	0.065	0.039	14.387	-0.143	-0.143	0.000	0.000	0.000	0.000
18	A	64	ASN	0	-0.043	-0.044	17.140	-0.222	-0.222	0.000	0.000	0.000	0.000
19	A	65	ARG	1	0.903	0.933	20.343	-10.990	-10.990	0.000	0.000	0.000	0.000
20	A	66	VAL	0	-0.031	-0.003	19.380	-0.384	-0.384	0.000	0.000	0.000	0.000
21	A	67	LEU	0	0.064	0.037	14.186	-0.270	-0.270	0.000	0.000	0.000	0.000
22	A	68	LYS	1	0.927	0.980	18.177	-13.673	-13.673	0.000	0.000	0.000	0.000
23	A	69	LYS	1	0.858	0.946	20.719	-10.283	-10.283	0.000	0.000	0.000	0.000
24	A	70	ILE	0	0.044	0.012	20.342	-0.448	-0.448	0.000	0.000	0.000	0.000
25	A	71	LYS	1	0.876	0.937	23.038	-9.316	-9.316	0.000	0.000	0.000	0.000
26	A	72	ASP	-1	-0.886	-0.936	23.313	11.873	11.873	0.000	0.000	0.000	0.000
27	A	73	LEU	0	0.012	-0.011	17.040	0.088	0.088	0.000	0.000	0.000	0.000
28	A	74	LYS	1	0.908	0.937	16.776	-14.934	-14.934	0.000	0.000	0.000	0.000
29	A	75	HIS	0	0.079	0.074	19.883	0.316	0.316	0.000	0.000	0.000	0.000
30	A	76	TYR	0	-0.090	-0.086	19.563	-0.185	-0.185	0.000	0.000	0.000	0.000
31	A	77	ASP	-1	-0.907	-0.957	16.751	15.123	15.123	0.000	0.000	0.000	0.000
32	A	78	PRO	0	-0.079	-0.032	14.389	0.676	0.676	0.000	0.000	0.000	0.000
33	A	79	MET	0	-0.003	0.010	6.747	1.201	1.201	0.000	0.000	0.000	0.000
34	A	80	ILE	0	-0.019	-0.028	8.913	-1.055	-1.055	0.000	0.000	0.000	0.000
35	A	81	GLU	-1	-0.855	-0.931	3.530	37.117	37.893	0.030	-0.279	-0.528	-0.002
36	A	82	LYS	1	0.857	0.935	4.106	-25.667	-25.483	-0.001	-0.021	-0.163	0.000
37	A	83	ILE	0	-0.030	0.011	2.597	1.557	2.585	0.507	-0.638	-0.897	-0.009
38	A	84	PHE	0	0.045	0.005	3.943	-3.275	-3.097	-0.001	-0.020	-0.158	0.000
39	A	85	ASP	-1	-0.879	-0.932	5.710	28.971	28.971	0.000	0.000	0.000	0.000
40	A	86	GLU	-1	-0.834	-0.927	7.888	21.475	21.475	0.000	0.000	0.000	0.000
41	A	87	LYS	1	0.969	0.973	10.551	-18.500	-18.500	0.000	0.000	0.000	0.000
42	A	88	GLY	0	-0.011	0.005	13.308	-1.211	-1.211	0.000	0.000	0.000	0.000
43	A	89	LYS	1	0.742	0.864	10.989	-23.158	-23.158	0.000	0.000	0.000	0.000
44	A	90	GLU	-1	-0.918	-0.959	7.639	23.609	23.609	0.000	0.000	0.000	0.000
45	A	91	MET	0	-0.039	0.001	8.463	-1.521	-1.521	0.000	0.000	0.000	0.000
46	A	92	GLY	0	0.000	-0.037	8.345	-1.278	-1.278	0.000	0.000	0.000	0.000
47	A	93	LEU	0	-0.011	0.005	7.402	0.931	0.931	0.000	0.000	0.000	0.000
48	A	94	ASN	0	-0.002	-0.002	5.953	-3.249	-3.249	0.000	0.000	0.000	0.000
49	A	95	VAL	0	0.008	0.004	8.146	0.691	0.691	0.000	0.000	0.000	0.000
50	A	96	GLU	-1	-0.922	-0.979	10.989	18.811	18.811	0.000	0.000	0.000	0.000
51	A	97	ILE	0	-0.021	0.003	12.703	0.064	0.064	0.000	0.000	0.000	0.000
52	A	98	GLN	0	0.059	0.013	15.237	-1.360	-1.360	0.000	0.000	0.000	0.000
53	A	99	ILE	0	-0.037	-0.054	18.504	-0.418	-0.418	0.000	0.000	0.000	0.000
54	A	100	ASN	0	-0.087	-0.056	21.973	-0.491	-0.491	0.000	0.000	0.000	0.000
55	A	101	PRO	0	0.061	0.043	20.882	0.192	0.192	0.000	0.000	0.000	0.000
56	A	102	GLU	-1	-0.879	-0.925	21.932	11.471	11.471	0.000	0.000	0.000	0.000
57	A	103	VAL	0	-0.083	-0.042	23.870	-0.065	-0.065	0.000	0.000	0.000	0.000
58	A	104	LYS	1	0.993	0.982	15.375	-16.718	-16.718	0.000	0.000	0.000	0.000
59	A	105	ASP	-1	-0.877	-0.922	15.764	17.485	17.485	0.000	0.000	0.000	0.000
60	A	106	PHE	0	-0.067	-0.018	18.601	-0.418	-0.418	0.000	0.000	0.000	0.000
61	A	107	PHE	0	-0.012	-0.027	21.340	-0.430	-0.430	0.000	0.000	0.000	0.000
62	A	108	THR	0	0.023	0.045	16.358	0.148	0.148	0.000	0.000	0.000	0.000
63	A	109	PHE	0	0.033	0.005	16.773	-0.527	-0.527	0.000	0.000	0.000	0.000
64	A	110	LYS	1	0.978	0.993	11.917	-17.300	-17.300	0.000	0.000	0.000	0.000
65	A	111	SER	0	-0.005	0.003	13.125	-1.367	-1.367	0.000	0.000	0.000	0.000
66	A	112	ILE	0	0.019	0.032	9.531	0.945	0.945	0.000	0.000	0.000	0.000
67	A	113	SER	0	-0.032	-0.034	10.440	-1.641	-1.641	0.000	0.000	0.000	0.000
68	A	114	THR	0	-0.027	-0.011	10.214	1.053	1.053	0.000	0.000	0.000	0.000
69	A	115	THR	0	0.075	0.039	12.211	-0.430	-0.430	0.000	0.000	0.000	0.000
70	A	116	ASN	0	0.036	0.013	14.449	-0.395	-0.395	0.000	0.000	0.000	0.000
71	A	117	LYS	1	0.892	0.961	15.841	-14.951	-14.951	0.000	0.000	0.000	0.000
72	A	118	GLN	0	0.049	-0.006	15.023	0.106	0.106	0.000	0.000	0.000	0.000
73	A	119	ARG	1	0.757	0.823	15.105	-15.015	-15.015	0.000	0.000	0.000	0.000
74	A	120	CYS	0	-0.036	0.000	15.387	0.815	0.815	0.000	0.000	0.000	0.000
75	A	121	PHE	0	0.028	0.011	15.231	-0.430	-0.430	0.000	0.000	0.000	0.000
76	A	122	LEU	0	0.017	0.025	18.134	0.262	0.262	0.000	0.000	0.000	0.000
77	A	123	SER	0	-0.042	-0.026	17.995	0.035	0.035	0.000	0.000	0.000	0.000
78	A	124	LEU	0	-0.001	0.004	20.079	-0.074	-0.074	0.000	0.000	0.000	0.000
79	A	125	ARG	1	0.931	0.960	22.935	-10.708	-10.708	0.000	0.000	0.000	0.000
80	A	126	GLY	0	0.037	0.028	19.813	-0.100	-0.100	0.000	0.000	0.000	0.000
81	A	127	GLU	-1	-0.845	-0.885	20.430	11.539	11.539	0.000	0.000	0.000	0.000
82	A	128	THR	0	-0.034	-0.027	17.031	0.081	0.081	0.000	0.000	0.000	0.000
83	A	129	ARG	1	0.812	0.888	20.074	-10.809	-10.809	0.000	0.000	0.000	0.000
84	A	130	GLU	-1	-0.772	-0.823	19.935	13.693	13.693	0.000	0.000	0.000	0.000
85	A	131	ILE	0	-0.027	-0.028	21.085	-0.577	-0.577	0.000	0.000	0.000	0.000
86	A	132	LEU	0	-0.001	0.002	21.748	0.388	0.388	0.000	0.000	0.000	0.000
87	A	134	ASP	-1	-0.825	-0.919	22.040	9.879	9.879	0.000	0.000	0.000	0.000
88	A	135	ASN	0	0.018	-0.012	24.910	0.322	0.322	0.000	0.000	0.000	0.000
89	A	136	LYS	1	0.941	0.967	26.994	-8.735	-8.735	0.000	0.000	0.000	0.000
90	A	137	LEU	0	0.035	0.034	21.204	-0.110	-0.110	0.000	0.000	0.000	0.000
91	A	138	TYR	0	-0.001	-0.005	20.170	-0.003	-0.003	0.000	0.000	0.000	0.000
92	A	139	ASN	0	0.016	-0.005	24.105	0.250	0.250	0.000	0.000	0.000	0.000
93	A	140	MET	0	-0.009	0.016	27.122	-0.038	-0.038	0.000	0.000	0.000	0.000
94	A	141	LEU	0	0.027	0.008	20.383	-0.049	-0.049	0.000	0.000	0.000	0.000
95	A	142	LEU	0	-0.056	-0.011	23.508	0.078	0.078	0.000	0.000	0.000	0.000
96	A	143	ALA	0	-0.074	-0.033	25.821	-0.144	-0.144	0.000	0.000	0.000	0.000
97	A	144	VAL	0	0.039	0.020	25.092	-0.114	-0.114	0.000	0.000	0.000	0.000
98	A	145	PHE	0	0.068	0.074	20.258	-0.139	-0.139	0.000	0.000	0.000	0.000
99	A	146	ASN	0	-0.045	0.019	25.103	0.241	0.241	0.000	0.000	0.000	0.000
100	A	147	SER	0	-0.106	-0.093	27.684	-0.372	-0.372	0.000	0.000	0.000	0.000
101	A	148	TYR	0	0.010	0.012	27.752	-0.343	-0.343	0.000	0.000	0.000	0.000
102	A	149	ASP	-1	-0.849	-0.918	29.639	8.386	8.386	0.000	0.000	0.000	0.000
103	A	150	PRO	0	0.006	-0.004	31.703	-0.131	-0.131	0.000	0.000	0.000	0.000
104	A	151	ASN	0	-0.071	-0.045	34.079	-0.176	-0.176	0.000	0.000	0.000	0.000
105	A	152	ASP	-1	-0.924	-0.971	36.003	7.485	7.485	0.000	0.000	0.000	0.000
106	A	153	LEU	0	0.036	0.020	32.149	0.144	0.144	0.000	0.000	0.000	0.000
107	A	154	LEU	0	-0.002	0.009	33.918	0.173	0.173	0.000	0.000	0.000	0.000
108	A	155	LYS	1	0.993	0.991	35.007	-7.826	-7.826	0.000	0.000	0.000	0.000
109	A	156	HIS	0	-0.016	-0.008	26.688	0.264	0.264	0.000	0.000	0.000	0.000
110	A	157	ILE	0	0.022	0.001	31.017	0.159	0.159	0.000	0.000	0.000	0.000
111	A	158	SER	0	-0.015	-0.008	32.126	0.009	0.009	0.000	0.000	0.000	0.000
112	A	159	THR	0	-0.049	-0.017	30.143	0.167	0.167	0.000	0.000	0.000	0.000
113	A	160	VAL	0	0.061	0.028	26.833	0.209	0.209	0.000	0.000	0.000	0.000
114	A	161	GLU	-1	-0.928	-0.978	28.675	9.234	9.234	0.000	0.000	0.000	0.000
115	A	162	SER	0	-0.072	-0.045	31.168	-0.139	-0.139	0.000	0.000	0.000	0.000
116	A	163	LEU	0	0.005	0.014	23.524	-0.072	-0.072	0.000	0.000	0.000	0.000
117	A	164	LYS	1	0.955	0.994	26.725	-9.998	-9.998	0.000	0.000	0.000	0.000
118	A	165	LYS	1	0.989	1.000	28.540	-8.036	-8.036	0.000	0.000	0.000	0.000
119	A	166	ILE	0	-0.001	-0.009	26.588	-0.072	-0.072	0.000	0.000	0.000	0.000
120	A	167	PHE	0	-0.015	-0.012	22.776	-0.004	-0.004	0.000	0.000	0.000	0.000
121	A	168	TYR	0	-0.047	-0.040	26.953	0.163	0.163	0.000	0.000	0.000	0.000
122	A	169	THR	0	-0.070	-0.025	29.970	-0.300	-0.300	0.000	0.000	0.000	0.000
123	A	170	ILE	0	-0.064	-0.015	24.682	-0.156	-0.156	0.000	0.000	0.000	0.000
124	A	171	THR	0	-0.056	-0.051	28.861	0.066	0.066	0.000	0.000	0.000	0.000
125	A	172	CYS	0	-0.051	-0.027	25.981	0.227	0.227	0.000	0.000	0.000	0.000
126	A	173	GLU	-1	-0.886	-0.907	28.603	8.341	8.341	0.000	0.000	0.000	0.000
127	A	174	ALA	0	-0.010	-0.006	30.883	0.168	0.168	0.000	0.000	0.000	0.000
128	A	175	VAL	0	-0.003	-0.010	32.785	-0.206	-0.206	0.000	0.000	0.000	0.000
129	A	176	TYR	0	-0.001	0.009	34.588	0.009	0.009	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

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