FMO DATABASE

FMODB ID: LZG99

Calculation Name: 3CNW-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3CNW

Chain ID: A

ChEMBL ID:

UniProt ID: Q81AY6

Base Structure: X-ray

Registration Date: 2023-06-22

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	142
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1316560.974195
FMO2-HF: Nuclear repulsion	1260552.103727
FMO2-HF: Total energy	-56008.870468
FMO2-MP2: Total energy	-56173.911584

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:3:MET)

Summations of interaction energy for fragment #1(A:3:MET)

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.
-22.415	-11.959	7.961	-5.673	-12.744	-0.051

Interaction energy analysis for fragmet #1(A:3:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.065 / q_NPA : -0.023

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	5	HIS	0	0.011	0.002	2.809	-2.238	0.976	0.224	-1.542	-1.896	0.000
4	A	6	THR	0	-0.012	0.003	5.899	0.317	0.317	0.000	0.000	0.000	0.000
5	A	7	THR	0	-0.025	-0.038	9.540	0.242	0.242	0.000	0.000	0.000	0.000
6	A	8	THR	0	0.001	0.011	12.704	-0.042	-0.042	0.000	0.000	0.000	0.000
7	A	9	SER	0	0.019	-0.007	16.331	0.028	0.028	0.000	0.000	0.000	0.000
8	A	10	MET	0	-0.048	-0.012	19.446	-0.005	-0.005	0.000	0.000	0.000	0.000
9	A	11	GLU	-1	-0.812	-0.877	23.078	-0.160	-0.160	0.000	0.000	0.000	0.000
10	A	12	ILE	0	-0.013	-0.006	24.132	-0.010	-0.010	0.000	0.000	0.000	0.000
11	A	13	PHE	0	0.013	-0.002	28.068	0.013	0.013	0.000	0.000	0.000	0.000
12	A	14	GLY	0	0.067	0.024	30.666	0.007	0.007	0.000	0.000	0.000	0.000
13	A	15	SER	0	0.009	0.013	30.131	-0.006	-0.006	0.000	0.000	0.000	0.000
14	A	16	PRO	0	0.062	0.019	26.785	-0.007	-0.007	0.000	0.000	0.000	0.000
15	A	17	GLU	-1	-0.803	-0.898	27.287	-0.038	-0.038	0.000	0.000	0.000	0.000
16	A	18	GLN	0	-0.039	-0.008	29.483	-0.001	-0.001	0.000	0.000	0.000	0.000
17	A	19	VAL	0	0.038	0.022	25.014	-0.004	-0.004	0.000	0.000	0.000	0.000
18	A	20	TRP	0	0.001	0.003	20.482	-0.016	-0.016	0.000	0.000	0.000	0.000
19	A	21	GLN	0	-0.055	-0.036	25.591	0.001	0.001	0.000	0.000	0.000	0.000
20	A	22	LEU	0	-0.040	0.005	26.799	0.003	0.003	0.000	0.000	0.000	0.000
21	A	23	ILE	0	0.007	-0.004	21.141	-0.011	-0.011	0.000	0.000	0.000	0.000
22	A	24	GLY	0	0.010	0.001	21.672	-0.012	-0.012	0.000	0.000	0.000	0.000
23	A	25	GLY	0	-0.007	-0.004	22.048	0.019	0.019	0.000	0.000	0.000	0.000
24	A	26	PHE	0	0.004	-0.006	15.872	-0.017	-0.017	0.000	0.000	0.000	0.000
25	A	27	ASN	0	-0.019	-0.023	20.476	-0.023	-0.023	0.000	0.000	0.000	0.000
26	A	28	SER	0	0.020	-0.004	23.242	0.000	0.000	0.000	0.000	0.000	0.000
27	A	29	LEU	0	-0.027	0.008	18.096	-0.009	-0.009	0.000	0.000	0.000	0.000
28	A	30	PRO	0	0.011	-0.001	22.533	-0.012	-0.012	0.000	0.000	0.000	0.000
29	A	31	ASP	-1	-0.908	-0.935	25.768	-0.136	-0.136	0.000	0.000	0.000	0.000
30	A	32	TRP	0	-0.054	-0.034	18.648	-0.010	-0.010	0.000	0.000	0.000	0.000
31	A	33	LEU	0	-0.034	0.002	18.605	-0.023	-0.023	0.000	0.000	0.000	0.000
32	A	34	PRO	0	0.003	0.004	23.006	0.008	0.008	0.000	0.000	0.000	0.000
33	A	35	TYR	0	0.009	-0.001	17.797	-0.008	-0.008	0.000	0.000	0.000	0.000
34	A	36	ILE	0	-0.026	-0.028	18.473	-0.015	-0.015	0.000	0.000	0.000	0.000
35	A	37	PRO	0	0.026	0.018	22.359	0.029	0.029	0.000	0.000	0.000	0.000
36	A	38	SER	0	-0.048	-0.023	24.642	0.030	0.030	0.000	0.000	0.000	0.000
37	A	39	SER	0	0.057	0.009	22.583	-0.027	-0.027	0.000	0.000	0.000	0.000
38	A	40	LYS	1	0.881	0.951	23.491	0.083	0.083	0.000	0.000	0.000	0.000
39	A	41	LEU	0	0.053	0.041	22.292	-0.001	-0.001	0.000	0.000	0.000	0.000
40	A	42	THR	0	-0.065	-0.041	21.973	0.006	0.006	0.000	0.000	0.000	0.000
41	A	43	GLU	-1	-0.761	-0.868	19.606	0.114	0.114	0.000	0.000	0.000	0.000
42	A	44	GLY	0	-0.034	-0.020	23.389	0.015	0.015	0.000	0.000	0.000	0.000
43	A	45	GLY	0	0.009	0.000	23.330	0.003	0.003	0.000	0.000	0.000	0.000
44	A	46	ARG	1	0.853	0.917	18.904	-0.128	-0.128	0.000	0.000	0.000	0.000
45	A	47	VAL	0	0.021	0.019	17.242	0.005	0.005	0.000	0.000	0.000	0.000
46	A	48	ARG	1	0.772	0.876	15.342	0.282	0.282	0.000	0.000	0.000	0.000
47	A	49	HIS	0	-0.039	-0.025	18.622	-0.028	-0.028	0.000	0.000	0.000	0.000
48	A	50	LEU	0	0.002	0.002	17.321	0.019	0.019	0.000	0.000	0.000	0.000
49	A	51	ALA	0	0.006	0.004	21.203	0.003	0.003	0.000	0.000	0.000	0.000
50	A	52	ASN	0	0.027	0.015	19.813	0.034	0.034	0.000	0.000	0.000	0.000
51	A	53	PRO	0	-0.043	-0.036	22.169	0.030	0.030	0.000	0.000	0.000	0.000
52	A	54	ASP	-1	-0.948	-0.965	23.097	-0.353	-0.353	0.000	0.000	0.000	0.000
53	A	55	GLY	0	-0.032	-0.007	24.671	0.022	0.022	0.000	0.000	0.000	0.000
54	A	56	ASP	-1	-0.898	-0.933	19.988	-0.358	-0.358	0.000	0.000	0.000	0.000
55	A	57	THR	0	-0.075	-0.049	20.667	0.008	0.008	0.000	0.000	0.000	0.000
56	A	58	ILE	0	0.003	0.006	15.248	-0.022	-0.022	0.000	0.000	0.000	0.000
57	A	59	ILE	0	-0.041	-0.025	16.168	0.046	0.046	0.000	0.000	0.000	0.000
58	A	60	GLU	-1	-0.770	-0.880	13.793	-0.478	-0.478	0.000	0.000	0.000	0.000
59	A	61	ARG	1	0.887	0.931	13.283	-0.085	-0.085	0.000	0.000	0.000	0.000
60	A	62	LEU	0	-0.038	-0.001	13.342	-0.026	-0.026	0.000	0.000	0.000	0.000
61	A	63	GLU	-1	-0.890	-0.926	10.363	0.273	0.273	0.000	0.000	0.000	0.000
62	A	64	VAL	0	-0.034	-0.025	12.970	0.064	0.064	0.000	0.000	0.000	0.000
63	A	65	PHE	0	0.007	-0.004	15.624	-0.059	-0.059	0.000	0.000	0.000	0.000
64	A	66	ASN	0	-0.051	-0.038	18.805	0.011	0.011	0.000	0.000	0.000	0.000
65	A	67	ASP	-1	-0.827	-0.901	21.508	-0.018	-0.018	0.000	0.000	0.000	0.000
66	A	68	LYS	1	0.822	0.903	24.494	-0.016	-0.016	0.000	0.000	0.000	0.000
67	A	69	GLU	-1	-0.860	-0.903	21.250	0.138	0.138	0.000	0.000	0.000	0.000
68	A	70	ARG	1	0.755	0.866	22.001	0.030	0.030	0.000	0.000	0.000	0.000
69	A	71	TYR	0	-0.014	-0.032	16.756	-0.019	-0.019	0.000	0.000	0.000	0.000
70	A	72	TYR	0	-0.044	-0.010	15.756	0.024	0.024	0.000	0.000	0.000	0.000
71	A	73	THR	0	-0.009	-0.013	10.586	-0.025	-0.025	0.000	0.000	0.000	0.000
72	A	74	TYR	0	0.010	-0.008	11.353	0.053	0.053	0.000	0.000	0.000	0.000
73	A	75	SER	0	-0.013	-0.028	8.634	-0.110	-0.110	0.000	0.000	0.000	0.000
74	A	76	ILE	0	0.009	0.006	9.062	0.033	0.033	0.000	0.000	0.000	0.000
75	A	77	MET	0	-0.095	-0.047	10.407	0.060	0.060	0.000	0.000	0.000	0.000
76	A	78	ASN	0	-0.010	-0.021	13.186	0.019	0.019	0.000	0.000	0.000	0.000
77	A	79	ALA	0	0.019	0.015	12.975	-0.007	-0.007	0.000	0.000	0.000	0.000
78	A	80	PRO	0	0.031	0.036	14.843	0.003	0.003	0.000	0.000	0.000	0.000
79	A	81	PHE	0	0.004	-0.007	11.916	-0.032	-0.032	0.000	0.000	0.000	0.000
80	A	82	PRO	0	0.044	0.041	11.800	0.017	0.017	0.000	0.000	0.000	0.000
81	A	83	VAL	0	-0.022	-0.022	6.746	-0.318	-0.318	0.000	0.000	0.000	0.000
82	A	84	THR	0	0.001	0.000	5.423	0.579	0.579	0.000	0.000	0.000	0.000
83	A	85	ASN	0	-0.056	-0.029	2.177	-1.289	-1.263	2.000	-0.519	-1.508	0.002
84	A	86	TYR	0	0.013	0.034	2.949	-1.986	-0.981	0.246	-0.537	-0.714	-0.006
85	A	87	LEU	0	0.003	-0.005	4.577	0.613	0.743	-0.001	-0.004	-0.125	0.000
86	A	88	SER	0	-0.016	-0.012	6.282	-0.318	-0.318	0.000	0.000	0.000	0.000
87	A	89	THR	0	0.000	0.004	9.443	0.215	0.215	0.000	0.000	0.000	0.000
88	A	90	ILE	0	0.027	0.027	12.434	-0.096	-0.096	0.000	0.000	0.000	0.000
89	A	91	GLN	0	-0.016	-0.023	15.905	0.055	0.055	0.000	0.000	0.000	0.000
90	A	92	VAL	0	-0.005	0.016	18.844	-0.038	-0.038	0.000	0.000	0.000	0.000
91	A	93	LYS	1	0.812	0.904	17.751	0.195	0.195	0.000	0.000	0.000	0.000
92	A	94	GLU	-1	-0.845	-0.921	23.405	-0.045	-0.045	0.000	0.000	0.000	0.000
93	A	95	GLY	0	0.014	0.011	26.412	-0.012	-0.012	0.000	0.000	0.000	0.000
94	A	96	THR	0	-0.104	-0.081	28.398	0.017	0.017	0.000	0.000	0.000	0.000
95	A	97	GLU	-1	-0.889	-0.941	31.201	-0.071	-0.071	0.000	0.000	0.000	0.000
96	A	98	SER	0	-0.081	-0.029	32.412	0.000	0.000	0.000	0.000	0.000	0.000
97	A	99	ASN	0	-0.053	-0.040	34.117	0.003	0.003	0.000	0.000	0.000	0.000
98	A	100	THR	0	-0.019	0.004	30.343	-0.004	-0.004	0.000	0.000	0.000	0.000
99	A	101	SER	0	-0.005	-0.015	26.169	0.008	0.008	0.000	0.000	0.000	0.000
100	A	102	LEU	0	0.000	0.011	21.945	-0.019	-0.019	0.000	0.000	0.000	0.000
101	A	103	VAL	0	-0.018	-0.002	19.953	0.015	0.015	0.000	0.000	0.000	0.000
102	A	104	GLU	-1	-0.833	-0.909	16.555	-0.287	-0.287	0.000	0.000	0.000	0.000
103	A	105	TRP	0	0.005	0.003	13.040	0.062	0.062	0.000	0.000	0.000	0.000
104	A	106	SER	0	-0.013	-0.003	10.680	-0.049	-0.049	0.000	0.000	0.000	0.000
105	A	107	GLY	0	0.045	0.025	7.802	0.214	0.214	0.000	0.000	0.000	0.000
106	A	108	THR	0	-0.033	-0.019	2.253	-0.271	-0.061	1.773	-0.394	-1.589	-0.001
107	A	109	PHE	0	0.018	-0.008	2.708	-1.316	0.179	1.192	-0.696	-1.990	-0.007
108	A	110	THR	0	-0.006	-0.013	2.664	-9.297	-5.350	2.510	-1.917	-4.540	-0.039
109	A	111	PRO	0	0.021	0.019	3.691	0.653	0.997	0.018	-0.039	-0.323	0.000
110	A	112	VAL	0	-0.033	-0.033	6.475	0.420	0.420	0.000	0.000	0.000	0.000
111	A	113	GLU	-1	-0.957	-0.986	9.667	-0.473	-0.473	0.000	0.000	0.000	0.000
112	A	114	VAL	0	-0.047	-0.004	9.696	0.068	0.068	0.000	0.000	0.000	0.000
113	A	115	SER	0	-0.034	-0.050	9.606	-0.145	-0.145	0.000	0.000	0.000	0.000
114	A	116	ASP	-1	-0.860	-0.954	4.379	-5.640	-5.555	-0.001	-0.025	-0.059	0.000
115	A	117	GLU	-1	-0.892	-0.952	7.344	-1.884	-1.884	0.000	0.000	0.000	0.000
116	A	118	GLU	-1	-0.844	-0.878	10.849	-0.911	-0.911	0.000	0.000	0.000	0.000
117	A	119	ALA	0	0.017	0.014	7.694	0.131	0.131	0.000	0.000	0.000	0.000
118	A	120	ILE	0	-0.026	-0.022	7.154	0.095	0.095	0.000	0.000	0.000	0.000
119	A	121	ASN	0	-0.066	-0.051	10.194	0.357	0.357	0.000	0.000	0.000	0.000
120	A	122	LEU	0	-0.008	0.015	12.437	0.154	0.154	0.000	0.000	0.000	0.000
121	A	123	PHE	0	0.019	0.002	9.591	0.157	0.157	0.000	0.000	0.000	0.000
122	A	124	HIS	0	-0.021	0.007	12.546	0.252	0.252	0.000	0.000	0.000	0.000
123	A	125	GLY	0	0.003	0.006	14.352	0.134	0.134	0.000	0.000	0.000	0.000
124	A	126	ILE	0	-0.012	-0.005	14.376	0.098	0.098	0.000	0.000	0.000	0.000
125	A	127	TYR	0	-0.017	-0.033	10.208	0.013	0.013	0.000	0.000	0.000	0.000
126	A	128	SER	0	0.004	-0.005	16.553	0.085	0.085	0.000	0.000	0.000	0.000
127	A	129	ASP	-1	-0.880	-0.940	19.572	-0.336	-0.336	0.000	0.000	0.000	0.000
128	A	130	GLY	0	0.042	0.015	20.259	0.045	0.045	0.000	0.000	0.000	0.000
129	A	131	LEU	0	0.003	-0.008	18.196	0.044	0.044	0.000	0.000	0.000	0.000
130	A	132	LYS	1	0.810	0.906	21.900	0.315	0.315	0.000	0.000	0.000	0.000
131	A	133	ALA	0	0.016	0.000	24.627	0.032	0.032	0.000	0.000	0.000	0.000
132	A	134	LEU	0	0.017	0.013	23.089	0.027	0.027	0.000	0.000	0.000	0.000
133	A	135	GLN	0	-0.020	-0.013	26.041	0.013	0.013	0.000	0.000	0.000	0.000
134	A	136	GLN	0	-0.025	-0.015	27.864	0.006	0.006	0.000	0.000	0.000	0.000
135	A	137	ALA	0	0.040	0.019	29.334	0.015	0.015	0.000	0.000	0.000	0.000
136	A	138	PHE	0	-0.026	-0.009	28.649	0.016	0.016	0.000	0.000	0.000	0.000
137	A	139	LEU	0	-0.058	-0.020	32.225	0.009	0.009	0.000	0.000	0.000	0.000
138	A	140	ASP	-1	-0.939	-0.953	34.074	-0.152	-0.152	0.000	0.000	0.000	0.000
139	A	141	LEU	0	-0.031	-0.027	36.311	0.007	0.007	0.000	0.000	0.000	0.000
140	A	142	GLU	-1	-0.914	-0.937	37.945	-0.088	-0.088	0.000	0.000	0.000	0.000
141	A	143	HIS	0	-0.084	-0.051	41.325	0.008	0.008	0.000	0.000	0.000	0.000
142	A	144	HIS	0	-0.089	-0.043	42.113	0.003	0.003	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:MET)