FMO DATABASE

FMODB ID: JQYZ9

Calculation Name: 2CWP-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2CWP

Chain ID: A

ChEMBL ID:

UniProt ID: O58023

Base Structure: X-ray

Registration Date: 2023-09-23

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	109
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-852612.992824
FMO2-HF: Nuclear repulsion	809464.961444
FMO2-HF: Total energy	-43148.03138
FMO2-MP2: Total energy	-43275.294203

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:4:MET)

Summations of interaction energy for fragment #1(A:4: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.
0.048	2.22	0.014	-0.884	-1.303	0.002

Interaction energy analysis for fragmet #1(A:4:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.001 / q_NPA : -0.008

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	6	LEU	0	-0.013	0.005	3.119	-0.832	1.340	0.014	-0.884	-1.303	0.002
4	A	7	TYR	0	-0.071	-0.060	5.543	0.694	0.694	0.000	0.000	0.000	0.000
5	A	8	ASP	-1	-0.848	-0.931	9.268	-0.308	-0.308	0.000	0.000	0.000	0.000
6	A	9	VAL	0	0.017	0.003	12.417	-0.028	-0.028	0.000	0.000	0.000	0.000
7	A	10	ASP	-1	-0.871	-0.943	15.170	-0.258	-0.258	0.000	0.000	0.000	0.000
8	A	11	GLU	-1	-0.853	-0.902	13.249	-0.602	-0.602	0.000	0.000	0.000	0.000
9	A	12	PHE	0	-0.007	-0.007	13.673	-0.012	-0.012	0.000	0.000	0.000	0.000
10	A	13	TRP	0	0.026	0.000	15.503	0.038	0.038	0.000	0.000	0.000	0.000
11	A	14	LYS	1	0.783	0.904	16.302	0.582	0.582	0.000	0.000	0.000	0.000
12	A	15	PHE	0	-0.031	-0.005	15.114	0.034	0.034	0.000	0.000	0.000	0.000
13	A	16	GLN	0	-0.032	-0.018	19.553	0.022	0.022	0.000	0.000	0.000	0.000
14	A	17	MET	0	0.013	0.001	18.030	-0.006	-0.006	0.000	0.000	0.000	0.000
15	A	18	LYS	1	0.837	0.925	22.918	0.151	0.151	0.000	0.000	0.000	0.000
16	A	19	VAL	0	0.056	0.033	26.105	-0.006	-0.006	0.000	0.000	0.000	0.000
17	A	20	GLY	0	-0.002	-0.002	28.050	0.003	0.003	0.000	0.000	0.000	0.000
18	A	21	LEU	0	0.010	0.004	30.389	0.000	0.000	0.000	0.000	0.000	0.000
19	A	22	VAL	0	-0.017	-0.008	31.133	-0.002	-0.002	0.000	0.000	0.000	0.000
20	A	23	LYS	1	0.800	0.879	33.705	0.089	0.089	0.000	0.000	0.000	0.000
21	A	24	LYS	1	0.880	0.942	36.169	0.081	0.081	0.000	0.000	0.000	0.000
22	A	25	ALA	0	-0.034	-0.018	33.563	-0.008	-0.008	0.000	0.000	0.000	0.000
23	A	26	GLU	-1	-0.812	-0.873	35.066	-0.076	-0.076	0.000	0.000	0.000	0.000
24	A	27	LYS	1	0.866	0.924	33.435	0.083	0.083	0.000	0.000	0.000	0.000
25	A	28	ILE	0	-0.016	0.010	31.760	0.005	0.005	0.000	0.000	0.000	0.000
26	A	29	LYS	1	1.014	0.998	35.440	0.070	0.070	0.000	0.000	0.000	0.000
27	A	30	ARG	1	0.931	0.954	37.905	0.082	0.082	0.000	0.000	0.000	0.000
28	A	31	THR	0	-0.041	-0.012	32.190	-0.003	-0.003	0.000	0.000	0.000	0.000
29	A	32	LYS	1	1.007	0.983	32.250	0.081	0.081	0.000	0.000	0.000	0.000
30	A	33	LYS	1	0.883	0.929	24.464	0.150	0.150	0.000	0.000	0.000	0.000
31	A	34	LEU	0	0.002	0.021	27.718	-0.006	-0.006	0.000	0.000	0.000	0.000
32	A	35	ILE	0	0.028	0.013	29.803	0.011	0.011	0.000	0.000	0.000	0.000
33	A	36	LYS	1	0.818	0.899	30.480	0.088	0.088	0.000	0.000	0.000	0.000
34	A	37	LEU	0	0.024	0.009	28.389	0.009	0.009	0.000	0.000	0.000	0.000
35	A	38	ILE	0	-0.017	-0.011	32.538	-0.004	-0.004	0.000	0.000	0.000	0.000
36	A	39	VAL	0	-0.003	-0.001	29.837	0.005	0.005	0.000	0.000	0.000	0.000
37	A	40	ASP	-1	-0.800	-0.874	33.066	-0.092	-0.092	0.000	0.000	0.000	0.000
38	A	41	PHE	0	0.015	-0.016	28.030	-0.005	-0.005	0.000	0.000	0.000	0.000
39	A	42	GLY	0	0.048	0.026	33.108	-0.002	-0.002	0.000	0.000	0.000	0.000
40	A	43	ASN	0	-0.084	-0.057	33.558	0.002	0.002	0.000	0.000	0.000	0.000
41	A	44	GLU	-1	-0.810	-0.880	32.031	-0.140	-0.140	0.000	0.000	0.000	0.000
42	A	45	GLU	-1	-0.855	-0.918	34.975	-0.088	-0.088	0.000	0.000	0.000	0.000
43	A	46	ARG	1	0.767	0.872	28.313	0.162	0.162	0.000	0.000	0.000	0.000
44	A	47	THR	0	-0.013	0.001	32.701	0.005	0.005	0.000	0.000	0.000	0.000
45	A	48	ILE	0	-0.035	-0.012	26.817	-0.010	-0.010	0.000	0.000	0.000	0.000
46	A	49	VAL	0	-0.023	-0.019	27.921	0.011	0.011	0.000	0.000	0.000	0.000
47	A	50	THR	0	0.039	0.024	25.182	-0.018	-0.018	0.000	0.000	0.000	0.000
48	A	51	GLY	0	0.017	-0.006	24.838	0.013	0.013	0.000	0.000	0.000	0.000
49	A	52	ILE	0	0.070	0.041	23.933	-0.004	-0.004	0.000	0.000	0.000	0.000
50	A	53	ALA	0	0.008	0.012	26.576	0.010	0.010	0.000	0.000	0.000	0.000
51	A	54	ASP	-1	-0.868	-0.930	26.665	-0.115	-0.115	0.000	0.000	0.000	0.000
52	A	55	GLN	0	-0.029	-0.011	23.487	0.011	0.011	0.000	0.000	0.000	0.000
53	A	56	ILE	0	0.025	0.027	26.635	0.004	0.004	0.000	0.000	0.000	0.000
54	A	57	PRO	0	-0.007	0.016	29.778	-0.006	-0.006	0.000	0.000	0.000	0.000
55	A	58	PRO	0	0.008	-0.024	32.882	-0.003	-0.003	0.000	0.000	0.000	0.000
56	A	59	GLU	-1	-0.830	-0.913	34.245	-0.071	-0.071	0.000	0.000	0.000	0.000
57	A	60	GLU	-1	-0.893	-0.955	30.903	-0.072	-0.072	0.000	0.000	0.000	0.000
58	A	61	LEU	0	-0.041	-0.019	28.157	-0.003	-0.003	0.000	0.000	0.000	0.000
59	A	62	GLU	-1	-0.857	-0.942	32.137	-0.076	-0.076	0.000	0.000	0.000	0.000
60	A	63	GLY	0	0.003	0.010	35.672	0.004	0.004	0.000	0.000	0.000	0.000
61	A	64	LYS	1	0.828	0.903	31.827	0.078	0.078	0.000	0.000	0.000	0.000
62	A	65	LYS	1	0.840	0.922	30.420	0.073	0.073	0.000	0.000	0.000	0.000
63	A	66	PHE	0	0.003	0.004	26.001	0.002	0.002	0.000	0.000	0.000	0.000
64	A	67	ILE	0	0.051	0.032	21.199	0.000	0.000	0.000	0.000	0.000	0.000
65	A	68	PHE	0	0.010	0.001	23.709	-0.007	-0.007	0.000	0.000	0.000	0.000
66	A	69	VAL	0	0.018	0.010	19.295	-0.001	-0.001	0.000	0.000	0.000	0.000
67	A	70	VAL	0	-0.016	-0.016	22.513	0.011	0.011	0.000	0.000	0.000	0.000
68	A	71	ASN	0	-0.006	-0.001	22.283	0.001	0.001	0.000	0.000	0.000	0.000
69	A	72	LEU	0	0.031	0.028	19.111	-0.014	-0.014	0.000	0.000	0.000	0.000
70	A	73	LYS	1	0.943	0.962	22.898	0.283	0.283	0.000	0.000	0.000	0.000
71	A	74	PRO	0	0.052	0.038	24.934	-0.009	-0.009	0.000	0.000	0.000	0.000
72	A	75	LYS	1	0.866	0.933	23.885	0.226	0.226	0.000	0.000	0.000	0.000
73	A	76	LYS	1	1.042	1.039	27.825	0.129	0.129	0.000	0.000	0.000	0.000
74	A	77	PHE	0	0.049	0.020	23.914	0.007	0.007	0.000	0.000	0.000	0.000
75	A	78	SER	0	-0.032	-0.024	29.923	0.006	0.006	0.000	0.000	0.000	0.000
76	A	79	GLY	0	-0.064	-0.024	33.084	0.009	0.009	0.000	0.000	0.000	0.000
77	A	80	VAL	0	-0.018	-0.011	32.842	0.004	0.004	0.000	0.000	0.000	0.000
78	A	81	GLU	-1	-0.901	-0.969	30.479	-0.165	-0.165	0.000	0.000	0.000	0.000
79	A	82	SER	0	0.014	0.011	26.531	0.009	0.009	0.000	0.000	0.000	0.000
80	A	83	GLN	0	0.020	0.003	27.908	-0.012	-0.012	0.000	0.000	0.000	0.000
81	A	84	GLY	0	0.044	0.017	25.381	0.002	0.002	0.000	0.000	0.000	0.000
82	A	85	MET	0	-0.033	-0.009	17.926	0.000	0.000	0.000	0.000	0.000	0.000
83	A	86	LEU	0	0.020	0.023	23.130	-0.003	-0.003	0.000	0.000	0.000	0.000
84	A	87	ILE	0	-0.035	-0.019	17.838	-0.022	-0.022	0.000	0.000	0.000	0.000
85	A	88	LEU	0	-0.040	-0.023	19.280	0.025	0.025	0.000	0.000	0.000	0.000
86	A	89	ALA	0	0.029	0.012	17.966	-0.024	-0.024	0.000	0.000	0.000	0.000
87	A	90	GLU	-1	-0.953	-0.992	16.937	-0.218	-0.218	0.000	0.000	0.000	0.000
88	A	91	THR	0	-0.019	-0.011	16.346	-0.002	-0.002	0.000	0.000	0.000	0.000
89	A	92	GLU	-1	-0.883	-0.958	13.158	-0.062	-0.062	0.000	0.000	0.000	0.000
90	A	93	ASP	-1	-0.894	-0.918	15.754	-0.094	-0.094	0.000	0.000	0.000	0.000
91	A	94	GLY	0	-0.010	0.006	18.546	0.000	0.000	0.000	0.000	0.000	0.000
92	A	95	LYS	1	0.836	0.927	19.905	0.081	0.081	0.000	0.000	0.000	0.000
93	A	96	VAL	0	0.002	-0.005	20.735	-0.006	-0.006	0.000	0.000	0.000	0.000
94	A	97	TYR	0	-0.027	-0.035	20.474	0.025	0.025	0.000	0.000	0.000	0.000
95	A	98	LEU	0	-0.005	0.002	22.623	-0.016	-0.016	0.000	0.000	0.000	0.000
96	A	99	ILE	0	0.006	0.007	19.343	0.008	0.008	0.000	0.000	0.000	0.000
97	A	100	PRO	0	-0.012	-0.004	24.028	-0.009	-0.009	0.000	0.000	0.000	0.000
98	A	101	VAL	0	-0.042	-0.026	25.966	-0.001	-0.001	0.000	0.000	0.000	0.000
99	A	102	PRO	0	0.004	0.000	27.942	0.003	0.003	0.000	0.000	0.000	0.000
100	A	103	GLU	-1	-0.817	-0.900	31.109	-0.079	-0.079	0.000	0.000	0.000	0.000
101	A	104	GLU	-1	-0.904	-0.968	34.132	-0.057	-0.057	0.000	0.000	0.000	0.000
102	A	105	VAL	0	-0.055	-0.019	29.345	-0.001	-0.001	0.000	0.000	0.000	0.000
103	A	106	PRO	0	-0.016	-0.014	32.683	-0.001	-0.001	0.000	0.000	0.000	0.000
104	A	107	VAL	0	0.023	0.017	31.989	-0.007	-0.007	0.000	0.000	0.000	0.000
105	A	108	GLY	0	-0.005	-0.004	31.207	0.003	0.003	0.000	0.000	0.000	0.000
106	A	109	ALA	0	-0.032	-0.011	29.536	-0.007	-0.007	0.000	0.000	0.000	0.000
107	A	110	ARG	1	0.827	0.905	21.049	0.242	0.242	0.000	0.000	0.000	0.000
108	A	111	VAL	0	-0.003	-0.002	20.980	0.010	0.010	0.000	0.000	0.000	0.000
109	A	112	TRP	0	0.002	0.001	19.327	-0.016	-0.016	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:MET)