FMO DATABASE

FMODB ID: NN8MQ

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	OptHSide
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	-851653.465532
FMO2-HF: Nuclear repulsion	808505.814024
FMO2-HF: Total energy	-43147.651508
FMO2-MP2: Total energy	-43274.910136

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.
-1.35	-0.021	-0.009	-0.554	-0.766	0.001

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 : -0.064 / q_NPA : -0.049

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	-0.009	0.012	3.829	-1.655	-0.326	-0.009	-0.554	-0.766	0.001
4	A	7	TYR	0	-0.067	-0.062	6.240	0.135	0.135	0.000	0.000	0.000	0.000
5	A	8	ASP	-1	-0.856	-0.926	9.912	0.388	0.388	0.000	0.000	0.000	0.000
6	A	9	VAL	0	0.039	0.002	13.193	-0.102	-0.102	0.000	0.000	0.000	0.000
7	A	10	ASP	-1	-0.874	-0.939	15.496	0.031	0.031	0.000	0.000	0.000	0.000
8	A	11	GLU	-1	-0.843	-0.903	13.602	-0.229	-0.229	0.000	0.000	0.000	0.000
9	A	12	PHE	0	-0.046	-0.026	13.674	-0.060	-0.060	0.000	0.000	0.000	0.000
10	A	13	TRP	0	0.006	-0.011	15.435	-0.028	-0.028	0.000	0.000	0.000	0.000
11	A	14	LYS	1	0.814	0.930	16.836	0.205	0.205	0.000	0.000	0.000	0.000
12	A	15	PHE	0	-0.034	-0.004	15.330	-0.010	-0.010	0.000	0.000	0.000	0.000
13	A	16	GLN	0	-0.033	-0.029	19.704	0.020	0.020	0.000	0.000	0.000	0.000
14	A	17	MET	0	0.005	0.008	17.701	-0.026	-0.026	0.000	0.000	0.000	0.000
15	A	18	LYS	1	0.888	0.958	22.619	0.090	0.090	0.000	0.000	0.000	0.000
16	A	19	VAL	0	0.024	0.018	26.053	-0.013	-0.013	0.000	0.000	0.000	0.000
17	A	20	GLY	0	0.001	0.004	27.951	0.006	0.006	0.000	0.000	0.000	0.000
18	A	21	LEU	0	0.006	-0.001	30.118	-0.003	-0.003	0.000	0.000	0.000	0.000
19	A	22	VAL	0	-0.012	-0.009	30.775	-0.001	-0.001	0.000	0.000	0.000	0.000
20	A	23	LYS	1	0.830	0.913	33.454	0.063	0.063	0.000	0.000	0.000	0.000
21	A	24	LYS	1	0.882	0.942	36.136	0.083	0.083	0.000	0.000	0.000	0.000
22	A	25	ALA	0	-0.021	-0.020	33.481	-0.007	-0.007	0.000	0.000	0.000	0.000
23	A	26	GLU	-1	-0.834	-0.891	35.177	-0.083	-0.083	0.000	0.000	0.000	0.000
24	A	27	LYS	1	0.902	0.948	33.301	0.126	0.126	0.000	0.000	0.000	0.000
25	A	28	ILE	0	0.000	0.016	31.907	0.007	0.007	0.000	0.000	0.000	0.000
26	A	29	LYS	1	0.982	0.982	35.501	0.085	0.085	0.000	0.000	0.000	0.000
27	A	30	ARG	1	0.919	0.949	37.169	0.100	0.100	0.000	0.000	0.000	0.000
28	A	31	THR	0	-0.001	0.003	32.299	-0.009	-0.009	0.000	0.000	0.000	0.000
29	A	32	LYS	1	1.001	0.983	31.884	0.142	0.142	0.000	0.000	0.000	0.000
30	A	33	LYS	1	0.920	0.947	24.452	0.238	0.238	0.000	0.000	0.000	0.000
31	A	34	LEU	0	-0.031	0.018	27.794	-0.004	-0.004	0.000	0.000	0.000	0.000
32	A	35	ILE	0	0.030	0.023	29.781	0.012	0.012	0.000	0.000	0.000	0.000
33	A	36	LYS	1	0.854	0.919	30.457	0.091	0.091	0.000	0.000	0.000	0.000
34	A	37	LEU	0	0.003	0.007	28.643	0.007	0.007	0.000	0.000	0.000	0.000
35	A	38	ILE	0	-0.027	0.003	32.657	-0.003	-0.003	0.000	0.000	0.000	0.000
36	A	39	VAL	0	-0.005	-0.012	29.834	0.004	0.004	0.000	0.000	0.000	0.000
37	A	40	ASP	-1	-0.765	-0.854	33.046	-0.058	-0.058	0.000	0.000	0.000	0.000
38	A	41	PHE	0	-0.014	-0.039	27.730	-0.003	-0.003	0.000	0.000	0.000	0.000
39	A	42	GLY	0	0.038	0.016	32.851	0.004	0.004	0.000	0.000	0.000	0.000
40	A	43	ASN	0	-0.092	-0.048	33.685	0.003	0.003	0.000	0.000	0.000	0.000
41	A	44	GLU	-1	-0.828	-0.895	32.071	-0.079	-0.079	0.000	0.000	0.000	0.000
42	A	45	GLU	-1	-0.889	-0.951	35.038	-0.071	-0.071	0.000	0.000	0.000	0.000
43	A	46	ARG	1	0.778	0.877	28.520	0.108	0.108	0.000	0.000	0.000	0.000
44	A	47	THR	0	-0.012	0.006	32.685	0.001	0.001	0.000	0.000	0.000	0.000
45	A	48	ILE	0	-0.047	-0.010	26.613	-0.008	-0.008	0.000	0.000	0.000	0.000
46	A	49	VAL	0	0.000	-0.013	28.106	0.007	0.007	0.000	0.000	0.000	0.000
47	A	50	THR	0	0.030	0.023	25.148	-0.020	-0.020	0.000	0.000	0.000	0.000
48	A	51	GLY	0	0.012	-0.026	24.913	0.015	0.015	0.000	0.000	0.000	0.000
49	A	52	ILE	0	0.096	0.049	23.821	-0.012	-0.012	0.000	0.000	0.000	0.000
50	A	53	ALA	0	-0.033	0.003	26.456	0.008	0.008	0.000	0.000	0.000	0.000
51	A	54	ASP	-1	-0.890	-0.937	26.671	-0.199	-0.199	0.000	0.000	0.000	0.000
52	A	55	GLN	0	-0.034	-0.027	22.827	0.012	0.012	0.000	0.000	0.000	0.000
53	A	56	ILE	0	0.005	0.002	26.501	0.006	0.006	0.000	0.000	0.000	0.000
54	A	57	PRO	0	0.008	0.023	29.555	-0.003	-0.003	0.000	0.000	0.000	0.000
55	A	58	PRO	0	0.021	-0.019	32.657	-0.001	-0.001	0.000	0.000	0.000	0.000
56	A	59	GLU	-1	-0.848	-0.927	34.084	-0.095	-0.095	0.000	0.000	0.000	0.000
57	A	60	GLU	-1	-0.916	-0.963	31.080	-0.109	-0.109	0.000	0.000	0.000	0.000
58	A	61	LEU	0	-0.081	-0.046	28.112	-0.001	-0.001	0.000	0.000	0.000	0.000
59	A	62	GLU	-1	-0.824	-0.919	32.063	-0.078	-0.078	0.000	0.000	0.000	0.000
60	A	63	GLY	0	-0.006	0.006	35.406	0.003	0.003	0.000	0.000	0.000	0.000
61	A	64	LYS	1	0.864	0.935	31.297	0.089	0.089	0.000	0.000	0.000	0.000
62	A	65	LYS	1	0.847	0.916	30.355	0.046	0.046	0.000	0.000	0.000	0.000
63	A	66	PHE	0	-0.003	0.000	25.699	-0.003	-0.003	0.000	0.000	0.000	0.000
64	A	67	ILE	0	0.052	0.032	20.996	0.009	0.009	0.000	0.000	0.000	0.000
65	A	68	PHE	0	0.018	0.007	23.504	-0.018	-0.018	0.000	0.000	0.000	0.000
66	A	69	VAL	0	0.018	0.012	18.934	0.013	0.013	0.000	0.000	0.000	0.000
67	A	70	VAL	0	-0.009	-0.024	22.159	-0.004	-0.004	0.000	0.000	0.000	0.000
68	A	71	ASN	0	-0.034	-0.012	22.317	-0.008	-0.008	0.000	0.000	0.000	0.000
69	A	72	LEU	0	0.040	0.029	19.400	-0.009	-0.009	0.000	0.000	0.000	0.000
70	A	73	LYS	1	0.914	0.946	23.113	0.206	0.206	0.000	0.000	0.000	0.000
71	A	74	PRO	0	0.069	0.044	25.145	-0.013	-0.013	0.000	0.000	0.000	0.000
72	A	75	LYS	1	0.891	0.943	24.541	0.187	0.187	0.000	0.000	0.000	0.000
73	A	76	LYS	1	1.032	1.020	27.945	0.136	0.136	0.000	0.000	0.000	0.000
74	A	77	PHE	0	0.020	0.004	24.369	-0.007	-0.007	0.000	0.000	0.000	0.000
75	A	78	SER	0	-0.014	-0.016	30.269	0.007	0.007	0.000	0.000	0.000	0.000
76	A	79	GLY	0	-0.063	-0.036	33.451	0.008	0.008	0.000	0.000	0.000	0.000
77	A	80	VAL	0	-0.002	0.007	32.755	0.008	0.008	0.000	0.000	0.000	0.000
78	A	81	GLU	-1	-0.904	-0.937	31.105	-0.145	-0.145	0.000	0.000	0.000	0.000
79	A	82	SER	0	0.007	0.011	26.610	0.009	0.009	0.000	0.000	0.000	0.000
80	A	83	GLN	0	0.011	-0.021	28.362	-0.006	-0.006	0.000	0.000	0.000	0.000
81	A	84	GLY	0	0.056	0.022	25.220	0.011	0.011	0.000	0.000	0.000	0.000
82	A	85	MET	0	-0.033	-0.015	17.875	-0.011	-0.011	0.000	0.000	0.000	0.000
83	A	86	LEU	0	0.023	0.021	22.751	0.003	0.003	0.000	0.000	0.000	0.000
84	A	87	ILE	0	-0.028	-0.015	17.591	-0.024	-0.024	0.000	0.000	0.000	0.000
85	A	88	LEU	0	-0.037	-0.015	19.036	0.031	0.031	0.000	0.000	0.000	0.000
86	A	89	ALA	0	0.022	0.014	17.532	-0.028	-0.028	0.000	0.000	0.000	0.000
87	A	90	GLU	-1	-0.954	-0.999	16.550	-0.373	-0.373	0.000	0.000	0.000	0.000
88	A	91	THR	0	-0.019	-0.016	15.549	-0.020	-0.020	0.000	0.000	0.000	0.000
89	A	92	GLU	-1	-0.881	-0.954	12.359	-0.402	-0.402	0.000	0.000	0.000	0.000
90	A	93	ASP	-1	-0.916	-0.932	14.988	-0.286	-0.286	0.000	0.000	0.000	0.000
91	A	94	GLY	0	-0.011	0.002	17.769	0.023	0.023	0.000	0.000	0.000	0.000
92	A	95	LYS	1	0.872	0.962	19.398	0.203	0.203	0.000	0.000	0.000	0.000
93	A	96	VAL	0	0.010	-0.004	20.149	-0.011	-0.011	0.000	0.000	0.000	0.000
94	A	97	TYR	0	-0.038	-0.035	20.306	0.040	0.040	0.000	0.000	0.000	0.000
95	A	98	LEU	0	-0.002	0.001	22.445	-0.010	-0.010	0.000	0.000	0.000	0.000
96	A	99	ILE	0	0.017	0.007	19.268	0.006	0.006	0.000	0.000	0.000	0.000
97	A	100	PRO	0	-0.030	-0.013	23.969	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	101	VAL	0	-0.034	-0.020	25.730	0.003	0.003	0.000	0.000	0.000	0.000
99	A	102	PRO	0	0.002	0.000	27.565	0.001	0.001	0.000	0.000	0.000	0.000
100	A	103	GLU	-1	-0.845	-0.931	30.760	-0.058	-0.058	0.000	0.000	0.000	0.000
101	A	104	GLU	-1	-0.903	-0.948	33.677	-0.031	-0.031	0.000	0.000	0.000	0.000
102	A	105	VAL	0	-0.044	-0.016	28.908	0.004	0.004	0.000	0.000	0.000	0.000
103	A	106	PRO	0	0.017	0.015	32.170	-0.006	-0.006	0.000	0.000	0.000	0.000
104	A	107	VAL	0	0.022	0.013	31.937	-0.003	-0.003	0.000	0.000	0.000	0.000
105	A	108	GLY	0	-0.003	-0.007	30.863	0.005	0.005	0.000	0.000	0.000	0.000
106	A	109	ALA	0	-0.050	-0.011	29.118	0.002	0.002	0.000	0.000	0.000	0.000
107	A	110	ARG	1	0.847	0.905	21.488	0.051	0.051	0.000	0.000	0.000	0.000
108	A	111	VAL	0	-0.012	-0.016	20.950	0.010	0.010	0.000	0.000	0.000	0.000
109	A	112	TRP	0	0.005	0.005	19.483	-0.014	-0.014	0.000	0.000	0.000	0.000

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