FMO DATABASE

FMODB ID: 897ZY

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

Total energy (hartree)

FMO2-HF: Electronic energy	-850914.735579
FMO2-HF: Nuclear repulsion	807767.911549
FMO2-HF: Total energy	-43146.824029
FMO2-MP2: Total energy	-43274.111433

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.
-1.364	-0.068	-0.009	-0.519	-0.767	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 : -0.058 / q_NPA : -0.044

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	0.000	0.015	3.829	-1.799	-0.503	-0.009	-0.519	-0.767	0.001
4	A	7	TYR	0	-0.017	-0.014	6.084	0.434	0.434	0.000	0.000	0.000	0.000
5	A	8	ASP	-1	-0.841	-0.914	9.763	0.358	0.358	0.000	0.000	0.000	0.000
6	A	9	VAL	0	0.035	0.002	13.041	-0.109	-0.109	0.000	0.000	0.000	0.000
7	A	10	ASP	-1	-0.913	-0.959	15.360	0.027	0.027	0.000	0.000	0.000	0.000
8	A	11	GLU	-1	-0.898	-0.945	13.527	-0.205	-0.205	0.000	0.000	0.000	0.000
9	A	12	PHE	0	-0.027	-0.023	13.599	-0.065	-0.065	0.000	0.000	0.000	0.000
10	A	13	TRP	0	0.026	-0.005	15.228	-0.036	-0.036	0.000	0.000	0.000	0.000
11	A	14	LYS	1	0.873	0.984	16.306	0.249	0.249	0.000	0.000	0.000	0.000
12	A	15	PHE	0	-0.041	-0.013	15.604	-0.010	-0.010	0.000	0.000	0.000	0.000
13	A	16	GLN	0	-0.036	-0.030	19.499	0.022	0.022	0.000	0.000	0.000	0.000
14	A	17	MET	0	0.007	0.014	17.257	-0.023	-0.023	0.000	0.000	0.000	0.000
15	A	18	LYS	1	0.933	0.973	22.430	0.122	0.122	0.000	0.000	0.000	0.000
16	A	19	VAL	0	0.035	0.028	25.869	-0.015	-0.015	0.000	0.000	0.000	0.000
17	A	20	GLY	0	0.003	0.008	27.779	0.010	0.010	0.000	0.000	0.000	0.000
18	A	21	LEU	0	-0.005	-0.008	29.950	-0.005	-0.005	0.000	0.000	0.000	0.000
19	A	22	VAL	0	-0.009	-0.003	30.685	0.001	0.001	0.000	0.000	0.000	0.000
20	A	23	LYS	1	0.920	0.970	33.307	0.089	0.089	0.000	0.000	0.000	0.000
21	A	24	LYS	1	0.943	0.978	35.984	0.103	0.103	0.000	0.000	0.000	0.000
22	A	25	ALA	0	-0.038	-0.024	33.343	-0.008	-0.008	0.000	0.000	0.000	0.000
23	A	26	GLU	-1	-0.924	-0.953	35.076	-0.108	-0.108	0.000	0.000	0.000	0.000
24	A	27	LYS	1	0.939	0.975	33.831	0.152	0.152	0.000	0.000	0.000	0.000
25	A	28	ILE	0	0.018	0.029	31.807	0.008	0.008	0.000	0.000	0.000	0.000
26	A	29	LYS	1	0.969	0.979	35.395	0.104	0.104	0.000	0.000	0.000	0.000
27	A	30	ARG	1	0.916	0.946	37.075	0.116	0.116	0.000	0.000	0.000	0.000
28	A	31	THR	0	0.004	0.008	32.245	-0.009	-0.009	0.000	0.000	0.000	0.000
29	A	32	LYS	1	0.967	0.957	31.867	0.170	0.170	0.000	0.000	0.000	0.000
30	A	33	LYS	1	0.991	0.991	24.562	0.296	0.296	0.000	0.000	0.000	0.000
31	A	34	LEU	0	-0.037	0.018	27.780	-0.007	-0.007	0.000	0.000	0.000	0.000
32	A	35	ILE	0	0.042	0.029	29.669	0.014	0.014	0.000	0.000	0.000	0.000
33	A	36	LYS	1	0.923	0.967	30.335	0.115	0.115	0.000	0.000	0.000	0.000
34	A	37	LEU	0	0.021	0.007	28.416	0.007	0.007	0.000	0.000	0.000	0.000
35	A	38	ILE	0	-0.035	-0.001	32.515	-0.002	-0.002	0.000	0.000	0.000	0.000
36	A	39	VAL	0	-0.010	-0.016	29.722	0.003	0.003	0.000	0.000	0.000	0.000
37	A	40	ASP	-1	-0.823	-0.899	32.883	-0.083	-0.083	0.000	0.000	0.000	0.000
38	A	41	PHE	0	-0.012	-0.040	27.608	-0.005	-0.005	0.000	0.000	0.000	0.000
39	A	42	GLY	0	0.021	0.001	32.670	0.004	0.004	0.000	0.000	0.000	0.000
40	A	43	ASN	0	-0.062	-0.027	33.735	0.001	0.001	0.000	0.000	0.000	0.000
41	A	44	GLU	-1	-0.923	-0.965	31.347	-0.106	-0.106	0.000	0.000	0.000	0.000
42	A	45	GLU	-1	-0.913	-0.954	34.870	-0.096	-0.096	0.000	0.000	0.000	0.000
43	A	46	ARG	1	0.836	0.921	28.159	0.136	0.136	0.000	0.000	0.000	0.000
44	A	47	THR	0	-0.032	-0.002	32.496	0.001	0.001	0.000	0.000	0.000	0.000
45	A	48	ILE	0	-0.027	0.001	26.499	-0.008	-0.008	0.000	0.000	0.000	0.000
46	A	49	VAL	0	-0.007	-0.008	27.889	0.007	0.007	0.000	0.000	0.000	0.000
47	A	50	THR	0	0.023	0.021	25.167	-0.025	-0.025	0.000	0.000	0.000	0.000
48	A	51	GLY	0	0.001	-0.034	24.807	0.019	0.019	0.000	0.000	0.000	0.000
49	A	52	ILE	0	0.091	0.051	23.757	-0.014	-0.014	0.000	0.000	0.000	0.000
50	A	53	ALA	0	-0.040	-0.007	26.375	0.008	0.008	0.000	0.000	0.000	0.000
51	A	54	ASP	-1	-0.952	-0.983	26.798	-0.245	-0.245	0.000	0.000	0.000	0.000
52	A	55	GLN	0	-0.042	-0.028	22.832	0.013	0.013	0.000	0.000	0.000	0.000
53	A	56	ILE	0	-0.003	0.001	26.431	0.006	0.006	0.000	0.000	0.000	0.000
54	A	57	PRO	0	-0.008	0.015	29.483	-0.002	-0.002	0.000	0.000	0.000	0.000
55	A	58	PRO	0	0.012	-0.028	32.566	-0.001	-0.001	0.000	0.000	0.000	0.000
56	A	59	GLU	-1	-0.864	-0.938	33.983	-0.128	-0.128	0.000	0.000	0.000	0.000
57	A	60	GLU	-1	-0.926	-0.962	31.235	-0.155	-0.155	0.000	0.000	0.000	0.000
58	A	61	LEU	0	-0.084	-0.050	27.965	-0.004	-0.004	0.000	0.000	0.000	0.000
59	A	62	GLU	-1	-0.823	-0.930	31.947	-0.105	-0.105	0.000	0.000	0.000	0.000
60	A	63	GLY	0	-0.020	0.000	35.281	0.003	0.003	0.000	0.000	0.000	0.000
61	A	64	LYS	1	0.943	0.981	31.435	0.128	0.128	0.000	0.000	0.000	0.000
62	A	65	LYS	1	0.887	0.938	30.193	0.083	0.083	0.000	0.000	0.000	0.000
63	A	66	PHE	0	0.009	0.007	25.537	-0.005	-0.005	0.000	0.000	0.000	0.000
64	A	67	ILE	0	0.059	0.033	20.917	0.014	0.014	0.000	0.000	0.000	0.000
65	A	68	PHE	0	0.015	0.007	23.357	-0.021	-0.021	0.000	0.000	0.000	0.000
66	A	69	VAL	0	0.009	0.009	18.829	0.016	0.016	0.000	0.000	0.000	0.000
67	A	70	VAL	0	0.001	-0.019	21.976	0.000	0.000	0.000	0.000	0.000	0.000
68	A	71	ASN	0	-0.019	0.000	21.834	-0.006	-0.006	0.000	0.000	0.000	0.000
69	A	72	LEU	0	0.043	0.028	19.228	-0.008	-0.008	0.000	0.000	0.000	0.000
70	A	73	LYS	1	0.900	0.942	22.900	0.242	0.242	0.000	0.000	0.000	0.000
71	A	74	PRO	0	0.080	0.047	24.969	-0.016	-0.016	0.000	0.000	0.000	0.000
72	A	75	LYS	1	0.910	0.949	24.395	0.216	0.216	0.000	0.000	0.000	0.000
73	A	76	LYS	1	1.037	1.022	27.794	0.155	0.155	0.000	0.000	0.000	0.000
74	A	77	PHE	0	0.016	0.002	24.362	-0.006	-0.006	0.000	0.000	0.000	0.000
75	A	78	SER	0	-0.019	-0.015	30.149	0.010	0.010	0.000	0.000	0.000	0.000
76	A	79	GLY	0	-0.065	-0.039	33.341	0.008	0.008	0.000	0.000	0.000	0.000
77	A	80	VAL	0	0.004	0.009	32.479	0.009	0.009	0.000	0.000	0.000	0.000
78	A	81	GLU	-1	-0.927	-0.945	31.221	-0.163	-0.163	0.000	0.000	0.000	0.000
79	A	82	SER	0	-0.007	-0.003	26.307	0.008	0.008	0.000	0.000	0.000	0.000
80	A	83	GLN	0	-0.011	-0.036	28.199	-0.005	-0.005	0.000	0.000	0.000	0.000
81	A	84	GLY	0	0.044	0.014	25.045	0.010	0.010	0.000	0.000	0.000	0.000
82	A	85	MET	0	-0.041	-0.020	17.987	-0.010	-0.010	0.000	0.000	0.000	0.000
83	A	86	LEU	0	0.021	0.023	22.590	0.002	0.002	0.000	0.000	0.000	0.000
84	A	87	ILE	0	-0.025	-0.011	17.950	-0.028	-0.028	0.000	0.000	0.000	0.000
85	A	88	LEU	0	-0.040	-0.016	18.911	0.037	0.037	0.000	0.000	0.000	0.000
86	A	89	ALA	0	0.014	0.009	17.443	-0.039	-0.039	0.000	0.000	0.000	0.000
87	A	90	GLU	-1	-0.947	-0.995	16.499	-0.485	-0.485	0.000	0.000	0.000	0.000
88	A	91	THR	0	-0.047	-0.028	15.504	-0.041	-0.041	0.000	0.000	0.000	0.000
89	A	92	GLU	-1	-0.882	-0.962	12.281	-0.589	-0.589	0.000	0.000	0.000	0.000
90	A	93	ASP	-1	-0.921	-0.935	14.864	-0.367	-0.367	0.000	0.000	0.000	0.000
91	A	94	GLY	0	-0.018	0.007	17.817	0.036	0.036	0.000	0.000	0.000	0.000
92	A	95	LYS	1	0.901	0.978	19.454	0.282	0.282	0.000	0.000	0.000	0.000
93	A	96	VAL	0	0.012	-0.003	20.133	-0.023	-0.023	0.000	0.000	0.000	0.000
94	A	97	TYR	0	-0.023	-0.024	20.200	0.049	0.049	0.000	0.000	0.000	0.000
95	A	98	LEU	0	-0.010	-0.005	22.358	-0.014	-0.014	0.000	0.000	0.000	0.000
96	A	99	ILE	0	0.015	0.006	19.227	0.003	0.003	0.000	0.000	0.000	0.000
97	A	100	PRO	0	-0.041	-0.020	23.859	0.001	0.001	0.000	0.000	0.000	0.000
98	A	101	VAL	0	-0.031	-0.015	25.664	0.000	0.000	0.000	0.000	0.000	0.000
99	A	102	PRO	0	0.000	-0.004	27.408	0.003	0.003	0.000	0.000	0.000	0.000
100	A	103	GLU	-1	-0.867	-0.939	30.629	-0.095	-0.095	0.000	0.000	0.000	0.000
101	A	104	GLU	-1	-0.925	-0.968	33.536	-0.066	-0.066	0.000	0.000	0.000	0.000
102	A	105	VAL	0	-0.041	-0.010	28.791	0.005	0.005	0.000	0.000	0.000	0.000
103	A	106	PRO	0	0.002	0.005	32.013	-0.006	-0.006	0.000	0.000	0.000	0.000
104	A	107	VAL	0	0.023	0.017	31.763	-0.005	-0.005	0.000	0.000	0.000	0.000
105	A	108	GLY	0	0.018	0.003	30.675	0.007	0.007	0.000	0.000	0.000	0.000
106	A	109	ALA	0	-0.052	-0.016	28.837	0.002	0.002	0.000	0.000	0.000	0.000
107	A	110	ARG	1	0.830	0.889	21.244	0.093	0.093	0.000	0.000	0.000	0.000
108	A	111	VAL	0	0.001	-0.005	20.590	0.010	0.010	0.000	0.000	0.000	0.000
109	A	112	TRP	0	-0.001	0.003	19.303	-0.015	-0.015	0.000	0.000	0.000	0.000

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