FMO DATABASE

FMODB ID: N1JJQ

Calculation Name: 1WWP-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1WWP

Chain ID: A

ChEMBL ID:

UniProt ID: Q5SKK7

Base Structure: X-ray

Registration Date: 2023-06-19

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	119
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1028889.038551
FMO2-HF: Nuclear repulsion	981262.296457
FMO2-HF: Total energy	-47626.742094
FMO2-MP2: Total energy	-47767.263517

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:1:MET)

Summations of interaction energy for fragment #1(A:1: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.
-3.445	2.155	4.588	-2.978	-7.209	-0.009

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.011 / q_NPA : -0.005

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

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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	3	GLU	-1	-0.825	-0.908	3.876	-3.621	-2.178	-0.008	-0.519	-0.916	0.001
4	A	4	LYS	1	0.956	0.975	4.073	2.127	2.454	0.000	-0.041	-0.286	0.000
5	A	5	ALA	0	-0.011	-0.004	2.459	0.048	0.793	0.956	-0.497	-1.205	0.000
6	A	6	LEU	0	0.041	0.036	4.447	0.699	0.902	0.000	-0.029	-0.173	0.000
7	A	7	ALA	0	-0.040	-0.024	7.300	0.438	0.438	0.000	0.000	0.000	0.000
8	A	8	THR	0	-0.034	-0.016	6.833	0.187	0.187	0.000	0.000	0.000	0.000
9	A	9	LEU	0	-0.005	0.011	8.240	0.231	0.231	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.900	0.957	9.737	1.033	1.033	0.000	0.000	0.000	0.000
11	A	11	GLU	-1	-0.959	-0.967	11.705	-0.813	-0.813	0.000	0.000	0.000	0.000
12	A	12	LEU	0	-0.001	-0.019	12.272	0.070	0.070	0.000	0.000	0.000	0.000
13	A	13	ALA	0	-0.010	-0.016	13.249	0.067	0.067	0.000	0.000	0.000	0.000
14	A	14	PHE	0	-0.079	-0.038	15.125	0.055	0.055	0.000	0.000	0.000	0.000
15	A	15	LEU	0	-0.014	0.017	17.735	0.025	0.025	0.000	0.000	0.000	0.000
16	A	16	GLU	-1	-0.948	-0.982	20.126	-0.175	-0.175	0.000	0.000	0.000	0.000
17	A	17	ASP	-1	-0.962	-0.983	23.561	-0.166	-0.166	0.000	0.000	0.000	0.000
18	A	18	PRO	0	-0.069	-0.003	19.632	-0.003	-0.003	0.000	0.000	0.000	0.000
19	A	19	SER	0	0.021	-0.028	21.219	0.024	0.024	0.000	0.000	0.000	0.000
20	A	20	PRO	0	-0.009	-0.043	20.612	-0.018	-0.018	0.000	0.000	0.000	0.000
21	A	21	VAL	0	0.042	0.030	17.856	-0.010	-0.010	0.000	0.000	0.000	0.000
22	A	22	GLU	-1	-0.811	-0.880	16.712	-0.349	-0.349	0.000	0.000	0.000	0.000
23	A	23	ARG	1	0.904	0.961	15.609	0.155	0.155	0.000	0.000	0.000	0.000
24	A	24	ASP	-1	-0.871	-0.932	15.412	-0.258	-0.258	0.000	0.000	0.000	0.000
25	A	25	ALA	0	-0.049	-0.023	12.622	-0.044	-0.044	0.000	0.000	0.000	0.000
26	A	26	ALA	0	-0.001	-0.011	11.054	-0.138	-0.138	0.000	0.000	0.000	0.000
27	A	27	ILE	0	-0.007	-0.005	11.106	-0.061	-0.061	0.000	0.000	0.000	0.000
28	A	28	GLN	0	0.057	0.039	7.428	0.086	0.086	0.000	0.000	0.000	0.000
29	A	29	ARG	1	0.867	0.917	6.564	0.833	0.833	0.000	0.000	0.000	0.000
30	A	30	PHE	0	-0.003	0.008	6.316	-0.288	-0.288	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.824	-0.879	7.705	-0.145	-0.145	0.000	0.000	0.000	0.000
32	A	32	TYR	0	-0.024	-0.021	2.450	-0.698	0.121	1.431	-0.427	-1.822	-0.002
33	A	33	THR	0	-0.026	-0.025	3.120	-1.317	-0.115	0.117	-0.659	-0.661	-0.006
34	A	34	PHE	0	0.015	0.003	4.863	0.664	0.690	-0.001	-0.005	-0.019	0.000
35	A	35	GLU	-1	-0.867	-0.935	5.282	1.204	1.204	0.000	0.000	0.000	0.000
36	A	36	ALA	0	-0.021	-0.012	2.369	-0.666	-0.026	2.092	-0.776	-1.956	-0.002
37	A	37	PHE	0	0.030	0.009	3.982	0.386	0.581	0.001	-0.025	-0.171	0.000
38	A	38	TRP	0	-0.026	-0.018	6.978	0.151	0.151	0.000	0.000	0.000	0.000
39	A	39	LYS	1	0.898	0.968	5.608	-1.845	-1.845	0.000	0.000	0.000	0.000
40	A	40	ALA	0	0.035	0.026	5.503	-0.147	-0.147	0.000	0.000	0.000	0.000
41	A	41	LEU	0	0.015	0.000	7.339	-0.482	-0.482	0.000	0.000	0.000	0.000
42	A	42	GLN	0	-0.069	-0.050	10.541	0.034	0.034	0.000	0.000	0.000	0.000
43	A	43	ALA	0	-0.015	-0.004	9.138	-0.158	-0.158	0.000	0.000	0.000	0.000
44	A	44	TYR	0	0.055	0.028	10.752	-0.184	-0.184	0.000	0.000	0.000	0.000
45	A	45	LEU	0	-0.005	-0.015	12.173	-0.121	-0.121	0.000	0.000	0.000	0.000
46	A	46	ARG	1	0.944	0.986	14.278	-0.725	-0.725	0.000	0.000	0.000	0.000
47	A	47	GLU	-1	-1.000	-1.016	11.493	0.634	0.634	0.000	0.000	0.000	0.000
48	A	48	LYN	0	-0.049	-0.023	12.986	-0.098	-0.098	0.000	0.000	0.000	0.000
49	A	49	GLU	-1	-0.935	-0.960	16.956	0.215	0.215	0.000	0.000	0.000	0.000
50	A	50	GLY	0	-0.022	0.015	18.693	-0.033	-0.033	0.000	0.000	0.000	0.000
51	A	51	LEU	0	-0.055	-0.027	19.119	-0.017	-0.017	0.000	0.000	0.000	0.000
52	A	52	GLU	-1	-0.896	-0.960	17.866	0.573	0.573	0.000	0.000	0.000	0.000
53	A	53	GLY	0	0.012	0.006	16.719	-0.051	-0.051	0.000	0.000	0.000	0.000
54	A	54	ALA	0	-0.023	-0.005	15.747	0.090	0.090	0.000	0.000	0.000	0.000
55	A	55	SER	0	0.001	-0.009	15.178	0.074	0.074	0.000	0.000	0.000	0.000
56	A	56	PRO	0	0.105	0.044	12.650	-0.029	-0.029	0.000	0.000	0.000	0.000
57	A	57	LYS	1	0.941	0.958	14.435	-0.228	-0.228	0.000	0.000	0.000	0.000
58	A	58	GLY	0	-0.044	-0.013	17.958	-0.040	-0.040	0.000	0.000	0.000	0.000
59	A	59	VAL	0	0.065	0.035	12.689	-0.034	-0.034	0.000	0.000	0.000	0.000
60	A	60	ILE	0	0.010	0.018	14.667	-0.037	-0.037	0.000	0.000	0.000	0.000
61	A	61	ARG	1	0.853	0.924	16.934	-0.277	-0.277	0.000	0.000	0.000	0.000
62	A	62	LEU	0	0.079	0.044	18.219	-0.021	-0.021	0.000	0.000	0.000	0.000
63	A	63	ALA	0	0.028	0.008	15.960	-0.022	-0.022	0.000	0.000	0.000	0.000
64	A	64	ARG	1	0.874	0.937	18.033	-0.198	-0.198	0.000	0.000	0.000	0.000
65	A	65	GLU	-1	-0.993	-0.984	21.190	0.211	0.211	0.000	0.000	0.000	0.000
66	A	66	VAL	0	0.027	0.022	18.607	-0.019	-0.019	0.000	0.000	0.000	0.000
67	A	67	GLY	0	-0.027	-0.005	21.691	-0.018	-0.018	0.000	0.000	0.000	0.000
68	A	68	LEU	0	-0.053	-0.029	14.448	-0.023	-0.023	0.000	0.000	0.000	0.000
69	A	69	LEU	0	-0.068	-0.026	15.808	-0.021	-0.021	0.000	0.000	0.000	0.000
70	A	70	ARG	1	0.971	0.975	19.452	-0.044	-0.044	0.000	0.000	0.000	0.000
71	A	71	ASP	-1	-0.825	-0.933	22.270	0.097	0.097	0.000	0.000	0.000	0.000
72	A	72	GLU	-1	-0.966	-0.985	23.702	-0.017	-0.017	0.000	0.000	0.000	0.000
73	A	73	GLU	-1	-0.737	-0.824	18.935	0.016	0.016	0.000	0.000	0.000	0.000
74	A	74	ALA	0	0.009	0.002	19.300	0.011	0.011	0.000	0.000	0.000	0.000
75	A	75	ARG	1	0.916	0.950	19.902	-0.083	-0.083	0.000	0.000	0.000	0.000
76	A	76	LEU	0	0.058	0.043	17.744	0.004	0.004	0.000	0.000	0.000	0.000
77	A	77	ALA	0	0.021	0.005	15.901	-0.009	-0.009	0.000	0.000	0.000	0.000
78	A	78	LEU	0	-0.093	-0.067	16.532	0.025	0.025	0.000	0.000	0.000	0.000
79	A	79	GLY	0	0.033	0.031	18.971	0.008	0.008	0.000	0.000	0.000	0.000
80	A	80	MET	0	-0.021	0.008	12.239	-0.043	-0.043	0.000	0.000	0.000	0.000
81	A	81	VAL	0	-0.033	-0.024	14.152	0.020	0.020	0.000	0.000	0.000	0.000
82	A	82	ASP	-1	-0.883	-0.938	15.585	0.129	0.129	0.000	0.000	0.000	0.000
83	A	83	ASP	-1	-0.770	-0.841	15.962	-0.066	-0.066	0.000	0.000	0.000	0.000
84	A	84	ARG	1	0.811	0.910	9.393	-0.214	-0.214	0.000	0.000	0.000	0.000
85	A	85	SER	0	-0.109	-0.074	13.861	0.004	0.004	0.000	0.000	0.000	0.000
86	A	86	LEU	0	0.015	-0.013	16.707	-0.007	-0.007	0.000	0.000	0.000	0.000
87	A	87	THR	0	-0.044	-0.057	12.505	0.011	0.011	0.000	0.000	0.000	0.000
88	A	88	VAL	0	-0.001	0.015	15.486	-0.029	-0.029	0.000	0.000	0.000	0.000
89	A	89	HIS	0	0.000	0.000	16.652	-0.006	-0.006	0.000	0.000	0.000	0.000
90	A	90	THR	0	-0.088	-0.048	16.710	-0.009	-0.009	0.000	0.000	0.000	0.000
91	A	91	TYR	0	0.045	0.040	19.524	-0.013	-0.013	0.000	0.000	0.000	0.000
92	A	92	ASN	0	0.001	-0.012	21.720	-0.003	-0.003	0.000	0.000	0.000	0.000
93	A	93	GLU	-1	-0.860	-0.939	23.020	-0.129	-0.129	0.000	0.000	0.000	0.000
94	A	94	PRO	0	-0.026	-0.010	23.700	-0.010	-0.010	0.000	0.000	0.000	0.000
95	A	95	LEU	0	0.031	0.017	19.964	-0.008	-0.008	0.000	0.000	0.000	0.000
96	A	96	ALA	0	0.096	0.054	19.034	-0.010	-0.010	0.000	0.000	0.000	0.000
97	A	97	ARG	1	0.934	0.968	19.312	0.118	0.118	0.000	0.000	0.000	0.000
98	A	98	ALA	0	-0.076	-0.046	21.506	-0.009	-0.009	0.000	0.000	0.000	0.000
99	A	99	ILE	0	-0.007	-0.010	15.421	0.003	0.003	0.000	0.000	0.000	0.000
100	A	100	PHE	0	0.023	0.000	16.364	-0.011	-0.011	0.000	0.000	0.000	0.000
101	A	101	ARG	1	0.923	0.956	17.947	0.097	0.097	0.000	0.000	0.000	0.000
102	A	102	ARG	1	0.898	0.960	17.884	0.081	0.081	0.000	0.000	0.000	0.000
103	A	103	LEU	0	-0.018	0.012	12.977	-0.006	-0.006	0.000	0.000	0.000	0.000
104	A	104	PRO	0	0.015	0.018	14.951	-0.041	-0.041	0.000	0.000	0.000	0.000
105	A	105	ASP	-1	-0.880	-0.949	16.791	-0.189	-0.189	0.000	0.000	0.000	0.000
106	A	106	TYR	0	-0.059	-0.065	13.074	0.019	0.019	0.000	0.000	0.000	0.000
107	A	107	ALA	0	0.017	0.006	12.054	-0.013	-0.013	0.000	0.000	0.000	0.000
108	A	108	ARG	1	0.962	0.977	12.927	0.251	0.251	0.000	0.000	0.000	0.000
109	A	109	LEU	0	-0.008	0.008	14.724	0.011	0.011	0.000	0.000	0.000	0.000
110	A	110	MET	0	-0.006	-0.005	9.633	0.059	0.059	0.000	0.000	0.000	0.000
111	A	111	GLU	-1	-0.901	-0.967	11.301	-0.555	-0.555	0.000	0.000	0.000	0.000
112	A	112	GLN	0	-0.034	-0.032	12.358	0.051	0.051	0.000	0.000	0.000	0.000
113	A	113	VAL	0	-0.025	-0.008	12.339	0.037	0.037	0.000	0.000	0.000	0.000
114	A	114	LEU	0	0.011	-0.005	6.860	0.087	0.087	0.000	0.000	0.000	0.000
115	A	115	GLY	0	-0.036	-0.009	10.032	-0.004	-0.004	0.000	0.000	0.000	0.000
116	A	116	ARG	1	0.821	0.864	12.422	0.007	0.007	0.000	0.000	0.000	0.000
117	A	117	LEU	0	-0.011	0.015	9.028	0.029	0.029	0.000	0.000	0.000	0.000
118	A	118	ARG	1	0.899	0.974	11.334	0.355	0.355	0.000	0.000	0.000	0.000
119	A	119	ARG	1	0.934	0.962	12.303	-0.163	-0.163	0.000	0.000	0.000	0.000

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