FMO DATABASE

FMODB ID: 39YQL

Calculation Name: 1JWI-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1JWI

Chain ID: A

ChEMBL ID:

UniProt ID: Q7LZK5

Base Structure: X-ray

Registration Date: 2023-09-20

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	121
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1034063.755772
FMO2-HF: Nuclear repulsion	983306.766352
FMO2-HF: Total energy	-50756.98942
FMO2-MP2: Total energy	-50901.739152

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:CYS)

Summations of interaction energy for fragment #1(A:4:CYS)

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.
-43.772	-36.848	26.569	-12.56	-20.932	-0.014

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.070 / q_NPA : -0.041

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	6	PRO	0	0.003	-0.001	3.328	-2.123	-0.510	0.083	-0.824	-0.872	0.000
4	A	7	ASP	-1	-0.824	-0.891	5.779	-1.209	-1.209	0.000	0.000	0.000	0.000
5	A	8	TRP	0	-0.029	-0.012	2.314	-2.132	-0.168	1.891	-1.007	-2.848	-0.006
6	A	9	SER	0	-0.021	-0.006	3.683	-0.406	0.305	0.029	-0.229	-0.512	-0.001
7	A	10	SER	0	0.044	0.002	2.494	-5.929	-2.514	7.966	-5.197	-6.184	-0.004
8	A	11	TYR	0	-0.025	-0.021	1.961	-14.106	-17.218	5.747	0.286	-2.921	0.038
9	A	12	LYS	1	0.853	0.903	3.098	-1.409	-0.834	0.553	0.009	-1.136	-0.001
10	A	13	GLY	0	0.007	0.011	3.860	-3.365	-2.105	-0.013	-0.746	-0.500	-0.003
13	A	17	LYS	1	0.802	0.888	3.846	1.505	3.706	-0.022	-1.119	-1.060	0.006
14	A	18	VAL	0	0.009	0.019	6.655	-0.130	-0.130	0.000	0.000	0.000	0.000
15	A	19	PHE	0	-0.006	-0.014	8.696	0.213	0.213	0.000	0.000	0.000	0.000
16	A	20	LYS	1	0.927	0.940	12.686	0.420	0.420	0.000	0.000	0.000	0.000
17	A	21	LYS	1	0.829	0.951	14.179	1.188	1.188	0.000	0.000	0.000	0.000
18	A	22	VAL	0	0.009	-0.002	17.437	-0.086	-0.086	0.000	0.000	0.000	0.000
19	A	23	GLY	0	-0.022	-0.012	19.318	0.026	0.026	0.000	0.000	0.000	0.000
20	A	24	THR	0	-0.032	-0.011	20.116	-0.013	-0.013	0.000	0.000	0.000	0.000
21	A	25	TRP	0	0.036	0.021	17.018	-0.082	-0.082	0.000	0.000	0.000	0.000
22	A	26	GLU	-1	-0.748	-0.872	17.594	-0.994	-0.994	0.000	0.000	0.000	0.000
23	A	27	ASP	-1	-0.872	-0.919	18.675	-0.794	-0.794	0.000	0.000	0.000	0.000
24	A	28	ALA	0	-0.024	-0.007	14.782	-0.089	-0.089	0.000	0.000	0.000	0.000
25	A	29	GLU	-1	-0.717	-0.841	13.067	-2.493	-2.493	0.000	0.000	0.000	0.000
26	A	30	LYS	1	0.799	0.880	13.511	0.763	0.763	0.000	0.000	0.000	0.000
27	A	31	PHE	0	0.051	0.013	11.781	-0.046	-0.046	0.000	0.000	0.000	0.000
28	A	32	CYS	0	-0.064	0.008	7.373	0.037	0.037	0.000	0.000	0.000	0.000
29	A	33	VAL	0	-0.011	0.007	9.278	-0.413	-0.413	0.000	0.000	0.000	0.000
30	A	34	GLU	-1	-0.945	-0.973	11.422	-1.177	-1.177	0.000	0.000	0.000	0.000
31	A	35	ASN	0	-0.089	-0.055	7.513	0.114	0.114	0.000	0.000	0.000	0.000
32	A	36	SER	0	-0.040	-0.020	6.744	-0.462	-0.462	0.000	0.000	0.000	0.000
33	A	37	GLY	0	-0.013	-0.014	6.740	-1.077	-1.077	0.000	0.000	0.000	0.000
34	A	38	HIS	1	0.807	0.876	7.527	3.813	3.813	0.000	0.000	0.000	0.000
35	A	39	LEU	0	0.035	0.014	8.685	-0.702	-0.702	0.000	0.000	0.000	0.000
36	A	40	ALA	0	-0.050	-0.029	8.450	-0.269	-0.269	0.000	0.000	0.000	0.000
37	A	41	SER	0	0.062	0.042	9.241	0.361	0.361	0.000	0.000	0.000	0.000
38	A	42	ILE	0	-0.055	-0.042	9.494	-0.273	-0.273	0.000	0.000	0.000	0.000
39	A	43	ASP	-1	-0.892	-0.939	10.507	-1.164	-1.164	0.000	0.000	0.000	0.000
40	A	44	SER	0	0.004	-0.003	11.130	0.369	0.369	0.000	0.000	0.000	0.000
41	A	45	LYS	1	0.884	0.923	13.337	-0.145	-0.145	0.000	0.000	0.000	0.000
42	A	46	GLU	-1	-0.812	-0.902	11.962	1.097	1.097	0.000	0.000	0.000	0.000
43	A	47	GLU	-1	-0.787	-0.830	7.380	-2.080	-2.080	0.000	0.000	0.000	0.000
44	A	48	ALA	0	0.026	0.006	10.774	0.057	0.057	0.000	0.000	0.000	0.000
45	A	49	ASP	-1	-0.783	-0.870	13.754	0.330	0.330	0.000	0.000	0.000	0.000
46	A	50	PHE	0	-0.033	-0.010	5.861	0.307	0.307	0.000	0.000	0.000	0.000
47	A	51	VAL	0	0.041	0.013	9.073	0.077	0.077	0.000	0.000	0.000	0.000
48	A	52	THR	0	-0.010	-0.015	10.979	-0.061	-0.061	0.000	0.000	0.000	0.000
49	A	53	LYS	1	0.931	0.984	12.716	-1.424	-1.424	0.000	0.000	0.000	0.000
50	A	54	LEU	0	0.017	0.010	7.054	-0.105	-0.105	0.000	0.000	0.000	0.000
51	A	55	ALA	0	0.025	0.020	11.258	-0.169	-0.169	0.000	0.000	0.000	0.000
52	A	56	SER	0	0.020	-0.012	13.737	-0.047	-0.047	0.000	0.000	0.000	0.000
53	A	57	GLN	0	-0.050	-0.040	13.745	0.121	0.121	0.000	0.000	0.000	0.000
54	A	58	THR	0	-0.042	-0.014	11.977	-0.032	-0.032	0.000	0.000	0.000	0.000
55	A	59	LEU	0	-0.058	-0.019	14.476	-0.104	-0.104	0.000	0.000	0.000	0.000
56	A	60	THR	0	-0.030	-0.010	17.501	0.024	0.024	0.000	0.000	0.000	0.000
57	A	61	LYS	1	0.930	0.966	19.942	0.081	0.081	0.000	0.000	0.000	0.000
58	A	62	PHE	0	0.008	-0.007	19.539	-0.001	-0.001	0.000	0.000	0.000	0.000
59	A	63	VAL	0	-0.017	-0.012	23.229	0.001	0.001	0.000	0.000	0.000	0.000
60	A	64	TYR	0	0.012	0.008	21.042	-0.013	-0.013	0.000	0.000	0.000	0.000
61	A	65	ASP	-1	-0.712	-0.826	20.919	-0.329	-0.329	0.000	0.000	0.000	0.000
62	A	66	ALA	0	-0.007	-0.018	15.722	-0.030	-0.030	0.000	0.000	0.000	0.000
63	A	67	TRP	0	-0.030	0.000	16.208	-0.062	-0.062	0.000	0.000	0.000	0.000
64	A	68	ILE	0	0.009	-0.006	13.128	-0.166	-0.166	0.000	0.000	0.000	0.000
65	A	69	GLY	0	0.001	0.008	12.951	0.096	0.096	0.000	0.000	0.000	0.000
66	A	70	LEU	0	-0.052	-0.027	13.938	-0.008	-0.008	0.000	0.000	0.000	0.000
67	A	71	ARG	1	0.775	0.835	17.489	0.913	0.913	0.000	0.000	0.000	0.000
68	A	72	ASP	-1	-0.758	-0.855	20.940	-0.518	-0.518	0.000	0.000	0.000	0.000
69	A	73	GLU	-1	-0.819	-0.886	22.253	-0.820	-0.820	0.000	0.000	0.000	0.000
70	A	74	SER	0	-0.052	-0.037	24.848	0.038	0.038	0.000	0.000	0.000	0.000
71	A	75	LYS	1	0.887	0.921	28.584	0.381	0.381	0.000	0.000	0.000	0.000
72	A	76	THR	0	-0.044	-0.014	30.888	0.017	0.017	0.000	0.000	0.000	0.000
73	A	77	GLN	0	0.002	-0.017	31.217	-0.023	-0.023	0.000	0.000	0.000	0.000
74	A	78	GLN	0	-0.026	-0.016	31.452	-0.007	-0.007	0.000	0.000	0.000	0.000
75	A	79	CYS	0	-0.018	0.003	28.610	-0.003	-0.003	0.000	0.000	0.000	0.000
76	A	80	SER	0	-0.009	-0.003	31.349	-0.002	-0.002	0.000	0.000	0.000	0.000
77	A	81	PRO	0	0.029	0.012	34.305	0.001	0.001	0.000	0.000	0.000	0.000
78	A	82	GLN	0	-0.066	-0.049	36.580	0.005	0.005	0.000	0.000	0.000	0.000
79	A	83	TRP	0	0.027	0.031	39.518	-0.007	-0.007	0.000	0.000	0.000	0.000
80	A	84	THR	0	0.002	-0.017	42.229	0.001	0.001	0.000	0.000	0.000	0.000
81	A	85	ASP	-1	-0.870	-0.900	43.988	-0.170	-0.170	0.000	0.000	0.000	0.000
82	A	86	GLY	0	0.000	0.009	44.179	0.006	0.006	0.000	0.000	0.000	0.000
83	A	87	SER	0	-0.072	-0.050	44.608	-0.009	-0.009	0.000	0.000	0.000	0.000
84	A	88	SER	0	0.001	-0.018	41.546	-0.005	-0.005	0.000	0.000	0.000	0.000
85	A	89	VAL	0	-0.034	0.004	37.274	0.009	0.009	0.000	0.000	0.000	0.000
86	A	90	VAL	0	-0.051	-0.034	39.323	-0.010	-0.010	0.000	0.000	0.000	0.000
87	A	91	TYR	0	-0.057	-0.031	40.279	-0.005	-0.005	0.000	0.000	0.000	0.000
88	A	92	GLU	-1	-0.741	-0.874	35.552	-0.334	-0.334	0.000	0.000	0.000	0.000
89	A	93	ASN	0	-0.018	-0.009	39.405	0.004	0.004	0.000	0.000	0.000	0.000
90	A	94	VAL	0	-0.007	-0.002	33.588	0.014	0.014	0.000	0.000	0.000	0.000
91	A	95	ASP	-1	-0.943	-0.963	36.347	-0.256	-0.256	0.000	0.000	0.000	0.000
92	A	96	GLU	-1	-0.884	-0.960	30.768	-0.371	-0.371	0.000	0.000	0.000	0.000
93	A	97	PRO	0	-0.045	-0.027	30.146	-0.007	-0.007	0.000	0.000	0.000	0.000
94	A	98	THR	0	-0.040	-0.021	27.257	-0.034	-0.034	0.000	0.000	0.000	0.000
95	A	99	LYS	1	0.807	0.900	25.875	0.469	0.469	0.000	0.000	0.000	0.000
96	A	100	CYS	0	-0.076	-0.020	20.889	-0.092	-0.092	0.000	0.000	0.000	0.000
97	A	101	PHE	0	0.069	0.025	19.249	0.061	0.061	0.000	0.000	0.000	0.000
98	A	102	GLY	0	-0.001	-0.002	17.802	-0.138	-0.138	0.000	0.000	0.000	0.000
99	A	103	LEU	0	-0.059	-0.033	13.628	0.080	0.080	0.000	0.000	0.000	0.000
100	A	104	ASP	-1	-0.715	-0.847	18.197	-0.231	-0.231	0.000	0.000	0.000	0.000
101	A	105	VAL	0	-0.068	-0.027	21.521	0.062	0.062	0.000	0.000	0.000	0.000
102	A	106	HIS	1	0.802	0.893	22.378	0.301	0.301	0.000	0.000	0.000	0.000
103	A	107	THR	0	-0.030	-0.031	23.311	0.030	0.030	0.000	0.000	0.000	0.000
104	A	108	GLU	-1	-0.947	-0.970	21.149	0.118	0.118	0.000	0.000	0.000	0.000
105	A	109	TYR	0	-0.083	-0.069	16.801	0.062	0.062	0.000	0.000	0.000	0.000
106	A	110	ARG	1	0.846	0.938	17.143	-0.257	-0.257	0.000	0.000	0.000	0.000
107	A	111	THR	0	-0.039	-0.021	19.683	-0.011	-0.011	0.000	0.000	0.000	0.000
108	A	112	TRP	0	-0.005	-0.019	15.423	-0.075	-0.075	0.000	0.000	0.000	0.000
109	A	113	THR	0	-0.002	0.004	20.884	0.062	0.062	0.000	0.000	0.000	0.000
110	A	114	ASP	-1	-0.875	-0.901	22.337	-0.468	-0.468	0.000	0.000	0.000	0.000
111	A	115	LEU	0	0.016	0.000	21.743	0.036	0.036	0.000	0.000	0.000	0.000
112	A	116	PRO	0	0.067	0.042	25.049	-0.046	-0.046	0.000	0.000	0.000	0.000
113	A	118	GLY	0	0.003	-0.009	23.445	-0.056	-0.056	0.000	0.000	0.000	0.000
114	A	119	GLU	-1	-0.822	-0.904	24.386	-0.442	-0.442	0.000	0.000	0.000	0.000
115	A	120	LYS	1	0.846	0.917	22.367	0.556	0.556	0.000	0.000	0.000	0.000
116	A	121	ASN	0	0.007	0.010	19.803	0.097	0.097	0.000	0.000	0.000	0.000
117	A	122	PRO	0	-0.026	-0.016	16.282	-0.078	-0.078	0.000	0.000	0.000	0.000
118	A	123	PHE	0	0.007	0.002	12.047	0.000	0.000	0.000	0.000	0.000	0.000
119	A	124	ILE	0	0.004	-0.001	8.086	0.090	0.090	0.000	0.000	0.000	0.000
120	A	126	LYS	1	0.834	0.905	4.277	4.407	4.627	-0.002	-0.059	-0.159	0.000
121	A	127	SER	0	0.059	0.033	1.852	-12.398	-14.321	10.337	-3.674	-4.740	-0.043

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