FMO DATABASE

FMODB ID: N951Q

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1028819.986957
FMO2-HF: Nuclear repulsion	978063.890519
FMO2-HF: Total energy	-50756.096437
FMO2-MP2: Total energy	-50900.801351

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.
-47.082	-47.972	39.015	-16.215	-21.91	-0.001

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 : -0.049 / q_NPA : -0.035

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	0.005	-0.004	3.417	-2.358	-0.856	0.063	-0.741	-0.824	0.000
4	A	7	ASP	-1	-0.904	-0.945	5.786	-1.683	-1.683	0.000	0.000	0.000	0.000
5	A	8	TRP	0	-0.006	-0.005	2.215	-2.068	-0.023	2.338	-1.205	-3.178	-0.007
6	A	9	SER	0	-0.027	-0.016	3.784	-0.775	-0.076	0.016	-0.211	-0.503	-0.001
7	A	10	SER	0	0.032	0.003	2.323	-4.597	-3.402	11.649	-5.815	-7.030	-0.004
8	A	11	TYR	0	-0.022	-0.021	1.779	-15.032	-22.317	11.913	-1.288	-3.341	0.049
9	A	12	LYS	1	0.956	0.972	3.323	-4.244	-3.599	0.192	-0.034	-0.803	0.000
10	A	13	GLY	0	0.019	0.012	3.806	-3.177	-1.636	-0.020	-0.915	-0.606	-0.004
13	A	17	LYS	1	0.914	0.966	3.823	0.809	3.483	-0.030	-1.424	-1.219	0.007
14	A	18	VAL	0	0.009	0.020	6.597	-0.182	-0.182	0.000	0.000	0.000	0.000
15	A	19	PHE	0	-0.023	-0.025	8.297	0.200	0.200	0.000	0.000	0.000	0.000
16	A	20	LYS	1	0.982	0.966	12.432	0.584	0.584	0.000	0.000	0.000	0.000
17	A	21	LYS	1	0.813	0.945	14.702	1.156	1.156	0.000	0.000	0.000	0.000
18	A	22	VAL	0	0.048	0.014	17.002	-0.090	-0.090	0.000	0.000	0.000	0.000
19	A	23	GLY	0	-0.020	-0.012	19.222	0.012	0.012	0.000	0.000	0.000	0.000
20	A	24	THR	0	-0.016	0.006	20.026	-0.007	-0.007	0.000	0.000	0.000	0.000
21	A	25	TRP	0	0.063	0.029	16.955	-0.073	-0.073	0.000	0.000	0.000	0.000
22	A	26	GLU	-1	-0.912	-0.972	17.816	-0.886	-0.886	0.000	0.000	0.000	0.000
23	A	27	ASP	-1	-0.917	-0.961	18.192	-0.881	-0.881	0.000	0.000	0.000	0.000
24	A	28	ALA	0	-0.046	-0.017	15.058	-0.118	-0.118	0.000	0.000	0.000	0.000
25	A	29	GLU	-1	-0.717	-0.852	13.363	-2.369	-2.369	0.000	0.000	0.000	0.000
26	A	30	LYS	1	0.910	0.952	13.438	0.726	0.726	0.000	0.000	0.000	0.000
27	A	31	PHE	0	0.107	0.049	11.087	0.036	0.036	0.000	0.000	0.000	0.000
28	A	32	CYS	0	-0.070	0.000	7.209	0.000	0.000	0.000	0.000	0.000	0.000
29	A	33	VAL	0	-0.016	0.010	9.287	-0.408	-0.408	0.000	0.000	0.000	0.000
30	A	34	GLU	-1	-0.979	-0.985	11.124	-1.381	-1.381	0.000	0.000	0.000	0.000
31	A	35	ASN	0	-0.123	-0.061	7.456	0.035	0.035	0.000	0.000	0.000	0.000
32	A	36	SER	0	-0.037	-0.028	6.817	-0.462	-0.462	0.000	0.000	0.000	0.000
33	A	37	GLY	0	-0.019	-0.012	6.839	-1.168	-1.168	0.000	0.000	0.000	0.000
34	A	38	HIS	1	0.813	0.884	7.646	3.641	3.641	0.000	0.000	0.000	0.000
35	A	39	LEU	0	0.035	0.033	8.632	-0.690	-0.690	0.000	0.000	0.000	0.000
36	A	40	ALA	0	-0.050	-0.034	8.356	-0.235	-0.235	0.000	0.000	0.000	0.000
37	A	41	SER	0	0.029	0.030	8.938	0.313	0.313	0.000	0.000	0.000	0.000
38	A	42	ILE	0	-0.030	-0.031	9.315	-0.220	-0.220	0.000	0.000	0.000	0.000
39	A	43	ASP	-1	-0.882	-0.947	10.515	-0.912	-0.912	0.000	0.000	0.000	0.000
40	A	44	SER	0	-0.022	-0.001	11.399	0.303	0.303	0.000	0.000	0.000	0.000
41	A	45	LYS	1	0.902	0.931	13.361	-0.338	-0.338	0.000	0.000	0.000	0.000
42	A	46	GLU	-1	-0.911	-0.957	12.116	1.401	1.401	0.000	0.000	0.000	0.000
43	A	47	GLU	-1	-0.822	-0.877	7.205	-1.478	-1.478	0.000	0.000	0.000	0.000
44	A	48	ALA	0	0.018	-0.006	10.395	0.141	0.141	0.000	0.000	0.000	0.000
45	A	49	ASP	-1	-0.810	-0.900	13.122	0.604	0.604	0.000	0.000	0.000	0.000
46	A	50	PHE	0	-0.058	-0.019	5.766	0.486	0.486	0.000	0.000	0.000	0.000
47	A	51	VAL	0	0.030	0.005	8.958	0.053	0.053	0.000	0.000	0.000	0.000
48	A	52	THR	0	0.002	-0.012	10.789	-0.144	-0.144	0.000	0.000	0.000	0.000
49	A	53	LYS	1	0.940	0.978	12.398	-1.792	-1.792	0.000	0.000	0.000	0.000
50	A	54	LEU	0	-0.018	-0.007	7.037	-0.151	-0.151	0.000	0.000	0.000	0.000
51	A	55	ALA	0	0.021	0.015	11.132	-0.239	-0.239	0.000	0.000	0.000	0.000
52	A	56	SER	0	0.041	0.003	13.602	-0.115	-0.115	0.000	0.000	0.000	0.000
53	A	57	GLN	0	-0.059	-0.037	13.926	0.042	0.042	0.000	0.000	0.000	0.000
54	A	58	THR	0	-0.079	-0.029	12.378	-0.047	-0.047	0.000	0.000	0.000	0.000
55	A	59	LEU	0	-0.044	-0.009	14.887	-0.118	-0.118	0.000	0.000	0.000	0.000
56	A	60	THR	0	-0.048	-0.022	17.695	0.010	0.010	0.000	0.000	0.000	0.000
57	A	61	LYS	1	0.922	0.973	19.978	0.087	0.087	0.000	0.000	0.000	0.000
58	A	62	PHE	0	0.042	0.018	20.129	0.004	0.004	0.000	0.000	0.000	0.000
59	A	63	VAL	0	-0.047	-0.036	22.947	0.003	0.003	0.000	0.000	0.000	0.000
60	A	64	TYR	0	-0.009	0.003	20.794	-0.015	-0.015	0.000	0.000	0.000	0.000
61	A	65	ASP	-1	-0.761	-0.860	20.666	-0.269	-0.269	0.000	0.000	0.000	0.000
62	A	66	ALA	0	-0.031	-0.037	15.199	-0.043	-0.043	0.000	0.000	0.000	0.000
63	A	67	TRP	0	-0.015	0.005	15.934	-0.023	-0.023	0.000	0.000	0.000	0.000
64	A	68	ILE	0	0.002	-0.009	13.057	-0.150	-0.150	0.000	0.000	0.000	0.000
65	A	69	GLY	0	0.002	-0.017	12.855	0.075	0.075	0.000	0.000	0.000	0.000
66	A	70	LEU	0	-0.040	-0.002	14.135	-0.012	-0.012	0.000	0.000	0.000	0.000
67	A	71	ARG	1	0.831	0.879	17.334	0.836	0.836	0.000	0.000	0.000	0.000
68	A	72	ASP	-1	-0.824	-0.882	20.651	-0.461	-0.461	0.000	0.000	0.000	0.000
69	A	73	GLU	-1	-0.835	-0.919	21.676	-0.792	-0.792	0.000	0.000	0.000	0.000
70	A	74	SER	0	-0.045	-0.017	25.055	0.031	0.031	0.000	0.000	0.000	0.000
71	A	75	LYS	1	0.923	0.954	28.799	0.353	0.353	0.000	0.000	0.000	0.000
72	A	76	THR	0	-0.063	-0.036	31.013	0.001	0.001	0.000	0.000	0.000	0.000
73	A	77	GLN	0	-0.007	-0.020	31.457	-0.021	-0.021	0.000	0.000	0.000	0.000
74	A	78	GLN	0	0.017	0.015	31.502	-0.009	-0.009	0.000	0.000	0.000	0.000
75	A	79	CYS	0	0.011	0.005	29.608	0.002	0.002	0.000	0.000	0.000	0.000
76	A	80	SER	0	-0.043	0.002	31.634	-0.002	-0.002	0.000	0.000	0.000	0.000
77	A	81	PRO	0	0.018	0.003	34.198	0.002	0.002	0.000	0.000	0.000	0.000
78	A	82	GLN	0	-0.025	-0.034	36.620	0.013	0.013	0.000	0.000	0.000	0.000
79	A	83	TRP	0	0.035	0.037	39.768	-0.002	-0.002	0.000	0.000	0.000	0.000
80	A	84	THR	0	-0.011	-0.021	42.396	0.001	0.001	0.000	0.000	0.000	0.000
81	A	85	ASP	-1	-0.886	-0.919	44.075	-0.144	-0.144	0.000	0.000	0.000	0.000
82	A	86	GLY	0	0.000	-0.002	44.421	0.005	0.005	0.000	0.000	0.000	0.000
83	A	87	SER	0	-0.076	-0.037	45.043	-0.007	-0.007	0.000	0.000	0.000	0.000
84	A	88	SER	0	-0.008	-0.034	41.457	-0.004	-0.004	0.000	0.000	0.000	0.000
85	A	89	VAL	0	-0.020	0.024	37.935	0.008	0.008	0.000	0.000	0.000	0.000
86	A	90	VAL	0	-0.049	-0.022	39.344	-0.011	-0.011	0.000	0.000	0.000	0.000
87	A	91	TYR	0	-0.029	-0.020	40.250	-0.008	-0.008	0.000	0.000	0.000	0.000
88	A	92	GLU	-1	-0.737	-0.869	35.966	-0.292	-0.292	0.000	0.000	0.000	0.000
89	A	93	ASN	0	-0.045	-0.029	39.802	-0.011	-0.011	0.000	0.000	0.000	0.000
90	A	94	VAL	0	-0.021	-0.011	33.839	0.011	0.011	0.000	0.000	0.000	0.000
91	A	95	ASP	-1	-0.948	-0.966	36.625	-0.234	-0.234	0.000	0.000	0.000	0.000
92	A	96	GLU	-1	-0.911	-0.964	31.180	-0.323	-0.323	0.000	0.000	0.000	0.000
93	A	97	PRO	0	-0.074	-0.038	30.375	-0.004	-0.004	0.000	0.000	0.000	0.000
94	A	98	THR	0	-0.034	-0.034	27.199	-0.021	-0.021	0.000	0.000	0.000	0.000
95	A	99	LYS	1	0.844	0.905	25.503	0.453	0.453	0.000	0.000	0.000	0.000
96	A	100	CYS	0	-0.070	-0.025	20.777	-0.089	-0.089	0.000	0.000	0.000	0.000
97	A	101	PHE	0	0.066	0.031	19.196	0.060	0.060	0.000	0.000	0.000	0.000
98	A	102	GLY	0	0.005	0.000	17.766	-0.127	-0.127	0.000	0.000	0.000	0.000
99	A	103	LEU	0	-0.092	-0.047	13.811	0.086	0.086	0.000	0.000	0.000	0.000
100	A	104	ASP	-1	-0.766	-0.900	18.348	-0.182	-0.182	0.000	0.000	0.000	0.000
101	A	105	VAL	0	0.014	0.005	21.794	0.070	0.070	0.000	0.000	0.000	0.000
102	A	106	HIS	1	0.866	0.931	22.721	0.193	0.193	0.000	0.000	0.000	0.000
103	A	107	THR	0	-0.021	0.024	22.852	0.030	0.030	0.000	0.000	0.000	0.000
104	A	108	GLU	-1	-0.963	-0.989	21.333	0.203	0.203	0.000	0.000	0.000	0.000
105	A	109	TYR	0	-0.090	-0.057	16.869	0.071	0.071	0.000	0.000	0.000	0.000
106	A	110	ARG	1	0.906	0.988	17.259	-0.353	-0.353	0.000	0.000	0.000	0.000
107	A	111	THR	0	-0.036	-0.037	19.506	-0.009	-0.009	0.000	0.000	0.000	0.000
108	A	112	TRP	0	-0.010	-0.023	15.184	-0.067	-0.067	0.000	0.000	0.000	0.000
109	A	113	THR	0	0.009	0.012	20.862	0.034	0.034	0.000	0.000	0.000	0.000
110	A	114	ASP	-1	-0.855	-0.888	22.490	-0.391	-0.391	0.000	0.000	0.000	0.000
111	A	115	LEU	0	0.018	-0.007	21.794	0.026	0.026	0.000	0.000	0.000	0.000
112	A	116	PRO	0	0.083	0.044	25.107	-0.045	-0.045	0.000	0.000	0.000	0.000
113	A	118	GLY	0	-0.010	-0.010	23.478	-0.051	-0.051	0.000	0.000	0.000	0.000
114	A	119	GLU	-1	-0.845	-0.894	24.386	-0.397	-0.397	0.000	0.000	0.000	0.000
115	A	120	LYS	1	0.878	0.929	22.372	0.485	0.485	0.000	0.000	0.000	0.000
116	A	121	ASN	0	0.007	-0.011	19.654	0.095	0.095	0.000	0.000	0.000	0.000
117	A	122	PRO	0	-0.037	-0.005	15.928	-0.097	-0.097	0.000	0.000	0.000	0.000
118	A	123	PHE	0	0.017	-0.002	12.042	0.017	0.017	0.000	0.000	0.000	0.000
119	A	124	ILE	0	0.002	0.008	8.287	0.021	0.021	0.000	0.000	0.000	0.000
120	A	126	LYS	1	0.875	0.929	4.099	4.285	4.559	-0.001	-0.082	-0.191	0.000
121	A	127	SER	0	0.042	0.030	1.760	-12.091	-16.271	12.895	-4.500	-4.215	-0.041

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