FMO DATABASE

FMODB ID: VRJM1

Calculation Name: 2GUJ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2GUJ

Chain ID: A

ChEMBL ID:

UniProt ID: P54332

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	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	139
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1218510.583873
FMO2-HF: Nuclear repulsion	1163771.795898
FMO2-HF: Total energy	-54738.787975
FMO2-MP2: Total energy	-54897.223336

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:5:ALA)

Summations of interaction energy for fragment #1(A:5:ALA)

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.
-10.172	-6.365	0.065	-1.747	-2.124	0.004

Interaction energy analysis for fragmet #1(A:5:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.002 / q_NPA : -0.022

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	7	ASN	0	-0.110	-0.037	3.144	-3.266	-0.386	0.053	-1.346	-1.587	0.007
4	A	8	THR	0	-0.003	-0.034	4.346	-0.594	-0.317	-0.001	-0.034	-0.242	0.000
5	A	9	ILE	0	0.015	-0.007	5.474	0.593	0.593	0.000	0.000	0.000	0.000
6	A	10	SER	0	0.004	-0.005	9.228	-0.137	-0.137	0.000	0.000	0.000	0.000
7	A	11	GLY	0	0.018	0.007	11.876	0.087	0.087	0.000	0.000	0.000	0.000
8	A	12	LYS	1	0.959	0.986	15.626	0.266	0.266	0.000	0.000	0.000	0.000
9	A	13	GLU	-1	-0.853	-0.922	18.731	-0.160	-0.160	0.000	0.000	0.000	0.000
10	A	14	GLY	0	0.037	0.021	20.701	0.016	0.016	0.000	0.000	0.000	0.000
11	A	15	ARG	1	0.757	0.881	21.667	0.150	0.150	0.000	0.000	0.000	0.000
12	A	16	LEU	0	0.009	0.023	21.644	0.003	0.003	0.000	0.000	0.000	0.000
13	A	17	PHE	0	-0.029	-0.033	23.581	0.005	0.005	0.000	0.000	0.000	0.000
14	A	18	LEU	0	0.017	-0.002	26.044	0.000	0.000	0.000	0.000	0.000	0.000
15	A	19	ASP	-1	-0.913	-0.959	28.043	-0.040	-0.040	0.000	0.000	0.000	0.000
16	A	20	GLY	0	0.011	0.013	29.563	0.006	0.006	0.000	0.000	0.000	0.000
17	A	21	GLU	-1	-0.996	-0.987	31.070	-0.067	-0.067	0.000	0.000	0.000	0.000
18	A	22	GLU	-1	-0.882	-0.933	27.906	-0.111	-0.111	0.000	0.000	0.000	0.000
19	A	23	MET	0	-0.028	-0.008	26.525	0.003	0.003	0.000	0.000	0.000	0.000
20	A	24	ALA	0	0.006	-0.023	24.596	-0.001	-0.001	0.000	0.000	0.000	0.000
21	A	25	HIS	0	-0.111	-0.046	24.859	-0.011	-0.011	0.000	0.000	0.000	0.000
22	A	26	ILE	0	0.033	0.014	18.663	0.001	0.001	0.000	0.000	0.000	0.000
23	A	27	LYS	1	0.841	0.911	20.769	0.198	0.198	0.000	0.000	0.000	0.000
24	A	28	THR	0	0.029	0.015	15.217	0.006	0.006	0.000	0.000	0.000	0.000
25	A	29	PHE	0	0.026	0.010	12.911	0.001	0.001	0.000	0.000	0.000	0.000
26	A	30	GLU	-1	-0.869	-0.926	7.668	-1.786	-1.786	0.000	0.000	0.000	0.000
27	A	31	ALA	0	-0.032	-0.009	9.372	-0.064	-0.064	0.000	0.000	0.000	0.000
28	A	32	ASN	0	-0.021	-0.033	3.375	-2.194	-1.544	0.013	-0.367	-0.295	-0.003
29	A	33	VAL	0	-0.016	0.017	6.544	0.218	0.218	0.000	0.000	0.000	0.000
30	A	34	GLU	-1	-0.820	-0.901	6.716	0.749	0.749	0.000	0.000	0.000	0.000
31	A	35	LYS	1	0.937	0.969	7.049	-1.736	-1.736	0.000	0.000	0.000	0.000
32	A	36	ASN	0	-0.041	-0.028	8.739	0.006	0.006	0.000	0.000	0.000	0.000
33	A	37	LYS	1	0.880	0.926	11.502	-0.311	-0.311	0.000	0.000	0.000	0.000
34	A	38	SER	0	-0.018	-0.012	14.076	0.071	0.071	0.000	0.000	0.000	0.000
35	A	39	GLU	-1	-0.761	-0.862	13.892	0.343	0.343	0.000	0.000	0.000	0.000
36	A	40	VAL	0	-0.041	-0.021	12.871	0.126	0.126	0.000	0.000	0.000	0.000
37	A	41	ASN	0	-0.023	-0.009	11.018	0.235	0.235	0.000	0.000	0.000	0.000
38	A	42	ILE	0	0.034	0.015	10.768	-0.080	-0.080	0.000	0.000	0.000	0.000
39	A	43	MET	0	0.044	0.049	7.739	-0.123	-0.123	0.000	0.000	0.000	0.000
40	A	44	GLY	0	0.001	-0.013	11.506	-0.119	-0.119	0.000	0.000	0.000	0.000
41	A	45	ARG	1	0.756	0.863	13.363	-0.477	-0.477	0.000	0.000	0.000	0.000
42	A	46	ARG	0	0.083	0.090	14.803	-0.028	-0.028	0.000	0.000	0.000	0.000
43	A	47	MET	0	0.059	0.035	12.258	-0.062	-0.062	0.000	0.000	0.000	0.000
44	A	48	THR	0	-0.067	-0.040	16.829	-0.039	-0.039	0.000	0.000	0.000	0.000
45	A	49	GLY	0	-0.027	-0.010	19.436	0.028	0.028	0.000	0.000	0.000	0.000
46	A	50	HIS	0	0.013	0.027	20.458	-0.005	-0.005	0.000	0.000	0.000	0.000
47	A	51	LYN	0	-0.046	-0.029	14.199	0.045	0.045	0.000	0.000	0.000	0.000
48	A	52	THR	0	0.019	0.019	17.533	-0.037	-0.037	0.000	0.000	0.000	0.000
49	A	53	THR	0	-0.001	-0.009	18.679	0.017	0.017	0.000	0.000	0.000	0.000
50	A	54	GLY	0	-0.031	-0.020	16.433	-0.017	-0.017	0.000	0.000	0.000	0.000
51	A	55	ALA	0	0.037	0.007	12.834	-0.021	-0.021	0.000	0.000	0.000	0.000
52	A	56	ASN	0	0.002	0.034	13.240	-0.056	-0.056	0.000	0.000	0.000	0.000
53	A	57	GLY	0	0.040	-0.006	10.291	0.105	0.105	0.000	0.000	0.000	0.000
54	A	58	THR	0	-0.028	0.003	9.136	0.000	0.000	0.000	0.000	0.000	0.000
55	A	59	GLY	0	0.015	-0.013	9.135	-0.112	-0.112	0.000	0.000	0.000	0.000
56	A	60	THR	0	-0.026	0.002	10.300	0.105	0.105	0.000	0.000	0.000	0.000
57	A	61	ALA	0	0.034	0.010	12.798	-0.021	-0.021	0.000	0.000	0.000	0.000
58	A	62	THR	0	0.010	0.045	15.607	0.032	0.032	0.000	0.000	0.000	0.000
59	A	63	PHE	0	0.000	-0.015	18.856	0.020	0.020	0.000	0.000	0.000	0.000
60	A	64	TYR	0	-0.004	-0.001	22.258	0.008	0.008	0.000	0.000	0.000	0.000
61	A	65	LYS	1	0.905	0.964	24.931	0.130	0.130	0.000	0.000	0.000	0.000
62	A	66	VAL	0	0.079	0.026	26.655	-0.003	-0.003	0.000	0.000	0.000	0.000
63	A	67	THR	0	-0.034	-0.005	29.225	0.011	0.011	0.000	0.000	0.000	0.000
64	A	68	SER	0	0.113	0.039	32.097	0.000	0.000	0.000	0.000	0.000	0.000
65	A	69	LYS	1	0.927	0.966	34.069	0.076	0.076	0.000	0.000	0.000	0.000
66	A	70	PHE	0	0.072	0.043	25.278	0.004	0.004	0.000	0.000	0.000	0.000
67	A	71	VAL	0	0.066	0.055	29.951	0.001	0.001	0.000	0.000	0.000	0.000
68	A	72	LEU	0	-0.011	-0.012	31.234	0.002	0.002	0.000	0.000	0.000	0.000
69	A	73	LEU	0	-0.021	-0.006	30.335	0.004	0.004	0.000	0.000	0.000	0.000
70	A	74	MET	0	0.018	-0.005	26.072	0.006	0.006	0.000	0.000	0.000	0.000
71	A	75	MET	0	0.015	0.014	30.099	0.001	0.001	0.000	0.000	0.000	0.000
72	A	76	ASP	-1	-0.844	-0.935	32.729	-0.063	-0.063	0.000	0.000	0.000	0.000
73	A	77	TYR	0	-0.013	-0.009	29.463	0.009	0.009	0.000	0.000	0.000	0.000
74	A	78	VAL	0	0.090	0.042	28.904	0.004	0.004	0.000	0.000	0.000	0.000
75	A	79	LYS	1	0.771	0.908	30.669	0.073	0.073	0.000	0.000	0.000	0.000
76	A	80	LYS	1	0.766	0.906	32.578	0.070	0.070	0.000	0.000	0.000	0.000
77	A	81	GLY	0	0.002	-0.003	30.757	0.004	0.004	0.000	0.000	0.000	0.000
78	A	82	SER	0	-0.092	-0.055	28.466	0.006	0.006	0.000	0.000	0.000	0.000
79	A	83	ASP	-1	-0.787	-0.857	23.660	-0.131	-0.131	0.000	0.000	0.000	0.000
80	A	84	PRO	0	-0.066	-0.030	25.503	0.009	0.009	0.000	0.000	0.000	0.000
81	A	85	TYR	0	-0.006	0.001	20.311	-0.010	-0.010	0.000	0.000	0.000	0.000
82	A	86	PHE	0	-0.014	-0.018	21.938	0.009	0.009	0.000	0.000	0.000	0.000
83	A	87	THR	0	0.023	0.016	21.496	0.001	0.001	0.000	0.000	0.000	0.000
84	A	88	LEU	0	-0.023	-0.010	17.160	0.006	0.006	0.000	0.000	0.000	0.000
85	A	89	GLN	0	-0.005	-0.014	19.370	0.009	0.009	0.000	0.000	0.000	0.000
86	A	90	ALA	0	0.008	0.006	18.142	0.002	0.002	0.000	0.000	0.000	0.000
87	A	91	VAL	0	-0.023	-0.006	20.148	0.029	0.029	0.000	0.000	0.000	0.000
88	A	92	LEU	0	-0.015	-0.003	13.977	-0.032	-0.032	0.000	0.000	0.000	0.000
89	A	93	ASP	-1	-0.895	-0.953	14.309	-0.414	-0.414	0.000	0.000	0.000	0.000
90	A	94	ASP	-1	-0.806	-0.893	14.111	-0.177	-0.177	0.000	0.000	0.000	0.000
91	A	95	GLN	0	-0.050	-0.042	14.916	0.035	0.035	0.000	0.000	0.000	0.000
92	A	96	SER	0	-0.043	-0.018	14.548	0.048	0.048	0.000	0.000	0.000	0.000
93	A	97	SER	0	-0.006	0.000	16.545	0.028	0.028	0.000	0.000	0.000	0.000
94	A	98	GLY	0	-0.032	-0.002	17.929	0.019	0.019	0.000	0.000	0.000	0.000
95	A	99	ARG	1	0.709	0.817	18.733	-0.039	-0.039	0.000	0.000	0.000	0.000
96	A	100	GLY	0	0.032	0.003	21.513	0.001	0.001	0.000	0.000	0.000	0.000
97	A	101	THR	0	-0.046	-0.015	20.813	-0.014	-0.014	0.000	0.000	0.000	0.000
98	A	102	GLU	-1	-0.804	-0.873	19.828	0.006	0.006	0.000	0.000	0.000	0.000
99	A	103	ARG	1	0.815	0.912	20.081	0.047	0.047	0.000	0.000	0.000	0.000
100	A	104	VAL	0	0.017	0.004	14.814	0.019	0.019	0.000	0.000	0.000	0.000
101	A	105	THR	0	-0.054	-0.027	18.273	-0.020	-0.020	0.000	0.000	0.000	0.000
102	A	106	LEU	0	-0.028	-0.026	13.358	0.009	0.009	0.000	0.000	0.000	0.000
103	A	107	TYR	0	-0.054	-0.058	17.296	-0.019	-0.019	0.000	0.000	0.000	0.000
104	A	108	ASP	-1	-0.810	-0.924	18.257	-0.053	-0.053	0.000	0.000	0.000	0.000
105	A	109	VAL	0	-0.002	0.018	17.111	-0.012	-0.012	0.000	0.000	0.000	0.000
106	A	110	ASN	0	-0.022	-0.019	17.775	0.005	0.005	0.000	0.000	0.000	0.000
107	A	111	PHE	0	-0.005	-0.010	18.219	-0.022	-0.022	0.000	0.000	0.000	0.000
108	A	112	ASP	-1	-0.866	-0.927	20.148	-0.156	-0.156	0.000	0.000	0.000	0.000
109	A	113	SER	0	0.018	-0.055	22.527	-0.005	-0.005	0.000	0.000	0.000	0.000
110	A	114	ALA	0	0.007	0.016	25.920	-0.003	-0.003	0.000	0.000	0.000	0.000
111	A	115	LYS	1	0.904	0.966	18.282	0.271	0.271	0.000	0.000	0.000	0.000
112	A	116	ILE	0	-0.039	-0.014	23.003	-0.007	-0.007	0.000	0.000	0.000	0.000
113	A	117	ALA	0	-0.032	-0.022	25.200	0.005	0.005	0.000	0.000	0.000	0.000
114	A	118	SER	0	-0.019	-0.030	26.255	0.005	0.005	0.000	0.000	0.000	0.000
115	A	119	LEU	0	-0.040	-0.011	23.302	-0.006	-0.006	0.000	0.000	0.000	0.000
116	A	120	ASP	-1	-0.988	-0.993	27.271	-0.120	-0.120	0.000	0.000	0.000	0.000
117	A	121	VAL	0	-0.079	-0.039	30.972	0.005	0.005	0.000	0.000	0.000	0.000
118	A	122	ASP	-1	-0.907	-0.948	30.848	-0.114	-0.114	0.000	0.000	0.000	0.000
119	A	123	SER	0	-0.028	-0.019	30.504	-0.007	-0.007	0.000	0.000	0.000	0.000
120	A	124	GLU	-1	-0.995	-0.985	28.879	-0.134	-0.134	0.000	0.000	0.000	0.000
121	A	125	ALA	0	0.001	-0.001	26.307	-0.010	-0.010	0.000	0.000	0.000	0.000
122	A	126	LEU	0	-0.054	-0.022	21.481	-0.007	-0.007	0.000	0.000	0.000	0.000
123	A	127	GLU	-1	-0.973	-0.988	19.862	-0.365	-0.365	0.000	0.000	0.000	0.000
124	A	128	GLU	-1	-0.949	-0.980	21.135	-0.241	-0.241	0.000	0.000	0.000	0.000
125	A	129	GLU	-1	-0.935	-0.971	13.684	-0.676	-0.676	0.000	0.000	0.000	0.000
126	A	130	VAL	0	0.000	0.008	17.313	0.002	0.002	0.000	0.000	0.000	0.000
127	A	131	PRO	0	-0.002	-0.018	14.324	-0.024	-0.024	0.000	0.000	0.000	0.000
128	A	132	PHE	0	-0.053	-0.035	13.445	0.058	0.058	0.000	0.000	0.000	0.000
129	A	133	THR	0	-0.015	-0.025	13.399	-0.069	-0.069	0.000	0.000	0.000	0.000
130	A	134	PHE	0	-0.027	0.009	10.143	0.027	0.027	0.000	0.000	0.000	0.000
131	A	135	GLU	-1	-0.836	-0.922	14.859	-0.044	-0.044	0.000	0.000	0.000	0.000
132	A	136	ASH	0	-0.086	-0.094	15.695	0.054	0.054	0.000	0.000	0.000	0.000
133	A	137	PHE	0	-0.029	-0.017	12.485	-0.032	-0.032	0.000	0.000	0.000	0.000
134	A	138	ASP	-1	-0.814	-0.883	15.595	0.061	0.061	0.000	0.000	0.000	0.000
135	A	139	VAL	0	-0.053	-0.036	16.131	-0.035	-0.035	0.000	0.000	0.000	0.000
136	A	140	PRO	0	0.002	0.028	19.065	0.013	0.013	0.000	0.000	0.000	0.000
137	A	141	GLU	-1	-0.837	-0.894	22.793	-0.035	-0.035	0.000	0.000	0.000	0.000
138	A	142	LYS	1	0.923	0.942	23.143	-0.019	-0.019	0.000	0.000	0.000	0.000
139	A	143	LEU	0	0.021	0.017	24.467	-0.006	-0.006	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:5:ALA)