FMO DATABASE

FMODB ID: 1JG3Z

Calculation Name: 1VCQ-A-Xray310

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1VCQ

Chain ID: A

ChEMBL ID:

UniProt ID: P03315

Base Structure: X-ray

Registration Date: 2021-09-06

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

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. 1.20200116

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	148
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1364910.356314
FMO2-HF: Nuclear repulsion	1307574.492894
FMO2-HF: Total energy	-57335.86342
FMO2-MP2: Total energy	-57502.01267

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:134:CYS )

Summations of interaction energy for fragment #1(A:134: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.
-35.681	-25.31	19.705	-8.467	-21.608	0.028

Interaction energy analysis for fragmet #1(A:134:CYS )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.009 / q_NPA : 0.010

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	121	PHE	0	0.050	0.033	1.904	-12.391	-15.407	12.362	-3.891	-5.455	0.062
4	A	122	GLU	-1	-0.895	-0.968	3.330	-3.330	-3.536	0.133	0.914	-0.841	-0.001
5	A	123	VAL	0	-0.027	-0.024	3.943	-0.425	-0.341	0.004	-0.004	-0.084	0.000
6	A	124	LYS	1	0.919	0.981	6.522	-0.018	-0.018	0.000	0.000	0.000	0.000
7	A	125	HIS	0	0.034	0.008	10.317	-0.286	-0.286	0.000	0.000	0.000	0.000
8	A	126	GLU	-1	-0.901	-0.939	13.215	-0.437	-0.437	0.000	0.000	0.000	0.000
9	A	127	GLY	0	0.006	0.016	15.263	0.075	0.075	0.000	0.000	0.000	0.000
10	A	128	LYS	1	0.883	0.925	14.732	0.345	0.345	0.000	0.000	0.000	0.000
11	A	129	VAL	0	-0.018	-0.004	9.004	-0.255	-0.255	0.000	0.000	0.000	0.000
12	A	130	THR	0	-0.042	-0.043	9.855	0.084	0.084	0.000	0.000	0.000	0.000
13	A	131	GLY	0	0.043	0.030	7.117	-0.053	-0.053	0.000	0.000	0.000	0.000
14	A	132	TYR	0	-0.072	-0.021	3.843	-0.150	2.080	-0.012	-1.064	-1.153	-0.003
17	A	136	VAL	0	-0.002	-0.021	2.708	-2.798	0.812	3.257	-2.319	-4.548	-0.011
18	A	137	GLY	0	-0.004	0.001	4.768	-0.889	-0.759	0.011	-0.015	-0.126	0.000
19	A	138	ASP	-1	-0.884	-0.939	7.644	-0.768	-0.768	0.000	0.000	0.000	0.000
20	A	139	LYS	1	0.928	0.958	8.298	1.159	1.159	0.000	0.000	0.000	0.000
21	A	140	VAL	0	0.043	0.027	4.427	-0.504	-0.200	0.001	-0.067	-0.237	0.000
22	A	141	MET	0	-0.061	-0.040	3.457	0.623	1.674	0.009	-0.285	-0.775	0.000
23	A	142	LYS	1	0.956	0.978	2.685	-2.357	-2.705	0.627	0.848	-1.128	-0.010
24	A	143	PRO	0	0.006	0.009	4.415	2.669	2.842	0.000	-0.015	-0.159	0.000
25	A	144	ALA	0	-0.034	-0.013	7.507	0.187	0.187	0.000	0.000	0.000	0.000
26	A	145	HIS	1	0.788	0.879	10.184	2.393	2.393	0.000	0.000	0.000	0.000
27	A	146	VAL	0	-0.038	-0.010	7.385	0.312	0.312	0.000	0.000	0.000	0.000
28	A	147	LYS	1	0.981	0.987	9.694	1.210	1.210	0.000	0.000	0.000	0.000
29	A	148	GLY	0	0.058	0.035	10.162	-0.143	-0.143	0.000	0.000	0.000	0.000
30	A	149	VAL	0	-0.029	-0.016	9.321	-0.323	-0.323	0.000	0.000	0.000	0.000
31	A	150	ILE	0	0.010	-0.015	4.620	-0.236	-0.139	0.000	-0.007	-0.090	0.000
32	A	151	ASP	-1	-0.903	-0.934	7.226	0.541	0.541	0.000	0.000	0.000	0.000
33	A	152	ASN	0	0.023	-0.001	7.460	0.298	0.298	0.000	0.000	0.000	0.000
34	A	153	ALA	0	0.008	-0.004	9.255	-0.291	-0.291	0.000	0.000	0.000	0.000
35	A	154	ASP	-1	-0.837	-0.928	11.122	-0.242	-0.242	0.000	0.000	0.000	0.000
36	A	155	LEU	0	0.011	-0.014	5.103	-0.306	-0.211	-0.001	-0.004	-0.091	0.000
37	A	156	ALA	0	-0.045	-0.004	9.144	-0.493	-0.493	0.000	0.000	0.000	0.000
38	A	157	LYS	1	0.867	0.926	10.830	0.520	0.520	0.000	0.000	0.000	0.000
39	A	158	LEU	0	0.006	0.034	9.532	0.062	0.062	0.000	0.000	0.000	0.000
40	A	159	ALA	0	0.007	0.006	13.093	-0.085	-0.085	0.000	0.000	0.000	0.000
41	A	160	PHE	0	-0.007	-0.002	6.833	-0.113	-0.113	0.000	0.000	0.000	0.000
42	A	161	LYS	1	0.930	0.978	12.165	1.367	1.367	0.000	0.000	0.000	0.000
43	A	162	LYS	1	0.951	0.965	12.002	1.528	1.528	0.000	0.000	0.000	0.000
44	A	163	SER	0	-0.050	-0.016	12.739	0.351	0.351	0.000	0.000	0.000	0.000
45	A	164	SER	0	0.055	0.015	13.579	-0.206	-0.206	0.000	0.000	0.000	0.000
46	A	165	LYS	1	0.931	0.983	16.076	0.753	0.753	0.000	0.000	0.000	0.000
47	A	166	TYR	0	0.013	-0.027	12.267	0.131	0.131	0.000	0.000	0.000	0.000
48	A	167	ASP	-1	-0.798	-0.863	11.601	-2.605	-2.605	0.000	0.000	0.000	0.000
49	A	168	LEU	0	0.027	0.013	6.931	-0.554	-0.554	0.000	0.000	0.000	0.000
50	A	169	GLU	-1	-0.855	-0.963	8.031	-2.427	-2.427	0.000	0.000	0.000	0.000
51	A	170	CYS	0	-0.033	-0.010	7.493	-0.598	-0.598	0.000	0.000	0.000	0.000
52	A	171	ALA	0	0.052	0.023	8.213	0.593	0.593	0.000	0.000	0.000	0.000
53	A	172	GLN	0	-0.030	-0.018	9.351	-0.049	-0.049	0.000	0.000	0.000	0.000
54	A	173	ILE	0	0.031	0.031	6.071	0.069	0.069	0.000	0.000	0.000	0.000
55	A	174	PRO	0	0.011	0.020	9.468	0.106	0.106	0.000	0.000	0.000	0.000
56	A	175	VAL	0	0.021	-0.024	11.050	0.021	0.021	0.000	0.000	0.000	0.000
57	A	176	HIS	0	-0.018	-0.019	12.095	-0.028	-0.028	0.000	0.000	0.000	0.000
58	A	177	MET	0	0.042	0.032	7.019	0.049	0.049	0.000	0.000	0.000	0.000
59	A	178	ARG	1	0.846	0.932	7.004	0.279	0.279	0.000	0.000	0.000	0.000
60	A	179	SER	0	0.004	0.014	8.320	0.102	0.102	0.000	0.000	0.000	0.000
61	A	180	ASP	-1	-0.932	-0.964	4.407	-0.414	-0.353	0.000	-0.009	-0.051	0.000
62	A	181	ALA	0	-0.052	-0.005	3.248	-3.180	-1.993	0.030	-0.502	-0.715	-0.004
63	A	182	SER	0	0.011	0.000	2.147	-0.823	-0.226	1.688	-0.824	-1.460	-0.002
64	A	183	LYS	1	0.962	0.971	4.171	-1.528	-1.414	0.002	-0.029	-0.086	0.000
65	A	184	TYR	0	0.022	0.024	7.025	0.889	0.889	0.000	0.000	0.000	0.000
66	A	185	THR	0	-0.019	-0.017	8.264	-0.389	-0.389	0.000	0.000	0.000	0.000
67	A	186	HIS	0	0.039	0.008	11.584	0.040	0.040	0.000	0.000	0.000	0.000
68	A	187	GLU	-1	-0.915	-0.953	14.295	0.544	0.544	0.000	0.000	0.000	0.000
69	A	188	LYS	1	0.812	0.928	13.217	-0.248	-0.248	0.000	0.000	0.000	0.000
70	A	189	PRO	0	0.009	0.016	16.117	-0.107	-0.107	0.000	0.000	0.000	0.000
71	A	190	GLU	-1	-0.831	-0.917	18.635	0.343	0.343	0.000	0.000	0.000	0.000
72	A	191	GLY	0	0.005	0.001	20.273	0.024	0.024	0.000	0.000	0.000	0.000
73	A	192	HIS	0	-0.074	-0.038	18.062	-0.031	-0.031	0.000	0.000	0.000	0.000
74	A	193	TYR	0	-0.024	-0.031	12.675	0.126	0.126	0.000	0.000	0.000	0.000
75	A	194	ASN	0	-0.032	-0.025	11.117	-0.003	-0.003	0.000	0.000	0.000	0.000
76	A	195	TRP	0	0.056	0.012	9.028	0.407	0.407	0.000	0.000	0.000	0.000
77	A	196	HIS	0	-0.005	0.007	9.393	-0.253	-0.253	0.000	0.000	0.000	0.000
78	A	197	HIS	1	0.831	0.915	10.949	-1.075	-1.075	0.000	0.000	0.000	0.000
79	A	198	GLY	0	0.040	0.030	14.201	-0.211	-0.211	0.000	0.000	0.000	0.000
80	A	199	ALA	0	0.009	0.006	14.287	0.174	0.174	0.000	0.000	0.000	0.000
81	A	200	VAL	0	0.001	-0.006	12.580	-0.074	-0.074	0.000	0.000	0.000	0.000
82	A	201	GLN	0	-0.031	-0.007	16.050	0.074	0.074	0.000	0.000	0.000	0.000
83	A	202	TYR	0	-0.047	-0.022	16.542	-0.049	-0.049	0.000	0.000	0.000	0.000
84	A	203	SER	0	0.076	0.030	18.645	-0.006	-0.006	0.000	0.000	0.000	0.000
85	A	204	GLY	0	0.021	0.020	21.878	-0.036	-0.036	0.000	0.000	0.000	0.000
86	A	205	GLY	0	-0.033	-0.015	19.485	-0.044	-0.044	0.000	0.000	0.000	0.000
87	A	206	ARG	1	0.858	0.906	18.443	-0.045	-0.045	0.000	0.000	0.000	0.000
88	A	207	PHE	0	0.043	0.018	13.109	0.094	0.094	0.000	0.000	0.000	0.000
89	A	208	THR	0	0.009	-0.004	16.747	-0.092	-0.092	0.000	0.000	0.000	0.000
90	A	209	ILE	0	-0.049	-0.002	14.466	0.128	0.128	0.000	0.000	0.000	0.000
91	A	210	PRO	0	-0.017	-0.004	17.865	-0.084	-0.084	0.000	0.000	0.000	0.000
92	A	211	THR	0	0.046	-0.004	19.910	0.023	0.023	0.000	0.000	0.000	0.000
93	A	212	GLY	0	0.035	0.025	19.871	0.014	0.014	0.000	0.000	0.000	0.000
94	A	213	ALA	0	-0.058	-0.016	16.461	0.037	0.037	0.000	0.000	0.000	0.000
95	A	214	GLY	0	-0.052	-0.030	14.518	0.099	0.099	0.000	0.000	0.000	0.000
96	A	215	LYS	1	0.942	0.992	15.034	-0.289	-0.289	0.000	0.000	0.000	0.000
97	A	216	PRO	0	0.057	-0.003	14.241	-0.073	-0.073	0.000	0.000	0.000	0.000
98	A	217	GLY	0	0.008	0.011	11.045	0.183	0.183	0.000	0.000	0.000	0.000
99	A	218	ASP	-1	-0.845	-0.914	9.873	0.431	0.431	0.000	0.000	0.000	0.000
100	A	219	SER	0	0.041	0.008	7.851	0.135	0.135	0.000	0.000	0.000	0.000
101	A	220	GLY	0	-0.023	-0.024	4.331	-0.792	-0.748	0.000	-0.017	-0.027	0.000
102	A	221	ARG	1	0.817	0.911	3.234	-1.976	-0.952	0.061	-0.355	-0.730	-0.003
103	A	222	PRO	0	-0.005	-0.002	3.027	-3.063	-1.547	1.261	-0.520	-2.257	0.000
104	A	223	ILE	0	0.016	0.017	5.099	-0.223	-0.171	0.000	-0.018	-0.034	0.000
105	A	224	PHE	0	-0.013	-0.026	5.418	0.018	0.190	0.000	-0.008	-0.165	0.000
106	A	225	ASP	-1	-0.725	-0.847	9.048	1.228	1.228	0.000	0.000	0.000	0.000
107	A	226	ASN	0	0.058	0.004	11.601	0.274	0.274	0.000	0.000	0.000	0.000
108	A	227	LYS	1	0.830	0.924	12.767	-1.237	-1.237	0.000	0.000	0.000	0.000
109	A	228	GLY	0	0.023	0.020	8.706	-0.123	-0.123	0.000	0.000	0.000	0.000
110	A	229	ARG	1	0.764	0.886	7.405	-0.448	-0.448	0.000	0.000	0.000	0.000
111	A	230	VAL	0	-0.004	-0.011	3.450	-0.828	-0.020	0.250	-0.190	-0.868	0.000
112	A	231	VAL	0	0.004	-0.001	6.751	-0.824	-0.824	0.000	0.000	0.000	0.000
113	A	232	ALA	0	-0.010	-0.025	8.046	-0.591	-0.591	0.000	0.000	0.000	0.000
114	A	233	ILE	0	-0.041	-0.010	3.293	0.325	0.917	0.022	-0.086	-0.528	0.000
115	A	234	VAL	0	0.018	0.014	6.426	-0.393	-0.393	0.000	0.000	0.000	0.000
116	A	235	LEU	0	-0.058	-0.022	8.198	-1.026	-1.026	0.000	0.000	0.000	0.000
117	A	236	GLY	0	0.073	0.024	10.560	-0.060	-0.060	0.000	0.000	0.000	0.000
118	A	237	GLY	0	-0.021	-0.003	13.932	0.139	0.139	0.000	0.000	0.000	0.000
119	A	238	ALA	0	0.059	0.059	16.830	-0.019	-0.019	0.000	0.000	0.000	0.000
120	A	239	ASN	0	0.001	-0.011	20.578	0.105	0.105	0.000	0.000	0.000	0.000
121	A	240	GLU	-1	-0.791	-0.873	22.472	-0.061	-0.061	0.000	0.000	0.000	0.000
122	A	241	GLY	0	0.025	0.017	25.241	0.028	0.028	0.000	0.000	0.000	0.000
123	A	242	SER	0	-0.008	-0.014	25.925	0.006	0.006	0.000	0.000	0.000	0.000
124	A	243	ARG	1	0.900	0.956	19.900	-0.316	-0.316	0.000	0.000	0.000	0.000
125	A	244	THR	0	0.036	0.017	18.112	-0.053	-0.053	0.000	0.000	0.000	0.000
126	A	245	ALA	0	0.002	0.004	19.000	0.086	0.086	0.000	0.000	0.000	0.000
127	A	246	LEU	0	-0.045	-0.032	12.387	-0.067	-0.067	0.000	0.000	0.000	0.000
128	A	247	SER	0	0.011	0.007	14.378	0.028	0.028	0.000	0.000	0.000	0.000
129	A	248	VAL	0	-0.028	-0.027	10.564	-0.120	-0.120	0.000	0.000	0.000	0.000
130	A	249	VAL	0	0.034	0.042	7.737	0.024	0.024	0.000	0.000	0.000	0.000
131	A	250	THR	0	0.027	-0.007	9.036	0.367	0.367	0.000	0.000	0.000	0.000
132	A	251	TRP	0	0.024	0.014	5.528	-0.093	-0.093	0.000	0.000	0.000	0.000
133	A	252	ASN	0	-0.058	-0.038	12.462	0.138	0.138	0.000	0.000	0.000	0.000
134	A	253	LYS	1	0.975	0.967	16.234	-0.133	-0.133	0.000	0.000	0.000	0.000
135	A	254	ASP	-1	-0.896	-0.925	15.618	-0.225	-0.225	0.000	0.000	0.000	0.000
136	A	255	MET	0	0.009	0.021	15.017	-0.075	-0.075	0.000	0.000	0.000	0.000
137	A	256	VAL	0	-0.036	-0.028	10.147	0.058	0.058	0.000	0.000	0.000	0.000
138	A	257	THR	0	-0.005	-0.011	12.738	-0.058	-0.058	0.000	0.000	0.000	0.000
139	A	258	ARG	1	0.921	0.952	12.519	1.048	1.048	0.000	0.000	0.000	0.000
140	A	259	VAL	0	-0.035	0.000	14.052	0.070	0.070	0.000	0.000	0.000	0.000
141	A	260	THR	0	-0.008	-0.017	15.204	-0.084	-0.084	0.000	0.000	0.000	0.000
142	A	261	PRO	0	-0.022	0.000	17.323	0.025	0.025	0.000	0.000	0.000	0.000
143	A	262	GLU	-1	-0.880	-0.916	20.567	-0.314	-0.314	0.000	0.000	0.000	0.000
144	A	263	GLY	0	0.038	0.004	23.447	0.035	0.035	0.000	0.000	0.000	0.000
145	A	264	SER	0	-0.106	-0.076	18.015	0.023	0.023	0.000	0.000	0.000	0.000
146	A	265	GLU	-1	-0.878	-0.917	17.882	-0.508	-0.508	0.000	0.000	0.000	0.000
147	A	266	GLU	-1	-1.016	-1.025	13.957	-1.452	-1.452	0.000	0.000	0.000	0.000
148	A	267	TRP	-1	-0.804	-0.893	11.009	-1.722	-1.722	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:134:CYS )