FMO DATABASE

FMODB ID: 14YJZ

Calculation Name: 1VCQ-A-Xray372

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: 2023-03-13

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	148
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1364548.657321
FMO2-HF: Nuclear repulsion	1307211.210341
FMO2-HF: Total energy	-57337.44698
FMO2-MP2: Total energy	-57503.543074

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:119:CYS)

Summations of interaction energy for fragment #1(A:119: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.
-34.64	-22.528	18.295	-8.575	-21.833	0.025

Interaction energy analysis for fragmet #1(A:119:CYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.016 / q_NPA : 0.012

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	0.067	0.041	1.922	-11.800	-13.411	10.841	-4.133	-5.096	0.057
4	A	122	GLU	-1	-0.852	-0.944	3.330	-2.813	-3.064	0.132	0.929	-0.811	-0.001
5	A	123	VAL	0	-0.028	-0.023	3.866	-0.381	-0.293	0.005	-0.002	-0.091	0.000
6	A	124	LYS	1	0.802	0.901	6.522	-0.303	-0.303	0.000	0.000	0.000	0.000
7	A	125	HIS	0	0.004	-0.012	10.317	-0.365	-0.365	0.000	0.000	0.000	0.000
8	A	126	GLU	-1	-0.868	-0.916	13.215	-0.429	-0.429	0.000	0.000	0.000	0.000
9	A	127	GLY	0	0.035	0.026	15.265	0.065	0.065	0.000	0.000	0.000	0.000
10	A	128	LYS	1	0.862	0.914	14.732	0.289	0.289	0.000	0.000	0.000	0.000
11	A	129	VAL	0	-0.005	0.007	8.948	-0.222	-0.222	0.000	0.000	0.000	0.000
12	A	130	THR	0	0.016	-0.012	9.886	0.182	0.182	0.000	0.000	0.000	0.000
13	A	131	GLY	0	-0.029	-0.011	7.111	-0.074	-0.074	0.000	0.000	0.000	0.000
14	A	132	TYR	0	-0.050	-0.012	3.843	-0.138	2.122	-0.019	-1.068	-1.174	-0.002
17	A	136	VAL	0	0.017	-0.014	2.655	-3.120	0.759	3.550	-2.275	-5.154	-0.012
18	A	137	GLY	0	-0.002	0.004	4.596	-0.897	-0.802	0.017	0.022	-0.133	0.000
19	A	138	ASP	-1	-0.798	-0.881	7.590	-0.899	-0.899	0.000	0.000	0.000	0.000
20	A	139	LYS	1	0.816	0.886	8.214	0.927	0.927	0.000	0.000	0.000	0.000
21	A	140	VAL	0	0.029	0.023	4.593	-0.455	-0.178	-0.002	-0.055	-0.220	0.000
22	A	141	MET	0	-0.060	-0.036	3.379	0.560	1.661	0.011	-0.298	-0.814	0.000
23	A	142	LYS	1	0.926	0.945	2.703	-2.505	-2.957	0.604	0.870	-1.022	-0.009
24	A	143	PRO	0	-0.017	-0.009	4.557	2.287	2.476	-0.002	-0.012	-0.176	0.000
25	A	144	ALA	0	-0.006	0.003	7.507	0.183	0.183	0.000	0.000	0.000	0.000
26	A	145	HIS	1	0.782	0.873	10.184	2.220	2.220	0.000	0.000	0.000	0.000
27	A	146	VAL	0	-0.060	-0.026	7.052	0.363	0.363	0.000	0.000	0.000	0.000
28	A	147	LYS	1	0.999	1.000	9.694	1.143	1.143	0.000	0.000	0.000	0.000
29	A	148	GLY	0	0.065	0.040	10.162	-0.146	-0.146	0.000	0.000	0.000	0.000
30	A	149	VAL	0	-0.048	-0.027	9.314	-0.317	-0.317	0.000	0.000	0.000	0.000
31	A	150	ILE	0	0.000	-0.017	4.729	-0.225	-0.108	-0.002	-0.006	-0.109	0.000
32	A	151	ASP	-1	-0.844	-0.890	7.226	0.564	0.564	0.000	0.000	0.000	0.000
33	A	152	ASN	0	0.009	-0.013	7.363	0.272	0.272	0.000	0.000	0.000	0.000
34	A	153	ALA	0	0.006	0.000	9.255	-0.269	-0.269	0.000	0.000	0.000	0.000
35	A	154	ASP	-1	-0.780	-0.893	10.996	-0.174	-0.174	0.000	0.000	0.000	0.000
36	A	155	LEU	0	0.005	-0.022	4.997	-0.279	-0.174	-0.002	-0.003	-0.100	0.000
37	A	156	ALA	0	-0.034	0.000	9.144	-0.469	-0.469	0.000	0.000	0.000	0.000
38	A	157	LYS	1	0.868	0.925	10.830	0.508	0.508	0.000	0.000	0.000	0.000
39	A	158	LEU	0	0.004	0.036	9.448	0.057	0.057	0.000	0.000	0.000	0.000
40	A	159	ALA	0	0.007	0.004	13.093	-0.073	-0.073	0.000	0.000	0.000	0.000
41	A	160	PHE	0	-0.016	-0.005	6.995	-0.159	-0.159	0.000	0.000	0.000	0.000
42	A	161	LYS	1	0.941	0.980	12.178	1.328	1.328	0.000	0.000	0.000	0.000
43	A	162	LYS	1	0.898	0.931	12.019	1.738	1.738	0.000	0.000	0.000	0.000
44	A	163	SER	0	-0.053	-0.012	12.743	0.329	0.329	0.000	0.000	0.000	0.000
45	A	164	SER	0	0.063	0.017	13.586	-0.199	-0.199	0.000	0.000	0.000	0.000
46	A	165	LYS	1	0.955	0.988	16.081	0.712	0.712	0.000	0.000	0.000	0.000
47	A	166	TYR	0	0.014	-0.018	12.210	0.138	0.138	0.000	0.000	0.000	0.000
48	A	167	ASP	-1	-0.775	-0.849	11.742	-2.510	-2.510	0.000	0.000	0.000	0.000
49	A	168	LEU	0	0.005	0.007	6.544	-0.545	-0.545	0.000	0.000	0.000	0.000
50	A	169	GLU	-1	-0.777	-0.899	8.047	-2.274	-2.274	0.000	0.000	0.000	0.000
51	A	170	CYS	0	-0.039	-0.007	7.502	-0.575	-0.575	0.000	0.000	0.000	0.000
52	A	171	ALA	0	0.069	0.025	8.249	0.558	0.558	0.000	0.000	0.000	0.000
53	A	172	GLN	0	-0.033	-0.013	9.374	-0.066	-0.066	0.000	0.000	0.000	0.000
54	A	173	ILE	0	0.027	0.028	6.256	0.083	0.083	0.000	0.000	0.000	0.000
55	A	174	PRO	0	0.017	0.022	9.440	0.095	0.095	0.000	0.000	0.000	0.000
56	A	175	VAL	0	0.012	-0.018	11.053	0.002	0.002	0.000	0.000	0.000	0.000
57	A	176	HIS	0	-0.007	-0.020	12.091	-0.052	-0.052	0.000	0.000	0.000	0.000
58	A	177	MET	0	0.018	0.018	7.010	0.058	0.058	0.000	0.000	0.000	0.000
59	A	178	ARG	1	0.842	0.923	6.996	0.287	0.287	0.000	0.000	0.000	0.000
60	A	179	SER	0	-0.025	-0.006	8.546	0.085	0.085	0.000	0.000	0.000	0.000
61	A	180	ASP	-1	-0.908	-0.940	4.367	-0.642	-0.567	-0.002	-0.008	-0.065	0.000
62	A	181	ALA	0	-0.064	-0.015	3.268	-3.400	-2.228	0.028	-0.485	-0.715	-0.004
63	A	182	SER	0	-0.002	-0.002	2.147	-0.963	-0.277	1.756	-0.866	-1.576	-0.002
64	A	183	LYS	1	0.980	0.982	4.103	-1.159	-1.043	0.001	-0.032	-0.084	0.000
65	A	184	TYR	0	0.036	0.021	6.873	0.924	0.924	0.000	0.000	0.000	0.000
66	A	185	THR	0	-0.020	-0.013	8.238	-0.399	-0.399	0.000	0.000	0.000	0.000
67	A	186	HIS	0	0.020	0.010	11.572	0.022	0.022	0.000	0.000	0.000	0.000
68	A	187	GLU	-1	-0.865	-0.918	14.269	0.608	0.608	0.000	0.000	0.000	0.000
69	A	188	LYS	1	0.862	0.944	13.693	-0.191	-0.191	0.000	0.000	0.000	0.000
70	A	189	PRO	0	0.006	0.013	16.171	-0.098	-0.098	0.000	0.000	0.000	0.000
71	A	190	GLU	-1	-0.785	-0.883	18.729	0.327	0.327	0.000	0.000	0.000	0.000
72	A	191	GLY	0	0.002	0.000	20.396	0.019	0.019	0.000	0.000	0.000	0.000
73	A	192	HIS	0	-0.070	-0.040	18.234	-0.038	-0.038	0.000	0.000	0.000	0.000
74	A	193	TYR	0	-0.020	-0.030	12.826	0.124	0.124	0.000	0.000	0.000	0.000
75	A	194	ASN	0	-0.054	-0.035	11.305	-0.056	-0.056	0.000	0.000	0.000	0.000
76	A	195	TRP	0	0.062	0.015	9.150	0.326	0.326	0.000	0.000	0.000	0.000
77	A	196	HIS	0	0.007	0.012	9.440	-0.223	-0.223	0.000	0.000	0.000	0.000
78	A	197	HIS	1	0.804	0.889	11.102	-1.106	-1.106	0.000	0.000	0.000	0.000
79	A	198	GLY	0	0.053	0.037	14.333	-0.205	-0.205	0.000	0.000	0.000	0.000
80	A	199	ALA	0	0.011	0.007	14.381	0.170	0.170	0.000	0.000	0.000	0.000
81	A	200	VAL	0	-0.009	-0.012	12.561	-0.065	-0.065	0.000	0.000	0.000	0.000
82	A	201	GLN	0	-0.037	0.015	16.055	0.050	0.050	0.000	0.000	0.000	0.000
83	A	202	TYR	0	-0.005	-0.014	16.622	-0.036	-0.036	0.000	0.000	0.000	0.000
84	A	203	SER	0	0.046	0.001	18.747	0.001	0.001	0.000	0.000	0.000	0.000
85	A	204	GLY	0	0.020	0.009	21.958	-0.034	-0.034	0.000	0.000	0.000	0.000
86	A	205	GLY	0	-0.048	-0.020	19.511	-0.043	-0.043	0.000	0.000	0.000	0.000
87	A	206	ARG	1	0.783	0.848	18.468	-0.037	-0.037	0.000	0.000	0.000	0.000
88	A	207	PHE	0	0.060	0.026	13.435	0.085	0.085	0.000	0.000	0.000	0.000
89	A	208	THR	0	0.035	0.017	16.687	-0.088	-0.088	0.000	0.000	0.000	0.000
90	A	209	ILE	0	-0.027	0.003	14.496	0.122	0.122	0.000	0.000	0.000	0.000
91	A	210	PRO	0	0.001	0.003	17.868	-0.077	-0.077	0.000	0.000	0.000	0.000
92	A	211	THR	0	0.023	-0.013	19.936	0.028	0.028	0.000	0.000	0.000	0.000
93	A	212	GLY	0	0.041	0.026	19.889	0.011	0.011	0.000	0.000	0.000	0.000
94	A	213	ALA	0	-0.036	-0.006	16.587	0.035	0.035	0.000	0.000	0.000	0.000
95	A	214	GLY	0	-0.045	-0.036	14.559	0.100	0.100	0.000	0.000	0.000	0.000
96	A	215	LYS	1	0.903	0.975	13.868	-0.274	-0.274	0.000	0.000	0.000	0.000
97	A	216	PRO	0	0.066	-0.002	14.234	-0.081	-0.081	0.000	0.000	0.000	0.000
98	A	217	GLY	0	0.023	0.012	11.053	0.140	0.140	0.000	0.000	0.000	0.000
99	A	218	ASP	-1	-0.822	-0.889	9.822	0.489	0.489	0.000	0.000	0.000	0.000
100	A	219	SER	0	0.008	0.001	7.780	0.258	0.258	0.000	0.000	0.000	0.000
101	A	220	GLY	0	0.008	-0.009	4.329	-0.542	-0.504	-0.002	-0.017	-0.019	0.000
102	A	221	ARG	1	0.831	0.929	3.217	-2.385	-1.379	0.061	-0.350	-0.718	-0.003
103	A	222	PRO	0	-0.003	0.001	3.057	-3.158	-1.627	1.055	-0.475	-2.111	0.001
104	A	223	ILE	0	0.012	0.011	5.098	-0.175	-0.127	-0.002	-0.015	-0.031	0.000
105	A	224	PHE	0	-0.003	-0.016	5.543	-0.013	0.141	-0.002	-0.007	-0.146	0.000
106	A	225	ASP	-1	-0.732	-0.858	9.098	1.044	1.044	0.000	0.000	0.000	0.000
107	A	226	ASN	0	0.042	0.001	11.590	0.221	0.221	0.000	0.000	0.000	0.000
108	A	227	LYS	1	0.817	0.910	12.812	-1.205	-1.205	0.000	0.000	0.000	0.000
109	A	228	GLY	0	0.014	0.013	8.767	-0.136	-0.136	0.000	0.000	0.000	0.000
110	A	229	ARG	1	0.737	0.859	7.460	-0.326	-0.326	0.000	0.000	0.000	0.000
111	A	230	VAL	0	-0.017	-0.018	3.518	-0.820	0.015	0.222	-0.191	-0.865	0.000
112	A	231	VAL	0	0.003	-0.002	6.834	-0.776	-0.776	0.000	0.000	0.000	0.000
113	A	232	ALA	0	-0.012	-0.019	8.099	-0.574	-0.574	0.000	0.000	0.000	0.000
114	A	233	ILE	0	-0.043	-0.019	3.017	0.184	0.838	0.047	-0.098	-0.603	0.000
115	A	234	VAL	0	0.028	0.022	6.477	-0.399	-0.399	0.000	0.000	0.000	0.000
116	A	235	LEU	0	-0.035	-0.009	8.169	-1.006	-1.006	0.000	0.000	0.000	0.000
117	A	236	GLY	0	0.033	-0.005	10.547	-0.087	-0.087	0.000	0.000	0.000	0.000
118	A	237	GLY	0	-0.009	0.006	13.917	0.117	0.117	0.000	0.000	0.000	0.000
119	A	238	ALA	0	0.045	0.055	16.774	-0.021	-0.021	0.000	0.000	0.000	0.000
120	A	239	ASN	0	-0.004	-0.013	20.519	0.098	0.098	0.000	0.000	0.000	0.000
121	A	240	GLU	-1	-0.745	-0.824	22.438	-0.041	-0.041	0.000	0.000	0.000	0.000
122	A	241	GLY	0	0.033	0.023	25.201	0.025	0.025	0.000	0.000	0.000	0.000
123	A	242	SER	0	0.004	-0.006	25.925	0.004	0.004	0.000	0.000	0.000	0.000
124	A	243	ARG	1	0.859	0.937	19.869	-0.299	-0.299	0.000	0.000	0.000	0.000
125	A	244	THR	0	0.028	0.013	17.789	-0.058	-0.058	0.000	0.000	0.000	0.000
126	A	245	ALA	0	-0.004	0.004	18.969	0.081	0.081	0.000	0.000	0.000	0.000
127	A	246	LEU	0	-0.047	-0.034	12.256	-0.068	-0.068	0.000	0.000	0.000	0.000
128	A	247	SER	0	0.025	0.023	14.519	0.023	0.023	0.000	0.000	0.000	0.000
129	A	248	VAL	0	-0.029	-0.034	10.717	-0.113	-0.113	0.000	0.000	0.000	0.000
130	A	249	VAL	0	0.047	0.048	7.371	0.023	0.023	0.000	0.000	0.000	0.000
131	A	250	THR	0	0.013	-0.002	9.034	0.346	0.346	0.000	0.000	0.000	0.000
132	A	251	TRP	0	0.047	0.024	5.485	-0.096	-0.096	0.000	0.000	0.000	0.000
133	A	252	ASN	0	-0.060	-0.036	12.427	0.130	0.130	0.000	0.000	0.000	0.000
134	A	253	LYS	1	0.979	0.976	16.195	-0.117	-0.117	0.000	0.000	0.000	0.000
135	A	254	ASP	-1	-0.903	-0.929	15.500	-0.219	-0.219	0.000	0.000	0.000	0.000
136	A	255	MET	0	0.025	0.021	14.925	-0.072	-0.072	0.000	0.000	0.000	0.000
137	A	256	VAL	0	-0.032	-0.024	9.906	0.065	0.065	0.000	0.000	0.000	0.000
138	A	257	THR	0	-0.036	-0.019	12.633	-0.049	-0.049	0.000	0.000	0.000	0.000
139	A	258	ARG	1	0.877	0.912	12.445	0.971	0.971	0.000	0.000	0.000	0.000
140	A	259	VAL	0	-0.009	0.009	14.023	0.066	0.066	0.000	0.000	0.000	0.000
141	A	260	THR	0	0.008	-0.014	15.197	-0.099	-0.099	0.000	0.000	0.000	0.000
142	A	261	PRO	0	-0.013	0.005	17.487	0.018	0.018	0.000	0.000	0.000	0.000
143	A	262	GLU	-1	-0.874	-0.912	20.577	-0.292	-0.292	0.000	0.000	0.000	0.000
144	A	263	GLY	0	0.049	0.015	23.459	0.035	0.035	0.000	0.000	0.000	0.000
145	A	264	SER	0	-0.100	-0.077	17.942	0.021	0.021	0.000	0.000	0.000	0.000
146	A	265	GLU	-1	-0.907	-0.930	18.003	-0.479	-0.479	0.000	0.000	0.000	0.000
147	A	266	GLU	-1	-0.982	-1.007	13.972	-1.441	-1.441	0.000	0.000	0.000	0.000
148	A	267	TRP	0	0.019	0.021	10.347	0.030	0.030	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:119:CYS)