FMO DATABASE

FMODB ID: 3JRGL

Calculation Name: 3QC7-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3QC7

Chain ID: A

ChEMBL ID:

UniProt ID: B3VMP4

Base Structure: X-ray

Registration Date: 2023-09-23

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	164
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-945888.589157
FMO2-HF: Nuclear repulsion	886936.66848
FMO2-HF: Total energy	-58951.920677
FMO2-MP2: Total energy	-59126.729747

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:118:ILE)

Summations of interaction energy for fragment #1(A:118:ILE)

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.
-3.695	-0.299	0.566	-1.501	-2.461	0

Interaction energy analysis for fragmet #1(A:118:ILE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.011 / q_NPA : 0.006

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].
3	A	120	ILE	0	-0.017	0.011	2.724	-2.476	0.851	0.567	-1.490	-2.404
4	A	121	GLU	-1	-0.937	-0.969	4.704	-0.730	-0.661	-0.001	-0.011	-0.057
5	A	122	VAL	0	0.015	-0.012	8.434	0.037	0.037	0.000	0.000	0.000
6	A	123	GLU	-1	-0.805	-0.905	11.217	-0.467	-0.467	0.000	0.000	0.000
7	A	124	ASP	-1	-0.842	-0.914	6.126	-1.150	-1.150	0.000	0.000	0.000
8	A	125	ILE	0	-0.069	-0.034	8.756	0.045	0.045	0.000	0.000	0.000
9	A	126	LYS	1	0.862	0.913	10.193	0.605	0.605	0.000	0.000	0.000
10	A	127	ASP	-1	-0.918	-0.939	12.677	-0.387	-0.387	0.000	0.000	0.000
11	A	128	ALA	0	-0.018	0.003	14.135	0.020	0.020	0.000	0.000	0.000
12	A	129	GLY	0	0.026	0.008	15.787	0.030	0.030	0.000	0.000	0.000
13	A	130	ASP	-1	-0.879	-0.943	18.753	-0.303	-0.303	0.000	0.000	0.000
14	A	131	THR	0	-0.004	-0.025	20.630	-0.019	-0.019	0.000	0.000	0.000
15	A	132	GLY	0	0.010	0.009	18.982	-0.011	-0.011	0.000	0.000	0.000
16	A	133	LYS	1	0.970	0.989	14.163	0.412	0.412	0.000	0.000	0.000
17	A	134	ARG	1	0.942	0.971	17.144	0.238	0.238	0.000	0.000	0.000
18	A	135	LEU	0	0.002	-0.010	20.085	-0.003	-0.003	0.000	0.000	0.000
19	A	136	LEU	0	-0.035	-0.006	12.205	-0.005	-0.005	0.000	0.000	0.000
20	A	137	LYS	1	0.853	0.915	14.916	0.471	0.471	0.000	0.000	0.000
21	A	138	ILE	0	-0.090	-0.009	17.332	0.029	0.029	0.000	0.000	0.000
22	A	139	ASN	0	0.050	0.018	19.761	-0.047	-0.047	0.000	0.000	0.000
23	A	140	THR	0	0.004	0.001	21.381	0.014	0.014	0.000	0.000	0.000
24	A	141	PRO	0	0.068	0.012	24.681	-0.002	-0.002	0.000	0.000	0.000
25	A	142	SER	0	-0.011	0.001	26.767	0.006	0.006	0.000	0.000	0.000
26	A	143	GLY	0	0.038	0.018	25.730	0.008	0.008	0.000	0.000	0.000
27	A	144	ALA	0	0.035	0.008	24.140	0.000	0.000	0.000	0.000	0.000
28	A	145	ARG	1	0.891	0.932	25.624	0.186	0.186	0.000	0.000	0.000
29	A	146	ASN	0	-0.046	-0.027	28.270	0.022	0.022	0.000	0.000	0.000
30	A	147	ILE	0	-0.070	-0.016	23.011	0.004	0.004	0.000	0.000	0.000
31	A	148	ILE	0	-0.013	-0.010	25.181	0.006	0.006	0.000	0.000	0.000
32	A	149	ILE	0	-0.042	-0.008	28.639	0.010	0.010	0.000	0.000	0.000
33	A	150	GLU	-1	-0.895	-0.943	31.698	-0.158	-0.158	0.000	0.000	0.000
34	A	151	ASN	0	-0.026	-0.007	33.942	0.007	0.007	0.000	0.000	0.000
35	A	152	GLU	-1	-0.826	-0.936	35.807	-0.141	-0.141	0.000	0.000	0.000
36	A	153	ASP	-1	-0.824	-0.908	38.567	-0.098	-0.098	0.000	0.000	0.000
37	A	154	ALA	0	0.015	-0.004	37.786	0.001	0.001	0.000	0.000	0.000
38	A	155	LYS	1	0.901	0.957	33.029	0.156	0.156	0.000	0.000	0.000
39	A	156	ALA	0	0.000	0.002	36.431	-0.003	-0.003	0.000	0.000	0.000
40	A	157	LEU	0	-0.020	-0.011	39.244	0.001	0.001	0.000	0.000	0.000
41	A	158	ILE	0	-0.030	-0.016	33.666	-0.001	-0.001	0.000	0.000	0.000
42	A	159	ASN	0	-0.020	-0.006	34.108	-0.013	-0.013	0.000	0.000	0.000
43	A	160	GLY	0	-0.023	0.000	36.595	0.001	0.001	0.000	0.000	0.000
44	A	161	GLU	-1	-0.974	-0.977	39.606	-0.100	-0.100	0.000	0.000	0.000
45	A	162	THR	0	0.005	0.016	41.394	0.001	0.001	0.000	0.000	0.000
46	A	163	THR	0	0.032	0.011	43.986	0.006	0.006	0.000	0.000	0.000
47	A	164	ASN	0	0.037	-0.010	46.669	-0.001	-0.001	0.000	0.000	0.000
48	A	165	THR	0	0.019	0.009	46.881	0.002	0.002	0.000	0.000	0.000
49	A	166	ASN	0	0.034	0.018	42.425	0.000	0.000	0.000	0.000	0.000
50	A	167	LYS	1	0.911	0.959	45.614	0.082	0.082	0.000	0.000	0.000
51	A	168	LYS	1	0.946	0.979	47.962	0.067	0.067	0.000	0.000	0.000
52	A	169	ASN	0	0.003	-0.001	45.217	0.005	0.005	0.000	0.000	0.000
53	A	170	LEU	0	-0.027	-0.024	42.177	0.000	0.000	0.000	0.000	0.000
54	A	171	GLN	0	0.015	0.012	46.146	0.003	0.003	0.000	0.000	0.000
55	A	172	ASP	-1	-0.910	-0.960	48.797	-0.068	-0.068	0.000	0.000	0.000
56	A	173	LEU	0	-0.081	-0.034	42.865	0.000	0.000	0.000	0.000	0.000
57	A	174	LEU	0	-0.044	-0.011	45.232	0.000	0.000	0.000	0.000	0.000
58	A	175	PHE	0	-0.025	-0.003	48.396	0.002	0.002	0.000	0.000	0.000
59	A	176	SER	0	0.012	-0.004	52.099	0.000	0.000	0.000	0.000	0.000
60	A	177	ASP	-1	-0.813	-0.902	54.036	-0.049	-0.049	0.000	0.000	0.000
61	A	178	GLY	0	0.022	-0.004	57.297	-0.001	-0.001	0.000	0.000	0.000
62	A	179	ASN	0	0.042	0.019	58.625	0.000	0.000	0.000	0.000	0.000
63	A	180	VAL	0	0.006	-0.001	56.479	0.000	0.000	0.000	0.000	0.000
64	A	181	LYS	1	0.905	0.958	52.927	0.063	0.063	0.000	0.000	0.000
65	A	182	ALA	0	-0.012	0.007	56.611	-0.001	-0.001	0.000	0.000	0.000
66	A	183	PHE	0	-0.009	-0.016	58.973	0.000	0.000	0.000	0.000	0.000
67	A	184	LEU	0	-0.037	-0.011	53.679	0.000	0.000	0.000	0.000	0.000
68	A	185	GLN	0	-0.069	-0.040	52.966	-0.001	-0.001	0.000	0.000	0.000
69	A	186	ALA	0	-0.028	-0.001	56.854	0.001	0.001	0.000	0.000	0.000
70	A	187	THR	0	-0.049	-0.024	60.034	0.002	0.002	0.000	0.000	0.000
71	A	188	THR	0	-0.018	0.005	61.725	0.000	0.000	0.000	0.000	0.000
72	A	189	THR	0	0.034	0.005	64.293	0.001	0.001	0.000	0.000	0.000
73	A	190	ASP	-1	-0.850	-0.935	66.866	-0.037	-0.037	0.000	0.000	0.000
74	A	191	GLU	-1	-0.921	-0.966	67.277	-0.039	-0.039	0.000	0.000	0.000
75	A	192	ASN	0	-0.023	-0.011	62.730	-0.001	-0.001	0.000	0.000	0.000
76	A	193	LYS	1	0.885	0.932	65.771	0.041	0.041	0.000	0.000	0.000
77	A	194	THR	0	0.032	0.027	68.179	0.001	0.001	0.000	0.000	0.000
78	A	195	ALA	0	-0.005	0.001	65.655	0.000	0.000	0.000	0.000	0.000
79	A	196	LEU	0	-0.035	-0.030	62.134	0.000	0.000	0.000	0.000	0.000
80	A	197	GLN	0	0.005	-0.005	66.128	0.001	0.001	0.000	0.000	0.000
81	A	198	GLN	0	-0.013	-0.014	68.874	0.001	0.001	0.000	0.000	0.000
82	A	199	LEU	0	-0.044	-0.005	62.453	0.000	0.000	0.000	0.000	0.000
83	A	200	LEU	0	-0.064	-0.022	65.014	0.000	0.000	0.000	0.000	0.000
84	A	201	VAL	0	-0.021	-0.003	68.195	0.001	0.001	0.000	0.000	0.000
85	A	202	SER	0	0.030	0.006	71.853	0.000	0.000	0.000	0.000	0.000
86	A	203	ASN	0	0.021	0.015	73.455	0.001	0.001	0.000	0.000	0.000
87	A	204	ALA	0	0.089	0.030	77.050	0.000	0.000	0.000	0.000	0.000
88	A	205	ASP	-1	-0.812	-0.910	78.295	-0.027	-0.027	0.000	0.000	0.000
89	A	206	VAL	0	-0.015	-0.014	76.344	0.000	0.000	0.000	0.000	0.000
90	A	207	LEU	0	-0.006	0.003	72.557	0.000	0.000	0.000	0.000	0.000
91	A	208	GLY	0	0.041	0.031	76.278	0.000	0.000	0.000	0.000	0.000
92	A	209	LEU	0	-0.052	-0.029	79.333	0.000	0.000	0.000	0.000	0.000
93	A	210	LEU	0	-0.042	-0.021	72.922	0.000	0.000	0.000	0.000	0.000
94	A	211	SER	0	-0.011	0.000	75.552	0.000	0.000	0.000	0.000	0.000
95	A	212	GLY	0	-0.016	-0.003	76.570	0.000	0.000	0.000	0.000	0.000
96	A	213	ASN	0	-0.088	-0.048	79.445	0.001	0.001	0.000	0.000	0.000
97	A	214	PRO	0	-0.015	0.011	81.448	0.000	0.000	0.000	0.000	0.000
98	A	215	THR	0	0.058	0.024	82.338	0.001	0.001	0.000	0.000	0.000
99	A	216	SER	0	-0.010	-0.036	84.872	0.000	0.000	0.000	0.000	0.000
100	A	217	ASP	-1	-0.860	-0.925	86.131	-0.023	-0.023	0.000	0.000	0.000
101	A	218	ASN	0	0.020	0.005	81.556	0.000	0.000	0.000	0.000	0.000
102	A	219	LYS	1	0.926	0.967	84.790	0.024	0.024	0.000	0.000	0.000
103	A	220	ILE	0	-0.028	-0.013	87.303	0.000	0.000	0.000	0.000	0.000
104	A	221	ASN	0	0.020	0.001	84.908	0.001	0.001	0.000	0.000	0.000
105	A	222	LEU	0	-0.013	0.003	81.644	0.000	0.000	0.000	0.000	0.000
106	A	223	ARG	1	0.890	0.951	85.695	0.022	0.022	0.000	0.000	0.000
107	A	224	THR	0	0.003	0.002	88.725	0.000	0.000	0.000	0.000	0.000
108	A	225	MET	0	-0.069	-0.023	81.476	0.000	0.000	0.000	0.000	0.000
109	A	226	ILE	0	-0.048	-0.024	84.798	0.000	0.000	0.000	0.000	0.000
110	A	227	GLY	0	0.017	0.026	87.413	0.000	0.000	0.000	0.000	0.000
111	A	228	ALA	0	-0.045	-0.011	90.379	0.000	0.000	0.000	0.000	0.000
112	A	229	GLY	0	0.023	0.006	92.070	0.000	0.000	0.000	0.000	0.000
113	A	230	VAL	0	-0.065	-0.043	94.230	0.000	0.000	0.000	0.000	0.000
114	A	231	PRO	0	0.012	-0.008	95.017	0.000	0.000	0.000	0.000	0.000
115	A	232	TYR	0	0.027	0.022	97.969	0.000	0.000	0.000	0.000	0.000
116	A	233	SER	0	-0.007	-0.005	101.480	0.000	0.000	0.000	0.000	0.000
117	A	234	LEU	0	0.000	-0.008	104.503	0.000	0.000	0.000	0.000	0.000
118	A	235	PRO	0	-0.002	0.027	107.696	0.000	0.000	0.000	0.000	0.000
119	A	236	ALA	0	0.018	-0.007	110.189	0.000	0.000	0.000	0.000	0.000
120	A	237	ALA	0	0.006	0.010	113.976	0.000	0.000	0.000	0.000	0.000
121	A	238	THR	0	0.012	0.008	114.981	0.000	0.000	0.000	0.000	0.000
122	A	239	THR	0	-0.014	-0.021	117.482	0.000	0.000	0.000	0.000	0.000
123	A	240	THR	0	-0.016	-0.002	115.666	0.000	0.000	0.000	0.000	0.000
124	A	241	THR	0	-0.040	-0.009	111.123	0.000	0.000	0.000	0.000	0.000
125	A	242	LEU	0	0.024	0.011	111.755	0.000	0.000	0.000	0.000	0.000
126	A	243	GLY	0	0.034	0.007	112.129	0.000	0.000	0.000	0.000	0.000
127	A	244	GLY	0	-0.029	-0.003	112.777	0.000	0.000	0.000	0.000	0.000
128	A	245	VAL	0	0.012	0.007	113.909	0.000	0.000	0.000	0.000	0.000
129	A	246	LYS	1	0.956	0.978	115.431	0.014	0.014	0.000	0.000	0.000
130	A	247	LYS	1	0.984	0.982	118.343	0.013	0.013	0.000	0.000	0.000
131	A	248	GLY	0	0.039	0.016	120.622	0.000	0.000	0.000	0.000	0.000
132	A	249	ALA	0	-0.016	-0.010	124.304	0.000	0.000	0.000	0.000	0.000
133	A	250	ALA	0	0.008	-0.002	126.334	0.000	0.000	0.000	0.000	0.000
134	A	251	VAL	0	0.003	-0.002	128.682	0.000	0.000	0.000	0.000	0.000
135	A	252	THR	0	-0.028	-0.009	131.861	0.000	0.000	0.000	0.000	0.000
136	A	253	ALA	0	0.012	0.010	134.858	0.000	0.000	0.000	0.000	0.000
137	A	254	SER	0	-0.036	-0.045	136.559	0.000	0.000	0.000	0.000	0.000
138	A	255	THR	0	-0.016	-0.014	139.919	0.000	0.000	0.000	0.000	0.000
139	A	256	ALA	0	-0.016	0.004	143.296	0.000	0.000	0.000	0.000	0.000
140	A	257	THR	0	0.038	0.015	145.271	0.000	0.000	0.000	0.000	0.000
141	A	258	ASP	-1	-0.866	-0.896	148.338	-0.009	-0.009	0.000	0.000	0.000
142	A	259	VAL	0	0.044	0.002	147.043	0.000	0.000	0.000	0.000	0.000
143	A	260	ALA	0	0.013	0.005	146.086	0.000	0.000	0.000	0.000	0.000
144	A	261	THR	0	-0.034	-0.046	143.851	0.000	0.000	0.000	0.000	0.000
145	A	262	ALA	0	0.050	0.026	142.849	0.000	0.000	0.000	0.000	0.000
146	A	263	VAL	0	-0.027	-0.008	141.382	0.000	0.000	0.000	0.000	0.000
147	A	264	LYS	1	0.948	0.983	140.502	0.009	0.009	0.000	0.000	0.000
148	A	265	ASP	-1	-0.798	-0.892	138.536	-0.010	-0.010	0.000	0.000	0.000
149	A	266	LEU	0	-0.013	-0.003	135.905	0.000	0.000	0.000	0.000	0.000
150	A	267	ASN	0	0.015	-0.018	135.704	0.000	0.000	0.000	0.000	0.000
151	A	268	SER	0	-0.030	-0.006	134.883	0.000	0.000	0.000	0.000	0.000
152	A	269	LEU	0	0.015	0.016	130.217	0.000	0.000	0.000	0.000	0.000
153	A	270	ILE	0	0.002	0.002	130.820	0.000	0.000	0.000	0.000	0.000
154	A	271	THR	0	-0.041	-0.022	130.323	0.000	0.000	0.000	0.000	0.000
155	A	272	VAL	0	0.008	0.020	127.218	0.000	0.000	0.000	0.000	0.000
156	A	273	LEU	0	0.004	-0.011	126.254	0.000	0.000	0.000	0.000	0.000
157	A	274	LYS	1	0.927	0.968	125.447	0.011	0.011	0.000	0.000	0.000
158	A	275	ASN	0	-0.017	-0.012	125.234	0.000	0.000	0.000	0.000	0.000
159	A	276	ALA	0	-0.077	-0.026	122.040	0.000	0.000	0.000	0.000	0.000
160	A	277	GLY	0	-0.002	-0.003	120.927	0.000	0.000	0.000	0.000	0.000
161	A	278	ILE	0	-0.055	-0.015	121.092	0.000	0.000	0.000	0.000	0.000
162	A	279	ILE	0	-0.022	-0.007	122.959	0.000	0.000	0.000	0.000	0.000
163	A	280	SER	0	-0.001	-0.011	124.005	0.000	0.000	0.000	0.000	0.000
164	A	281	LEU	0	0.008	0.013	125.755	0.000	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

Interactive mode: IFIE and PIEDA for fragment #1(A:118:ILE)