FMO DATABASE

FMODB ID: G5771

Calculation Name: 4XA1-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4XA1

Chain ID: A

ChEMBL ID:

UniProt ID: Q15691

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	OptAll
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	153
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-925005.197553
FMO2-HF: Nuclear repulsion	862646.189819
FMO2-HF: Total energy	-62359.007734
FMO2-MP2: Total energy	-62541.836369

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:2:PRO)

Summations of interaction energy for fragment #1(A:2:PRO)

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.
-6.127	-1.661	1.546	-2.408	-3.603	-0.018

Interaction energy analysis for fragmet #1(A:2:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.063 / q_NPA : -0.031

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	4	LYS	1	0.793	0.889	3.371	-2.053	0.241	0.045	-1.118	-1.221	-0.002
4	A	5	PRO	0	-0.011	-0.024	5.290	-0.339	-0.306	-0.001	-0.002	-0.029	0.000
5	A	6	GLU	-1	-0.785	-0.896	7.894	0.024	0.024	0.000	0.000	0.000	0.000
6	A	7	GLU	-1	-0.843	-0.907	6.447	0.222	0.222	0.000	0.000	0.000	0.000
7	A	8	HIS	0	-0.006	0.001	7.353	-0.225	-0.225	0.000	0.000	0.000	0.000
8	A	9	GLU	-1	-0.869	-0.944	9.064	-0.227	-0.227	0.000	0.000	0.000	0.000
9	A	10	ASP	-1	-0.910	-0.937	12.730	-0.076	-0.076	0.000	0.000	0.000	0.000
10	A	11	ILE	0	-0.040	-0.021	9.385	0.041	0.041	0.000	0.000	0.000	0.000
11	A	12	LEU	0	-0.005	-0.011	11.460	0.022	0.022	0.000	0.000	0.000	0.000
12	A	13	ASN	0	-0.071	-0.048	14.445	0.058	0.058	0.000	0.000	0.000	0.000
13	A	14	LYS	1	0.782	0.871	15.667	0.171	0.171	0.000	0.000	0.000	0.000
14	A	15	LEU	0	-0.060	-0.034	13.881	0.020	0.020	0.000	0.000	0.000	0.000
15	A	16	LEU	0	-0.017	0.009	17.720	0.012	0.012	0.000	0.000	0.000	0.000
16	A	17	ASP	-1	-0.833	-0.903	20.473	-0.087	-0.087	0.000	0.000	0.000	0.000
17	A	18	PRO	0	-0.042	-0.015	22.560	-0.010	-0.010	0.000	0.000	0.000	0.000
18	A	19	GLU	-1	-0.958	-0.985	24.760	-0.069	-0.069	0.000	0.000	0.000	0.000
19	A	20	LEU	0	-0.029	0.009	18.322	0.006	0.006	0.000	0.000	0.000	0.000
20	A	21	ALA	0	0.039	0.009	22.975	-0.007	-0.007	0.000	0.000	0.000	0.000
21	A	22	GLN	0	0.069	0.016	21.548	-0.019	-0.019	0.000	0.000	0.000	0.000
22	A	23	SER	0	-0.052	-0.027	20.922	-0.011	-0.011	0.000	0.000	0.000	0.000
23	A	24	GLU	-1	-0.759	-0.838	16.742	-0.145	-0.145	0.000	0.000	0.000	0.000
24	A	25	ARG	1	0.849	0.914	16.708	0.135	0.135	0.000	0.000	0.000	0.000
25	A	26	THR	0	-0.046	-0.051	16.443	-0.036	-0.036	0.000	0.000	0.000	0.000
26	A	27	GLU	-1	-0.940	-0.960	14.504	-0.176	-0.176	0.000	0.000	0.000	0.000
27	A	28	ALA	0	0.018	0.010	12.449	-0.074	-0.074	0.000	0.000	0.000	0.000
28	A	29	LEU	0	0.017	-0.003	11.495	-0.095	-0.095	0.000	0.000	0.000	0.000
29	A	30	GLN	0	-0.013	0.003	11.757	-0.089	-0.089	0.000	0.000	0.000	0.000
30	A	31	GLN	0	0.016	-0.009	7.360	-0.135	-0.135	0.000	0.000	0.000	0.000
31	A	32	LEU	0	0.059	0.040	6.762	-0.303	-0.303	0.000	0.000	0.000	0.000
32	A	33	ARG	1	0.878	0.943	7.568	0.271	0.271	0.000	0.000	0.000	0.000
33	A	34	VAL	0	-0.015	-0.013	6.408	0.001	0.001	0.000	0.000	0.000	0.000
34	A	35	ASN	0	0.033	0.036	2.454	-2.864	-1.626	1.415	-0.975	-1.678	-0.013
35	A	36	TYR	0	0.039	0.022	4.297	-0.084	0.059	-0.001	-0.003	-0.139	0.000
36	A	37	GLY	0	0.009	0.003	7.103	0.117	0.117	0.000	0.000	0.000	0.000
37	A	38	SER	0	-0.034	-0.028	3.205	-0.880	-0.122	0.088	-0.310	-0.536	-0.003
38	A	39	PHE	0	0.031	0.021	5.379	0.133	0.133	0.000	0.000	0.000	0.000
39	A	40	VAL	0	0.007	-0.004	6.130	0.182	0.182	0.000	0.000	0.000	0.000
40	A	41	SER	0	-0.053	-0.029	7.784	0.110	0.110	0.000	0.000	0.000	0.000
41	A	42	GLU	-1	-0.825	-0.909	5.421	-0.334	-0.334	0.000	0.000	0.000	0.000
42	A	43	TYR	0	-0.050	-0.018	8.320	0.115	0.115	0.000	0.000	0.000	0.000
43	A	44	ASN	0	-0.013	-0.019	10.601	0.097	0.097	0.000	0.000	0.000	0.000
44	A	45	ASP	-1	-0.735	-0.839	12.087	-0.130	-0.130	0.000	0.000	0.000	0.000
45	A	46	LEU	0	0.003	0.005	13.712	0.010	0.010	0.000	0.000	0.000	0.000
46	A	47	THR	0	-0.043	-0.027	15.623	0.021	0.021	0.000	0.000	0.000	0.000
47	A	48	LYS	1	0.827	0.893	9.039	0.304	0.304	0.000	0.000	0.000	0.000
48	A	49	SER	0	-0.022	-0.027	14.690	-0.003	-0.003	0.000	0.000	0.000	0.000
49	A	1173	LYS	1	0.758	0.863	16.714	0.081	0.081	0.000	0.000	0.000	0.000
50	A	1174	MET	0	0.009	0.003	15.656	0.011	0.011	0.000	0.000	0.000	0.000
51	A	1175	ARG	1	0.870	0.939	13.550	0.260	0.260	0.000	0.000	0.000	0.000
52	A	1176	ARG	1	0.952	0.979	18.189	0.135	0.135	0.000	0.000	0.000	0.000
53	A	1177	ASP	-1	-0.823	-0.891	21.676	-0.068	-0.068	0.000	0.000	0.000	0.000
54	A	1178	LEU	0	-0.006	-0.002	19.752	0.008	0.008	0.000	0.000	0.000	0.000
55	A	1179	GLU	-1	-0.900	-0.930	22.276	-0.106	-0.106	0.000	0.000	0.000	0.000
56	A	1180	GLU	-1	-0.918	-0.968	23.988	-0.066	-0.066	0.000	0.000	0.000	0.000
57	A	1181	ALA	0	-0.012	-0.007	26.275	0.007	0.007	0.000	0.000	0.000	0.000
58	A	1182	THR	0	-0.038	-0.022	25.381	0.008	0.008	0.000	0.000	0.000	0.000
59	A	1183	LEU	0	0.058	0.027	27.340	0.005	0.005	0.000	0.000	0.000	0.000
60	A	1184	GLN	0	-0.023	-0.016	30.246	0.005	0.005	0.000	0.000	0.000	0.000
61	A	1185	HIS	0	-0.016	0.014	30.830	0.006	0.006	0.000	0.000	0.000	0.000
62	A	1186	GLU	-1	-0.927	-0.969	30.440	-0.055	-0.055	0.000	0.000	0.000	0.000
63	A	1187	ALA	0	0.001	0.001	33.779	0.003	0.003	0.000	0.000	0.000	0.000
64	A	1188	THR	0	-0.038	-0.032	35.874	0.004	0.004	0.000	0.000	0.000	0.000
65	A	1189	ALA	0	-0.023	-0.017	36.180	0.003	0.003	0.000	0.000	0.000	0.000
66	A	1190	ALA	0	-0.003	0.004	38.024	0.002	0.002	0.000	0.000	0.000	0.000
67	A	1191	ALA	0	0.013	0.007	39.864	0.002	0.002	0.000	0.000	0.000	0.000
68	A	1192	LEU	0	-0.022	-0.020	40.558	0.002	0.002	0.000	0.000	0.000	0.000
69	A	1193	ARG	1	0.904	0.955	38.619	0.029	0.029	0.000	0.000	0.000	0.000
70	A	1194	LYS	1	0.836	0.910	43.921	0.026	0.026	0.000	0.000	0.000	0.000
71	A	1195	LYS	1	1.010	1.007	46.025	0.019	0.019	0.000	0.000	0.000	0.000
72	A	1196	HIS	0	-0.005	0.011	46.919	0.001	0.001	0.000	0.000	0.000	0.000
73	A	1197	ALA	0	0.013	0.000	48.068	0.001	0.001	0.000	0.000	0.000	0.000
74	A	1198	ASP	-1	-0.808	-0.890	49.841	-0.023	-0.023	0.000	0.000	0.000	0.000
75	A	1199	SER	0	-0.017	-0.025	51.305	0.001	0.001	0.000	0.000	0.000	0.000
76	A	1200	VAL	0	-0.040	-0.023	51.519	0.001	0.001	0.000	0.000	0.000	0.000
77	A	1201	ALA	0	-0.020	-0.001	54.122	0.001	0.001	0.000	0.000	0.000	0.000
78	A	1202	GLU	-1	-0.877	-0.928	56.051	-0.013	-0.013	0.000	0.000	0.000	0.000
79	A	1203	LEU	0	0.004	-0.002	55.620	0.001	0.001	0.000	0.000	0.000	0.000
80	A	1204	GLY	0	0.007	0.012	58.152	0.001	0.001	0.000	0.000	0.000	0.000
81	A	1205	GLU	-1	-0.900	-0.954	59.648	-0.014	-0.014	0.000	0.000	0.000	0.000
82	A	1206	GLN	0	-0.076	-0.041	60.344	0.001	0.001	0.000	0.000	0.000	0.000
83	A	1207	ILE	0	0.008	0.003	60.128	0.001	0.001	0.000	0.000	0.000	0.000
84	A	1208	ASP	-1	-0.890	-0.943	63.040	-0.011	-0.011	0.000	0.000	0.000	0.000
85	A	1209	ASN	0	-0.067	-0.049	65.606	0.001	0.001	0.000	0.000	0.000	0.000
86	A	1210	LEU	0	0.001	-0.003	66.397	0.001	0.001	0.000	0.000	0.000	0.000
87	A	1211	GLN	0	-0.058	-0.021	64.881	0.001	0.001	0.000	0.000	0.000	0.000
88	A	1212	ARG	1	0.870	0.927	69.658	0.010	0.010	0.000	0.000	0.000	0.000
89	A	1213	VAL	0	0.004	-0.002	71.770	0.000	0.000	0.000	0.000	0.000	0.000
90	A	1214	LYS	1	0.820	0.897	71.762	0.006	0.006	0.000	0.000	0.000	0.000
91	A	1215	GLN	0	0.050	0.021	71.830	0.000	0.000	0.000	0.000	0.000	0.000
92	A	1216	LYS	1	0.812	0.896	75.630	0.008	0.008	0.000	0.000	0.000	0.000
93	A	1217	LEU	0	0.030	0.010	76.210	0.000	0.000	0.000	0.000	0.000	0.000
94	A	1218	GLU	-1	-0.845	-0.907	75.752	-0.006	-0.006	0.000	0.000	0.000	0.000
95	A	1219	LYS	1	0.802	0.896	79.631	0.007	0.007	0.000	0.000	0.000	0.000
96	A	1220	GLU	-1	-0.785	-0.866	81.670	-0.007	-0.007	0.000	0.000	0.000	0.000
97	A	1221	LYS	1	0.929	0.964	80.625	0.005	0.005	0.000	0.000	0.000	0.000
98	A	1222	SER	0	-0.072	-0.054	83.091	0.000	0.000	0.000	0.000	0.000	0.000
99	A	1223	GLU	-1	-0.763	-0.862	85.209	-0.006	-0.006	0.000	0.000	0.000	0.000
100	A	1224	PHE	0	0.043	0.024	86.382	0.000	0.000	0.000	0.000	0.000	0.000
101	A	1225	LYS	1	0.768	0.869	87.454	0.004	0.004	0.000	0.000	0.000	0.000
102	A	1226	LEU	0	-0.039	-0.017	88.125	0.000	0.000	0.000	0.000	0.000	0.000
103	A	1227	GLU	-1	-0.888	-0.947	91.463	-0.005	-0.005	0.000	0.000	0.000	0.000
104	A	1228	LEU	0	-0.015	-0.005	91.606	0.000	0.000	0.000	0.000	0.000	0.000
105	A	1229	ASP	-1	-0.813	-0.876	92.702	-0.003	-0.003	0.000	0.000	0.000	0.000
106	A	1230	ASP	-1	-0.947	-0.956	95.769	-0.004	-0.004	0.000	0.000	0.000	0.000
107	A	1231	VAL	0	0.026	0.002	97.766	0.000	0.000	0.000	0.000	0.000	0.000
108	A	1232	THR	0	-0.049	-0.036	97.818	0.000	0.000	0.000	0.000	0.000	0.000
109	A	1233	SER	0	-0.016	-0.018	99.600	0.000	0.000	0.000	0.000	0.000	0.000
110	A	1234	ASN	0	-0.021	-0.010	101.865	0.000	0.000	0.000	0.000	0.000	0.000
111	A	1235	MET	0	-0.029	-0.017	102.803	0.000	0.000	0.000	0.000	0.000	0.000
112	A	1236	GLU	-1	-0.900	-0.951	102.846	-0.002	-0.002	0.000	0.000	0.000	0.000
113	A	1237	GLN	0	-0.070	-0.041	106.345	0.000	0.000	0.000	0.000	0.000	0.000
114	A	1238	ILE	0	0.014	0.002	106.850	0.000	0.000	0.000	0.000	0.000	0.000
115	A	211	GLU	-1	-0.859	-0.908	107.370	-0.002	-0.002	0.000	0.000	0.000	0.000
116	A	212	LYS	1	0.954	0.971	110.603	0.002	0.002	0.000	0.000	0.000	0.000
117	A	213	GLU	-1	-0.865	-0.892	112.484	-0.003	-0.003	0.000	0.000	0.000	0.000
118	A	214	ARG	1	0.752	0.832	110.495	0.002	0.002	0.000	0.000	0.000	0.000
119	A	215	ASP	-1	-0.805	-0.874	113.835	-0.002	-0.002	0.000	0.000	0.000	0.000
120	A	216	PHE	0	-0.001	-0.006	116.591	0.000	0.000	0.000	0.000	0.000	0.000
121	A	217	TYR	0	-0.096	-0.093	116.138	0.000	0.000	0.000	0.000	0.000	0.000
122	A	218	PHE	0	0.044	0.017	119.120	0.000	0.000	0.000	0.000	0.000	0.000
123	A	219	GLY	0	0.029	0.015	120.615	0.000	0.000	0.000	0.000	0.000	0.000
124	A	220	LYS	1	0.791	0.919	121.030	0.002	0.002	0.000	0.000	0.000	0.000
125	A	221	LEU	0	0.018	0.017	122.449	0.000	0.000	0.000	0.000	0.000	0.000
126	A	222	ARG	1	0.872	0.920	124.666	0.002	0.002	0.000	0.000	0.000	0.000
127	A	223	ASN	0	-0.016	-0.018	125.897	0.000	0.000	0.000	0.000	0.000	0.000
128	A	224	ILE	0	-0.004	-0.003	127.896	0.000	0.000	0.000	0.000	0.000	0.000
129	A	225	GLU	-1	-0.750	-0.841	128.095	-0.002	-0.002	0.000	0.000	0.000	0.000
130	A	226	LEU	0	-0.041	-0.016	129.099	0.000	0.000	0.000	0.000	0.000	0.000
131	A	227	ILE	0	0.029	0.020	132.313	0.000	0.000	0.000	0.000	0.000	0.000
132	A	228	CYS	0	-0.060	-0.031	133.613	0.000	0.000	0.000	0.000	0.000	0.000
133	A	229	GLN	0	0.023	0.016	131.039	0.000	0.000	0.000	0.000	0.000	0.000
134	A	230	GLU	-1	-1.004	-0.995	136.163	-0.001	-0.001	0.000	0.000	0.000	0.000
135	A	231	ASN	0	-0.081	-0.054	138.459	0.000	0.000	0.000	0.000	0.000	0.000
136	A	232	GLU	-1	-0.949	-0.965	136.999	-0.002	-0.002	0.000	0.000	0.000	0.000
137	A	233	GLY	0	-0.011	0.009	140.910	0.000	0.000	0.000	0.000	0.000	0.000
138	A	234	GLU	-1	-0.944	-0.988	144.059	-0.001	-0.001	0.000	0.000	0.000	0.000
139	A	235	ASN	0	-0.120	-0.059	142.533	0.000	0.000	0.000	0.000	0.000	0.000
140	A	236	ASP	-1	-0.768	-0.875	141.351	-0.002	-0.002	0.000	0.000	0.000	0.000
141	A	237	PRO	0	-0.007	-0.007	141.399	0.000	0.000	0.000	0.000	0.000	0.000
142	A	238	VAL	0	-0.092	-0.058	137.949	0.000	0.000	0.000	0.000	0.000	0.000
143	A	239	LEU	0	0.055	0.006	137.299	0.000	0.000	0.000	0.000	0.000	0.000
144	A	240	GLN	0	-0.064	-0.022	136.508	0.000	0.000	0.000	0.000	0.000	0.000
145	A	241	ARG	1	0.949	0.971	135.115	0.002	0.002	0.000	0.000	0.000	0.000
146	A	242	ILE	0	-0.027	-0.007	131.917	0.000	0.000	0.000	0.000	0.000	0.000
147	A	243	VAL	0	0.033	0.016	131.720	0.000	0.000	0.000	0.000	0.000	0.000
148	A	244	ASP	-1	-0.875	-0.936	131.645	-0.002	-0.002	0.000	0.000	0.000	0.000
149	A	245	ILE	0	-0.092	-0.050	127.892	0.000	0.000	0.000	0.000	0.000	0.000
150	A	246	LEU	0	-0.051	-0.021	127.323	0.000	0.000	0.000	0.000	0.000	0.000
151	A	247	TYR	0	-0.101	-0.067	126.884	0.000	0.000	0.000	0.000	0.000	0.000
152	A	248	ALA	0	0.019	0.032	126.234	0.000	0.000	0.000	0.000	0.000	0.000
153	A	249	THR	0	-0.079	-0.042	121.480	0.000	0.000	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:PRO)