FMO DATABASE

FMODB ID: 94YG2

Calculation Name: 5I97-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5I97

Chain ID: A

ChEMBL ID:

UniProt ID: Q17U16

Base Structure: X-ray

Registration Date: 2023-06-21

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

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	143
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1361875.14338
FMO2-HF: Nuclear repulsion	1304157.88445
FMO2-HF: Total energy	-57717.25893
FMO2-MP2: Total energy	-57887.192588

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:88:THR)

Summations of interaction energy for fragment #1(A:88:THR)

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.
-12.343	-3.975	1.612	-3.726	-6.251	-0.003

Interaction energy analysis for fragmet #1(A:88:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.021 / q_NPA : 0.004

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	90	ASP	-1	-0.854	-0.914	3.802	-0.559	2.242	-0.015	-1.441	-1.344	0.001
4	A	91	GLN	0	-0.036	-0.027	5.250	-0.763	-0.763	0.000	0.000	0.000	0.000
5	A	92	THR	0	0.031	0.032	8.144	0.130	0.130	0.000	0.000	0.000	0.000
6	A	93	SER	0	-0.058	-0.051	10.576	0.031	0.031	0.000	0.000	0.000	0.000
7	A	94	TYR	0	0.008	-0.012	2.824	-0.975	-0.217	0.151	-0.295	-0.614	-0.002
8	A	95	GLY	0	0.010	0.012	9.500	0.026	0.026	0.000	0.000	0.000	0.000
9	A	96	ASP	-1	-0.806	-0.921	13.117	-0.321	-0.321	0.000	0.000	0.000	0.000
10	A	97	GLU	-1	-0.924	-0.973	15.105	-0.369	-0.369	0.000	0.000	0.000	0.000
11	A	98	ILE	0	0.004	0.001	8.790	0.024	0.024	0.000	0.000	0.000	0.000
12	A	99	ASP	-1	-0.673	-0.808	11.312	-0.606	-0.606	0.000	0.000	0.000	0.000
13	A	100	LYS	1	0.966	0.987	12.918	0.265	0.265	0.000	0.000	0.000	0.000
14	A	101	PHE	0	-0.006	0.018	12.188	0.072	0.072	0.000	0.000	0.000	0.000
15	A	102	TRP	0	0.058	0.020	8.810	0.079	0.079	0.000	0.000	0.000	0.000
16	A	103	LEU	0	0.007	0.002	13.035	0.078	0.078	0.000	0.000	0.000	0.000
17	A	104	THR	0	-0.053	-0.053	15.668	0.046	0.046	0.000	0.000	0.000	0.000
18	A	105	GLN	0	-0.014	0.001	14.866	0.049	0.049	0.000	0.000	0.000	0.000
19	A	106	TYR	0	-0.010	-0.005	14.634	0.026	0.026	0.000	0.000	0.000	0.000
20	A	107	VAL	0	0.018	0.003	16.745	0.026	0.026	0.000	0.000	0.000	0.000
21	A	108	ILE	0	-0.020	-0.007	20.051	0.015	0.015	0.000	0.000	0.000	0.000
22	A	109	HIS	1	0.832	0.916	16.234	0.070	0.070	0.000	0.000	0.000	0.000
23	A	110	ARG	1	0.902	0.968	19.749	-0.008	-0.008	0.000	0.000	0.000	0.000
24	A	111	GLU	-1	-0.881	-0.935	21.629	-0.009	-0.009	0.000	0.000	0.000	0.000
25	A	112	SER	0	-0.083	-0.058	23.963	-0.002	-0.002	0.000	0.000	0.000	0.000
26	A	113	TYR	0	-0.084	-0.068	25.796	0.009	0.009	0.000	0.000	0.000	0.000
27	A	114	ASP	-1	-0.802	-0.915	26.877	0.000	0.000	0.000	0.000	0.000	0.000
28	A	115	PHE	0	-0.004	0.017	27.181	0.005	0.005	0.000	0.000	0.000	0.000
29	A	116	TYR	0	-0.052	-0.039	28.237	0.007	0.007	0.000	0.000	0.000	0.000
30	A	117	SER	0	0.009	0.000	23.316	0.003	0.003	0.000	0.000	0.000	0.000
31	A	118	VAL	0	0.001	0.012	22.936	0.002	0.002	0.000	0.000	0.000	0.000
32	A	119	GLN	0	0.007	0.000	21.575	0.015	0.015	0.000	0.000	0.000	0.000
33	A	120	VAL	0	0.021	0.008	18.125	0.013	0.013	0.000	0.000	0.000	0.000
34	A	121	ASP	-1	-0.803	-0.883	18.229	-0.005	-0.005	0.000	0.000	0.000	0.000
35	A	122	TYR	0	0.003	0.000	18.767	0.001	0.001	0.000	0.000	0.000	0.000
36	A	123	THR	0	-0.019	-0.013	15.195	0.025	0.025	0.000	0.000	0.000	0.000
37	A	124	ALA	0	-0.027	-0.014	14.235	0.025	0.025	0.000	0.000	0.000	0.000
38	A	125	VAL	0	0.022	0.006	14.019	0.004	0.004	0.000	0.000	0.000	0.000
39	A	126	GLY	0	-0.026	0.033	15.418	0.012	0.012	0.000	0.000	0.000	0.000
40	A	127	LEU	0	-0.035	-0.012	10.447	0.057	0.057	0.000	0.000	0.000	0.000
41	A	128	MET	0	-0.041	0.006	10.388	0.064	0.064	0.000	0.000	0.000	0.000
42	A	129	SER	0	-0.016	-0.040	11.927	-0.073	-0.073	0.000	0.000	0.000	0.000
43	A	130	THR	0	-0.016	-0.001	13.466	0.070	0.070	0.000	0.000	0.000	0.000
44	A	131	PRO	0	0.058	0.008	14.378	-0.036	-0.036	0.000	0.000	0.000	0.000
45	A	132	ASN	0	0.048	0.029	17.302	-0.024	-0.024	0.000	0.000	0.000	0.000
46	A	133	VAL	0	-0.030	-0.004	17.181	-0.019	-0.019	0.000	0.000	0.000	0.000
47	A	134	ALA	0	0.005	-0.005	16.796	-0.019	-0.019	0.000	0.000	0.000	0.000
48	A	135	GLU	-1	-0.914	-0.949	18.818	0.112	0.112	0.000	0.000	0.000	0.000
49	A	136	SER	0	-0.060	-0.025	22.040	-0.017	-0.017	0.000	0.000	0.000	0.000
50	A	137	TYR	0	-0.021	-0.020	20.532	-0.010	-0.010	0.000	0.000	0.000	0.000
51	A	138	GLN	0	0.032	-0.007	18.699	-0.008	-0.008	0.000	0.000	0.000	0.000
52	A	139	SER	0	-0.037	-0.002	23.475	-0.002	-0.002	0.000	0.000	0.000	0.000
53	A	140	LYS	1	0.983	0.994	26.312	-0.027	-0.027	0.000	0.000	0.000	0.000
54	A	141	PHE	0	0.015	0.019	24.225	-0.005	-0.005	0.000	0.000	0.000	0.000
55	A	142	LYS	1	0.933	0.973	26.048	-0.087	-0.087	0.000	0.000	0.000	0.000
56	A	143	GLY	0	0.006	0.005	29.308	-0.005	-0.005	0.000	0.000	0.000	0.000
57	A	144	ARG	1	0.963	0.950	32.854	-0.044	-0.044	0.000	0.000	0.000	0.000
58	A	145	ASN	0	0.002	0.010	35.041	-0.002	-0.002	0.000	0.000	0.000	0.000
59	A	146	GLY	0	0.000	0.020	30.920	-0.001	-0.001	0.000	0.000	0.000	0.000
60	A	147	LEU	0	0.038	-0.002	28.305	-0.002	-0.002	0.000	0.000	0.000	0.000
61	A	148	ASP	-1	-0.856	-0.934	28.569	0.054	0.054	0.000	0.000	0.000	0.000
62	A	149	LYS	1	0.865	0.937	29.824	-0.068	-0.068	0.000	0.000	0.000	0.000
63	A	150	VAL	0	-0.044	-0.004	33.504	-0.002	-0.002	0.000	0.000	0.000	0.000
64	A	151	LEU	0	-0.022	0.003	31.674	-0.002	-0.002	0.000	0.000	0.000	0.000
65	A	152	GLY	0	0.062	0.056	33.340	-0.003	-0.003	0.000	0.000	0.000	0.000
66	A	153	ASP	-1	-0.781	-0.869	32.867	0.014	0.014	0.000	0.000	0.000	0.000
67	A	154	SER	0	-0.049	-0.029	34.673	-0.004	-0.004	0.000	0.000	0.000	0.000
68	A	155	GLU	-1	-0.810	-0.883	34.043	0.004	0.004	0.000	0.000	0.000	0.000
69	A	156	THR	0	-0.038	-0.017	30.741	0.001	0.001	0.000	0.000	0.000	0.000
70	A	157	THR	0	0.017	0.004	29.259	-0.003	-0.003	0.000	0.000	0.000	0.000
71	A	158	ARG	1	0.949	0.999	28.353	0.029	0.029	0.000	0.000	0.000	0.000
72	A	159	VAL	0	0.056	0.020	24.248	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	160	LYS	1	0.904	0.957	26.880	0.075	0.075	0.000	0.000	0.000	0.000
74	A	161	ILE	0	0.042	0.020	22.189	0.002	0.002	0.000	0.000	0.000	0.000
75	A	162	ASN	0	-0.097	-0.063	25.486	0.003	0.003	0.000	0.000	0.000	0.000
76	A	163	SER	0	-0.004	-0.006	25.837	-0.003	-0.003	0.000	0.000	0.000	0.000
77	A	164	VAL	0	0.023	-0.001	19.434	0.005	0.005	0.000	0.000	0.000	0.000
78	A	165	ILE	0	-0.001	0.010	22.854	-0.008	-0.008	0.000	0.000	0.000	0.000
79	A	166	LEU	0	-0.006	0.002	16.399	0.008	0.008	0.000	0.000	0.000	0.000
80	A	167	ASP	-1	-0.807	-0.871	19.407	-0.175	-0.175	0.000	0.000	0.000	0.000
81	A	168	LYS	1	0.867	0.923	14.632	0.351	0.351	0.000	0.000	0.000	0.000
82	A	169	PRO	0	-0.024	-0.015	15.550	-0.023	-0.023	0.000	0.000	0.000	0.000
83	A	170	HIS	1	0.840	0.886	17.309	0.175	0.175	0.000	0.000	0.000	0.000
84	A	171	GLY	0	0.065	0.062	15.162	0.025	0.025	0.000	0.000	0.000	0.000
85	A	172	VAL	0	-0.011	0.006	15.797	0.039	0.039	0.000	0.000	0.000	0.000
86	A	173	ALA	0	0.003	-0.002	17.972	-0.025	-0.025	0.000	0.000	0.000	0.000
87	A	174	THR	0	-0.038	-0.010	19.861	0.027	0.027	0.000	0.000	0.000	0.000
88	A	175	ILE	0	0.002	-0.005	19.062	-0.012	-0.012	0.000	0.000	0.000	0.000
89	A	176	ARG	1	0.909	0.975	23.496	0.093	0.093	0.000	0.000	0.000	0.000
90	A	177	PHE	0	-0.012	-0.009	25.350	-0.010	-0.010	0.000	0.000	0.000	0.000
91	A	178	THR	0	0.003	-0.008	27.493	0.008	0.008	0.000	0.000	0.000	0.000
92	A	179	THR	0	0.045	0.041	28.505	-0.004	-0.004	0.000	0.000	0.000	0.000
93	A	180	VAL	0	-0.039	-0.028	30.867	0.001	0.001	0.000	0.000	0.000	0.000
94	A	181	ARG	1	0.845	0.894	33.091	0.000	0.000	0.000	0.000	0.000	0.000
95	A	182	ARG	1	0.853	0.937	34.778	0.007	0.007	0.000	0.000	0.000	0.000
96	A	183	VAL	0	0.034	0.013	36.657	0.003	0.003	0.000	0.000	0.000	0.000
97	A	184	ARG	1	0.841	0.896	33.708	-0.008	-0.008	0.000	0.000	0.000	0.000
98	A	185	SER	0	-0.006	0.001	40.152	0.000	0.000	0.000	0.000	0.000	0.000
99	A	186	ASN	0	-0.011	0.010	42.558	0.001	0.001	0.000	0.000	0.000	0.000
100	A	187	PRO	0	0.020	0.008	43.235	0.000	0.000	0.000	0.000	0.000	0.000
101	A	188	VAL	0	-0.020	-0.012	42.783	-0.001	-0.001	0.000	0.000	0.000	0.000
102	A	189	ASP	-1	-0.880	-0.949	37.693	-0.016	-0.016	0.000	0.000	0.000	0.000
103	A	190	ASP	-1	-0.856	-0.933	37.862	-0.008	-0.008	0.000	0.000	0.000	0.000
104	A	191	GLN	0	-0.028	-0.027	38.719	-0.002	-0.002	0.000	0.000	0.000	0.000
105	A	192	PRO	0	-0.028	-0.023	35.170	0.000	0.000	0.000	0.000	0.000	0.000
106	A	193	GLN	0	0.000	0.020	33.702	0.001	0.001	0.000	0.000	0.000	0.000
107	A	194	ARG	1	0.932	0.965	31.885	0.052	0.052	0.000	0.000	0.000	0.000
108	A	195	TRP	0	0.011	-0.006	28.340	0.005	0.005	0.000	0.000	0.000	0.000
109	A	196	ILE	0	-0.013	-0.006	26.789	-0.010	-0.010	0.000	0.000	0.000	0.000
110	A	197	ALA	0	0.018	0.007	22.520	0.009	0.009	0.000	0.000	0.000	0.000
111	A	198	ILE	0	-0.034	-0.011	22.962	-0.015	-0.015	0.000	0.000	0.000	0.000
112	A	199	MET	0	-0.045	-0.026	16.868	0.011	0.011	0.000	0.000	0.000	0.000
113	A	200	GLY	0	0.019	0.022	17.328	-0.020	-0.020	0.000	0.000	0.000	0.000
114	A	201	TYR	0	-0.085	-0.058	11.620	0.053	0.053	0.000	0.000	0.000	0.000
115	A	202	GLU	-1	-0.813	-0.907	9.994	0.203	0.203	0.000	0.000	0.000	0.000
116	A	203	TYR	0	-0.057	-0.048	4.937	-0.011	-0.011	0.000	0.000	0.000	0.000
117	A	204	LYS	1	0.900	0.958	5.637	-0.678	-0.678	0.000	0.000	0.000	0.000
118	A	205	SER	0	0.001	0.014	2.948	0.138	1.513	0.782	-0.695	-1.462	0.007
119	A	206	LEU	0	-0.005	-0.005	3.782	-3.226	-3.256	0.051	0.228	-0.249	0.002
120	A	207	ALA	0	0.012	0.002	5.711	0.363	0.363	0.000	0.000	0.000	0.000
121	A	208	MET	0	-0.025	-0.004	2.512	-0.648	-0.178	0.320	-0.221	-0.569	-0.001
122	A	209	ASN	0	0.043	0.028	7.633	-0.034	-0.034	0.000	0.000	0.000	0.000
123	A	210	ALA	0	0.015	-0.023	9.266	-0.008	-0.008	0.000	0.000	0.000	0.000
124	A	211	GLU	-1	-0.903	-0.946	11.369	0.186	0.186	0.000	0.000	0.000	0.000
125	A	212	GLN	0	0.041	0.010	8.687	0.063	0.063	0.000	0.000	0.000	0.000
126	A	213	ARG	1	0.945	0.978	5.595	-1.206	-1.206	0.000	0.000	0.000	0.000
127	A	214	TYR	0	-0.032	0.000	7.726	-0.194	-0.194	0.000	0.000	0.000	0.000
128	A	215	VAL	0	-0.010	0.002	9.884	-0.047	-0.047	0.000	0.000	0.000	0.000
129	A	216	ASN	0	-0.046	-0.056	7.894	-0.286	-0.286	0.000	0.000	0.000	0.000
130	A	217	PRO	0	0.010	0.014	5.311	0.014	0.014	0.000	0.000	0.000	0.000
131	A	218	LEU	0	-0.060	-0.030	2.827	-4.714	-2.495	0.265	-0.916	-1.567	-0.006
132	A	219	GLY	0	0.036	0.027	3.307	-0.115	0.651	0.059	-0.383	-0.441	-0.004
133	A	220	PHE	0	-0.022	-0.002	4.790	0.230	0.239	-0.001	-0.003	-0.005	0.000
134	A	221	ARG	1	0.873	0.930	7.601	-0.315	-0.315	0.000	0.000	0.000	0.000
135	A	222	VAL	0	0.024	0.005	10.558	-0.060	-0.060	0.000	0.000	0.000	0.000
136	A	223	THR	0	-0.065	-0.058	13.536	0.047	0.047	0.000	0.000	0.000	0.000
137	A	224	SER	0	-0.022	-0.011	15.855	0.006	0.006	0.000	0.000	0.000	0.000
138	A	225	TYR	0	-0.029	-0.048	19.045	-0.020	-0.020	0.000	0.000	0.000	0.000
139	A	226	ARG	1	0.937	0.984	21.206	0.047	0.047	0.000	0.000	0.000	0.000
140	A	227	VAL	0	0.034	0.022	24.684	-0.011	-0.011	0.000	0.000	0.000	0.000
141	A	228	ASN	0	-0.047	-0.024	26.885	0.003	0.003	0.000	0.000	0.000	0.000
142	A	229	PRO	0	0.067	0.030	30.333	-0.005	-0.005	0.000	0.000	0.000	0.000
143	A	230	GLU	-1	-0.900	-0.944	31.576	-0.061	-0.061	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:88:THR)