FMO DATABASE

FMODB ID: MVM3Z

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1362039.811796
FMO2-HF: Nuclear repulsion	1304321.963477
FMO2-HF: Total energy	-57717.848318
FMO2-MP2: Total energy	-57887.796271

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.
-11.551	-3.885	1.737	-3.206	-6.195	-0.004

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 : 0.010 / q_NPA : -0.007

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	-0.803	-0.880	3.826	-0.420	2.361	-0.023	-1.466	-1.291	0.001
4	A	91	GLN	0	-0.047	-0.015	5.497	-0.817	-0.817	0.000	0.000	0.000	0.000
5	A	92	THR	0	0.051	0.038	8.256	0.121	0.121	0.000	0.000	0.000	0.000
6	A	93	SER	0	-0.041	-0.056	10.931	0.037	0.037	0.000	0.000	0.000	0.000
7	A	94	TYR	0	0.021	-0.008	3.356	-0.974	-0.257	0.099	-0.284	-0.533	-0.002
8	A	95	GLY	0	0.022	0.027	9.685	0.035	0.035	0.000	0.000	0.000	0.000
9	A	96	ASP	-1	-0.823	-0.905	13.260	-0.295	-0.295	0.000	0.000	0.000	0.000
10	A	97	GLU	-1	-0.885	-0.953	14.937	-0.312	-0.312	0.000	0.000	0.000	0.000
11	A	98	ILE	0	0.002	-0.001	8.543	0.019	0.019	0.000	0.000	0.000	0.000
12	A	99	ASP	-1	-0.677	-0.776	11.284	-0.576	-0.576	0.000	0.000	0.000	0.000
13	A	100	LYS	1	0.971	0.990	12.797	0.237	0.237	0.000	0.000	0.000	0.000
14	A	101	PHE	0	-0.011	0.016	11.824	0.062	0.062	0.000	0.000	0.000	0.000
15	A	102	TRP	0	0.056	0.018	8.392	0.051	0.051	0.000	0.000	0.000	0.000
16	A	103	LEU	0	0.005	0.005	13.023	0.067	0.067	0.000	0.000	0.000	0.000
17	A	104	THR	0	-0.045	-0.051	15.670	0.042	0.042	0.000	0.000	0.000	0.000
18	A	105	GLN	0	0.013	0.017	14.724	0.046	0.046	0.000	0.000	0.000	0.000
19	A	106	TYR	0	-0.012	-0.006	14.506	0.024	0.024	0.000	0.000	0.000	0.000
20	A	107	VAL	0	0.015	0.001	16.748	0.024	0.024	0.000	0.000	0.000	0.000
21	A	108	ILE	0	-0.023	-0.009	20.052	0.015	0.015	0.000	0.000	0.000	0.000
22	A	109	HIS	1	0.829	0.902	16.372	0.104	0.104	0.000	0.000	0.000	0.000
23	A	110	ARG	1	0.879	0.958	19.555	0.021	0.021	0.000	0.000	0.000	0.000
24	A	111	GLU	-1	-0.870	-0.919	21.632	-0.024	-0.024	0.000	0.000	0.000	0.000
25	A	112	SER	0	-0.068	-0.038	24.078	0.001	0.001	0.000	0.000	0.000	0.000
26	A	113	TYR	0	-0.098	-0.072	25.790	0.007	0.007	0.000	0.000	0.000	0.000
27	A	114	ASP	-1	-0.772	-0.911	27.020	-0.012	-0.012	0.000	0.000	0.000	0.000
28	A	115	PHE	0	-0.013	0.020	27.176	0.003	0.003	0.000	0.000	0.000	0.000
29	A	116	TYR	0	-0.071	-0.057	28.234	0.006	0.006	0.000	0.000	0.000	0.000
30	A	117	SER	0	-0.015	-0.022	23.341	0.002	0.002	0.000	0.000	0.000	0.000
31	A	118	VAL	0	0.002	0.012	22.931	0.000	0.000	0.000	0.000	0.000	0.000
32	A	119	GLN	0	0.009	0.002	21.823	0.008	0.008	0.000	0.000	0.000	0.000
33	A	120	VAL	0	0.024	0.011	18.250	0.009	0.009	0.000	0.000	0.000	0.000
34	A	121	ASP	-1	-0.802	-0.869	18.225	-0.036	-0.036	0.000	0.000	0.000	0.000
35	A	122	TYR	0	0.003	0.001	18.762	-0.001	-0.001	0.000	0.000	0.000	0.000
36	A	123	THR	0	-0.026	-0.021	15.229	0.019	0.019	0.000	0.000	0.000	0.000
37	A	124	ALA	0	-0.024	-0.012	14.230	0.016	0.016	0.000	0.000	0.000	0.000
38	A	125	VAL	0	0.008	-0.004	14.015	-0.001	-0.001	0.000	0.000	0.000	0.000
39	A	126	GLY	0	-0.015	0.013	15.415	0.010	0.010	0.000	0.000	0.000	0.000
40	A	127	LEU	0	-0.029	-0.010	10.490	0.050	0.050	0.000	0.000	0.000	0.000
41	A	128	MET	0	-0.041	0.006	10.386	0.055	0.055	0.000	0.000	0.000	0.000
42	A	129	SER	0	-0.001	0.004	11.925	-0.058	-0.058	0.000	0.000	0.000	0.000
43	A	130	THR	0	-0.007	0.005	13.465	0.060	0.060	0.000	0.000	0.000	0.000
44	A	131	PRO	0	0.064	0.011	14.461	-0.030	-0.030	0.000	0.000	0.000	0.000
45	A	132	ASN	0	0.019	0.014	17.304	-0.012	-0.012	0.000	0.000	0.000	0.000
46	A	133	VAL	0	-0.009	0.000	17.189	-0.015	-0.015	0.000	0.000	0.000	0.000
47	A	134	ALA	0	0.008	0.003	16.774	-0.015	-0.015	0.000	0.000	0.000	0.000
48	A	135	GLU	-1	-0.876	-0.937	18.817	0.076	0.076	0.000	0.000	0.000	0.000
49	A	136	SER	0	-0.054	-0.025	22.040	-0.012	-0.012	0.000	0.000	0.000	0.000
50	A	137	TYR	0	-0.024	-0.019	20.490	-0.007	-0.007	0.000	0.000	0.000	0.000
51	A	138	GLN	0	0.035	-0.008	18.926	-0.003	-0.003	0.000	0.000	0.000	0.000
52	A	139	SER	0	-0.032	-0.004	23.474	0.000	0.000	0.000	0.000	0.000	0.000
53	A	140	LYS	1	0.978	0.998	26.263	-0.003	-0.003	0.000	0.000	0.000	0.000
54	A	141	PHE	0	0.004	0.009	24.234	-0.004	-0.004	0.000	0.000	0.000	0.000
55	A	142	LYS	1	0.896	0.963	25.576	-0.067	-0.067	0.000	0.000	0.000	0.000
56	A	143	GLY	0	0.014	0.009	29.309	-0.004	-0.004	0.000	0.000	0.000	0.000
57	A	144	ARG	1	0.955	0.956	32.855	-0.028	-0.028	0.000	0.000	0.000	0.000
58	A	145	ASN	0	-0.010	-0.005	35.066	0.000	0.000	0.000	0.000	0.000	0.000
59	A	146	GLY	0	0.020	0.030	30.912	-0.002	-0.002	0.000	0.000	0.000	0.000
60	A	147	LEU	0	0.036	-0.002	28.168	-0.002	-0.002	0.000	0.000	0.000	0.000
61	A	148	ASP	-1	-0.778	-0.886	28.509	0.032	0.032	0.000	0.000	0.000	0.000
62	A	149	LYS	1	0.785	0.886	28.733	-0.041	-0.041	0.000	0.000	0.000	0.000
63	A	150	VAL	0	-0.053	-0.006	33.502	-0.001	-0.001	0.000	0.000	0.000	0.000
64	A	151	LEU	0	-0.012	0.008	31.833	-0.001	-0.001	0.000	0.000	0.000	0.000
65	A	152	GLY	0	0.059	0.058	33.341	-0.002	-0.002	0.000	0.000	0.000	0.000
66	A	153	ASP	-1	-0.752	-0.841	32.863	0.000	0.000	0.000	0.000	0.000	0.000
67	A	154	SER	0	-0.043	-0.034	34.669	-0.003	-0.003	0.000	0.000	0.000	0.000
68	A	155	GLU	-1	-0.821	-0.890	34.219	-0.008	-0.008	0.000	0.000	0.000	0.000
69	A	156	THR	0	-0.032	-0.013	30.694	0.000	0.000	0.000	0.000	0.000	0.000
70	A	157	THR	0	0.002	0.000	29.494	-0.002	-0.002	0.000	0.000	0.000	0.000
71	A	158	ARG	1	0.893	0.947	28.352	0.031	0.031	0.000	0.000	0.000	0.000
72	A	159	VAL	0	0.047	0.015	24.162	0.000	0.000	0.000	0.000	0.000	0.000
73	A	160	LYS	1	0.899	0.951	26.886	0.078	0.078	0.000	0.000	0.000	0.000
74	A	161	ILE	0	0.050	0.027	22.013	0.002	0.002	0.000	0.000	0.000	0.000
75	A	162	ASN	0	-0.098	-0.053	25.384	0.002	0.002	0.000	0.000	0.000	0.000
76	A	163	SER	0	-0.002	-0.004	25.603	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	164	VAL	0	0.015	-0.003	19.241	0.003	0.003	0.000	0.000	0.000	0.000
78	A	165	ILE	0	-0.006	0.008	22.707	-0.006	-0.006	0.000	0.000	0.000	0.000
79	A	166	LEU	0	-0.001	-0.001	16.440	0.005	0.005	0.000	0.000	0.000	0.000
80	A	167	ASP	-1	-0.802	-0.872	19.462	-0.168	-0.168	0.000	0.000	0.000	0.000
81	A	168	LYS	1	0.864	0.899	15.139	0.306	0.306	0.000	0.000	0.000	0.000
82	A	169	PRO	0	-0.028	-0.015	15.808	-0.025	-0.025	0.000	0.000	0.000	0.000
83	A	170	HIS	1	0.824	0.878	17.400	0.170	0.170	0.000	0.000	0.000	0.000
84	A	171	GLY	0	0.066	0.063	15.154	0.020	0.020	0.000	0.000	0.000	0.000
85	A	172	VAL	0	-0.015	0.005	15.790	0.034	0.034	0.000	0.000	0.000	0.000
86	A	173	ALA	0	0.001	-0.001	17.926	-0.020	-0.020	0.000	0.000	0.000	0.000
87	A	174	THR	0	-0.035	-0.008	19.857	0.023	0.023	0.000	0.000	0.000	0.000
88	A	175	ILE	0	0.008	-0.004	19.089	-0.009	-0.009	0.000	0.000	0.000	0.000
89	A	176	ARG	1	0.855	0.920	23.496	0.087	0.087	0.000	0.000	0.000	0.000
90	A	177	PHE	0	-0.007	-0.010	25.345	-0.008	-0.008	0.000	0.000	0.000	0.000
91	A	178	THR	0	-0.014	-0.026	27.495	0.007	0.007	0.000	0.000	0.000	0.000
92	A	179	THR	0	0.062	0.052	28.571	-0.004	-0.004	0.000	0.000	0.000	0.000
93	A	180	VAL	0	-0.039	-0.030	30.871	0.001	0.001	0.000	0.000	0.000	0.000
94	A	181	ARG	1	0.826	0.881	33.097	0.010	0.010	0.000	0.000	0.000	0.000
95	A	182	ARG	1	0.836	0.916	34.783	0.014	0.014	0.000	0.000	0.000	0.000
96	A	183	VAL	0	0.039	0.019	36.650	0.002	0.002	0.000	0.000	0.000	0.000
97	A	184	ARG	1	0.818	0.878	33.581	0.003	0.003	0.000	0.000	0.000	0.000
98	A	185	SER	0	-0.002	0.008	40.146	0.000	0.000	0.000	0.000	0.000	0.000
99	A	186	ASN	0	-0.012	0.005	42.490	0.001	0.001	0.000	0.000	0.000	0.000
100	A	187	PRO	0	0.037	0.021	43.228	0.000	0.000	0.000	0.000	0.000	0.000
101	A	188	VAL	0	-0.015	-0.014	42.783	-0.001	-0.001	0.000	0.000	0.000	0.000
102	A	189	ASP	-1	-0.837	-0.899	37.200	-0.023	-0.023	0.000	0.000	0.000	0.000
103	A	190	ASP	-1	-0.840	-0.918	37.899	-0.015	-0.015	0.000	0.000	0.000	0.000
104	A	191	GLN	0	-0.015	-0.016	38.724	-0.002	-0.002	0.000	0.000	0.000	0.000
105	A	192	PRO	0	-0.015	-0.020	35.079	0.000	0.000	0.000	0.000	0.000	0.000
106	A	193	GLN	0	-0.009	0.017	33.639	0.001	0.001	0.000	0.000	0.000	0.000
107	A	194	ARG	1	0.927	0.961	31.879	0.054	0.054	0.000	0.000	0.000	0.000
108	A	195	TRP	0	0.008	-0.008	28.375	0.005	0.005	0.000	0.000	0.000	0.000
109	A	196	ILE	0	-0.018	-0.012	26.791	-0.008	-0.008	0.000	0.000	0.000	0.000
110	A	197	ALA	0	0.020	0.010	22.509	0.007	0.007	0.000	0.000	0.000	0.000
111	A	198	ILE	0	-0.038	-0.016	23.022	-0.013	-0.013	0.000	0.000	0.000	0.000
112	A	199	MET	0	-0.050	-0.023	16.782	0.010	0.010	0.000	0.000	0.000	0.000
113	A	200	GLY	0	0.029	0.025	17.322	-0.017	-0.017	0.000	0.000	0.000	0.000
114	A	201	TYR	0	-0.098	-0.075	11.576	0.047	0.047	0.000	0.000	0.000	0.000
115	A	202	GLU	-1	-0.777	-0.874	9.728	0.135	0.135	0.000	0.000	0.000	0.000
116	A	203	TYR	0	-0.062	-0.063	4.932	0.005	0.005	0.000	0.000	0.000	0.000
117	A	204	LYS	1	0.816	0.905	5.634	-0.515	-0.515	0.000	0.000	0.000	0.000
118	A	205	SER	0	0.027	0.025	2.731	0.275	1.104	0.956	-0.279	-1.506	0.005
119	A	206	LEU	0	-0.032	-0.023	3.782	-3.020	-3.051	0.047	0.228	-0.244	0.002
120	A	207	ALA	0	0.002	-0.004	5.723	0.283	0.283	0.000	0.000	0.000	0.000
121	A	208	MET	0	-0.031	-0.001	2.916	-0.574	-0.167	0.087	-0.124	-0.370	0.000
122	A	209	ASN	0	0.054	0.029	7.642	-0.019	-0.019	0.000	0.000	0.000	0.000
123	A	210	ALA	0	0.021	-0.022	9.271	-0.040	-0.040	0.000	0.000	0.000	0.000
124	A	211	GLU	-1	-0.906	-0.945	11.373	0.119	0.119	0.000	0.000	0.000	0.000
125	A	212	GLN	0	0.046	0.010	8.852	0.016	0.016	0.000	0.000	0.000	0.000
126	A	213	ARG	1	0.936	0.974	5.183	-0.887	-0.887	0.000	0.000	0.000	0.000
127	A	214	TYR	0	-0.036	-0.001	7.726	-0.171	-0.171	0.000	0.000	0.000	0.000
128	A	215	VAL	0	-0.006	0.000	9.865	-0.020	-0.020	0.000	0.000	0.000	0.000
129	A	216	ASN	0	-0.055	-0.056	7.625	-0.269	-0.269	0.000	0.000	0.000	0.000
130	A	217	PRO	0	0.026	0.022	5.289	-0.036	-0.036	0.000	0.000	0.000	0.000
131	A	218	LEU	0	-0.060	-0.027	2.722	-4.727	-2.505	0.515	-0.937	-1.799	-0.006
132	A	219	GLY	0	0.036	0.024	3.307	-0.157	0.574	0.057	-0.341	-0.447	-0.004
133	A	220	PHE	0	-0.024	-0.006	4.790	0.255	0.265	-0.001	-0.003	-0.005	0.000
134	A	221	ARG	1	0.852	0.908	7.600	-0.240	-0.240	0.000	0.000	0.000	0.000
135	A	222	VAL	0	0.021	0.006	10.555	-0.051	-0.051	0.000	0.000	0.000	0.000
136	A	223	THR	0	-0.050	-0.055	13.486	0.043	0.043	0.000	0.000	0.000	0.000
137	A	224	SER	0	-0.018	-0.010	15.849	0.007	0.007	0.000	0.000	0.000	0.000
138	A	225	TYR	0	-0.047	-0.069	19.040	-0.019	-0.019	0.000	0.000	0.000	0.000
139	A	226	ARG	1	0.941	0.986	21.202	0.059	0.059	0.000	0.000	0.000	0.000
140	A	227	VAL	0	0.030	0.018	24.731	-0.010	-0.010	0.000	0.000	0.000	0.000
141	A	228	ASN	0	-0.041	-0.017	26.883	0.003	0.003	0.000	0.000	0.000	0.000
142	A	229	PRO	0	0.082	0.038	30.332	-0.005	-0.005	0.000	0.000	0.000	0.000
143	A	230	GLU	-1	-0.850	-0.888	31.560	-0.065	-0.065	0.000	0.000	0.000	0.000

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