FMO DATABASE

FMODB ID: 3JZGL

Calculation Name: 1M1S-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1M1S

Chain ID: A

ChEMBL ID:

UniProt ID: Q23246

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	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	109
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-802857.056021
FMO2-HF: Nuclear repulsion	761620.900965
FMO2-HF: Total energy	-41236.155056
FMO2-MP2: Total energy	-41357.754093

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:98:HIS)

Summations of interaction energy for fragment #1(A:98:HIS)

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.
-2.934	-0.428	0.053	-0.984	-1.574	0.009

Interaction energy analysis for fragmet #1(A:98:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.062 / q_NPA : 0.036

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	100	MET	0	0.026	0.041	3.480	-4.928	-2.422	0.053	-0.984	-1.574	0.009
4	A	101	ILE	0	-0.014	-0.010	5.600	-0.166	-0.166	0.000	0.000	0.000	0.000
5	A	102	ASN	0	0.007	0.016	6.464	1.738	1.738	0.000	0.000	0.000	0.000
6	A	103	VAL	0	-0.025	-0.020	8.776	-0.357	-0.357	0.000	0.000	0.000	0.000
7	A	104	ASP	-1	-0.855	-0.887	11.492	0.636	0.636	0.000	0.000	0.000	0.000
8	A	105	PRO	0	0.010	-0.016	14.181	-0.057	-0.057	0.000	0.000	0.000	0.000
9	A	106	PRO	0	0.098	0.051	10.224	0.005	0.005	0.000	0.000	0.000	0.000
10	A	107	THR	0	-0.060	-0.052	11.964	-0.133	-0.133	0.000	0.000	0.000	0.000
11	A	108	GLY	0	0.016	0.022	15.002	0.043	0.043	0.000	0.000	0.000	0.000
12	A	109	ASN	0	-0.018	-0.015	18.548	-0.011	-0.011	0.000	0.000	0.000	0.000
13	A	110	TYR	0	-0.014	-0.025	20.369	0.011	0.011	0.000	0.000	0.000	0.000
14	A	111	PRO	0	0.029	0.018	24.755	-0.011	-0.011	0.000	0.000	0.000	0.000
15	A	112	ALA	0	0.041	0.016	28.366	0.002	0.002	0.000	0.000	0.000	0.000
16	A	113	THR	0	0.036	0.005	29.289	0.000	0.000	0.000	0.000	0.000	0.000
17	A	114	GLY	0	-0.014	-0.007	29.907	0.001	0.001	0.000	0.000	0.000	0.000
18	A	115	GLY	0	-0.011	-0.020	26.932	0.000	0.000	0.000	0.000	0.000	0.000
19	A	116	ASN	0	-0.004	-0.012	25.170	0.005	0.005	0.000	0.000	0.000	0.000
20	A	117	SER	0	0.014	0.029	20.761	-0.001	-0.001	0.000	0.000	0.000	0.000
21	A	118	THR	0	0.019	0.021	21.099	-0.007	-0.007	0.000	0.000	0.000	0.000
22	A	119	HIS	1	0.788	0.886	15.074	-0.213	-0.213	0.000	0.000	0.000	0.000
23	A	120	ASN	0	-0.034	-0.024	15.538	-0.071	-0.071	0.000	0.000	0.000	0.000
24	A	121	ILE	0	0.014	0.011	12.321	0.074	0.074	0.000	0.000	0.000	0.000
25	A	122	THR	0	0.021	-0.002	11.930	-0.041	-0.041	0.000	0.000	0.000	0.000
26	A	123	SER	0	-0.035	-0.013	10.228	0.153	0.153	0.000	0.000	0.000	0.000
27	A	124	GLU	-1	-0.849	-0.943	6.036	0.312	0.312	0.000	0.000	0.000	0.000
28	A	125	SER	0	-0.033	-0.006	7.615	-0.203	-0.203	0.000	0.000	0.000	0.000
29	A	126	ASP	-1	-0.871	-0.926	8.730	0.124	0.124	0.000	0.000	0.000	0.000
30	A	127	SER	0	-0.021	-0.010	11.099	0.044	0.044	0.000	0.000	0.000	0.000
31	A	128	ARG	1	0.863	0.943	12.406	-0.094	-0.094	0.000	0.000	0.000	0.000
32	A	129	LEU	0	0.019	0.019	9.722	0.004	0.004	0.000	0.000	0.000	0.000
33	A	130	ALA	0	-0.002	0.009	13.717	-0.003	-0.003	0.000	0.000	0.000	0.000
34	A	131	PHE	0	-0.025	-0.029	14.547	0.033	0.033	0.000	0.000	0.000	0.000
35	A	132	LYS	1	0.890	0.953	15.356	-0.047	-0.047	0.000	0.000	0.000	0.000
36	A	133	VAL	0	-0.027	-0.008	15.428	0.015	0.015	0.000	0.000	0.000	0.000
37	A	134	LYS	1	0.798	0.926	13.785	0.090	0.090	0.000	0.000	0.000	0.000
38	A	135	SER	0	-0.006	-0.012	17.115	-0.007	-0.007	0.000	0.000	0.000	0.000
39	A	136	SER	0	-0.015	-0.015	19.067	-0.007	-0.007	0.000	0.000	0.000	0.000
40	A	137	ASN	0	0.008	-0.031	20.789	0.003	0.003	0.000	0.000	0.000	0.000
41	A	138	ASN	0	-0.017	-0.008	23.408	0.018	0.018	0.000	0.000	0.000	0.000
42	A	139	GLU	-1	-0.885	-0.940	25.672	-0.036	-0.036	0.000	0.000	0.000	0.000
43	A	140	HIS	0	0.011	0.032	26.452	-0.002	-0.002	0.000	0.000	0.000	0.000
44	A	141	TYR	0	-0.013	-0.008	22.368	0.013	0.013	0.000	0.000	0.000	0.000
45	A	142	ARG	1	0.928	0.972	24.914	-0.047	-0.047	0.000	0.000	0.000	0.000
46	A	143	VAL	0	0.031	0.001	19.028	0.008	0.008	0.000	0.000	0.000	0.000
47	A	144	ARG	1	0.891	0.959	22.104	-0.061	-0.061	0.000	0.000	0.000	0.000
48	A	145	PRO	0	0.045	0.049	20.448	0.010	0.010	0.000	0.000	0.000	0.000
49	A	146	VAL	0	0.011	-0.008	20.813	0.004	0.004	0.000	0.000	0.000	0.000
50	A	147	TYR	0	0.044	-0.003	19.489	0.005	0.005	0.000	0.000	0.000	0.000
51	A	148	GLY	0	0.025	0.007	19.766	-0.004	-0.004	0.000	0.000	0.000	0.000
52	A	149	PHE	0	0.039	0.029	17.734	0.016	0.016	0.000	0.000	0.000	0.000
53	A	150	VAL	0	-0.013	0.002	14.113	0.013	0.013	0.000	0.000	0.000	0.000
54	A	151	ASP	-1	-0.900	-0.946	14.926	0.126	0.126	0.000	0.000	0.000	0.000
55	A	152	ALA	0	0.029	0.011	13.309	0.023	0.023	0.000	0.000	0.000	0.000
56	A	153	LYS	1	0.776	0.893	9.068	0.034	0.034	0.000	0.000	0.000	0.000
57	A	154	GLY	0	0.023	0.024	12.699	0.020	0.020	0.000	0.000	0.000	0.000
58	A	155	LYS	1	0.946	0.951	14.359	-0.161	-0.161	0.000	0.000	0.000	0.000
59	A	156	SER	0	-0.005	-0.013	16.605	-0.042	-0.042	0.000	0.000	0.000	0.000
60	A	157	LYS	1	0.786	0.889	17.494	-0.093	-0.093	0.000	0.000	0.000	0.000
61	A	158	LEU	0	-0.011	-0.001	15.844	-0.017	-0.017	0.000	0.000	0.000	0.000
62	A	159	ASP	-1	-0.806	-0.909	19.324	0.120	0.120	0.000	0.000	0.000	0.000
63	A	160	ILE	0	0.004	0.020	17.299	-0.012	-0.012	0.000	0.000	0.000	0.000
64	A	161	ASN	0	-0.036	-0.023	21.962	0.005	0.005	0.000	0.000	0.000	0.000
65	A	162	ARG	1	0.817	0.921	24.874	0.016	0.016	0.000	0.000	0.000	0.000
66	A	163	LEU	0	-0.058	-0.023	26.435	0.005	0.005	0.000	0.000	0.000	0.000
67	A	164	PRO	0	0.025	-0.004	29.585	-0.004	-0.004	0.000	0.000	0.000	0.000
68	A	165	GLY	0	0.035	0.030	30.314	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	166	PRO	0	-0.023	-0.008	28.975	0.002	0.002	0.000	0.000	0.000	0.000
70	A	167	PRO	0	0.000	0.003	27.775	0.001	0.001	0.000	0.000	0.000	0.000
71	A	168	LYS	1	0.863	0.918	23.270	0.092	0.092	0.000	0.000	0.000	0.000
72	A	169	GLU	-1	-0.834	-0.906	18.475	-0.164	-0.164	0.000	0.000	0.000	0.000
73	A	170	ASP	-1	-0.807	-0.880	19.974	-0.096	-0.096	0.000	0.000	0.000	0.000
74	A	171	LYS	1	0.943	0.963	14.060	0.312	0.312	0.000	0.000	0.000	0.000
75	A	172	ILE	0	0.028	0.016	14.538	0.008	0.008	0.000	0.000	0.000	0.000
76	A	173	VAL	0	-0.090	-0.043	11.348	-0.011	-0.011	0.000	0.000	0.000	0.000
77	A	174	ILE	0	0.018	0.011	11.242	-0.013	-0.013	0.000	0.000	0.000	0.000
78	A	175	GLN	0	0.012	-0.006	10.701	0.056	0.056	0.000	0.000	0.000	0.000
79	A	176	TYR	0	-0.003	-0.022	5.483	0.242	0.242	0.000	0.000	0.000	0.000
80	A	177	ALA	0	0.043	0.024	11.966	-0.022	-0.022	0.000	0.000	0.000	0.000
81	A	178	GLU	-1	-0.813	-0.888	9.103	-0.066	-0.066	0.000	0.000	0.000	0.000
82	A	179	VAL	0	-0.040	-0.031	12.571	-0.002	-0.002	0.000	0.000	0.000	0.000
83	A	180	PRO	0	0.048	0.028	16.156	0.000	0.000	0.000	0.000	0.000	0.000
84	A	181	ALA	0	-0.007	-0.024	18.544	0.002	0.002	0.000	0.000	0.000	0.000
85	A	182	GLU	-1	-0.968	-0.989	20.511	0.057	0.057	0.000	0.000	0.000	0.000
86	A	183	GLU	-1	-0.889	-0.934	20.256	0.058	0.058	0.000	0.000	0.000	0.000
87	A	184	THR	0	0.015	0.012	22.321	0.006	0.006	0.000	0.000	0.000	0.000
88	A	185	ASP	-1	-0.760	-0.883	24.248	0.057	0.057	0.000	0.000	0.000	0.000
89	A	186	PRO	0	-0.020	-0.005	20.459	0.002	0.002	0.000	0.000	0.000	0.000
90	A	187	MET	0	-0.045	-0.053	20.225	0.001	0.001	0.000	0.000	0.000	0.000
91	A	188	ALA	0	0.024	0.045	22.165	-0.008	-0.008	0.000	0.000	0.000	0.000
92	A	189	PRO	0	0.058	0.026	16.998	-0.009	-0.009	0.000	0.000	0.000	0.000
93	A	190	PHE	0	-0.025	-0.025	14.909	-0.008	-0.008	0.000	0.000	0.000	0.000
94	A	191	LYS	1	0.771	0.876	19.579	-0.049	-0.049	0.000	0.000	0.000	0.000
95	A	192	ALA	0	0.010	0.014	20.451	-0.009	-0.009	0.000	0.000	0.000	0.000
96	A	193	GLY	0	-0.065	-0.014	19.002	-0.007	-0.007	0.000	0.000	0.000	0.000
97	A	194	ALA	0	0.008	-0.007	16.109	-0.007	-0.007	0.000	0.000	0.000	0.000
98	A	195	GLN	0	-0.042	-0.018	13.259	0.042	0.042	0.000	0.000	0.000	0.000
99	A	196	GLN	0	-0.017	-0.024	8.779	-0.036	-0.036	0.000	0.000	0.000	0.000
100	A	197	GLY	0	0.011	0.006	7.748	0.116	0.116	0.000	0.000	0.000	0.000
101	A	198	GLU	-1	-0.860	-0.957	7.457	-0.251	-0.251	0.000	0.000	0.000	0.000
102	A	199	ILE	0	0.022	0.038	5.701	-0.297	-0.297	0.000	0.000	0.000	0.000
103	A	200	ILE	0	-0.031	-0.031	7.796	-0.053	-0.053	0.000	0.000	0.000	0.000
104	A	201	VAL	0	0.003	0.014	10.342	-0.009	-0.009	0.000	0.000	0.000	0.000
105	A	202	LYS	1	0.910	0.942	12.711	0.192	0.192	0.000	0.000	0.000	0.000
106	A	203	LEU	0	-0.007	-0.011	15.073	0.051	0.051	0.000	0.000	0.000	0.000
107	A	204	ILE	0	0.004	0.011	17.954	-0.019	-0.019	0.000	0.000	0.000	0.000
108	A	205	ALA	0	-0.007	0.007	21.053	0.020	0.020	0.000	0.000	0.000	0.000
109	A	206	ALA	0	0.051	0.030	24.703	-0.007	-0.007	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:98:HIS)