FMO DATABASE

FMODB ID: JQYK9

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

Total energy (hartree)

FMO2-HF: Electronic energy	-801727.829881
FMO2-HF: Nuclear repulsion	760492.586802
FMO2-HF: Total energy	-41235.243079
FMO2-MP2: Total energy	-41356.84833

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.
-0.261	1.614	0.037	-0.56	-1.352	0.004

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 : 0.020 / q_NPA : -0.016

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	0.015	0.031	3.581	-2.504	-0.773	0.038	-0.552	-1.217	0.004
4	A	101	ILE	0	-0.004	-0.007	5.385	-0.586	-0.442	-0.001	-0.008	-0.135	0.000
5	A	102	ASN	0	0.019	0.021	6.490	1.570	1.570	0.000	0.000	0.000	0.000
6	A	103	VAL	0	-0.040	-0.028	8.909	-0.318	-0.318	0.000	0.000	0.000	0.000
7	A	104	ASP	-1	-0.903	-0.910	11.768	0.680	0.680	0.000	0.000	0.000	0.000
8	A	105	PRO	0	-0.011	-0.035	14.449	-0.047	-0.047	0.000	0.000	0.000	0.000
9	A	106	PRO	0	0.093	0.044	10.415	0.021	0.021	0.000	0.000	0.000	0.000
10	A	107	THR	0	-0.077	-0.053	12.163	-0.121	-0.121	0.000	0.000	0.000	0.000
11	A	108	GLY	0	0.015	0.020	15.163	0.041	0.041	0.000	0.000	0.000	0.000
12	A	109	ASN	0	-0.003	-0.007	18.719	-0.002	-0.002	0.000	0.000	0.000	0.000
13	A	110	TYR	0	0.002	-0.016	20.665	0.014	0.014	0.000	0.000	0.000	0.000
14	A	111	PRO	0	0.017	0.011	24.903	-0.015	-0.015	0.000	0.000	0.000	0.000
15	A	112	ALA	0	0.045	0.016	28.501	0.006	0.006	0.000	0.000	0.000	0.000
16	A	113	THR	0	0.000	-0.012	29.401	0.005	0.005	0.000	0.000	0.000	0.000
17	A	114	GLY	0	0.016	0.005	30.069	0.003	0.003	0.000	0.000	0.000	0.000
18	A	115	GLY	0	-0.015	-0.024	27.110	-0.005	-0.005	0.000	0.000	0.000	0.000
19	A	116	ASN	0	0.024	0.002	25.393	0.016	0.016	0.000	0.000	0.000	0.000
20	A	117	SER	0	-0.004	0.021	20.980	-0.006	-0.006	0.000	0.000	0.000	0.000
21	A	118	THR	0	0.016	0.019	21.337	-0.001	-0.001	0.000	0.000	0.000	0.000
22	A	119	HIS	1	0.800	0.893	15.676	-0.322	-0.322	0.000	0.000	0.000	0.000
23	A	120	ASN	0	0.024	0.007	16.067	-0.002	-0.002	0.000	0.000	0.000	0.000
24	A	121	ILE	0	0.019	0.017	12.454	0.062	0.062	0.000	0.000	0.000	0.000
25	A	122	THR	0	0.012	-0.005	12.180	-0.045	-0.045	0.000	0.000	0.000	0.000
26	A	123	SER	0	-0.026	-0.008	10.028	0.239	0.239	0.000	0.000	0.000	0.000
27	A	124	GLU	-1	-0.897	-0.951	5.987	0.467	0.467	0.000	0.000	0.000	0.000
28	A	125	SER	0	0.005	0.013	7.429	-0.137	-0.137	0.000	0.000	0.000	0.000
29	A	126	ASP	-1	-0.916	-0.965	8.652	0.473	0.473	0.000	0.000	0.000	0.000
30	A	127	SER	0	-0.021	-0.019	11.273	-0.127	-0.127	0.000	0.000	0.000	0.000
31	A	128	ARG	1	0.882	0.967	12.534	-0.416	-0.416	0.000	0.000	0.000	0.000
32	A	129	LEU	0	0.023	0.019	9.635	0.075	0.075	0.000	0.000	0.000	0.000
33	A	130	ALA	0	0.002	0.017	14.008	-0.114	-0.114	0.000	0.000	0.000	0.000
34	A	131	PHE	0	-0.032	-0.029	14.715	0.083	0.083	0.000	0.000	0.000	0.000
35	A	132	LYS	1	0.931	0.977	15.530	-0.381	-0.381	0.000	0.000	0.000	0.000
36	A	133	VAL	0	-0.023	-0.011	15.589	0.032	0.032	0.000	0.000	0.000	0.000
37	A	134	LYS	1	0.872	0.949	15.657	-0.245	-0.245	0.000	0.000	0.000	0.000
38	A	135	SER	0	0.013	0.001	17.225	-0.007	-0.007	0.000	0.000	0.000	0.000
39	A	136	SER	0	-0.031	-0.017	19.087	-0.005	-0.005	0.000	0.000	0.000	0.000
40	A	137	ASN	0	0.035	-0.007	20.853	-0.004	-0.004	0.000	0.000	0.000	0.000
41	A	138	ASN	0	-0.071	-0.041	23.782	0.019	0.019	0.000	0.000	0.000	0.000
42	A	139	GLU	-1	-0.909	-0.958	25.786	0.023	0.023	0.000	0.000	0.000	0.000
43	A	140	HIS	0	0.046	0.074	26.387	-0.006	-0.006	0.000	0.000	0.000	0.000
44	A	141	TYR	0	-0.003	-0.008	22.885	0.010	0.010	0.000	0.000	0.000	0.000
45	A	142	ARG	1	0.944	0.979	25.062	-0.125	-0.125	0.000	0.000	0.000	0.000
46	A	143	VAL	0	0.008	-0.010	19.160	0.003	0.003	0.000	0.000	0.000	0.000
47	A	144	ARG	1	0.898	0.966	22.320	-0.175	-0.175	0.000	0.000	0.000	0.000
48	A	145	PRO	0	0.059	0.049	20.502	0.000	0.000	0.000	0.000	0.000	0.000
49	A	146	VAL	0	-0.004	-0.006	21.006	0.005	0.005	0.000	0.000	0.000	0.000
50	A	147	TYR	0	0.036	-0.001	19.679	0.026	0.026	0.000	0.000	0.000	0.000
51	A	148	GLY	0	0.021	0.002	19.772	-0.034	-0.034	0.000	0.000	0.000	0.000
52	A	149	PHE	0	0.040	0.030	17.858	0.053	0.053	0.000	0.000	0.000	0.000
53	A	150	VAL	0	-0.013	0.010	13.788	-0.027	-0.027	0.000	0.000	0.000	0.000
54	A	151	ASP	-1	-0.907	-0.954	14.846	0.471	0.471	0.000	0.000	0.000	0.000
55	A	152	ALA	0	0.033	0.012	13.149	0.060	0.060	0.000	0.000	0.000	0.000
56	A	153	LYS	1	0.885	0.961	9.919	-0.518	-0.518	0.000	0.000	0.000	0.000
57	A	154	GLY	0	0.021	0.025	12.520	-0.062	-0.062	0.000	0.000	0.000	0.000
58	A	155	LYS	1	0.951	0.952	14.202	-0.289	-0.289	0.000	0.000	0.000	0.000
59	A	156	SER	0	-0.003	-0.016	16.441	-0.047	-0.047	0.000	0.000	0.000	0.000
60	A	157	LYS	1	0.819	0.922	17.622	-0.208	-0.208	0.000	0.000	0.000	0.000
61	A	158	LEU	0	-0.010	0.000	16.037	-0.008	-0.008	0.000	0.000	0.000	0.000
62	A	159	ASP	-1	-0.819	-0.934	19.582	0.223	0.223	0.000	0.000	0.000	0.000
63	A	160	ILE	0	-0.006	0.011	17.583	-0.005	-0.005	0.000	0.000	0.000	0.000
64	A	161	ASN	0	-0.047	-0.032	22.171	-0.009	-0.009	0.000	0.000	0.000	0.000
65	A	162	ARG	1	0.837	0.948	25.126	-0.033	-0.033	0.000	0.000	0.000	0.000
66	A	163	LEU	0	-0.034	-0.015	26.602	0.002	0.002	0.000	0.000	0.000	0.000
67	A	164	PRO	0	0.011	-0.012	29.722	-0.005	-0.005	0.000	0.000	0.000	0.000
68	A	165	GLY	0	0.033	0.020	30.392	0.002	0.002	0.000	0.000	0.000	0.000
69	A	166	PRO	0	-0.030	-0.010	28.842	-0.002	-0.002	0.000	0.000	0.000	0.000
70	A	167	PRO	0	0.002	-0.003	27.855	0.005	0.005	0.000	0.000	0.000	0.000
71	A	168	LYS	1	0.894	0.958	23.547	0.043	0.043	0.000	0.000	0.000	0.000
72	A	169	GLU	-1	-0.929	-0.961	19.686	-0.124	-0.124	0.000	0.000	0.000	0.000
73	A	170	ASP	-1	-0.820	-0.924	20.032	-0.021	-0.021	0.000	0.000	0.000	0.000
74	A	171	LYS	1	0.952	0.967	14.451	0.147	0.147	0.000	0.000	0.000	0.000
75	A	172	ILE	0	0.019	0.012	14.457	0.006	0.006	0.000	0.000	0.000	0.000
76	A	173	VAL	0	-0.063	-0.026	11.424	-0.006	-0.006	0.000	0.000	0.000	0.000
77	A	174	ILE	0	-0.004	-0.001	11.419	-0.030	-0.030	0.000	0.000	0.000	0.000
78	A	175	GLN	0	-0.014	-0.010	10.851	0.093	0.093	0.000	0.000	0.000	0.000
79	A	176	TYR	0	0.018	-0.013	5.412	-0.133	-0.133	0.000	0.000	0.000	0.000
80	A	177	ALA	0	0.036	0.016	12.045	0.016	0.016	0.000	0.000	0.000	0.000
81	A	178	GLU	-1	-0.898	-0.949	9.425	1.639	1.639	0.000	0.000	0.000	0.000
82	A	179	VAL	0	-0.051	-0.033	13.287	-0.097	-0.097	0.000	0.000	0.000	0.000
83	A	180	PRO	0	0.043	0.022	16.797	0.007	0.007	0.000	0.000	0.000	0.000
84	A	181	ALA	0	-0.015	-0.030	19.141	-0.012	-0.012	0.000	0.000	0.000	0.000
85	A	182	GLU	-1	-0.971	-0.990	20.881	0.276	0.276	0.000	0.000	0.000	0.000
86	A	183	GLU	-1	-0.892	-0.940	20.824	0.322	0.322	0.000	0.000	0.000	0.000
87	A	184	THR	0	-0.003	0.002	22.837	0.000	0.000	0.000	0.000	0.000	0.000
88	A	185	ASP	-1	-0.868	-0.961	24.627	0.282	0.282	0.000	0.000	0.000	0.000
89	A	186	PRO	0	-0.019	-0.001	20.740	0.029	0.029	0.000	0.000	0.000	0.000
90	A	187	MET	0	-0.042	-0.046	20.247	0.023	0.023	0.000	0.000	0.000	0.000
91	A	188	ALA	0	0.039	0.050	22.138	-0.004	-0.004	0.000	0.000	0.000	0.000
92	A	189	PRO	0	0.053	0.025	17.139	-0.019	-0.019	0.000	0.000	0.000	0.000
93	A	190	PHE	0	-0.035	-0.029	14.906	0.001	0.001	0.000	0.000	0.000	0.000
94	A	191	LYS	1	0.866	0.929	19.560	-0.253	-0.253	0.000	0.000	0.000	0.000
95	A	192	ALA	0	0.009	0.016	20.365	-0.030	-0.030	0.000	0.000	0.000	0.000
96	A	193	GLY	0	-0.079	-0.020	18.988	-0.011	-0.011	0.000	0.000	0.000	0.000
97	A	194	ALA	0	0.025	-0.003	16.123	0.002	0.002	0.000	0.000	0.000	0.000
98	A	195	GLN	0	-0.040	-0.009	13.245	0.129	0.129	0.000	0.000	0.000	0.000
99	A	196	GLN	0	0.017	0.001	8.908	-0.323	-0.323	0.000	0.000	0.000	0.000
100	A	197	GLY	0	0.007	0.005	7.735	0.379	0.379	0.000	0.000	0.000	0.000
101	A	198	GLU	-1	-0.958	-1.006	7.514	-0.129	-0.129	0.000	0.000	0.000	0.000
102	A	199	ILE	0	0.028	0.041	5.717	-0.305	-0.305	0.000	0.000	0.000	0.000
103	A	200	ILE	0	-0.039	-0.029	7.944	-0.118	-0.118	0.000	0.000	0.000	0.000
104	A	201	VAL	0	-0.005	0.004	10.437	-0.036	-0.036	0.000	0.000	0.000	0.000
105	A	202	LYS	1	0.975	0.978	12.435	0.231	0.231	0.000	0.000	0.000	0.000
106	A	203	LEU	0	0.011	-0.008	15.169	0.048	0.048	0.000	0.000	0.000	0.000
107	A	204	ILE	0	0.032	0.028	18.186	-0.020	-0.020	0.000	0.000	0.000	0.000
108	A	205	ALA	0	-0.025	-0.002	21.142	0.019	0.019	0.000	0.000	0.000	0.000
109	A	206	ALA	0	0.049	0.028	24.802	-0.008	-0.008	0.000	0.000	0.000	0.000

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