FMO DATABASE

FMODB ID: NNZMQ

Calculation Name: 2H36-X-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2H36

Chain ID: X

ChEMBL ID:

UniProt ID: Q914L6

Base Structure: X-ray

Registration Date: 2023-09-22

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	108
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-862444.837452
FMO2-HF: Nuclear repulsion	816850.821933
FMO2-HF: Total energy	-45594.015518
FMO2-MP2: Total energy	-45728.06616

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(X:2:LYS)

Summations of interaction energy for fragment #1(X:2:LYS)

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.
-175.192	-169.95	0.096	-2.501	-2.838	-0.015

Interaction energy analysis for fragmet #1(X:2:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.931 / q_NPA : 0.950

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	X	4	ASP	-1	-0.840	-0.906	3.180	-40.426	-35.184	0.096	-2.501	-2.838	-0.015
4	X	5	LEU	0	-0.030	-0.017	4.867	2.299	2.299	0.000	0.000	0.000	0.000
5	X	6	GLU	-1	-0.910	-0.948	7.136	-23.499	-23.499	0.000	0.000	0.000	0.000
6	X	7	LYS	1	0.919	0.947	8.474	21.244	21.244	0.000	0.000	0.000	0.000
7	X	8	ILE	0	-0.029	-0.015	8.228	1.109	1.109	0.000	0.000	0.000	0.000
8	X	9	GLU	-1	-0.957	-0.974	11.103	-21.932	-21.932	0.000	0.000	0.000	0.000
9	X	10	SER	0	-0.086	-0.041	12.864	1.299	1.299	0.000	0.000	0.000	0.000
10	X	11	ASP	-1	-0.985	-0.982	13.963	-15.269	-15.269	0.000	0.000	0.000	0.000
11	X	12	ILE	0	-0.046	-0.017	15.754	0.298	0.298	0.000	0.000	0.000	0.000
12	X	13	ILE	0	-0.038	0.004	18.607	0.034	0.034	0.000	0.000	0.000	0.000
13	X	14	ASN	0	-0.014	0.006	21.097	-0.060	-0.060	0.000	0.000	0.000	0.000
14	X	15	ASP	-1	-0.943	-1.034	23.195	-11.210	-11.210	0.000	0.000	0.000	0.000
15	X	16	TRP	0	-0.132	-0.035	26.045	-0.072	-0.072	0.000	0.000	0.000	0.000
16	X	17	THR	0	-0.053	-0.003	28.288	-0.265	-0.265	0.000	0.000	0.000	0.000
17	X	18	GLU	-1	-0.911	-0.979	30.908	-8.436	-8.436	0.000	0.000	0.000	0.000
18	X	19	ALA	0	-0.012	-0.016	34.255	0.244	0.244	0.000	0.000	0.000	0.000
19	X	20	ASP	-1	-0.762	-0.888	31.461	-9.175	-9.175	0.000	0.000	0.000	0.000
20	X	21	ASP	-1	-0.871	-0.933	34.790	-8.147	-8.147	0.000	0.000	0.000	0.000
21	X	22	LEU	0	-0.087	-0.045	36.292	0.273	0.273	0.000	0.000	0.000	0.000
22	X	23	ASP	-1	-0.888	-0.954	37.812	-7.565	-7.565	0.000	0.000	0.000	0.000
23	X	24	ASP	-1	-0.881	-0.930	37.570	-7.752	-7.752	0.000	0.000	0.000	0.000
24	X	25	ALA	0	-0.078	-0.035	39.561	0.213	0.213	0.000	0.000	0.000	0.000
25	X	26	LEU	0	-0.054	-0.045	42.416	0.256	0.256	0.000	0.000	0.000	0.000
26	X	27	ASP	-1	-0.812	-0.903	41.479	-7.131	-7.131	0.000	0.000	0.000	0.000
27	X	28	PHE	0	-0.124	-0.059	44.021	0.250	0.250	0.000	0.000	0.000	0.000
28	X	29	LEU	0	-0.066	-0.060	45.762	0.201	0.201	0.000	0.000	0.000	0.000
29	X	30	PHE	0	0.056	0.031	47.414	0.152	0.152	0.000	0.000	0.000	0.000
30	X	31	MET	0	-0.091	-0.035	48.311	0.135	0.135	0.000	0.000	0.000	0.000
31	X	32	GLU	-1	-0.895	-0.957	50.800	-5.419	-5.419	0.000	0.000	0.000	0.000
32	X	33	LYS	1	0.852	0.928	51.432	5.923	5.923	0.000	0.000	0.000	0.000
33	X	34	VAL	0	-0.046	0.000	50.720	0.099	0.099	0.000	0.000	0.000	0.000
34	X	35	SER	0	0.010	-0.006	54.098	0.004	0.004	0.000	0.000	0.000	0.000
35	X	36	GLU	-1	-0.957	-0.983	54.791	-5.286	-5.286	0.000	0.000	0.000	0.000
36	X	37	PHE	0	-0.036	0.003	48.177	0.008	0.008	0.000	0.000	0.000	0.000
37	X	38	LYS	1	0.954	0.969	51.283	5.747	5.747	0.000	0.000	0.000	0.000
38	X	39	ILE	0	-0.017	0.002	44.822	0.024	0.024	0.000	0.000	0.000	0.000
39	X	40	LYS	1	0.901	0.941	48.044	5.877	5.877	0.000	0.000	0.000	0.000
40	X	41	PHE	0	0.012	0.008	41.626	-0.001	-0.001	0.000	0.000	0.000	0.000
41	X	42	LYS	1	0.859	0.931	44.315	6.663	6.663	0.000	0.000	0.000	0.000
42	X	43	ASP	-1	-0.930	-0.958	40.376	-7.242	-7.242	0.000	0.000	0.000	0.000
43	X	44	PRO	0	-0.042	-0.034	40.986	0.012	0.012	0.000	0.000	0.000	0.000
44	X	45	LEU	0	0.045	0.029	37.596	-0.130	-0.130	0.000	0.000	0.000	0.000
45	X	46	LYS	1	0.888	0.943	32.763	9.171	9.171	0.000	0.000	0.000	0.000
46	X	47	VAL	0	0.100	0.073	35.693	-0.081	-0.081	0.000	0.000	0.000	0.000
47	X	48	THR	0	-0.021	-0.002	32.338	0.179	0.179	0.000	0.000	0.000	0.000
48	X	49	GLU	-1	-0.828	-0.929	35.763	-7.963	-7.963	0.000	0.000	0.000	0.000
49	X	50	GLU	-1	-0.998	-1.012	32.954	-9.233	-9.233	0.000	0.000	0.000	0.000
50	X	51	GLU	-1	-0.699	-0.854	32.296	-9.199	-9.199	0.000	0.000	0.000	0.000
51	X	52	TYR	0	-0.057	-0.070	36.415	0.163	0.163	0.000	0.000	0.000	0.000
52	X	53	ARG	1	0.874	0.930	37.736	8.297	8.297	0.000	0.000	0.000	0.000
53	X	54	GLU	-1	-0.950	-0.974	35.321	-8.680	-8.680	0.000	0.000	0.000	0.000
54	X	55	LEU	0	-0.009	0.015	38.872	0.092	0.092	0.000	0.000	0.000	0.000
55	X	56	LEU	0	-0.106	-0.025	41.418	0.186	0.186	0.000	0.000	0.000	0.000
56	X	57	GLY	0	0.028	0.028	43.263	0.167	0.167	0.000	0.000	0.000	0.000
57	X	58	ASN	0	-0.081	-0.039	44.355	0.045	0.045	0.000	0.000	0.000	0.000
58	X	59	TYR	0	0.030	0.048	46.452	0.104	0.104	0.000	0.000	0.000	0.000
59	X	60	ASP	-1	-0.822	-0.914	50.436	-5.930	-5.930	0.000	0.000	0.000	0.000
60	X	61	SER	0	-0.108	-0.064	53.767	0.057	0.057	0.000	0.000	0.000	0.000
61	X	62	SER	0	0.020	0.010	51.022	-0.031	-0.031	0.000	0.000	0.000	0.000
62	X	63	ASN	0	-0.044	-0.016	53.665	0.091	0.091	0.000	0.000	0.000	0.000
63	X	64	SER	0	0.035	0.035	51.164	-0.006	-0.006	0.000	0.000	0.000	0.000
64	X	65	VAL	0	-0.047	-0.024	53.521	0.089	0.089	0.000	0.000	0.000	0.000
65	X	66	SER	0	-0.001	-0.040	51.442	-0.094	-0.094	0.000	0.000	0.000	0.000
66	X	67	SER	0	0.001	0.046	53.557	0.014	0.014	0.000	0.000	0.000	0.000
67	X	68	ASN	0	-0.042	-0.031	53.440	-0.045	-0.045	0.000	0.000	0.000	0.000
68	X	69	GLY	0	0.007	-0.012	49.199	-0.043	-0.043	0.000	0.000	0.000	0.000
69	X	70	ILE	0	-0.039	-0.017	48.380	-0.137	-0.137	0.000	0.000	0.000	0.000
70	X	71	THR	0	0.006	0.012	48.455	0.125	0.125	0.000	0.000	0.000	0.000
71	X	72	ILE	0	-0.032	0.005	49.834	-0.083	-0.083	0.000	0.000	0.000	0.000
72	X	73	ASP	-1	-0.775	-0.860	48.049	-6.459	-6.459	0.000	0.000	0.000	0.000
73	X	74	GLN	0	-0.039	-0.019	50.964	0.035	0.035	0.000	0.000	0.000	0.000
74	X	75	TYR	0	-0.038	-0.065	47.590	-0.038	-0.038	0.000	0.000	0.000	0.000
75	X	76	THR	0	-0.003	0.006	52.031	0.115	0.115	0.000	0.000	0.000	0.000
76	X	77	TYR	0	-0.034	-0.066	47.247	-0.057	-0.057	0.000	0.000	0.000	0.000
77	X	78	ASP	-1	-0.919	-0.958	53.800	-5.401	-5.401	0.000	0.000	0.000	0.000
78	X	79	GLU	-1	-0.831	-0.913	54.449	-5.771	-5.771	0.000	0.000	0.000	0.000
79	X	80	ASP	-1	-0.944	-0.973	56.990	-5.447	-5.447	0.000	0.000	0.000	0.000
80	X	81	ASP	-1	-1.026	-1.023	59.723	-4.942	-4.942	0.000	0.000	0.000	0.000
81	X	82	ASP	-1	-0.979	-0.989	62.809	-4.809	-4.809	0.000	0.000	0.000	0.000
82	X	83	ILE	0	-0.077	-0.033	58.794	0.060	0.060	0.000	0.000	0.000	0.000
83	X	84	MET	0	0.022	0.017	58.152	-0.085	-0.085	0.000	0.000	0.000	0.000
84	X	85	TYR	0	-0.012	-0.008	51.629	0.026	0.026	0.000	0.000	0.000	0.000
85	X	86	LYS	1	0.834	0.915	54.428	5.391	5.391	0.000	0.000	0.000	0.000
86	X	87	LEU	0	0.019	0.017	46.721	0.002	0.002	0.000	0.000	0.000	0.000
87	X	88	GLU	-1	-0.904	-0.970	51.005	-5.725	-5.725	0.000	0.000	0.000	0.000
88	X	89	PHE	0	0.054	0.017	44.139	-0.047	-0.047	0.000	0.000	0.000	0.000
89	X	90	THR	0	-0.003	0.002	48.496	0.075	0.075	0.000	0.000	0.000	0.000
90	X	91	TYR	0	-0.003	-0.026	44.555	-0.150	-0.150	0.000	0.000	0.000	0.000
91	X	92	ARG	1	0.887	0.978	44.976	6.971	6.971	0.000	0.000	0.000	0.000
92	X	93	LYS	1	0.867	0.916	41.091	7.435	7.435	0.000	0.000	0.000	0.000
93	X	94	GLU	-1	-1.021	-0.980	40.539	-7.328	-7.328	0.000	0.000	0.000	0.000
94	X	95	ASP	-1	-0.779	-0.915	38.321	-7.736	-7.736	0.000	0.000	0.000	0.000
95	X	96	ASN	0	-0.145	-0.074	36.324	-0.514	-0.514	0.000	0.000	0.000	0.000
96	X	97	LYS	1	0.893	0.946	33.243	9.021	9.021	0.000	0.000	0.000	0.000
97	X	98	ILE	0	-0.018	-0.018	37.630	0.183	0.183	0.000	0.000	0.000	0.000
98	X	99	TYR	0	0.005	0.000	37.296	-0.229	-0.229	0.000	0.000	0.000	0.000
99	X	100	ILE	0	0.062	0.033	41.031	0.246	0.246	0.000	0.000	0.000	0.000
100	X	101	TYR	0	-0.034	-0.037	43.447	-0.071	-0.071	0.000	0.000	0.000	0.000
101	X	102	GLU	-1	-0.980	-0.997	46.141	-5.871	-5.871	0.000	0.000	0.000	0.000
102	X	103	VAL	0	0.061	0.059	44.927	-0.004	-0.004	0.000	0.000	0.000	0.000
103	X	104	GLN	0	-0.066	-0.019	48.269	0.147	0.147	0.000	0.000	0.000	0.000
104	X	105	GLY	0	0.081	0.040	51.321	-0.081	-0.081	0.000	0.000	0.000	0.000
105	X	106	TRP	0	-0.066	-0.031	52.617	0.039	0.039	0.000	0.000	0.000	0.000
106	X	107	ARG	1	0.834	0.930	53.069	5.665	5.665	0.000	0.000	0.000	0.000
107	X	108	GLU	-1	-0.911	-0.957	58.289	-5.121	-5.121	0.000	0.000	0.000	0.000
108	X	109	LYS	1	0.953	0.989	61.562	4.681	4.681	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(X:2:LYS)