FMO DATABASE

FMODB ID: 3JK5L

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	OptAll
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	-860675.427982
FMO2-HF: Nuclear repulsion	815079.391552
FMO2-HF: Total energy	-45596.036429
FMO2-MP2: Total energy	-45729.90906

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.
-188.008	-182.292	3.812	-4.531	-4.997	-0.047

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 : 0.939 / q_NPA : 0.954

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	-0.879	-0.939	2.419	-53.180	-47.711	3.813	-4.503	-4.779	-0.047
4	X	5	LEU	0	-0.004	-0.005	4.783	3.472	3.719	-0.001	-0.028	-0.218	0.000
5	X	6	GLU	-1	-0.878	-0.924	6.859	-23.609	-23.609	0.000	0.000	0.000	0.000
6	X	7	LYS	1	0.780	0.862	8.380	21.364	21.364	0.000	0.000	0.000	0.000
7	X	8	ILE	0	-0.052	-0.025	7.725	1.368	1.368	0.000	0.000	0.000	0.000
8	X	9	GLU	-1	-0.964	-0.980	10.887	-22.567	-22.567	0.000	0.000	0.000	0.000
9	X	10	SER	0	-0.046	-0.023	12.795	1.327	1.327	0.000	0.000	0.000	0.000
10	X	11	ASP	-1	-0.848	-0.887	14.020	-17.153	-17.153	0.000	0.000	0.000	0.000
11	X	12	ILE	0	-0.038	-0.020	15.678	0.244	0.244	0.000	0.000	0.000	0.000
12	X	13	ILE	0	-0.069	-0.018	17.402	0.016	0.016	0.000	0.000	0.000	0.000
13	X	14	ASN	0	-0.056	-0.016	20.563	-0.209	-0.209	0.000	0.000	0.000	0.000
14	X	15	ASP	-1	-0.888	-0.981	22.672	-11.605	-11.605	0.000	0.000	0.000	0.000
15	X	16	TRP	0	-0.102	-0.040	25.765	-0.033	-0.033	0.000	0.000	0.000	0.000
16	X	17	THR	0	-0.053	-0.040	27.845	-0.329	-0.329	0.000	0.000	0.000	0.000
17	X	18	GLU	-1	-0.857	-0.945	30.530	-8.423	-8.423	0.000	0.000	0.000	0.000
18	X	19	ALA	0	-0.024	-0.013	33.871	0.272	0.272	0.000	0.000	0.000	0.000
19	X	20	ASP	-1	-0.748	-0.886	31.314	-9.157	-9.157	0.000	0.000	0.000	0.000
20	X	21	ASP	-1	-0.927	-0.945	34.702	-8.160	-8.160	0.000	0.000	0.000	0.000
21	X	22	LEU	0	-0.059	-0.028	36.227	0.262	0.262	0.000	0.000	0.000	0.000
22	X	23	ASP	-1	-0.866	-0.945	37.806	-7.495	-7.495	0.000	0.000	0.000	0.000
23	X	24	ASP	-1	-0.941	-0.962	37.296	-7.617	-7.617	0.000	0.000	0.000	0.000
24	X	25	ALA	0	-0.035	-0.022	39.407	0.216	0.216	0.000	0.000	0.000	0.000
25	X	26	LEU	0	-0.033	-0.032	42.150	0.239	0.239	0.000	0.000	0.000	0.000
26	X	27	ASP	-1	-0.882	-0.931	42.093	-6.855	-6.855	0.000	0.000	0.000	0.000
27	X	28	PHE	0	-0.047	-0.033	43.934	0.248	0.248	0.000	0.000	0.000	0.000
28	X	29	LEU	0	-0.074	-0.052	45.816	0.197	0.197	0.000	0.000	0.000	0.000
29	X	30	PHE	0	0.063	0.048	46.457	0.162	0.162	0.000	0.000	0.000	0.000
30	X	31	MET	0	-0.074	-0.008	47.121	0.175	0.175	0.000	0.000	0.000	0.000
31	X	32	GLU	-1	-0.902	-0.958	50.576	-5.408	-5.408	0.000	0.000	0.000	0.000
32	X	33	LYS	1	0.861	0.919	50.634	6.014	6.014	0.000	0.000	0.000	0.000
33	X	34	VAL	0	-0.049	-0.005	50.735	0.061	0.061	0.000	0.000	0.000	0.000
34	X	35	SER	0	-0.051	-0.040	54.163	-0.016	-0.016	0.000	0.000	0.000	0.000
35	X	36	GLU	-1	-0.886	-0.934	54.673	-5.263	-5.263	0.000	0.000	0.000	0.000
36	X	37	PHE	0	-0.012	-0.003	47.550	-0.027	-0.027	0.000	0.000	0.000	0.000
37	X	38	LYS	1	0.777	0.861	50.916	5.786	5.786	0.000	0.000	0.000	0.000
38	X	39	ILE	0	0.007	0.017	44.683	0.024	0.024	0.000	0.000	0.000	0.000
39	X	40	LYS	1	0.888	0.953	47.373	5.848	5.848	0.000	0.000	0.000	0.000
40	X	41	PHE	0	0.028	0.016	41.002	-0.029	-0.029	0.000	0.000	0.000	0.000
41	X	42	LYS	1	0.741	0.846	42.399	7.071	7.071	0.000	0.000	0.000	0.000
42	X	43	ASP	-1	-0.825	-0.898	39.990	-7.205	-7.205	0.000	0.000	0.000	0.000
43	X	44	PRO	0	-0.059	-0.019	40.581	-0.026	-0.026	0.000	0.000	0.000	0.000
44	X	45	LEU	0	0.053	0.035	37.061	-0.130	-0.130	0.000	0.000	0.000	0.000
45	X	46	LYS	1	0.868	0.934	33.116	9.022	9.022	0.000	0.000	0.000	0.000
46	X	47	VAL	0	0.056	0.041	35.322	-0.150	-0.150	0.000	0.000	0.000	0.000
47	X	48	THR	0	-0.066	-0.080	32.372	0.157	0.157	0.000	0.000	0.000	0.000
48	X	49	GLU	-1	-0.855	-0.960	35.652	-7.747	-7.747	0.000	0.000	0.000	0.000
49	X	50	GLU	-1	-0.933	-0.964	33.183	-8.971	-8.971	0.000	0.000	0.000	0.000
50	X	51	GLU	-1	-0.654	-0.770	32.747	-9.169	-9.169	0.000	0.000	0.000	0.000
51	X	52	TYR	0	-0.050	-0.048	36.166	0.154	0.154	0.000	0.000	0.000	0.000
52	X	53	ARG	1	0.824	0.894	37.014	8.392	8.392	0.000	0.000	0.000	0.000
53	X	54	GLU	-1	-0.972	-0.967	34.911	-8.630	-8.630	0.000	0.000	0.000	0.000
54	X	55	LEU	0	0.009	0.001	37.783	0.138	0.138	0.000	0.000	0.000	0.000
55	X	56	LEU	0	-0.049	-0.006	40.971	0.200	0.200	0.000	0.000	0.000	0.000
56	X	57	GLY	0	0.005	0.017	42.730	0.174	0.174	0.000	0.000	0.000	0.000
57	X	58	ASN	0	-0.112	-0.060	43.971	0.036	0.036	0.000	0.000	0.000	0.000
58	X	59	TYR	0	0.029	0.028	46.455	0.057	0.057	0.000	0.000	0.000	0.000
59	X	60	ASP	-1	-0.840	-0.908	49.833	-5.962	-5.962	0.000	0.000	0.000	0.000
60	X	61	SER	0	-0.073	-0.045	53.259	0.080	0.080	0.000	0.000	0.000	0.000
61	X	62	SER	0	0.010	0.012	50.811	-0.046	-0.046	0.000	0.000	0.000	0.000
62	X	63	ASN	0	-0.075	-0.030	53.289	0.117	0.117	0.000	0.000	0.000	0.000
63	X	64	SER	0	0.010	0.016	51.054	-0.010	-0.010	0.000	0.000	0.000	0.000
64	X	65	VAL	0	-0.034	-0.015	53.465	0.100	0.100	0.000	0.000	0.000	0.000
65	X	66	SER	0	0.033	0.021	51.309	-0.095	-0.095	0.000	0.000	0.000	0.000
66	X	67	SER	0	-0.063	-0.023	53.142	0.122	0.122	0.000	0.000	0.000	0.000
67	X	68	ASN	0	-0.042	-0.037	53.102	-0.037	-0.037	0.000	0.000	0.000	0.000
68	X	69	GLY	0	0.013	0.009	48.806	-0.040	-0.040	0.000	0.000	0.000	0.000
69	X	70	ILE	0	-0.031	-0.014	47.857	-0.142	-0.142	0.000	0.000	0.000	0.000
70	X	71	THR	0	0.009	-0.004	48.213	0.159	0.159	0.000	0.000	0.000	0.000
71	X	72	ILE	0	-0.016	0.001	49.445	-0.072	-0.072	0.000	0.000	0.000	0.000
72	X	73	ASP	-1	-0.778	-0.865	47.467	-6.484	-6.484	0.000	0.000	0.000	0.000
73	X	74	GLN	0	-0.015	-0.009	50.098	-0.012	-0.012	0.000	0.000	0.000	0.000
74	X	75	TYR	0	-0.003	-0.029	47.823	-0.027	-0.027	0.000	0.000	0.000	0.000
75	X	76	THR	0	0.002	-0.005	51.796	0.068	0.068	0.000	0.000	0.000	0.000
76	X	77	TYR	0	-0.023	-0.027	46.817	-0.051	-0.051	0.000	0.000	0.000	0.000
77	X	78	ASP	-1	-0.919	-0.962	53.216	-5.422	-5.422	0.000	0.000	0.000	0.000
78	X	79	GLU	-1	-0.863	-0.938	54.139	-5.777	-5.777	0.000	0.000	0.000	0.000
79	X	80	ASP	-1	-0.933	-0.971	57.125	-5.379	-5.379	0.000	0.000	0.000	0.000
80	X	81	ASP	-1	-0.997	-1.006	59.733	-4.938	-4.938	0.000	0.000	0.000	0.000
81	X	82	ASP	-1	-0.963	-0.972	62.740	-4.805	-4.805	0.000	0.000	0.000	0.000
82	X	83	ILE	0	-0.060	-0.003	58.405	0.060	0.060	0.000	0.000	0.000	0.000
83	X	84	MET	0	-0.021	0.001	57.683	-0.047	-0.047	0.000	0.000	0.000	0.000
84	X	85	TYR	0	0.019	0.002	50.508	0.034	0.034	0.000	0.000	0.000	0.000
85	X	86	LYS	1	0.832	0.921	54.203	5.469	5.469	0.000	0.000	0.000	0.000
86	X	87	LEU	0	0.032	0.020	46.228	-0.012	-0.012	0.000	0.000	0.000	0.000
87	X	88	GLU	-1	-0.859	-0.929	50.230	-5.687	-5.687	0.000	0.000	0.000	0.000
88	X	89	PHE	0	0.061	0.035	43.494	-0.069	-0.069	0.000	0.000	0.000	0.000
89	X	90	THR	0	-0.032	-0.019	47.871	0.141	0.141	0.000	0.000	0.000	0.000
90	X	91	TYR	0	-0.064	-0.055	44.024	-0.133	-0.133	0.000	0.000	0.000	0.000
91	X	92	ARG	1	0.793	0.882	44.119	7.070	7.070	0.000	0.000	0.000	0.000
92	X	93	LYS	1	0.855	0.910	41.765	7.328	7.328	0.000	0.000	0.000	0.000
93	X	94	GLU	-1	-0.865	-0.887	40.618	-7.087	-7.087	0.000	0.000	0.000	0.000
94	X	95	ASP	-1	-0.775	-0.889	38.291	-7.716	-7.716	0.000	0.000	0.000	0.000
95	X	96	ASN	0	-0.080	-0.036	35.927	-0.541	-0.541	0.000	0.000	0.000	0.000
96	X	97	LYS	1	0.832	0.919	32.942	8.774	8.774	0.000	0.000	0.000	0.000
97	X	98	ILE	0	-0.003	-0.002	37.399	0.200	0.200	0.000	0.000	0.000	0.000
98	X	99	TYR	0	0.002	0.007	36.876	-0.297	-0.297	0.000	0.000	0.000	0.000
99	X	100	ILE	0	0.064	0.022	40.718	0.254	0.254	0.000	0.000	0.000	0.000
100	X	101	TYR	0	-0.008	-0.019	43.044	-0.058	-0.058	0.000	0.000	0.000	0.000
101	X	102	GLU	-1	-0.902	-0.963	45.725	-5.817	-5.817	0.000	0.000	0.000	0.000
102	X	103	VAL	0	0.041	0.040	44.312	-0.052	-0.052	0.000	0.000	0.000	0.000
103	X	104	GLN	0	-0.032	-0.018	47.657	0.115	0.115	0.000	0.000	0.000	0.000
104	X	105	GLY	0	0.082	0.038	50.707	-0.085	-0.085	0.000	0.000	0.000	0.000
105	X	106	TRP	0	-0.129	-0.070	52.461	0.011	0.011	0.000	0.000	0.000	0.000
106	X	107	ARG	1	0.819	0.927	52.813	5.670	5.670	0.000	0.000	0.000	0.000
107	X	108	GLU	-1	-0.899	-0.942	58.021	-5.162	-5.162	0.000	0.000	0.000	0.000
108	X	109	LYS	1	0.905	0.931	61.125	4.749	4.749	0.000	0.000	0.000	0.000

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