FMO DATABASE

FMODB ID: 89GQY

Calculation Name: 2QHE-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2QHE

Chain ID: A

ChEMBL ID:

UniProt ID: P48650

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	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	115
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1033802.80532
FMO2-HF: Nuclear repulsion	982009.708529
FMO2-HF: Total energy	-51793.096791
FMO2-MP2: Total energy	-51932.541322

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:1:SER)

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

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.
-53.208	-58.085	58.654	-26.818	-26.958	-0.086

Interaction energy analysis for fragmet #1(A:1:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.019 / q_NPA : 0.003

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

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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	3	VAL	0	-0.045	-0.010	2.292	-9.002	-3.820	2.265	-3.429	-4.018	0.029
4	A	4	GLU	-1	-0.725	-0.841	1.590	-26.573	-38.225	29.146	-11.357	-6.138	-0.100
5	A	5	LEU	0	0.027	0.032	3.782	2.360	2.772	-0.001	-0.122	-0.289	0.000
6	A	6	GLY	0	0.035	-0.006	5.391	1.236	1.329	-0.001	-0.005	-0.086	0.000
7	A	7	LYS	1	0.914	0.975	7.228	1.736	1.736	0.000	0.000	0.000	0.000
8	A	8	MET	0	0.010	0.015	6.447	0.594	0.594	0.000	0.000	0.000	0.000
9	A	9	ILE	0	0.012	0.013	9.340	0.387	0.387	0.000	0.000	0.000	0.000
10	A	10	ILE	0	-0.006	0.011	11.167	0.234	0.234	0.000	0.000	0.000	0.000
11	A	11	GLN	0	-0.032	-0.012	12.557	0.018	0.018	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.788	-0.854	13.159	-0.714	-0.714	0.000	0.000	0.000	0.000
13	A	13	THR	0	-0.045	-0.047	15.095	0.119	0.119	0.000	0.000	0.000	0.000
14	A	14	GLY	0	-0.001	0.018	16.686	0.073	0.073	0.000	0.000	0.000	0.000
15	A	16	LYS	1	0.838	0.940	16.788	0.444	0.444	0.000	0.000	0.000	0.000
16	A	17	SER	0	0.052	0.014	13.664	-0.128	-0.128	0.000	0.000	0.000	0.000
17	A	18	PRO	0	0.033	0.012	9.702	0.072	0.072	0.000	0.000	0.000	0.000
18	A	19	PHE	0	-0.011	0.049	12.622	0.056	0.056	0.000	0.000	0.000	0.000
19	A	20	PRO	0	0.001	-0.023	14.526	0.020	0.020	0.000	0.000	0.000	0.000
20	A	21	SER	0	-0.032	-0.019	16.669	0.007	0.007	0.000	0.000	0.000	0.000
21	A	22	TYR	0	0.078	0.007	13.731	-0.001	-0.001	0.000	0.000	0.000	0.000
22	A	23	THR	0	-0.005	-0.011	11.887	-0.027	-0.027	0.000	0.000	0.000	0.000
23	A	24	SER	0	0.000	-0.004	14.097	0.033	0.033	0.000	0.000	0.000	0.000
24	A	25	TYR	0	-0.091	-0.061	17.012	0.024	0.024	0.000	0.000	0.000	0.000
25	A	26	GLY	0	-0.019	-0.016	18.669	-0.025	-0.025	0.000	0.000	0.000	0.000
26	A	27	CYS	0	-0.068	-0.022	20.984	0.026	0.026	0.000	0.000	0.000	0.000
27	A	28	PHE	0	0.037	0.012	16.957	0.016	0.016	0.000	0.000	0.000	0.000
28	A	29	CYS	0	-0.099	-0.020	13.833	-0.186	-0.186	0.000	0.000	0.000	0.000
29	A	30	GLY	0	-0.003	0.003	11.936	0.060	0.060	0.000	0.000	0.000	0.000
30	A	31	GLY	0	-0.067	-0.038	12.925	0.051	0.051	0.000	0.000	0.000	0.000
31	A	32	GLY	0	0.033	0.033	14.319	0.019	0.019	0.000	0.000	0.000	0.000
32	A	33	GLU	-1	-0.905	-0.970	17.514	-0.226	-0.226	0.000	0.000	0.000	0.000
33	A	34	ARG	1	0.831	0.906	19.981	0.127	0.127	0.000	0.000	0.000	0.000
34	A	35	GLY	0	0.042	0.053	22.741	-0.018	-0.018	0.000	0.000	0.000	0.000
35	A	36	PRO	0	-0.027	-0.023	24.609	0.023	0.023	0.000	0.000	0.000	0.000
36	A	37	PRO	0	-0.017	-0.021	21.880	0.000	0.000	0.000	0.000	0.000	0.000
37	A	38	LEU	0	-0.016	-0.008	23.456	0.015	0.015	0.000	0.000	0.000	0.000
38	A	39	ASP	-1	-0.808	-0.886	22.452	-0.309	-0.309	0.000	0.000	0.000	0.000
39	A	40	ALA	0	0.021	-0.005	22.521	-0.017	-0.017	0.000	0.000	0.000	0.000
40	A	41	THR	0	0.016	0.011	17.890	-0.059	-0.059	0.000	0.000	0.000	0.000
41	A	42	ASP	-1	-0.709	-0.869	17.880	-0.399	-0.399	0.000	0.000	0.000	0.000
42	A	43	ARG	1	0.932	0.975	18.626	0.263	0.263	0.000	0.000	0.000	0.000
43	A	44	CYS	0	-0.107	-0.017	14.731	0.130	0.130	0.000	0.000	0.000	0.000
44	A	46	LEU	0	0.023	0.039	14.392	-0.039	-0.039	0.000	0.000	0.000	0.000
45	A	47	ALA	0	0.013	-0.004	15.720	0.004	0.004	0.000	0.000	0.000	0.000
46	A	48	HIS	0	-0.073	-0.041	7.036	0.327	0.327	0.000	0.000	0.000	0.000
47	A	49	SER	0	0.030	0.006	11.237	-0.113	-0.113	0.000	0.000	0.000	0.000
48	A	133	CYS	0	0.008	-0.005	12.808	0.022	0.022	0.000	0.000	0.000	0.000
49	A	51	CYS	0	-0.053	-0.011	7.559	0.150	0.150	0.000	0.000	0.000	0.000
50	A	52	TYR	0	-0.045	-0.071	4.896	0.061	0.061	0.000	0.000	0.000	0.000
51	A	53	ASP	-1	-0.861	-0.916	10.425	-0.215	-0.215	0.000	0.000	0.000	0.000
52	A	54	THR	0	-0.165	-0.072	13.402	0.084	0.084	0.000	0.000	0.000	0.000
53	A	55	LEU	0	-0.103	-0.065	8.151	0.030	0.030	0.000	0.000	0.000	0.000
54	A	59	PRO	0	0.041	0.023	11.067	0.057	0.057	0.000	0.000	0.000	0.000
55	A	60	ASP	-1	-0.845	-0.913	13.461	0.100	0.100	0.000	0.000	0.000	0.000
56	A	61	CYS	0	0.014	0.015	8.299	-0.026	-0.026	0.000	0.000	0.000	0.000
57	A	67	SER	0	0.079	0.049	7.019	-0.179	-0.179	0.000	0.000	0.000	0.000
58	A	68	PRO	0	0.035	0.007	4.652	0.334	0.628	-0.001	-0.056	-0.238	0.000
59	A	69	LYS	1	1.000	0.995	2.424	-4.066	-1.488	2.097	-2.348	-2.327	-0.023
60	A	70	THR	0	-0.063	-0.048	2.363	-0.718	-0.013	3.524	-1.959	-2.270	-0.022
61	A	71	ASP	-1	-0.828	-0.908	2.978	2.273	2.366	0.555	0.232	-0.880	-0.005
62	A	72	ARG	1	0.856	0.922	1.817	-14.255	-17.324	17.498	-6.491	-7.938	0.038
63	A	73	TYR	0	-0.046	-0.067	1.970	0.791	0.528	3.539	-0.941	-2.335	-0.002
64	A	74	LYS	1	0.863	0.927	5.342	-0.552	-0.578	-0.001	-0.001	0.028	0.000
65	A	75	TYR	0	-0.011	-0.030	6.740	-0.016	-0.016	0.000	0.000	0.000	0.000
66	A	76	LYS	1	0.848	0.933	9.736	0.449	0.449	0.000	0.000	0.000	0.000
67	A	77	ARG	1	0.780	0.846	12.996	0.741	0.741	0.000	0.000	0.000	0.000
68	A	78	GLU	-1	-0.828	-0.889	15.493	-0.353	-0.353	0.000	0.000	0.000	0.000
69	A	79	ASN	0	0.023	-0.004	18.889	-0.013	-0.013	0.000	0.000	0.000	0.000
70	A	80	GLY	0	0.012	0.008	19.301	0.005	0.005	0.000	0.000	0.000	0.000
71	A	81	GLU	-1	-0.867	-0.907	16.164	-0.630	-0.630	0.000	0.000	0.000	0.000
72	A	82	ILE	0	-0.013	-0.005	10.295	0.017	0.017	0.000	0.000	0.000	0.000
73	A	83	ILE	0	0.016	0.005	13.349	0.023	0.023	0.000	0.000	0.000	0.000
74	A	84	CYS	0	-0.045	-0.003	5.467	-0.900	-0.900	0.000	0.000	0.000	0.000
75	A	85	GLU	-1	-0.794	-0.903	10.667	-0.288	-0.288	0.000	0.000	0.000	0.000
76	A	86	ASN	0	-0.050	-0.020	8.749	-0.005	-0.005	0.000	0.000	0.000	0.000
77	A	88	SER	0	0.052	0.029	11.680	-0.027	-0.027	0.000	0.000	0.000	0.000
78	A	89	THR	0	-0.003	-0.016	11.068	-0.008	-0.008	0.000	0.000	0.000	0.000
79	A	90	SER	0	0.076	0.037	11.320	-0.021	-0.021	0.000	0.000	0.000	0.000
80	A	92	LYS	1	0.812	0.898	5.731	-1.537	-1.537	0.000	0.000	0.000	0.000
81	A	93	LYS	1	0.794	0.892	6.895	0.217	0.217	0.000	0.000	0.000	0.000
82	A	94	ARG	1	0.865	0.912	9.227	-0.096	-0.096	0.000	0.000	0.000	0.000
83	A	95	ILE	0	0.051	0.031	3.244	-0.618	-0.220	0.029	-0.129	-0.297	0.000
84	A	97	GLU	-1	-0.779	-0.892	6.273	-0.951	-0.951	0.000	0.000	0.000	0.000
85	A	99	ASP	-1	-0.724	-0.823	3.560	-7.229	-6.851	0.005	-0.212	-0.170	-0.001
86	A	100	LYS	1	0.850	0.908	7.234	1.054	1.054	0.000	0.000	0.000	0.000
87	A	101	ALA	0	-0.034	-0.010	10.010	0.187	0.187	0.000	0.000	0.000	0.000
88	A	102	VAL	0	0.033	0.019	9.179	0.156	0.156	0.000	0.000	0.000	0.000
89	A	103	ALA	0	-0.012	-0.011	10.042	0.163	0.163	0.000	0.000	0.000	0.000
90	A	104	VAL	0	-0.004	-0.010	11.938	0.194	0.194	0.000	0.000	0.000	0.000
91	A	106	LEU	0	0.038	0.008	12.932	0.107	0.107	0.000	0.000	0.000	0.000
92	A	107	ARG	1	0.882	0.944	16.392	0.691	0.691	0.000	0.000	0.000	0.000
93	A	108	LYS	1	0.900	0.942	18.224	0.457	0.457	0.000	0.000	0.000	0.000
94	A	109	ASN	0	-0.011	-0.008	19.491	0.087	0.087	0.000	0.000	0.000	0.000
95	A	110	LEU	0	0.047	0.023	19.298	0.027	0.027	0.000	0.000	0.000	0.000
96	A	111	ASN	0	-0.050	-0.029	21.689	0.028	0.028	0.000	0.000	0.000	0.000
97	A	112	THR	0	-0.049	-0.019	23.963	0.024	0.024	0.000	0.000	0.000	0.000
98	A	113	TYR	0	-0.046	-0.016	18.889	0.034	0.034	0.000	0.000	0.000	0.000
99	A	114	ASN	0	0.077	0.026	23.264	0.035	0.035	0.000	0.000	0.000	0.000
100	A	115	LYS	1	0.990	0.979	24.419	0.175	0.175	0.000	0.000	0.000	0.000
101	A	116	LYS	1	0.901	0.951	25.479	0.118	0.118	0.000	0.000	0.000	0.000
102	A	117	TYR	0	-0.004	-0.006	23.315	0.022	0.022	0.000	0.000	0.000	0.000
103	A	118	THR	0	-0.018	-0.004	20.057	-0.007	-0.007	0.000	0.000	0.000	0.000
104	A	119	TYR	0	-0.004	-0.007	20.292	-0.014	-0.014	0.000	0.000	0.000	0.000
105	A	120	TYR	0	0.003	0.007	22.497	0.030	0.030	0.000	0.000	0.000	0.000
106	A	121	PRO	0	0.027	0.024	22.532	-0.006	-0.006	0.000	0.000	0.000	0.000
107	A	122	ASN	0	0.122	0.046	18.821	0.015	0.015	0.000	0.000	0.000	0.000
108	A	124	PHE	0	0.012	0.016	22.869	-0.003	-0.003	0.000	0.000	0.000	0.000
109	A	125	TRP	0	-0.073	-0.041	25.981	0.010	0.010	0.000	0.000	0.000	0.000
110	A	127	LYS	1	0.874	0.909	25.986	0.091	0.091	0.000	0.000	0.000	0.000
111	A	128	GLY	0	0.059	0.055	27.521	0.010	0.010	0.000	0.000	0.000	0.000
112	A	129	ASP	-1	-0.905	-0.941	27.854	-0.115	-0.115	0.000	0.000	0.000	0.000
113	A	130	ILE	0	-0.038	-0.023	23.208	-0.012	-0.012	0.000	0.000	0.000	0.000
114	A	131	GLU	-1	-0.820	-0.936	21.628	-0.228	-0.228	0.000	0.000	0.000	0.000
115	A	132	LYS	1	0.906	0.989	21.304	0.173	0.173	0.000	0.000	0.000	0.000

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