FMO DATABASE

FMODB ID: NNZLQ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1034436.875788
FMO2-HF: Nuclear repulsion	982643.578322
FMO2-HF: Total energy	-51793.297466
FMO2-MP2: Total energy	-51932.686747

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.
-58.255	-68.253	66.084	-29.093	-26.997	-0.092

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 : -0.033 / q_NPA : -0.004

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	3	VAL	0	-0.037	0.000	2.229	-8.393	-3.537	2.806	-3.542	-4.120	0.028
4	A	4	GLU	-1	-0.726	-0.839	1.563	-24.552	-40.928	36.876	-13.525	-6.976	-0.107
5	A	5	LEU	0	0.059	0.041	3.731	2.196	2.684	0.000	-0.167	-0.321	0.000
6	A	6	GLY	0	0.010	-0.010	5.558	1.194	1.194	0.000	0.000	0.000	0.000
7	A	7	LYS	1	0.899	0.962	7.105	1.775	1.775	0.000	0.000	0.000	0.000
8	A	8	MET	0	-0.006	0.009	6.255	0.528	0.528	0.000	0.000	0.000	0.000
9	A	9	ILE	0	0.004	0.001	9.603	0.351	0.351	0.000	0.000	0.000	0.000
10	A	10	ILE	0	-0.001	0.018	11.052	0.212	0.212	0.000	0.000	0.000	0.000
11	A	11	GLN	0	-0.015	-0.006	12.656	0.001	0.001	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.775	-0.849	13.053	-0.728	-0.728	0.000	0.000	0.000	0.000
13	A	13	THR	0	-0.067	-0.065	15.217	0.100	0.100	0.000	0.000	0.000	0.000
14	A	14	GLY	0	0.020	0.023	16.981	0.065	0.065	0.000	0.000	0.000	0.000
15	A	16	LYS	1	0.814	0.931	16.378	0.407	0.407	0.000	0.000	0.000	0.000
16	A	17	SER	0	0.048	0.022	13.250	-0.124	-0.124	0.000	0.000	0.000	0.000
17	A	18	PRO	0	0.035	0.020	9.554	0.045	0.045	0.000	0.000	0.000	0.000
18	A	19	PHE	0	0.007	0.045	12.601	0.035	0.035	0.000	0.000	0.000	0.000
19	A	20	PRO	0	-0.008	-0.028	14.264	0.016	0.016	0.000	0.000	0.000	0.000
20	A	21	SER	0	-0.048	-0.044	16.379	-0.008	-0.008	0.000	0.000	0.000	0.000
21	A	22	TYR	0	0.042	-0.008	13.699	-0.018	-0.018	0.000	0.000	0.000	0.000
22	A	23	THR	0	-0.011	-0.008	12.114	-0.042	-0.042	0.000	0.000	0.000	0.000
23	A	24	SER	0	-0.005	-0.013	14.327	0.044	0.044	0.000	0.000	0.000	0.000
24	A	25	TYR	0	-0.069	-0.048	17.231	0.023	0.023	0.000	0.000	0.000	0.000
25	A	26	GLY	0	-0.016	-0.018	18.762	-0.033	-0.033	0.000	0.000	0.000	0.000
26	A	27	CYS	0	-0.082	-0.033	20.963	0.034	0.034	0.000	0.000	0.000	0.000
27	A	28	PHE	0	0.030	0.014	16.720	0.017	0.017	0.000	0.000	0.000	0.000
28	A	29	CYS	0	-0.131	-0.033	14.225	-0.182	-0.182	0.000	0.000	0.000	0.000
29	A	30	GLY	0	0.037	0.026	11.950	0.078	0.078	0.000	0.000	0.000	0.000
30	A	31	GLY	0	-0.049	-0.044	11.950	-0.033	-0.033	0.000	0.000	0.000	0.000
31	A	32	GLY	0	0.030	0.037	14.348	0.035	0.035	0.000	0.000	0.000	0.000
32	A	33	GLU	-1	-0.898	-0.967	17.320	-0.230	-0.230	0.000	0.000	0.000	0.000
33	A	34	ARG	1	0.837	0.910	19.877	0.124	0.124	0.000	0.000	0.000	0.000
34	A	35	GLY	0	0.042	0.044	23.038	-0.013	-0.013	0.000	0.000	0.000	0.000
35	A	36	PRO	0	-0.039	-0.022	24.936	0.021	0.021	0.000	0.000	0.000	0.000
36	A	37	PRO	0	0.003	-0.002	21.851	0.005	0.005	0.000	0.000	0.000	0.000
37	A	38	LEU	0	-0.025	0.010	23.589	0.009	0.009	0.000	0.000	0.000	0.000
38	A	39	ASP	-1	-0.815	-0.892	22.700	-0.288	-0.288	0.000	0.000	0.000	0.000
39	A	40	ALA	0	0.028	-0.001	22.932	-0.016	-0.016	0.000	0.000	0.000	0.000
40	A	41	THR	0	0.011	0.006	18.397	-0.059	-0.059	0.000	0.000	0.000	0.000
41	A	42	ASP	-1	-0.720	-0.885	18.240	-0.374	-0.374	0.000	0.000	0.000	0.000
42	A	43	ARG	1	0.878	0.934	18.749	0.244	0.244	0.000	0.000	0.000	0.000
43	A	44	CYS	0	-0.069	-0.005	15.268	0.124	0.124	0.000	0.000	0.000	0.000
44	A	46	LEU	0	0.016	0.027	14.493	-0.047	-0.047	0.000	0.000	0.000	0.000
45	A	47	ALA	0	0.013	0.001	16.152	-0.005	-0.005	0.000	0.000	0.000	0.000
46	A	48	HIS	0	-0.087	-0.050	7.444	0.310	0.310	0.000	0.000	0.000	0.000
47	A	49	SER	0	0.014	0.007	11.614	-0.103	-0.103	0.000	0.000	0.000	0.000
48	A	133	CYS	0	0.031	0.011	13.131	-0.015	-0.015	0.000	0.000	0.000	0.000
49	A	51	CYS	0	-0.040	0.000	8.103	0.176	0.176	0.000	0.000	0.000	0.000
50	A	52	TYR	0	-0.044	-0.069	5.149	-0.112	-0.038	-0.001	-0.003	-0.070	0.000
51	A	53	ASP	-1	-0.870	-0.923	10.657	-0.300	-0.300	0.000	0.000	0.000	0.000
52	A	54	THR	0	-0.133	-0.071	13.723	0.084	0.084	0.000	0.000	0.000	0.000
53	A	55	LEU	0	-0.110	-0.057	8.277	0.008	0.008	0.000	0.000	0.000	0.000
54	A	59	PRO	0	0.027	0.013	11.164	0.038	0.038	0.000	0.000	0.000	0.000
55	A	60	ASP	-1	-0.822	-0.906	13.545	-0.078	-0.078	0.000	0.000	0.000	0.000
56	A	61	CYS	0	0.011	0.023	8.328	-0.055	-0.055	0.000	0.000	0.000	0.000
57	A	67	SER	0	0.061	0.034	7.255	-0.139	-0.139	0.000	0.000	0.000	0.000
58	A	68	PRO	0	0.049	0.017	4.828	0.263	0.263	0.000	0.000	0.000	0.000
59	A	69	LYS	1	0.944	0.968	2.575	-4.048	-1.433	0.908	-1.623	-1.901	-0.018
60	A	70	THR	0	-0.068	-0.050	2.209	-1.295	-0.221	3.656	-2.483	-2.247	-0.024
61	A	71	ASP	-1	-0.803	-0.903	2.756	2.255	1.774	1.042	0.479	-1.039	-0.013
62	A	72	ARG	1	0.836	0.923	1.895	-20.609	-22.776	15.439	-6.154	-7.119	0.051
63	A	73	TYR	0	-0.029	-0.051	1.918	-0.685	-1.262	5.347	-1.887	-2.884	-0.009
64	A	74	LYS	1	0.846	0.914	5.247	-0.344	-0.346	-0.001	-0.002	0.005	0.000
65	A	75	TYR	0	-0.008	-0.024	6.657	0.024	0.024	0.000	0.000	0.000	0.000
66	A	76	LYS	1	0.829	0.921	9.607	0.486	0.486	0.000	0.000	0.000	0.000
67	A	77	ARG	1	0.781	0.842	12.958	0.715	0.715	0.000	0.000	0.000	0.000
68	A	78	GLU	-1	-0.812	-0.884	15.577	-0.378	-0.378	0.000	0.000	0.000	0.000
69	A	79	ASN	0	-0.002	-0.016	19.010	-0.021	-0.021	0.000	0.000	0.000	0.000
70	A	80	GLY	0	0.038	0.031	19.544	0.020	0.020	0.000	0.000	0.000	0.000
71	A	81	GLU	-1	-0.901	-0.935	15.759	-0.666	-0.666	0.000	0.000	0.000	0.000
72	A	82	ILE	0	-0.006	-0.006	10.013	0.017	0.017	0.000	0.000	0.000	0.000
73	A	83	ILE	0	0.020	0.013	13.137	0.010	0.010	0.000	0.000	0.000	0.000
74	A	84	CYS	0	-0.018	0.013	5.582	-0.616	-0.616	0.000	0.000	0.000	0.000
75	A	85	GLU	-1	-0.803	-0.902	10.476	-0.316	-0.316	0.000	0.000	0.000	0.000
76	A	86	ASN	0	-0.039	-0.027	8.654	-0.013	-0.013	0.000	0.000	0.000	0.000
77	A	88	SER	0	0.080	0.032	11.483	-0.039	-0.039	0.000	0.000	0.000	0.000
78	A	89	THR	0	-0.012	-0.004	10.834	-0.018	-0.018	0.000	0.000	0.000	0.000
79	A	90	SER	0	0.055	0.022	10.950	0.038	0.038	0.000	0.000	0.000	0.000
80	A	92	LYS	1	0.806	0.885	6.194	-1.483	-1.483	0.000	0.000	0.000	0.000
81	A	93	LYS	1	0.775	0.893	6.903	0.288	0.288	0.000	0.000	0.000	0.000
82	A	94	ARG	1	0.863	0.907	9.060	0.095	0.095	0.000	0.000	0.000	0.000
83	A	95	ILE	0	0.036	0.025	3.366	-0.387	-0.053	0.012	-0.100	-0.246	0.000
84	A	97	GLU	-1	-0.745	-0.886	6.315	-0.894	-0.894	0.000	0.000	0.000	0.000
85	A	99	ASP	-1	-0.731	-0.824	3.887	-6.493	-6.329	0.000	-0.086	-0.079	0.000
86	A	100	LYS	1	0.842	0.913	7.566	1.164	1.164	0.000	0.000	0.000	0.000
87	A	101	ALA	0	-0.034	-0.004	10.287	0.202	0.202	0.000	0.000	0.000	0.000
88	A	102	VAL	0	0.030	0.015	9.820	0.156	0.156	0.000	0.000	0.000	0.000
89	A	103	ALA	0	0.000	0.002	10.495	0.175	0.175	0.000	0.000	0.000	0.000
90	A	104	VAL	0	-0.005	-0.009	12.488	0.186	0.186	0.000	0.000	0.000	0.000
91	A	106	LEU	0	0.023	0.004	13.442	0.097	0.097	0.000	0.000	0.000	0.000
92	A	107	ARG	1	0.871	0.933	16.634	0.680	0.680	0.000	0.000	0.000	0.000
93	A	108	LYS	1	0.893	0.937	18.489	0.436	0.436	0.000	0.000	0.000	0.000
94	A	109	ASN	0	-0.016	-0.012	20.074	0.081	0.081	0.000	0.000	0.000	0.000
95	A	110	LEU	0	0.032	0.028	19.449	0.027	0.027	0.000	0.000	0.000	0.000
96	A	111	ASN	0	-0.056	-0.036	21.961	0.028	0.028	0.000	0.000	0.000	0.000
97	A	112	THR	0	0.002	-0.003	24.439	0.019	0.019	0.000	0.000	0.000	0.000
98	A	113	TYR	0	-0.023	-0.014	19.224	0.008	0.008	0.000	0.000	0.000	0.000
99	A	114	ASN	0	0.054	0.019	23.581	0.038	0.038	0.000	0.000	0.000	0.000
100	A	115	LYS	1	0.988	0.976	24.395	0.129	0.129	0.000	0.000	0.000	0.000
101	A	116	LYS	1	0.930	0.961	25.349	0.089	0.089	0.000	0.000	0.000	0.000
102	A	117	TYR	0	0.034	0.019	23.470	0.020	0.020	0.000	0.000	0.000	0.000
103	A	118	THR	0	-0.027	0.010	19.916	-0.018	-0.018	0.000	0.000	0.000	0.000
104	A	119	TYR	0	0.011	0.011	20.323	-0.007	-0.007	0.000	0.000	0.000	0.000
105	A	120	TYR	0	0.015	0.016	22.490	0.027	0.027	0.000	0.000	0.000	0.000
106	A	121	PRO	0	0.033	0.025	22.595	-0.006	-0.006	0.000	0.000	0.000	0.000
107	A	122	ASN	0	0.087	0.039	18.797	0.022	0.022	0.000	0.000	0.000	0.000
108	A	124	PHE	0	0.026	0.019	22.892	-0.006	-0.006	0.000	0.000	0.000	0.000
109	A	125	TRP	0	-0.077	-0.054	26.225	0.007	0.007	0.000	0.000	0.000	0.000
110	A	127	LYS	1	0.894	0.932	26.145	0.078	0.078	0.000	0.000	0.000	0.000
111	A	128	GLY	0	0.053	0.049	28.056	0.009	0.009	0.000	0.000	0.000	0.000
112	A	129	ASP	-1	-0.887	-0.934	28.139	-0.113	-0.113	0.000	0.000	0.000	0.000
113	A	130	ILE	0	-0.038	-0.026	23.399	-0.007	-0.007	0.000	0.000	0.000	0.000
114	A	131	GLU	-1	-0.811	-0.931	21.764	-0.224	-0.224	0.000	0.000	0.000	0.000
115	A	132	LYS	1	0.915	0.981	21.458	0.190	0.190	0.000	0.000	0.000	0.000

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