FMO DATABASE

FMODB ID: QVN9Y

Calculation Name: 3ERW-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3ERW

Chain ID: A

ChEMBL ID:

UniProt ID: O31687

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	133
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1263203.307309
FMO2-HF: Nuclear repulsion	1209659.46415
FMO2-HF: Total energy	-53543.843158
FMO2-MP2: Total energy	-53700.01929

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:31:PRO)

Summations of interaction energy for fragment #1(A:31:PRO)

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.
-11.297	-3.297	7.189	-5.192	-9.994	-0.03

Interaction energy analysis for fragmet #1(A:31:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.013 / q_NPA : -0.018

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	33	VAL	0	-0.060	-0.038	3.639	-0.128	1.284	-0.003	-0.572	-0.836	0.003
4	A	34	PRO	0	0.004	0.007	3.248	-1.791	-0.973	0.050	-0.366	-0.502	-0.003
5	A	35	ALA	0	-0.003	-0.004	4.801	0.849	0.849	0.000	0.000	0.000	0.000
6	A	36	VAL	0	-0.020	0.004	5.887	-0.171	-0.171	0.000	0.000	0.000	0.000
7	A	37	PHE	0	-0.037	-0.017	4.976	0.273	0.273	0.000	0.000	0.000	0.000
8	A	38	LEU	0	-0.004	-0.006	10.131	0.085	0.085	0.000	0.000	0.000	0.000
9	A	39	MET	0	-0.041	-0.022	11.693	0.022	0.022	0.000	0.000	0.000	0.000
10	A	40	LYS	1	0.805	0.898	15.179	0.138	0.138	0.000	0.000	0.000	0.000
11	A	41	THR	0	-0.059	-0.026	18.231	0.006	0.006	0.000	0.000	0.000	0.000
12	A	42	ILE	0	-0.003	0.008	19.110	-0.009	-0.009	0.000	0.000	0.000	0.000
13	A	43	GLU	-1	-0.825	-0.937	21.498	0.024	0.024	0.000	0.000	0.000	0.000
14	A	44	GLY	0	-0.030	-0.017	22.768	-0.004	-0.004	0.000	0.000	0.000	0.000
15	A	45	GLU	-1	-0.810	-0.897	20.012	-0.052	-0.052	0.000	0.000	0.000	0.000
16	A	46	ASP	-1	-0.867	-0.919	19.150	-0.156	-0.156	0.000	0.000	0.000	0.000
17	A	47	ILE	0	-0.004	0.013	13.613	0.009	0.009	0.000	0.000	0.000	0.000
18	A	48	SER	0	-0.021	-0.036	12.112	-0.020	-0.020	0.000	0.000	0.000	0.000
19	A	49	ILE	0	-0.058	-0.003	7.313	0.105	0.105	0.000	0.000	0.000	0.000
20	A	50	PRO	0	0.096	0.058	5.989	-0.209	-0.209	0.000	0.000	0.000	0.000
21	A	51	ASN	0	-0.020	-0.013	8.615	-0.030	-0.030	0.000	0.000	0.000	0.000
22	A	52	LYS	1	0.989	0.981	12.331	0.250	0.250	0.000	0.000	0.000	0.000
23	A	53	GLY	0	-0.051	-0.006	14.181	0.040	0.040	0.000	0.000	0.000	0.000
24	A	54	GLN	0	0.023	-0.001	13.551	0.026	0.026	0.000	0.000	0.000	0.000
25	A	55	LYS	1	0.869	0.932	11.642	-0.271	-0.271	0.000	0.000	0.000	0.000
26	A	56	THR	0	-0.029	-0.001	9.178	-0.062	-0.062	0.000	0.000	0.000	0.000
27	A	57	ILE	0	0.006	0.008	10.087	0.128	0.128	0.000	0.000	0.000	0.000
28	A	58	LEU	0	-0.002	0.023	6.170	-0.084	-0.084	0.000	0.000	0.000	0.000
29	A	59	HIS	1	0.843	0.909	9.933	-0.305	-0.305	0.000	0.000	0.000	0.000
30	A	60	PHE	0	0.075	0.037	7.326	-0.088	-0.088	0.000	0.000	0.000	0.000
31	A	61	TRP	0	-0.038	-0.035	12.811	0.016	0.016	0.000	0.000	0.000	0.000
32	A	62	THR	0	0.044	0.020	16.505	-0.016	-0.016	0.000	0.000	0.000	0.000
33	A	63	SER	0	-0.064	-0.069	19.542	0.011	0.011	0.000	0.000	0.000	0.000
34	A	64	TRP	0	-0.056	-0.036	20.395	0.010	0.010	0.000	0.000	0.000	0.000
35	A	65	CYS	0	0.035	0.058	18.839	0.027	0.027	0.000	0.000	0.000	0.000
36	A	66	PRO	0	0.028	0.007	22.413	0.001	0.001	0.000	0.000	0.000	0.000
37	A	67	PRO	0	-0.028	-0.036	20.642	-0.010	-0.010	0.000	0.000	0.000	0.000
38	A	69	LYS	1	0.985	1.001	20.648	-0.163	-0.163	0.000	0.000	0.000	0.000
39	A	70	LYS	1	0.937	0.962	24.080	-0.238	-0.238	0.000	0.000	0.000	0.000
40	A	71	GLU	-1	-0.798	-0.909	17.677	0.432	0.432	0.000	0.000	0.000	0.000
41	A	72	LEU	0	0.032	0.014	19.600	0.002	0.002	0.000	0.000	0.000	0.000
42	A	73	PRO	0	-0.005	-0.006	22.193	-0.010	-0.010	0.000	0.000	0.000	0.000
43	A	74	GLN	0	-0.025	0.024	21.492	-0.016	-0.016	0.000	0.000	0.000	0.000
44	A	75	PHE	0	0.038	0.011	15.375	0.000	0.000	0.000	0.000	0.000	0.000
45	A	76	GLN	0	-0.033	-0.018	20.695	-0.009	-0.009	0.000	0.000	0.000	0.000
46	A	77	SER	0	-0.024	-0.007	23.772	-0.008	-0.008	0.000	0.000	0.000	0.000
47	A	78	PHE	0	0.025	-0.005	17.509	-0.006	-0.006	0.000	0.000	0.000	0.000
48	A	79	TYR	0	0.000	-0.005	20.513	-0.011	-0.011	0.000	0.000	0.000	0.000
49	A	80	ASP	-1	-0.857	-0.917	22.415	0.081	0.081	0.000	0.000	0.000	0.000
50	A	81	ALA	0	-0.097	-0.047	25.343	-0.010	-0.010	0.000	0.000	0.000	0.000
51	A	82	HIS	0	-0.076	-0.032	22.008	0.004	0.004	0.000	0.000	0.000	0.000
52	A	83	PRO	0	-0.028	-0.015	21.925	-0.005	-0.005	0.000	0.000	0.000	0.000
53	A	84	SER	0	0.025	0.005	19.625	-0.015	-0.015	0.000	0.000	0.000	0.000
54	A	85	ASP	-1	-0.809	-0.881	21.249	0.027	0.027	0.000	0.000	0.000	0.000
55	A	86	SER	0	-0.044	-0.024	18.305	-0.021	-0.021	0.000	0.000	0.000	0.000
56	A	87	VAL	0	-0.064	-0.038	14.391	0.000	0.000	0.000	0.000	0.000	0.000
57	A	88	LYS	1	0.888	0.937	14.258	0.020	0.020	0.000	0.000	0.000	0.000
58	A	89	LEU	0	-0.040	-0.007	13.762	0.040	0.040	0.000	0.000	0.000	0.000
59	A	90	VAL	0	0.012	0.001	11.349	-0.045	-0.045	0.000	0.000	0.000	0.000
60	A	91	THR	0	-0.026	-0.009	12.542	0.105	0.105	0.000	0.000	0.000	0.000
61	A	92	VAL	0	0.013	0.007	10.155	-0.064	-0.064	0.000	0.000	0.000	0.000
62	A	93	ASN	0	-0.033	-0.035	13.567	0.048	0.048	0.000	0.000	0.000	0.000
63	A	94	LEU	0	0.025	0.006	11.998	-0.038	-0.038	0.000	0.000	0.000	0.000
64	A	95	VAL	0	0.083	0.028	15.828	0.001	0.001	0.000	0.000	0.000	0.000
65	A	96	ASN	0	-0.072	-0.042	16.251	-0.009	-0.009	0.000	0.000	0.000	0.000
66	A	97	SER	0	-0.045	-0.011	17.400	0.017	0.017	0.000	0.000	0.000	0.000
67	A	98	GLU	-1	-0.749	-0.835	19.797	0.173	0.173	0.000	0.000	0.000	0.000
68	A	99	GLN	0	-0.046	-0.012	22.607	-0.017	-0.017	0.000	0.000	0.000	0.000
69	A	100	ASN	0	0.029	-0.001	24.753	-0.012	-0.012	0.000	0.000	0.000	0.000
70	A	101	GLN	0	0.010	-0.014	22.813	0.004	0.004	0.000	0.000	0.000	0.000
71	A	102	GLN	0	-0.035	-0.010	24.254	-0.003	-0.003	0.000	0.000	0.000	0.000
72	A	103	VAL	0	0.010	0.000	26.395	0.005	0.005	0.000	0.000	0.000	0.000
73	A	104	VAL	0	-0.017	0.004	21.034	0.009	0.009	0.000	0.000	0.000	0.000
74	A	105	GLU	-1	-0.769	-0.890	23.922	0.020	0.020	0.000	0.000	0.000	0.000
75	A	106	ASP	-1	-0.903	-0.941	26.198	0.043	0.043	0.000	0.000	0.000	0.000
76	A	107	PHE	0	-0.040	-0.013	23.659	0.007	0.007	0.000	0.000	0.000	0.000
77	A	108	ILE	0	0.048	0.020	21.638	0.009	0.009	0.000	0.000	0.000	0.000
78	A	109	LYS	1	0.970	0.991	25.791	-0.031	-0.031	0.000	0.000	0.000	0.000
79	A	110	ALA	0	-0.052	-0.034	29.207	0.000	0.000	0.000	0.000	0.000	0.000
80	A	111	ASN	0	-0.155	-0.092	27.096	0.007	0.007	0.000	0.000	0.000	0.000
81	A	112	LYS	1	0.918	0.960	28.312	-0.064	-0.064	0.000	0.000	0.000	0.000
82	A	113	LEU	0	-0.024	-0.001	22.512	0.005	0.005	0.000	0.000	0.000	0.000
83	A	114	THR	0	-0.029	-0.019	24.698	-0.014	-0.014	0.000	0.000	0.000	0.000
84	A	115	PHE	0	-0.009	0.007	18.940	-0.003	-0.003	0.000	0.000	0.000	0.000
85	A	116	PRO	0	0.033	0.016	17.055	0.000	0.000	0.000	0.000	0.000	0.000
86	A	117	ILE	0	-0.057	-0.027	17.306	0.038	0.038	0.000	0.000	0.000	0.000
87	A	118	VAL	0	0.048	0.022	13.082	-0.033	-0.033	0.000	0.000	0.000	0.000
88	A	119	LEU	0	0.011	0.011	15.452	0.047	0.047	0.000	0.000	0.000	0.000
89	A	120	ASP	-1	-0.769	-0.891	11.199	-0.085	-0.085	0.000	0.000	0.000	0.000
90	A	121	SER	0	-0.017	-0.034	13.954	0.014	0.014	0.000	0.000	0.000	0.000
91	A	122	LYS	1	0.904	0.950	14.076	0.174	0.174	0.000	0.000	0.000	0.000
92	A	123	GLY	0	0.036	0.039	12.599	-0.023	-0.023	0.000	0.000	0.000	0.000
93	A	124	GLU	-1	-0.806	-0.890	8.973	-0.779	-0.779	0.000	0.000	0.000	0.000
94	A	125	LEU	0	0.011	0.018	6.879	-0.124	-0.124	0.000	0.000	0.000	0.000
95	A	126	MET	0	0.005	-0.014	6.555	0.217	0.217	0.000	0.000	0.000	0.000
96	A	127	LYS	1	0.795	0.886	7.753	1.103	1.103	0.000	0.000	0.000	0.000
97	A	128	GLU	-1	-0.835	-0.921	2.236	-4.358	-3.839	0.941	-0.471	-0.988	0.000
98	A	129	TYR	0	-0.005	-0.004	2.352	-3.706	-0.872	4.294	-2.874	-4.254	-0.028
99	A	130	HIS	0	-0.040	-0.011	3.572	1.500	2.162	0.042	-0.150	-0.554	-0.001
100	A	131	ILE	0	-0.023	-0.002	6.127	0.079	0.079	0.000	0.000	0.000	0.000
101	A	132	ILE	0	-0.010	-0.002	8.967	-0.252	-0.252	0.000	0.000	0.000	0.000
102	A	133	THR	0	-0.038	-0.020	11.969	-0.102	-0.102	0.000	0.000	0.000	0.000
103	A	134	ILE	0	-0.003	0.034	12.944	0.087	0.087	0.000	0.000	0.000	0.000
104	A	135	PRO	0	0.012	-0.026	15.423	-0.059	-0.059	0.000	0.000	0.000	0.000
105	A	136	THR	0	-0.035	-0.025	9.346	0.053	0.053	0.000	0.000	0.000	0.000
106	A	137	SER	0	-0.021	-0.015	10.784	-0.110	-0.110	0.000	0.000	0.000	0.000
107	A	138	PHE	0	0.035	0.015	5.911	0.166	0.166	0.000	0.000	0.000	0.000
108	A	139	LEU	0	-0.017	0.006	8.336	-0.250	-0.250	0.000	0.000	0.000	0.000
109	A	140	LEU	0	0.016	0.011	4.411	0.114	0.245	-0.001	-0.011	-0.119	0.000
110	A	141	ASN	0	0.003	-0.024	7.644	-0.227	-0.227	0.000	0.000	0.000	0.000
111	A	142	GLU	-1	-0.898	-0.961	8.464	-0.282	-0.282	0.000	0.000	0.000	0.000
112	A	143	LYS	1	0.774	0.870	8.485	0.288	0.288	0.000	0.000	0.000	0.000
113	A	144	GLY	0	0.004	-0.022	4.918	-0.334	-0.334	0.000	0.000	0.000	0.000
114	A	145	GLU	-1	-0.836	-0.878	3.100	-2.008	-1.055	0.088	-0.344	-0.697	-0.003
115	A	146	ILE	0	0.007	-0.009	2.247	-1.082	-0.418	1.779	-0.402	-2.041	0.002
116	A	147	GLU	-1	-0.829	-0.896	4.993	0.277	0.284	-0.001	-0.002	-0.003	0.000
117	A	148	LYS	1	0.775	0.880	8.644	-0.551	-0.551	0.000	0.000	0.000	0.000
118	A	149	THR	0	0.051	0.022	7.398	0.192	0.192	0.000	0.000	0.000	0.000
119	A	150	LYS	1	0.834	0.917	9.741	-0.763	-0.763	0.000	0.000	0.000	0.000
120	A	151	ILE	0	0.052	0.034	11.347	0.001	0.001	0.000	0.000	0.000	0.000
121	A	152	GLY	0	-0.007	-0.008	14.117	-0.092	-0.092	0.000	0.000	0.000	0.000
122	A	153	PRO	0	-0.059	-0.042	16.615	0.024	0.024	0.000	0.000	0.000	0.000
123	A	154	MET	0	-0.001	0.043	15.281	0.044	0.044	0.000	0.000	0.000	0.000
124	A	155	THR	0	-0.003	-0.032	19.128	-0.033	-0.033	0.000	0.000	0.000	0.000
125	A	156	ALA	0	0.076	0.016	20.659	0.021	0.021	0.000	0.000	0.000	0.000
126	A	157	GLU	-1	-0.840	-0.902	22.176	0.182	0.182	0.000	0.000	0.000	0.000
127	A	158	GLN	0	-0.025	-0.022	18.714	0.021	0.021	0.000	0.000	0.000	0.000
128	A	159	LEU	0	-0.021	-0.005	15.977	0.029	0.029	0.000	0.000	0.000	0.000
129	A	160	LYS	1	0.893	0.934	18.223	-0.171	-0.171	0.000	0.000	0.000	0.000
130	A	161	GLU	-1	-0.808	-0.883	18.381	0.393	0.393	0.000	0.000	0.000	0.000
131	A	162	TRP	0	-0.084	-0.056	11.331	0.051	0.051	0.000	0.000	0.000	0.000
132	A	163	THR	0	-0.024	-0.016	16.118	-0.014	-0.014	0.000	0.000	0.000	0.000
133	A	164	GLU	-1	-0.988	-0.976	18.365	0.165	0.165	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:31:PRO)