FMO DATABASE

FMODB ID: 39Q5L

Calculation Name: 3W1Z-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3W1Z

Chain ID: A

ChEMBL ID:

UniProt ID: O14368

Base Structure: X-ray

Registration Date: 2023-06-21

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	134
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1033185.983845
FMO2-HF: Nuclear repulsion	981804.50703
FMO2-HF: Total energy	-51381.476815
FMO2-MP2: Total energy	-51534.747258

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:10:PRO)

Summations of interaction energy for fragment #1(A:10: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.
-3.326	-1.356	-0.012	-0.68	-1.278	0.002

Interaction energy analysis for fragmet #1(A:10:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.009 / q_NPA : -0.028

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	12	THR	0	0.018	0.016	3.896	-0.724	0.530	-0.013	-0.465	-0.775	0.001
4	A	13	VAL	0	-0.009	-0.007	6.236	0.373	0.373	0.000	0.000	0.000	0.000
5	A	14	ASN	0	-0.006	-0.021	9.473	-0.130	-0.130	0.000	0.000	0.000	0.000
6	A	15	ASP	-1	-0.804	-0.878	11.860	-0.249	-0.249	0.000	0.000	0.000	0.000
7	A	16	LEU	0	0.009	0.003	11.800	0.047	0.047	0.000	0.000	0.000	0.000
8	A	17	PHE	0	-0.032	-0.036	15.209	0.027	0.027	0.000	0.000	0.000	0.000
9	A	18	SER	0	0.003	0.013	16.954	0.022	0.022	0.000	0.000	0.000	0.000
10	A	19	ASP	-1	-0.817	-0.893	18.787	-0.025	-0.025	0.000	0.000	0.000	0.000
11	A	20	PHE	0	-0.014	0.005	21.093	0.016	0.016	0.000	0.000	0.000	0.000
12	A	21	VAL	0	-0.051	-0.035	16.433	0.023	0.023	0.000	0.000	0.000	0.000
13	A	22	SER	0	0.034	0.022	16.649	-0.017	-0.017	0.000	0.000	0.000	0.000
14	A	23	TYR	0	0.010	0.008	8.285	0.079	0.079	0.000	0.000	0.000	0.000
15	A	24	SER	0	-0.005	-0.018	12.519	0.014	0.014	0.000	0.000	0.000	0.000
16	A	25	PRO	0	-0.011	0.011	11.941	0.010	0.010	0.000	0.000	0.000	0.000
17	A	26	ARG	1	0.908	0.949	12.879	-0.246	-0.246	0.000	0.000	0.000	0.000
18	A	27	LEU	0	-0.001	-0.008	13.220	0.085	0.085	0.000	0.000	0.000	0.000
19	A	28	ASN	0	0.004	0.001	8.885	-0.277	-0.277	0.000	0.000	0.000	0.000
20	A	29	ASN	0	-0.010	-0.016	9.678	-0.005	-0.005	0.000	0.000	0.000	0.000
21	A	30	GLN	0	0.039	0.030	3.898	-2.015	-1.518	0.001	-0.185	-0.314	0.001
22	A	31	ILE	0	0.025	0.021	5.798	-0.212	-0.212	0.000	0.000	0.000	0.000
23	A	32	PRO	0	-0.032	-0.026	3.783	-0.415	-0.196	0.000	-0.030	-0.189	0.000
24	A	33	GLY	0	0.016	0.012	5.530	0.042	0.042	0.000	0.000	0.000	0.000
25	A	34	GLU	-1	-0.894	-0.943	8.234	-0.292	-0.292	0.000	0.000	0.000	0.000
26	A	35	LEU	0	-0.023	-0.008	9.221	-0.264	-0.264	0.000	0.000	0.000	0.000
27	A	36	SER	0	0.008	0.010	8.330	0.075	0.075	0.000	0.000	0.000	0.000
28	A	37	PRO	0	-0.007	0.000	9.561	-0.137	-0.137	0.000	0.000	0.000	0.000
29	A	38	SER	0	-0.010	-0.018	9.978	-0.080	-0.080	0.000	0.000	0.000	0.000
30	A	39	ILE	0	-0.040	-0.022	10.908	0.107	0.107	0.000	0.000	0.000	0.000
31	A	40	ASP	-1	-0.854	-0.901	11.842	-0.396	-0.396	0.000	0.000	0.000	0.000
32	A	41	VAL	0	-0.036	-0.026	14.298	0.035	0.035	0.000	0.000	0.000	0.000
33	A	42	HIS	0	-0.040	-0.018	16.801	0.042	0.042	0.000	0.000	0.000	0.000
34	A	43	GLU	-1	-0.843	-0.914	20.011	-0.076	-0.076	0.000	0.000	0.000	0.000
35	A	44	GLY	0	-0.010	-0.002	23.347	0.009	0.009	0.000	0.000	0.000	0.000
36	A	45	LYS	1	0.743	0.856	26.487	0.065	0.065	0.000	0.000	0.000	0.000
37	A	46	ASP	-1	-0.776	-0.896	29.976	-0.063	-0.063	0.000	0.000	0.000	0.000
38	A	47	THR	0	-0.021	-0.015	26.386	0.004	0.004	0.000	0.000	0.000	0.000
39	A	48	VAL	0	0.004	0.009	21.928	0.002	0.002	0.000	0.000	0.000	0.000
40	A	49	SER	0	-0.001	0.011	22.067	0.011	0.011	0.000	0.000	0.000	0.000
41	A	50	VAL	0	-0.013	-0.010	17.698	-0.008	-0.008	0.000	0.000	0.000	0.000
42	A	51	ASP	-1	-0.829	-0.894	17.669	-0.227	-0.227	0.000	0.000	0.000	0.000
43	A	52	VAL	0	0.008	-0.011	15.061	-0.047	-0.047	0.000	0.000	0.000	0.000
44	A	53	GLU	-1	-0.889	-0.913	12.260	-0.582	-0.582	0.000	0.000	0.000	0.000
45	A	54	LEU	0	-0.023	-0.020	14.988	-0.037	-0.037	0.000	0.000	0.000	0.000
46	A	55	PRO	0	0.035	0.021	15.501	0.047	0.047	0.000	0.000	0.000	0.000
47	A	56	GLY	0	-0.028	-0.024	18.481	-0.012	-0.012	0.000	0.000	0.000	0.000
48	A	57	VAL	0	0.013	0.011	19.128	0.001	0.001	0.000	0.000	0.000	0.000
49	A	58	LYS	1	0.801	0.892	22.190	0.184	0.184	0.000	0.000	0.000	0.000
50	A	59	LYS	1	0.860	0.901	24.970	0.133	0.133	0.000	0.000	0.000	0.000
51	A	60	GLU	-1	-0.798	-0.889	26.456	-0.141	-0.141	0.000	0.000	0.000	0.000
52	A	61	ASP	-1	-0.855	-0.911	23.862	-0.176	-0.176	0.000	0.000	0.000	0.000
53	A	62	VAL	0	-0.071	-0.027	21.302	-0.011	-0.011	0.000	0.000	0.000	0.000
54	A	63	GLN	0	-0.012	0.006	23.357	0.013	0.013	0.000	0.000	0.000	0.000
55	A	64	VAL	0	0.005	-0.005	22.858	-0.017	-0.017	0.000	0.000	0.000	0.000
56	A	65	HIS	0	0.009	0.012	24.608	0.021	0.021	0.000	0.000	0.000	0.000
57	A	66	TYR	0	0.018	-0.013	25.160	-0.006	-0.006	0.000	0.000	0.000	0.000
58	A	67	ASP	-1	-0.823	-0.891	27.110	-0.060	-0.060	0.000	0.000	0.000	0.000
59	A	68	SER	0	-0.055	-0.045	27.601	-0.001	-0.001	0.000	0.000	0.000	0.000
60	A	69	GLY	0	-0.045	-0.010	27.130	0.006	0.006	0.000	0.000	0.000	0.000
61	A	70	LYS	1	0.802	0.884	22.706	0.057	0.057	0.000	0.000	0.000	0.000
62	A	71	LEU	0	0.016	0.018	20.955	0.007	0.007	0.000	0.000	0.000	0.000
63	A	72	THR	0	0.005	-0.008	20.481	-0.007	-0.007	0.000	0.000	0.000	0.000
64	A	73	ILE	0	-0.006	0.000	18.629	0.014	0.014	0.000	0.000	0.000	0.000
65	A	74	SER	0	-0.020	-0.030	18.753	-0.025	-0.025	0.000	0.000	0.000	0.000
66	A	75	GLY	0	0.050	0.020	20.491	0.011	0.011	0.000	0.000	0.000	0.000
67	A	76	GLU	-1	-0.850	-0.901	20.609	-0.232	-0.232	0.000	0.000	0.000	0.000
68	A	77	VAL	0	-0.033	-0.008	16.603	0.001	0.001	0.000	0.000	0.000	0.000
69	A	78	VAL	0	0.060	0.025	19.693	-0.007	-0.007	0.000	0.000	0.000	0.000
70	A	79	ASN	0	-0.003	-0.008	21.109	-0.009	-0.009	0.000	0.000	0.000	0.000
71	A	80	GLU	-1	-0.819	-0.927	22.581	-0.154	-0.154	0.000	0.000	0.000	0.000
72	A	81	ARG	1	0.870	0.941	24.690	0.175	0.175	0.000	0.000	0.000	0.000
73	A	82	LYS	1	0.947	0.993	25.314	0.139	0.139	0.000	0.000	0.000	0.000
74	A	83	ASN	0	-0.065	-0.042	27.257	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	84	GLU	-1	-0.789	-0.854	30.652	-0.074	-0.074	0.000	0.000	0.000	0.000
76	A	85	SER	0	-0.057	-0.050	30.145	-0.009	-0.009	0.000	0.000	0.000	0.000
77	A	86	THR	0	-0.074	-0.060	30.788	0.001	0.001	0.000	0.000	0.000	0.000
78	A	87	GLU	-1	-0.915	-0.942	31.769	-0.106	-0.106	0.000	0.000	0.000	0.000
79	A	88	GLY	0	-0.020	-0.016	31.011	0.002	0.002	0.000	0.000	0.000	0.000
80	A	89	ASN	0	-0.048	-0.032	27.239	0.004	0.004	0.000	0.000	0.000	0.000
81	A	90	GLN	0	0.030	0.029	21.344	-0.010	-0.010	0.000	0.000	0.000	0.000
82	A	91	ARG	1	0.937	0.964	23.444	0.111	0.111	0.000	0.000	0.000	0.000
83	A	92	TRP	0	-0.049	-0.033	15.659	0.029	0.029	0.000	0.000	0.000	0.000
84	A	93	SER	0	-0.051	-0.052	18.003	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	94	GLU	-1	-0.840	-0.894	13.469	-0.427	-0.427	0.000	0.000	0.000	0.000
86	A	95	ARG	1	0.840	0.931	13.351	0.257	0.257	0.000	0.000	0.000	0.000
87	A	96	ARG	1	0.906	0.956	5.897	1.634	1.634	0.000	0.000	0.000	0.000
88	A	97	PHE	0	-0.024	-0.027	13.922	0.026	0.026	0.000	0.000	0.000	0.000
89	A	98	GLY	0	0.017	0.018	16.464	-0.016	-0.016	0.000	0.000	0.000	0.000
90	A	99	SER	0	0.002	-0.026	18.444	-0.011	-0.011	0.000	0.000	0.000	0.000
91	A	100	PHE	0	-0.044	-0.018	15.594	-0.042	-0.042	0.000	0.000	0.000	0.000
92	A	101	SER	0	0.029	-0.006	16.458	0.043	0.043	0.000	0.000	0.000	0.000
93	A	102	ARG	1	0.802	0.915	9.725	0.663	0.663	0.000	0.000	0.000	0.000
94	A	103	THR	0	-0.006	-0.005	16.400	0.026	0.026	0.000	0.000	0.000	0.000
95	A	104	ILE	0	-0.023	-0.017	16.724	-0.027	-0.027	0.000	0.000	0.000	0.000
96	A	105	THR	0	0.005	0.007	18.779	0.023	0.023	0.000	0.000	0.000	0.000
97	A	106	ILE	0	-0.004	-0.003	20.509	-0.007	-0.007	0.000	0.000	0.000	0.000
98	A	107	PRO	0	-0.016	-0.001	20.836	0.014	0.014	0.000	0.000	0.000	0.000
99	A	108	ALA	0	0.011	0.004	23.254	0.012	0.012	0.000	0.000	0.000	0.000
100	A	109	LYS	1	0.920	0.964	26.899	0.054	0.054	0.000	0.000	0.000	0.000
101	A	110	ILE	0	0.022	0.007	26.835	0.002	0.002	0.000	0.000	0.000	0.000
102	A	111	ASP	-1	-0.882	-0.921	30.070	-0.059	-0.059	0.000	0.000	0.000	0.000
103	A	112	ALA	0	0.050	0.012	31.539	-0.005	-0.005	0.000	0.000	0.000	0.000
104	A	113	ASP	-1	-0.902	-0.948	32.615	-0.070	-0.070	0.000	0.000	0.000	0.000
105	A	114	ARG	1	0.764	0.857	33.824	0.072	0.072	0.000	0.000	0.000	0.000
106	A	115	ILE	0	-0.046	-0.009	27.517	-0.004	-0.004	0.000	0.000	0.000	0.000
107	A	116	GLU	-1	-0.867	-0.899	28.666	-0.118	-0.118	0.000	0.000	0.000	0.000
108	A	117	ALA	0	-0.003	-0.021	25.592	-0.011	-0.011	0.000	0.000	0.000	0.000
109	A	118	ASN	0	-0.044	-0.012	25.632	0.013	0.013	0.000	0.000	0.000	0.000
110	A	119	PHE	0	0.013	0.003	21.532	-0.012	-0.012	0.000	0.000	0.000	0.000
111	A	120	SER	0	-0.009	-0.014	23.950	0.015	0.015	0.000	0.000	0.000	0.000
112	A	121	ASN	0	-0.026	-0.019	23.184	-0.009	-0.009	0.000	0.000	0.000	0.000
113	A	122	GLY	0	0.007	0.012	20.462	-0.015	-0.015	0.000	0.000	0.000	0.000
114	A	123	LEU	0	-0.005	0.010	17.769	-0.040	-0.040	0.000	0.000	0.000	0.000
115	A	124	LEU	0	-0.024	-0.015	19.414	0.031	0.031	0.000	0.000	0.000	0.000
116	A	125	THR	0	0.014	-0.001	20.195	-0.017	-0.017	0.000	0.000	0.000	0.000
117	A	126	VAL	0	-0.032	-0.024	22.011	0.016	0.016	0.000	0.000	0.000	0.000
118	A	127	THR	0	-0.044	-0.032	23.516	-0.009	-0.009	0.000	0.000	0.000	0.000
119	A	128	LEU	0	0.009	-0.007	23.476	0.008	0.008	0.000	0.000	0.000	0.000
120	A	129	PRO	0	0.015	0.021	27.286	0.003	0.003	0.000	0.000	0.000	0.000
121	A	130	LYS	1	0.840	0.909	27.417	0.079	0.079	0.000	0.000	0.000	0.000
122	A	131	VAL	0	-0.015	-0.014	31.009	0.003	0.003	0.000	0.000	0.000	0.000
123	A	132	GLU	-1	-0.863	-0.912	33.404	-0.038	-0.038	0.000	0.000	0.000	0.000
124	A	133	LYS	1	0.907	0.934	32.929	0.050	0.050	0.000	0.000	0.000	0.000
125	A	134	SER	0	-0.011	-0.006	34.811	-0.001	-0.001	0.000	0.000	0.000	0.000
126	A	135	GLN	0	0.014	0.002	32.091	-0.005	-0.005	0.000	0.000	0.000	0.000
127	A	136	THR	0	0.026	0.009	31.437	0.003	0.003	0.000	0.000	0.000	0.000
128	A	137	LYS	1	0.904	0.964	24.958	0.087	0.087	0.000	0.000	0.000	0.000
129	A	138	LYS	1	0.901	0.939	30.187	0.029	0.029	0.000	0.000	0.000	0.000
130	A	139	GLN	0	0.029	0.022	29.036	-0.005	-0.005	0.000	0.000	0.000	0.000
131	A	140	ILE	0	0.001	0.001	29.876	0.003	0.003	0.000	0.000	0.000	0.000
132	A	141	ALA	0	0.018	0.007	30.760	-0.003	-0.003	0.000	0.000	0.000	0.000
133	A	142	ILE	0	0.013	0.006	28.056	0.004	0.004	0.000	0.000	0.000	0.000
134	A	143	LYS	1	0.975	0.997	31.407	-0.006	-0.006	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:10:PRO)