FMO DATABASE

FMODB ID: N91MQ

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	OptH
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	-1029322.672079
FMO2-HF: Nuclear repulsion	977942.900175
FMO2-HF: Total energy	-51379.771904
FMO2-MP2: Total energy	-51533.02185

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.
-1.336	0.772	-0.003	-0.716	-1.389	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 : 0.008 / q_NPA : -0.016

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	0.039	0.014	3.837	-0.249	1.145	-0.015	-0.566	-0.813	0.002
4	A	13	VAL	0	-0.025	0.002	6.230	0.404	0.404	0.000	0.000	0.000	0.000
5	A	14	ASN	0	-0.006	-0.011	9.878	-0.116	-0.116	0.000	0.000	0.000	0.000
6	A	15	ASP	-1	-0.824	-0.915	12.114	-0.423	-0.423	0.000	0.000	0.000	0.000
7	A	16	LEU	0	-0.031	-0.015	11.638	0.036	0.036	0.000	0.000	0.000	0.000
8	A	17	PHE	0	-0.023	-0.028	15.106	0.040	0.040	0.000	0.000	0.000	0.000
9	A	18	SER	0	0.011	0.014	17.129	0.040	0.040	0.000	0.000	0.000	0.000
10	A	19	ASP	-1	-0.851	-0.925	19.054	-0.102	-0.102	0.000	0.000	0.000	0.000
11	A	20	PHE	0	-0.074	-0.027	21.325	0.021	0.021	0.000	0.000	0.000	0.000
12	A	21	VAL	0	-0.035	-0.027	16.757	0.028	0.028	0.000	0.000	0.000	0.000
13	A	22	SER	0	0.014	0.011	16.914	-0.020	-0.020	0.000	0.000	0.000	0.000
14	A	23	TYR	0	0.001	-0.006	8.200	0.025	0.025	0.000	0.000	0.000	0.000
15	A	24	SER	0	0.005	-0.007	12.789	0.074	0.074	0.000	0.000	0.000	0.000
16	A	25	PRO	0	0.018	0.019	11.902	-0.042	-0.042	0.000	0.000	0.000	0.000
17	A	26	ARG	1	0.938	0.981	12.848	0.010	0.010	0.000	0.000	0.000	0.000
18	A	27	LEU	0	-0.009	-0.018	12.995	0.022	0.022	0.000	0.000	0.000	0.000
19	A	28	ASN	0	0.042	0.015	9.036	-0.005	-0.005	0.000	0.000	0.000	0.000
20	A	29	ASN	0	-0.033	-0.024	9.599	-0.052	-0.052	0.000	0.000	0.000	0.000
21	A	30	GLN	0	-0.006	-0.004	3.202	-0.356	0.043	0.010	-0.098	-0.311	0.000
22	A	31	ILE	0	0.024	0.012	7.337	-0.206	-0.206	0.000	0.000	0.000	0.000
23	A	32	PRO	0	0.005	0.001	3.785	-0.506	-0.191	0.002	-0.052	-0.265	0.000
24	A	33	GLY	0	-0.008	-0.003	5.731	0.431	0.431	0.000	0.000	0.000	0.000
25	A	34	GLU	-1	-0.889	-0.934	7.147	-0.726	-0.726	0.000	0.000	0.000	0.000
26	A	35	LEU	0	-0.078	-0.040	8.823	-0.281	-0.281	0.000	0.000	0.000	0.000
27	A	36	SER	0	0.023	0.004	8.328	0.032	0.032	0.000	0.000	0.000	0.000
28	A	37	PRO	0	-0.024	0.000	9.826	-0.136	-0.136	0.000	0.000	0.000	0.000
29	A	38	SER	0	0.016	0.007	9.352	-0.119	-0.119	0.000	0.000	0.000	0.000
30	A	39	ILE	0	-0.031	-0.021	10.626	0.132	0.132	0.000	0.000	0.000	0.000
31	A	40	ASP	-1	-0.886	-0.914	11.859	-0.558	-0.558	0.000	0.000	0.000	0.000
32	A	41	VAL	0	-0.037	-0.035	14.292	0.034	0.034	0.000	0.000	0.000	0.000
33	A	42	HIS	0	-0.015	0.000	16.991	0.053	0.053	0.000	0.000	0.000	0.000
34	A	43	GLU	-1	-0.885	-0.947	19.912	-0.118	-0.118	0.000	0.000	0.000	0.000
35	A	44	GLY	0	-0.047	-0.019	23.069	0.015	0.015	0.000	0.000	0.000	0.000
36	A	45	LYS	1	0.789	0.895	26.226	0.071	0.071	0.000	0.000	0.000	0.000
37	A	46	ASP	-1	-0.843	-0.951	29.783	-0.084	-0.084	0.000	0.000	0.000	0.000
38	A	47	THR	0	-0.017	-0.006	25.722	-0.003	-0.003	0.000	0.000	0.000	0.000
39	A	48	VAL	0	0.052	0.039	21.902	0.004	0.004	0.000	0.000	0.000	0.000
40	A	49	SER	0	-0.028	-0.011	21.715	0.004	0.004	0.000	0.000	0.000	0.000
41	A	50	VAL	0	0.003	-0.002	17.401	-0.013	-0.013	0.000	0.000	0.000	0.000
42	A	51	ASP	-1	-0.832	-0.878	16.928	-0.292	-0.292	0.000	0.000	0.000	0.000
43	A	52	VAL	0	0.001	-0.018	14.932	-0.065	-0.065	0.000	0.000	0.000	0.000
44	A	53	GLU	-1	-0.947	-0.964	12.682	-0.650	-0.650	0.000	0.000	0.000	0.000
45	A	54	LEU	0	-0.049	-0.037	15.093	-0.059	-0.059	0.000	0.000	0.000	0.000
46	A	55	PRO	0	0.046	0.020	15.542	0.063	0.063	0.000	0.000	0.000	0.000
47	A	56	GLY	0	-0.063	-0.047	18.587	-0.014	-0.014	0.000	0.000	0.000	0.000
48	A	57	VAL	0	0.019	0.023	19.467	0.009	0.009	0.000	0.000	0.000	0.000
49	A	58	LYS	1	0.943	0.975	22.285	0.234	0.234	0.000	0.000	0.000	0.000
50	A	59	LYS	1	1.002	0.976	25.294	0.182	0.182	0.000	0.000	0.000	0.000
51	A	60	GLU	-1	-1.015	-1.000	26.515	-0.190	-0.190	0.000	0.000	0.000	0.000
52	A	61	ASP	-1	-0.856	-0.926	24.386	-0.240	-0.240	0.000	0.000	0.000	0.000
53	A	62	VAL	0	-0.080	-0.023	21.800	-0.021	-0.021	0.000	0.000	0.000	0.000
54	A	63	GLN	0	-0.008	0.033	23.805	0.007	0.007	0.000	0.000	0.000	0.000
55	A	64	VAL	0	0.012	-0.005	23.042	-0.026	-0.026	0.000	0.000	0.000	0.000
56	A	65	HIS	0	0.005	0.005	24.585	0.030	0.030	0.000	0.000	0.000	0.000
57	A	66	TYR	0	0.013	0.003	25.172	-0.013	-0.013	0.000	0.000	0.000	0.000
58	A	67	ASP	-1	-0.804	-0.854	26.635	-0.131	-0.131	0.000	0.000	0.000	0.000
59	A	68	SER	0	-0.050	-0.076	27.271	-0.002	-0.002	0.000	0.000	0.000	0.000
60	A	69	GLY	0	-0.027	-0.007	26.782	0.006	0.006	0.000	0.000	0.000	0.000
61	A	70	LYS	1	0.848	0.922	23.067	0.142	0.142	0.000	0.000	0.000	0.000
62	A	71	LEU	0	0.019	0.020	20.547	0.012	0.012	0.000	0.000	0.000	0.000
63	A	72	THR	0	0.048	0.029	20.616	-0.035	-0.035	0.000	0.000	0.000	0.000
64	A	73	ILE	0	-0.022	-0.001	18.268	0.027	0.027	0.000	0.000	0.000	0.000
65	A	74	SER	0	-0.038	-0.060	18.941	-0.041	-0.041	0.000	0.000	0.000	0.000
66	A	75	GLY	0	0.046	0.017	20.598	0.028	0.028	0.000	0.000	0.000	0.000
67	A	76	GLU	-1	-0.857	-0.926	20.443	-0.382	-0.382	0.000	0.000	0.000	0.000
68	A	77	VAL	0	-0.028	0.001	16.520	0.019	0.019	0.000	0.000	0.000	0.000
69	A	78	VAL	0	0.076	0.032	19.551	-0.012	-0.012	0.000	0.000	0.000	0.000
70	A	79	ASN	0	-0.057	-0.032	20.710	0.014	0.014	0.000	0.000	0.000	0.000
71	A	80	GLU	-1	-0.853	-0.955	22.207	-0.214	-0.214	0.000	0.000	0.000	0.000
72	A	81	ARG	1	0.874	0.941	24.020	0.225	0.225	0.000	0.000	0.000	0.000
73	A	82	LYS	1	0.968	0.998	24.533	0.204	0.204	0.000	0.000	0.000	0.000
74	A	83	ASN	0	-0.077	-0.049	26.387	0.003	0.003	0.000	0.000	0.000	0.000
75	A	84	GLU	-1	-0.821	-0.917	29.610	-0.106	-0.106	0.000	0.000	0.000	0.000
76	A	85	SER	0	-0.068	-0.023	29.349	-0.012	-0.012	0.000	0.000	0.000	0.000
77	A	86	THR	0	-0.025	-0.023	30.422	0.005	0.005	0.000	0.000	0.000	0.000
78	A	87	GLU	-1	-0.981	-0.969	31.464	-0.133	-0.133	0.000	0.000	0.000	0.000
79	A	88	GLY	0	0.000	0.024	30.800	-0.005	-0.005	0.000	0.000	0.000	0.000
80	A	89	ASN	0	0.001	-0.018	26.873	-0.004	-0.004	0.000	0.000	0.000	0.000
81	A	90	GLN	0	0.030	0.058	20.640	-0.014	-0.014	0.000	0.000	0.000	0.000
82	A	91	ARG	1	0.930	0.958	23.648	0.125	0.125	0.000	0.000	0.000	0.000
83	A	92	TRP	0	-0.033	-0.022	15.836	0.027	0.027	0.000	0.000	0.000	0.000
84	A	93	SER	0	-0.032	-0.067	16.820	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	94	GLU	-1	-0.870	-0.923	12.732	-0.434	-0.434	0.000	0.000	0.000	0.000
86	A	95	ARG	1	0.894	0.954	12.480	0.327	0.327	0.000	0.000	0.000	0.000
87	A	96	ARG	1	0.935	0.976	5.868	1.726	1.726	0.000	0.000	0.000	0.000
88	A	97	PHE	0	-0.032	-0.027	13.608	0.010	0.010	0.000	0.000	0.000	0.000
89	A	98	GLY	0	0.027	0.022	15.863	-0.046	-0.046	0.000	0.000	0.000	0.000
90	A	99	SER	0	0.022	0.006	18.214	-0.009	-0.009	0.000	0.000	0.000	0.000
91	A	100	PHE	0	-0.025	-0.013	15.594	-0.075	-0.075	0.000	0.000	0.000	0.000
92	A	101	SER	0	0.027	-0.003	16.846	0.072	0.072	0.000	0.000	0.000	0.000
93	A	102	ARG	1	0.817	0.920	9.934	0.954	0.954	0.000	0.000	0.000	0.000
94	A	103	THR	0	-0.009	-0.009	16.531	0.044	0.044	0.000	0.000	0.000	0.000
95	A	104	ILE	0	-0.014	-0.007	16.422	-0.032	-0.032	0.000	0.000	0.000	0.000
96	A	105	THR	0	-0.023	-0.010	18.456	0.033	0.033	0.000	0.000	0.000	0.000
97	A	106	ILE	0	-0.018	-0.014	20.743	0.000	0.000	0.000	0.000	0.000	0.000
98	A	107	PRO	0	0.006	0.025	20.686	0.018	0.018	0.000	0.000	0.000	0.000
99	A	108	ALA	0	0.006	-0.018	23.287	0.016	0.016	0.000	0.000	0.000	0.000
100	A	109	LYS	1	0.935	0.979	26.839	0.082	0.082	0.000	0.000	0.000	0.000
101	A	110	ILE	0	0.027	0.003	26.783	0.005	0.005	0.000	0.000	0.000	0.000
102	A	111	ASP	-1	-0.909	-0.953	30.191	-0.094	-0.094	0.000	0.000	0.000	0.000
103	A	112	ALA	0	0.016	-0.016	31.139	-0.006	-0.006	0.000	0.000	0.000	0.000
104	A	113	ASP	-1	-0.892	-0.935	32.185	-0.108	-0.108	0.000	0.000	0.000	0.000
105	A	114	ARG	1	0.817	0.903	33.623	0.101	0.101	0.000	0.000	0.000	0.000
106	A	115	ILE	0	-0.043	0.003	27.300	-0.004	-0.004	0.000	0.000	0.000	0.000
107	A	116	GLU	-1	-0.946	-0.954	28.687	-0.137	-0.137	0.000	0.000	0.000	0.000
108	A	117	ALA	0	-0.013	-0.013	25.549	-0.015	-0.015	0.000	0.000	0.000	0.000
109	A	118	ASN	0	-0.034	-0.011	25.437	0.020	0.020	0.000	0.000	0.000	0.000
110	A	119	PHE	0	-0.011	-0.003	20.777	-0.011	-0.011	0.000	0.000	0.000	0.000
111	A	120	SER	0	-0.015	-0.012	23.810	0.018	0.018	0.000	0.000	0.000	0.000
112	A	121	ASN	0	0.003	-0.003	22.857	-0.009	-0.009	0.000	0.000	0.000	0.000
113	A	122	GLY	0	-0.005	0.006	20.545	-0.018	-0.018	0.000	0.000	0.000	0.000
114	A	123	LEU	0	0.023	0.026	17.214	-0.049	-0.049	0.000	0.000	0.000	0.000
115	A	124	LEU	0	-0.036	-0.018	19.348	0.040	0.040	0.000	0.000	0.000	0.000
116	A	125	THR	0	0.010	-0.020	19.885	-0.023	-0.023	0.000	0.000	0.000	0.000
117	A	126	VAL	0	-0.040	-0.026	21.780	0.022	0.022	0.000	0.000	0.000	0.000
118	A	127	THR	0	0.022	0.002	23.285	-0.010	-0.010	0.000	0.000	0.000	0.000
119	A	128	LEU	0	-0.007	-0.006	23.408	0.008	0.008	0.000	0.000	0.000	0.000
120	A	129	PRO	0	0.020	0.021	27.159	0.005	0.005	0.000	0.000	0.000	0.000
121	A	130	LYS	1	0.891	0.938	27.107	0.104	0.104	0.000	0.000	0.000	0.000
122	A	131	VAL	0	-0.050	-0.029	30.641	0.006	0.006	0.000	0.000	0.000	0.000
123	A	132	GLU	-1	-0.957	-0.966	32.948	-0.052	-0.052	0.000	0.000	0.000	0.000
124	A	133	LYS	1	0.970	0.974	32.770	0.070	0.070	0.000	0.000	0.000	0.000
125	A	134	SER	0	0.012	0.009	34.563	0.001	0.001	0.000	0.000	0.000	0.000
126	A	135	GLN	0	0.013	-0.004	32.649	-0.007	-0.007	0.000	0.000	0.000	0.000
127	A	136	THR	0	0.032	0.011	31.703	0.003	0.003	0.000	0.000	0.000	0.000
128	A	137	LYS	1	0.958	0.985	26.791	0.077	0.077	0.000	0.000	0.000	0.000
129	A	138	LYS	1	0.958	0.968	30.572	0.021	0.021	0.000	0.000	0.000	0.000
130	A	139	GLN	0	0.024	0.026	29.273	-0.004	-0.004	0.000	0.000	0.000	0.000
131	A	140	ILE	0	-0.013	-0.009	29.953	0.002	0.002	0.000	0.000	0.000	0.000
132	A	141	ALA	0	0.000	0.003	30.633	0.001	0.001	0.000	0.000	0.000	0.000
133	A	142	ILE	0	0.016	0.003	28.295	0.004	0.004	0.000	0.000	0.000	0.000
134	A	143	LYS	1	0.991	1.005	31.645	-0.043	-0.043	0.000	0.000	0.000	0.000

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