FMO DATABASE

FMODB ID: 7G9QK

Calculation Name: 1WKA-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1WKA

Chain ID: A

ChEMBL ID:

UniProt ID: P96142

Base Structure: X-ray

Registration Date: 2023-06-20

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	143
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1364492.273554
FMO2-HF: Nuclear repulsion	1308862.084464
FMO2-HF: Total energy	-55630.18909
FMO2-MP2: Total energy	-55796.76938

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:195:GLY)

Summations of interaction energy for fragment #1(A:195:GLY)

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.
-2.229	0.046	0.002	-0.967	-1.31	-0.001

Interaction energy analysis for fragmet #1(A:195:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.003 / q_NPA : -0.014

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	197	LEU	0	-0.034	-0.003	3.869	1.427	2.718	-0.014	-0.666	-0.611	-0.001
4	A	198	TYR	0	0.012	-0.002	5.759	0.250	0.250	0.000	0.000	0.000	0.000
5	A	199	THR	0	0.007	0.010	9.758	-0.022	-0.022	0.000	0.000	0.000	0.000
6	A	200	LEU	0	0.009	0.004	13.151	0.023	0.023	0.000	0.000	0.000	0.000
7	A	201	ARG	1	0.817	0.913	15.929	-0.069	-0.069	0.000	0.000	0.000	0.000
8	A	202	TYR	0	-0.014	-0.028	17.061	0.027	0.027	0.000	0.000	0.000	0.000
9	A	203	GLU	-1	-0.842	-0.917	21.930	0.088	0.088	0.000	0.000	0.000	0.000
10	A	204	VAL	0	0.004	-0.002	25.669	0.006	0.006	0.000	0.000	0.000	0.000
11	A	205	GLU	-1	-0.811	-0.880	28.070	0.051	0.051	0.000	0.000	0.000	0.000
12	A	206	GLY	0	-0.038	-0.023	31.473	-0.006	-0.006	0.000	0.000	0.000	0.000
13	A	207	GLY	0	-0.021	-0.011	31.719	-0.004	-0.004	0.000	0.000	0.000	0.000
14	A	208	GLY	0	-0.016	-0.002	28.896	-0.003	-0.003	0.000	0.000	0.000	0.000
15	A	209	PHE	0	0.005	-0.015	23.381	0.007	0.007	0.000	0.000	0.000	0.000
16	A	210	ILE	0	0.001	0.013	21.786	-0.013	-0.013	0.000	0.000	0.000	0.000
17	A	211	GLU	-1	-0.803	-0.910	18.459	0.017	0.017	0.000	0.000	0.000	0.000
18	A	212	ILE	0	-0.002	0.016	14.892	-0.021	-0.021	0.000	0.000	0.000	0.000
19	A	213	ALA	0	0.040	0.030	11.760	0.026	0.026	0.000	0.000	0.000	0.000
20	A	214	THR	0	-0.001	-0.006	10.276	0.084	0.084	0.000	0.000	0.000	0.000
21	A	215	VAL	0	0.060	0.026	4.869	-0.022	-0.022	0.000	0.000	0.000	0.000
22	A	216	ARG	1	0.725	0.832	6.251	0.412	0.412	0.000	0.000	0.000	0.000
23	A	217	PRO	0	0.060	0.041	8.223	-0.255	-0.255	0.000	0.000	0.000	0.000
24	A	218	GLU	-1	-0.686	-0.819	9.936	1.205	1.205	0.000	0.000	0.000	0.000
25	A	219	THR	0	-0.070	-0.053	12.458	-0.145	-0.145	0.000	0.000	0.000	0.000
26	A	220	VAL	0	0.028	0.028	14.130	-0.061	-0.061	0.000	0.000	0.000	0.000
27	A	221	PHE	0	0.063	0.025	16.091	-0.049	-0.049	0.000	0.000	0.000	0.000
28	A	222	ALA	0	-0.035	-0.004	18.345	-0.035	-0.035	0.000	0.000	0.000	0.000
29	A	223	ASP	-1	-0.736	-0.847	17.656	0.256	0.256	0.000	0.000	0.000	0.000
30	A	224	GLN	0	-0.041	-0.031	20.372	-0.008	-0.008	0.000	0.000	0.000	0.000
31	A	225	ALA	0	-0.010	-0.013	22.494	-0.017	-0.017	0.000	0.000	0.000	0.000
32	A	226	ILE	0	0.002	0.011	20.506	0.018	0.018	0.000	0.000	0.000	0.000
33	A	227	ALA	0	0.004	0.015	21.457	-0.013	-0.013	0.000	0.000	0.000	0.000
34	A	228	VAL	0	0.027	0.008	21.617	-0.002	-0.002	0.000	0.000	0.000	0.000
35	A	229	HIS	0	0.091	0.055	23.809	0.005	0.005	0.000	0.000	0.000	0.000
36	A	230	PRO	0	-0.013	-0.014	25.618	0.002	0.002	0.000	0.000	0.000	0.000
37	A	231	GLU	-1	-0.921	-0.965	28.840	-0.032	-0.032	0.000	0.000	0.000	0.000
38	A	232	ASP	-1	-0.796	-0.866	24.128	-0.051	-0.051	0.000	0.000	0.000	0.000
39	A	233	GLU	-1	-0.837	-0.921	27.592	-0.041	-0.041	0.000	0.000	0.000	0.000
40	A	234	ARG	1	0.747	0.846	21.367	0.077	0.077	0.000	0.000	0.000	0.000
41	A	235	TYR	0	-0.008	-0.036	21.113	0.013	0.013	0.000	0.000	0.000	0.000
42	A	236	ARG	1	0.896	0.953	27.418	0.022	0.022	0.000	0.000	0.000	0.000
43	A	237	HIS	0	-0.008	0.006	29.253	0.004	0.004	0.000	0.000	0.000	0.000
44	A	238	LEU	0	-0.018	-0.015	26.500	0.004	0.004	0.000	0.000	0.000	0.000
45	A	239	LEU	0	0.008	0.016	28.431	0.007	0.007	0.000	0.000	0.000	0.000
46	A	240	GLY	0	-0.061	-0.023	30.578	-0.002	-0.002	0.000	0.000	0.000	0.000
47	A	241	LYS	1	0.850	0.936	30.486	-0.021	-0.021	0.000	0.000	0.000	0.000
48	A	242	ARG	1	0.857	0.903	28.818	-0.055	-0.055	0.000	0.000	0.000	0.000
49	A	243	ALA	0	0.013	-0.001	24.435	-0.007	-0.007	0.000	0.000	0.000	0.000
50	A	244	ARG	1	0.817	0.890	25.478	-0.109	-0.109	0.000	0.000	0.000	0.000
51	A	245	ILE	0	-0.028	-0.015	20.187	0.005	0.005	0.000	0.000	0.000	0.000
52	A	246	PRO	0	-0.008	0.003	18.470	-0.001	-0.001	0.000	0.000	0.000	0.000
53	A	247	LEU	0	-0.029	-0.017	18.523	0.026	0.026	0.000	0.000	0.000	0.000
54	A	248	THR	0	-0.060	-0.026	22.068	-0.002	-0.002	0.000	0.000	0.000	0.000
55	A	249	GLU	-1	-0.789	-0.873	24.735	0.097	0.097	0.000	0.000	0.000	0.000
56	A	250	VAL	0	-0.022	-0.007	24.968	-0.012	-0.012	0.000	0.000	0.000	0.000
57	A	251	TRP	0	-0.047	-0.026	25.948	0.002	0.002	0.000	0.000	0.000	0.000
58	A	252	ILE	0	-0.042	-0.012	22.076	-0.004	-0.004	0.000	0.000	0.000	0.000
59	A	253	PRO	0	-0.027	-0.010	26.683	-0.006	-0.006	0.000	0.000	0.000	0.000
60	A	254	ILE	0	0.047	0.031	25.390	0.006	0.006	0.000	0.000	0.000	0.000
61	A	255	LEU	0	-0.046	-0.028	25.496	-0.007	-0.007	0.000	0.000	0.000	0.000
62	A	256	ALA	0	0.042	0.014	26.146	-0.002	-0.002	0.000	0.000	0.000	0.000
63	A	257	ASP	-1	-0.754	-0.868	24.274	0.026	0.026	0.000	0.000	0.000	0.000
64	A	258	PRO	0	-0.018	-0.023	25.129	-0.005	-0.005	0.000	0.000	0.000	0.000
65	A	259	ALA	0	0.001	0.018	22.408	-0.009	-0.009	0.000	0.000	0.000	0.000
66	A	260	VAL	0	-0.062	-0.017	19.845	-0.005	-0.005	0.000	0.000	0.000	0.000
67	A	261	GLU	-1	-0.822	-0.918	19.105	-0.111	-0.111	0.000	0.000	0.000	0.000
68	A	262	LYS	1	0.825	0.900	19.833	0.054	0.054	0.000	0.000	0.000	0.000
69	A	263	ASP	-1	-0.864	-0.930	19.387	-0.133	-0.133	0.000	0.000	0.000	0.000
70	A	264	PHE	0	-0.068	-0.028	11.542	-0.045	-0.045	0.000	0.000	0.000	0.000
71	A	265	GLY	0	0.009	0.001	13.739	0.041	0.041	0.000	0.000	0.000	0.000
72	A	266	THR	0	-0.046	-0.055	14.475	-0.011	-0.011	0.000	0.000	0.000	0.000
73	A	267	GLY	0	0.048	0.054	17.814	0.008	0.008	0.000	0.000	0.000	0.000
74	A	268	ALA	0	-0.065	-0.028	18.837	0.013	0.013	0.000	0.000	0.000	0.000
75	A	269	LEU	0	0.001	0.003	15.589	0.002	0.002	0.000	0.000	0.000	0.000
76	A	270	LYS	1	0.801	0.891	13.584	-0.363	-0.363	0.000	0.000	0.000	0.000
77	A	271	VAL	0	0.022	0.022	17.421	0.002	0.002	0.000	0.000	0.000	0.000
78	A	272	THR	0	-0.026	-0.034	16.544	0.022	0.022	0.000	0.000	0.000	0.000
79	A	273	PRO	0	0.033	-0.003	18.750	0.013	0.013	0.000	0.000	0.000	0.000
80	A	274	ALA	0	-0.020	0.004	20.842	-0.012	-0.012	0.000	0.000	0.000	0.000
81	A	275	HIS	0	-0.042	-0.032	15.494	0.041	0.041	0.000	0.000	0.000	0.000
82	A	276	ASP	-1	-0.772	-0.869	13.800	0.224	0.224	0.000	0.000	0.000	0.000
83	A	277	PRO	0	0.014	0.020	15.896	-0.014	-0.014	0.000	0.000	0.000	0.000
84	A	278	LEU	0	0.053	0.033	16.923	-0.015	-0.015	0.000	0.000	0.000	0.000
85	A	279	ASP	-1	-0.773	-0.884	16.966	0.168	0.168	0.000	0.000	0.000	0.000
86	A	280	TYR	0	-0.138	-0.080	19.741	0.000	0.000	0.000	0.000	0.000	0.000
87	A	281	GLU	-1	-0.841	-0.892	22.250	0.010	0.010	0.000	0.000	0.000	0.000
88	A	282	ILE	0	-0.024	-0.015	20.379	-0.007	-0.007	0.000	0.000	0.000	0.000
89	A	283	GLY	0	0.013	-0.007	23.644	-0.002	-0.002	0.000	0.000	0.000	0.000
90	A	284	GLU	-1	-0.878	-0.920	25.246	0.050	0.050	0.000	0.000	0.000	0.000
91	A	285	ARG	1	0.727	0.830	24.250	-0.026	-0.026	0.000	0.000	0.000	0.000
92	A	286	HIS	1	0.765	0.863	26.315	-0.045	-0.045	0.000	0.000	0.000	0.000
93	A	287	GLY	0	0.018	0.028	29.693	0.002	0.002	0.000	0.000	0.000	0.000
94	A	288	LEU	0	-0.060	-0.022	24.339	0.004	0.004	0.000	0.000	0.000	0.000
95	A	289	LYS	1	0.976	0.982	26.730	-0.076	-0.076	0.000	0.000	0.000	0.000
96	A	290	PRO	0	0.051	0.035	24.336	0.009	0.009	0.000	0.000	0.000	0.000
97	A	291	VAL	0	-0.011	-0.006	22.893	-0.006	-0.006	0.000	0.000	0.000	0.000
98	A	292	SER	0	0.001	0.000	20.742	0.026	0.026	0.000	0.000	0.000	0.000
99	A	293	VAL	0	0.002	-0.004	17.598	-0.014	-0.014	0.000	0.000	0.000	0.000
100	A	294	ILE	0	-0.025	-0.017	14.533	0.048	0.048	0.000	0.000	0.000	0.000
101	A	295	ASN	0	0.000	0.000	18.854	-0.012	-0.012	0.000	0.000	0.000	0.000
102	A	296	LEU	0	0.031	0.002	19.615	0.024	0.024	0.000	0.000	0.000	0.000
103	A	297	GLU	-1	-0.887	-0.932	20.141	0.212	0.212	0.000	0.000	0.000	0.000
104	A	298	GLY	0	-0.017	0.004	16.623	0.016	0.016	0.000	0.000	0.000	0.000
105	A	299	ARG	1	0.829	0.895	16.044	-0.186	-0.186	0.000	0.000	0.000	0.000
106	A	300	MET	0	-0.021	0.012	15.786	0.012	0.012	0.000	0.000	0.000	0.000
107	A	301	GLU	-1	-0.914	-0.954	18.863	0.178	0.178	0.000	0.000	0.000	0.000
108	A	302	GLY	0	0.049	0.017	22.348	0.005	0.005	0.000	0.000	0.000	0.000
109	A	303	GLU	-1	-0.968	-0.988	24.637	0.146	0.146	0.000	0.000	0.000	0.000
110	A	304	ARG	1	0.836	0.879	22.294	-0.186	-0.186	0.000	0.000	0.000	0.000
111	A	305	VAL	0	-0.012	0.020	19.373	0.014	0.014	0.000	0.000	0.000	0.000
112	A	306	PRO	0	0.044	0.021	19.725	-0.023	-0.023	0.000	0.000	0.000	0.000
113	A	307	GLU	-1	-0.856	-0.916	21.737	0.187	0.187	0.000	0.000	0.000	0.000
114	A	308	ALA	0	-0.013	-0.010	21.383	0.005	0.005	0.000	0.000	0.000	0.000
115	A	309	LEU	0	-0.027	-0.021	16.150	0.035	0.035	0.000	0.000	0.000	0.000
116	A	310	ARG	1	0.819	0.900	18.857	-0.176	-0.176	0.000	0.000	0.000	0.000
117	A	311	GLY	0	-0.008	0.001	21.392	-0.007	-0.007	0.000	0.000	0.000	0.000
118	A	312	LEU	0	-0.028	-0.005	16.569	0.001	0.001	0.000	0.000	0.000	0.000
119	A	313	ASP	-1	-0.797	-0.898	13.111	0.651	0.651	0.000	0.000	0.000	0.000
120	A	314	ARG	1	0.913	0.945	10.051	-0.812	-0.812	0.000	0.000	0.000	0.000
121	A	315	PHE	0	-0.047	-0.039	7.433	0.153	0.153	0.000	0.000	0.000	0.000
122	A	316	GLU	-1	-0.784	-0.881	10.251	0.733	0.733	0.000	0.000	0.000	0.000
123	A	317	ALA	0	0.004	0.003	12.952	-0.015	-0.015	0.000	0.000	0.000	0.000
124	A	318	ARG	1	0.798	0.877	4.985	-2.995	-2.995	0.000	0.000	0.000	0.000
125	A	319	ARG	1	0.844	0.911	8.732	-0.900	-0.900	0.000	0.000	0.000	0.000
126	A	320	LYS	1	0.915	0.949	10.522	-0.533	-0.533	0.000	0.000	0.000	0.000
127	A	321	ALA	0	0.013	0.009	12.645	-0.076	-0.076	0.000	0.000	0.000	0.000
128	A	322	VAL	0	-0.012	0.006	8.858	-0.067	-0.067	0.000	0.000	0.000	0.000
129	A	323	GLU	-1	-0.786	-0.853	12.160	0.243	0.243	0.000	0.000	0.000	0.000
130	A	324	LEU	0	0.026	0.016	14.763	-0.060	-0.060	0.000	0.000	0.000	0.000
131	A	325	PHE	0	-0.023	-0.030	13.702	-0.043	-0.043	0.000	0.000	0.000	0.000
132	A	326	ARG	1	0.715	0.805	11.320	-0.253	-0.253	0.000	0.000	0.000	0.000
133	A	327	GLU	-1	-0.963	-0.983	16.867	0.173	0.173	0.000	0.000	0.000	0.000
134	A	328	ALA	0	-0.028	-0.011	20.024	-0.023	-0.023	0.000	0.000	0.000	0.000
135	A	329	GLY	0	-0.002	0.010	20.420	-0.013	-0.013	0.000	0.000	0.000	0.000
136	A	330	HIS	0	-0.002	-0.006	18.473	-0.010	-0.010	0.000	0.000	0.000	0.000
137	A	331	LEU	0	-0.037	-0.011	12.162	0.005	0.005	0.000	0.000	0.000	0.000
138	A	332	VAL	0	-0.074	-0.022	15.792	-0.032	-0.032	0.000	0.000	0.000	0.000
139	A	333	LYS	1	0.799	0.872	13.429	0.210	0.210	0.000	0.000	0.000	0.000
140	A	334	GLU	-1	-0.829	-0.914	8.775	0.219	0.219	0.000	0.000	0.000	0.000
141	A	335	GLU	-1	-0.806	-0.895	8.340	-0.376	-0.376	0.000	0.000	0.000	0.000
142	A	336	ASP	-1	-0.879	-0.917	5.045	-2.065	-2.016	-0.001	-0.019	-0.029	0.000
143	A	337	TYR	0	-0.033	-0.010	3.456	0.478	1.413	0.017	-0.282	-0.670	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:195:GLY)