FMO DATABASE

FMODB ID: 53YGZ

Calculation Name: 2CIU-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2CIU

Chain ID: A

ChEMBL ID:

UniProt ID: P53220

Base Structure: X-ray

Registration Date: 2023-03-13

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	123
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1058023.64626
FMO2-HF: Nuclear repulsion	1007597.732131
FMO2-HF: Total energy	-50425.914129
FMO2-MP2: Total energy	-50573.371715

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:103:SER)

Summations of interaction energy for fragment #1(A:103: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.
-3.912	-3.813	13.678	-6.693	-7.084	0.022

Interaction energy analysis for fragmet #1(A:103:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.066 / 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	105	ASP	-1	-0.742	-0.862	3.809	-2.035	-0.746	-0.003	-0.505	-0.781	0.002
4	A	106	THR	0	0.004	0.006	2.482	-1.594	0.020	0.834	-0.979	-1.469	0.003
5	A	107	GLN	0	-0.020	-0.010	1.531	-2.629	-5.663	12.845	-5.130	-4.681	0.017
6	A	108	LEU	0	-0.029	-0.005	3.907	1.184	1.414	0.002	-0.079	-0.153	0.000
7	A	109	PHE	0	0.071	0.019	6.866	0.429	0.429	0.000	0.000	0.000	0.000
8	A	110	ASN	0	0.033	0.014	5.747	0.034	0.034	0.000	0.000	0.000	0.000
9	A	111	ARG	1	0.875	0.951	7.846	0.654	0.654	0.000	0.000	0.000	0.000
10	A	112	ALA	0	0.012	-0.007	9.716	0.104	0.104	0.000	0.000	0.000	0.000
11	A	113	VAL	0	0.034	0.012	11.233	0.062	0.062	0.000	0.000	0.000	0.000
12	A	114	SER	0	-0.042	-0.033	11.466	0.073	0.073	0.000	0.000	0.000	0.000
13	A	115	MET	0	-0.033	-0.024	13.983	0.007	0.007	0.000	0.000	0.000	0.000
14	A	116	VAL	0	-0.006	-0.003	16.035	0.016	0.016	0.000	0.000	0.000	0.000
15	A	117	GLU	-1	-0.862	-0.908	16.891	0.068	0.068	0.000	0.000	0.000	0.000
16	A	118	LYS	1	0.825	0.898	15.271	-0.033	-0.033	0.000	0.000	0.000	0.000
17	A	119	ASN	0	0.014	0.032	20.148	0.007	0.007	0.000	0.000	0.000	0.000
18	A	120	LYS	1	0.992	0.995	22.308	-0.001	-0.001	0.000	0.000	0.000	0.000
19	A	121	ASP	-1	-0.775	-0.876	25.907	-0.018	-0.018	0.000	0.000	0.000	0.000
20	A	122	ILE	0	-0.019	-0.014	21.683	0.001	0.001	0.000	0.000	0.000	0.000
21	A	123	ARG	1	0.738	0.817	21.756	-0.016	-0.016	0.000	0.000	0.000	0.000
22	A	124	SER	0	-0.010	-0.001	25.330	0.004	0.004	0.000	0.000	0.000	0.000
23	A	125	LEU	0	-0.018	-0.001	26.322	0.001	0.001	0.000	0.000	0.000	0.000
24	A	126	LEU	0	-0.050	-0.031	22.239	0.001	0.001	0.000	0.000	0.000	0.000
25	A	127	GLN	0	-0.031	-0.003	26.949	0.006	0.006	0.000	0.000	0.000	0.000
26	A	128	CYS	0	-0.076	-0.018	25.341	0.002	0.002	0.000	0.000	0.000	0.000
27	A	129	ASP	-1	-0.933	-0.951	27.997	0.023	0.023	0.000	0.000	0.000	0.000
28	A	130	ASP	-1	-0.808	-0.892	27.017	0.024	0.024	0.000	0.000	0.000	0.000
29	A	131	GLY	0	0.055	0.013	29.679	-0.003	-0.003	0.000	0.000	0.000	0.000
30	A	132	ILE	0	-0.007	-0.008	31.459	0.003	0.003	0.000	0.000	0.000	0.000
31	A	133	THR	0	-0.013	0.001	32.677	0.002	0.002	0.000	0.000	0.000	0.000
32	A	134	GLY	0	0.003	0.008	28.629	0.005	0.005	0.000	0.000	0.000	0.000
33	A	135	LYS	1	0.913	0.961	22.731	-0.033	-0.033	0.000	0.000	0.000	0.000
34	A	136	GLU	-1	-0.756	-0.864	24.903	0.030	0.030	0.000	0.000	0.000	0.000
35	A	137	ARG	1	0.923	0.958	21.562	-0.067	-0.067	0.000	0.000	0.000	0.000
36	A	138	LEU	0	0.010	0.006	19.791	-0.002	-0.002	0.000	0.000	0.000	0.000
37	A	139	LYS	1	0.966	0.999	18.645	-0.032	-0.032	0.000	0.000	0.000	0.000
38	A	140	ALA	0	0.011	0.006	14.759	-0.014	-0.014	0.000	0.000	0.000	0.000
39	A	141	TYR	0	-0.094	-0.062	14.495	0.017	0.017	0.000	0.000	0.000	0.000
40	A	142	GLY	0	0.044	0.018	14.268	-0.024	-0.024	0.000	0.000	0.000	0.000
41	A	143	GLU	-1	-0.919	-0.970	14.816	-0.013	-0.013	0.000	0.000	0.000	0.000
42	A	144	LEU	0	0.004	0.004	17.742	0.013	0.013	0.000	0.000	0.000	0.000
43	A	145	ILE	0	-0.044	-0.011	19.989	-0.002	-0.002	0.000	0.000	0.000	0.000
44	A	146	THR	0	0.065	0.007	22.723	0.004	0.004	0.000	0.000	0.000	0.000
45	A	147	ASN	0	-0.006	0.018	26.124	-0.001	-0.001	0.000	0.000	0.000	0.000
46	A	148	ASP	-1	-0.885	-0.954	28.652	0.007	0.007	0.000	0.000	0.000	0.000
47	A	149	LYS	1	0.859	0.946	30.335	-0.012	-0.012	0.000	0.000	0.000	0.000
48	A	150	TRP	0	0.068	0.014	25.432	-0.001	-0.001	0.000	0.000	0.000	0.000
49	A	151	THR	0	0.012	0.007	23.926	-0.001	-0.001	0.000	0.000	0.000	0.000
50	A	152	ARG	1	0.866	0.941	21.219	-0.024	-0.024	0.000	0.000	0.000	0.000
51	A	153	ASN	0	0.011	0.019	15.718	-0.004	-0.004	0.000	0.000	0.000	0.000
52	A	154	ARG	1	0.921	0.964	15.649	-0.007	-0.007	0.000	0.000	0.000	0.000
53	A	155	PRO	0	0.012	-0.005	11.652	-0.013	-0.013	0.000	0.000	0.000	0.000
54	A	156	ILE	0	0.013	0.001	8.725	-0.004	-0.004	0.000	0.000	0.000	0.000
55	A	157	VAL	0	-0.016	0.001	8.866	0.037	0.037	0.000	0.000	0.000	0.000
56	A	158	SER	0	-0.072	-0.054	9.280	-0.070	-0.070	0.000	0.000	0.000	0.000
57	A	159	THR	0	-0.011	-0.005	11.497	0.093	0.093	0.000	0.000	0.000	0.000
58	A	160	LYS	1	0.973	0.971	10.225	-0.303	-0.303	0.000	0.000	0.000	0.000
59	A	161	LYS	1	0.971	0.983	15.175	0.050	0.050	0.000	0.000	0.000	0.000
60	A	162	LEU	0	0.039	0.027	18.743	-0.016	-0.016	0.000	0.000	0.000	0.000
61	A	163	ASP	-1	-0.787	-0.856	20.560	-0.085	-0.085	0.000	0.000	0.000	0.000
62	A	164	LYS	1	0.964	0.946	22.985	0.046	0.046	0.000	0.000	0.000	0.000
63	A	165	GLU	-1	-0.961	-0.965	23.960	-0.074	-0.074	0.000	0.000	0.000	0.000
64	A	166	GLY	0	0.001	0.016	22.673	-0.002	-0.002	0.000	0.000	0.000	0.000
65	A	167	ARG	1	0.880	0.931	17.139	0.145	0.145	0.000	0.000	0.000	0.000
66	A	168	THR	0	0.000	-0.008	14.386	0.013	0.013	0.000	0.000	0.000	0.000
67	A	169	HIS	1	0.689	0.815	15.995	0.081	0.081	0.000	0.000	0.000	0.000
68	A	170	HIS	0	-0.016	-0.019	9.854	0.003	0.003	0.000	0.000	0.000	0.000
69	A	171	TYR	0	-0.043	-0.018	13.883	-0.031	-0.031	0.000	0.000	0.000	0.000
70	A	172	MET	0	0.001	0.000	8.374	0.020	0.020	0.000	0.000	0.000	0.000
71	A	173	ARG	1	0.908	0.956	13.941	0.053	0.053	0.000	0.000	0.000	0.000
72	A	174	PHE	0	-0.016	-0.009	13.216	-0.004	-0.004	0.000	0.000	0.000	0.000
73	A	175	HIS	0	0.056	0.033	15.939	0.002	0.002	0.000	0.000	0.000	0.000
74	A	176	VAL	0	-0.002	-0.010	17.003	-0.002	-0.002	0.000	0.000	0.000	0.000
75	A	177	GLU	-1	-0.897	-0.934	19.304	0.018	0.018	0.000	0.000	0.000	0.000
76	A	178	SER	0	0.010	-0.015	22.391	0.006	0.006	0.000	0.000	0.000	0.000
77	A	179	LYS	1	0.923	0.940	25.055	-0.033	-0.033	0.000	0.000	0.000	0.000
78	A	180	LYS	1	0.935	0.979	28.183	-0.010	-0.010	0.000	0.000	0.000	0.000
79	A	181	LYS	1	0.868	0.950	27.235	0.002	0.002	0.000	0.000	0.000	0.000
80	A	182	ILE	0	0.053	0.035	22.715	0.001	0.001	0.000	0.000	0.000	0.000
81	A	183	ALA	0	-0.005	-0.005	21.636	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	184	LEU	0	-0.040	-0.007	19.638	0.000	0.000	0.000	0.000	0.000	0.000
83	A	185	VAL	0	-0.004	-0.005	16.395	-0.001	-0.001	0.000	0.000	0.000	0.000
84	A	186	HIS	0	0.035	0.028	17.700	0.000	0.000	0.000	0.000	0.000	0.000
85	A	187	LEU	0	-0.004	-0.012	11.757	-0.002	-0.002	0.000	0.000	0.000	0.000
86	A	188	GLU	-1	-0.846	-0.899	15.729	-0.108	-0.108	0.000	0.000	0.000	0.000
87	A	189	ALA	0	-0.001	-0.004	12.332	-0.014	-0.014	0.000	0.000	0.000	0.000
88	A	190	LYS	1	0.972	0.985	14.385	0.186	0.186	0.000	0.000	0.000	0.000
89	A	191	GLU	-1	-0.823	-0.889	12.041	-0.283	-0.283	0.000	0.000	0.000	0.000
90	A	192	SER	0	0.055	0.055	13.475	0.061	0.061	0.000	0.000	0.000	0.000
91	A	193	LYS	1	0.823	0.877	15.027	0.213	0.213	0.000	0.000	0.000	0.000
92	A	194	GLN	0	-0.004	0.010	17.395	0.007	0.007	0.000	0.000	0.000	0.000
93	A	195	ASN	0	0.008	0.001	14.161	0.033	0.033	0.000	0.000	0.000	0.000
94	A	196	TYR	0	0.018	0.022	5.536	-0.046	-0.046	0.000	0.000	0.000	0.000
95	A	197	GLN	0	0.018	0.005	9.208	-0.148	-0.148	0.000	0.000	0.000	0.000
96	A	198	PRO	0	-0.021	-0.010	8.720	0.101	0.101	0.000	0.000	0.000	0.000
97	A	199	ASP	-1	-0.848	-0.931	11.818	-0.215	-0.215	0.000	0.000	0.000	0.000
98	A	200	PHE	0	-0.034	-0.034	10.844	-0.020	-0.020	0.000	0.000	0.000	0.000
99	A	201	ILE	0	-0.029	-0.025	15.541	0.029	0.029	0.000	0.000	0.000	0.000
100	A	202	ASN	0	0.058	0.005	18.080	0.027	0.027	0.000	0.000	0.000	0.000
101	A	203	MET	0	-0.024	0.008	14.787	-0.026	-0.026	0.000	0.000	0.000	0.000
102	A	204	TYR	0	-0.047	-0.013	18.984	0.014	0.014	0.000	0.000	0.000	0.000
103	A	205	VAL	0	0.019	0.004	19.997	-0.008	-0.008	0.000	0.000	0.000	0.000
104	A	206	ASP	-1	-0.750	-0.850	22.315	-0.037	-0.037	0.000	0.000	0.000	0.000
105	A	207	VAL	0	0.018	0.006	24.816	0.001	0.001	0.000	0.000	0.000	0.000
106	A	208	PRO	0	0.012	-0.005	26.974	0.001	0.001	0.000	0.000	0.000	0.000
107	A	209	GLY	0	0.023	0.004	30.142	0.002	0.002	0.000	0.000	0.000	0.000
108	A	210	GLU	-1	-0.899	-0.929	29.463	-0.011	-0.011	0.000	0.000	0.000	0.000
109	A	211	LYS	1	0.922	0.967	30.636	0.024	0.024	0.000	0.000	0.000	0.000
110	A	212	ARG	1	0.819	0.893	25.593	0.043	0.043	0.000	0.000	0.000	0.000
111	A	213	TYR	0	-0.052	-0.051	23.834	-0.002	-0.002	0.000	0.000	0.000	0.000
112	A	214	TYR	0	-0.047	-0.039	23.383	-0.004	-0.004	0.000	0.000	0.000	0.000
113	A	215	LEU	0	-0.019	-0.003	18.458	0.005	0.005	0.000	0.000	0.000	0.000
114	A	216	ILE	0	-0.013	-0.009	17.011	-0.003	-0.003	0.000	0.000	0.000	0.000
115	A	217	LYS	1	0.961	0.983	21.123	0.046	0.046	0.000	0.000	0.000	0.000
116	A	218	PRO	0	0.031	0.016	22.764	-0.004	-0.004	0.000	0.000	0.000	0.000
117	A	219	LYS	1	0.983	0.994	24.051	0.083	0.083	0.000	0.000	0.000	0.000
118	A	220	LEU	0	-0.028	-0.011	26.006	0.006	0.006	0.000	0.000	0.000	0.000
119	A	221	HIS	0	-0.037	-0.012	27.703	0.001	0.001	0.000	0.000	0.000	0.000
120	A	222	PRO	0	0.017	-0.001	29.806	0.002	0.002	0.000	0.000	0.000	0.000
121	A	223	VAL	0	0.093	0.036	32.958	0.000	0.000	0.000	0.000	0.000	0.000
122	A	224	SER	0	-0.041	0.000	36.135	0.002	0.002	0.000	0.000	0.000	0.000
123	A	225	ASN	0	-0.015	-0.007	30.897	-0.003	-0.003	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:103:SER)