FMO DATABASE

FMODB ID: K35M3

Calculation Name: 2R2C-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2R2C

Chain ID: A

ChEMBL ID:

UniProt ID: Q9S3Q1

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:

Apendix: None

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
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	121
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1018777.718525
FMO2-HF: Nuclear repulsion	971083.438653
FMO2-HF: Total energy	-47694.279873
FMO2-MP2: Total energy	-47835.933196

3D Structure Molmil

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:36:LYS)

Summations of interaction energy for fragment #1(A:36:LYS)

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.
-55.263	-49.887	1.876	-2.838	-4.412	-0.01

Interaction energy analysis for fragmet #1(A:36:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 1.003 / q_NPA : 1.001

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	38	TYR	0	0.014	0.001	2.764	-13.079	-8.256	1.867	-2.614	-4.075	-0.009
4	A	39	LYS	1	0.848	0.929	5.926	20.471	20.471	0.000	0.000	0.000	0.000
5	A	40	THR	0	0.015	0.000	9.742	-1.161	-1.161	0.000	0.000	0.000	0.000
6	A	41	TRP	0	0.018	0.003	12.164	0.260	0.260	0.000	0.000	0.000	0.000
7	A	42	ASP	-1	-0.844	-0.907	15.003	-17.440	-17.440	0.000	0.000	0.000	0.000
8	A	43	VAL	0	0.028	0.010	17.971	0.043	0.043	0.000	0.000	0.000	0.000
9	A	44	PRO	0	-0.013	-0.004	21.544	0.085	0.085	0.000	0.000	0.000	0.000
10	A	45	ILE	0	0.007	0.015	24.165	0.357	0.357	0.000	0.000	0.000	0.000
11	A	53	ALA	0	0.023	0.007	34.535	-0.005	-0.005	0.000	0.000	0.000	0.000
12	A	54	LYS	1	0.812	0.901	34.252	8.978	8.978	0.000	0.000	0.000	0.000
13	A	55	ILE	0	-0.019	-0.010	32.439	0.232	0.232	0.000	0.000	0.000	0.000
14	A	56	ASN	0	-0.037	-0.026	33.178	0.152	0.152	0.000	0.000	0.000	0.000
15	A	57	ILE	0	-0.037	-0.017	28.358	0.123	0.123	0.000	0.000	0.000	0.000
16	A	58	PHE	0	-0.004	-0.002	31.124	-0.019	-0.019	0.000	0.000	0.000	0.000
17	A	59	ALA	0	0.025	0.000	27.456	-0.117	-0.117	0.000	0.000	0.000	0.000
18	A	60	VAL	0	0.004	0.011	29.223	0.104	0.104	0.000	0.000	0.000	0.000
19	A	61	ALA	0	0.021	0.010	24.421	-0.118	-0.118	0.000	0.000	0.000	0.000
20	A	62	GLU	-1	-0.835	-0.904	25.935	-10.428	-10.428	0.000	0.000	0.000	0.000
21	A	63	TYR	0	0.011	-0.013	19.611	-0.663	-0.663	0.000	0.000	0.000	0.000
22	A	64	THR	0	-0.011	-0.012	24.717	0.499	0.499	0.000	0.000	0.000	0.000
23	A	65	ASP	-1	-0.817	-0.918	21.938	-13.720	-13.720	0.000	0.000	0.000	0.000
24	A	66	THR	0	-0.035	-0.023	20.407	-0.205	-0.205	0.000	0.000	0.000	0.000
25	A	67	GLN	0	-0.034	-0.019	14.748	-0.297	-0.297	0.000	0.000	0.000	0.000
26	A	68	LYS	1	0.795	0.910	17.263	16.776	16.776	0.000	0.000	0.000	0.000
27	A	69	ILE	0	0.001	0.013	19.806	0.532	0.532	0.000	0.000	0.000	0.000
28	A	70	LYS	1	0.848	0.920	22.795	10.550	10.550	0.000	0.000	0.000	0.000
29	A	71	VAL	0	0.003	-0.007	23.481	-0.063	-0.063	0.000	0.000	0.000	0.000
30	A	72	THR	0	-0.028	-0.004	26.482	0.242	0.242	0.000	0.000	0.000	0.000
31	A	73	VAL	0	0.018	-0.007	26.712	-0.213	-0.213	0.000	0.000	0.000	0.000
32	A	74	LYS	1	0.841	0.907	30.051	8.725	8.725	0.000	0.000	0.000	0.000
33	A	75	GLY	0	0.052	0.024	32.915	-0.142	-0.142	0.000	0.000	0.000	0.000
34	A	76	LYS	1	0.789	0.875	34.018	7.797	7.797	0.000	0.000	0.000	0.000
35	A	77	ILE	0	0.047	0.019	37.222	-0.100	-0.100	0.000	0.000	0.000	0.000
36	A	78	LEU	0	-0.040	-0.006	37.856	0.188	0.188	0.000	0.000	0.000	0.000
37	A	79	GLU	-1	-0.818	-0.910	40.922	-7.034	-7.034	0.000	0.000	0.000	0.000
38	A	80	GLY	0	-0.031	-0.009	44.676	0.038	0.038	0.000	0.000	0.000	0.000
39	A	81	ASN	0	-0.041	0.000	39.485	0.167	0.167	0.000	0.000	0.000	0.000
40	A	82	THR	0	-0.055	-0.035	41.345	-0.014	-0.014	0.000	0.000	0.000	0.000
41	A	83	LEU	0	0.010	-0.008	33.572	-0.080	-0.080	0.000	0.000	0.000	0.000
42	A	84	PRO	0	0.016	0.022	35.137	0.129	0.129	0.000	0.000	0.000	0.000
43	A	85	LYS	1	0.825	0.908	33.447	8.767	8.767	0.000	0.000	0.000	0.000
44	A	86	SER	0	0.034	-0.001	31.191	-0.178	-0.178	0.000	0.000	0.000	0.000
45	A	87	MET	0	-0.042	0.005	26.224	0.299	0.299	0.000	0.000	0.000	0.000
46	A	88	VAL	0	0.021	0.003	27.060	0.060	0.060	0.000	0.000	0.000	0.000
47	A	89	GLN	0	-0.035	0.002	20.248	-0.582	-0.582	0.000	0.000	0.000	0.000
48	A	90	VAL	0	0.006	-0.006	21.674	0.242	0.242	0.000	0.000	0.000	0.000
49	A	91	TYR	0	-0.065	-0.043	16.546	-0.746	-0.746	0.000	0.000	0.000	0.000
50	A	92	LEU	0	0.009	0.016	14.524	0.667	0.667	0.000	0.000	0.000	0.000
51	A	93	LEU	0	-0.028	-0.013	14.455	-1.367	-1.367	0.000	0.000	0.000	0.000
52	A	94	GLU	-1	-0.750	-0.854	11.223	-27.249	-27.249	0.000	0.000	0.000	0.000
53	A	95	ASP	-1	-0.825	-0.900	12.667	-18.182	-18.182	0.000	0.000	0.000	0.000
54	A	96	LYS	1	0.812	0.892	8.534	25.685	25.685	0.000	0.000	0.000	0.000
55	A	114	ASN	0	-0.003	-0.009	12.764	0.640	0.640	0.000	0.000	0.000	0.000
56	A	115	HIS	0	-0.034	-0.021	12.769	-1.540	-1.540	0.000	0.000	0.000	0.000
57	A	116	VAL	0	-0.004	-0.004	7.779	-0.264	-0.264	0.000	0.000	0.000	0.000
58	A	117	LEU	0	-0.016	-0.016	10.956	1.064	1.064	0.000	0.000	0.000	0.000
59	A	118	ARG	1	0.765	0.860	9.221	26.832	26.832	0.000	0.000	0.000	0.000
60	A	119	GLY	0	0.011	0.007	11.813	-1.128	-1.128	0.000	0.000	0.000	0.000
61	A	120	ALA	0	-0.002	0.005	14.323	0.981	0.981	0.000	0.000	0.000	0.000
62	A	121	VAL	0	-0.026	-0.017	17.183	0.346	0.346	0.000	0.000	0.000	0.000
63	A	122	ASN	0	-0.007	-0.005	19.815	-0.116	-0.116	0.000	0.000	0.000	0.000
64	A	123	GLY	0	0.037	0.029	19.986	0.530	0.530	0.000	0.000	0.000	0.000
65	A	124	ILE	0	0.007	-0.013	17.152	-0.322	-0.322	0.000	0.000	0.000	0.000
66	A	125	TRP	0	0.020	0.021	19.902	0.571	0.571	0.000	0.000	0.000	0.000
67	A	126	GLY	0	0.025	0.038	22.389	0.335	0.335	0.000	0.000	0.000	0.000
68	A	127	GLU	-1	-0.796	-0.881	24.092	-10.692	-10.692	0.000	0.000	0.000	0.000
69	A	128	GLU	-1	-0.762	-0.874	27.837	-9.165	-9.165	0.000	0.000	0.000	0.000
70	A	129	PHE	0	-0.031	-0.009	30.795	0.051	0.051	0.000	0.000	0.000	0.000
71	A	130	VAL	0	-0.002	-0.002	32.215	0.286	0.286	0.000	0.000	0.000	0.000
72	A	131	ASN	0	0.059	0.020	35.782	-0.199	-0.199	0.000	0.000	0.000	0.000
73	A	132	LEU	0	-0.019	-0.016	37.426	0.164	0.164	0.000	0.000	0.000	0.000
74	A	133	LYS	1	0.850	0.958	31.906	9.905	9.905	0.000	0.000	0.000	0.000
75	A	134	ASP	-1	-0.858	-0.912	34.512	-8.862	-8.862	0.000	0.000	0.000	0.000
76	A	135	TYR	0	-0.067	-0.047	29.469	0.120	0.120	0.000	0.000	0.000	0.000
77	A	136	LEU	0	-0.017	-0.016	29.048	0.000	0.000	0.000	0.000	0.000	0.000
78	A	137	TYR	0	-0.032	-0.047	24.185	-0.117	-0.117	0.000	0.000	0.000	0.000
79	A	138	THR	0	-0.018	-0.016	24.042	0.151	0.151	0.000	0.000	0.000	0.000
80	A	139	TYR	0	0.011	0.008	15.219	-0.679	-0.679	0.000	0.000	0.000	0.000
81	A	140	ALA	0	0.005	0.010	16.683	0.514	0.514	0.000	0.000	0.000	0.000
82	A	141	VAL	0	-0.006	0.006	15.200	-1.095	-1.095	0.000	0.000	0.000	0.000
83	A	142	GLU	-1	-0.785	-0.898	11.406	-19.927	-19.927	0.000	0.000	0.000	0.000
84	A	143	PRO	0	0.010	0.025	9.576	-0.900	-0.900	0.000	0.000	0.000	0.000
85	A	144	LEU	0	0.003	-0.004	5.084	-2.285	-2.285	0.000	0.000	0.000	0.000
86	A	145	SER	0	-0.022	-0.033	3.347	0.054	0.281	0.009	-0.047	-0.188	0.000
87	A	146	GLY	0	0.006	0.007	3.765	-11.292	-10.966	0.000	-0.177	-0.149	-0.001
88	A	147	MET	0	-0.062	-0.001	6.515	3.158	3.158	0.000	0.000	0.000	0.000
89	A	148	SER	0	0.026	0.013	8.936	0.128	0.128	0.000	0.000	0.000	0.000
90	A	149	PHE	0	0.010	0.007	12.188	-1.168	-1.168	0.000	0.000	0.000	0.000
91	A	150	VAL	0	-0.013	-0.013	14.165	0.803	0.803	0.000	0.000	0.000	0.000
92	A	151	ALA	0	0.051	0.032	16.927	-0.389	-0.389	0.000	0.000	0.000	0.000
93	A	152	GLU	-1	-0.877	-0.955	19.315	-15.185	-15.185	0.000	0.000	0.000	0.000
94	A	153	ASN	0	-0.040	-0.011	15.228	0.885	0.885	0.000	0.000	0.000	0.000
95	A	154	TYR	0	-0.083	-0.050	12.020	-0.759	-0.759	0.000	0.000	0.000	0.000
96	A	155	SER	0	-0.044	-0.017	17.665	1.182	1.182	0.000	0.000	0.000	0.000
97	A	156	ILE	0	0.013	-0.001	18.756	-0.827	-0.827	0.000	0.000	0.000	0.000
98	A	157	VAL	0	0.026	0.027	19.139	0.631	0.631	0.000	0.000	0.000	0.000
99	A	158	ALA	0	0.000	-0.007	21.707	-0.387	-0.387	0.000	0.000	0.000	0.000
100	A	159	PHE	0	0.001	0.005	20.471	0.345	0.345	0.000	0.000	0.000	0.000
101	A	160	VAL	0	0.006	0.004	25.669	-0.103	-0.103	0.000	0.000	0.000	0.000
102	A	161	TYR	0	-0.077	-0.058	24.177	0.009	0.009	0.000	0.000	0.000	0.000
103	A	162	ASP	-1	-0.727	-0.820	27.985	-9.333	-9.333	0.000	0.000	0.000	0.000
104	A	163	VAL	0	-0.018	-0.014	28.621	-0.322	-0.322	0.000	0.000	0.000	0.000
105	A	164	GLN	0	-0.095	-0.053	29.649	0.126	0.126	0.000	0.000	0.000	0.000
106	A	165	THR	0	-0.041	-0.030	30.459	-0.039	-0.039	0.000	0.000	0.000	0.000
107	A	166	PHE	0	-0.039	-0.017	25.165	-0.193	-0.193	0.000	0.000	0.000	0.000
108	A	167	GLU	-1	-0.778	-0.873	26.418	-9.485	-9.485	0.000	0.000	0.000	0.000
109	A	168	VAL	0	-0.004	-0.017	23.859	0.002	0.002	0.000	0.000	0.000	0.000
110	A	169	TYR	0	-0.057	-0.064	27.253	0.241	0.241	0.000	0.000	0.000	0.000
111	A	170	ASP	-1	-0.789	-0.878	29.030	-9.612	-9.612	0.000	0.000	0.000	0.000
112	A	171	VAL	0	-0.034	-0.032	23.826	-0.443	-0.443	0.000	0.000	0.000	0.000
113	A	172	VAL	0	-0.006	0.019	26.266	0.256	0.256	0.000	0.000	0.000	0.000
114	A	173	HIS	0	-0.025	-0.026	19.377	-0.078	-0.078	0.000	0.000	0.000	0.000
115	A	174	VAL	0	-0.038	-0.009	23.772	0.418	0.418	0.000	0.000	0.000	0.000
116	A	175	LYS	1	1.000	0.981	23.108	11.362	11.362	0.000	0.000	0.000	0.000
117	A	176	ILE	0	-0.006	0.016	19.600	0.359	0.359	0.000	0.000	0.000	0.000
118	A	177	ASN	0	-0.042	-0.024	23.920	0.084	0.084	0.000	0.000	0.000	0.000
119	A	178	PRO	0	0.030	0.001	26.362	-0.320	-0.320	0.000	0.000	0.000	0.000
120	A	179	GLN	0	-0.002	0.010	26.719	0.170	0.170	0.000	0.000	0.000	0.000
121	A	180	SER	0	-0.029	-0.005	29.072	0.294	0.294	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:36:LYS)