FMO DATABASE

FMODB ID: K9R33

Calculation Name: 5I27-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5I27

Chain ID: A

ChEMBL ID:

UniProt ID: P10258

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	87
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-643095.157909
FMO2-HF: Nuclear repulsion	608217.249811
FMO2-HF: Total energy	-34877.908098
FMO2-MP2: Total energy	-34982.326493

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:7:SER)

Summations of interaction energy for fragment #1(A:7: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.
-1.569	3.051	2.217	-2.495	-4.342	-0.013

Interaction energy analysis for fragmet #1(A:7:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.053 / q_NPA : 0.022

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

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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	9	GLY	0	0.070	0.044	3.866	-1.153	-0.074	-0.007	-0.468	-0.605	0.003
4	A	10	GLN	0	0.036	0.028	2.646	-3.934	-1.081	2.195	-1.801	-3.248	-0.016
5	A	11	LYS	1	0.908	0.927	4.863	1.695	1.789	-0.001	-0.009	-0.084	0.000
6	A	12	LEU	0	0.036	0.036	6.810	0.198	0.198	0.000	0.000	0.000	0.000
7	A	13	PHE	0	0.068	0.039	8.252	0.062	0.062	0.000	0.000	0.000	0.000
8	A	14	VAL	0	-0.004	-0.006	7.480	0.068	0.068	0.000	0.000	0.000	0.000
9	A	15	SER	0	-0.045	-0.025	10.120	0.131	0.131	0.000	0.000	0.000	0.000
10	A	16	VAL	0	0.019	0.011	12.536	0.065	0.065	0.000	0.000	0.000	0.000
11	A	17	LEU	0	0.010	0.007	11.704	0.033	0.033	0.000	0.000	0.000	0.000
12	A	18	GLN	0	-0.023	-0.030	12.592	-0.014	-0.014	0.000	0.000	0.000	0.000
13	A	19	ARG	1	0.879	0.947	15.733	0.229	0.229	0.000	0.000	0.000	0.000
14	A	20	LEU	0	-0.005	-0.004	17.598	0.030	0.030	0.000	0.000	0.000	0.000
15	A	21	LEU	0	0.026	0.016	17.269	0.028	0.028	0.000	0.000	0.000	0.000
16	A	22	SER	0	0.011	-0.003	19.222	0.016	0.016	0.000	0.000	0.000	0.000
17	A	23	GLU	-1	-0.852	-0.918	21.689	-0.135	-0.135	0.000	0.000	0.000	0.000
18	A	24	ARG	1	0.793	0.894	22.626	0.162	0.162	0.000	0.000	0.000	0.000
19	A	25	GLY	0	0.011	0.016	25.077	0.007	0.007	0.000	0.000	0.000	0.000
20	A	26	LEU	0	-0.047	-0.009	22.163	-0.009	-0.009	0.000	0.000	0.000	0.000
21	A	27	HIS	0	0.030	0.007	19.609	-0.045	-0.045	0.000	0.000	0.000	0.000
22	A	28	VAL	0	0.000	-0.005	14.454	0.000	0.000	0.000	0.000	0.000	0.000
23	A	29	LYS	1	0.991	0.998	15.013	0.450	0.450	0.000	0.000	0.000	0.000
24	A	30	GLU	-1	-0.778	-0.883	8.795	-1.477	-1.477	0.000	0.000	0.000	0.000
25	A	31	SER	0	0.021	0.006	9.706	-0.134	-0.134	0.000	0.000	0.000	0.000
26	A	32	SER	0	0.002	0.002	10.346	-0.041	-0.041	0.000	0.000	0.000	0.000
27	A	33	ALA	0	0.052	0.032	10.869	0.095	0.095	0.000	0.000	0.000	0.000
28	A	34	ILE	0	-0.023	-0.013	5.292	-0.021	-0.021	0.000	0.000	0.000	0.000
29	A	35	GLU	-1	-0.767	-0.855	7.171	-0.595	-0.595	0.000	0.000	0.000	0.000
30	A	36	PHE	0	-0.001	-0.001	9.677	0.171	0.171	0.000	0.000	0.000	0.000
31	A	37	TYR	0	0.023	0.000	3.401	-0.440	-0.252	0.010	-0.058	-0.140	0.000
32	A	38	GLN	0	-0.024	-0.035	3.168	0.541	0.885	0.021	-0.154	-0.210	0.000
33	A	39	PHE	0	0.008	-0.001	6.587	0.307	0.307	0.000	0.000	0.000	0.000
34	A	40	LEU	0	-0.003	0.003	9.646	0.123	0.123	0.000	0.000	0.000	0.000
35	A	41	ILE	0	0.007	-0.009	4.580	0.101	0.163	-0.001	-0.005	-0.055	0.000
36	A	42	LYS	1	0.872	0.957	8.864	0.151	0.151	0.000	0.000	0.000	0.000
37	A	43	VAL	0	-0.068	-0.031	10.801	0.004	0.004	0.000	0.000	0.000	0.000
38	A	44	SER	0	-0.026	-0.040	12.552	-0.048	-0.048	0.000	0.000	0.000	0.000
39	A	45	PRO	0	-0.020	-0.011	10.657	0.035	0.035	0.000	0.000	0.000	0.000
40	A	46	TRP	0	0.029	-0.002	11.255	0.183	0.183	0.000	0.000	0.000	0.000
41	A	47	PHE	0	-0.033	-0.018	10.766	-0.035	-0.035	0.000	0.000	0.000	0.000
42	A	48	PRO	0	-0.077	-0.057	8.053	-0.077	-0.077	0.000	0.000	0.000	0.000
43	A	49	GLU	-1	-0.984	-0.973	10.555	0.926	0.926	0.000	0.000	0.000	0.000
44	A	50	GLU	-1	-0.835	-0.917	13.751	0.364	0.364	0.000	0.000	0.000	0.000
45	A	51	GLY	0	-0.031	0.005	15.097	-0.068	-0.068	0.000	0.000	0.000	0.000
46	A	52	GLY	0	0.001	0.004	15.614	0.009	0.009	0.000	0.000	0.000	0.000
47	A	53	LEU	0	-0.049	-0.029	15.256	-0.017	-0.017	0.000	0.000	0.000	0.000
48	A	54	ASN	0	0.009	-0.007	17.497	-0.034	-0.034	0.000	0.000	0.000	0.000
49	A	55	LEU	0	0.063	0.024	20.623	0.010	0.010	0.000	0.000	0.000	0.000
50	A	56	GLN	0	0.033	0.023	23.048	-0.013	-0.013	0.000	0.000	0.000	0.000
51	A	57	ASP	-1	-0.736	-0.874	17.887	0.234	0.234	0.000	0.000	0.000	0.000
52	A	58	TRP	0	-0.028	-0.015	14.015	0.006	0.006	0.000	0.000	0.000	0.000
53	A	59	LYS	1	0.889	0.933	19.334	-0.070	-0.070	0.000	0.000	0.000	0.000
54	A	60	ARG	1	0.749	0.880	18.732	-0.352	-0.352	0.000	0.000	0.000	0.000
55	A	61	VAL	0	0.072	0.028	14.936	0.003	0.003	0.000	0.000	0.000	0.000
56	A	62	GLY	0	-0.005	0.002	17.495	-0.014	-0.014	0.000	0.000	0.000	0.000
57	A	63	ARG	1	0.901	0.948	20.223	-0.139	-0.139	0.000	0.000	0.000	0.000
58	A	64	GLU	-1	-0.776	-0.846	17.196	0.298	0.298	0.000	0.000	0.000	0.000
59	A	65	MET	0	-0.026	-0.003	14.067	-0.016	-0.016	0.000	0.000	0.000	0.000
60	A	66	LYS	1	0.928	0.960	18.133	-0.016	-0.016	0.000	0.000	0.000	0.000
61	A	67	ARG	1	0.829	0.895	18.137	-0.220	-0.220	0.000	0.000	0.000	0.000
62	A	68	TYR	0	0.072	0.037	15.667	-0.024	-0.024	0.000	0.000	0.000	0.000
63	A	69	ALA	0	0.005	-0.013	19.520	-0.012	-0.012	0.000	0.000	0.000	0.000
64	A	70	ALA	0	-0.050	-0.018	21.639	-0.008	-0.008	0.000	0.000	0.000	0.000
65	A	71	GLU	-1	-0.857	-0.896	19.989	0.177	0.177	0.000	0.000	0.000	0.000
66	A	72	HIS	0	-0.060	-0.031	18.382	0.016	0.016	0.000	0.000	0.000	0.000
67	A	73	GLY	0	0.051	0.050	21.797	-0.014	-0.014	0.000	0.000	0.000	0.000
68	A	74	THR	0	-0.045	-0.043	21.902	0.005	0.005	0.000	0.000	0.000	0.000
69	A	75	ASP	-1	-0.904	-0.947	21.406	-0.112	-0.112	0.000	0.000	0.000	0.000
70	A	76	SER	0	-0.019	-0.026	16.193	0.012	0.012	0.000	0.000	0.000	0.000
71	A	77	ILE	0	-0.024	0.010	16.220	-0.001	-0.001	0.000	0.000	0.000	0.000
72	A	78	PRO	0	-0.039	-0.016	12.899	-0.016	-0.016	0.000	0.000	0.000	0.000
73	A	79	LYS	1	0.855	0.913	15.349	0.536	0.536	0.000	0.000	0.000	0.000
74	A	80	GLN	0	-0.031	-0.036	13.536	0.091	0.091	0.000	0.000	0.000	0.000
75	A	81	ALA	0	-0.017	-0.010	15.100	0.008	0.008	0.000	0.000	0.000	0.000
76	A	82	TYR	0	0.058	0.024	16.413	0.026	0.026	0.000	0.000	0.000	0.000
77	A	83	PRO	0	0.015	-0.003	19.802	0.014	0.014	0.000	0.000	0.000	0.000
78	A	84	ILE	0	0.017	0.010	14.864	0.006	0.006	0.000	0.000	0.000	0.000
79	A	85	TRP	0	-0.021	-0.008	17.298	0.009	0.009	0.000	0.000	0.000	0.000
80	A	86	LEU	0	0.017	0.013	18.462	0.022	0.022	0.000	0.000	0.000	0.000
81	A	87	GLN	0	0.019	0.001	20.664	0.014	0.014	0.000	0.000	0.000	0.000
82	A	88	LEU	0	0.005	-0.005	15.463	0.006	0.006	0.000	0.000	0.000	0.000
83	A	89	ARG	1	0.767	0.861	19.965	0.061	0.061	0.000	0.000	0.000	0.000
84	A	90	GLU	-1	-0.784	-0.852	22.536	-0.040	-0.040	0.000	0.000	0.000	0.000
85	A	91	ILE	0	-0.045	-0.021	21.048	0.006	0.006	0.000	0.000	0.000	0.000
86	A	92	LEU	0	-0.080	-0.019	19.187	0.012	0.012	0.000	0.000	0.000	0.000
87	A	93	THR	0	-0.041	-0.027	23.713	0.019	0.019	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:7:SER)