FMO DATABASE

FMODB ID: K3L13

Calculation Name: 1U0S-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1U0S

Chain ID: A

ChEMBL ID:

UniProt ID: Q56310

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	86
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-619955.30284
FMO2-HF: Nuclear repulsion	585721.105304
FMO2-HF: Total energy	-34234.197536
FMO2-MP2: Total energy	-34336.285871

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:175:GLY)

Summations of interaction energy for fragment #1(A:175: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.
0.463	1.315	0.011	-0.448	-0.414	0.001

Interaction energy analysis for fragmet #1(A:175:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.002 / q_NPA : -0.015

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	177	LYS	1	0.808	0.893	3.762	0.413	1.265	0.011	-0.448	-0.414	0.001
4	A	178	THR	0	0.025	0.002	6.505	0.379	0.379	0.000	0.000	0.000	0.000
5	A	179	PHE	0	-0.038	-0.021	9.655	-0.078	-0.078	0.000	0.000	0.000	0.000
6	A	180	TYR	0	-0.052	-0.028	13.141	0.046	0.046	0.000	0.000	0.000	0.000
7	A	181	ILE	0	-0.004	-0.016	15.908	-0.040	-0.040	0.000	0.000	0.000	0.000
8	A	182	LYS	1	0.790	0.887	19.122	0.034	0.034	0.000	0.000	0.000	0.000
9	A	183	VAL	0	0.002	-0.005	22.937	-0.015	-0.015	0.000	0.000	0.000	0.000
10	A	184	ILE	0	0.012	0.003	25.295	0.008	0.008	0.000	0.000	0.000	0.000
11	A	185	LEU	0	-0.015	-0.009	28.894	-0.007	-0.007	0.000	0.000	0.000	0.000
12	A	186	LYS	1	0.892	0.932	31.856	0.045	0.045	0.000	0.000	0.000	0.000
13	A	187	GLU	-1	-0.845	-0.919	35.486	-0.012	-0.012	0.000	0.000	0.000	0.000
14	A	188	GLY	0	-0.031	-0.004	38.430	0.002	0.002	0.000	0.000	0.000	0.000
15	A	189	THR	0	-0.065	-0.053	33.165	-0.002	-0.002	0.000	0.000	0.000	0.000
16	A	190	GLN	0	-0.007	-0.009	36.627	0.002	0.002	0.000	0.000	0.000	0.000
17	A	191	LEU	0	-0.022	-0.005	35.863	-0.002	-0.002	0.000	0.000	0.000	0.000
18	A	192	LYS	1	0.964	0.991	32.707	0.000	0.000	0.000	0.000	0.000	0.000
19	A	193	SER	0	0.010	-0.019	31.127	-0.002	-0.002	0.000	0.000	0.000	0.000
20	A	194	ALA	0	-0.017	-0.007	30.031	-0.001	-0.001	0.000	0.000	0.000	0.000
21	A	195	ARG	1	0.795	0.891	29.699	0.028	0.028	0.000	0.000	0.000	0.000
22	A	196	ILE	0	0.030	0.007	25.593	-0.008	-0.008	0.000	0.000	0.000	0.000
23	A	197	TYR	0	-0.003	-0.011	25.526	-0.001	-0.001	0.000	0.000	0.000	0.000
24	A	198	LEU	0	-0.009	-0.008	25.085	-0.003	-0.003	0.000	0.000	0.000	0.000
25	A	199	VAL	0	0.004	-0.002	21.139	-0.012	-0.012	0.000	0.000	0.000	0.000
26	A	200	PHE	0	0.027	0.009	20.926	-0.008	-0.008	0.000	0.000	0.000	0.000
27	A	201	HIS	0	0.035	0.039	20.423	0.008	0.008	0.000	0.000	0.000	0.000
28	A	202	LYS	1	0.803	0.891	20.009	0.112	0.112	0.000	0.000	0.000	0.000
29	A	203	LEU	0	-0.006	-0.017	15.784	-0.030	-0.030	0.000	0.000	0.000	0.000
30	A	204	GLU	-1	-0.885	-0.932	15.908	0.035	0.035	0.000	0.000	0.000	0.000
31	A	205	GLU	-1	-0.869	-0.914	16.851	-0.128	-0.128	0.000	0.000	0.000	0.000
32	A	206	LEU	0	-0.064	-0.045	14.026	-0.035	-0.035	0.000	0.000	0.000	0.000
33	A	207	LYS	1	0.812	0.909	12.219	0.144	0.144	0.000	0.000	0.000	0.000
34	A	208	CYS	0	-0.069	-0.023	11.503	-0.017	-0.017	0.000	0.000	0.000	0.000
35	A	209	GLU	-1	-0.885	-0.937	12.169	0.557	0.557	0.000	0.000	0.000	0.000
36	A	210	VAL	0	0.009	-0.008	13.777	-0.007	-0.007	0.000	0.000	0.000	0.000
37	A	211	VAL	0	0.002	0.016	12.907	0.008	0.008	0.000	0.000	0.000	0.000
38	A	212	ARG	1	0.867	0.916	16.227	-0.187	-0.187	0.000	0.000	0.000	0.000
39	A	213	THR	0	-0.019	-0.023	19.382	-0.010	-0.010	0.000	0.000	0.000	0.000
40	A	214	ILE	0	-0.034	0.012	22.234	0.010	0.010	0.000	0.000	0.000	0.000
41	A	215	PRO	0	0.052	0.032	25.318	-0.010	-0.010	0.000	0.000	0.000	0.000
42	A	216	SER	0	-0.007	-0.042	26.125	0.004	0.004	0.000	0.000	0.000	0.000
43	A	217	VAL	0	0.037	0.001	24.158	-0.006	-0.006	0.000	0.000	0.000	0.000
44	A	218	GLU	-1	-0.840	-0.912	27.048	0.043	0.043	0.000	0.000	0.000	0.000
45	A	219	GLU	-1	-0.831	-0.895	30.215	0.039	0.039	0.000	0.000	0.000	0.000
46	A	220	ILE	0	-0.036	-0.019	25.590	-0.007	-0.007	0.000	0.000	0.000	0.000
47	A	221	GLU	-1	-0.963	-0.996	27.894	0.035	0.035	0.000	0.000	0.000	0.000
48	A	222	GLU	-1	-0.899	-0.953	31.454	0.030	0.030	0.000	0.000	0.000	0.000
49	A	223	GLU	-1	-0.852	-0.903	33.556	-0.002	-0.002	0.000	0.000	0.000	0.000
50	A	224	LYS	1	0.792	0.926	33.844	-0.037	-0.037	0.000	0.000	0.000	0.000
51	A	225	PHE	0	-0.073	-0.049	30.915	0.002	0.002	0.000	0.000	0.000	0.000
52	A	226	GLU	-1	-0.869	-0.929	33.529	0.000	0.000	0.000	0.000	0.000	0.000
53	A	227	ASN	0	-0.071	-0.032	33.288	0.000	0.000	0.000	0.000	0.000	0.000
54	A	228	GLU	-1	-0.853	-0.935	28.211	-0.019	-0.019	0.000	0.000	0.000	0.000
55	A	229	VAL	0	0.022	0.030	24.533	0.006	0.006	0.000	0.000	0.000	0.000
56	A	230	GLU	-1	-0.857	-0.904	22.459	-0.011	-0.011	0.000	0.000	0.000	0.000
57	A	231	LEU	0	-0.005	-0.006	18.891	0.013	0.013	0.000	0.000	0.000	0.000
58	A	232	PHE	0	-0.050	-0.025	12.384	-0.019	-0.019	0.000	0.000	0.000	0.000
59	A	233	VAL	0	0.017	0.007	12.994	0.034	0.034	0.000	0.000	0.000	0.000
60	A	234	ILE	0	0.023	0.017	7.760	-0.047	-0.047	0.000	0.000	0.000	0.000
61	A	235	SER	0	-0.004	-0.026	8.658	0.037	0.037	0.000	0.000	0.000	0.000
62	A	236	PRO	0	0.007	0.013	6.727	-0.400	-0.400	0.000	0.000	0.000	0.000
63	A	237	VAL	0	-0.025	-0.003	7.788	-0.233	-0.233	0.000	0.000	0.000	0.000
64	A	238	ASH	0	-0.020	-0.055	9.724	0.013	0.013	0.000	0.000	0.000	0.000
65	A	239	LEU	0	0.062	0.035	10.818	0.098	0.098	0.000	0.000	0.000	0.000
66	A	240	GLU	-1	-0.759	-0.827	14.028	-0.380	-0.380	0.000	0.000	0.000	0.000
67	A	241	LYS	1	0.861	0.914	14.018	0.449	0.449	0.000	0.000	0.000	0.000
68	A	242	LEU	0	0.041	0.036	13.263	0.048	0.048	0.000	0.000	0.000	0.000
69	A	243	SER	0	-0.003	-0.027	15.803	0.055	0.055	0.000	0.000	0.000	0.000
70	A	244	GLH	0	-0.028	-0.013	18.965	0.032	0.032	0.000	0.000	0.000	0.000
71	A	245	ALA	0	0.015	0.026	18.294	0.024	0.024	0.000	0.000	0.000	0.000
72	A	246	LEU	0	0.035	0.014	18.751	0.025	0.025	0.000	0.000	0.000	0.000
73	A	247	SER	0	-0.080	-0.048	21.609	0.017	0.017	0.000	0.000	0.000	0.000
74	A	248	SER	0	-0.071	-0.045	23.524	0.012	0.012	0.000	0.000	0.000	0.000
75	A	249	ILE	0	-0.028	0.001	23.104	0.009	0.009	0.000	0.000	0.000	0.000
76	A	250	ALA	0	0.004	-0.005	27.053	0.002	0.002	0.000	0.000	0.000	0.000
77	A	251	ASP	-1	-0.853	-0.936	30.748	-0.029	-0.029	0.000	0.000	0.000	0.000
78	A	252	ILE	0	0.063	0.041	26.325	0.005	0.005	0.000	0.000	0.000	0.000
79	A	253	GLU	-1	-0.917	-0.936	30.158	-0.041	-0.041	0.000	0.000	0.000	0.000
80	A	254	ARG	1	0.904	0.943	26.553	0.060	0.060	0.000	0.000	0.000	0.000
81	A	255	VAL	0	0.052	0.038	21.498	0.005	0.005	0.000	0.000	0.000	0.000
82	A	256	ILE	0	-0.075	-0.033	21.878	-0.010	-0.010	0.000	0.000	0.000	0.000
83	A	257	ILE	0	0.030	0.018	16.047	0.007	0.007	0.000	0.000	0.000	0.000
84	A	258	LYS	1	0.920	0.958	16.714	0.066	0.066	0.000	0.000	0.000	0.000
85	A	259	GLU	-1	-0.758	-0.856	9.065	-0.726	-0.726	0.000	0.000	0.000	0.000
86	A	260	VAL	0	-0.030	-0.002	10.436	0.044	0.044	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:175:GLY)