FMO DATABASE

FMODB ID: 1N6KZ

Calculation Name: 1UFB-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1UFB

Chain ID: A

ChEMBL ID:

UniProt ID: P83963

Base Structure: X-ray

Registration Date: 2023-09-22

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	127
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1081126.913321
FMO2-HF: Nuclear repulsion	1032232.823248
FMO2-HF: Total energy	-48894.090073
FMO2-MP2: Total energy	-49039.305223

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:1:MET)

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

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.
-34.861	-37.398	24.332	-9.095	-12.701	0.056

Interaction energy analysis for fragmet #1(A:1:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.063 / q_NPA : 0.045

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	3	ARG	1	0.925	0.946	3.907	-3.241	-1.788	-0.005	-0.622	-0.826	0.002
4	A	4	ALA	0	0.027	0.032	2.508	-0.498	0.647	0.438	-0.493	-1.090	-0.001
5	A	5	ARG	1	0.891	0.919	2.302	-22.094	-29.355	22.070	-7.167	-7.642	0.064
6	A	6	ASP	-1	-0.737	-0.862	4.699	2.055	2.140	-0.001	-0.013	-0.070	0.000
7	A	7	TRP	0	-0.018	-0.001	7.087	-0.142	-0.142	0.000	0.000	0.000	0.000
8	A	8	LEU	0	0.077	0.039	6.039	0.027	0.027	0.000	0.000	0.000	0.000
9	A	9	GLU	-1	-1.004	-0.987	8.384	1.988	1.988	0.000	0.000	0.000	0.000
10	A	10	GLN	0	-0.057	-0.029	10.827	0.028	0.028	0.000	0.000	0.000	0.000
11	A	11	ALA	0	-0.006	0.003	11.366	-0.005	-0.005	0.000	0.000	0.000	0.000
12	A	12	ARG	1	0.875	0.909	7.782	-0.158	-0.158	0.000	0.000	0.000	0.000
13	A	13	HIS	0	-0.002	0.014	13.933	0.063	0.063	0.000	0.000	0.000	0.000
14	A	14	ASN	0	-0.020	-0.010	16.215	0.080	0.080	0.000	0.000	0.000	0.000
15	A	15	LEU	0	0.054	0.028	16.262	0.009	0.009	0.000	0.000	0.000	0.000
16	A	16	ARG	1	0.915	0.951	15.271	-0.255	-0.255	0.000	0.000	0.000	0.000
17	A	17	HIS	0	0.002	0.007	20.067	0.027	0.027	0.000	0.000	0.000	0.000
18	A	18	ALA	0	0.013	0.015	21.519	0.003	0.003	0.000	0.000	0.000	0.000
19	A	19	GLN	0	-0.001	-0.002	21.105	0.026	0.026	0.000	0.000	0.000	0.000
20	A	20	GLY	0	-0.001	0.000	24.154	0.010	0.010	0.000	0.000	0.000	0.000
21	A	21	SER	0	-0.048	-0.035	25.901	0.003	0.003	0.000	0.000	0.000	0.000
22	A	22	LEU	0	-0.052	-0.025	27.067	-0.001	-0.001	0.000	0.000	0.000	0.000
23	A	23	GLY	0	-0.039	-0.017	28.544	0.002	0.002	0.000	0.000	0.000	0.000
24	A	24	LEU	0	-0.042	-0.019	29.592	0.007	0.007	0.000	0.000	0.000	0.000
25	A	25	GLY	0	0.014	0.018	31.807	0.002	0.002	0.000	0.000	0.000	0.000
26	A	26	ASP	-1	-0.912	-0.941	30.411	-0.041	-0.041	0.000	0.000	0.000	0.000
27	A	27	TYR	0	0.005	-0.023	29.808	-0.013	-0.013	0.000	0.000	0.000	0.000
28	A	28	ALA	0	0.014	0.016	29.113	-0.018	-0.018	0.000	0.000	0.000	0.000
29	A	29	TRP	0	0.009	-0.012	26.600	-0.024	-0.024	0.000	0.000	0.000	0.000
30	A	30	ALA	0	0.008	0.013	25.462	-0.011	-0.011	0.000	0.000	0.000	0.000
31	A	31	CYS	0	-0.002	0.009	24.232	-0.022	-0.022	0.000	0.000	0.000	0.000
32	A	32	PHE	0	-0.044	-0.007	23.474	-0.034	-0.034	0.000	0.000	0.000	0.000
33	A	33	ALA	0	-0.025	-0.011	21.470	-0.033	-0.033	0.000	0.000	0.000	0.000
34	A	34	ALA	0	0.040	0.018	19.757	-0.028	-0.028	0.000	0.000	0.000	0.000
35	A	35	GLN	0	0.035	0.027	19.075	-0.021	-0.021	0.000	0.000	0.000	0.000
36	A	36	GLN	0	-0.075	-0.066	18.339	-0.047	-0.047	0.000	0.000	0.000	0.000
37	A	37	ALA	0	-0.023	-0.004	15.578	-0.044	-0.044	0.000	0.000	0.000	0.000
38	A	38	ALA	0	0.054	0.022	14.132	-0.116	-0.116	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.743	-0.837	13.995	-0.654	-0.654	0.000	0.000	0.000	0.000
40	A	40	ALA	0	-0.029	-0.018	12.683	-0.146	-0.146	0.000	0.000	0.000	0.000
41	A	41	ALA	0	0.037	0.015	9.752	-0.217	-0.217	0.000	0.000	0.000	0.000
42	A	42	LEU	0	0.049	0.027	8.969	-0.502	-0.502	0.000	0.000	0.000	0.000
43	A	43	LYS	1	0.760	0.880	10.182	0.436	0.436	0.000	0.000	0.000	0.000
44	A	44	GLY	0	0.023	0.003	6.763	-0.241	-0.241	0.000	0.000	0.000	0.000
45	A	45	LEU	0	0.000	0.000	5.544	-1.526	-1.526	0.000	0.000	0.000	0.000
46	A	46	HIS	1	0.802	0.869	6.828	1.197	1.197	0.000	0.000	0.000	0.000
47	A	47	LEU	0	0.019	0.025	5.604	-0.102	-0.102	0.000	0.000	0.000	0.000
48	A	48	ALA	0	-0.051	-0.025	2.477	-2.247	-1.335	1.282	-0.738	-1.457	-0.004
49	A	49	ARG	1	0.770	0.877	3.512	2.718	2.837	0.002	0.287	-0.408	-0.001
50	A	50	GLY	0	-0.018	0.002	5.635	0.843	0.843	0.000	0.000	0.000	0.000
51	A	51	GLN	0	0.000	0.004	7.285	0.437	0.437	0.000	0.000	0.000	0.000
52	A	52	VAL	0	-0.008	-0.001	9.339	-0.191	-0.191	0.000	0.000	0.000	0.000
53	A	53	ALA	0	0.027	0.011	11.460	0.061	0.061	0.000	0.000	0.000	0.000
54	A	54	TRP	0	0.011	-0.005	13.767	0.095	0.095	0.000	0.000	0.000	0.000
55	A	55	GLY	0	0.027	0.016	16.944	-0.018	-0.018	0.000	0.000	0.000	0.000
56	A	56	HIS	1	0.811	0.865	18.716	0.382	0.382	0.000	0.000	0.000	0.000
57	A	57	SER	0	-0.014	-0.007	20.501	0.013	0.013	0.000	0.000	0.000	0.000
58	A	58	ILE	0	0.012	-0.016	17.238	-0.069	-0.069	0.000	0.000	0.000	0.000
59	A	59	LEU	0	0.016	0.008	18.122	-0.073	-0.073	0.000	0.000	0.000	0.000
60	A	60	ASP	-1	-0.859	-0.895	19.752	-0.616	-0.616	0.000	0.000	0.000	0.000
61	A	61	LEU	0	-0.072	-0.029	14.108	-0.092	-0.092	0.000	0.000	0.000	0.000
62	A	62	LEU	0	0.018	0.016	14.635	-0.202	-0.202	0.000	0.000	0.000	0.000
63	A	63	ALA	0	0.004	0.004	16.539	-0.065	-0.065	0.000	0.000	0.000	0.000
64	A	64	ASP	-1	-0.922	-0.952	15.596	-0.935	-0.935	0.000	0.000	0.000	0.000
65	A	65	LEU	0	-0.103	-0.050	11.195	-0.221	-0.221	0.000	0.000	0.000	0.000
66	A	66	PRO	0	-0.016	-0.012	10.602	0.128	0.128	0.000	0.000	0.000	0.000
67	A	67	GLU	-1	-0.916	-0.955	13.907	-0.806	-0.806	0.000	0.000	0.000	0.000
68	A	68	ASP	-1	-0.861	-0.902	11.454	-2.024	-2.024	0.000	0.000	0.000	0.000
69	A	69	VAL	0	-0.072	-0.036	10.914	-0.045	-0.045	0.000	0.000	0.000	0.000
70	A	70	ASP	-1	-0.843	-0.919	13.587	-0.795	-0.795	0.000	0.000	0.000	0.000
71	A	71	VAL	0	0.018	-0.008	15.299	-0.124	-0.124	0.000	0.000	0.000	0.000
72	A	72	PRO	0	0.018	0.020	17.575	0.088	0.088	0.000	0.000	0.000	0.000
73	A	73	GLU	-1	-0.790	-0.910	20.498	-0.514	-0.514	0.000	0.000	0.000	0.000
74	A	74	ASP	-1	-0.853	-0.926	21.699	-0.497	-0.497	0.000	0.000	0.000	0.000
75	A	75	LEU	0	0.002	0.008	16.182	0.022	0.022	0.000	0.000	0.000	0.000
76	A	76	VAL	0	0.034	0.023	20.099	-0.008	-0.008	0.000	0.000	0.000	0.000
77	A	77	GLU	-1	-0.902	-0.951	22.034	-0.341	-0.341	0.000	0.000	0.000	0.000
78	A	78	ALA	0	-0.005	-0.006	20.424	0.028	0.028	0.000	0.000	0.000	0.000
79	A	79	ALA	0	-0.002	0.001	20.121	0.024	0.024	0.000	0.000	0.000	0.000
80	A	80	LYS	1	0.833	0.914	21.759	0.472	0.472	0.000	0.000	0.000	0.000
81	A	81	VAL	0	-0.023	0.009	25.107	0.038	0.038	0.000	0.000	0.000	0.000
82	A	82	LEU	0	0.019	0.000	19.796	0.028	0.028	0.000	0.000	0.000	0.000
83	A	83	ASP	-1	-0.767	-0.881	21.870	-0.495	-0.495	0.000	0.000	0.000	0.000
84	A	84	LYS	1	0.799	0.894	24.253	0.338	0.338	0.000	0.000	0.000	0.000
85	A	85	TYR	0	0.011	-0.007	25.021	0.030	0.030	0.000	0.000	0.000	0.000
86	A	86	TYR	0	0.028	0.029	22.529	0.022	0.022	0.000	0.000	0.000	0.000
87	A	87	ILE	0	0.011	-0.005	25.098	0.024	0.024	0.000	0.000	0.000	0.000
88	A	88	PRO	0	0.050	0.012	28.731	0.023	0.023	0.000	0.000	0.000	0.000
89	A	89	THR	0	0.015	0.025	27.454	0.020	0.020	0.000	0.000	0.000	0.000
90	A	90	ARG	1	0.833	0.907	26.482	0.182	0.182	0.000	0.000	0.000	0.000
91	A	91	TYR	0	0.001	0.019	29.147	0.010	0.010	0.000	0.000	0.000	0.000
92	A	92	PRO	0	-0.041	-0.035	34.160	-0.006	-0.006	0.000	0.000	0.000	0.000
93	A	93	ASP	-1	-0.877	-0.935	36.416	-0.128	-0.128	0.000	0.000	0.000	0.000
94	A	94	ALA	0	-0.027	0.005	34.081	-0.005	-0.005	0.000	0.000	0.000	0.000
95	A	95	HIS	1	0.811	0.892	34.174	0.134	0.134	0.000	0.000	0.000	0.000
96	A	96	PRO	0	0.024	0.017	38.825	0.006	0.006	0.000	0.000	0.000	0.000
97	A	97	ALA	0	0.046	0.021	42.078	0.007	0.007	0.000	0.000	0.000	0.000
98	A	98	GLY	0	-0.001	0.013	41.975	-0.003	-0.003	0.000	0.000	0.000	0.000
99	A	99	PRO	0	0.040	0.014	38.426	-0.007	-0.007	0.000	0.000	0.000	0.000
100	A	100	ALA	0	0.049	0.015	33.926	0.000	0.000	0.000	0.000	0.000	0.000
101	A	101	ALA	0	0.059	0.011	33.930	-0.006	-0.006	0.000	0.000	0.000	0.000
102	A	102	ARG	1	0.845	0.917	34.971	0.083	0.083	0.000	0.000	0.000	0.000
103	A	103	HIS	0	-0.101	-0.042	35.877	-0.001	-0.001	0.000	0.000	0.000	0.000
104	A	104	TYR	0	0.019	0.024	31.805	-0.007	-0.007	0.000	0.000	0.000	0.000
105	A	105	THR	0	-0.049	-0.049	33.400	0.015	0.015	0.000	0.000	0.000	0.000
106	A	106	ARG	1	0.866	0.912	31.950	0.076	0.076	0.000	0.000	0.000	0.000
107	A	107	LEU	0	0.018	0.006	30.733	-0.005	-0.005	0.000	0.000	0.000	0.000
108	A	108	GLU	-1	-0.740	-0.849	30.096	-0.171	-0.171	0.000	0.000	0.000	0.000
109	A	109	ALA	0	0.006	-0.005	27.421	-0.020	-0.020	0.000	0.000	0.000	0.000
110	A	110	GLU	-1	-0.820	-0.907	25.992	-0.112	-0.112	0.000	0.000	0.000	0.000
111	A	111	GLU	-1	-0.890	-0.938	25.525	-0.265	-0.265	0.000	0.000	0.000	0.000
112	A	112	ALA	0	-0.014	-0.014	24.180	-0.034	-0.034	0.000	0.000	0.000	0.000
113	A	113	LEU	0	-0.023	-0.025	21.509	-0.036	-0.036	0.000	0.000	0.000	0.000
114	A	114	ASP	-1	-0.870	-0.927	20.617	-0.267	-0.267	0.000	0.000	0.000	0.000
115	A	115	LEU	0	-0.061	-0.038	20.456	-0.060	-0.060	0.000	0.000	0.000	0.000
116	A	116	ALA	0	-0.005	-0.004	18.154	-0.073	-0.073	0.000	0.000	0.000	0.000
117	A	117	GLN	0	-0.032	-0.024	14.838	-0.020	-0.020	0.000	0.000	0.000	0.000
118	A	118	LYS	1	0.851	0.920	15.926	0.373	0.373	0.000	0.000	0.000	0.000
119	A	119	ILE	0	-0.005	0.012	13.764	-0.096	-0.096	0.000	0.000	0.000	0.000
120	A	120	LEU	0	-0.024	-0.024	11.293	-0.187	-0.187	0.000	0.000	0.000	0.000
121	A	121	ALA	0	0.021	0.016	10.954	-0.180	-0.180	0.000	0.000	0.000	0.000
122	A	122	PHE	0	0.026	0.018	11.550	-0.159	-0.159	0.000	0.000	0.000	0.000
123	A	123	VAL	0	-0.014	-0.010	7.518	-0.267	-0.267	0.000	0.000	0.000	0.000
124	A	124	GLU	-1	-0.912	-0.967	6.844	-1.157	-1.157	0.000	0.000	0.000	0.000
125	A	125	GLU	-1	-0.900	-0.927	7.228	-1.244	-1.244	0.000	0.000	0.000	0.000
126	A	126	LYS	1	0.761	0.880	8.400	1.028	1.028	0.000	0.000	0.000	0.000
127	A	127	LEU	0	-0.128	-0.059	2.505	-3.444	-2.434	0.546	-0.349	-1.208	-0.004

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