FMO DATABASE

FMODB ID: XQ86Y

Calculation Name: 1R29-A-Xray13

Preferred Name: B-cell lymphoma 6 protein

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 1R29

Chain ID: A

ChEMBL ID: CHEMBL4105786

UniProt ID: P41182

Base Structure: X-ray

Registration Date: 2018-03-01

Reference:

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	Missing residues were capped by ACE, NME. Missing atoms were corrected by Structure prepareation by MOE.
Water	No
Procedure	Auto-FMO protocol ver. 1.20181228

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	124
LigandCharge
Software	MIZUHO/ABINIT-MP 3.0

Total energy (hartree)

FMO2-HF: Electronic energy	-1033973.952942
FMO2-HF: Nuclear repulsion	983473.680985
FMO2-HF: Total energy	-50500.271957
FMO2-MP2: Total energy	-50643.920438

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:6:ACE)

Summations of interaction energy for fragment #1(A:6:ACE)

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.
1.233	2.132	-0.014	-0.405	-0.481	0

Interaction energy analysis for fragmet #1(A:6:ACE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.018 / q_NPA : -0.002

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].
3	A	8	GLN	0	-0.010	0.012	3.814	0.970	1.869	-0.014	-0.405	-0.481
4	A	9	ILE	0	0.032	0.014	7.137	0.002	0.002	0.000	0.000	0.000
5	A	10	GLN	0	0.000	0.000	9.160	-0.038	-0.038	0.000	0.000	0.000
6	A	11	PHE	0	0.021	0.009	11.667	0.077	0.077	0.000	0.000	0.000
7	A	12	THR	0	-0.004	-0.014	15.094	0.002	0.002	0.000	0.000	0.000
8	A	13	ARG	1	1.008	1.001	17.077	0.097	0.097	0.000	0.000	0.000
9	A	14	HIS	0	0.049	0.038	18.416	0.018	0.018	0.000	0.000	0.000
10	A	15	ALA	0	0.040	0.016	19.995	0.011	0.011	0.000	0.000	0.000
11	A	16	SER	0	0.030	0.010	21.753	0.009	0.009	0.000	0.000	0.000
12	A	17	ASP	-1	-0.919	-0.954	23.367	-0.088	-0.088	0.000	0.000	0.000
13	A	18	VAL	0	-0.057	-0.033	22.839	0.010	0.010	0.000	0.000	0.000
14	A	19	LEU	0	0.008	0.013	25.587	0.008	0.008	0.000	0.000	0.000
15	A	20	LEU	0	0.031	0.017	27.942	0.009	0.009	0.000	0.000	0.000
16	A	21	ASN	0	-0.012	-0.012	27.396	0.015	0.015	0.000	0.000	0.000
17	A	22	LEU	0	0.038	0.023	27.940	0.006	0.006	0.000	0.000	0.000
18	A	23	ASN	0	0.051	0.018	31.470	0.007	0.007	0.000	0.000	0.000
19	A	24	ARG	1	0.866	0.930	30.953	0.067	0.067	0.000	0.000	0.000
20	A	25	LEU	0	-0.014	0.000	32.113	0.005	0.005	0.000	0.000	0.000
21	A	26	ARG	1	0.918	0.980	35.766	0.064	0.064	0.000	0.000	0.000
22	A	27	SER	0	-0.101	-0.054	37.774	0.004	0.004	0.000	0.000	0.000
23	A	28	ARG	1	0.919	0.949	37.814	0.047	0.047	0.000	0.000	0.000
24	A	29	ASP	-1	-0.778	-0.844	40.596	-0.045	-0.045	0.000	0.000	0.000
25	A	30	ILE	0	-0.039	-0.011	36.519	0.001	0.001	0.000	0.000	0.000
26	A	31	LEU	0	0.001	-0.017	34.424	-0.004	-0.004	0.000	0.000	0.000
27	A	32	THR	0	-0.061	-0.039	37.401	-0.003	-0.003	0.000	0.000	0.000
28	A	33	ASP	-1	-0.819	-0.911	37.117	-0.067	-0.067	0.000	0.000	0.000
29	A	34	VAL	0	-0.058	-0.037	39.623	0.001	0.001	0.000	0.000	0.000
30	A	35	VAL	0	-0.026	0.000	42.059	0.000	0.000	0.000	0.000	0.000
31	A	36	ILE	0	-0.007	-0.010	41.173	0.000	0.000	0.000	0.000	0.000
32	A	37	VAL	0	0.015	0.001	44.833	0.001	0.001	0.000	0.000	0.000
33	A	38	VAL	0	0.020	0.005	45.875	-0.001	-0.001	0.000	0.000	0.000
34	A	39	SER	0	0.065	0.036	49.112	0.002	0.002	0.000	0.000	0.000
35	A	40	ARG	1	0.898	0.940	52.851	0.030	0.030	0.000	0.000	0.000
36	A	41	GLU	-1	-0.933	-0.955	49.392	-0.036	-0.036	0.000	0.000	0.000
37	A	42	GLN	0	-0.013	-0.017	48.138	-0.002	-0.002	0.000	0.000	0.000
38	A	43	PHE	0	0.021	0.015	43.014	0.000	0.000	0.000	0.000	0.000
39	A	44	ARG	1	0.862	0.930	42.439	0.046	0.046	0.000	0.000	0.000
40	A	45	ALA	0	0.003	-0.007	37.729	-0.001	-0.001	0.000	0.000	0.000
41	A	46	HIS	0	0.017	0.023	34.198	-0.001	-0.001	0.000	0.000	0.000
42	A	47	LYS	1	0.860	0.934	35.151	0.059	0.059	0.000	0.000	0.000
43	A	48	THR	0	0.001	-0.004	30.271	-0.002	-0.002	0.000	0.000	0.000
44	A	49	VAL	0	0.016	0.014	30.586	-0.007	-0.007	0.000	0.000	0.000
45	A	50	LEU	0	0.017	0.002	31.947	-0.002	-0.002	0.000	0.000	0.000
46	A	51	MET	0	-0.080	-0.037	32.021	-0.001	-0.001	0.000	0.000	0.000
47	A	52	ALA	0	-0.033	-0.008	27.936	-0.004	-0.004	0.000	0.000	0.000
48	A	53	CYS	0	-0.052	-0.007	29.069	-0.007	-0.007	0.000	0.000	0.000
49	A	54	SER	0	-0.035	-0.026	31.656	0.004	0.004	0.000	0.000	0.000
50	A	55	GLY	0	0.066	0.025	34.513	-0.002	-0.002	0.000	0.000	0.000
51	A	56	LEU	0	-0.015	0.003	35.369	0.001	0.001	0.000	0.000	0.000
52	A	57	PHE	0	0.033	-0.009	36.377	0.002	0.002	0.000	0.000	0.000
53	A	58	TYR	0	0.000	0.005	29.749	0.001	0.001	0.000	0.000	0.000
54	A	59	SER	0	-0.001	-0.015	34.809	0.000	0.000	0.000	0.000	0.000
55	A	60	ILE	0	-0.066	-0.022	37.438	0.003	0.003	0.000	0.000	0.000
56	A	61	PHE	0	0.027	0.000	36.173	0.002	0.002	0.000	0.000	0.000
57	A	62	THR	0	-0.005	0.004	33.716	-0.001	-0.001	0.000	0.000	0.000
58	A	63	ASP	-1	-0.827	-0.893	35.578	-0.061	-0.061	0.000	0.000	0.000
59	A	64	GLN	0	0.012	-0.011	38.736	-0.002	-0.002	0.000	0.000	0.000
60	A	65	LEU	0	-0.057	-0.019	40.051	0.003	0.003	0.000	0.000	0.000
61	A	66	LYS	1	0.963	0.970	41.700	0.057	0.057	0.000	0.000	0.000
62	A	67	ARG	1	0.860	0.946	34.766	0.081	0.081	0.000	0.000	0.000
63	A	68	ASN	0	-0.005	-0.013	39.665	-0.003	-0.003	0.000	0.000	0.000
64	A	69	LEU	0	-0.009	0.011	42.027	0.003	0.003	0.000	0.000	0.000
65	A	70	SER	0	0.034	0.003	42.603	-0.003	-0.003	0.000	0.000	0.000
66	A	71	VAL	0	-0.013	-0.004	44.617	0.000	0.000	0.000	0.000	0.000
67	A	72	ILE	0	-0.027	-0.007	42.430	0.000	0.000	0.000	0.000	0.000
68	A	73	ASN	0	-0.016	-0.007	45.845	0.001	0.001	0.000	0.000	0.000
69	A	74	LEU	0	-0.032	-0.012	43.675	-0.001	-0.001	0.000	0.000	0.000
70	A	75	ASP	-1	-0.861	-0.934	47.577	-0.039	-0.039	0.000	0.000	0.000
71	A	76	PRO	0	-0.029	-0.019	49.845	0.000	0.000	0.000	0.000	0.000
72	A	77	GLU	-1	-0.925	-0.961	51.509	-0.033	-0.033	0.000	0.000	0.000
73	A	78	ILE	0	-0.089	-0.028	45.905	-0.001	-0.001	0.000	0.000	0.000
74	A	79	ASN	0	0.039	0.019	47.441	0.000	0.000	0.000	0.000	0.000
75	A	80	PRO	0	0.043	0.001	47.479	-0.002	-0.002	0.000	0.000	0.000
76	A	81	GLU	-1	-0.936	-0.959	46.353	-0.039	-0.039	0.000	0.000	0.000
77	A	82	GLY	0	0.011	-0.004	44.696	-0.002	-0.002	0.000	0.000	0.000
78	A	83	PHE	0	0.032	0.010	41.021	-0.004	-0.004	0.000	0.000	0.000
79	A	84	ASN	0	0.005	-0.005	41.640	-0.005	-0.005	0.000	0.000	0.000
80	A	85	ILE	0	-0.011	0.006	40.224	-0.002	-0.002	0.000	0.000	0.000
81	A	86	LEU	0	-0.020	-0.013	37.865	-0.004	-0.004	0.000	0.000	0.000
82	A	87	LEU	0	0.001	0.007	36.884	-0.005	-0.005	0.000	0.000	0.000
83	A	88	ASP	-1	-0.828	-0.928	36.463	-0.059	-0.059	0.000	0.000	0.000
84	A	89	PHE	0	-0.042	-0.005	31.069	-0.004	-0.004	0.000	0.000	0.000
85	A	90	MET	0	-0.055	-0.028	32.622	-0.006	-0.006	0.000	0.000	0.000
86	A	91	TYR	0	-0.017	-0.035	31.385	-0.006	-0.006	0.000	0.000	0.000
87	A	92	THR	0	-0.048	-0.051	31.591	0.000	0.000	0.000	0.000	0.000
88	A	93	SER	0	-0.064	-0.026	28.325	-0.005	-0.005	0.000	0.000	0.000
89	A	94	ARG	1	0.905	0.955	30.593	0.064	0.064	0.000	0.000	0.000
90	A	95	LEU	0	0.051	0.029	33.721	0.001	0.001	0.000	0.000	0.000
91	A	96	ASN	0	-0.024	-0.010	36.521	0.002	0.002	0.000	0.000	0.000
92	A	97	LEU	0	0.014	0.009	39.031	0.001	0.001	0.000	0.000	0.000
93	A	98	ARG	1	0.951	0.966	41.386	0.039	0.039	0.000	0.000	0.000
94	A	99	GLU	-1	-0.827	-0.928	44.753	-0.034	-0.034	0.000	0.000	0.000
95	A	100	GLY	0	0.002	0.011	47.719	0.000	0.000	0.000	0.000	0.000
96	A	101	ASN	0	-0.005	-0.007	43.829	-0.001	-0.001	0.000	0.000	0.000
97	A	102	ILE	0	0.005	0.014	43.198	-0.002	-0.002	0.000	0.000	0.000
98	A	103	MET	0	0.019	0.002	44.786	-0.002	-0.002	0.000	0.000	0.000
99	A	104	ALA	0	0.048	0.031	46.648	-0.001	-0.001	0.000	0.000	0.000
100	A	105	VAL	0	0.018	0.016	40.863	-0.002	-0.002	0.000	0.000	0.000
101	A	106	MET	0	0.008	-0.004	41.832	-0.003	-0.003	0.000	0.000	0.000
102	A	107	ALA	0	0.017	0.005	42.674	-0.002	-0.002	0.000	0.000	0.000
103	A	108	THR	0	0.007	-0.008	42.590	-0.001	-0.001	0.000	0.000	0.000
104	A	109	ALA	0	0.004	-0.008	38.569	-0.002	-0.002	0.000	0.000	0.000
105	A	110	MET	0	-0.052	-0.027	39.446	-0.003	-0.003	0.000	0.000	0.000
106	A	111	TYR	0	0.039	0.039	41.221	-0.002	-0.002	0.000	0.000	0.000
107	A	112	LEU	0	-0.013	-0.016	38.670	-0.001	-0.001	0.000	0.000	0.000
108	A	113	GLN	0	-0.005	0.010	37.056	-0.008	-0.008	0.000	0.000	0.000
109	A	114	MET	0	-0.016	0.006	34.522	-0.004	-0.004	0.000	0.000	0.000
110	A	115	GLU	-1	-0.832	-0.923	33.384	-0.072	-0.072	0.000	0.000	0.000
111	A	116	HIS	0	0.015	0.008	27.031	0.003	0.003	0.000	0.000	0.000
112	A	117	VAL	0	0.011	0.008	32.720	0.003	0.003	0.000	0.000	0.000
113	A	118	VAL	0	0.051	0.027	35.401	0.005	0.005	0.000	0.000	0.000
114	A	119	ASP	-1	-0.887	-0.955	33.755	-0.074	-0.074	0.000	0.000	0.000
115	A	120	THR	0	-0.066	-0.036	33.908	0.003	0.003	0.000	0.000	0.000
116	A	121	CYS	0	-0.023	0.001	36.262	0.005	0.005	0.000	0.000	0.000
117	A	122	ARG	1	0.945	0.975	37.305	0.065	0.065	0.000	0.000	0.000
118	A	123	LYS	1	0.878	0.939	33.609	0.069	0.069	0.000	0.000	0.000
119	A	124	PHE	0	0.018	0.010	39.098	0.003	0.003	0.000	0.000	0.000
120	A	125	ILE	0	0.034	0.004	41.055	0.002	0.002	0.000	0.000	0.000
121	A	126	LYS	1	0.913	0.966	39.899	0.048	0.048	0.000	0.000	0.000
122	A	127	ALA	0	-0.036	-0.020	40.658	0.002	0.002	0.000	0.000	0.000
123	A	128	SER	0	0.013	0.023	42.798	0.002	0.002	0.000	0.000	0.000
124	A	129	NME	0	-0.071	-0.027	45.864	0.002	0.002	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:6:ACE)