FMO DATABASE

FMODB ID: 851RY

Calculation Name: 5I7Q-A-Xray372

Preferred Name: FK506-binding protein 1A

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 5I7Q

Chain ID: A

ChEMBL ID: CHEMBL1902

UniProt ID: P62942

Base Structure: X-ray

Registration Date: 2023-09-20

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptHSide
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	156
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1357561.318057
FMO2-HF: Nuclear repulsion	1296301.146725
FMO2-HF: Total energy	-61260.171332
FMO2-MP2: Total energy	-61436.570557

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:1:GLY)

Summations of interaction energy for fragment #1(A:1: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.
-7.335	-8.063	17.287	-8.519	-8.039	-0.039

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.008 / q_NPA : -0.014

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	GLN	0	-0.046	-0.009	3.805	1.152	2.230	-0.015	-0.456	-0.607	0.001
4	A	4	VAL	0	0.026	0.005	6.539	-0.330	-0.330	0.000	0.000	0.000	0.000
5	A	5	GLU	-1	-0.822	-0.886	9.763	0.278	0.278	0.000	0.000	0.000	0.000
6	A	6	THR	0	-0.032	-0.020	13.097	-0.076	-0.076	0.000	0.000	0.000	0.000
7	A	7	ILE	0	-0.030	-0.007	16.371	0.021	0.021	0.000	0.000	0.000	0.000
8	A	8	SER	0	0.009	-0.013	19.024	0.014	0.014	0.000	0.000	0.000	0.000
9	A	9	PRO	0	-0.017	-0.005	20.499	-0.016	-0.016	0.000	0.000	0.000	0.000
10	A	10	GLY	0	0.063	0.034	21.068	-0.010	-0.010	0.000	0.000	0.000	0.000
11	A	11	ASP	-1	-0.802	-0.874	22.470	-0.023	-0.023	0.000	0.000	0.000	0.000
12	A	12	GLY	0	-0.024	-0.013	21.567	0.011	0.011	0.000	0.000	0.000	0.000
13	A	13	ARG	1	0.862	0.927	22.647	0.006	0.006	0.000	0.000	0.000	0.000
14	A	14	THR	0	-0.056	-0.050	23.347	0.002	0.002	0.000	0.000	0.000	0.000
15	A	15	PHE	0	0.023	0.013	17.047	-0.009	-0.009	0.000	0.000	0.000	0.000
16	A	16	PRO	0	0.033	0.036	16.738	0.013	0.013	0.000	0.000	0.000	0.000
17	A	17	LYS	1	0.814	0.901	18.145	0.073	0.073	0.000	0.000	0.000	0.000
18	A	18	ARG	1	0.997	0.982	17.746	0.128	0.128	0.000	0.000	0.000	0.000
19	A	19	GLY	0	-0.014	-0.001	19.083	0.019	0.019	0.000	0.000	0.000	0.000
20	A	20	GLN	0	0.007	0.011	20.980	0.001	0.001	0.000	0.000	0.000	0.000
21	A	21	THR	0	-0.005	0.000	20.521	-0.025	-0.025	0.000	0.000	0.000	0.000
22	A	22	ALA	0	0.022	0.018	18.241	0.024	0.024	0.000	0.000	0.000	0.000
23	A	23	VAL	0	-0.046	-0.023	20.313	-0.014	-0.014	0.000	0.000	0.000	0.000
24	A	24	VAL	0	0.030	0.007	17.376	0.016	0.016	0.000	0.000	0.000	0.000
25	A	25	HIS	0	0.027	0.029	20.627	-0.008	-0.008	0.000	0.000	0.000	0.000
26	A	26	TYR	0	-0.029	-0.054	16.978	0.003	0.003	0.000	0.000	0.000	0.000
27	A	27	THR	0	-0.031	-0.017	18.160	0.036	0.036	0.000	0.000	0.000	0.000
28	A	28	GLY	0	0.014	0.010	15.372	-0.032	-0.032	0.000	0.000	0.000	0.000
29	A	29	MET	0	-0.024	-0.025	14.706	0.079	0.079	0.000	0.000	0.000	0.000
30	A	30	LEU	0	0.029	0.014	13.542	-0.092	-0.092	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.856	-0.912	10.422	-0.120	-0.120	0.000	0.000	0.000	0.000
32	A	32	ASP	-1	-0.890	-0.942	13.178	-0.144	-0.144	0.000	0.000	0.000	0.000
33	A	33	GLY	0	-0.016	-0.011	16.323	0.033	0.033	0.000	0.000	0.000	0.000
34	A	34	LYS	1	0.902	0.960	18.045	0.237	0.237	0.000	0.000	0.000	0.000
35	A	35	LYS	1	0.826	0.897	18.151	0.149	0.149	0.000	0.000	0.000	0.000
36	A	36	PHE	0	-0.014	-0.013	13.799	0.018	0.018	0.000	0.000	0.000	0.000
37	A	37	ASP	-1	-0.747	-0.835	18.033	-0.345	-0.345	0.000	0.000	0.000	0.000
38	A	38	SER	0	-0.039	-0.044	19.626	-0.003	-0.003	0.000	0.000	0.000	0.000
39	A	39	SER	0	0.004	0.004	21.550	0.005	0.005	0.000	0.000	0.000	0.000
40	A	40	ARG	1	0.846	0.893	21.439	0.193	0.193	0.000	0.000	0.000	0.000
41	A	41	ASP	-1	-0.795	-0.854	25.206	-0.162	-0.162	0.000	0.000	0.000	0.000
42	A	42	ARG	1	0.843	0.913	21.319	0.276	0.276	0.000	0.000	0.000	0.000
43	A	43	ASN	0	-0.072	-0.028	27.952	0.011	0.011	0.000	0.000	0.000	0.000
44	A	44	LYS	1	0.967	0.978	26.869	0.165	0.165	0.000	0.000	0.000	0.000
45	A	45	PRO	0	-0.046	-0.013	24.211	-0.015	-0.015	0.000	0.000	0.000	0.000
46	A	46	PHE	0	0.007	0.008	17.302	0.013	0.013	0.000	0.000	0.000	0.000
47	A	47	LYS	1	0.830	0.884	21.151	0.153	0.153	0.000	0.000	0.000	0.000
48	A	48	PHE	0	0.039	0.028	14.578	-0.019	-0.019	0.000	0.000	0.000	0.000
49	A	49	MET	0	-0.036	-0.014	19.280	0.025	0.025	0.000	0.000	0.000	0.000
50	A	50	LEU	0	0.009	0.005	14.684	-0.026	-0.026	0.000	0.000	0.000	0.000
51	A	51	GLY	0	-0.042	-0.039	14.929	0.050	0.050	0.000	0.000	0.000	0.000
52	A	52	LYS	1	0.873	0.942	15.901	0.233	0.233	0.000	0.000	0.000	0.000
53	A	53	GLN	0	-0.027	-0.017	12.695	0.004	0.004	0.000	0.000	0.000	0.000
54	A	54	GLU	-1	-0.831	-0.907	14.547	-0.290	-0.290	0.000	0.000	0.000	0.000
55	A	55	VAL	0	-0.057	-0.018	12.378	0.004	0.004	0.000	0.000	0.000	0.000
56	A	56	ILE	0	0.025	0.028	8.816	0.001	0.001	0.000	0.000	0.000	0.000
57	A	57	ARG	1	0.925	0.953	5.106	0.438	0.438	0.000	0.000	0.000	0.000
58	A	58	GLY	0	0.039	0.005	5.452	0.062	0.062	0.000	0.000	0.000	0.000
59	A	59	TRP	0	-0.020	-0.010	6.251	0.384	0.384	0.000	0.000	0.000	0.000
60	A	60	GLU	-1	-0.799	-0.888	9.583	-0.240	-0.240	0.000	0.000	0.000	0.000
61	A	61	GLU	-1	-0.830	-0.919	5.042	0.346	0.502	-0.001	-0.004	-0.150	0.000
62	A	62	GLY	0	0.024	0.019	8.360	0.174	0.174	0.000	0.000	0.000	0.000
63	A	63	VAL	0	0.012	-0.021	9.405	0.162	0.162	0.000	0.000	0.000	0.000
64	A	64	ALA	0	-0.036	-0.006	11.979	0.082	0.082	0.000	0.000	0.000	0.000
65	A	65	GLN	0	-0.069	-0.042	7.718	0.168	0.168	0.000	0.000	0.000	0.000
66	A	66	MET	0	-0.079	-0.014	13.242	0.016	0.016	0.000	0.000	0.000	0.000
67	A	67	SER	0	-0.013	-0.012	15.940	0.005	0.005	0.000	0.000	0.000	0.000
68	A	68	VAL	0	0.015	-0.020	19.685	-0.014	-0.014	0.000	0.000	0.000	0.000
69	A	69	GLY	0	-0.011	-0.007	22.346	0.018	0.018	0.000	0.000	0.000	0.000
70	A	70	GLN	0	-0.033	0.008	16.281	0.002	0.002	0.000	0.000	0.000	0.000
71	A	71	ARG	1	0.822	0.868	18.710	0.111	0.111	0.000	0.000	0.000	0.000
72	A	72	ALA	0	-0.008	-0.011	13.865	0.045	0.045	0.000	0.000	0.000	0.000
73	A	73	LYS	1	0.871	0.921	12.379	-0.067	-0.067	0.000	0.000	0.000	0.000
74	A	74	LEU	0	-0.027	-0.019	9.077	0.059	0.059	0.000	0.000	0.000	0.000
75	A	75	THR	0	0.014	0.011	7.229	-0.043	-0.043	0.000	0.000	0.000	0.000
76	A	76	ILE	0	-0.042	-0.017	4.692	-0.293	-0.256	-0.001	-0.037	0.001	0.000
77	A	77	SER	0	0.037	0.004	1.941	-3.821	-6.516	8.408	-3.210	-2.503	-0.025
78	A	78	PRO	0	0.085	0.028	3.850	-0.329	-0.223	-0.001	-0.022	-0.083	0.000
79	A	79	ASP	-1	-0.872	-0.902	3.812	-5.338	-4.615	0.005	-0.349	-0.379	-0.002
80	A	80	TYR	0	-0.066	-0.023	2.626	-0.493	-0.640	8.893	-4.436	-4.311	-0.013
81	A	81	ALA	0	-0.004	-0.022	4.900	0.492	0.506	-0.001	-0.005	-0.007	0.000
82	A	82	TYR	0	-0.012	-0.013	8.155	0.185	0.185	0.000	0.000	0.000	0.000
83	A	83	GLY	0	0.037	0.034	9.282	0.196	0.196	0.000	0.000	0.000	0.000
84	A	84	VAL	0	0.000	-0.008	9.610	-0.051	-0.051	0.000	0.000	0.000	0.000
85	A	85	PRO	0	-0.003	-0.010	12.022	0.034	0.034	0.000	0.000	0.000	0.000
86	A	86	SER	0	-0.015	-0.013	15.774	0.018	0.018	0.000	0.000	0.000	0.000
87	A	87	PRO	0	0.021	-0.002	18.538	0.003	0.003	0.000	0.000	0.000	0.000
88	A	88	ASP	-1	-0.865	-0.924	21.608	-0.179	-0.179	0.000	0.000	0.000	0.000
89	A	89	LEU	0	-0.040	-0.011	19.052	0.010	0.010	0.000	0.000	0.000	0.000
90	A	90	ILE	0	-0.032	0.000	21.870	-0.005	-0.005	0.000	0.000	0.000	0.000
91	A	91	GLN	0	-0.049	-0.024	24.995	0.018	0.018	0.000	0.000	0.000	0.000
92	A	92	TYR	0	-0.016	-0.008	28.560	-0.002	-0.002	0.000	0.000	0.000	0.000
93	A	93	PHE	0	0.010	0.009	29.458	0.003	0.003	0.000	0.000	0.000	0.000
94	A	94	SER	0	-0.030	-0.026	34.613	0.002	0.002	0.000	0.000	0.000	0.000
95	A	95	ARG	1	0.864	0.902	37.728	0.076	0.076	0.000	0.000	0.000	0.000
96	A	96	ARG	1	0.797	0.893	38.970	0.082	0.082	0.000	0.000	0.000	0.000
97	A	97	GLU	-1	-0.871	-0.937	36.054	-0.098	-0.098	0.000	0.000	0.000	0.000
98	A	98	PHE	0	-0.005	-0.002	34.817	-0.007	-0.007	0.000	0.000	0.000	0.000
99	A	99	MET	0	-0.050	-0.034	37.659	0.008	0.008	0.000	0.000	0.000	0.000
100	A	100	ASP	-1	-0.919	-0.937	35.657	-0.116	-0.116	0.000	0.000	0.000	0.000
101	A	101	ALA	0	-0.054	-0.037	38.795	0.005	0.005	0.000	0.000	0.000	0.000
102	A	102	GLY	0	-0.029	-0.012	39.571	-0.003	-0.003	0.000	0.000	0.000	0.000
103	A	103	GLU	-1	-0.827	-0.887	40.150	-0.077	-0.077	0.000	0.000	0.000	0.000
104	A	104	PRO	0	0.003	0.005	35.611	-0.004	-0.004	0.000	0.000	0.000	0.000
105	A	105	GLU	-1	-0.940	-0.969	34.432	-0.100	-0.100	0.000	0.000	0.000	0.000
106	A	106	ILE	0	-0.035	-0.039	29.347	-0.008	-0.008	0.000	0.000	0.000	0.000
107	A	107	GLY	0	-0.041	-0.021	27.610	0.001	0.001	0.000	0.000	0.000	0.000
108	A	108	ALA	0	-0.006	0.008	28.316	-0.010	-0.010	0.000	0.000	0.000	0.000
109	A	109	ILE	0	-0.035	-0.026	26.024	-0.008	-0.008	0.000	0.000	0.000	0.000
110	A	110	MET	0	0.010	0.019	28.855	0.012	0.012	0.000	0.000	0.000	0.000
111	A	111	LEU	0	0.001	0.001	28.466	-0.016	-0.016	0.000	0.000	0.000	0.000
112	A	112	PHE	0	0.040	0.020	29.184	0.012	0.012	0.000	0.000	0.000	0.000
113	A	113	THR	0	-0.031	-0.011	29.740	-0.008	-0.008	0.000	0.000	0.000	0.000
114	A	114	ALA	0	0.020	0.007	26.773	0.003	0.003	0.000	0.000	0.000	0.000
115	A	115	MET	0	-0.013	-0.024	27.868	0.012	0.012	0.000	0.000	0.000	0.000
116	A	116	ASP	-1	-0.897	-0.919	25.478	-0.182	-0.182	0.000	0.000	0.000	0.000
117	A	117	GLY	0	-0.027	-0.010	28.851	0.007	0.007	0.000	0.000	0.000	0.000
118	A	118	SER	0	-0.116	-0.072	26.765	0.001	0.001	0.000	0.000	0.000	0.000
119	A	119	GLU	-1	-0.909	-0.958	28.996	-0.149	-0.149	0.000	0.000	0.000	0.000
120	A	120	MET	0	-0.041	-0.016	24.461	-0.020	-0.020	0.000	0.000	0.000	0.000
121	A	121	PRO	0	-0.019	-0.019	23.103	0.013	0.013	0.000	0.000	0.000	0.000
122	A	122	GLY	0	0.045	0.019	24.185	-0.019	-0.019	0.000	0.000	0.000	0.000
123	A	123	VAL	0	-0.061	-0.018	23.472	0.010	0.010	0.000	0.000	0.000	0.000
124	A	124	ILE	0	0.013	0.018	26.249	0.001	0.001	0.000	0.000	0.000	0.000
125	A	125	ARG	1	0.820	0.893	20.631	0.234	0.234	0.000	0.000	0.000	0.000
126	A	126	GLU	-1	-0.853	-0.918	28.078	-0.107	-0.107	0.000	0.000	0.000	0.000
127	A	127	ILE	0	0.006	0.009	31.383	-0.002	-0.002	0.000	0.000	0.000	0.000
128	A	128	ASN	0	-0.050	-0.013	33.497	0.009	0.009	0.000	0.000	0.000	0.000
129	A	129	GLY	0	0.002	-0.006	37.217	0.002	0.002	0.000	0.000	0.000	0.000
130	A	130	ASP	-1	-0.839	-0.922	39.780	-0.079	-0.079	0.000	0.000	0.000	0.000
131	A	131	SER	0	-0.020	0.004	35.271	-0.004	-0.004	0.000	0.000	0.000	0.000
132	A	132	ILE	0	0.017	0.003	32.020	0.001	0.001	0.000	0.000	0.000	0.000
133	A	133	THR	0	-0.027	-0.038	27.782	0.000	0.000	0.000	0.000	0.000	0.000
134	A	134	VAL	0	0.000	0.000	27.055	-0.004	-0.004	0.000	0.000	0.000	0.000
135	A	135	ASP	-1	-0.812	-0.891	21.676	-0.269	-0.269	0.000	0.000	0.000	0.000
136	A	136	PHE	0	0.047	0.002	22.748	-0.006	-0.006	0.000	0.000	0.000	0.000
137	A	137	ASN	0	-0.064	-0.018	17.589	-0.058	-0.058	0.000	0.000	0.000	0.000
138	A	138	HIS	0	0.064	0.036	15.158	0.002	0.002	0.000	0.000	0.000	0.000
139	A	139	PRO	0	0.026	0.003	16.659	-0.021	-0.021	0.000	0.000	0.000	0.000
140	A	140	LEU	0	-0.068	-0.039	13.291	0.019	0.019	0.000	0.000	0.000	0.000
141	A	141	ALA	0	-0.012	-0.001	12.396	-0.114	-0.114	0.000	0.000	0.000	0.000
142	A	142	GLY	0	-0.045	-0.030	10.663	0.096	0.096	0.000	0.000	0.000	0.000
143	A	143	GLN	0	-0.060	-0.026	10.923	0.106	0.106	0.000	0.000	0.000	0.000
144	A	144	THR	0	-0.025	-0.022	6.417	-0.330	-0.330	0.000	0.000	0.000	0.000
145	A	145	LEU	0	-0.078	-0.026	8.011	0.274	0.274	0.000	0.000	0.000	0.000
146	A	146	VAL	0	0.036	0.011	8.928	-0.172	-0.172	0.000	0.000	0.000	0.000
147	A	147	PHE	0	-0.008	-0.009	10.725	0.104	0.104	0.000	0.000	0.000	0.000
148	A	148	ASP	-1	-0.797	-0.846	13.455	-0.171	-0.171	0.000	0.000	0.000	0.000
149	A	149	VAL	0	0.036	0.002	13.676	-0.001	-0.001	0.000	0.000	0.000	0.000
150	A	150	GLU	-1	-0.824	-0.896	16.564	-0.104	-0.104	0.000	0.000	0.000	0.000
151	A	151	LEU	0	0.007	0.005	18.018	-0.017	-0.017	0.000	0.000	0.000	0.000
152	A	152	LEU	0	-0.023	-0.006	20.047	0.027	0.027	0.000	0.000	0.000	0.000
153	A	153	LYS	1	0.855	0.906	23.071	0.127	0.127	0.000	0.000	0.000	0.000
154	A	154	LEU	0	-0.004	0.006	20.012	-0.018	-0.018	0.000	0.000	0.000	0.000
155	A	155	GLU	-1	-0.817	-0.880	23.937	-0.116	-0.116	0.000	0.000	0.000	0.000
156	A	156	ALA	0	0.044	0.028	24.951	-0.006	-0.006	0.000	0.000	0.000	0.000

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