FMO DATABASE

FMODB ID: 392LL

Calculation Name: 5I7P-A-Xray372

Preferred Name: FK506-binding protein 1A

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 5I7P

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	155
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1345865.509364
FMO2-HF: Nuclear repulsion	1284881.3179
FMO2-HF: Total energy	-60984.191464
FMO2-MP2: Total energy	-61160.697592

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.
-1.646	-3.792	18.051	-8.621	-7.283	-0.029

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 : 0.043 / q_NPA : 0.018

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	-0.027	-0.005	3.637	-0.627	1.277	-0.003	-1.063	-0.838	0.002
4	A	4	VAL	0	0.020	0.001	6.564	0.049	0.049	0.000	0.000	0.000	0.000
5	A	5	GLU	-1	-0.835	-0.891	9.996	-0.532	-0.532	0.000	0.000	0.000	0.000
6	A	6	THR	0	-0.019	-0.014	13.196	0.006	0.006	0.000	0.000	0.000	0.000
7	A	7	ILE	0	-0.017	-0.007	16.439	0.019	0.019	0.000	0.000	0.000	0.000
8	A	8	SER	0	-0.039	-0.035	19.134	0.047	0.047	0.000	0.000	0.000	0.000
9	A	9	PRO	0	0.007	0.007	20.404	-0.027	-0.027	0.000	0.000	0.000	0.000
10	A	10	GLY	0	0.061	0.031	20.944	0.003	0.003	0.000	0.000	0.000	0.000
11	A	11	ASP	-1	-0.803	-0.908	22.306	-0.121	-0.121	0.000	0.000	0.000	0.000
12	A	12	GLY	0	-0.022	-0.003	20.993	0.016	0.016	0.000	0.000	0.000	0.000
13	A	13	ARG	1	0.837	0.912	22.080	0.114	0.114	0.000	0.000	0.000	0.000
14	A	14	THR	0	-0.067	-0.028	22.960	0.018	0.018	0.000	0.000	0.000	0.000
15	A	15	PHE	0	0.033	0.016	16.720	-0.012	-0.012	0.000	0.000	0.000	0.000
16	A	16	PRO	0	0.014	0.021	16.576	0.040	0.040	0.000	0.000	0.000	0.000
17	A	17	LYS	1	0.834	0.916	17.579	0.112	0.112	0.000	0.000	0.000	0.000
18	A	18	ARG	1	0.969	0.976	15.420	-0.032	-0.032	0.000	0.000	0.000	0.000
19	A	19	GLY	0	-0.009	0.000	19.158	0.011	0.011	0.000	0.000	0.000	0.000
20	A	20	GLN	0	0.014	0.008	20.802	-0.010	-0.010	0.000	0.000	0.000	0.000
21	A	21	THR	0	-0.015	-0.005	20.571	-0.015	-0.015	0.000	0.000	0.000	0.000
22	A	22	ALA	0	0.026	0.016	18.370	0.009	0.009	0.000	0.000	0.000	0.000
23	A	23	VAL	0	-0.043	-0.026	20.367	-0.004	-0.004	0.000	0.000	0.000	0.000
24	A	24	VAL	0	0.029	0.006	17.364	-0.001	-0.001	0.000	0.000	0.000	0.000
25	A	25	HIS	0	0.018	0.032	20.639	0.008	0.008	0.000	0.000	0.000	0.000
26	A	26	TYR	0	-0.021	-0.046	16.894	-0.016	-0.016	0.000	0.000	0.000	0.000
27	A	27	THR	0	0.005	-0.004	17.921	0.072	0.072	0.000	0.000	0.000	0.000
28	A	28	GLY	0	0.001	0.011	15.563	-0.074	-0.074	0.000	0.000	0.000	0.000
29	A	29	MET	0	-0.040	-0.031	14.913	0.122	0.122	0.000	0.000	0.000	0.000
30	A	30	LEU	0	0.058	0.024	13.817	-0.129	-0.129	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.858	-0.919	10.237	-0.970	-0.970	0.000	0.000	0.000	0.000
32	A	32	ASP	-1	-0.900	-0.946	13.249	-0.417	-0.417	0.000	0.000	0.000	0.000
33	A	33	GLY	0	0.008	0.005	16.269	0.050	0.050	0.000	0.000	0.000	0.000
34	A	34	LYS	1	0.893	0.949	17.826	0.332	0.332	0.000	0.000	0.000	0.000
35	A	35	LYS	1	0.829	0.882	18.301	0.260	0.260	0.000	0.000	0.000	0.000
36	A	36	PHE	0	-0.016	-0.012	14.285	0.046	0.046	0.000	0.000	0.000	0.000
37	A	37	ASP	-1	-0.740	-0.832	18.600	-0.336	-0.336	0.000	0.000	0.000	0.000
38	A	38	SER	0	0.016	0.007	19.812	-0.032	-0.032	0.000	0.000	0.000	0.000
39	A	39	SER	0	-0.028	-0.008	21.443	0.020	0.020	0.000	0.000	0.000	0.000
40	A	40	ARG	1	0.836	0.894	21.001	0.366	0.366	0.000	0.000	0.000	0.000
41	A	41	ASP	-1	-0.805	-0.866	25.169	-0.260	-0.260	0.000	0.000	0.000	0.000
42	A	42	ARG	1	0.794	0.879	21.096	0.315	0.315	0.000	0.000	0.000	0.000
43	A	43	ASN	0	-0.071	-0.027	28.174	0.013	0.013	0.000	0.000	0.000	0.000
44	A	44	LYS	1	0.959	0.977	27.273	0.170	0.170	0.000	0.000	0.000	0.000
45	A	45	PRO	0	-0.041	-0.014	24.356	-0.015	-0.015	0.000	0.000	0.000	0.000
46	A	46	PHE	0	0.021	0.005	17.413	0.023	0.023	0.000	0.000	0.000	0.000
47	A	47	LYS	1	0.806	0.884	21.456	0.147	0.147	0.000	0.000	0.000	0.000
48	A	48	PHE	0	0.056	0.032	14.914	-0.012	-0.012	0.000	0.000	0.000	0.000
49	A	49	MET	0	-0.046	-0.010	19.770	0.014	0.014	0.000	0.000	0.000	0.000
50	A	50	LEU	0	-0.008	0.007	13.831	0.000	0.000	0.000	0.000	0.000	0.000
51	A	51	GLY	0	-0.059	-0.053	15.143	0.046	0.046	0.000	0.000	0.000	0.000
52	A	52	LYS	1	0.913	0.951	16.119	0.097	0.097	0.000	0.000	0.000	0.000
53	A	53	GLN	0	-0.019	-0.009	12.022	0.048	0.048	0.000	0.000	0.000	0.000
54	A	54	GLU	-1	-0.830	-0.910	15.249	-0.178	-0.178	0.000	0.000	0.000	0.000
55	A	55	VAL	0	-0.051	-0.014	12.505	-0.028	-0.028	0.000	0.000	0.000	0.000
56	A	56	ILE	0	0.024	0.037	8.955	0.042	0.042	0.000	0.000	0.000	0.000
57	A	57	ARG	1	0.917	0.931	5.429	-0.982	-0.982	0.000	0.000	0.000	0.000
58	A	58	GLY	0	0.043	0.005	5.612	-0.051	-0.051	0.000	0.000	0.000	0.000
59	A	59	TRP	0	-0.020	-0.014	6.432	0.157	0.157	0.000	0.000	0.000	0.000
60	A	60	GLU	-1	-0.813	-0.901	9.707	-0.135	-0.135	0.000	0.000	0.000	0.000
61	A	61	GLU	-1	-0.816	-0.900	5.848	0.707	0.707	0.000	0.000	0.000	0.000
62	A	62	GLY	0	0.020	0.025	8.520	0.034	0.034	0.000	0.000	0.000	0.000
63	A	63	VAL	0	0.001	-0.024	9.392	0.137	0.137	0.000	0.000	0.000	0.000
64	A	64	ALA	0	-0.030	-0.005	12.014	0.085	0.085	0.000	0.000	0.000	0.000
65	A	65	GLN	0	-0.051	-0.040	7.565	0.124	0.124	0.000	0.000	0.000	0.000
66	A	66	MET	0	-0.079	-0.011	13.078	-0.007	-0.007	0.000	0.000	0.000	0.000
67	A	67	SER	0	-0.009	-0.007	15.765	0.048	0.048	0.000	0.000	0.000	0.000
68	A	68	VAL	0	0.002	-0.028	19.472	-0.025	-0.025	0.000	0.000	0.000	0.000
69	A	69	GLY	0	-0.004	-0.003	22.270	0.015	0.015	0.000	0.000	0.000	0.000
70	A	70	GLN	0	-0.003	0.028	16.066	0.030	0.030	0.000	0.000	0.000	0.000
71	A	71	ARG	1	0.780	0.847	18.756	0.347	0.347	0.000	0.000	0.000	0.000
72	A	72	ALA	0	0.007	-0.003	13.964	0.026	0.026	0.000	0.000	0.000	0.000
73	A	73	LYS	1	0.869	0.925	11.945	0.805	0.805	0.000	0.000	0.000	0.000
74	A	74	LEU	0	-0.016	-0.011	9.298	-0.059	-0.059	0.000	0.000	0.000	0.000
75	A	75	THR	0	0.002	0.000	6.682	0.288	0.288	0.000	0.000	0.000	0.000
76	A	76	ILE	0	-0.056	-0.024	4.984	-1.259	-1.252	-0.001	-0.030	0.025	0.000
77	A	77	SER	0	0.055	0.048	1.759	1.225	-4.473	13.607	-4.812	-3.097	-0.018
78	A	78	PRO	0	0.094	0.036	3.993	0.080	0.270	-0.001	-0.071	-0.118	0.000
79	A	79	ASP	-1	-0.870	-0.918	4.310	0.460	0.543	-0.001	-0.005	-0.077	0.000
80	A	80	TYR	0	-0.096	-0.049	2.704	-1.087	0.246	4.451	-2.637	-3.147	-0.013
81	A	81	ALA	0	0.000	-0.014	5.020	-0.032	0.003	-0.001	-0.003	-0.031	0.000
82	A	82	TYR	0	-0.031	-0.030	8.389	0.210	0.210	0.000	0.000	0.000	0.000
83	A	83	GLY	0	0.034	0.031	9.126	0.128	0.128	0.000	0.000	0.000	0.000
84	A	84	GLN	0	-0.019	-0.036	7.049	-0.213	-0.213	0.000	0.000	0.000	0.000
85	A	85	TYR	0	-0.059	-0.050	10.861	0.010	0.010	0.000	0.000	0.000	0.000
86	A	86	ASP	-1	-0.810	-0.903	14.468	0.093	0.093	0.000	0.000	0.000	0.000
87	A	87	GLU	-1	-0.926	-0.974	16.909	0.018	0.018	0.000	0.000	0.000	0.000
88	A	88	ASN	0	-0.097	-0.054	19.508	0.000	0.000	0.000	0.000	0.000	0.000
89	A	89	LEU	0	-0.064	-0.015	18.552	-0.004	-0.004	0.000	0.000	0.000	0.000
90	A	90	VAL	0	-0.016	0.006	21.324	-0.017	-0.017	0.000	0.000	0.000	0.000
91	A	91	GLN	0	-0.015	0.001	23.978	0.018	0.018	0.000	0.000	0.000	0.000
92	A	92	ARG	0	0.008	0.014	27.642	-0.013	-0.013	0.000	0.000	0.000	0.000
93	A	93	VAL	0	0.014	-0.007	30.968	0.006	0.006	0.000	0.000	0.000	0.000
94	A	94	PRO	0	0.020	-0.010	33.668	-0.004	-0.004	0.000	0.000	0.000	0.000
95	A	95	LYS	1	0.835	0.919	36.589	0.035	0.035	0.000	0.000	0.000	0.000
96	A	96	ASP	-1	-0.893	-0.946	38.159	-0.018	-0.018	0.000	0.000	0.000	0.000
97	A	97	VAL	0	-0.055	-0.030	35.741	0.000	0.000	0.000	0.000	0.000	0.000
98	A	98	PHE	0	-0.034	-0.011	32.434	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	99	MET	0	0.012	0.003	38.566	0.002	0.002	0.000	0.000	0.000	0.000
100	A	100	GLY	0	-0.015	0.001	41.603	-0.001	-0.001	0.000	0.000	0.000	0.000
101	A	101	VAL	0	-0.049	-0.030	42.427	0.001	0.001	0.000	0.000	0.000	0.000
102	A	102	ASP	-1	-0.928	-0.961	43.047	-0.045	-0.045	0.000	0.000	0.000	0.000
103	A	103	GLU	-1	-0.945	-0.966	39.680	-0.065	-0.065	0.000	0.000	0.000	0.000
104	A	104	LEU	0	-0.008	0.004	35.370	-0.002	-0.002	0.000	0.000	0.000	0.000
105	A	105	GLN	0	-0.078	-0.048	34.615	-0.005	-0.005	0.000	0.000	0.000	0.000
106	A	106	VAL	0	0.018	-0.009	30.049	-0.001	-0.001	0.000	0.000	0.000	0.000
107	A	107	GLY	0	-0.011	-0.009	28.223	-0.003	-0.003	0.000	0.000	0.000	0.000
108	A	108	MET	0	-0.053	-0.011	28.847	-0.007	-0.007	0.000	0.000	0.000	0.000
109	A	109	ARG	1	0.891	0.922	22.081	0.164	0.164	0.000	0.000	0.000	0.000
110	A	110	PHE	0	-0.034	-0.025	28.362	0.004	0.004	0.000	0.000	0.000	0.000
111	A	111	LEU	0	-0.028	-0.008	27.505	-0.004	-0.004	0.000	0.000	0.000	0.000
112	A	112	ALA	0	0.016	0.016	28.666	0.005	0.005	0.000	0.000	0.000	0.000
113	A	113	GLU	-1	-0.950	-0.985	29.308	-0.019	-0.019	0.000	0.000	0.000	0.000
114	A	114	THR	0	-0.022	-0.020	26.082	0.004	0.004	0.000	0.000	0.000	0.000
115	A	115	ASP	-1	-0.876	-0.929	26.134	0.025	0.025	0.000	0.000	0.000	0.000
116	A	116	GLN	0	-0.063	-0.041	22.810	0.011	0.011	0.000	0.000	0.000	0.000
117	A	117	GLY	0	-0.020	0.000	25.883	-0.003	-0.003	0.000	0.000	0.000	0.000
118	A	118	PRO	0	-0.042	-0.015	27.638	-0.004	-0.004	0.000	0.000	0.000	0.000
119	A	119	VAL	0	0.017	0.012	23.589	-0.009	-0.009	0.000	0.000	0.000	0.000
120	A	120	PRO	0	-0.053	-0.043	23.223	0.002	0.002	0.000	0.000	0.000	0.000
121	A	121	VAL	0	0.002	0.014	23.849	-0.003	-0.003	0.000	0.000	0.000	0.000
122	A	122	GLU	-1	-0.862	-0.929	24.531	-0.168	-0.168	0.000	0.000	0.000	0.000
123	A	123	ILE	0	0.004	0.027	26.570	0.007	0.007	0.000	0.000	0.000	0.000
124	A	124	THR	0	0.024	0.019	24.150	-0.003	-0.003	0.000	0.000	0.000	0.000
125	A	125	ALA	0	0.008	-0.004	27.589	-0.002	-0.002	0.000	0.000	0.000	0.000
126	A	126	VAL	0	-0.002	0.015	30.573	0.005	0.005	0.000	0.000	0.000	0.000
127	A	127	GLH	0	-0.109	-0.076	32.202	0.000	0.000	0.000	0.000	0.000	0.000
128	A	128	ASP	-1	-0.886	-0.949	36.250	-0.029	-0.029	0.000	0.000	0.000	0.000
129	A	129	ASP	-1	-0.909	-0.936	38.810	-0.019	-0.019	0.000	0.000	0.000	0.000
130	A	130	HIS	0	-0.001	-0.005	33.983	0.001	0.001	0.000	0.000	0.000	0.000
131	A	131	VAL	0	-0.013	-0.002	32.069	-0.005	-0.005	0.000	0.000	0.000	0.000
132	A	132	VAL	0	-0.008	0.010	26.877	0.006	0.006	0.000	0.000	0.000	0.000
133	A	133	VAL	0	-0.020	-0.021	27.212	-0.009	-0.009	0.000	0.000	0.000	0.000
134	A	134	ASP	-1	-0.749	-0.858	21.446	-0.110	-0.110	0.000	0.000	0.000	0.000
135	A	135	GLY	0	0.021	-0.004	22.622	-0.012	-0.012	0.000	0.000	0.000	0.000
136	A	136	ASN	0	-0.057	-0.020	17.135	-0.015	-0.015	0.000	0.000	0.000	0.000
137	A	137	HIS	0	0.007	0.001	15.304	-0.019	-0.019	0.000	0.000	0.000	0.000
138	A	138	MET	0	0.022	0.007	16.876	-0.012	-0.012	0.000	0.000	0.000	0.000
139	A	139	LEU	0	-0.073	-0.045	13.338	-0.017	-0.017	0.000	0.000	0.000	0.000
140	A	140	ALA	0	0.008	0.004	12.487	-0.106	-0.106	0.000	0.000	0.000	0.000
141	A	141	GLY	0	-0.010	-0.012	10.607	0.031	0.031	0.000	0.000	0.000	0.000
142	A	142	GLN	0	-0.061	-0.011	11.004	-0.055	-0.055	0.000	0.000	0.000	0.000
143	A	143	ASN	0	-0.041	-0.032	6.816	-0.597	-0.597	0.000	0.000	0.000	0.000
144	A	144	LEU	0	-0.037	-0.019	8.230	0.284	0.284	0.000	0.000	0.000	0.000
145	A	145	VAL	0	0.003	-0.002	9.262	-0.382	-0.382	0.000	0.000	0.000	0.000
146	A	146	PHE	0	-0.001	-0.006	11.035	0.226	0.226	0.000	0.000	0.000	0.000
147	A	147	ASP	-1	-0.807	-0.860	13.521	-0.494	-0.494	0.000	0.000	0.000	0.000
148	A	148	VAL	0	0.031	0.004	13.754	0.059	0.059	0.000	0.000	0.000	0.000
149	A	149	GLU	-1	-0.785	-0.873	16.628	-0.286	-0.286	0.000	0.000	0.000	0.000
150	A	150	LEU	0	0.002	0.006	17.932	0.014	0.014	0.000	0.000	0.000	0.000
151	A	151	LEU	0	-0.024	-0.010	20.058	0.030	0.030	0.000	0.000	0.000	0.000
152	A	152	LYS	1	0.858	0.904	22.993	0.162	0.162	0.000	0.000	0.000	0.000
153	A	153	LEU	0	0.003	0.022	20.520	-0.019	-0.019	0.000	0.000	0.000	0.000
154	A	154	GLU	-1	-0.816	-0.884	23.732	-0.125	-0.125	0.000	0.000	0.000	0.000
155	A	155	ALA	0	0.035	0.022	24.977	0.001	0.001	0.000	0.000	0.000	0.000

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