FMO DATABASE

FMODB ID: 8N6GY

Calculation Name: 2ES9-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

PDB ID: 2ES9

Chain ID: A

ChEMBL ID:

UniProt ID: Q8ZRJ2

Base Structure: X-ray

Registration Date: 2025-07-08

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	OptH
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	187
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-733495.983737
FMO2-HF: Nuclear repulsion	694761.508769
FMO2-HF: Total energy	-38734.474967
FMO2-MP2: Total energy	-38847.287566

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:11:THR)

Summations of interaction energy for fragment #1(A:11:THR)

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.
-4.647	-3.702	9.794	-5.15	-5.585	-0.047

Interaction energy analysis for fragmet #1(A:11:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.121 / q_NPA : 0.075

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].
4	A	12	ALA	0	-0.060	0.123	4.596	0.049	0.218	-0.001	-0.075	-0.093	0.000
5	A	13	ILE	0	0.063	-0.099	3.582	0.547	1.671	-0.004	-0.530	-0.589	0.002
6	A	13	ILE	0	-0.045	0.100	4.359	-0.126	-0.030	-0.001	-0.023	-0.072	0.000
7	A	14	GLU	0	0.025	-0.146	3.264	1.703	1.730	0.020	0.214	-0.261	-0.001
8	A	14	GLU	-1	-0.929	-0.816	1.971	-8.129	-10.300	9.508	-4.105	-3.231	-0.042
9	A	15	LYS	0	0.161	-0.080	3.904	0.531	0.793	-0.001	-0.083	-0.177	0.000
10	A	15	LYS	1	0.818	1.082	4.798	-1.481	-1.448	-0.001	-0.011	-0.020	0.000
11	A	16	ALA	0	0.030	-0.127	5.727	0.337	0.337	0.000	0.000	0.000	0.000
12	A	16	ALA	0	-0.072	0.107	8.046	-0.041	-0.041	0.000	0.000	0.000	0.000
13	A	17	LEU	0	0.037	-0.138	7.653	0.321	0.321	0.000	0.000	0.000	0.000
14	A	17	LEU	0	-0.086	0.098	7.706	0.004	0.004	0.000	0.000	0.000	0.000
15	A	18	ASP	0	0.115	-0.076	8.001	-0.002	-0.002	0.000	0.000	0.000	0.000
16	A	18	ASP	-1	-0.959	-0.855	6.642	0.440	0.440	0.000	0.000	0.000	0.000
17	A	19	PHE	0	0.006	-0.116	9.558	0.064	0.064	0.000	0.000	0.000	0.000
18	A	19	PHE	0	-0.037	0.071	10.362	0.052	0.052	0.000	0.000	0.000	0.000
19	A	20	ILE	0	0.011	-0.117	11.926	0.065	0.065	0.000	0.000	0.000	0.000
20	A	20	ILE	0	-0.084	0.116	12.542	-0.009	-0.009	0.000	0.000	0.000	0.000
21	A	21	GLY	0	0.024	-0.084	12.557	0.012	0.012	0.000	0.000	0.000	0.000
22	A	22	GLY	0	-0.047	-0.009	14.015	0.036	0.036	0.000	0.000	0.000	0.000
23	A	23	MET	0	0.089	0.023	15.706	0.040	0.040	0.000	0.000	0.000	0.000
24	A	23	MET	0	-0.176	0.082	16.293	-0.008	-0.008	0.000	0.000	0.000	0.000
25	A	24	ASN	0	0.156	-0.042	18.383	-0.002	-0.002	0.000	0.000	0.000	0.000
26	A	24	ASN	0	-0.155	0.042	23.006	-0.005	-0.005	0.000	0.000	0.000	0.000
27	A	25	THR	0	0.014	-0.134	19.126	-0.008	-0.008	0.000	0.000	0.000	0.000
28	A	25	THR	0	-0.020	0.112	16.996	0.004	0.004	0.000	0.000	0.000	0.000
29	A	26	SER	0	0.117	-0.061	20.277	-0.027	-0.027	0.000	0.000	0.000	0.000
30	A	26	SER	0	-0.018	0.098	22.699	0.006	0.006	0.000	0.000	0.000	0.000
31	A	27	ALA	0	0.091	-0.103	23.708	0.000	0.000	0.000	0.000	0.000	0.000
32	A	27	ALA	0	-0.094	0.121	24.650	0.003	0.003	0.000	0.000	0.000	0.000
33	A	28	SER	0	0.001	-0.087	24.512	-0.018	-0.018	0.000	0.000	0.000	0.000
34	A	28	SER	0	-0.029	0.068	28.435	0.002	0.002	0.000	0.000	0.000	0.000
35	A	29	VAL	0	0.081	-0.114	26.319	-0.019	-0.019	0.000	0.000	0.000	0.000
36	A	29	VAL	0	-0.108	0.105	28.134	0.000	0.000	0.000	0.000	0.000	0.000
37	A	30	PRO	0	-0.014	-0.100	22.376	0.016	0.016	0.000	0.000	0.000	0.000
38	A	31	HIS	0	0.105	0.003	24.301	-0.001	-0.001	0.000	0.000	0.000	0.000
39	A	31	HIS	0	-0.048	0.120	24.636	0.008	0.008	0.000	0.000	0.000	0.000
40	A	32	SER	0	0.080	-0.034	24.323	-0.011	-0.011	0.000	0.000	0.000	0.000
41	A	32	SER	0	-0.055	0.046	27.521	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	33	MET	0	0.107	-0.109	23.857	-0.016	-0.016	0.000	0.000	0.000	0.000
43	A	33	MET	0	-0.056	0.115	23.331	0.006	0.006	0.000	0.000	0.000	0.000
44	A	34	ASP	0	0.180	-0.072	20.235	0.011	0.011	0.000	0.000	0.000	0.000
45	A	34	ASP	-1	-0.961	-0.838	20.622	-0.037	-0.037	0.000	0.000	0.000	0.000
46	A	35	GLU	0	0.146	-0.105	19.869	-0.029	-0.029	0.000	0.000	0.000	0.000
47	A	35	GLU	-1	-1.018	-0.849	23.199	-0.127	-0.127	0.000	0.000	0.000	0.000
48	A	36	SER	0	-0.038	-0.110	20.789	-0.035	-0.035	0.000	0.000	0.000	0.000
49	A	36	SER	0	-0.044	0.069	22.749	0.004	0.004	0.000	0.000	0.000	0.000
50	A	37	THR	0	0.005	-0.100	18.616	-0.018	-0.018	0.000	0.000	0.000	0.000
51	A	37	THR	0	-0.019	0.086	16.587	0.017	0.017	0.000	0.000	0.000	0.000
52	A	38	ALA	0	0.129	-0.078	16.146	-0.010	-0.010	0.000	0.000	0.000	0.000
53	A	38	ALA	0	-0.051	0.099	17.368	-0.004	-0.004	0.000	0.000	0.000	0.000
54	A	39	LYS	0	0.008	-0.129	16.183	-0.072	-0.072	0.000	0.000	0.000	0.000
55	A	39	LYS	1	0.737	1.007	20.177	0.168	0.168	0.000	0.000	0.000	0.000
56	A	40	GLY	0	-0.018	-0.101	17.520	-0.031	-0.031	0.000	0.000	0.000	0.000
57	A	41	ILE	0	0.127	0.014	13.298	0.010	0.010	0.000	0.000	0.000	0.000
58	A	41	ILE	0	-0.086	0.100	11.228	0.000	0.000	0.000	0.000	0.000	0.000
59	A	42	LEU	0	0.013	-0.117	12.774	-0.094	-0.094	0.000	0.000	0.000	0.000
60	A	42	LEU	0	-0.086	0.106	13.036	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	43	LYS	0	0.178	-0.044	14.248	-0.077	-0.077	0.000	0.000	0.000	0.000
62	A	43	LYS	1	0.742	0.985	17.808	0.196	0.196	0.000	0.000	0.000	0.000
63	A	44	TYR	0	0.023	-0.094	14.227	-0.020	-0.020	0.000	0.000	0.000	0.000
64	A	44	TYR	0	-0.049	0.089	11.443	0.041	0.041	0.000	0.000	0.000	0.000
65	A	45	LEU	0	0.068	-0.109	10.454	0.114	0.114	0.000	0.000	0.000	0.000
66	A	45	LEU	0	-0.053	0.121	7.910	-0.007	-0.007	0.000	0.000	0.000	0.000
67	A	46	HIS	0	0.104	-0.079	11.474	-0.094	-0.094	0.000	0.000	0.000	0.000
68	A	46	HIS	0	-0.062	0.092	14.614	-0.049	-0.049	0.000	0.000	0.000	0.000
69	A	47	ASP	0	0.071	-0.109	13.831	-0.021	-0.021	0.000	0.000	0.000	0.000
70	A	47	ASP	-1	-0.953	-0.841	15.849	-0.233	-0.233	0.000	0.000	0.000	0.000
71	A	48	LEU	0	-0.054	-0.153	11.710	0.066	0.066	0.000	0.000	0.000	0.000
72	A	48	LEU	0	-0.101	0.111	10.325	0.008	0.008	0.000	0.000	0.000	0.000
73	A	49	GLY	0	0.004	-0.086	12.035	0.011	0.011	0.000	0.000	0.000	0.000
74	A	50	VAL	0	-0.001	-0.038	8.285	0.005	0.005	0.000	0.000	0.000	0.000
75	A	50	VAL	0	-0.085	0.107	6.163	-0.097	-0.097	0.000	0.000	0.000	0.000
76	A	51	PRO	0	0.032	-0.087	9.521	-0.073	-0.073	0.000	0.000	0.000	0.000
77	A	52	VAL	0	0.081	-0.012	9.878	-0.316	-0.316	0.000	0.000	0.000	0.000
78	A	52	VAL	0	-0.074	0.117	8.861	0.007	0.007	0.000	0.000	0.000	0.000
79	A	53	SER	0	0.040	-0.094	10.931	0.206	0.206	0.000	0.000	0.000	0.000
80	A	53	SER	0	-0.004	0.084	12.853	-0.049	-0.049	0.000	0.000	0.000	0.000
81	A	54	PRO	0	0.043	-0.087	13.492	-0.049	-0.049	0.000	0.000	0.000	0.000
82	A	55	GLU	0	0.074	0.005	15.789	0.037	0.037	0.000	0.000	0.000	0.000
83	A	55	GLU	-1	-0.950	-0.838	14.882	-0.633	-0.633	0.000	0.000	0.000	0.000
84	A	56	VAL	0	0.080	-0.107	10.938	0.106	0.106	0.000	0.000	0.000	0.000
85	A	56	VAL	0	-0.049	0.112	8.884	-0.046	-0.046	0.000	0.000	0.000	0.000
86	A	57	VAL	0	0.029	-0.101	12.268	-0.063	-0.063	0.000	0.000	0.000	0.000
87	A	57	VAL	0	-0.080	0.075	13.330	0.018	0.018	0.000	0.000	0.000	0.000
88	A	58	VAL	0	0.099	-0.098	14.097	0.049	0.049	0.000	0.000	0.000	0.000
89	A	58	VAL	0	-0.067	0.096	17.697	0.010	0.010	0.000	0.000	0.000	0.000
90	A	59	ALA	0	0.132	-0.075	14.589	0.095	0.095	0.000	0.000	0.000	0.000
91	A	59	ALA	0	-0.112	0.104	13.635	-0.024	-0.024	0.000	0.000	0.000	0.000
92	A	60	ARG	0	0.054	-0.128	12.490	0.067	0.067	0.000	0.000	0.000	0.000
93	A	60	ARG	1	0.821	1.091	7.567	0.674	0.674	0.000	0.000	0.000	0.000
94	A	61	GLY	0	-0.001	-0.119	13.473	0.080	0.080	0.000	0.000	0.000	0.000
95	A	62	GLU	0	0.051	-0.020	16.814	0.065	0.065	0.000	0.000	0.000	0.000
96	A	62	GLU	-1	-1.012	-0.866	18.177	-0.388	-0.388	0.000	0.000	0.000	0.000
97	A	63	GLN	0	0.084	-0.090	15.124	0.062	0.062	0.000	0.000	0.000	0.000
98	A	63	GLN	0	-0.135	0.073	12.059	-0.106	-0.106	0.000	0.000	0.000	0.000
99	A	64	GLU	0	-0.003	-0.148	15.709	0.044	0.044	0.000	0.000	0.000	0.000
100	A	64	GLU	-1	-0.961	-0.831	12.690	-0.236	-0.236	0.000	0.000	0.000	0.000
101	A	65	GLY	0	-0.003	-0.091	16.665	0.047	0.047	0.000	0.000	0.000	0.000
102	A	66	TRP	0	0.060	-0.006	18.984	0.042	0.042	0.000	0.000	0.000	0.000
103	A	66	TRP	0	-0.091	0.058	13.459	-0.025	-0.025	0.000	0.000	0.000	0.000
104	A	67	ASN	0	0.140	-0.057	20.104	-0.005	-0.005	0.000	0.000	0.000	0.000
105	A	67	ASN	0	-0.193	0.059	23.547	-0.015	-0.015	0.000	0.000	0.000	0.000
106	A	68	PRO	0	0.030	-0.093	22.444	-0.019	-0.019	0.000	0.000	0.000	0.000
107	A	69	GLU	0	0.123	-0.002	23.477	-0.030	-0.030	0.000	0.000	0.000	0.000
108	A	69	GLU	-1	-1.027	-0.865	26.383	-0.158	-0.158	0.000	0.000	0.000	0.000
109	A	70	PHE	0	0.071	-0.123	22.014	-0.006	-0.006	0.000	0.000	0.000	0.000
110	A	70	PHE	0	-0.104	0.106	17.561	0.004	0.004	0.000	0.000	0.000	0.000
111	A	71	THR	0	0.005	-0.120	19.076	-0.012	-0.012	0.000	0.000	0.000	0.000
112	A	71	THR	0	0.014	0.123	17.891	-0.007	-0.007	0.000	0.000	0.000	0.000
113	A	72	LYS	0	0.129	-0.074	19.958	-0.048	-0.048	0.000	0.000	0.000	0.000
114	A	72	LYS	1	0.838	1.070	24.190	0.196	0.196	0.000	0.000	0.000	0.000
115	A	73	LYS	0	-0.067	-0.130	22.473	-0.017	-0.017	0.000	0.000	0.000	0.000
116	A	73	LYS	1	0.899	1.085	22.967	0.180	0.180	0.000	0.000	0.000	0.000
117	A	74	VAL	0	0.144	-0.114	18.032	0.010	0.010	0.000	0.000	0.000	0.000
118	A	74	VAL	0	-0.063	0.132	15.953	-0.001	-0.001	0.000	0.000	0.000	0.000
119	A	75	ALA	0	0.071	-0.136	17.719	-0.047	-0.047	0.000	0.000	0.000	0.000
120	A	75	ALA	0	-0.035	0.144	18.633	0.001	0.001	0.000	0.000	0.000	0.000
121	A	76	GLY	0	-0.018	-0.097	18.761	-0.016	-0.016	0.000	0.000	0.000	0.000
122	A	77	TRP	0	-0.005	-0.039	20.124	0.016	0.016	0.000	0.000	0.000	0.000
123	A	77	TRP	0	-0.043	0.091	19.303	0.014	0.014	0.000	0.000	0.000	0.000
124	A	78	ALA	0	0.109	-0.105	16.253	0.042	0.042	0.000	0.000	0.000	0.000
125	A	78	ALA	0	-0.022	0.144	15.516	-0.015	-0.015	0.000	0.000	0.000	0.000
126	A	79	GLU	0	0.087	-0.122	17.301	-0.046	-0.046	0.000	0.000	0.000	0.000
127	A	79	GLU	-1	-1.022	-0.842	20.579	-0.320	-0.320	0.000	0.000	0.000	0.000
128	A	80	LYS	0	0.055	-0.066	19.983	0.005	0.005	0.000	0.000	0.000	0.000
129	A	80	LYS	1	0.856	1.017	22.053	0.215	0.215	0.000	0.000	0.000	0.000
130	A	81	VAL	0	0.060	-0.085	17.989	0.040	0.040	0.000	0.000	0.000	0.000
131	A	81	VAL	0	-0.088	0.107	16.387	0.007	0.007	0.000	0.000	0.000	0.000
132	A	82	ALA	0	0.123	-0.096	17.766	0.020	0.020	0.000	0.000	0.000	0.000
133	A	82	ALA	0	-0.059	0.129	16.852	-0.011	-0.011	0.000	0.000	0.000	0.000
134	A	83	SER	0	-0.081	-0.125	18.405	-0.004	-0.004	0.000	0.000	0.000	0.000
135	A	83	SER	0	-0.105	0.024	22.765	0.019	0.019	0.000	0.000	0.000	0.000
136	A	84	GLY	0	0.005	-0.070	21.175	0.020	0.020	0.000	0.000	0.000	0.000
137	A	85	ASN	0	0.065	0.018	22.361	0.026	0.026	0.000	0.000	0.000	0.000
138	A	85	ASN	0	-0.127	0.048	25.113	0.013	0.013	0.000	0.000	0.000	0.000
139	A	86	ARG	0	0.102	-0.067	23.182	-0.017	-0.017	0.000	0.000	0.000	0.000
140	A	86	ARG	1	0.868	1.049	25.827	0.126	0.126	0.000	0.000	0.000	0.000
141	A	87	ILE	0	0.044	-0.120	23.053	0.003	0.003	0.000	0.000	0.000	0.000
142	A	87	ILE	0	-0.029	0.134	21.145	0.001	0.001	0.000	0.000	0.000	0.000
143	A	88	LEU	0	0.125	-0.116	24.432	0.009	0.009	0.000	0.000	0.000	0.000
144	A	88	LEU	0	-0.095	0.108	27.666	0.000	0.000	0.000	0.000	0.000	0.000
145	A	89	ILE	0	0.021	-0.146	23.488	-0.013	-0.013	0.000	0.000	0.000	0.000
146	A	89	ILE	0	-0.057	0.153	21.535	-0.002	-0.002	0.000	0.000	0.000	0.000
147	A	90	LYS	0	0.112	-0.062	24.777	0.011	0.011	0.000	0.000	0.000	0.000
148	A	90	LYS	1	0.829	1.045	27.466	0.037	0.037	0.000	0.000	0.000	0.000
149	A	91	ASN	0	0.043	-0.106	25.924	0.004	0.004	0.000	0.000	0.000	0.000
150	A	91	ASN	0	-0.093	0.067	26.367	-0.008	-0.008	0.000	0.000	0.000	0.000
151	A	92	PRO	0	0.051	-0.107	22.575	0.001	0.001	0.000	0.000	0.000	0.000
152	A	93	GLU	0	0.095	0.001	21.579	-0.002	-0.002	0.000	0.000	0.000	0.000
153	A	93	GLU	-1	-0.896	-0.811	24.631	0.009	0.009	0.000	0.000	0.000	0.000
154	A	94	TYR	0	0.030	-0.077	21.957	0.027	0.027	0.000	0.000	0.000	0.000
155	A	94	TYR	0	-0.087	0.062	21.825	-0.008	-0.008	0.000	0.000	0.000	0.000
156	A	95	PHE	0	0.063	-0.093	17.859	0.026	0.026	0.000	0.000	0.000	0.000
157	A	95	PHE	0	-0.075	0.110	13.507	-0.007	-0.007	0.000	0.000	0.000	0.000
158	A	96	SER	0	0.103	-0.043	18.210	-0.011	-0.011	0.000	0.000	0.000	0.000
159	A	96	SER	0	-0.059	0.047	17.534	0.017	0.017	0.000	0.000	0.000	0.000
160	A	97	THR	0	0.122	-0.067	16.792	0.005	0.005	0.000	0.000	0.000	0.000
161	A	97	THR	0	-0.029	0.090	18.246	-0.010	-0.010	0.000	0.000	0.000	0.000
162	A	98	TYR	0	0.118	-0.055	15.961	0.024	0.024	0.000	0.000	0.000	0.000
163	A	98	TYR	0	-0.106	0.079	13.886	0.012	0.012	0.000	0.000	0.000	0.000
164	A	99	MET	0	0.068	-0.101	12.830	0.142	0.142	0.000	0.000	0.000	0.000
165	A	99	MET	0	-0.108	0.087	13.293	-0.024	-0.024	0.000	0.000	0.000	0.000
166	A	100	GLN	0	0.138	-0.072	11.794	0.044	0.044	0.000	0.000	0.000	0.000
167	A	100	GLN	0	-0.113	0.087	14.579	-0.044	-0.044	0.000	0.000	0.000	0.000
168	A	101	GLU	0	0.061	-0.147	12.023	-0.021	-0.021	0.000	0.000	0.000	0.000
169	A	101	GLU	-1	-1.031	-0.853	14.304	0.345	0.345	0.000	0.000	0.000	0.000
170	A	102	GLN	0	0.168	-0.046	10.486	0.061	0.061	0.000	0.000	0.000	0.000
171	A	102	GLN	0	-0.105	0.078	8.706	0.342	0.342	0.000	0.000	0.000	0.000
172	A	103	LEU	0	0.073	-0.093	7.464	0.476	0.476	0.000	0.000	0.000	0.000
173	A	103	LEU	0	-0.089	0.084	7.194	-0.069	-0.069	0.000	0.000	0.000	0.000
174	A	104	LYS	0	0.164	-0.089	7.569	-0.065	-0.065	0.000	0.000	0.000	0.000
175	A	104	LYS	1	0.811	1.052	11.686	-0.347	-0.347	0.000	0.000	0.000	0.000
176	A	105	GLU	0	0.033	-0.135	9.249	-0.184	-0.184	0.000	0.000	0.000	0.000
177	A	105	GLU	-1	-1.021	-0.845	8.757	1.444	1.444	0.000	0.000	0.000	0.000
178	A	106	LEU	0	0.043	-0.111	4.658	-0.105	-0.047	-0.002	-0.005	-0.052	0.000
179	A	106	LEU	0	-0.090	0.100	3.668	-0.330	-0.021	0.017	-0.111	-0.214	0.000
180	A	107	VAL	0	0.108	-0.080	4.797	0.004	0.138	-0.002	-0.008	-0.124	0.000
181	A	107	VAL	0	-0.091	0.076	6.677	-0.099	-0.099	0.000	0.000	0.000	0.000
182	A	108	LEU	0	0.021	-0.110	6.501	-0.152	-0.152	0.000	0.000	0.000	0.000
183	A	108	LEU	0	-0.115	0.071	10.072	-0.023	-0.023	0.000	0.000	0.000	0.000
184	A	109	GLU	0	0.055	-0.099	7.442	-0.388	-0.388	0.000	0.000	0.000	0.000
185	A	109	GLU	-1	-1.026	-0.851	6.366	2.069	2.069	0.000	0.000	0.000	0.000
186	A	110	HIS	0	-0.132	-0.148	5.920	0.086	0.086	0.000	0.000	0.000	0.000
187	A	110	HIS	0	0.029	0.005	3.229	-1.631	-0.727	0.261	-0.413	-0.752	-0.006

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Interactive mode: IFIE and PIEDA for fragment #1(A:11:THR)