FMO DATABASE

FMODB ID: GY481

Calculation Name: 2ES9-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

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

Total energy (hartree)

FMO2-HF: Electronic energy	-737645.55816
FMO2-HF: Nuclear repulsion	698909.53769
FMO2-HF: Total energy	-38736.02047
FMO2-MP2: Total energy	-38848.83451

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: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.
-5.972	-8.718	11.876	-3.229	-5.895	-0.05

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 : 0.125 / q_NPA : 0.076

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	-0.051	0.122	4.549	0.002	0.169	-0.001	-0.074	-0.092	0.000
5	A	13	ILE	0	0.054	-0.098	3.711	0.769	1.944	-0.003	-0.587	-0.585	0.002
6	A	13	ILE	0	-0.050	0.099	4.499	-0.172	-0.089	-0.001	-0.016	-0.065	0.000
7	A	14	GLU	0	0.069	-0.127	3.338	0.995	1.077	0.017	0.148	-0.246	0.000
8	A	14	GLU	-1	-0.916	-0.801	1.875	-7.792	-11.764	11.541	-4.420	-3.148	-0.045
9	A	15	LYS	0	0.105	-0.097	4.141	0.340	0.650	-0.001	-0.129	-0.178	0.000
10	A	15	LYS	1	0.758	1.030	4.835	-2.338	-2.293	-0.001	-0.016	-0.028	0.000
11	A	16	ALA	0	0.079	-0.118	6.038	0.149	0.149	0.000	0.000	0.000	0.000
12	A	16	ALA	0	-0.065	0.096	8.048	-0.059	-0.059	0.000	0.000	0.000	0.000
13	A	17	LEU	0	0.056	-0.118	7.752	0.184	0.184	0.000	0.000	0.000	0.000
14	A	17	LEU	0	-0.088	0.092	7.231	-0.001	-0.001	0.000	0.000	0.000	0.000
15	A	18	ASP	0	0.103	-0.102	8.032	-0.099	-0.099	0.000	0.000	0.000	0.000
16	A	18	ASP	-1	-0.850	-0.773	7.182	1.728	1.728	0.000	0.000	0.000	0.000
17	A	19	PHE	0	-0.034	-0.096	9.700	0.007	0.007	0.000	0.000	0.000	0.000
18	A	19	PHE	0	-0.055	0.072	10.691	0.025	0.025	0.000	0.000	0.000	0.000
19	A	20	ILE	0	0.026	-0.109	12.020	0.016	0.016	0.000	0.000	0.000	0.000
20	A	20	ILE	0	-0.087	0.102	12.646	-0.017	-0.017	0.000	0.000	0.000	0.000
21	A	21	GLY	0	0.063	-0.086	12.607	-0.014	-0.014	0.000	0.000	0.000	0.000
22	A	22	GLY	0	-0.034	-0.009	14.128	0.011	0.011	0.000	0.000	0.000	0.000
23	A	23	MET	0	0.062	0.018	15.910	0.017	0.017	0.000	0.000	0.000	0.000
24	A	23	MET	0	-0.172	0.066	16.418	-0.016	-0.016	0.000	0.000	0.000	0.000
25	A	24	ASN	0	0.149	-0.028	18.541	0.009	0.009	0.000	0.000	0.000	0.000
26	A	24	ASN	0	-0.140	0.033	23.148	-0.002	-0.002	0.000	0.000	0.000	0.000
27	A	25	THR	0	-0.004	-0.162	19.009	-0.028	-0.028	0.000	0.000	0.000	0.000
28	A	25	THR	0	-0.010	0.118	16.916	-0.002	-0.002	0.000	0.000	0.000	0.000
29	A	26	SER	0	0.107	-0.056	20.144	-0.029	-0.029	0.000	0.000	0.000	0.000
30	A	26	SER	0	-0.014	0.095	22.539	0.005	0.005	0.000	0.000	0.000	0.000
31	A	27	ALA	0	0.077	-0.100	23.647	-0.010	-0.010	0.000	0.000	0.000	0.000
32	A	27	ALA	0	-0.103	0.111	24.907	0.002	0.002	0.000	0.000	0.000	0.000
33	A	28	SER	0	-0.024	-0.096	24.726	-0.011	-0.011	0.000	0.000	0.000	0.000
34	A	28	SER	0	-0.011	0.067	28.335	0.002	0.002	0.000	0.000	0.000	0.000
35	A	29	VAL	0	0.062	-0.102	26.755	-0.017	-0.017	0.000	0.000	0.000	0.000
36	A	29	VAL	0	-0.113	0.101	28.142	-0.001	-0.001	0.000	0.000	0.000	0.000
37	A	30	PRO	0	0.035	-0.086	22.264	0.015	0.015	0.000	0.000	0.000	0.000
38	A	31	HIS	0	0.078	0.009	24.326	-0.011	-0.011	0.000	0.000	0.000	0.000
39	A	31	HIS	0	-0.048	0.124	25.078	0.011	0.011	0.000	0.000	0.000	0.000
40	A	32	SER	0	0.102	-0.071	24.661	-0.009	-0.009	0.000	0.000	0.000	0.000
41	A	32	SER	0	-0.011	0.065	27.859	0.003	0.003	0.000	0.000	0.000	0.000
42	A	33	MET	0	0.025	-0.093	24.033	-0.018	-0.018	0.000	0.000	0.000	0.000
43	A	33	MET	0	-0.062	0.109	23.466	0.004	0.004	0.000	0.000	0.000	0.000
44	A	34	ASP	0	0.108	-0.070	20.496	0.003	0.003	0.000	0.000	0.000	0.000
45	A	34	ASP	-1	-0.850	-0.808	20.840	0.053	0.053	0.000	0.000	0.000	0.000
46	A	35	GLU	0	0.162	-0.060	20.019	-0.017	-0.017	0.000	0.000	0.000	0.000
47	A	35	GLU	-1	-0.918	-0.813	22.957	-0.097	-0.097	0.000	0.000	0.000	0.000
48	A	36	SER	0	-0.021	-0.128	21.024	-0.035	-0.035	0.000	0.000	0.000	0.000
49	A	36	SER	0	-0.065	0.051	23.020	-0.001	-0.001	0.000	0.000	0.000	0.000
50	A	37	THR	0	0.008	-0.094	18.689	-0.028	-0.028	0.000	0.000	0.000	0.000
51	A	37	THR	0	-0.044	0.061	16.568	0.015	0.015	0.000	0.000	0.000	0.000
52	A	38	ALA	0	0.121	-0.073	16.026	-0.006	-0.006	0.000	0.000	0.000	0.000
53	A	38	ALA	0	-0.050	0.101	17.201	-0.003	-0.003	0.000	0.000	0.000	0.000
54	A	39	LYS	0	0.029	-0.109	16.244	-0.069	-0.069	0.000	0.000	0.000	0.000
55	A	39	LYS	1	0.703	0.969	20.331	0.126	0.126	0.000	0.000	0.000	0.000
56	A	40	GLY	0	-0.003	-0.104	17.546	-0.041	-0.041	0.000	0.000	0.000	0.000
57	A	41	ILE	0	0.114	0.039	13.336	-0.029	-0.029	0.000	0.000	0.000	0.000
58	A	41	ILE	0	-0.099	0.087	11.227	0.007	0.007	0.000	0.000	0.000	0.000
59	A	42	LEU	0	0.062	-0.096	12.714	-0.112	-0.112	0.000	0.000	0.000	0.000
60	A	42	LEU	0	-0.109	0.084	12.983	0.002	0.002	0.000	0.000	0.000	0.000
61	A	43	LYS	0	0.145	-0.058	14.035	-0.109	-0.109	0.000	0.000	0.000	0.000
62	A	43	LYS	1	0.692	0.946	17.806	0.267	0.267	0.000	0.000	0.000	0.000
63	A	44	TYR	0	0.073	-0.084	14.562	-0.051	-0.051	0.000	0.000	0.000	0.000
64	A	44	TYR	0	-0.054	0.088	12.338	0.027	0.027	0.000	0.000	0.000	0.000
65	A	45	LEU	0	0.051	-0.109	10.419	0.077	0.077	0.000	0.000	0.000	0.000
66	A	45	LEU	0	-0.069	0.113	7.834	0.006	0.006	0.000	0.000	0.000	0.000
67	A	46	HIS	0	0.127	-0.066	11.378	-0.143	-0.143	0.000	0.000	0.000	0.000
68	A	46	HIS	0	-0.086	0.079	14.438	-0.045	-0.045	0.000	0.000	0.000	0.000
69	A	47	ASP	0	0.053	-0.106	13.816	-0.026	-0.026	0.000	0.000	0.000	0.000
70	A	47	ASP	-1	-0.918	-0.822	15.874	-0.275	-0.275	0.000	0.000	0.000	0.000
71	A	48	LEU	0	-0.026	-0.126	11.917	0.076	0.076	0.000	0.000	0.000	0.000
72	A	48	LEU	0	-0.088	0.101	10.352	0.005	0.005	0.000	0.000	0.000	0.000
73	A	49	GLY	0	0.018	-0.091	12.074	-0.046	-0.046	0.000	0.000	0.000	0.000
74	A	50	VAL	0	-0.021	-0.020	8.355	0.021	0.021	0.000	0.000	0.000	0.000
75	A	50	VAL	0	-0.077	0.100	6.198	-0.106	-0.106	0.000	0.000	0.000	0.000
76	A	51	PRO	0	0.040	-0.099	9.171	-0.119	-0.119	0.000	0.000	0.000	0.000
77	A	52	VAL	0	0.054	-0.016	10.208	-0.274	-0.274	0.000	0.000	0.000	0.000
78	A	52	VAL	0	-0.083	0.107	8.680	0.009	0.009	0.000	0.000	0.000	0.000
79	A	53	SER	0	0.046	-0.093	11.014	0.209	0.209	0.000	0.000	0.000	0.000
80	A	53	SER	0	-0.046	0.051	13.244	-0.062	-0.062	0.000	0.000	0.000	0.000
81	A	54	PRO	0	0.004	-0.120	13.894	-0.016	-0.016	0.000	0.000	0.000	0.000
82	A	55	GLU	0	0.088	-0.001	16.322	0.045	0.045	0.000	0.000	0.000	0.000
83	A	55	GLU	-1	-0.846	-0.754	14.914	-0.740	-0.740	0.000	0.000	0.000	0.000
84	A	56	VAL	0	0.053	-0.110	11.432	0.105	0.105	0.000	0.000	0.000	0.000
85	A	56	VAL	0	-0.068	0.110	9.316	-0.040	-0.040	0.000	0.000	0.000	0.000
86	A	57	VAL	0	0.053	-0.096	12.240	-0.011	-0.011	0.000	0.000	0.000	0.000
87	A	57	VAL	0	-0.100	0.075	13.270	0.015	0.015	0.000	0.000	0.000	0.000
88	A	58	VAL	0	0.094	-0.086	13.912	0.071	0.071	0.000	0.000	0.000	0.000
89	A	58	VAL	0	-0.116	0.077	17.544	0.007	0.007	0.000	0.000	0.000	0.000
90	A	59	ALA	0	0.177	-0.077	14.341	0.094	0.094	0.000	0.000	0.000	0.000
91	A	59	ALA	0	-0.098	0.109	13.433	-0.021	-0.021	0.000	0.000	0.000	0.000
92	A	60	ARG	0	0.057	-0.109	11.940	0.059	0.059	0.000	0.000	0.000	0.000
93	A	60	ARG	1	0.658	0.966	7.409	-0.155	-0.155	0.000	0.000	0.000	0.000
94	A	61	GLY	0	0.010	-0.119	12.952	0.093	0.093	0.000	0.000	0.000	0.000
95	A	62	GLU	0	0.063	-0.015	16.425	0.063	0.063	0.000	0.000	0.000	0.000
96	A	62	GLU	-1	-1.002	-0.868	17.671	-0.287	-0.287	0.000	0.000	0.000	0.000
97	A	63	GLN	0	0.061	-0.099	14.473	0.045	0.045	0.000	0.000	0.000	0.000
98	A	63	GLN	0	-0.126	0.077	11.093	-0.110	-0.110	0.000	0.000	0.000	0.000
99	A	64	GLU	0	-0.002	-0.145	15.429	0.035	0.035	0.000	0.000	0.000	0.000
100	A	64	GLU	-1	-0.875	-0.766	12.063	0.132	0.132	0.000	0.000	0.000	0.000
101	A	65	GLY	0	-0.012	-0.099	16.368	0.038	0.038	0.000	0.000	0.000	0.000
102	A	66	TRP	0	0.058	-0.017	18.563	0.033	0.033	0.000	0.000	0.000	0.000
103	A	66	TRP	0	-0.089	0.081	13.020	-0.037	-0.037	0.000	0.000	0.000	0.000
104	A	67	ASN	0	0.176	-0.035	19.738	-0.016	-0.016	0.000	0.000	0.000	0.000
105	A	67	ASN	0	-0.189	0.039	23.239	-0.015	-0.015	0.000	0.000	0.000	0.000
106	A	68	PRO	0	0.024	-0.090	21.969	-0.019	-0.019	0.000	0.000	0.000	0.000
107	A	69	GLU	0	0.115	0.016	23.311	-0.028	-0.028	0.000	0.000	0.000	0.000
108	A	69	GLU	-1	-0.900	-0.793	26.459	-0.113	-0.113	0.000	0.000	0.000	0.000
109	A	70	PHE	0	0.096	-0.116	21.896	-0.015	-0.015	0.000	0.000	0.000	0.000
110	A	70	PHE	0	-0.111	0.114	17.331	0.002	0.002	0.000	0.000	0.000	0.000
111	A	71	THR	0	0.014	-0.101	18.910	-0.012	-0.012	0.000	0.000	0.000	0.000
112	A	71	THR	0	-0.023	0.092	17.721	-0.001	-0.001	0.000	0.000	0.000	0.000
113	A	72	LYS	0	0.151	-0.071	19.589	-0.048	-0.048	0.000	0.000	0.000	0.000
114	A	72	LYS	1	0.672	0.979	23.828	0.136	0.136	0.000	0.000	0.000	0.000
115	A	73	LYS	0	-0.030	-0.111	22.292	-0.027	-0.027	0.000	0.000	0.000	0.000
116	A	73	LYS	1	0.813	1.023	22.668	0.109	0.109	0.000	0.000	0.000	0.000
117	A	74	VAL	0	0.104	-0.113	17.825	-0.002	-0.002	0.000	0.000	0.000	0.000
118	A	74	VAL	0	-0.060	0.113	15.778	-0.001	-0.001	0.000	0.000	0.000	0.000
119	A	75	ALA	0	0.112	-0.106	17.928	-0.048	-0.048	0.000	0.000	0.000	0.000
120	A	75	ALA	0	-0.050	0.132	18.671	0.001	0.001	0.000	0.000	0.000	0.000
121	A	76	GLY	0	-0.005	-0.097	18.958	-0.027	-0.027	0.000	0.000	0.000	0.000
122	A	77	TRP	0	-0.019	-0.032	20.160	0.006	0.006	0.000	0.000	0.000	0.000
123	A	77	TRP	0	-0.048	0.092	18.900	0.011	0.011	0.000	0.000	0.000	0.000
124	A	78	ALA	0	0.136	-0.079	16.439	0.020	0.020	0.000	0.000	0.000	0.000
125	A	78	ALA	0	-0.047	0.125	15.658	-0.009	-0.009	0.000	0.000	0.000	0.000
126	A	79	GLU	0	0.092	-0.111	17.362	-0.056	-0.056	0.000	0.000	0.000	0.000
127	A	79	GLU	-1	-1.044	-0.865	20.793	-0.277	-0.277	0.000	0.000	0.000	0.000
128	A	80	LYS	0	0.121	-0.044	20.035	-0.012	-0.012	0.000	0.000	0.000	0.000
129	A	80	LYS	1	0.839	1.029	22.346	0.200	0.200	0.000	0.000	0.000	0.000
130	A	81	VAL	0	0.053	-0.090	17.908	0.032	0.032	0.000	0.000	0.000	0.000
131	A	81	VAL	0	-0.113	0.097	16.065	0.008	0.008	0.000	0.000	0.000	0.000
132	A	82	ALA	0	0.162	-0.076	17.446	0.008	0.008	0.000	0.000	0.000	0.000
133	A	82	ALA	0	-0.064	0.113	16.672	-0.010	-0.010	0.000	0.000	0.000	0.000
134	A	83	SER	0	-0.092	-0.127	18.142	-0.013	-0.013	0.000	0.000	0.000	0.000
135	A	83	SER	0	-0.100	0.043	22.647	0.021	0.021	0.000	0.000	0.000	0.000
136	A	84	GLY	0	0.004	-0.092	20.778	0.023	0.023	0.000	0.000	0.000	0.000
137	A	85	ASN	0	0.043	0.017	22.080	0.023	0.023	0.000	0.000	0.000	0.000
138	A	85	ASN	0	-0.119	0.043	24.835	0.021	0.021	0.000	0.000	0.000	0.000
139	A	86	ARG	0	0.117	-0.056	23.237	-0.017	-0.017	0.000	0.000	0.000	0.000
140	A	86	ARG	1	0.859	1.038	25.768	0.137	0.137	0.000	0.000	0.000	0.000
141	A	87	ILE	0	0.055	-0.125	23.325	0.006	0.006	0.000	0.000	0.000	0.000
142	A	87	ILE	0	-0.035	0.138	21.195	0.002	0.002	0.000	0.000	0.000	0.000
143	A	88	LEU	0	0.106	-0.112	24.675	0.003	0.003	0.000	0.000	0.000	0.000
144	A	88	LEU	0	-0.095	0.110	27.812	0.000	0.000	0.000	0.000	0.000	0.000
145	A	89	ILE	0	0.028	-0.134	23.350	-0.006	-0.006	0.000	0.000	0.000	0.000
146	A	89	ILE	0	-0.045	0.149	21.341	0.000	0.000	0.000	0.000	0.000	0.000
147	A	90	LYS	0	0.099	-0.067	24.566	0.006	0.006	0.000	0.000	0.000	0.000
148	A	90	LYS	1	0.821	1.027	27.346	0.009	0.009	0.000	0.000	0.000	0.000
149	A	91	ASN	0	0.043	-0.081	25.582	0.001	0.001	0.000	0.000	0.000	0.000
150	A	91	ASN	0	-0.135	0.032	26.281	-0.006	-0.006	0.000	0.000	0.000	0.000
151	A	92	PRO	0	0.061	-0.107	22.263	0.007	0.007	0.000	0.000	0.000	0.000
152	A	93	GLU	0	0.073	0.010	21.332	0.003	0.003	0.000	0.000	0.000	0.000
153	A	93	GLU	-1	-0.847	-0.778	24.765	0.023	0.023	0.000	0.000	0.000	0.000
154	A	94	TYR	0	0.056	-0.090	21.828	0.028	0.028	0.000	0.000	0.000	0.000
155	A	94	TYR	0	-0.073	0.077	21.715	-0.009	-0.009	0.000	0.000	0.000	0.000
156	A	95	PHE	0	0.067	-0.074	17.739	0.045	0.045	0.000	0.000	0.000	0.000
157	A	95	PHE	0	-0.081	0.102	13.380	-0.008	-0.008	0.000	0.000	0.000	0.000
158	A	96	SER	0	0.080	-0.059	18.428	-0.022	-0.022	0.000	0.000	0.000	0.000
159	A	96	SER	0	-0.048	0.052	18.164	0.017	0.017	0.000	0.000	0.000	0.000
160	A	97	THR	0	0.082	-0.081	16.747	0.019	0.019	0.000	0.000	0.000	0.000
161	A	97	THR	0	-0.010	0.086	17.995	-0.003	-0.003	0.000	0.000	0.000	0.000
162	A	98	TYR	0	0.080	-0.048	15.743	0.005	0.005	0.000	0.000	0.000	0.000
163	A	98	TYR	0	-0.078	0.077	14.140	0.022	0.022	0.000	0.000	0.000	0.000
164	A	99	MET	0	0.089	-0.093	12.672	0.138	0.138	0.000	0.000	0.000	0.000
165	A	99	MET	0	-0.110	0.085	13.260	-0.018	-0.018	0.000	0.000	0.000	0.000
166	A	100	GLN	0	0.120	-0.076	11.720	0.025	0.025	0.000	0.000	0.000	0.000
167	A	100	GLN	0	-0.151	0.053	14.611	-0.028	-0.028	0.000	0.000	0.000	0.000
168	A	101	GLU	0	0.053	-0.114	12.072	-0.060	-0.060	0.000	0.000	0.000	0.000
169	A	101	GLU	-1	-0.908	-0.789	14.116	0.204	0.204	0.000	0.000	0.000	0.000
170	A	102	GLN	0	0.183	-0.039	10.087	-0.030	-0.030	0.000	0.000	0.000	0.000
171	A	102	GLN	0	-0.093	0.077	8.440	0.214	0.214	0.000	0.000	0.000	0.000
172	A	103	LEU	0	0.089	-0.089	7.411	0.406	0.406	0.000	0.000	0.000	0.000
173	A	103	LEU	0	-0.107	0.079	7.199	-0.057	-0.057	0.000	0.000	0.000	0.000
174	A	104	LYS	0	0.155	-0.078	7.572	-0.224	-0.224	0.000	0.000	0.000	0.000
175	A	104	LYS	1	0.721	0.982	11.647	-0.202	-0.202	0.000	0.000	0.000	0.000
176	A	105	GLU	0	0.049	-0.112	9.212	-0.233	-0.233	0.000	0.000	0.000	0.000
177	A	105	GLU	-1	-1.042	-0.862	8.785	1.148	1.148	0.000	0.000	0.000	0.000
178	A	106	LEU	0	0.054	-0.105	4.499	-0.221	-0.168	-0.001	-0.005	-0.046	0.000
179	A	106	LEU	0	-0.086	0.096	3.215	-0.279	0.086	0.076	-0.128	-0.313	0.001
180	A	107	VAL	0	0.123	-0.080	4.803	-0.395	-0.288	-0.002	-0.005	-0.100	0.000
181	A	107	VAL	0	-0.090	0.090	6.871	-0.073	-0.073	0.000	0.000	0.000	0.000
182	A	108	LEU	0	0.035	-0.100	6.899	-0.204	-0.204	0.000	0.000	0.000	0.000
183	A	108	LEU	0	-0.114	0.075	10.302	0.003	0.003	0.000	0.000	0.000	0.000
184	A	109	GLU	0	0.058	-0.094	7.627	-0.277	-0.277	0.000	0.000	0.000	0.000
185	A	109	GLU	-1	-1.020	-0.859	6.546	1.863	1.863	0.000	0.000	0.000	0.000
186	A	110	HIS	0	-0.151	-0.169	6.207	0.196	0.196	0.000	0.000	0.000	0.000
187	A	110	HIS	0	0.021	0.007	3.030	-0.277	-1.438	0.252	2.003	-1.094	-0.008

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