FMO DATABASE

FMODB ID: LQMZ9

Calculation Name: 4DOT-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4DOT

Chain ID: A

ChEMBL ID:

UniProt ID: P53816

Base Structure: X-ray

Registration Date: 2025-07-11

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
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	190
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-816868.422504
FMO2-HF: Nuclear repulsion	776198.171147
FMO2-HF: Total energy	-40670.251357
FMO2-MP2: Total energy	-40790.500364

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:6:PRO)

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

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.
-1.808	0.505	0.004	-1.045	-1.272	0.001

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.031 / q_NPA : -0.030

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	7	GLU	-1	-0.899	-0.756	4.638	-0.910	-0.563	-0.001	-0.089	-0.258	0.000
4	A	8	PRO	0	-0.074	-0.127	3.591	-1.466	0.500	0.005	-0.956	-1.014	0.001
5	A	9	LYS	0	0.038	-0.015	5.826	-0.044	-0.044	0.000	0.000	0.000	0.000
6	A	9	LYS	1	0.918	1.085	5.910	0.548	0.548	0.000	0.000	0.000	0.000
7	A	10	PRO	0	0.012	-0.084	8.325	0.069	0.069	0.000	0.000	0.000	0.000
8	A	11	GLY	0	-0.030	-0.033	11.921	0.005	0.005	0.000	0.000	0.000	0.000
9	A	12	ASP	0	0.114	-0.001	9.702	0.049	0.049	0.000	0.000	0.000	0.000
10	A	12	ASP	-1	-0.876	-0.803	7.807	-0.378	-0.378	0.000	0.000	0.000	0.000
11	A	13	LEU	0	0.059	-0.099	11.244	0.006	0.006	0.000	0.000	0.000	0.000
12	A	13	LEU	0	-0.084	0.110	13.257	0.002	0.002	0.000	0.000	0.000	0.000
13	A	14	ILE	0	0.046	-0.103	10.375	0.005	0.005	0.000	0.000	0.000	0.000
14	A	14	ILE	0	-0.076	0.098	8.498	0.011	0.011	0.000	0.000	0.000	0.000
15	A	15	GLU	0	0.147	-0.102	10.785	-0.042	-0.042	0.000	0.000	0.000	0.000
16	A	15	GLU	-1	-0.911	-0.760	11.631	0.163	0.163	0.000	0.000	0.000	0.000
17	A	16	ILE	0	0.062	-0.089	11.342	0.106	0.106	0.000	0.000	0.000	0.000
18	A	16	ILE	0	-0.073	0.081	12.535	-0.005	-0.005	0.000	0.000	0.000	0.000
19	A	17	PHE	0	0.048	-0.082	13.308	-0.060	-0.060	0.000	0.000	0.000	0.000
20	A	17	PHE	0	-0.148	0.059	10.647	-0.012	-0.012	0.000	0.000	0.000	0.000
21	A	18	ARG	0	0.159	-0.073	15.106	0.015	0.015	0.000	0.000	0.000	0.000
22	A	18	ARG	1	0.806	1.049	17.383	-0.127	-0.127	0.000	0.000	0.000	0.000
23	A	19	PRO	0	0.004	-0.101	18.087	-0.010	-0.010	0.000	0.000	0.000	0.000
24	A	20	PHE	0	0.002	0.001	20.796	-0.006	-0.006	0.000	0.000	0.000	0.000
25	A	20	PHE	0	-0.109	0.081	24.233	-0.001	-0.001	0.000	0.000	0.000	0.000
26	A	21	TYR	0	0.075	-0.137	20.949	-0.012	-0.012	0.000	0.000	0.000	0.000
27	A	21	TYR	0	-0.077	0.103	21.324	0.000	0.000	0.000	0.000	0.000	0.000
28	A	22	ARG	0	0.178	-0.049	17.622	0.013	0.013	0.000	0.000	0.000	0.000
29	A	22	ARG	1	0.791	1.038	16.509	-0.113	-0.113	0.000	0.000	0.000	0.000
30	A	23	HIS	0	0.074	-0.084	16.878	-0.024	-0.024	0.000	0.000	0.000	0.000
31	A	23	HIS	0	-0.109	0.036	17.204	0.004	0.004	0.000	0.000	0.000	0.000
32	A	24	TRP	0	0.049	-0.108	15.592	0.034	0.034	0.000	0.000	0.000	0.000
33	A	24	TRP	0	-0.089	0.099	14.092	0.006	0.006	0.000	0.000	0.000	0.000
34	A	25	ALA	0	0.123	-0.088	14.837	-0.014	-0.014	0.000	0.000	0.000	0.000
35	A	25	ALA	0	-0.082	0.097	14.256	0.001	0.001	0.000	0.000	0.000	0.000
36	A	26	ILE	0	0.006	-0.081	14.178	0.017	0.017	0.000	0.000	0.000	0.000
37	A	26	ILE	0	-0.083	0.074	14.859	-0.001	-0.001	0.000	0.000	0.000	0.000
38	A	27	TYR	0	0.171	-0.078	10.898	0.027	0.027	0.000	0.000	0.000	0.000
39	A	27	TYR	0	-0.143	0.045	9.158	0.028	0.028	0.000	0.000	0.000	0.000
40	A	28	VAL	0	-0.077	-0.158	12.422	-0.020	-0.020	0.000	0.000	0.000	0.000
41	A	28	VAL	0	-0.051	0.127	15.916	0.005	0.005	0.000	0.000	0.000	0.000
42	A	29	GLY	0	0.061	-0.096	11.803	-0.002	-0.002	0.000	0.000	0.000	0.000
43	A	30	ASP	0	0.022	-0.018	12.283	0.020	0.020	0.000	0.000	0.000	0.000
44	A	30	ASP	-1	-0.997	-0.851	14.496	-0.180	-0.180	0.000	0.000	0.000	0.000
45	A	31	GLY	0	0.060	-0.093	10.572	0.037	0.037	0.000	0.000	0.000	0.000
46	A	32	TYR	0	0.024	0.010	11.596	0.061	0.061	0.000	0.000	0.000	0.000
47	A	32	TYR	0	-0.053	0.077	15.402	0.004	0.004	0.000	0.000	0.000	0.000
48	A	33	VAL	0	0.049	-0.080	13.451	-0.042	-0.042	0.000	0.000	0.000	0.000
49	A	33	VAL	0	-0.052	0.081	12.511	0.009	0.009	0.000	0.000	0.000	0.000
50	A	34	VAL	0	0.075	-0.086	14.973	0.004	0.004	0.000	0.000	0.000	0.000
51	A	34	VAL	0	-0.052	0.090	18.285	-0.001	-0.001	0.000	0.000	0.000	0.000
52	A	35	HIS	0	-0.020	-0.080	17.902	0.002	0.002	0.000	0.000	0.000	0.000
53	A	35	HIS	0	-0.075	0.050	17.934	0.014	0.014	0.000	0.000	0.000	0.000
54	A	36	LEU	0	0.082	-0.092	19.958	-0.007	-0.007	0.000	0.000	0.000	0.000
55	A	36	LEU	0	-0.036	0.110	23.270	0.001	0.001	0.000	0.000	0.000	0.000
56	A	37	ALA	0	0.104	-0.097	22.306	0.011	0.011	0.000	0.000	0.000	0.000
57	A	37	ALA	0	-0.066	0.105	22.583	0.000	0.000	0.000	0.000	0.000	0.000
58	A	38	PRO	0	0.001	-0.106	24.114	-0.005	-0.005	0.000	0.000	0.000	0.000
59	A	39	PRO	0	0.006	0.012	26.977	0.002	0.002	0.000	0.000	0.000	0.000
60	A	58	ALA	0	0.158	0.018	28.296	0.001	0.001	0.000	0.000	0.000	0.000
61	A	58	ALA	0	-0.082	0.083	27.325	0.001	0.001	0.000	0.000	0.000	0.000
62	A	59	ILE	0	0.004	-0.119	27.411	-0.003	-0.003	0.000	0.000	0.000	0.000
63	A	59	ILE	0	-0.081	0.074	27.159	0.000	0.000	0.000	0.000	0.000	0.000
64	A	60	VAL	0	0.118	-0.107	24.327	0.007	0.007	0.000	0.000	0.000	0.000
65	A	60	VAL	0	-0.077	0.137	23.165	0.000	0.000	0.000	0.000	0.000	0.000
66	A	61	LYS	0	0.017	-0.101	22.760	-0.006	-0.006	0.000	0.000	0.000	0.000
67	A	61	LYS	1	0.859	1.062	22.211	-0.024	-0.024	0.000	0.000	0.000	0.000
68	A	62	LYS	0	0.166	-0.077	19.457	0.004	0.004	0.000	0.000	0.000	0.000
69	A	62	LYS	1	0.766	1.011	18.090	0.069	0.069	0.000	0.000	0.000	0.000
70	A	63	GLU	0	0.003	-0.124	18.037	-0.006	-0.006	0.000	0.000	0.000	0.000
71	A	63	GLU	-1	-0.918	-0.809	17.961	0.039	0.039	0.000	0.000	0.000	0.000
72	A	64	LEU	0	0.113	-0.084	14.723	-0.013	-0.013	0.000	0.000	0.000	0.000
73	A	64	LEU	0	-0.081	0.112	14.001	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	65	LEU	0	0.137	-0.103	10.979	0.026	0.026	0.000	0.000	0.000	0.000
75	A	65	LEU	0	-0.086	0.098	8.151	-0.013	-0.013	0.000	0.000	0.000	0.000
76	A	66	TYR	0	0.042	-0.084	11.645	0.071	0.071	0.000	0.000	0.000	0.000
77	A	66	TYR	0	-0.115	0.069	11.292	-0.004	-0.004	0.000	0.000	0.000	0.000
78	A	67	ASP	0	0.101	-0.092	12.518	0.034	0.034	0.000	0.000	0.000	0.000
79	A	67	ASP	-1	-0.949	-0.855	17.100	0.033	0.033	0.000	0.000	0.000	0.000
80	A	68	VAL	0	0.030	-0.085	15.374	0.007	0.007	0.000	0.000	0.000	0.000
81	A	68	VAL	0	-0.119	0.061	14.656	0.001	0.001	0.000	0.000	0.000	0.000
82	A	69	ALA	0	0.055	-0.121	11.859	-0.025	-0.025	0.000	0.000	0.000	0.000
83	A	69	ALA	0	-0.066	0.097	11.266	0.023	0.023	0.000	0.000	0.000	0.000
84	A	70	GLY	0	0.019	-0.067	13.319	-0.010	-0.010	0.000	0.000	0.000	0.000
85	A	71	SER	0	0.006	0.018	13.264	0.047	0.047	0.000	0.000	0.000	0.000
86	A	71	SER	0	-0.058	0.048	16.090	-0.017	-0.017	0.000	0.000	0.000	0.000
87	A	72	ASP	0	0.022	-0.125	14.101	0.006	0.006	0.000	0.000	0.000	0.000
88	A	72	ASP	-1	-0.950	-0.832	14.708	0.177	0.177	0.000	0.000	0.000	0.000
89	A	73	LYS	0	0.145	-0.062	10.499	0.079	0.079	0.000	0.000	0.000	0.000
90	A	73	LYS	1	0.847	1.026	10.943	-0.275	-0.275	0.000	0.000	0.000	0.000
91	A	74	TYR	0	0.020	-0.095	9.267	-0.135	-0.135	0.000	0.000	0.000	0.000
92	A	74	TYR	0	-0.049	0.089	5.977	0.039	0.039	0.000	0.000	0.000	0.000
93	A	75	GLN	0	0.054	-0.098	6.508	0.346	0.346	0.000	0.000	0.000	0.000
94	A	75	GLN	0	-0.113	0.070	7.337	0.001	0.001	0.000	0.000	0.000	0.000
95	A	76	VAL	0	0.121	-0.075	6.193	-0.045	-0.045	0.000	0.000	0.000	0.000
96	A	76	VAL	0	-0.050	0.103	5.943	-0.017	-0.017	0.000	0.000	0.000	0.000
97	A	77	ASN	0	0.013	-0.088	7.855	0.011	0.011	0.000	0.000	0.000	0.000
98	A	77	ASN	0	-0.130	0.023	11.243	-0.025	-0.025	0.000	0.000	0.000	0.000
99	A	78	ASN	0	0.166	-0.048	11.131	0.005	0.005	0.000	0.000	0.000	0.000
100	A	78	ASN	0	-0.159	0.074	10.673	0.021	0.021	0.000	0.000	0.000	0.000
101	A	79	LYS	0	0.160	-0.069	13.145	-0.013	-0.013	0.000	0.000	0.000	0.000
102	A	79	LYS	1	0.768	0.992	15.516	-0.069	-0.069	0.000	0.000	0.000	0.000
103	A	80	HIS	0	0.041	-0.071	15.544	-0.002	-0.002	0.000	0.000	0.000	0.000
104	A	80	HIS	0	-0.094	0.070	19.209	-0.001	-0.001	0.000	0.000	0.000	0.000
105	A	81	ASP	0	0.217	-0.083	16.267	0.001	0.001	0.000	0.000	0.000	0.000
106	A	81	ASP	-1	-0.831	-0.755	14.670	-0.064	-0.064	0.000	0.000	0.000	0.000
107	A	82	ASP	0	0.002	-0.067	17.642	-0.007	-0.007	0.000	0.000	0.000	0.000
108	A	82	ASP	-1	-0.942	-0.867	18.233	0.007	0.007	0.000	0.000	0.000	0.000
109	A	83	LYS	0	-0.054	-0.131	19.346	-0.002	-0.002	0.000	0.000	0.000	0.000
110	A	83	LYS	1	0.878	1.054	22.102	-0.001	-0.001	0.000	0.000	0.000	0.000
111	A	84	TYR	0	0.039	-0.097	21.166	0.000	0.000	0.000	0.000	0.000	0.000
112	A	84	TYR	0	-0.075	0.082	21.441	0.002	0.002	0.000	0.000	0.000	0.000
113	A	85	SER	0	0.053	-0.096	20.327	-0.003	-0.003	0.000	0.000	0.000	0.000
114	A	85	SER	0	-0.003	0.086	22.151	0.000	0.000	0.000	0.000	0.000	0.000
115	A	86	PRO	0	-0.063	-0.083	16.339	0.004	0.004	0.000	0.000	0.000	0.000
116	A	87	LEU	0	0.037	-0.014	19.048	-0.001	-0.001	0.000	0.000	0.000	0.000
117	A	87	LEU	0	-0.055	0.102	20.710	0.000	0.000	0.000	0.000	0.000	0.000
118	A	88	PRO	0	-0.021	-0.129	18.960	-0.009	-0.009	0.000	0.000	0.000	0.000
119	A	89	CYS	0	0.152	0.012	16.085	0.010	0.010	0.000	0.000	0.000	0.000
120	A	89	CYS	0	-0.108	0.105	13.869	0.003	0.003	0.000	0.000	0.000	0.000
121	A	90	SER	0	0.079	-0.030	17.437	-0.005	-0.005	0.000	0.000	0.000	0.000
122	A	90	SER	0	-0.044	0.025	20.400	0.002	0.002	0.000	0.000	0.000	0.000
123	A	91	LYS	0	0.085	-0.051	19.977	0.001	0.001	0.000	0.000	0.000	0.000
124	A	91	LYS	1	0.881	1.039	22.157	0.043	0.043	0.000	0.000	0.000	0.000
125	A	92	ILE	0	0.083	-0.056	18.140	0.010	0.010	0.000	0.000	0.000	0.000
126	A	92	ILE	0	-0.103	0.084	16.482	-0.003	-0.003	0.000	0.000	0.000	0.000
127	A	93	ILE	0	0.056	-0.091	18.182	0.012	0.012	0.000	0.000	0.000	0.000
128	A	93	ILE	0	-0.048	0.105	14.918	-0.001	-0.001	0.000	0.000	0.000	0.000
129	A	94	GLN	0	0.170	-0.070	18.820	0.005	0.005	0.000	0.000	0.000	0.000
130	A	94	GLN	0	-0.124	0.089	23.087	-0.001	-0.001	0.000	0.000	0.000	0.000
131	A	95	ARG	0	0.092	-0.091	22.527	0.005	0.005	0.000	0.000	0.000	0.000
132	A	95	ARG	1	0.833	1.075	22.549	0.020	0.020	0.000	0.000	0.000	0.000
133	A	96	ALA	0	0.068	-0.112	19.786	0.009	0.009	0.000	0.000	0.000	0.000
134	A	96	ALA	0	-0.067	0.080	19.423	-0.001	-0.001	0.000	0.000	0.000	0.000
135	A	97	GLU	0	0.081	-0.097	21.336	0.010	0.010	0.000	0.000	0.000	0.000
136	A	97	GLU	-1	-0.918	-0.810	19.346	-0.078	-0.078	0.000	0.000	0.000	0.000
137	A	98	GLU	0	0.017	-0.113	22.473	0.003	0.003	0.000	0.000	0.000	0.000
138	A	98	GLU	-1	-1.002	-0.890	25.729	-0.030	-0.030	0.000	0.000	0.000	0.000
139	A	99	LEU	0	0.067	-0.111	25.004	0.002	0.002	0.000	0.000	0.000	0.000
140	A	99	LEU	0	-0.104	0.086	23.932	0.001	0.001	0.000	0.000	0.000	0.000
141	A	100	VAL	0	0.053	-0.091	24.275	0.007	0.007	0.000	0.000	0.000	0.000
142	A	100	VAL	0	-0.095	0.109	22.318	0.000	0.000	0.000	0.000	0.000	0.000
143	A	101	GLY	0	-0.075	-0.140	25.208	-0.002	-0.002	0.000	0.000	0.000	0.000
144	A	102	GLN	0	0.059	-0.018	28.191	0.003	0.003	0.000	0.000	0.000	0.000
145	A	102	GLN	0	-0.094	0.097	28.746	0.001	0.001	0.000	0.000	0.000	0.000
146	A	103	GLU	0	0.091	-0.111	28.618	0.002	0.002	0.000	0.000	0.000	0.000
147	A	103	GLU	-1	-1.013	-0.846	31.786	0.008	0.008	0.000	0.000	0.000	0.000
148	A	104	VAL	0	-0.007	-0.112	28.977	-0.003	-0.003	0.000	0.000	0.000	0.000
149	A	104	VAL	0	-0.076	0.104	27.718	0.000	0.000	0.000	0.000	0.000	0.000
150	A	105	LEU	0	0.106	-0.099	30.415	0.002	0.002	0.000	0.000	0.000	0.000
151	A	105	LEU	0	-0.080	0.088	34.086	0.000	0.000	0.000	0.000	0.000	0.000
152	A	106	TYR	0	0.057	-0.073	30.967	0.000	0.000	0.000	0.000	0.000	0.000
153	A	106	TYR	0	-0.057	0.084	26.607	0.001	0.001	0.000	0.000	0.000	0.000
154	A	107	LYS	0	0.118	-0.061	30.144	0.000	0.000	0.000	0.000	0.000	0.000
155	A	107	LYS	1	0.882	1.042	30.026	-0.030	-0.030	0.000	0.000	0.000	0.000
156	A	108	LEU	0	0.021	-0.112	26.327	-0.002	-0.002	0.000	0.000	0.000	0.000
157	A	108	LEU	0	0.002	0.153	24.289	0.001	0.001	0.000	0.000	0.000	0.000
158	A	109	THR	0	-0.014	-0.076	25.684	0.002	0.002	0.000	0.000	0.000	0.000
159	A	109	THR	0	-0.019	0.059	26.394	-0.001	-0.001	0.000	0.000	0.000	0.000
160	A	110	SER	0	0.104	-0.079	21.587	-0.003	-0.003	0.000	0.000	0.000	0.000
161	A	110	SER	0	-0.028	0.070	20.687	0.000	0.000	0.000	0.000	0.000	0.000
162	A	111	GLU	0	0.024	-0.089	21.466	0.004	0.004	0.000	0.000	0.000	0.000
163	A	111	GLU	-1	-0.889	-0.833	24.590	0.046	0.046	0.000	0.000	0.000	0.000
164	A	112	ASN	0	0.067	-0.057	23.812	-0.003	-0.003	0.000	0.000	0.000	0.000
165	A	112	ASN	0	-0.155	0.028	25.932	-0.002	-0.002	0.000	0.000	0.000	0.000
166	A	113	CYS	0	0.166	-0.061	21.351	-0.009	-0.009	0.000	0.000	0.000	0.000
167	A	113	CYS	0	-0.139	0.084	20.383	0.001	0.001	0.000	0.000	0.000	0.000
168	A	114	GLU	0	0.109	-0.123	19.190	-0.004	-0.004	0.000	0.000	0.000	0.000
169	A	114	GLU	-1	-0.967	-0.829	18.322	0.061	0.061	0.000	0.000	0.000	0.000
170	A	115	HIS	0	0.037	-0.102	20.211	-0.005	-0.005	0.000	0.000	0.000	0.000
171	A	115	HIS	0	-0.096	0.084	24.639	0.002	0.002	0.000	0.000	0.000	0.000
172	A	116	PHE	0	0.115	-0.062	22.993	-0.007	-0.007	0.000	0.000	0.000	0.000
173	A	116	PHE	0	-0.071	0.077	21.101	-0.001	-0.001	0.000	0.000	0.000	0.000
174	A	117	VAL	0	0.064	-0.089	18.026	-0.011	-0.011	0.000	0.000	0.000	0.000
175	A	117	VAL	0	-0.071	0.092	16.722	0.001	0.001	0.000	0.000	0.000	0.000
176	A	118	ASN	0	0.088	-0.087	19.153	-0.013	-0.013	0.000	0.000	0.000	0.000
177	A	118	ASN	0	-0.082	0.051	18.767	0.000	0.000	0.000	0.000	0.000	0.000
178	A	119	GLU	0	0.096	-0.092	20.370	-0.007	-0.007	0.000	0.000	0.000	0.000
179	A	119	GLU	-1	-0.994	-0.838	24.205	0.002	0.002	0.000	0.000	0.000	0.000
180	A	120	LEU	0	0.012	-0.120	20.483	-0.004	-0.004	0.000	0.000	0.000	0.000
181	A	120	LEU	0	-0.083	0.099	19.722	-0.002	-0.002	0.000	0.000	0.000	0.000
182	A	121	ARG	0	0.103	-0.087	17.685	-0.010	-0.010	0.000	0.000	0.000	0.000
183	A	121	ARG	1	0.703	0.974	13.488	0.084	0.084	0.000	0.000	0.000	0.000
184	A	122	TYR	0	0.001	-0.134	18.793	-0.010	-0.010	0.000	0.000	0.000	0.000
185	A	122	TYR	0	-0.101	0.059	16.648	0.005	0.005	0.000	0.000	0.000	0.000
186	A	123	GLY	0	0.011	-0.076	21.579	0.000	0.000	0.000	0.000	0.000	0.000
187	A	124	VAL	0	0.059	-0.008	24.834	0.003	0.003	0.000	0.000	0.000	0.000
188	A	124	VAL	0	-0.107	0.100	27.511	0.000	0.000	0.000	0.000	0.000	0.000
189	A	125	ALA	0	-0.085	-0.157	25.859	0.000	0.000	0.000	0.000	0.000	0.000
190	A	125	ALA	0	0.061	0.045	29.381	0.000	0.000	0.000	0.000	0.000	0.000

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