FMO DATABASE

FMODB ID: M94JZ

Calculation Name: 1YN5-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1YN5

Chain ID: A

ChEMBL ID:

UniProt ID: A0A0H3

Base Structure: X-ray

Registration Date: 2025-07-09

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	OptHSide
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	199
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-776011.248892
FMO2-HF: Nuclear repulsion	735523.455223
FMO2-HF: Total energy	-40487.793669
FMO2-MP2: Total energy	-40606.612193

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:42:ALA)

Summations of interaction energy for fragment #1(A:42:ALA)

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.
-8.196	-0.448	1.142	-4.585	-4.308	-0.011

Interaction energy analysis for fragmet #1(A:42:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.189 / q_NPA : 0.039

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	43	LYS	1	0.864	1.065	4.334	0.269	0.641	0.000	-0.200	-0.171	0.000
5	A	44	GLU	0	0.161	-0.110	3.766	-4.073	-1.038	-0.043	-1.700	-1.292	0.003
6	A	44	GLU	-1	-0.902	-0.795	4.999	1.635	1.635	0.000	0.000	0.000	0.000
7	A	45	MET	0	0.093	-0.086	5.619	-0.609	-0.609	0.000	0.000	0.000	0.000
8	A	45	MET	0	-0.136	0.119	8.912	-0.082	-0.082	0.000	0.000	0.000	0.000
9	A	46	GLN	0	0.080	-0.106	8.352	0.225	0.225	0.000	0.000	0.000	0.000
10	A	46	GLN	0	-0.088	0.096	8.822	-0.020	-0.020	0.000	0.000	0.000	0.000
11	A	47	ASN	0	0.098	-0.079	10.458	-0.096	-0.096	0.000	0.000	0.000	0.000
12	A	47	ASN	0	-0.124	0.062	14.951	-0.024	-0.024	0.000	0.000	0.000	0.000
13	A	48	VAL	0	0.121	-0.119	14.200	0.042	0.042	0.000	0.000	0.000	0.000
14	A	48	VAL	0	-0.125	0.105	12.546	-0.011	-0.011	0.000	0.000	0.000	0.000
15	A	49	PRO	0	0.022	-0.087	15.295	-0.012	-0.012	0.000	0.000	0.000	0.000
16	A	50	TYR	0	0.044	0.007	19.067	-0.015	-0.015	0.000	0.000	0.000	0.000
17	A	50	TYR	0	-0.116	0.037	19.014	-0.008	-0.008	0.000	0.000	0.000	0.000
18	A	51	THR	0	0.007	-0.094	21.130	0.012	0.012	0.000	0.000	0.000	0.000
19	A	51	THR	0	-0.033	0.059	24.391	0.001	0.001	0.000	0.000	0.000	0.000
20	A	52	ILE	0	0.169	-0.088	24.860	-0.012	-0.012	0.000	0.000	0.000	0.000
21	A	52	ILE	0	-0.113	0.106	24.064	-0.001	-0.001	0.000	0.000	0.000	0.000
22	A	53	ALA	0	0.177	-0.095	26.982	0.009	0.009	0.000	0.000	0.000	0.000
23	A	53	ALA	0	-0.121	0.093	30.111	0.001	0.001	0.000	0.000	0.000	0.000
24	A	54	VAL	0	0.066	-0.110	30.384	-0.007	-0.007	0.000	0.000	0.000	0.000
25	A	54	VAL	0	-0.107	0.102	30.619	-0.001	-0.001	0.000	0.000	0.000	0.000
26	A	55	ASP	0	0.052	-0.098	32.707	0.005	0.005	0.000	0.000	0.000	0.000
27	A	55	ASP	-1	-0.881	-0.782	36.437	-0.072	-0.072	0.000	0.000	0.000	0.000
28	A	56	GLY	0	-0.024	-0.138	34.484	0.005	0.005	0.000	0.000	0.000	0.000
29	A	57	ILE	0	0.091	0.004	34.740	0.004	0.004	0.000	0.000	0.000	0.000
30	A	57	ILE	0	-0.072	0.115	33.991	0.000	0.000	0.000	0.000	0.000	0.000
31	A	58	MET	0	0.059	-0.097	30.990	-0.009	-0.009	0.000	0.000	0.000	0.000
32	A	58	MET	0	-0.087	0.109	28.747	0.001	0.001	0.000	0.000	0.000	0.000
33	A	59	ALA	0	0.112	-0.113	28.447	0.005	0.005	0.000	0.000	0.000	0.000
34	A	59	ALA	0	-0.017	0.104	27.958	-0.002	-0.002	0.000	0.000	0.000	0.000
35	A	60	PHE	0	0.115	-0.016	29.966	0.002	0.002	0.000	0.000	0.000	0.000
36	A	60	PHE	0	-0.114	0.081	31.203	0.000	0.000	0.000	0.000	0.000	0.000
37	A	61	ASN	0	0.038	-0.052	28.783	0.002	0.002	0.000	0.000	0.000	0.000
38	A	61	ASN	0	-0.172	0.025	28.253	0.004	0.004	0.000	0.000	0.000	0.000
39	A	62	GLN	0	0.217	-0.259	24.892	-0.006	-0.006	0.000	0.000	0.000	0.000
40	A	62	GLN	0	-0.002	0.158	22.939	-0.003	-0.003	0.000	0.000	0.000	0.000
41	A	63	SER	0	-0.158	0.016	22.526	0.017	0.017	0.000	0.000	0.000	0.000
42	A	63	SER	0	-0.039	0.070	21.970	0.002	0.002	0.000	0.000	0.000	0.000
43	A	64	TYR	0	0.064	-0.120	18.267	-0.006	-0.006	0.000	0.000	0.000	0.000
44	A	64	TYR	0	-0.067	0.101	17.207	0.006	0.006	0.000	0.000	0.000	0.000
45	A	65	LEU	0	0.141	-0.077	15.993	0.007	0.007	0.000	0.000	0.000	0.000
46	A	65	LEU	0	-0.086	0.097	13.745	-0.010	-0.010	0.000	0.000	0.000	0.000
47	A	66	ASN	0	0.103	-0.071	12.341	0.017	0.017	0.000	0.000	0.000	0.000
48	A	66	ASN	0	-0.125	0.046	11.719	0.027	0.027	0.000	0.000	0.000	0.000
49	A	67	LEU	0	0.046	-0.185	9.356	-0.067	-0.067	0.000	0.000	0.000	0.000
50	A	67	LEU	0	-0.002	0.139	8.984	-0.002	-0.002	0.000	0.000	0.000	0.000
51	A	68	PRO	0	-0.040	-0.086	4.329	0.275	0.359	-0.001	-0.033	-0.050	0.000
52	A	69	LYS	0	0.145	0.055	5.027	-0.262	-0.138	-0.002	-0.012	-0.111	0.000
53	A	69	LYS	1	0.765	1.018	3.693	-1.546	-1.397	0.001	-0.030	-0.120	0.000
54	A	70	ASP	0	-0.025	-0.141	2.862	-2.479	-1.061	0.481	-0.924	-0.976	-0.009
55	A	70	ASP	-1	-0.914	-0.807	2.550	0.134	0.785	0.332	-0.516	-0.467	0.002
56	A	71	SER	0	0.078	-0.090	3.189	-1.394	-0.089	0.101	-0.696	-0.710	-0.006
57	A	71	SER	0	-0.046	0.076	2.560	-1.102	-0.477	0.275	-0.461	-0.440	-0.001
58	A	72	GLN	0	0.134	-0.057	4.654	0.354	0.339	-0.002	-0.013	0.029	0.000
59	A	72	GLN	0	-0.091	0.097	6.779	0.103	0.103	0.000	0.000	0.000	0.000
60	A	73	LEU	0	0.105	-0.094	8.255	-0.138	-0.138	0.000	0.000	0.000	0.000
61	A	73	LEU	0	-0.065	0.105	6.952	0.020	0.020	0.000	0.000	0.000	0.000
62	A	74	SER	0	0.145	-0.042	9.858	0.110	0.110	0.000	0.000	0.000	0.000
63	A	74	SER	0	-0.030	0.096	13.530	0.029	0.029	0.000	0.000	0.000	0.000
64	A	75	TYR	0	0.055	-0.094	13.500	-0.010	-0.010	0.000	0.000	0.000	0.000
65	A	75	TYR	0	-0.079	0.085	16.512	0.026	0.026	0.000	0.000	0.000	0.000
66	A	76	LEU	0	0.062	-0.092	16.401	0.037	0.037	0.000	0.000	0.000	0.000
67	A	76	LEU	0	-0.065	0.114	17.467	0.000	0.000	0.000	0.000	0.000	0.000
68	A	77	ASP	0	0.128	-0.124	14.218	0.069	0.069	0.000	0.000	0.000	0.000
69	A	77	ASP	-1	-0.989	-0.822	13.149	-0.703	-0.703	0.000	0.000	0.000	0.000
70	A	78	LEU	0	0.048	-0.119	15.192	0.023	0.023	0.000	0.000	0.000	0.000
71	A	78	LEU	0	-0.082	0.113	13.911	-0.004	-0.004	0.000	0.000	0.000	0.000
72	A	79	GLY	0	-0.020	-0.111	15.810	0.043	0.043	0.000	0.000	0.000	0.000
73	A	80	ASN	0	0.097	0.031	18.464	0.045	0.045	0.000	0.000	0.000	0.000
74	A	80	ASN	0	-0.068	0.079	18.130	0.023	0.023	0.000	0.000	0.000	0.000
75	A	81	LYS	0	0.053	-0.081	17.031	0.033	0.033	0.000	0.000	0.000	0.000
76	A	81	LYS	1	0.863	1.042	11.976	0.558	0.558	0.000	0.000	0.000	0.000
77	A	82	VAL	0	0.098	-0.076	18.370	0.026	0.026	0.000	0.000	0.000	0.000
78	A	82	VAL	0	-0.101	0.092	19.040	0.001	0.001	0.000	0.000	0.000	0.000
79	A	83	LYS	0	0.135	-0.087	20.917	0.026	0.026	0.000	0.000	0.000	0.000
80	A	83	LYS	1	0.733	0.975	22.606	0.242	0.242	0.000	0.000	0.000	0.000
81	A	84	ALA	0	0.095	-0.086	21.484	0.026	0.026	0.000	0.000	0.000	0.000
82	A	84	ALA	0	-0.099	0.098	20.691	-0.006	-0.006	0.000	0.000	0.000	0.000
83	A	85	LEU	0	0.084	-0.082	21.902	0.017	0.017	0.000	0.000	0.000	0.000
84	A	85	LEU	0	-0.096	0.082	19.455	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	86	LEU	0	0.070	-0.074	23.266	0.018	0.018	0.000	0.000	0.000	0.000
86	A	86	LEU	0	-0.123	0.062	25.446	0.002	0.002	0.000	0.000	0.000	0.000
87	A	87	TYR	0	0.122	-0.067	26.196	0.016	0.016	0.000	0.000	0.000	0.000
88	A	87	TYR	0	-0.117	0.072	26.572	0.002	0.002	0.000	0.000	0.000	0.000
89	A	88	ASP	0	0.090	-0.119	25.435	0.015	0.015	0.000	0.000	0.000	0.000
90	A	88	ASP	-1	-1.019	-0.856	24.030	-0.158	-0.158	0.000	0.000	0.000	0.000
91	A	89	GLU	0	0.104	-0.128	26.460	0.011	0.011	0.000	0.000	0.000	0.000
92	A	89	GLU	-1	-0.860	-0.795	24.777	-0.098	-0.098	0.000	0.000	0.000	0.000
93	A	90	ARG	0	-0.122	-0.103	27.960	0.011	0.011	0.000	0.000	0.000	0.000
94	A	90	ARG	1	0.709	0.991	28.181	0.081	0.081	0.000	0.000	0.000	0.000
95	A	91	GLY	0	0.078	-0.067	30.135	0.006	0.006	0.000	0.000	0.000	0.000
96	A	92	VAL	0	0.044	-0.032	30.372	0.005	0.005	0.000	0.000	0.000	0.000
97	A	92	VAL	0	-0.140	0.100	29.613	0.000	0.000	0.000	0.000	0.000	0.000
98	A	93	THR	0	0.043	-0.074	29.737	-0.011	-0.011	0.000	0.000	0.000	0.000
99	A	93	THR	0	0.005	0.077	32.759	0.000	0.000	0.000	0.000	0.000	0.000
100	A	94	PRO	0	0.093	-0.081	28.871	0.002	0.002	0.000	0.000	0.000	0.000
101	A	95	GLU	0	0.112	-0.022	30.890	-0.002	-0.002	0.000	0.000	0.000	0.000
102	A	95	GLU	-1	-0.918	-0.786	35.333	-0.094	-0.094	0.000	0.000	0.000	0.000
103	A	96	LYS	0	0.078	-0.107	33.520	0.007	0.007	0.000	0.000	0.000	0.000
104	A	96	LYS	1	0.839	1.057	33.112	0.080	0.080	0.000	0.000	0.000	0.000
105	A	97	ILE	0	0.119	-0.090	30.516	0.008	0.008	0.000	0.000	0.000	0.000
106	A	97	ILE	0	-0.072	0.108	27.687	0.000	0.000	0.000	0.000	0.000	0.000
107	A	98	ARG	0	0.031	-0.129	31.941	0.000	0.000	0.000	0.000	0.000	0.000
108	A	98	ARG	1	0.825	1.026	33.009	0.115	0.115	0.000	0.000	0.000	0.000
109	A	99	ASN	0	0.049	-0.053	34.095	0.001	0.001	0.000	0.000	0.000	0.000
110	A	99	ASN	0	-0.113	0.061	37.706	0.002	0.002	0.000	0.000	0.000	0.000
111	A	100	ALA	0	0.091	-0.098	34.170	0.008	0.008	0.000	0.000	0.000	0.000
112	A	100	ALA	0	-0.083	0.102	33.566	-0.001	-0.001	0.000	0.000	0.000	0.000
113	A	101	LYS	0	0.099	-0.053	35.649	-0.002	-0.002	0.000	0.000	0.000	0.000
114	A	101	LYS	1	0.839	1.048	37.088	0.072	0.072	0.000	0.000	0.000	0.000
115	A	102	SER	0	-0.009	-0.119	33.404	-0.001	-0.001	0.000	0.000	0.000	0.000
116	A	102	SER	0	-0.039	0.057	32.679	0.003	0.003	0.000	0.000	0.000	0.000
117	A	103	ALA	0	0.118	-0.059	30.037	0.007	0.007	0.000	0.000	0.000	0.000
118	A	103	ALA	0	-0.071	0.104	29.193	-0.001	-0.001	0.000	0.000	0.000	0.000
119	A	104	VAL	0	0.021	-0.131	26.648	-0.007	-0.007	0.000	0.000	0.000	0.000
120	A	104	VAL	0	-0.060	0.124	26.436	0.001	0.001	0.000	0.000	0.000	0.000
121	A	105	TYR	0	0.110	-0.032	22.896	0.011	0.011	0.000	0.000	0.000	0.000
122	A	105	TYR	0	-0.040	0.081	18.725	-0.013	-0.013	0.000	0.000	0.000	0.000
123	A	106	THR	0	0.009	-0.077	23.373	-0.014	-0.014	0.000	0.000	0.000	0.000
124	A	106	THR	0	-0.072	0.066	24.083	-0.001	-0.001	0.000	0.000	0.000	0.000
125	A	107	ILE	0	0.107	-0.108	19.159	0.010	0.010	0.000	0.000	0.000	0.000
126	A	107	ILE	0	-0.069	0.101	17.123	-0.006	-0.006	0.000	0.000	0.000	0.000
127	A	108	THR	0	0.050	-0.072	19.637	0.005	0.005	0.000	0.000	0.000	0.000
128	A	108	THR	0	-0.070	0.068	20.684	0.009	0.009	0.000	0.000	0.000	0.000
129	A	109	TRP	0	0.158	-0.057	17.122	-0.007	-0.007	0.000	0.000	0.000	0.000
130	A	109	TRP	0	-0.101	0.102	14.178	-0.021	-0.021	0.000	0.000	0.000	0.000
131	A	110	LYS	0	0.046	-0.154	16.600	0.017	0.017	0.000	0.000	0.000	0.000
132	A	110	LYS	1	0.766	1.002	12.269	0.089	0.089	0.000	0.000	0.000	0.000
133	A	111	ASP	0	-0.014	-0.121	17.863	0.024	0.024	0.000	0.000	0.000	0.000
134	A	111	ASP	-1	-0.825	-0.747	19.826	-0.095	-0.095	0.000	0.000	0.000	0.000
135	A	112	GLY	0	-0.026	-0.102	20.679	0.009	0.009	0.000	0.000	0.000	0.000
136	A	113	SER	0	0.037	0.008	22.135	0.004	0.004	0.000	0.000	0.000	0.000
137	A	113	SER	0	-0.035	0.055	21.190	-0.008	-0.008	0.000	0.000	0.000	0.000
138	A	114	LYS	0	0.020	-0.140	21.907	-0.008	-0.008	0.000	0.000	0.000	0.000
139	A	114	LYS	1	0.836	1.035	23.536	0.083	0.083	0.000	0.000	0.000	0.000
140	A	115	LYS	0	0.084	-0.074	21.595	0.009	0.009	0.000	0.000	0.000	0.000
141	A	115	LYS	1	0.822	1.058	19.304	0.242	0.242	0.000	0.000	0.000	0.000
142	A	116	GLU	0	0.113	-0.111	22.583	-0.012	-0.012	0.000	0.000	0.000	0.000
143	A	116	GLU	-1	-1.008	-0.832	26.373	-0.109	-0.109	0.000	0.000	0.000	0.000
144	A	117	VAL	0	0.040	-0.137	22.594	0.004	0.004	0.000	0.000	0.000	0.000
145	A	117	VAL	0	-0.099	0.097	20.570	-0.005	-0.005	0.000	0.000	0.000	0.000
146	A	118	ASP	0	0.180	-0.080	24.025	0.002	0.002	0.000	0.000	0.000	0.000
147	A	118	ASP	-1	-0.938	-0.811	27.849	-0.132	-0.132	0.000	0.000	0.000	0.000
148	A	119	LEU	0	0.064	-0.110	25.885	-0.012	-0.012	0.000	0.000	0.000	0.000
149	A	119	LEU	0	-0.091	0.080	23.294	-0.001	-0.001	0.000	0.000	0.000	0.000
150	A	120	LYS	0	0.033	-0.105	26.751	-0.005	-0.005	0.000	0.000	0.000	0.000
151	A	120	LYS	1	0.741	1.000	31.284	0.105	0.105	0.000	0.000	0.000	0.000
152	A	121	LYS	0	0.005	-0.084	28.446	0.008	0.008	0.000	0.000	0.000	0.000
153	A	121	LYS	1	0.769	1.005	28.427	0.129	0.129	0.000	0.000	0.000	0.000
154	A	122	ASP	0	0.205	-0.043	25.634	-0.011	-0.011	0.000	0.000	0.000	0.000
155	A	122	ASP	-1	-0.953	-0.813	24.478	-0.223	-0.223	0.000	0.000	0.000	0.000
156	A	123	SER	0	-0.005	-0.133	24.933	0.013	0.013	0.000	0.000	0.000	0.000
157	A	123	SER	0	0.000	0.086	26.760	0.002	0.002	0.000	0.000	0.000	0.000
158	A	124	TYR	0	0.034	-0.083	22.831	-0.012	-0.012	0.000	0.000	0.000	0.000
159	A	124	TYR	0	-0.049	0.097	19.715	0.008	0.008	0.000	0.000	0.000	0.000
160	A	125	THR	0	0.003	-0.061	21.199	0.022	0.022	0.000	0.000	0.000	0.000
161	A	125	THR	0	-0.018	0.063	19.051	-0.005	-0.005	0.000	0.000	0.000	0.000
162	A	126	ALA	0	0.158	-0.099	18.269	-0.024	-0.024	0.000	0.000	0.000	0.000
163	A	126	ALA	0	-0.058	0.124	18.663	0.004	0.004	0.000	0.000	0.000	0.000
164	A	127	ASN	0	0.039	-0.069	16.626	-0.049	-0.049	0.000	0.000	0.000	0.000
165	A	127	ASN	0	-0.148	0.032	17.925	0.008	0.008	0.000	0.000	0.000	0.000
166	A	128	LEU	0	0.101	-0.122	12.778	0.016	0.016	0.000	0.000	0.000	0.000
167	A	128	LEU	0	-0.040	0.121	11.255	-0.011	-0.011	0.000	0.000	0.000	0.000
168	A	129	PHE	0	0.045	-0.074	12.146	0.071	0.071	0.000	0.000	0.000	0.000
169	A	129	PHE	0	-0.111	0.051	11.321	0.002	0.002	0.000	0.000	0.000	0.000
170	A	130	ASP	0	0.101	-0.102	9.580	-0.150	-0.150	0.000	0.000	0.000	0.000
171	A	130	ASP	-1	-0.869	-0.762	9.131	-0.369	-0.369	0.000	0.000	0.000	0.000
172	A	131	SER	0	0.083	-0.116	7.323	0.178	0.178	0.000	0.000	0.000	0.000
173	A	131	SER	0	-0.090	0.070	6.594	-0.107	-0.107	0.000	0.000	0.000	0.000
174	A	132	ASN	0	0.068	-0.098	8.602	0.066	0.066	0.000	0.000	0.000	0.000
175	A	132	ASN	0	-0.120	0.080	6.719	-0.041	-0.041	0.000	0.000	0.000	0.000
176	A	133	SER	0	0.047	-0.095	9.741	0.101	0.101	0.000	0.000	0.000	0.000
177	A	133	SER	0	-0.104	0.052	12.664	0.016	0.016	0.000	0.000	0.000	0.000
178	A	134	ILE	0	0.045	-0.119	12.164	0.052	0.052	0.000	0.000	0.000	0.000
179	A	134	ILE	0	-0.071	0.119	12.272	-0.007	-0.007	0.000	0.000	0.000	0.000
180	A	135	LYS	0	0.095	-0.074	13.955	0.024	0.024	0.000	0.000	0.000	0.000
181	A	135	LYS	1	0.848	1.059	17.538	0.033	0.033	0.000	0.000	0.000	0.000
182	A	136	GLN	0	0.084	-0.105	16.797	0.011	0.011	0.000	0.000	0.000	0.000
183	A	136	GLN	0	-0.141	0.057	20.099	0.013	0.013	0.000	0.000	0.000	0.000
184	A	137	ILE	0	0.055	-0.100	18.892	-0.009	-0.009	0.000	0.000	0.000	0.000
185	A	137	ILE	0	-0.099	0.088	15.729	-0.007	-0.007	0.000	0.000	0.000	0.000
186	A	138	ASP	0	0.137	-0.068	20.047	0.006	0.006	0.000	0.000	0.000	0.000
187	A	138	ASP	-1	-0.943	-0.780	24.193	-0.091	-0.091	0.000	0.000	0.000	0.000
188	A	139	ILE	0	0.152	-0.104	23.803	-0.007	-0.007	0.000	0.000	0.000	0.000
189	A	139	ILE	0	-0.124	0.099	21.523	-0.002	-0.002	0.000	0.000	0.000	0.000
190	A	140	ASN	0	0.084	-0.069	25.142	0.011	0.011	0.000	0.000	0.000	0.000
191	A	140	ASN	0	-0.140	0.051	28.614	0.002	0.002	0.000	0.000	0.000	0.000
192	A	141	VAL	0	0.120	-0.108	28.785	-0.005	-0.005	0.000	0.000	0.000	0.000
193	A	141	VAL	0	-0.081	0.121	28.739	-0.001	-0.001	0.000	0.000	0.000	0.000
194	A	142	LYS	0	0.123	-0.059	31.230	0.006	0.006	0.000	0.000	0.000	0.000
195	A	142	LYS	1	0.802	1.040	33.120	0.079	0.079	0.000	0.000	0.000	0.000
196	A	143	THR	0	0.105	-0.083	34.956	-0.004	-0.004	0.000	0.000	0.000	0.000
197	A	143	THR	0	-0.050	0.049	36.394	-0.001	-0.001	0.000	0.000	0.000	0.000
198	A	144	LYS	0	-0.060	-0.074	37.120	0.003	0.003	0.000	0.000	0.000	0.000
199	A	144	LYS	1	0.981	0.976	38.598	0.060	0.060	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:42:ALA)