FMO DATABASE

FMODB ID: LJQY9

Calculation Name: 1D02-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1D02

Chain ID: A

ChEMBL ID:

UniProt ID: P43642

Base Structure: X-ray

Registration Date: 2023-03-13

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	197
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2224845.918256
FMO2-HF: Nuclear repulsion	2146382.321505
FMO2-HF: Total energy	-78463.596751
FMO2-MP2: Total energy	-78698.305692

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:LEU)

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

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.
-14.546	-8.045	6.68	-5.47	-7.713	-0.019

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.048 / q_NPA : 0.025

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	8	GLY	0	0.073	0.029	3.736	-2.265	-0.385	-0.010	-0.973	-0.897	0.006
4	A	9	ARG	1	0.912	0.952	6.015	-0.782	-0.782	0.000	0.000	0.000	0.000
5	A	10	LEU	0	0.034	0.026	8.036	-0.012	-0.012	0.000	0.000	0.000	0.000
6	A	11	ASN	0	-0.008	-0.005	10.650	0.104	0.104	0.000	0.000	0.000	0.000
7	A	12	TRP	0	0.056	-0.002	12.780	-0.056	-0.056	0.000	0.000	0.000	0.000
8	A	13	GLN	0	-0.022	-0.008	15.657	-0.021	-0.021	0.000	0.000	0.000	0.000
9	A	14	ALA	0	0.067	0.045	15.655	-0.023	-0.023	0.000	0.000	0.000	0.000
10	A	15	LEU	0	-0.017	-0.002	17.091	-0.026	-0.026	0.000	0.000	0.000	0.000
11	A	16	ALA	0	-0.015	-0.017	18.874	-0.017	-0.017	0.000	0.000	0.000	0.000
12	A	17	GLY	0	0.034	0.019	20.750	-0.009	-0.009	0.000	0.000	0.000	0.000
13	A	18	LEU	0	0.006	0.016	20.991	-0.011	-0.011	0.000	0.000	0.000	0.000
14	A	19	LYS	1	0.920	0.972	23.026	-0.059	-0.059	0.000	0.000	0.000	0.000
15	A	20	ALA	0	-0.025	-0.018	25.012	-0.006	-0.006	0.000	0.000	0.000	0.000
16	A	21	SER	0	-0.083	-0.047	25.911	-0.005	-0.005	0.000	0.000	0.000	0.000
17	A	22	GLY	0	-0.026	-0.017	27.749	-0.006	-0.006	0.000	0.000	0.000	0.000
18	A	23	ALA	0	-0.006	0.009	26.447	-0.006	-0.006	0.000	0.000	0.000	0.000
19	A	24	GLU	-1	-0.948	-0.964	27.856	-0.007	-0.007	0.000	0.000	0.000	0.000
20	A	25	GLN	0	0.044	0.016	23.425	-0.008	-0.008	0.000	0.000	0.000	0.000
21	A	26	ASN	0	0.011	0.003	24.074	-0.012	-0.012	0.000	0.000	0.000	0.000
22	A	27	LEU	0	0.060	0.014	19.899	0.004	0.004	0.000	0.000	0.000	0.000
23	A	28	TYR	0	-0.004	-0.031	19.985	-0.003	-0.003	0.000	0.000	0.000	0.000
24	A	29	ASN	0	0.013	0.002	19.316	-0.005	-0.005	0.000	0.000	0.000	0.000
25	A	30	VAL	0	0.018	0.020	19.059	0.014	0.014	0.000	0.000	0.000	0.000
26	A	31	PHE	0	0.013	-0.017	14.976	0.011	0.011	0.000	0.000	0.000	0.000
27	A	32	ASN	0	-0.002	-0.003	14.863	-0.026	-0.026	0.000	0.000	0.000	0.000
28	A	33	ALA	0	0.026	0.028	15.100	0.011	0.011	0.000	0.000	0.000	0.000
29	A	34	VAL	0	-0.036	-0.012	13.439	0.035	0.035	0.000	0.000	0.000	0.000
30	A	35	PHE	0	0.004	-0.010	10.779	0.010	0.010	0.000	0.000	0.000	0.000
31	A	36	GLU	-1	-0.901	-0.929	10.206	0.081	0.081	0.000	0.000	0.000	0.000
32	A	37	GLY	0	0.005	0.005	8.395	0.066	0.066	0.000	0.000	0.000	0.000
33	A	38	THR	0	-0.074	-0.028	6.225	0.155	0.155	0.000	0.000	0.000	0.000
34	A	39	LYS	1	0.908	0.951	2.270	2.182	3.627	2.454	-1.239	-2.661	0.001
35	A	40	TYR	0	-0.014	-0.016	4.410	-0.470	-0.334	-0.001	-0.016	-0.119	0.000
36	A	41	VAL	0	0.041	0.031	7.875	0.114	0.114	0.000	0.000	0.000	0.000
37	A	42	LEU	0	-0.015	-0.002	10.691	-0.034	-0.034	0.000	0.000	0.000	0.000
38	A	43	TYR	0	-0.091	-0.086	12.241	0.042	0.042	0.000	0.000	0.000	0.000
39	A	44	GLU	-1	-0.900	-0.959	16.927	-0.105	-0.105	0.000	0.000	0.000	0.000
40	A	45	LYS	1	0.897	0.952	20.637	0.123	0.123	0.000	0.000	0.000	0.000
41	A	46	PRO	0	-0.024	0.004	18.399	-0.003	-0.003	0.000	0.000	0.000	0.000
42	A	47	LYS	1	0.967	0.953	20.150	0.199	0.199	0.000	0.000	0.000	0.000
43	A	48	HIS	0	0.058	0.030	15.317	0.049	0.049	0.000	0.000	0.000	0.000
44	A	49	LEU	0	0.036	0.035	20.570	0.003	0.003	0.000	0.000	0.000	0.000
45	A	50	LYS	1	0.900	0.951	23.770	0.177	0.177	0.000	0.000	0.000	0.000
46	A	51	ASN	0	-0.019	-0.013	26.133	0.024	0.024	0.000	0.000	0.000	0.000
47	A	52	LEU	0	-0.051	-0.033	25.768	-0.008	-0.008	0.000	0.000	0.000	0.000
48	A	53	TYR	0	0.023	-0.022	29.482	0.003	0.003	0.000	0.000	0.000	0.000
49	A	54	ALA	0	0.019	0.045	33.243	0.005	0.005	0.000	0.000	0.000	0.000
50	A	55	GLN	0	0.040	0.015	29.532	0.013	0.013	0.000	0.000	0.000	0.000
51	A	56	VAL	0	-0.061	-0.025	34.096	-0.001	-0.001	0.000	0.000	0.000	0.000
52	A	57	VAL	0	0.011	0.008	36.029	0.005	0.005	0.000	0.000	0.000	0.000
53	A	58	LEU	0	-0.021	-0.010	39.012	0.000	0.000	0.000	0.000	0.000	0.000
54	A	59	PRO	0	0.016	0.007	42.170	0.001	0.001	0.000	0.000	0.000	0.000
55	A	60	ASP	-1	-0.846	-0.939	45.309	-0.077	-0.077	0.000	0.000	0.000	0.000
56	A	61	ASP	-1	-0.998	-1.007	48.066	-0.061	-0.061	0.000	0.000	0.000	0.000
57	A	62	VAL	0	0.020	0.013	44.818	0.001	0.001	0.000	0.000	0.000	0.000
58	A	63	ILE	0	-0.018	-0.007	43.699	0.001	0.001	0.000	0.000	0.000	0.000
59	A	64	LYS	1	0.913	0.956	47.375	0.065	0.065	0.000	0.000	0.000	0.000
60	A	65	GLU	-1	-0.898	-0.934	50.166	-0.056	-0.056	0.000	0.000	0.000	0.000
61	A	66	ILE	0	-0.087	-0.021	44.468	0.000	0.000	0.000	0.000	0.000	0.000
62	A	67	PHE	0	-0.037	-0.025	46.030	0.001	0.001	0.000	0.000	0.000	0.000
63	A	68	ASN	0	-0.008	-0.019	45.795	-0.006	-0.006	0.000	0.000	0.000	0.000
64	A	69	PRO	0	-0.036	-0.012	43.091	0.002	0.002	0.000	0.000	0.000	0.000
65	A	70	LEU	0	0.015	0.010	45.046	-0.002	-0.002	0.000	0.000	0.000	0.000
66	A	71	ILE	0	-0.031	-0.029	38.641	-0.001	-0.001	0.000	0.000	0.000	0.000
67	A	72	ASP	-1	-0.752	-0.839	38.221	-0.109	-0.109	0.000	0.000	0.000	0.000
68	A	73	LEU	0	-0.004	-0.004	37.548	-0.005	-0.005	0.000	0.000	0.000	0.000
69	A	74	SER	0	-0.074	-0.045	35.420	-0.008	-0.008	0.000	0.000	0.000	0.000
70	A	75	THR	0	-0.047	-0.034	33.346	-0.009	-0.009	0.000	0.000	0.000	0.000
71	A	76	THR	0	-0.051	-0.018	33.448	0.000	0.000	0.000	0.000	0.000	0.000
72	A	77	GLN	0	-0.031	-0.018	27.198	-0.010	-0.010	0.000	0.000	0.000	0.000
73	A	78	TRP	0	0.015	0.004	31.203	0.003	0.003	0.000	0.000	0.000	0.000
74	A	79	GLY	0	0.032	0.017	28.541	-0.006	-0.006	0.000	0.000	0.000	0.000
75	A	80	VAL	0	-0.055	-0.024	25.570	0.014	0.014	0.000	0.000	0.000	0.000
76	A	81	SER	0	-0.060	-0.049	25.126	-0.007	-0.007	0.000	0.000	0.000	0.000
77	A	82	PRO	0	0.017	0.034	21.823	0.013	0.013	0.000	0.000	0.000	0.000
78	A	83	ALA	0	0.031	0.027	23.620	0.002	0.002	0.000	0.000	0.000	0.000
79	A	84	PHE	0	0.015	0.011	18.064	0.008	0.008	0.000	0.000	0.000	0.000
80	A	85	ALA	0	0.001	0.011	16.230	-0.005	-0.005	0.000	0.000	0.000	0.000
81	A	86	ILE	0	0.004	0.017	11.901	0.017	0.017	0.000	0.000	0.000	0.000
82	A	87	GLU	-1	-0.815	-0.871	9.191	-0.707	-0.707	0.000	0.000	0.000	0.000
83	A	88	ASN	0	0.037	0.042	5.556	-0.188	-0.188	0.000	0.000	0.000	0.000
84	A	89	THR	0	-0.040	-0.061	4.643	-0.226	-0.131	-0.001	-0.009	-0.085	0.000
85	A	90	GLU	-1	-0.932	-0.962	2.006	-13.384	-10.566	4.236	-3.191	-3.864	-0.026
86	A	91	THR	0	-0.063	-0.053	4.012	0.105	0.232	0.002	-0.042	-0.087	0.000
87	A	92	HIS	1	0.846	0.923	7.250	1.455	1.455	0.000	0.000	0.000	0.000
88	A	93	LYS	1	0.907	0.991	9.475	0.912	0.912	0.000	0.000	0.000	0.000
89	A	94	ILE	0	-0.041	-0.041	11.235	-0.015	-0.015	0.000	0.000	0.000	0.000
90	A	95	LEU	0	0.002	0.016	13.882	0.033	0.033	0.000	0.000	0.000	0.000
91	A	96	PHE	0	-0.015	-0.022	16.290	0.017	0.017	0.000	0.000	0.000	0.000
92	A	97	GLY	0	0.046	0.011	19.282	0.010	0.010	0.000	0.000	0.000	0.000
93	A	98	GLU	-1	-0.958	-0.991	21.530	-0.146	-0.146	0.000	0.000	0.000	0.000
94	A	99	ILE	0	0.046	0.025	23.561	0.003	0.003	0.000	0.000	0.000	0.000
95	A	100	LYS	1	0.842	0.922	26.856	0.104	0.104	0.000	0.000	0.000	0.000
96	A	101	ARG	1	0.957	0.986	27.842	0.076	0.076	0.000	0.000	0.000	0.000
97	A	102	GLN	0	-0.050	-0.041	32.697	-0.005	-0.005	0.000	0.000	0.000	0.000
98	A	103	ASP	-1	-0.855	-0.915	36.270	-0.033	-0.033	0.000	0.000	0.000	0.000
99	A	104	GLY	0	-0.003	-0.031	39.112	-0.004	-0.004	0.000	0.000	0.000	0.000
100	A	105	TRP	0	-0.096	-0.033	40.691	0.002	0.002	0.000	0.000	0.000	0.000
101	A	106	VAL	0	0.034	0.002	39.629	0.000	0.000	0.000	0.000	0.000	0.000
102	A	107	GLU	-1	-0.764	-0.863	41.976	-0.010	-0.010	0.000	0.000	0.000	0.000
103	A	108	GLY	0	-0.017	-0.010	45.292	0.000	0.000	0.000	0.000	0.000	0.000
104	A	109	LYS	1	0.892	0.963	43.182	0.018	0.018	0.000	0.000	0.000	0.000
105	A	110	ASP	-1	-0.822	-0.904	47.800	-0.017	-0.017	0.000	0.000	0.000	0.000
106	A	111	PRO	0	-0.002	-0.028	46.944	-0.002	-0.002	0.000	0.000	0.000	0.000
107	A	112	SER	0	-0.013	0.000	46.577	-0.003	-0.003	0.000	0.000	0.000	0.000
108	A	113	ALA	0	-0.005	-0.001	44.791	-0.002	-0.002	0.000	0.000	0.000	0.000
109	A	114	GLY	0	0.049	0.030	42.471	-0.002	-0.002	0.000	0.000	0.000	0.000
110	A	115	ARG	1	0.864	0.918	42.988	0.031	0.031	0.000	0.000	0.000	0.000
111	A	116	GLY	0	-0.038	-0.002	41.735	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	117	ASN	0	0.063	0.012	40.054	0.000	0.000	0.000	0.000	0.000	0.000
113	A	118	ALA	0	0.055	0.034	37.592	-0.004	-0.004	0.000	0.000	0.000	0.000
114	A	119	HIS	0	-0.006	-0.010	34.131	-0.007	-0.007	0.000	0.000	0.000	0.000
115	A	120	GLU	-1	-0.852	-0.920	33.971	-0.071	-0.071	0.000	0.000	0.000	0.000
116	A	121	ARG	1	0.918	0.959	32.263	0.084	0.084	0.000	0.000	0.000	0.000
117	A	122	SER	0	-0.104	-0.063	29.633	-0.008	-0.008	0.000	0.000	0.000	0.000
118	A	123	CYS	0	0.048	0.017	30.189	-0.010	-0.010	0.000	0.000	0.000	0.000
119	A	124	LYS	1	0.967	0.995	30.099	0.125	0.125	0.000	0.000	0.000	0.000
120	A	125	LEU	0	-0.018	-0.015	25.301	-0.004	-0.004	0.000	0.000	0.000	0.000
121	A	126	PHE	0	0.034	0.031	28.141	-0.012	-0.012	0.000	0.000	0.000	0.000
122	A	127	THR	0	-0.049	-0.016	30.596	0.001	0.001	0.000	0.000	0.000	0.000
123	A	128	PRO	0	0.072	0.020	30.289	-0.011	-0.011	0.000	0.000	0.000	0.000
124	A	129	GLY	0	-0.019	-0.007	29.734	-0.011	-0.011	0.000	0.000	0.000	0.000
125	A	130	LEU	0	0.003	-0.006	27.606	-0.012	-0.012	0.000	0.000	0.000	0.000
126	A	131	LEU	0	0.030	0.031	25.874	-0.019	-0.019	0.000	0.000	0.000	0.000
127	A	132	LYS	1	0.980	0.992	24.677	0.149	0.149	0.000	0.000	0.000	0.000
128	A	133	ALA	0	0.002	0.000	24.364	-0.019	-0.019	0.000	0.000	0.000	0.000
129	A	134	TYR	0	0.026	-0.007	21.893	-0.019	-0.019	0.000	0.000	0.000	0.000
130	A	135	ARG	1	0.855	0.927	20.165	0.223	0.223	0.000	0.000	0.000	0.000
131	A	136	THR	0	-0.056	-0.019	19.420	-0.035	-0.035	0.000	0.000	0.000	0.000
132	A	137	ILE	0	-0.056	-0.037	18.668	-0.029	-0.029	0.000	0.000	0.000	0.000
133	A	138	GLY	0	0.005	0.016	16.308	-0.033	-0.033	0.000	0.000	0.000	0.000
134	A	139	GLY	0	0.053	0.032	14.872	-0.079	-0.079	0.000	0.000	0.000	0.000
135	A	140	ILE	0	-0.032	-0.011	15.422	-0.024	-0.024	0.000	0.000	0.000	0.000
136	A	141	ASN	0	-0.009	-0.031	17.196	0.073	0.073	0.000	0.000	0.000	0.000
137	A	142	ASP	-1	-0.864	-0.915	18.105	-0.252	-0.252	0.000	0.000	0.000	0.000
138	A	143	GLU	-1	-0.922	-0.982	20.104	-0.197	-0.197	0.000	0.000	0.000	0.000
139	A	144	GLU	-1	-0.903	-0.880	20.511	-0.161	-0.161	0.000	0.000	0.000	0.000
140	A	145	ILE	0	-0.066	-0.012	18.681	0.018	0.018	0.000	0.000	0.000	0.000
141	A	146	LEU	0	-0.031	-0.013	22.079	-0.011	-0.011	0.000	0.000	0.000	0.000
142	A	147	PRO	0	-0.006	-0.010	20.082	-0.012	-0.012	0.000	0.000	0.000	0.000
143	A	148	PHE	0	-0.007	-0.004	20.139	-0.019	-0.019	0.000	0.000	0.000	0.000
144	A	149	TRP	0	0.012	0.004	18.293	0.002	0.002	0.000	0.000	0.000	0.000
145	A	150	VAL	0	-0.036	-0.012	22.325	0.000	0.000	0.000	0.000	0.000	0.000
146	A	151	VAL	0	0.026	0.021	22.751	0.008	0.008	0.000	0.000	0.000	0.000
147	A	152	PHE	0	-0.002	-0.014	25.838	0.002	0.002	0.000	0.000	0.000	0.000
148	A	153	GLU	-1	-0.833	-0.941	26.937	-0.061	-0.061	0.000	0.000	0.000	0.000
149	A	154	GLY	0	0.055	0.023	30.852	-0.002	-0.002	0.000	0.000	0.000	0.000
150	A	155	ASP	-1	-0.848	-0.928	34.392	-0.024	-0.024	0.000	0.000	0.000	0.000
151	A	156	ILE	0	-0.023	0.002	33.972	0.001	0.001	0.000	0.000	0.000	0.000
152	A	157	THR	0	-0.046	-0.038	31.092	0.002	0.002	0.000	0.000	0.000	0.000
153	A	158	ARG	1	0.788	0.858	34.060	0.015	0.015	0.000	0.000	0.000	0.000
154	A	159	ASP	-1	-0.745	-0.830	36.913	-0.031	-0.031	0.000	0.000	0.000	0.000
155	A	160	PRO	0	0.001	-0.009	38.723	-0.003	-0.003	0.000	0.000	0.000	0.000
156	A	161	LYS	1	0.955	0.977	40.657	0.033	0.033	0.000	0.000	0.000	0.000
157	A	162	ARG	1	0.865	0.928	37.284	0.045	0.045	0.000	0.000	0.000	0.000
158	A	163	VAL	0	0.034	0.029	34.330	-0.004	-0.004	0.000	0.000	0.000	0.000
159	A	164	ARG	1	0.900	0.951	35.557	0.024	0.024	0.000	0.000	0.000	0.000
160	A	165	GLU	-1	-0.800	-0.879	37.552	-0.059	-0.059	0.000	0.000	0.000	0.000
161	A	166	ILE	0	0.007	0.002	31.792	-0.004	-0.004	0.000	0.000	0.000	0.000
162	A	167	THR	0	-0.047	-0.030	32.850	-0.005	-0.005	0.000	0.000	0.000	0.000
163	A	168	PHE	0	-0.021	-0.022	33.743	-0.004	-0.004	0.000	0.000	0.000	0.000
164	A	169	TRP	0	-0.019	-0.021	33.738	-0.005	-0.005	0.000	0.000	0.000	0.000
165	A	170	TYR	0	-0.015	-0.008	27.209	-0.009	-0.009	0.000	0.000	0.000	0.000
166	A	171	ASP	-1	-0.843	-0.893	30.570	-0.086	-0.086	0.000	0.000	0.000	0.000
167	A	172	HIS	1	0.870	0.938	28.053	0.114	0.114	0.000	0.000	0.000	0.000
168	A	173	TYR	0	0.000	0.003	25.245	0.000	0.000	0.000	0.000	0.000	0.000
169	A	174	GLN	0	-0.025	-0.033	26.945	0.000	0.000	0.000	0.000	0.000	0.000
170	A	175	ASP	-1	-0.819	-0.900	21.962	-0.096	-0.096	0.000	0.000	0.000	0.000
171	A	176	ASN	0	-0.025	-0.023	21.812	-0.003	-0.003	0.000	0.000	0.000	0.000
172	A	177	TYR	0	-0.039	-0.034	24.055	-0.003	-0.003	0.000	0.000	0.000	0.000
173	A	178	PHE	0	-0.002	0.010	23.702	0.004	0.004	0.000	0.000	0.000	0.000
174	A	179	MET	0	-0.045	-0.011	25.801	-0.001	-0.001	0.000	0.000	0.000	0.000
175	A	180	TRP	0	-0.001	-0.002	24.606	0.002	0.002	0.000	0.000	0.000	0.000
176	A	181	ARG	1	0.877	0.925	27.816	0.030	0.030	0.000	0.000	0.000	0.000
177	A	182	PRO	0	0.035	0.002	30.564	0.003	0.003	0.000	0.000	0.000	0.000
178	A	183	ASN	0	-0.013	-0.010	32.061	0.002	0.002	0.000	0.000	0.000	0.000
179	A	184	GLU	-1	-0.815	-0.876	27.578	0.017	0.017	0.000	0.000	0.000	0.000
180	A	185	SER	0	-0.032	-0.006	24.898	-0.005	-0.005	0.000	0.000	0.000	0.000
181	A	186	GLY	0	0.078	0.022	22.409	-0.008	-0.008	0.000	0.000	0.000	0.000
182	A	187	GLU	-1	-0.987	-0.992	20.128	0.079	0.079	0.000	0.000	0.000	0.000
183	A	188	LYS	1	0.880	0.923	20.479	-0.024	-0.024	0.000	0.000	0.000	0.000
184	A	189	LEU	0	-0.007	0.015	20.314	-0.011	-0.011	0.000	0.000	0.000	0.000
185	A	190	VAL	0	0.003	-0.014	15.486	-0.021	-0.021	0.000	0.000	0.000	0.000
186	A	191	GLN	0	0.011	-0.008	16.970	-0.032	-0.032	0.000	0.000	0.000	0.000
187	A	192	HIS	0	0.015	0.027	18.588	0.007	0.007	0.000	0.000	0.000	0.000
188	A	193	PHE	0	0.045	0.013	11.610	-0.013	-0.013	0.000	0.000	0.000	0.000
189	A	194	ASN	0	0.025	0.009	12.677	-0.088	-0.088	0.000	0.000	0.000	0.000
190	A	195	GLU	-1	-0.977	-0.986	14.606	-0.001	-0.001	0.000	0.000	0.000	0.000
191	A	196	LYS	1	0.891	0.952	17.376	0.058	0.058	0.000	0.000	0.000	0.000
192	A	197	LEU	0	-0.010	-0.010	16.376	-0.019	-0.019	0.000	0.000	0.000	0.000
193	A	198	LYS	1	0.809	0.908	9.360	0.106	0.106	0.000	0.000	0.000	0.000
194	A	199	LYS	1	0.940	0.982	11.210	0.083	0.083	0.000	0.000	0.000	0.000
195	A	200	TYR	0	-0.092	-0.088	12.189	-0.076	-0.076	0.000	0.000	0.000	0.000
196	A	201	LEU	0	-0.045	-0.027	10.274	-0.016	-0.016	0.000	0.000	0.000	0.000
197	A	202	ASP	-1	-0.925	-0.954	7.599	-1.314	-1.314	0.000	0.000	0.000	0.000

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