FMO DATABASE

FMODB ID: 983R2

Calculation Name: 2NR7-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2NR7

Chain ID: A

ChEMBL ID:

UniProt ID: Q7MXB3

Base Structure: X-ray

Registration Date: 2023-09-24

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

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	194
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2184330.139265
FMO2-HF: Nuclear repulsion	2108446.732935
FMO2-HF: Total energy	-75883.40633
FMO2-MP2: Total energy	-76111.050897

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:-1:ASN)

Summations of interaction energy for fragment #1(A:-1:ASN)

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.
-9.575	-5.318	0.259	-2.13	-2.386	-0.009

Interaction energy analysis for fragmet #1(A:-1:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.001 / q_NPA : -0.015

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	1	MET	0	-0.002	0.020	3.022	-2.334	-0.412	0.096	-0.807	-1.211	0.003
4	A	2	ALA	0	-0.024	0.005	6.188	1.085	1.085	0.000	0.000	0.000	0.000
5	A	3	ASN	0	0.020	-0.007	9.908	0.011	0.011	0.000	0.000	0.000	0.000
6	A	4	VAL	0	0.089	0.047	12.260	0.216	0.216	0.000	0.000	0.000	0.000
7	A	5	LYS	1	0.839	0.900	15.563	0.851	0.851	0.000	0.000	0.000	0.000
8	A	6	LEU	0	-0.026	-0.006	13.124	0.114	0.114	0.000	0.000	0.000	0.000
9	A	7	LEU	0	-0.025	0.006	17.007	0.051	0.051	0.000	0.000	0.000	0.000
10	A	8	LEU	0	0.006	-0.008	18.878	0.080	0.080	0.000	0.000	0.000	0.000
11	A	9	PRO	0	0.038	0.014	20.693	0.057	0.057	0.000	0.000	0.000	0.000
12	A	10	TYR	0	-0.022	-0.026	21.870	0.043	0.043	0.000	0.000	0.000	0.000
13	A	11	ILE	0	-0.004	0.001	22.681	0.042	0.042	0.000	0.000	0.000	0.000
14	A	12	LEU	0	0.012	0.008	25.315	0.041	0.041	0.000	0.000	0.000	0.000
15	A	13	LYS	1	0.855	0.926	26.275	0.376	0.376	0.000	0.000	0.000	0.000
16	A	14	TRP	0	-0.060	-0.035	26.437	0.051	0.051	0.000	0.000	0.000	0.000
17	A	15	GLU	-1	-0.699	-0.830	28.578	-0.341	-0.341	0.000	0.000	0.000	0.000
18	A	16	GLY	0	0.025	0.018	30.916	0.020	0.020	0.000	0.000	0.000	0.000
19	A	17	GLY	0	-0.032	-0.012	32.117	0.022	0.022	0.000	0.000	0.000	0.000
20	A	18	PHE	0	-0.015	-0.021	32.731	0.020	0.020	0.000	0.000	0.000	0.000
21	A	19	VAL	0	-0.023	-0.014	32.382	-0.015	-0.015	0.000	0.000	0.000	0.000
22	A	20	HIS	0	0.039	0.025	31.361	0.020	0.020	0.000	0.000	0.000	0.000
23	A	21	ASP	-1	-0.838	-0.912	34.503	-0.174	-0.174	0.000	0.000	0.000	0.000
24	A	22	PRO	0	-0.009	-0.015	35.552	-0.007	-0.007	0.000	0.000	0.000	0.000
25	A	23	ALA	0	0.020	-0.002	36.294	0.006	0.006	0.000	0.000	0.000	0.000
26	A	24	ASP	-1	-0.937	-0.969	38.096	-0.137	-0.137	0.000	0.000	0.000	0.000
27	A	25	ALA	0	-0.026	-0.011	40.097	0.007	0.007	0.000	0.000	0.000	0.000
28	A	26	GLY	0	-0.004	0.000	41.232	0.004	0.004	0.000	0.000	0.000	0.000
29	A	27	GLY	0	-0.052	-0.021	37.785	-0.002	-0.002	0.000	0.000	0.000	0.000
30	A	28	ALA	0	-0.020	0.003	38.031	-0.009	-0.009	0.000	0.000	0.000	0.000
31	A	29	THR	0	0.000	-0.011	35.802	-0.005	-0.005	0.000	0.000	0.000	0.000
32	A	30	ASN	0	-0.053	-0.002	37.584	0.012	0.012	0.000	0.000	0.000	0.000
33	A	31	LYS	1	0.858	0.915	36.511	0.216	0.216	0.000	0.000	0.000	0.000
34	A	32	GLY	0	0.015	0.009	37.179	0.013	0.013	0.000	0.000	0.000	0.000
35	A	33	VAL	0	-0.045	-0.023	34.732	-0.003	-0.003	0.000	0.000	0.000	0.000
36	A	34	THR	0	-0.005	-0.009	34.118	-0.011	-0.011	0.000	0.000	0.000	0.000
37	A	35	ILE	0	-0.107	-0.041	31.184	0.015	0.015	0.000	0.000	0.000	0.000
38	A	36	ALA	0	0.051	0.030	31.049	-0.023	-0.023	0.000	0.000	0.000	0.000
39	A	37	THR	0	-0.101	-0.073	28.577	0.005	0.005	0.000	0.000	0.000	0.000
40	A	38	TRP	0	0.023	0.016	27.851	0.013	0.013	0.000	0.000	0.000	0.000
41	A	39	LYS	1	0.846	0.903	29.976	0.346	0.346	0.000	0.000	0.000	0.000
42	A	40	ARG	1	0.860	0.924	31.974	0.297	0.297	0.000	0.000	0.000	0.000
43	A	41	VAL	0	-0.026	-0.003	30.399	0.018	0.018	0.000	0.000	0.000	0.000
44	A	42	GLY	0	-0.003	0.002	31.530	-0.011	-0.011	0.000	0.000	0.000	0.000
45	A	43	TYR	0	-0.103	-0.060	28.076	-0.010	-0.010	0.000	0.000	0.000	0.000
46	A	44	ASP	-1	-0.849	-0.910	30.631	-0.262	-0.262	0.000	0.000	0.000	0.000
47	A	45	LYS	1	0.841	0.885	30.052	0.231	0.231	0.000	0.000	0.000	0.000
48	A	46	ASP	-1	-0.829	-0.900	30.306	-0.296	-0.296	0.000	0.000	0.000	0.000
49	A	47	GLY	0	0.000	-0.002	27.248	-0.029	-0.029	0.000	0.000	0.000	0.000
50	A	48	ASP	-1	-0.835	-0.899	26.106	-0.379	-0.379	0.000	0.000	0.000	0.000
51	A	49	GLY	0	0.008	0.002	26.946	-0.023	-0.023	0.000	0.000	0.000	0.000
52	A	50	ASP	-1	-0.852	-0.908	28.398	-0.256	-0.256	0.000	0.000	0.000	0.000
53	A	51	ILE	0	-0.015	0.022	26.669	0.016	0.016	0.000	0.000	0.000	0.000
54	A	52	ASP	-1	-0.859	-0.930	29.908	-0.281	-0.281	0.000	0.000	0.000	0.000
55	A	53	VAL	0	-0.033	-0.024	31.376	0.000	0.000	0.000	0.000	0.000	0.000
56	A	54	GLU	-1	-0.930	-0.950	34.037	-0.199	-0.199	0.000	0.000	0.000	0.000
57	A	55	ASP	-1	-0.782	-0.893	35.420	-0.251	-0.251	0.000	0.000	0.000	0.000
58	A	56	LEU	0	-0.005	0.003	28.718	-0.004	-0.004	0.000	0.000	0.000	0.000
59	A	57	LYS	1	0.734	0.850	31.799	0.244	0.244	0.000	0.000	0.000	0.000
60	A	58	LEU	0	-0.018	0.007	34.074	0.012	0.012	0.000	0.000	0.000	0.000
61	A	59	LEU	0	-0.024	0.002	30.126	0.002	0.002	0.000	0.000	0.000	0.000
62	A	60	THR	0	0.005	-0.023	28.755	-0.009	-0.009	0.000	0.000	0.000	0.000
63	A	61	ASP	-1	-0.844	-0.934	25.497	-0.399	-0.399	0.000	0.000	0.000	0.000
64	A	62	ASP	-1	-0.769	-0.899	22.109	-0.624	-0.624	0.000	0.000	0.000	0.000
65	A	63	ASP	-1	-0.797	-0.840	24.406	-0.375	-0.375	0.000	0.000	0.000	0.000
66	A	64	VAL	0	0.016	0.004	25.210	-0.018	-0.018	0.000	0.000	0.000	0.000
67	A	65	LEU	0	-0.032	-0.016	18.617	-0.032	-0.032	0.000	0.000	0.000	0.000
68	A	66	ASN	0	-0.073	-0.055	20.374	-0.100	-0.100	0.000	0.000	0.000	0.000
69	A	67	ARG	1	0.828	0.901	22.286	0.368	0.368	0.000	0.000	0.000	0.000
70	A	68	VAL	0	0.001	0.010	24.398	0.022	0.022	0.000	0.000	0.000	0.000
71	A	69	LEU	0	-0.001	0.001	20.360	-0.027	-0.027	0.000	0.000	0.000	0.000
72	A	70	LYS	1	0.776	0.856	13.640	1.279	1.279	0.000	0.000	0.000	0.000
73	A	71	PRO	0	0.015	0.017	18.876	-0.051	-0.051	0.000	0.000	0.000	0.000
74	A	72	PHE	0	0.003	0.002	20.585	-0.004	-0.004	0.000	0.000	0.000	0.000
75	A	73	TYR	0	-0.043	-0.024	21.016	0.029	0.029	0.000	0.000	0.000	0.000
76	A	74	TRP	0	-0.021	-0.031	12.148	0.127	0.127	0.000	0.000	0.000	0.000
77	A	75	ASP	-1	-0.790	-0.897	15.081	-1.298	-1.298	0.000	0.000	0.000	0.000
78	A	76	ARG	1	0.812	0.923	16.710	0.481	0.481	0.000	0.000	0.000	0.000
79	A	77	TRP	0	-0.006	-0.035	15.451	0.025	0.025	0.000	0.000	0.000	0.000
80	A	78	LYS	1	0.848	0.923	12.856	0.722	0.722	0.000	0.000	0.000	0.000
81	A	79	ALA	0	0.072	0.024	11.663	-0.254	-0.254	0.000	0.000	0.000	0.000
82	A	80	ASP	-1	-0.828	-0.884	9.570	-2.069	-2.069	0.000	0.000	0.000	0.000
83	A	81	LEU	0	-0.046	-0.025	7.107	-0.742	-0.742	0.000	0.000	0.000	0.000
84	A	82	ILE	0	0.006	0.017	7.831	0.016	0.016	0.000	0.000	0.000	0.000
85	A	83	GLU	-1	-0.861	-0.929	3.044	-7.934	-5.599	0.163	-1.323	-1.175	-0.012
86	A	84	SER	0	0.003	0.001	5.991	0.524	0.524	0.000	0.000	0.000	0.000
87	A	85	GLN	0	0.030	0.000	8.793	-0.008	-0.008	0.000	0.000	0.000	0.000
88	A	86	LYS	1	0.851	0.925	11.336	0.709	0.709	0.000	0.000	0.000	0.000
89	A	87	VAL	0	0.025	0.016	12.127	0.114	0.114	0.000	0.000	0.000	0.000
90	A	88	ALA	0	0.034	0.016	12.185	0.109	0.109	0.000	0.000	0.000	0.000
91	A	89	ASN	0	0.013	0.002	14.095	0.035	0.035	0.000	0.000	0.000	0.000
92	A	90	ILE	0	-0.016	0.004	16.889	0.084	0.084	0.000	0.000	0.000	0.000
93	A	91	LEU	0	0.051	0.032	15.241	0.093	0.093	0.000	0.000	0.000	0.000
94	A	92	VAL	0	0.004	0.005	16.714	0.079	0.079	0.000	0.000	0.000	0.000
95	A	93	ASP	-1	-0.776	-0.872	19.563	-0.422	-0.422	0.000	0.000	0.000	0.000
96	A	94	TRP	0	0.000	0.010	21.931	0.048	0.048	0.000	0.000	0.000	0.000
97	A	95	VAL	0	-0.008	-0.002	21.524	0.045	0.045	0.000	0.000	0.000	0.000
98	A	96	TRP	0	-0.052	-0.031	23.657	0.030	0.030	0.000	0.000	0.000	0.000
99	A	97	GLY	0	0.026	0.006	25.386	0.037	0.037	0.000	0.000	0.000	0.000
100	A	98	SER	0	-0.052	-0.063	27.156	0.029	0.029	0.000	0.000	0.000	0.000
101	A	99	GLY	0	0.034	0.030	27.104	0.021	0.021	0.000	0.000	0.000	0.000
102	A	100	LYS	1	0.869	0.927	25.917	0.262	0.262	0.000	0.000	0.000	0.000
103	A	101	TYR	0	0.007	-0.003	25.994	-0.006	-0.006	0.000	0.000	0.000	0.000
104	A	102	GLY	0	0.019	0.010	23.813	0.000	0.000	0.000	0.000	0.000	0.000
105	A	103	ILE	0	-0.035	-0.012	20.707	-0.063	-0.063	0.000	0.000	0.000	0.000
106	A	104	VAL	0	0.011	0.001	22.539	0.002	0.002	0.000	0.000	0.000	0.000
107	A	105	ILE	0	-0.037	-0.005	25.259	0.023	0.023	0.000	0.000	0.000	0.000
108	A	106	PRO	0	0.028	0.006	19.758	0.016	0.016	0.000	0.000	0.000	0.000
109	A	107	GLN	0	-0.005	-0.011	20.924	0.013	0.013	0.000	0.000	0.000	0.000
110	A	108	ARG	1	0.851	0.918	22.109	0.295	0.295	0.000	0.000	0.000	0.000
111	A	109	ILE	0	-0.062	-0.024	20.367	0.027	0.027	0.000	0.000	0.000	0.000
112	A	110	LEU	0	-0.016	-0.004	16.330	0.013	0.013	0.000	0.000	0.000	0.000
113	A	111	GLY	0	0.016	0.033	19.764	0.021	0.021	0.000	0.000	0.000	0.000
114	A	112	VAL	0	-0.113	-0.065	19.137	0.031	0.031	0.000	0.000	0.000	0.000
115	A	113	GLN	0	-0.043	-0.036	22.503	0.028	0.028	0.000	0.000	0.000	0.000
116	A	114	ALA	0	0.036	0.020	24.057	-0.031	-0.031	0.000	0.000	0.000	0.000
117	A	115	ASP	-1	-0.806	-0.891	23.822	-0.326	-0.326	0.000	0.000	0.000	0.000
118	A	116	GLY	0	-0.002	-0.016	24.411	0.011	0.011	0.000	0.000	0.000	0.000
119	A	117	ILE	0	-0.068	-0.031	20.985	-0.037	-0.037	0.000	0.000	0.000	0.000
120	A	118	VAL	0	0.043	0.031	15.809	0.022	0.022	0.000	0.000	0.000	0.000
121	A	119	GLY	0	0.026	0.016	17.247	-0.051	-0.051	0.000	0.000	0.000	0.000
122	A	120	ASN	0	0.035	0.004	13.058	-0.121	-0.121	0.000	0.000	0.000	0.000
123	A	121	LYS	1	0.978	0.990	14.590	0.157	0.157	0.000	0.000	0.000	0.000
124	A	122	THR	0	0.010	0.009	16.592	0.030	0.030	0.000	0.000	0.000	0.000
125	A	123	LEU	0	0.047	0.021	11.424	-0.003	-0.003	0.000	0.000	0.000	0.000
126	A	124	GLN	0	-0.039	-0.025	10.640	-0.038	-0.038	0.000	0.000	0.000	0.000
127	A	125	ALA	0	-0.015	0.009	12.616	0.017	0.017	0.000	0.000	0.000	0.000
128	A	126	VAL	0	-0.037	-0.024	11.315	0.031	0.031	0.000	0.000	0.000	0.000
129	A	127	ASN	0	-0.050	-0.055	6.386	0.210	0.210	0.000	0.000	0.000	0.000
130	A	128	SER	0	-0.040	-0.018	9.361	0.093	0.093	0.000	0.000	0.000	0.000
131	A	129	ALA	0	-0.039	-0.007	11.927	0.129	0.129	0.000	0.000	0.000	0.000
132	A	130	ASP	-1	-0.757	-0.876	11.553	-0.609	-0.609	0.000	0.000	0.000	0.000
133	A	131	PRO	0	-0.034	-0.031	8.803	-0.040	-0.040	0.000	0.000	0.000	0.000
134	A	132	ASP	-1	-0.854	-0.924	11.575	-0.554	-0.554	0.000	0.000	0.000	0.000
135	A	133	GLU	-1	-0.926	-0.958	14.897	-0.236	-0.236	0.000	0.000	0.000	0.000
136	A	134	LEU	0	0.004	0.020	13.490	0.032	0.032	0.000	0.000	0.000	0.000
137	A	135	PHE	0	-0.027	-0.020	15.065	0.012	0.012	0.000	0.000	0.000	0.000
138	A	136	GLU	-1	-0.750	-0.862	16.811	-0.361	-0.361	0.000	0.000	0.000	0.000
139	A	137	SER	0	-0.022	-0.015	19.638	0.046	0.046	0.000	0.000	0.000	0.000
140	A	138	ILE	0	-0.030	-0.023	17.002	0.025	0.025	0.000	0.000	0.000	0.000
141	A	139	PHE	0	0.007	-0.010	20.872	0.028	0.028	0.000	0.000	0.000	0.000
142	A	140	ASP	-1	-0.827	-0.908	22.598	-0.249	-0.249	0.000	0.000	0.000	0.000
143	A	141	ALA	0	0.005	0.009	23.981	0.021	0.021	0.000	0.000	0.000	0.000
144	A	142	ARG	1	0.774	0.867	22.197	0.493	0.493	0.000	0.000	0.000	0.000
145	A	143	ARG	1	0.781	0.867	26.029	0.297	0.297	0.000	0.000	0.000	0.000
146	A	144	GLU	-1	-0.860	-0.920	28.451	-0.234	-0.234	0.000	0.000	0.000	0.000
147	A	145	PHE	0	-0.007	-0.006	28.716	0.015	0.015	0.000	0.000	0.000	0.000
148	A	146	LEU	0	0.003	0.000	28.824	0.014	0.014	0.000	0.000	0.000	0.000
149	A	147	GLU	-1	-0.831	-0.917	32.000	-0.182	-0.182	0.000	0.000	0.000	0.000
150	A	148	ASP	-1	-0.826	-0.858	33.678	-0.182	-0.182	0.000	0.000	0.000	0.000
151	A	149	ILE	0	0.002	-0.004	32.822	0.016	0.016	0.000	0.000	0.000	0.000
152	A	150	THR	0	-0.034	-0.027	35.870	0.009	0.009	0.000	0.000	0.000	0.000
153	A	151	ALA	0	0.009	0.005	38.189	0.011	0.011	0.000	0.000	0.000	0.000
154	A	152	ARG	1	0.815	0.859	36.553	0.189	0.189	0.000	0.000	0.000	0.000
155	A	153	SER	0	-0.049	-0.002	40.295	0.006	0.006	0.000	0.000	0.000	0.000
156	A	154	ILE	0	0.010	-0.012	41.829	0.007	0.007	0.000	0.000	0.000	0.000
157	A	155	LYS	1	0.842	0.906	43.943	0.120	0.120	0.000	0.000	0.000	0.000
158	A	156	LYS	1	0.978	0.988	41.385	0.166	0.166	0.000	0.000	0.000	0.000
159	A	157	TYR	0	-0.023	-0.032	46.388	0.004	0.004	0.000	0.000	0.000	0.000
160	A	158	GLU	-1	-0.758	-0.880	48.333	-0.107	-0.107	0.000	0.000	0.000	0.000
161	A	159	ASP	-1	-0.814	-0.897	48.424	-0.108	-0.108	0.000	0.000	0.000	0.000
162	A	160	SER	0	-0.064	-0.030	50.617	0.003	0.003	0.000	0.000	0.000	0.000
163	A	161	ILE	0	-0.072	-0.022	52.364	0.003	0.003	0.000	0.000	0.000	0.000
164	A	162	GLY	0	-0.002	0.014	54.385	0.004	0.004	0.000	0.000	0.000	0.000
165	A	163	ARG	1	0.786	0.862	54.435	0.098	0.098	0.000	0.000	0.000	0.000
166	A	164	LYS	1	0.847	0.912	48.583	0.105	0.105	0.000	0.000	0.000	0.000
167	A	165	ALA	0	-0.006	0.005	49.597	0.003	0.003	0.000	0.000	0.000	0.000
168	A	166	THR	0	-0.025	-0.040	51.069	-0.001	-0.001	0.000	0.000	0.000	0.000
169	A	167	GLU	-1	-0.742	-0.865	45.935	-0.132	-0.132	0.000	0.000	0.000	0.000
170	A	168	ARG	1	0.941	0.963	48.188	0.098	0.098	0.000	0.000	0.000	0.000
171	A	169	GLU	-1	-0.746	-0.797	50.158	-0.104	-0.104	0.000	0.000	0.000	0.000
172	A	170	LEU	0	0.059	0.031	45.301	-0.005	-0.005	0.000	0.000	0.000	0.000
173	A	171	LEU	0	0.016	0.021	43.232	-0.008	-0.008	0.000	0.000	0.000	0.000
174	A	172	ARG	1	0.852	0.930	45.250	0.117	0.117	0.000	0.000	0.000	0.000
175	A	173	HIS	0	0.018	0.011	46.306	-0.007	-0.007	0.000	0.000	0.000	0.000
176	A	174	THR	0	-0.028	-0.016	43.249	-0.001	-0.001	0.000	0.000	0.000	0.000
177	A	175	ASN	0	0.045	-0.002	37.773	-0.001	-0.001	0.000	0.000	0.000	0.000
178	A	176	LYS	1	0.855	0.922	38.659	0.130	0.130	0.000	0.000	0.000	0.000
179	A	177	ARG	1	0.823	0.914	40.284	0.161	0.161	0.000	0.000	0.000	0.000
180	A	178	PHE	0	-0.001	-0.006	36.241	0.002	0.002	0.000	0.000	0.000	0.000
181	A	179	LEU	0	0.011	0.024	33.836	-0.010	-0.010	0.000	0.000	0.000	0.000
182	A	180	ARG	1	0.970	0.983	34.138	0.158	0.158	0.000	0.000	0.000	0.000
183	A	181	GLY	0	0.006	0.007	33.916	-0.005	-0.005	0.000	0.000	0.000	0.000
184	A	182	TRP	0	0.054	0.006	30.820	-0.014	-0.014	0.000	0.000	0.000	0.000
185	A	183	LEU	0	0.037	0.027	29.394	-0.023	-0.023	0.000	0.000	0.000	0.000
186	A	184	ASN	0	-0.024	-0.015	29.058	-0.011	-0.011	0.000	0.000	0.000	0.000
187	A	185	ARG	1	0.814	0.887	25.546	0.407	0.407	0.000	0.000	0.000	0.000
188	A	186	LEU	0	0.004	0.025	23.908	-0.032	-0.032	0.000	0.000	0.000	0.000
189	A	187	GLU	-1	-0.781	-0.884	24.174	-0.323	-0.323	0.000	0.000	0.000	0.000
190	A	188	ASP	-1	-0.826	-0.896	24.930	-0.349	-0.349	0.000	0.000	0.000	0.000
191	A	189	ILE	0	0.014	0.015	19.734	-0.018	-0.018	0.000	0.000	0.000	0.000
192	A	190	ARG	1	0.734	0.832	19.726	0.306	0.306	0.000	0.000	0.000	0.000
193	A	191	LYS	1	0.789	0.898	19.863	0.306	0.306	0.000	0.000	0.000	0.000
194	A	192	LEU	0	-0.026	0.015	16.731	0.009	0.009	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-1:ASN)