FMO DATABASE

FMODB ID: Q89LY

Calculation Name: 4HYN-A-Xray313

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4HYN

Chain ID: A

ChEMBL ID:

UniProt ID: G4FDE4

Base Structure: X-ray

Registration Date: 2021-09-06

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

DOI:

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. 1.20200116

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	202
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-2205861.848337
FMO2-HF: Nuclear repulsion	2126761.686656
FMO2-HF: Total energy	-79100.161681
FMO2-MP2: Total energy	-79324.360932

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:ALA )

Summations of interaction energy for fragment #1(A:1: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.
-5.366	-4.018	-0.002	-0.592	-0.753	0

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.081 / q_NPA : -0.062

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].
3	A	24	VAL	0	-0.045	-0.044	3.842	0.440	1.736	-0.002	-0.583	-0.710
4	A	25	LEU	0	-0.022	0.006	5.689	0.703	0.703	0.000	0.000	0.000
5	A	26	THR	0	-0.043	-0.025	9.035	0.240	0.240	0.000	0.000	0.000
6	A	27	PRO	0	-0.032	-0.044	10.751	-0.037	-0.037	0.000	0.000	0.000
7	A	28	GLU	-1	-0.857	-0.915	13.815	-0.085	-0.085	0.000	0.000	0.000
8	A	29	GLU	-1	-0.853	-0.929	11.287	-0.649	-0.649	0.000	0.000	0.000
9	A	30	LYS	1	0.864	0.934	9.301	0.444	0.444	0.000	0.000	0.000
10	A	31	ASP	-1	-0.877	-0.940	15.411	-0.050	-0.050	0.000	0.000	0.000
11	A	32	MET	0	-0.012	0.024	17.148	0.009	0.009	0.000	0.000	0.000
12	A	33	ILE	0	-0.061	-0.027	16.095	0.005	0.005	0.000	0.000	0.000
13	A	34	GLY	0	0.045	0.016	19.297	0.014	0.014	0.000	0.000	0.000
14	A	35	GLU	-1	-0.962	-0.976	21.424	-0.084	-0.084	0.000	0.000	0.000
15	A	36	ILE	0	-0.025	-0.022	21.850	0.010	0.010	0.000	0.000	0.000
16	A	37	GLY	0	0.004	0.009	23.253	0.004	0.004	0.000	0.000	0.000
17	A	38	ASN	0	-0.012	-0.031	24.378	0.017	0.017	0.000	0.000	0.000
18	A	39	ILE	0	-0.030	0.002	27.276	0.009	0.009	0.000	0.000	0.000
19	A	40	ALA	0	-0.006	-0.006	26.609	0.006	0.006	0.000	0.000	0.000
20	A	41	MET	0	0.004	-0.002	26.575	0.003	0.003	0.000	0.000	0.000
21	A	42	GLY	0	0.067	0.037	28.660	0.009	0.009	0.000	0.000	0.000
22	A	43	SER	0	-0.028	-0.021	31.317	0.011	0.011	0.000	0.000	0.000
23	A	44	ALA	0	-0.031	-0.021	31.006	0.005	0.005	0.000	0.000	0.000
24	A	45	ALA	0	0.030	0.017	32.498	0.004	0.004	0.000	0.000	0.000
25	A	46	THR	0	0.015	0.009	34.171	0.008	0.008	0.000	0.000	0.000
26	A	47	THR	0	-0.039	-0.019	36.175	0.005	0.005	0.000	0.000	0.000
27	A	48	LEU	0	-0.003	-0.003	35.156	0.004	0.004	0.000	0.000	0.000
28	A	49	SER	0	-0.030	-0.063	37.822	0.005	0.005	0.000	0.000	0.000
29	A	50	MET	0	-0.056	-0.019	39.821	0.004	0.004	0.000	0.000	0.000
30	A	51	ILE	0	-0.054	-0.014	39.599	0.002	0.002	0.000	0.000	0.000
31	A	52	LEU	0	-0.040	-0.014	39.168	0.003	0.003	0.000	0.000	0.000
32	A	53	GLY	0	-0.025	-0.012	43.129	0.001	0.001	0.000	0.000	0.000
33	A	54	ARG	1	0.863	0.927	41.375	0.046	0.046	0.000	0.000	0.000
34	A	55	ASP	-1	-0.871	-0.885	40.087	-0.046	-0.046	0.000	0.000	0.000
35	A	56	ILE	0	-0.058	-0.046	34.351	-0.001	-0.001	0.000	0.000	0.000
36	A	57	HIS	0	0.002	0.013	32.338	-0.005	-0.005	0.000	0.000	0.000
37	A	58	ILE	0	-0.015	-0.023	27.944	-0.003	-0.003	0.000	0.000	0.000
38	A	59	THR	0	0.013	0.021	26.153	0.004	0.004	0.000	0.000	0.000
39	A	60	VAL	0	-0.015	-0.008	21.100	-0.009	-0.009	0.000	0.000	0.000
40	A	61	PRO	0	-0.050	-0.010	22.413	0.003	0.003	0.000	0.000	0.000
41	A	62	THR	0	-0.001	0.001	16.612	0.017	0.017	0.000	0.000	0.000
42	A	63	VAL	0	0.022	0.015	14.474	-0.031	-0.031	0.000	0.000	0.000
43	A	64	ARG	1	0.831	0.899	11.534	0.248	0.248	0.000	0.000	0.000
44	A	65	GLU	-1	-0.784	-0.885	6.567	-2.369	-2.369	0.000	0.000	0.000
45	A	66	GLU	-1	-0.874	-0.926	8.257	-0.344	-0.344	0.000	0.000	0.000
46	A	67	LYS	1	0.948	0.977	4.342	0.465	0.517	0.000	-0.009	-0.043
47	A	68	MET	0	0.029	0.020	8.035	0.236	0.236	0.000	0.000	0.000
48	A	69	LYS	1	0.764	0.875	8.578	0.445	0.445	0.000	0.000	0.000
49	A	70	ASN	0	-0.032	-0.027	8.883	0.131	0.131	0.000	0.000	0.000
50	A	71	VAL	0	0.065	0.057	12.281	0.050	0.050	0.000	0.000	0.000
51	A	72	LYS	1	0.800	0.892	14.439	0.199	0.199	0.000	0.000	0.000
52	A	73	SER	0	-0.044	-0.024	14.967	0.028	0.028	0.000	0.000	0.000
53	A	74	ASP	-1	-0.900	-0.935	14.319	-0.242	-0.242	0.000	0.000	0.000
54	A	75	PHE	0	-0.077	-0.039	17.196	0.021	0.021	0.000	0.000	0.000
55	A	76	SER	0	-0.016	-0.009	20.810	0.003	0.003	0.000	0.000	0.000
56	A	77	GLY	0	0.047	0.028	23.861	-0.001	-0.001	0.000	0.000	0.000
57	A	78	GLU	-1	-0.923	-0.976	26.582	-0.092	-0.092	0.000	0.000	0.000
58	A	79	GLN	0	-0.043	-0.034	24.418	-0.002	-0.002	0.000	0.000	0.000
59	A	80	VAL	0	-0.006	0.001	28.047	-0.001	-0.001	0.000	0.000	0.000
60	A	81	VAL	0	-0.015	-0.004	23.800	-0.009	-0.009	0.000	0.000	0.000
61	A	82	VAL	0	0.015	0.000	26.341	0.008	0.008	0.000	0.000	0.000
62	A	83	SER	0	-0.025	-0.014	24.754	-0.016	-0.016	0.000	0.000	0.000
63	A	84	VAL	0	-0.001	-0.002	25.416	0.017	0.017	0.000	0.000	0.000
64	A	85	GLU	-1	-0.931	-0.980	23.868	-0.283	-0.283	0.000	0.000	0.000
65	A	86	TYR	0	-0.041	-0.025	22.436	0.026	0.026	0.000	0.000	0.000
66	A	87	THR	0	-0.020	-0.023	25.529	-0.011	-0.011	0.000	0.000	0.000
67	A	88	GLU	-1	-0.899	-0.957	27.792	-0.140	-0.140	0.000	0.000	0.000
68	A	89	GLY	0	0.057	0.040	26.559	0.008	0.008	0.000	0.000	0.000
69	A	90	LEU	0	-0.063	-0.053	21.107	-0.022	-0.022	0.000	0.000	0.000
70	A	91	GLU	-1	-0.943	-0.967	21.932	-0.243	-0.243	0.000	0.000	0.000
71	A	92	GLY	0	0.003	-0.002	20.155	-0.046	-0.046	0.000	0.000	0.000
72	A	93	LEU	0	-0.007	0.016	20.077	0.031	0.031	0.000	0.000	0.000
73	A	94	ASN	0	-0.012	-0.004	20.012	-0.052	-0.052	0.000	0.000	0.000
74	A	95	VAL	0	-0.007	-0.006	20.551	0.031	0.031	0.000	0.000	0.000
75	A	96	LEU	0	0.026	0.014	21.752	-0.011	-0.011	0.000	0.000	0.000
76	A	97	VAL	0	-0.038	-0.018	21.119	0.006	0.006	0.000	0.000	0.000
77	A	98	LEU	0	0.033	0.000	24.160	0.007	0.007	0.000	0.000	0.000
78	A	99	ASP	-1	-0.816	-0.914	27.349	-0.082	-0.082	0.000	0.000	0.000
79	A	100	LYS	1	0.921	0.951	28.785	0.084	0.084	0.000	0.000	0.000
80	A	101	LYS	1	0.928	0.974	32.150	0.054	0.054	0.000	0.000	0.000
81	A	102	LEU	0	0.032	0.037	29.216	0.003	0.003	0.000	0.000	0.000
82	A	103	VAL	0	-0.018	-0.014	31.277	0.002	0.002	0.000	0.000	0.000
83	A	104	ALA	0	-0.023	-0.016	33.785	0.003	0.003	0.000	0.000	0.000
84	A	105	VAL	0	-0.001	0.014	35.763	0.003	0.003	0.000	0.000	0.000
85	A	106	ILE	0	0.037	0.006	32.974	0.002	0.002	0.000	0.000	0.000
86	A	107	ALA	0	-0.022	-0.009	37.103	0.002	0.002	0.000	0.000	0.000
87	A	108	ASP	-1	-0.879	-0.957	39.257	-0.045	-0.045	0.000	0.000	0.000
88	A	109	LEU	0	-0.031	0.000	38.592	0.002	0.002	0.000	0.000	0.000
89	A	110	MET	0	-0.057	-0.019	39.111	0.001	0.001	0.000	0.000	0.000
90	A	111	MET	0	-0.093	-0.040	42.143	0.001	0.001	0.000	0.000	0.000
91	A	112	GLY	0	-0.046	-0.016	45.012	0.003	0.003	0.000	0.000	0.000
92	A	113	GLY	0	-0.014	0.008	45.545	0.003	0.003	0.000	0.000	0.000
93	A	114	SER	0	-0.043	-0.037	45.100	-0.001	-0.001	0.000	0.000	0.000
94	A	115	GLY	0	0.063	0.026	41.041	-0.001	-0.001	0.000	0.000	0.000
95	A	116	GLU	-1	-0.985	-0.996	40.159	-0.035	-0.035	0.000	0.000	0.000
96	A	117	VAL	0	-0.017	0.011	39.881	0.002	0.002	0.000	0.000	0.000
97	A	118	GLU	-1	-0.965	-0.996	40.181	-0.032	-0.032	0.000	0.000	0.000
98	A	119	THR	0	-0.046	-0.034	39.433	0.001	0.001	0.000	0.000	0.000
99	A	120	GLU	-1	-0.934	-0.976	33.027	-0.063	-0.063	0.000	0.000	0.000
100	A	121	GLU	-1	-0.930	-0.965	36.508	-0.054	-0.054	0.000	0.000	0.000
101	A	122	LEU	0	-0.028	-0.013	33.835	-0.001	-0.001	0.000	0.000	0.000
102	A	123	ASP	-1	-0.825	-0.920	38.608	-0.059	-0.059	0.000	0.000	0.000
103	A	124	GLU	-1	-0.891	-0.967	38.744	-0.084	-0.084	0.000	0.000	0.000
104	A	125	ILE	0	-0.048	-0.016	40.756	-0.002	-0.002	0.000	0.000	0.000
105	A	126	LYS	1	0.895	0.946	39.123	0.055	0.055	0.000	0.000	0.000
106	A	127	LEU	0	0.012	-0.009	34.948	-0.003	-0.003	0.000	0.000	0.000
107	A	128	SER	0	-0.047	-0.009	36.926	-0.006	-0.006	0.000	0.000	0.000
108	A	129	ALA	0	0.015	0.008	39.486	-0.002	-0.002	0.000	0.000	0.000
109	A	130	VAL	0	-0.003	-0.004	33.428	-0.001	-0.001	0.000	0.000	0.000
110	A	131	GLY	0	0.015	0.010	34.671	-0.006	-0.006	0.000	0.000	0.000
111	A	132	GLU	-1	-0.933	-0.961	35.755	-0.086	-0.086	0.000	0.000	0.000
112	A	133	ALA	0	0.022	0.011	35.779	-0.002	-0.002	0.000	0.000	0.000
113	A	134	MET	0	-0.042	-0.032	30.862	-0.007	-0.007	0.000	0.000	0.000
114	A	135	ASN	0	-0.041	-0.014	32.792	-0.010	-0.010	0.000	0.000	0.000
115	A	136	GLN	0	0.032	0.015	34.915	-0.005	-0.005	0.000	0.000	0.000
116	A	137	MET	0	-0.038	-0.004	31.688	-0.003	-0.003	0.000	0.000	0.000
117	A	138	MET	0	0.013	-0.008	26.471	-0.002	-0.002	0.000	0.000	0.000
118	A	139	GLY	0	0.044	0.034	30.655	-0.007	-0.007	0.000	0.000	0.000
119	A	140	SER	0	0.004	0.008	33.331	0.002	0.002	0.000	0.000	0.000
120	A	141	ALA	0	-0.002	0.009	28.014	0.000	0.000	0.000	0.000	0.000
121	A	142	ALA	0	0.034	0.015	28.567	-0.006	-0.006	0.000	0.000	0.000
122	A	143	THR	0	-0.019	-0.011	29.605	-0.001	-0.001	0.000	0.000	0.000
123	A	144	SER	0	-0.010	-0.002	30.488	0.001	0.001	0.000	0.000	0.000
124	A	145	LEU	0	0.023	0.004	23.763	0.000	0.000	0.000	0.000	0.000
125	A	146	SER	0	-0.024	-0.022	27.869	-0.005	-0.005	0.000	0.000	0.000
126	A	147	GLU	-1	-0.973	-0.984	29.786	-0.093	-0.093	0.000	0.000	0.000
127	A	148	LEU	0	-0.062	-0.023	25.877	0.004	0.004	0.000	0.000	0.000
128	A	149	LEU	0	-0.006	-0.029	23.012	0.001	0.001	0.000	0.000	0.000
129	A	150	GLY	0	-0.081	-0.016	26.968	0.000	0.000	0.000	0.000	0.000
130	A	151	ILE	0	-0.064	-0.035	26.141	0.002	0.002	0.000	0.000	0.000
131	A	152	THR	0	-0.012	-0.008	29.575	0.003	0.003	0.000	0.000	0.000
132	A	153	ILE	0	0.016	0.022	25.711	-0.010	-0.010	0.000	0.000	0.000
133	A	154	ASN	0	-0.039	-0.008	29.243	0.012	0.012	0.000	0.000	0.000
134	A	155	ILE	0	0.018	-0.004	28.015	-0.016	-0.016	0.000	0.000	0.000
135	A	156	SER	0	-0.023	0.008	29.111	0.012	0.012	0.000	0.000	0.000
136	A	157	PRO	0	-0.006	-0.017	31.364	0.000	0.000	0.000	0.000	0.000
137	A	158	PRO	0	0.034	0.019	30.434	-0.006	-0.006	0.000	0.000	0.000
138	A	159	LYS	1	0.926	0.979	27.679	0.184	0.184	0.000	0.000	0.000
139	A	160	VAL	0	-0.014	-0.010	29.628	-0.010	-0.010	0.000	0.000	0.000
140	A	161	GLU	-1	-0.922	-0.963	27.401	-0.157	-0.157	0.000	0.000	0.000
141	A	162	ILE	0	-0.035	-0.007	29.406	-0.004	-0.004	0.000	0.000	0.000
142	A	163	LEU	0	0.000	0.000	23.183	-0.001	-0.001	0.000	0.000	0.000
143	A	164	ASN	0	0.059	0.006	27.229	0.002	0.002	0.000	0.000	0.000
144	A	165	PHE	0	0.001	0.004	20.541	-0.009	-0.009	0.000	0.000	0.000
145	A	166	ASP	-1	-0.840	-0.918	23.646	-0.079	-0.079	0.000	0.000	0.000
146	A	167	ASP	-1	-0.939	-0.954	26.216	-0.089	-0.089	0.000	0.000	0.000
147	A	168	PRO	0	-0.037	-0.024	23.864	-0.014	-0.014	0.000	0.000	0.000
148	A	169	ASN	0	-0.057	-0.036	23.638	-0.011	-0.011	0.000	0.000	0.000
149	A	170	THR	0	-0.031	0.000	24.677	-0.015	-0.015	0.000	0.000	0.000
150	A	171	GLN	0	-0.019	-0.016	20.682	-0.025	-0.025	0.000	0.000	0.000
151	A	172	PHE	0	0.037	0.021	18.071	0.011	0.011	0.000	0.000	0.000
152	A	173	PRO	0	0.040	0.019	19.987	-0.015	-0.015	0.000	0.000	0.000
153	A	174	PRO	0	0.007	-0.001	18.329	-0.033	-0.033	0.000	0.000	0.000
154	A	175	VAL	0	-0.011	0.007	15.761	-0.010	-0.010	0.000	0.000	0.000
155	A	176	THR	0	0.007	0.003	11.838	-0.018	-0.018	0.000	0.000	0.000
156	A	177	ASP	-1	-0.859	-0.928	14.873	-0.499	-0.499	0.000	0.000	0.000
157	A	178	ASN	0	-0.043	-0.034	11.110	-0.042	-0.042	0.000	0.000	0.000
158	A	179	PRO	0	0.035	0.006	11.671	-0.101	-0.101	0.000	0.000	0.000
159	A	180	GLU	-1	-0.848	-0.938	7.048	-0.645	-0.645	0.000	0.000	0.000
160	A	181	LYS	1	0.851	0.939	6.584	0.336	0.336	0.000	0.000	0.000
161	A	182	ASP	-1	-0.826	-0.930	5.567	-3.402	-3.402	0.000	0.000	0.000
162	A	183	VAL	0	-0.038	-0.014	8.413	0.250	0.250	0.000	0.000	0.000
163	A	184	ALA	0	0.005	0.008	10.720	-0.099	-0.099	0.000	0.000	0.000
164	A	185	VAL	0	0.003	-0.006	13.294	0.062	0.062	0.000	0.000	0.000
165	A	186	VAL	0	-0.019	-0.023	15.437	0.024	0.024	0.000	0.000	0.000
166	A	187	GLU	-1	-0.927	-0.971	18.368	-0.087	-0.087	0.000	0.000	0.000
167	A	188	PHE	0	-0.005	-0.006	20.958	0.005	0.005	0.000	0.000	0.000
168	A	189	GLU	-1	-0.941	-0.986	24.593	-0.046	-0.046	0.000	0.000	0.000
169	A	190	MET	0	-0.017	-0.016	27.395	-0.002	-0.002	0.000	0.000	0.000
170	A	191	GLU	-1	-0.948	-0.979	30.814	-0.038	-0.038	0.000	0.000	0.000
171	A	192	ILE	0	0.039	0.018	34.178	-0.001	-0.001	0.000	0.000	0.000
172	A	193	GLU	-1	-0.860	-0.938	37.237	-0.033	-0.033	0.000	0.000	0.000
173	A	194	GLY	0	-0.040	-0.024	40.642	0.000	0.000	0.000	0.000	0.000
174	A	195	LEU	0	-0.021	0.005	38.207	0.001	0.001	0.000	0.000	0.000
175	A	196	PRO	0	-0.059	-0.027	35.567	0.001	0.001	0.000	0.000	0.000
176	A	197	LYS	1	0.944	0.977	30.992	0.028	0.028	0.000	0.000	0.000
177	A	198	SER	0	-0.036	0.002	30.558	-0.001	-0.001	0.000	0.000	0.000
178	A	199	LYS	1	0.952	0.969	23.713	0.089	0.089	0.000	0.000	0.000
179	A	200	PHE	0	-0.009	0.006	25.160	0.001	0.001	0.000	0.000	0.000
180	A	201	TYR	0	0.023	0.009	19.467	0.005	0.005	0.000	0.000	0.000
181	A	202	GLN	0	0.032	0.030	19.831	0.016	0.016	0.000	0.000	0.000
182	A	203	VAL	0	-0.041	-0.009	15.965	-0.022	-0.022	0.000	0.000	0.000
183	A	204	ILE	0	0.039	0.021	16.445	0.024	0.024	0.000	0.000	0.000
184	A	205	SER	0	0.057	0.021	13.688	-0.079	-0.079	0.000	0.000	0.000
185	A	206	ALA	0	0.038	0.008	10.044	0.062	0.062	0.000	0.000	0.000
186	A	207	ASP	-1	-0.963	-0.983	11.954	-0.801	-0.801	0.000	0.000	0.000
187	A	208	LEU	0	0.005	0.000	13.763	0.081	0.081	0.000	0.000	0.000
188	A	209	VAL	0	0.005	0.011	13.685	0.063	0.063	0.000	0.000	0.000
189	A	210	LYS	1	1.018	1.016	11.666	0.758	0.758	0.000	0.000	0.000
190	A	211	LYS	1	0.871	0.956	14.418	0.366	0.366	0.000	0.000	0.000
191	A	212	MET	0	-0.014	-0.021	17.851	0.046	0.046	0.000	0.000	0.000
192	A	213	TYR	0	0.079	0.022	15.777	0.044	0.044	0.000	0.000	0.000
193	A	214	GLU	-1	-0.947	-0.968	17.071	-0.313	-0.313	0.000	0.000	0.000
194	A	215	TYR	0	-0.091	-0.050	19.617	0.036	0.036	0.000	0.000	0.000
195	A	216	PHE	0	0.019	0.005	20.657	0.020	0.020	0.000	0.000	0.000
196	A	217	THR	0	-0.003	-0.018	18.925	0.025	0.025	0.000	0.000	0.000
197	A	218	LYS	1	0.895	0.959	21.969	0.149	0.149	0.000	0.000	0.000
198	A	219	LYS	1	0.931	0.959	24.742	0.127	0.127	0.000	0.000	0.000
199	A	220	GLN	0	0.002	0.020	22.462	0.005	0.005	0.000	0.000	0.000
200	A	221	SER	0	-0.076	-0.038	24.556	0.016	0.016	0.000	0.000	0.000
201	A	222	GLU	-1	-1.063	-1.020	27.052	-0.087	-0.087	0.000	0.000	0.000
202	A	223	ALA	-1	-0.945	-0.964	30.400	-0.048	-0.048	0.000	0.000	0.000

Top

Graph

Manual

About

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