FMO DATABASE

FMODB ID: 5JR5Z

Calculation Name: 2AR7-A-Xray372

Preferred Name: Adenylate kinase 4

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 2AR7

Chain ID: A

ChEMBL ID: CHEMBL4926

UniProt ID: P27144

Base Structure: X-ray

Registration Date: 2023-09-22

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

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

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	221
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2551453.700368
FMO2-HF: Nuclear repulsion	2464371.934081
FMO2-HF: Total energy	-87081.766287
FMO2-MP2: Total energy	-87339.025555

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:4:LYS)

Summations of interaction energy for fragment #1(A:4:LYS)

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.
6.045	8.67	0	-1.292	-1.334	0.004

Interaction energy analysis for fragmet #1(A:4:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 1.029 / q_NPA : 1.022

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	6	LEU	0	0.034	0.024	3.623	1.686	4.129	0.001	-1.256	-1.189	0.004
4	A	7	ARG	1	0.794	0.911	5.785	36.511	36.511	0.000	0.000	0.000	0.000
5	A	8	ALA	0	0.029	0.007	8.167	1.522	1.522	0.000	0.000	0.000	0.000
6	A	9	VAL	0	-0.008	0.010	11.162	0.412	0.412	0.000	0.000	0.000	0.000
7	A	10	ILE	0	0.011	0.004	14.839	0.544	0.544	0.000	0.000	0.000	0.000
8	A	11	LEU	0	0.000	-0.001	17.931	0.418	0.418	0.000	0.000	0.000	0.000
9	A	12	GLY	0	0.023	-0.005	21.125	0.075	0.075	0.000	0.000	0.000	0.000
10	A	13	PRO	0	-0.007	0.019	24.629	-0.079	-0.079	0.000	0.000	0.000	0.000
11	A	14	PRO	0	0.021	0.005	28.283	-0.176	-0.176	0.000	0.000	0.000	0.000
12	A	15	GLY	0	0.028	0.019	30.000	0.230	0.230	0.000	0.000	0.000	0.000
13	A	16	SER	0	-0.035	-0.024	26.344	-0.049	-0.049	0.000	0.000	0.000	0.000
14	A	17	GLY	0	0.031	0.012	26.615	-0.047	-0.047	0.000	0.000	0.000	0.000
15	A	18	LYS	1	0.898	0.942	21.803	12.477	12.477	0.000	0.000	0.000	0.000
16	A	19	GLY	0	0.052	0.041	21.918	-0.577	-0.577	0.000	0.000	0.000	0.000
17	A	20	THR	0	-0.009	-0.007	23.454	-0.287	-0.287	0.000	0.000	0.000	0.000
18	A	21	VAL	0	0.004	-0.008	19.567	-0.278	-0.278	0.000	0.000	0.000	0.000
19	A	22	CYS	0	-0.020	-0.002	18.583	-0.715	-0.715	0.000	0.000	0.000	0.000
20	A	23	GLN	0	0.042	0.029	18.889	-0.479	-0.479	0.000	0.000	0.000	0.000
21	A	24	ARG	1	0.870	0.931	20.991	12.129	12.129	0.000	0.000	0.000	0.000
22	A	25	ILE	0	0.004	0.016	14.854	-0.176	-0.176	0.000	0.000	0.000	0.000
23	A	26	ALA	0	-0.027	-0.006	16.236	-0.978	-0.978	0.000	0.000	0.000	0.000
24	A	27	GLN	0	-0.008	-0.006	16.749	-0.192	-0.192	0.000	0.000	0.000	0.000
25	A	28	ASN	0	-0.044	-0.034	18.136	0.060	0.060	0.000	0.000	0.000	0.000
26	A	29	PHE	0	-0.027	-0.021	12.393	0.065	0.065	0.000	0.000	0.000	0.000
27	A	30	GLY	0	0.018	0.028	12.738	-1.854	-1.854	0.000	0.000	0.000	0.000
28	A	31	LEU	0	-0.055	-0.015	10.672	-1.699	-1.699	0.000	0.000	0.000	0.000
29	A	32	GLN	0	0.067	0.026	13.296	0.802	0.802	0.000	0.000	0.000	0.000
30	A	33	HIS	0	-0.066	-0.059	15.296	-0.405	-0.405	0.000	0.000	0.000	0.000
31	A	34	LEU	0	-0.020	0.012	13.678	0.615	0.615	0.000	0.000	0.000	0.000
32	A	35	SER	0	0.046	0.008	18.299	0.483	0.483	0.000	0.000	0.000	0.000
33	A	36	SER	0	0.097	0.040	21.150	-0.003	-0.003	0.000	0.000	0.000	0.000
34	A	37	GLY	0	-0.032	-0.013	23.398	0.312	0.312	0.000	0.000	0.000	0.000
35	A	38	HIS	0	-0.059	-0.038	21.542	0.735	0.735	0.000	0.000	0.000	0.000
36	A	39	PHE	0	0.084	0.023	17.529	0.151	0.151	0.000	0.000	0.000	0.000
37	A	40	LEU	0	-0.004	0.021	23.456	0.261	0.261	0.000	0.000	0.000	0.000
38	A	41	ARG	1	0.970	0.979	26.871	11.760	11.760	0.000	0.000	0.000	0.000
39	A	42	GLU	-1	-0.887	-0.926	22.058	-14.208	-14.208	0.000	0.000	0.000	0.000
40	A	43	ASN	0	0.016	0.001	23.144	0.442	0.442	0.000	0.000	0.000	0.000
41	A	44	ILE	0	-0.015	-0.002	27.035	0.245	0.245	0.000	0.000	0.000	0.000
42	A	45	LYS	1	0.854	0.932	26.643	12.033	12.033	0.000	0.000	0.000	0.000
43	A	46	ALA	0	-0.070	-0.046	27.483	0.188	0.188	0.000	0.000	0.000	0.000
44	A	47	SER	0	-0.001	0.003	29.452	0.034	0.034	0.000	0.000	0.000	0.000
45	A	48	THR	0	-0.013	-0.018	25.747	0.228	0.228	0.000	0.000	0.000	0.000
46	A	49	GLU	-1	-0.789	-0.885	28.876	-10.451	-10.451	0.000	0.000	0.000	0.000
47	A	50	VAL	0	0.008	-0.013	25.807	0.304	0.304	0.000	0.000	0.000	0.000
48	A	51	GLY	0	0.016	0.013	28.917	0.159	0.159	0.000	0.000	0.000	0.000
49	A	52	GLU	-1	-0.817	-0.905	29.969	-8.893	-8.893	0.000	0.000	0.000	0.000
50	A	53	MET	0	-0.066	-0.029	31.759	0.197	0.197	0.000	0.000	0.000	0.000
51	A	54	ALA	0	-0.003	-0.008	30.482	0.259	0.259	0.000	0.000	0.000	0.000
52	A	55	LYS	1	0.898	0.936	32.622	8.606	8.606	0.000	0.000	0.000	0.000
53	A	56	GLN	0	0.052	0.032	35.194	0.504	0.504	0.000	0.000	0.000	0.000
54	A	57	TYR	0	-0.006	-0.009	33.897	0.107	0.107	0.000	0.000	0.000	0.000
55	A	58	ILE	0	-0.035	-0.001	33.040	0.176	0.176	0.000	0.000	0.000	0.000
56	A	59	GLU	-1	-0.852	-0.915	37.201	-7.993	-7.993	0.000	0.000	0.000	0.000
57	A	60	LYS	1	0.863	0.933	40.233	8.016	8.016	0.000	0.000	0.000	0.000
58	A	61	SER	0	-0.060	-0.045	38.237	0.121	0.121	0.000	0.000	0.000	0.000
59	A	62	LEU	0	-0.011	0.012	38.582	-0.008	-0.008	0.000	0.000	0.000	0.000
60	A	63	LEU	0	-0.004	-0.009	33.283	-0.138	-0.138	0.000	0.000	0.000	0.000
61	A	64	VAL	0	-0.018	0.000	29.881	0.021	0.021	0.000	0.000	0.000	0.000
62	A	65	PRO	0	0.021	0.019	31.252	-0.160	-0.160	0.000	0.000	0.000	0.000
63	A	66	ASP	-1	-0.697	-0.830	27.138	-11.206	-11.206	0.000	0.000	0.000	0.000
64	A	67	HIS	0	0.047	0.034	26.289	-0.611	-0.611	0.000	0.000	0.000	0.000
65	A	68	VAL	0	0.011	0.011	26.769	-0.367	-0.367	0.000	0.000	0.000	0.000
66	A	69	ILE	0	-0.001	-0.001	23.591	-0.482	-0.482	0.000	0.000	0.000	0.000
67	A	70	THR	0	-0.032	-0.043	21.611	-0.653	-0.653	0.000	0.000	0.000	0.000
68	A	71	ARG	1	0.826	0.905	21.953	10.777	10.777	0.000	0.000	0.000	0.000
69	A	72	LEU	0	0.006	0.003	22.520	-0.465	-0.465	0.000	0.000	0.000	0.000
70	A	73	MET	0	-0.004	0.008	18.085	-0.387	-0.387	0.000	0.000	0.000	0.000
71	A	74	MET	0	-0.003	0.008	16.818	-1.132	-1.132	0.000	0.000	0.000	0.000
72	A	75	SER	0	-0.019	0.001	17.370	-0.733	-0.733	0.000	0.000	0.000	0.000
73	A	76	GLU	-1	-0.792	-0.885	17.619	-16.766	-16.766	0.000	0.000	0.000	0.000
74	A	77	LEU	0	-0.037	-0.027	13.876	-1.022	-1.022	0.000	0.000	0.000	0.000
75	A	78	GLU	-1	-0.770	-0.848	12.641	-24.407	-24.407	0.000	0.000	0.000	0.000
76	A	79	ASN	0	-0.090	-0.040	12.787	-1.407	-1.407	0.000	0.000	0.000	0.000
77	A	80	ARG	1	0.820	0.893	10.989	19.073	19.073	0.000	0.000	0.000	0.000
78	A	81	ARG	1	0.853	0.904	8.332	22.790	22.790	0.000	0.000	0.000	0.000
79	A	82	GLY	0	-0.022	-0.001	5.002	-4.943	-4.943	0.000	0.000	0.000	0.000
80	A	83	GLN	0	-0.006	-0.007	5.540	-2.633	-2.633	0.000	0.000	0.000	0.000
81	A	84	HIS	0	0.047	0.044	4.599	-1.051	-0.869	-0.001	-0.036	-0.145	0.000
82	A	85	TRP	0	-0.030	-0.043	8.077	3.350	3.350	0.000	0.000	0.000	0.000
83	A	86	LEU	0	0.023	0.011	10.804	-0.066	-0.066	0.000	0.000	0.000	0.000
84	A	87	LEU	0	-0.022	-0.011	13.582	1.011	1.011	0.000	0.000	0.000	0.000
85	A	88	ASP	-1	-0.738	-0.872	15.941	-13.250	-13.250	0.000	0.000	0.000	0.000
86	A	89	GLY	0	-0.104	-0.076	19.354	0.469	0.469	0.000	0.000	0.000	0.000
87	A	90	PHE	0	-0.002	0.015	17.578	0.720	0.720	0.000	0.000	0.000	0.000
88	A	91	PRO	0	0.024	0.012	16.770	-0.774	-0.774	0.000	0.000	0.000	0.000
89	A	92	ARG	1	0.852	0.872	19.824	11.127	11.127	0.000	0.000	0.000	0.000
90	A	93	THR	0	0.006	0.005	23.464	0.232	0.232	0.000	0.000	0.000	0.000
91	A	94	LEU	0	0.073	0.018	21.939	-0.487	-0.487	0.000	0.000	0.000	0.000
92	A	95	GLY	0	0.059	0.042	22.106	-0.337	-0.337	0.000	0.000	0.000	0.000
93	A	96	GLN	0	-0.069	-0.047	21.056	-0.573	-0.573	0.000	0.000	0.000	0.000
94	A	97	ALA	0	0.018	0.002	18.068	-0.715	-0.715	0.000	0.000	0.000	0.000
95	A	98	GLU	-1	-0.850	-0.921	17.391	-12.730	-12.730	0.000	0.000	0.000	0.000
96	A	99	ALA	0	-0.110	-0.050	18.400	-0.426	-0.426	0.000	0.000	0.000	0.000
97	A	100	LEU	0	0.038	0.007	13.317	-0.650	-0.650	0.000	0.000	0.000	0.000
98	A	101	ASP	-1	-0.735	-0.837	13.516	-17.841	-17.841	0.000	0.000	0.000	0.000
99	A	102	LYS	1	0.852	0.925	13.793	13.795	13.795	0.000	0.000	0.000	0.000
100	A	103	ILE	0	-0.045	-0.014	13.163	-0.294	-0.294	0.000	0.000	0.000	0.000
101	A	104	CYS	0	-0.149	-0.063	8.772	-2.437	-2.437	0.000	0.000	0.000	0.000
102	A	105	GLU	-1	-0.805	-0.905	7.139	-18.394	-18.394	0.000	0.000	0.000	0.000
103	A	106	VAL	0	-0.030	-0.019	7.348	-2.124	-2.124	0.000	0.000	0.000	0.000
104	A	107	ASP	-1	-0.786	-0.896	5.207	-31.552	-31.552	0.000	0.000	0.000	0.000
105	A	108	LEU	0	-0.074	-0.047	8.367	1.040	1.040	0.000	0.000	0.000	0.000
106	A	109	VAL	0	0.017	0.023	11.034	-0.140	-0.140	0.000	0.000	0.000	0.000
107	A	110	ILE	0	0.036	0.022	14.710	0.681	0.681	0.000	0.000	0.000	0.000
108	A	111	SER	0	-0.043	-0.012	17.354	0.323	0.323	0.000	0.000	0.000	0.000
109	A	112	LEU	0	-0.003	-0.015	20.955	0.239	0.239	0.000	0.000	0.000	0.000
110	A	113	ASN	0	-0.023	-0.017	23.784	0.466	0.466	0.000	0.000	0.000	0.000
111	A	114	ILE	0	0.020	-0.001	26.612	0.188	0.188	0.000	0.000	0.000	0.000
112	A	115	PRO	0	0.036	0.027	29.371	0.128	0.128	0.000	0.000	0.000	0.000
113	A	116	PHE	0	0.052	0.018	32.503	-0.014	-0.014	0.000	0.000	0.000	0.000
114	A	117	GLU	-1	-0.783	-0.886	35.282	-7.170	-7.170	0.000	0.000	0.000	0.000
115	A	118	THR	0	-0.002	0.000	33.155	0.020	0.020	0.000	0.000	0.000	0.000
116	A	119	LEU	0	-0.031	-0.023	31.403	0.009	0.009	0.000	0.000	0.000	0.000
117	A	120	LYS	1	0.823	0.908	35.434	7.129	7.129	0.000	0.000	0.000	0.000
118	A	121	ASP	-1	-0.861	-0.930	38.926	-7.123	-7.123	0.000	0.000	0.000	0.000
119	A	122	ARG	1	0.851	0.928	33.119	8.654	8.654	0.000	0.000	0.000	0.000
120	A	123	LEU	0	-0.006	-0.012	37.172	0.057	0.057	0.000	0.000	0.000	0.000
121	A	124	SER	0	-0.011	-0.002	40.470	0.183	0.183	0.000	0.000	0.000	0.000
122	A	125	ARG	1	0.860	0.894	42.807	6.936	6.936	0.000	0.000	0.000	0.000
123	A	126	ARG	1	0.834	0.905	38.741	7.687	7.687	0.000	0.000	0.000	0.000
124	A	127	TRP	0	-0.030	-0.011	44.007	0.166	0.166	0.000	0.000	0.000	0.000
125	A	128	ILE	0	-0.006	-0.005	44.941	-0.145	-0.145	0.000	0.000	0.000	0.000
126	A	129	HIS	0	0.060	0.041	47.701	0.022	0.022	0.000	0.000	0.000	0.000
127	A	130	PRO	0	-0.022	-0.021	49.603	-0.088	-0.088	0.000	0.000	0.000	0.000
128	A	131	PRO	0	-0.016	-0.001	50.228	-0.086	-0.086	0.000	0.000	0.000	0.000
129	A	132	SER	0	-0.022	-0.038	49.403	-0.093	-0.093	0.000	0.000	0.000	0.000
130	A	133	GLY	0	0.003	0.012	46.044	-0.142	-0.142	0.000	0.000	0.000	0.000
131	A	134	ARG	1	0.798	0.875	44.810	6.241	6.241	0.000	0.000	0.000	0.000
132	A	135	VAL	0	0.008	0.000	40.960	0.081	0.081	0.000	0.000	0.000	0.000
133	A	136	TYR	0	0.010	-0.006	43.818	-0.106	-0.106	0.000	0.000	0.000	0.000
134	A	137	ASN	0	-0.042	-0.034	39.553	0.131	0.131	0.000	0.000	0.000	0.000
135	A	138	LEU	0	0.027	0.006	42.724	-0.030	-0.030	0.000	0.000	0.000	0.000
136	A	139	ASP	-1	-0.853	-0.883	40.991	-6.997	-6.997	0.000	0.000	0.000	0.000
137	A	140	PHE	0	-0.106	-0.059	36.409	-0.209	-0.209	0.000	0.000	0.000	0.000
138	A	141	ASN	0	-0.043	-0.028	40.755	-0.091	-0.091	0.000	0.000	0.000	0.000
139	A	142	PRO	0	0.018	0.016	43.036	0.058	0.058	0.000	0.000	0.000	0.000
140	A	143	PRO	0	0.011	0.017	46.462	-0.046	-0.046	0.000	0.000	0.000	0.000
141	A	144	HIS	0	-0.051	-0.030	48.321	0.139	0.139	0.000	0.000	0.000	0.000
142	A	145	VAL	0	-0.011	-0.001	51.680	0.100	0.100	0.000	0.000	0.000	0.000
143	A	146	HIS	0	0.010	-0.005	52.997	-0.025	-0.025	0.000	0.000	0.000	0.000
144	A	147	GLY	0	0.001	0.001	52.870	0.095	0.095	0.000	0.000	0.000	0.000
145	A	148	ILE	0	-0.032	-0.007	53.912	0.042	0.042	0.000	0.000	0.000	0.000
146	A	149	ASP	-1	-0.729	-0.802	50.921	-6.399	-6.399	0.000	0.000	0.000	0.000
147	A	150	ASP	-1	-0.817	-0.913	48.954	-6.374	-6.374	0.000	0.000	0.000	0.000
148	A	151	VAL	0	-0.085	-0.038	50.785	0.064	0.064	0.000	0.000	0.000	0.000
149	A	152	THR	0	-0.018	-0.041	53.550	0.108	0.108	0.000	0.000	0.000	0.000
150	A	153	GLY	0	0.008	0.017	55.652	0.117	0.117	0.000	0.000	0.000	0.000
151	A	154	GLU	-1	-0.877	-0.925	55.807	-5.602	-5.602	0.000	0.000	0.000	0.000
152	A	155	PRO	0	-0.005	-0.016	55.232	-0.099	-0.099	0.000	0.000	0.000	0.000
153	A	156	LEU	0	-0.028	0.007	49.446	-0.090	-0.090	0.000	0.000	0.000	0.000
154	A	157	VAL	0	-0.028	-0.018	50.459	0.106	0.106	0.000	0.000	0.000	0.000
155	A	158	GLN	0	-0.041	-0.022	46.930	-0.064	-0.064	0.000	0.000	0.000	0.000
156	A	159	GLN	0	-0.004	-0.010	43.356	0.182	0.182	0.000	0.000	0.000	0.000
157	A	160	GLU	-1	-0.898	-0.975	46.320	-6.492	-6.492	0.000	0.000	0.000	0.000
158	A	161	ASP	-1	-0.861	-0.930	41.762	-7.413	-7.413	0.000	0.000	0.000	0.000
159	A	162	ASP	-1	-0.802	-0.866	40.977	-7.678	-7.678	0.000	0.000	0.000	0.000
160	A	163	LYS	1	0.903	0.967	42.612	6.363	6.363	0.000	0.000	0.000	0.000
161	A	164	PRO	0	0.028	-0.006	41.981	-0.140	-0.140	0.000	0.000	0.000	0.000
162	A	165	GLU	-1	-0.837	-0.927	41.682	-7.088	-7.088	0.000	0.000	0.000	0.000
163	A	166	ALA	0	0.037	0.033	42.339	-0.103	-0.103	0.000	0.000	0.000	0.000
164	A	167	VAL	0	-0.033	-0.020	37.185	-0.236	-0.236	0.000	0.000	0.000	0.000
165	A	168	ALA	0	-0.007	-0.009	37.336	-0.265	-0.265	0.000	0.000	0.000	0.000
166	A	169	ALA	0	-0.022	-0.002	37.738	-0.161	-0.161	0.000	0.000	0.000	0.000
167	A	170	ARG	1	0.886	0.933	35.816	7.653	7.653	0.000	0.000	0.000	0.000
168	A	171	LEU	0	-0.057	-0.022	31.434	-0.326	-0.326	0.000	0.000	0.000	0.000
169	A	172	ARG	1	0.930	0.962	32.872	7.168	7.168	0.000	0.000	0.000	0.000
170	A	173	GLN	0	0.062	0.042	33.909	-0.136	-0.136	0.000	0.000	0.000	0.000
171	A	174	TYR	0	-0.011	-0.006	24.734	-0.324	-0.324	0.000	0.000	0.000	0.000
172	A	175	LYS	1	0.883	0.911	29.029	9.051	9.051	0.000	0.000	0.000	0.000
173	A	176	ASP	-1	-0.889	-0.925	29.378	-8.726	-8.726	0.000	0.000	0.000	0.000
174	A	177	VAL	0	-0.073	-0.026	27.093	-0.139	-0.139	0.000	0.000	0.000	0.000
175	A	178	ALA	0	-0.009	-0.012	25.128	-0.316	-0.316	0.000	0.000	0.000	0.000
176	A	179	LYS	1	0.904	0.951	24.480	9.189	9.189	0.000	0.000	0.000	0.000
177	A	180	PRO	0	0.028	0.004	25.065	-0.229	-0.229	0.000	0.000	0.000	0.000
178	A	181	VAL	0	0.034	0.031	19.670	-0.301	-0.301	0.000	0.000	0.000	0.000
179	A	182	ILE	0	-0.050	-0.025	20.246	-0.466	-0.466	0.000	0.000	0.000	0.000
180	A	183	GLU	-1	-0.794	-0.890	20.993	-10.700	-10.700	0.000	0.000	0.000	0.000
181	A	184	LEU	0	0.010	0.021	18.120	-0.040	-0.040	0.000	0.000	0.000	0.000
182	A	185	TYR	0	0.004	-0.019	14.131	-0.183	-0.183	0.000	0.000	0.000	0.000
183	A	186	LYS	1	0.834	0.901	16.989	10.603	10.603	0.000	0.000	0.000	0.000
184	A	187	SER	0	-0.097	-0.049	19.155	-0.063	-0.063	0.000	0.000	0.000	0.000
185	A	188	ARG	1	0.810	0.880	13.104	16.534	16.534	0.000	0.000	0.000	0.000
186	A	189	GLY	0	0.007	0.022	14.439	-0.609	-0.609	0.000	0.000	0.000	0.000
187	A	190	VAL	0	-0.004	-0.001	11.234	-0.356	-0.356	0.000	0.000	0.000	0.000
188	A	191	LEU	0	-0.080	-0.027	13.486	-0.313	-0.313	0.000	0.000	0.000	0.000
189	A	192	HIS	0	0.008	0.009	13.757	0.972	0.972	0.000	0.000	0.000	0.000
190	A	193	GLN	0	-0.002	-0.022	18.063	0.147	0.147	0.000	0.000	0.000	0.000
191	A	194	PHE	0	-0.006	0.016	21.593	0.270	0.270	0.000	0.000	0.000	0.000
192	A	195	SER	0	-0.005	-0.018	23.595	0.199	0.199	0.000	0.000	0.000	0.000
193	A	196	GLY	0	0.011	0.016	26.899	0.337	0.337	0.000	0.000	0.000	0.000
194	A	197	THR	0	0.058	0.011	28.802	-0.109	-0.109	0.000	0.000	0.000	0.000
195	A	198	GLU	-1	-0.861	-0.926	30.192	-9.041	-9.041	0.000	0.000	0.000	0.000
196	A	199	THR	0	0.076	0.021	28.818	-0.202	-0.202	0.000	0.000	0.000	0.000
197	A	200	ASN	0	-0.010	-0.004	28.018	-0.255	-0.255	0.000	0.000	0.000	0.000
198	A	201	LYS	1	0.897	0.951	26.287	9.349	9.349	0.000	0.000	0.000	0.000
199	A	202	ILE	0	-0.005	0.005	23.062	-0.375	-0.375	0.000	0.000	0.000	0.000
200	A	203	TRP	0	-0.010	-0.007	19.956	-0.461	-0.461	0.000	0.000	0.000	0.000
201	A	204	PRO	0	0.050	0.024	20.971	-0.549	-0.549	0.000	0.000	0.000	0.000
202	A	205	TYR	0	0.025	0.022	19.813	-0.605	-0.605	0.000	0.000	0.000	0.000
203	A	206	VAL	0	0.021	0.002	16.753	-0.493	-0.493	0.000	0.000	0.000	0.000
204	A	207	TYR	0	0.008	0.000	16.198	-1.004	-1.004	0.000	0.000	0.000	0.000
205	A	208	THR	0	-0.002	-0.019	15.893	-0.872	-0.872	0.000	0.000	0.000	0.000
206	A	209	LEU	0	0.004	0.016	13.932	-0.742	-0.742	0.000	0.000	0.000	0.000
207	A	210	PHE	0	-0.003	-0.010	11.414	-1.106	-1.106	0.000	0.000	0.000	0.000
208	A	211	SER	0	-0.047	-0.024	11.065	-1.235	-1.235	0.000	0.000	0.000	0.000
209	A	212	ASN	0	-0.040	-0.012	11.207	-0.140	-0.140	0.000	0.000	0.000	0.000
210	A	213	LYS	1	0.842	0.943	6.184	24.119	24.119	0.000	0.000	0.000	0.000
211	A	214	ILE	0	-0.008	-0.006	5.819	-3.104	-3.104	0.000	0.000	0.000	0.000
212	A	215	THR	0	0.037	0.010	8.962	1.586	1.586	0.000	0.000	0.000	0.000
213	A	216	PRO	0	-0.032	-0.011	11.739	-0.746	-0.746	0.000	0.000	0.000	0.000
214	A	217	ILE	0	0.023	0.004	13.838	-0.171	-0.171	0.000	0.000	0.000	0.000
215	A	218	GLN	0	-0.044	-0.030	17.007	0.482	0.482	0.000	0.000	0.000	0.000
216	A	219	SER	0	0.036	0.033	19.793	0.501	0.501	0.000	0.000	0.000	0.000
217	A	220	LYS	1	0.936	0.981	22.386	11.216	11.216	0.000	0.000	0.000	0.000
218	A	221	GLU	-1	-0.910	-0.972	24.205	-11.831	-11.831	0.000	0.000	0.000	0.000
219	A	222	ALA	0	0.032	0.037	21.947	-0.004	-0.004	0.000	0.000	0.000	0.000
220	A	223	TYR	0	-0.038	-0.036	21.024	0.334	0.334	0.000	0.000	0.000	0.000
221	A	224	LEU	0	0.043	0.043	26.857	0.089	0.089	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:LYS)