FMO DATABASE

FMODB ID: 6YR4Z

Calculation Name: 1VHC-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1VHC

Chain ID: A

ChEMBL ID:

UniProt ID: P44480

Base Structure: X-ray

Registration Date: 2023-09-23

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

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	212
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2383834.501346
FMO2-HF: Nuclear repulsion	2304301.141627
FMO2-HF: Total energy	-79533.359718
FMO2-MP2: Total energy	-79767.146912

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:2:SER)

Summations of interaction energy for fragment #1(A:2:SER)

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.
-0.258	1.179	-0.021	-0.575	-0.842	0.003

Interaction energy analysis for fragmet #1(A:2:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.018 / q_NPA : -0.020

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	4	THR	0	0.050	0.013	3.777	-1.093	0.216	-0.020	-0.565	-0.725	0.003
4	A	5	THR	0	0.084	0.011	6.410	0.186	0.186	0.000	0.000	0.000	0.000
5	A	6	GLN	0	0.001	0.010	9.284	0.106	0.106	0.000	0.000	0.000	0.000
6	A	7	GLN	0	0.057	0.031	6.447	-0.399	-0.399	0.000	0.000	0.000	0.000
7	A	8	ILE	0	0.003	0.014	5.451	0.157	0.157	0.000	0.000	0.000	0.000
8	A	9	ILE	0	-0.022	-0.008	9.237	0.141	0.141	0.000	0.000	0.000	0.000
9	A	10	GLU	-1	-0.831	-0.937	12.556	-0.136	-0.136	0.000	0.000	0.000	0.000
10	A	11	LYS	1	0.955	0.990	6.739	0.171	0.171	0.000	0.000	0.000	0.000
11	A	12	LEU	0	-0.037	-0.025	12.164	0.057	0.057	0.000	0.000	0.000	0.000
12	A	13	ARG	1	0.892	0.969	14.527	0.182	0.182	0.000	0.000	0.000	0.000
13	A	14	GLU	-1	-0.975	-0.994	14.040	0.010	0.010	0.000	0.000	0.000	0.000
14	A	15	LEU	0	-0.019	-0.002	13.126	0.016	0.016	0.000	0.000	0.000	0.000
15	A	16	LYS	1	0.914	0.958	17.543	0.055	0.055	0.000	0.000	0.000	0.000
16	A	17	ILE	0	-0.031	-0.016	19.619	-0.004	-0.004	0.000	0.000	0.000	0.000
17	A	18	VAL	0	-0.003	-0.002	16.126	0.006	0.006	0.000	0.000	0.000	0.000
18	A	19	PRO	0	0.013	0.011	17.494	-0.004	-0.004	0.000	0.000	0.000	0.000
19	A	20	VAL	0	-0.053	-0.024	18.479	0.006	0.006	0.000	0.000	0.000	0.000
20	A	21	ILE	0	0.040	0.010	18.416	-0.002	-0.002	0.000	0.000	0.000	0.000
21	A	22	ALA	0	-0.052	-0.037	20.672	0.004	0.004	0.000	0.000	0.000	0.000
22	A	23	LEU	0	-0.015	-0.002	20.395	-0.003	-0.003	0.000	0.000	0.000	0.000
23	A	24	ASP	-1	-0.861	-0.944	24.127	0.059	0.059	0.000	0.000	0.000	0.000
24	A	25	ASN	0	0.015	0.011	26.048	0.007	0.007	0.000	0.000	0.000	0.000
25	A	26	ALA	0	0.034	0.004	20.972	0.002	0.002	0.000	0.000	0.000	0.000
26	A	27	ASP	-1	-0.877	-0.939	21.538	0.151	0.151	0.000	0.000	0.000	0.000
27	A	28	ASP	-1	-0.874	-0.944	23.486	0.097	0.097	0.000	0.000	0.000	0.000
28	A	29	ILE	0	-0.083	-0.049	17.229	-0.004	-0.004	0.000	0.000	0.000	0.000
29	A	30	LEU	0	-0.012	0.004	18.191	0.008	0.008	0.000	0.000	0.000	0.000
30	A	31	PRO	0	0.064	0.035	20.483	0.000	0.000	0.000	0.000	0.000	0.000
31	A	32	LEU	0	-0.006	0.013	20.895	-0.010	-0.010	0.000	0.000	0.000	0.000
32	A	33	ALA	0	0.020	-0.003	16.679	-0.009	-0.009	0.000	0.000	0.000	0.000
33	A	34	ASP	-1	-0.820	-0.902	18.590	0.171	0.171	0.000	0.000	0.000	0.000
34	A	35	THR	0	-0.069	-0.043	20.517	-0.009	-0.009	0.000	0.000	0.000	0.000
35	A	36	LEU	0	-0.031	-0.006	18.310	-0.010	-0.010	0.000	0.000	0.000	0.000
36	A	37	ALA	0	0.035	0.031	16.964	-0.010	-0.010	0.000	0.000	0.000	0.000
37	A	38	LYS	1	0.870	0.936	18.581	-0.102	-0.102	0.000	0.000	0.000	0.000
38	A	39	ASN	0	-0.089	-0.046	22.031	-0.011	-0.011	0.000	0.000	0.000	0.000
39	A	40	GLY	0	0.045	0.032	19.713	-0.010	-0.010	0.000	0.000	0.000	0.000
40	A	41	LEU	0	-0.008	-0.005	17.786	-0.010	-0.010	0.000	0.000	0.000	0.000
41	A	42	SER	0	-0.014	-0.016	13.378	0.004	0.004	0.000	0.000	0.000	0.000
42	A	43	VAL	0	-0.020	-0.010	12.653	0.000	0.000	0.000	0.000	0.000	0.000
43	A	44	ALA	0	-0.001	0.004	13.427	0.000	0.000	0.000	0.000	0.000	0.000
44	A	45	GLU	-1	-0.897	-0.936	13.655	0.004	0.004	0.000	0.000	0.000	0.000
45	A	46	ILE	0	-0.002	-0.012	14.830	-0.008	-0.008	0.000	0.000	0.000	0.000
46	A	47	THR	0	-0.027	-0.001	16.831	0.000	0.000	0.000	0.000	0.000	0.000
47	A	48	PHE	0	0.073	0.001	15.376	0.008	0.008	0.000	0.000	0.000	0.000
48	A	49	ARG	1	0.871	0.941	20.152	-0.034	-0.034	0.000	0.000	0.000	0.000
49	A	50	SER	0	-0.046	-0.023	22.584	-0.006	-0.006	0.000	0.000	0.000	0.000
50	A	51	GLU	-1	-0.886	-0.946	22.294	0.079	0.079	0.000	0.000	0.000	0.000
51	A	52	ALA	0	0.018	0.022	22.477	0.009	0.009	0.000	0.000	0.000	0.000
52	A	53	ALA	0	-0.034	-0.012	18.059	0.021	0.021	0.000	0.000	0.000	0.000
53	A	54	ALA	0	0.047	0.012	16.223	0.029	0.029	0.000	0.000	0.000	0.000
54	A	55	ASP	-1	-0.841	-0.927	16.338	0.214	0.214	0.000	0.000	0.000	0.000
55	A	56	ALA	0	-0.002	-0.006	17.886	0.021	0.021	0.000	0.000	0.000	0.000
56	A	57	ILE	0	-0.023	-0.011	11.566	0.021	0.021	0.000	0.000	0.000	0.000
57	A	58	ARG	1	0.918	0.966	13.018	-0.194	-0.194	0.000	0.000	0.000	0.000
58	A	59	LEU	0	-0.027	-0.006	14.311	0.038	0.038	0.000	0.000	0.000	0.000
59	A	60	LEU	0	-0.003	0.000	13.088	0.005	0.005	0.000	0.000	0.000	0.000
60	A	61	ARG	1	0.807	0.918	7.081	-0.878	-0.878	0.000	0.000	0.000	0.000
61	A	62	ALA	0	-0.015	-0.012	11.303	0.035	0.035	0.000	0.000	0.000	0.000
62	A	63	ASN	0	-0.048	-0.024	13.437	-0.014	-0.014	0.000	0.000	0.000	0.000
63	A	64	ARG	1	0.846	0.918	12.854	-0.245	-0.245	0.000	0.000	0.000	0.000
64	A	65	PRO	0	0.023	0.012	9.373	0.023	0.023	0.000	0.000	0.000	0.000
65	A	66	ASP	-1	-0.947	-0.973	7.458	0.457	0.457	0.000	0.000	0.000	0.000
66	A	67	PHE	0	-0.026	-0.020	8.619	-0.105	-0.105	0.000	0.000	0.000	0.000
67	A	68	LEU	0	-0.017	-0.003	7.730	0.026	0.026	0.000	0.000	0.000	0.000
68	A	69	ILE	0	-0.005	-0.017	8.522	-0.020	-0.020	0.000	0.000	0.000	0.000
69	A	70	ALA	0	0.016	0.028	9.046	0.033	0.033	0.000	0.000	0.000	0.000
70	A	71	ALA	0	0.021	0.025	11.574	0.021	0.021	0.000	0.000	0.000	0.000
71	A	72	GLY	0	0.039	0.007	13.686	-0.045	-0.045	0.000	0.000	0.000	0.000
72	A	73	THR	0	-0.090	-0.061	16.825	0.015	0.015	0.000	0.000	0.000	0.000
73	A	74	VAL	0	0.031	0.034	15.049	0.007	0.007	0.000	0.000	0.000	0.000
74	A	75	LEU	0	-0.009	-0.015	18.454	-0.021	-0.021	0.000	0.000	0.000	0.000
75	A	76	THR	0	-0.048	-0.028	20.566	-0.009	-0.009	0.000	0.000	0.000	0.000
76	A	77	ALA	0	0.052	0.001	18.402	0.002	0.002	0.000	0.000	0.000	0.000
77	A	78	GLU	-1	-0.866	-0.930	17.704	0.031	0.031	0.000	0.000	0.000	0.000
78	A	79	GLN	0	0.021	0.010	17.914	0.009	0.009	0.000	0.000	0.000	0.000
79	A	80	VAL	0	0.019	0.025	13.057	0.033	0.033	0.000	0.000	0.000	0.000
80	A	81	VAL	0	0.027	0.009	13.149	0.046	0.046	0.000	0.000	0.000	0.000
81	A	82	LEU	0	-0.002	0.006	13.368	0.057	0.057	0.000	0.000	0.000	0.000
82	A	83	ALA	0	0.024	0.005	12.122	0.064	0.064	0.000	0.000	0.000	0.000
83	A	84	LYS	1	0.914	0.966	5.608	-0.181	-0.181	0.000	0.000	0.000	0.000
84	A	85	SER	0	-0.045	-0.022	8.901	0.244	0.244	0.000	0.000	0.000	0.000
85	A	86	SER	0	-0.030	-0.021	11.199	0.042	0.042	0.000	0.000	0.000	0.000
86	A	87	GLY	0	0.015	0.016	8.142	-0.001	-0.001	0.000	0.000	0.000	0.000
87	A	88	ALA	0	-0.023	-0.010	7.547	0.164	0.164	0.000	0.000	0.000	0.000
88	A	89	ASP	-1	-0.823	-0.907	4.617	0.656	0.784	-0.001	-0.010	-0.117	0.000
89	A	90	PHE	0	-0.065	-0.045	5.828	-0.334	-0.334	0.000	0.000	0.000	0.000
90	A	91	VAL	0	0.017	0.011	8.559	0.103	0.103	0.000	0.000	0.000	0.000
91	A	92	VAL	0	0.020	0.019	12.197	-0.066	-0.066	0.000	0.000	0.000	0.000
92	A	93	THR	0	-0.056	-0.063	15.444	0.019	0.019	0.000	0.000	0.000	0.000
93	A	94	PRO	0	-0.005	-0.006	18.864	-0.009	-0.009	0.000	0.000	0.000	0.000
94	A	95	GLY	0	0.058	0.036	22.397	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	96	LEU	0	0.036	0.039	20.553	-0.007	-0.007	0.000	0.000	0.000	0.000
96	A	97	ASN	0	-0.003	0.002	21.326	0.000	0.000	0.000	0.000	0.000	0.000
97	A	98	PRO	0	0.119	0.033	20.654	-0.008	-0.008	0.000	0.000	0.000	0.000
98	A	99	LYS	1	0.988	0.997	20.094	0.045	0.045	0.000	0.000	0.000	0.000
99	A	100	ILE	0	-0.033	-0.006	17.083	-0.007	-0.007	0.000	0.000	0.000	0.000
100	A	101	VAL	0	0.021	0.011	15.970	-0.012	-0.012	0.000	0.000	0.000	0.000
101	A	102	LYS	1	0.929	0.971	15.119	0.227	0.227	0.000	0.000	0.000	0.000
102	A	103	LEU	0	0.005	0.005	14.557	-0.030	-0.030	0.000	0.000	0.000	0.000
103	A	104	CYS	0	-0.027	-0.012	11.293	0.006	0.006	0.000	0.000	0.000	0.000
104	A	105	GLN	0	-0.018	-0.006	10.485	-0.069	-0.069	0.000	0.000	0.000	0.000
105	A	106	ASP	-1	-0.866	-0.936	11.394	-0.372	-0.372	0.000	0.000	0.000	0.000
106	A	107	LEU	0	-0.085	-0.034	10.022	-0.010	-0.010	0.000	0.000	0.000	0.000
107	A	108	ASN	0	-0.065	-0.031	4.943	0.100	0.100	0.000	0.000	0.000	0.000
108	A	109	PHE	0	-0.074	-0.032	5.670	-0.259	-0.259	0.000	0.000	0.000	0.000
109	A	110	PRO	0	0.039	0.010	5.648	0.135	0.135	0.000	0.000	0.000	0.000
110	A	111	ILE	0	0.050	0.014	8.675	0.155	0.155	0.000	0.000	0.000	0.000
111	A	112	THR	0	-0.041	-0.021	12.332	-0.025	-0.025	0.000	0.000	0.000	0.000
112	A	113	PRO	0	0.026	0.023	14.962	0.037	0.037	0.000	0.000	0.000	0.000
113	A	114	GLY	0	0.017	0.025	18.268	-0.003	-0.003	0.000	0.000	0.000	0.000
114	A	115	VAL	0	-0.021	-0.017	21.544	0.001	0.001	0.000	0.000	0.000	0.000
115	A	116	ASN	0	-0.027	-0.036	24.633	0.001	0.001	0.000	0.000	0.000	0.000
116	A	117	ASN	0	-0.018	-0.012	28.030	0.001	0.001	0.000	0.000	0.000	0.000
117	A	118	PRO	0	0.105	0.028	28.783	-0.006	-0.006	0.000	0.000	0.000	0.000
118	A	119	MET	0	0.002	0.023	29.359	-0.005	-0.005	0.000	0.000	0.000	0.000
119	A	120	ALA	0	-0.005	-0.005	25.748	-0.006	-0.006	0.000	0.000	0.000	0.000
120	A	121	ILE	0	-0.001	0.002	24.641	-0.011	-0.011	0.000	0.000	0.000	0.000
121	A	122	GLU	-1	-0.827	-0.885	24.591	-0.111	-0.111	0.000	0.000	0.000	0.000
122	A	123	ILE	0	-0.014	0.007	23.244	-0.007	-0.007	0.000	0.000	0.000	0.000
123	A	124	ALA	0	0.006	-0.011	20.476	-0.013	-0.013	0.000	0.000	0.000	0.000
124	A	125	LEU	0	-0.045	-0.011	20.442	-0.025	-0.025	0.000	0.000	0.000	0.000
125	A	126	GLU	-1	-0.926	-0.945	22.129	-0.158	-0.158	0.000	0.000	0.000	0.000
126	A	127	MET	0	-0.101	-0.044	18.729	-0.002	-0.002	0.000	0.000	0.000	0.000
127	A	128	GLY	0	0.020	0.019	17.742	-0.036	-0.036	0.000	0.000	0.000	0.000
128	A	129	ILE	0	-0.075	-0.042	15.439	-0.038	-0.038	0.000	0.000	0.000	0.000
129	A	130	SER	0	0.051	0.018	17.208	0.022	0.022	0.000	0.000	0.000	0.000
130	A	131	ALA	0	-0.040	-0.016	15.299	0.023	0.023	0.000	0.000	0.000	0.000
131	A	132	VAL	0	0.025	0.013	16.904	-0.014	-0.014	0.000	0.000	0.000	0.000
132	A	133	LYS	1	0.852	0.891	15.426	0.133	0.133	0.000	0.000	0.000	0.000
133	A	134	PHE	0	-0.012	0.006	20.221	0.001	0.001	0.000	0.000	0.000	0.000
134	A	135	PHE	0	-0.020	0.009	23.764	0.011	0.011	0.000	0.000	0.000	0.000
135	A	136	PRO	0	-0.027	-0.021	25.558	-0.003	-0.003	0.000	0.000	0.000	0.000
136	A	137	ALA	0	0.047	0.010	26.579	0.000	0.000	0.000	0.000	0.000	0.000
137	A	138	GLU	-1	-0.819	-0.894	28.467	-0.026	-0.026	0.000	0.000	0.000	0.000
138	A	139	ALA	0	-0.027	-0.013	31.936	0.000	0.000	0.000	0.000	0.000	0.000
139	A	140	SER	0	-0.023	-0.024	30.223	-0.001	-0.001	0.000	0.000	0.000	0.000
140	A	141	GLY	0	-0.013	-0.012	32.613	-0.003	-0.003	0.000	0.000	0.000	0.000
141	A	142	GLY	0	0.010	0.006	31.237	0.001	0.001	0.000	0.000	0.000	0.000
142	A	143	VAL	0	0.029	0.009	30.670	-0.005	-0.005	0.000	0.000	0.000	0.000
143	A	144	LYS	1	0.948	0.973	32.114	0.028	0.028	0.000	0.000	0.000	0.000
144	A	145	MET	0	-0.004	0.013	31.206	-0.003	-0.003	0.000	0.000	0.000	0.000
145	A	146	ILE	0	0.029	0.015	26.542	-0.004	-0.004	0.000	0.000	0.000	0.000
146	A	147	LYS	1	0.968	0.978	30.037	0.036	0.036	0.000	0.000	0.000	0.000
147	A	148	ALA	0	-0.027	-0.002	32.320	-0.002	-0.002	0.000	0.000	0.000	0.000
148	A	149	LEU	0	-0.006	-0.011	28.689	-0.002	-0.002	0.000	0.000	0.000	0.000
149	A	150	LEU	0	-0.021	-0.014	26.197	-0.005	-0.005	0.000	0.000	0.000	0.000
150	A	151	GLY	0	-0.027	0.004	30.054	-0.001	-0.001	0.000	0.000	0.000	0.000
151	A	152	PRO	0	-0.028	-0.012	31.996	-0.002	-0.002	0.000	0.000	0.000	0.000
152	A	153	TYR	0	-0.077	-0.087	26.863	-0.004	-0.004	0.000	0.000	0.000	0.000
153	A	154	ALA	0	0.061	0.039	27.132	-0.006	-0.006	0.000	0.000	0.000	0.000
154	A	155	GLN	0	-0.024	-0.021	23.853	0.008	0.008	0.000	0.000	0.000	0.000
155	A	156	LEU	0	0.004	0.014	22.083	-0.018	-0.018	0.000	0.000	0.000	0.000
156	A	157	GLN	0	-0.013	-0.011	16.668	0.018	0.018	0.000	0.000	0.000	0.000
157	A	158	ILE	0	0.004	-0.001	19.903	-0.008	-0.008	0.000	0.000	0.000	0.000
158	A	159	MET	0	0.027	0.042	15.769	0.003	0.003	0.000	0.000	0.000	0.000
159	A	160	PRO	0	0.033	0.025	20.190	0.005	0.005	0.000	0.000	0.000	0.000
160	A	161	THR	0	0.028	0.008	21.632	0.008	0.008	0.000	0.000	0.000	0.000
161	A	162	GLY	0	0.034	0.016	23.921	-0.002	-0.002	0.000	0.000	0.000	0.000
162	A	163	GLY	0	0.010	0.009	27.323	-0.003	-0.003	0.000	0.000	0.000	0.000
163	A	164	ILE	0	-0.010	-0.003	25.326	-0.001	-0.001	0.000	0.000	0.000	0.000
164	A	165	GLY	0	0.023	-0.004	28.655	0.005	0.005	0.000	0.000	0.000	0.000
165	A	166	LEU	0	0.016	0.004	30.121	-0.004	-0.004	0.000	0.000	0.000	0.000
166	A	167	HIS	0	-0.002	-0.003	31.705	0.000	0.000	0.000	0.000	0.000	0.000
167	A	168	ASN	0	0.053	0.039	30.711	-0.001	-0.001	0.000	0.000	0.000	0.000
168	A	169	ILE	0	0.002	0.000	24.959	-0.005	-0.005	0.000	0.000	0.000	0.000
169	A	170	ARG	1	0.899	0.943	28.257	0.003	0.003	0.000	0.000	0.000	0.000
170	A	171	ASP	-1	-0.913	-0.955	30.390	-0.023	-0.023	0.000	0.000	0.000	0.000
171	A	172	TYR	0	-0.108	-0.087	26.606	-0.008	-0.008	0.000	0.000	0.000	0.000
172	A	173	LEU	0	-0.002	-0.012	23.210	-0.006	-0.006	0.000	0.000	0.000	0.000
173	A	174	ALA	0	-0.015	0.013	26.722	-0.002	-0.002	0.000	0.000	0.000	0.000
174	A	175	ILE	0	-0.081	-0.037	27.128	-0.002	-0.002	0.000	0.000	0.000	0.000
175	A	176	PRO	0	0.069	0.026	25.978	-0.005	-0.005	0.000	0.000	0.000	0.000
176	A	177	ASN	0	-0.059	-0.026	23.553	0.001	0.001	0.000	0.000	0.000	0.000
177	A	178	ILE	0	-0.081	-0.032	22.246	-0.015	-0.015	0.000	0.000	0.000	0.000
178	A	179	VAL	0	-0.019	0.001	16.369	0.003	0.003	0.000	0.000	0.000	0.000
179	A	180	ALA	0	-0.018	-0.020	17.819	0.010	0.010	0.000	0.000	0.000	0.000
180	A	181	CYS	0	-0.044	-0.006	19.894	-0.008	-0.008	0.000	0.000	0.000	0.000
181	A	182	GLY	0	0.040	0.035	20.725	0.004	0.004	0.000	0.000	0.000	0.000
182	A	183	GLY	0	-0.020	-0.028	21.344	-0.002	-0.002	0.000	0.000	0.000	0.000
183	A	184	SER	0	0.018	0.009	23.013	0.004	0.004	0.000	0.000	0.000	0.000
184	A	185	TRP	0	0.014	0.010	25.163	0.004	0.004	0.000	0.000	0.000	0.000
185	A	186	PHE	0	0.051	0.017	22.046	0.003	0.003	0.000	0.000	0.000	0.000
186	A	187	VAL	0	-0.015	-0.004	22.234	0.006	0.006	0.000	0.000	0.000	0.000
187	A	188	GLU	-1	-0.815	-0.893	25.563	0.037	0.037	0.000	0.000	0.000	0.000
188	A	189	LYS	1	0.910	0.952	27.129	-0.045	-0.045	0.000	0.000	0.000	0.000
189	A	190	LYS	1	0.855	0.905	28.608	-0.028	-0.028	0.000	0.000	0.000	0.000
190	A	191	LEU	0	-0.006	-0.004	29.495	0.001	0.001	0.000	0.000	0.000	0.000
191	A	192	ILE	0	0.003	0.004	24.201	0.003	0.003	0.000	0.000	0.000	0.000
192	A	193	GLN	0	0.049	0.032	28.085	0.004	0.004	0.000	0.000	0.000	0.000
193	A	194	SER	0	-0.070	-0.014	30.626	0.000	0.000	0.000	0.000	0.000	0.000
194	A	195	ASN	0	-0.029	-0.024	29.188	-0.001	-0.001	0.000	0.000	0.000	0.000
195	A	196	ASN	0	-0.007	0.011	30.461	0.002	0.002	0.000	0.000	0.000	0.000
196	A	197	TRP	0	0.067	-0.001	25.640	-0.002	-0.002	0.000	0.000	0.000	0.000
197	A	198	ASP	-1	-0.892	-0.932	28.323	0.061	0.061	0.000	0.000	0.000	0.000
198	A	199	GLU	-1	-0.863	-0.929	30.826	0.034	0.034	0.000	0.000	0.000	0.000
199	A	200	ILE	0	-0.012	0.001	25.056	-0.002	-0.002	0.000	0.000	0.000	0.000
200	A	201	GLY	0	0.032	-0.003	26.139	-0.002	-0.002	0.000	0.000	0.000	0.000
201	A	202	ARG	1	0.784	0.892	27.179	-0.035	-0.035	0.000	0.000	0.000	0.000
202	A	203	LEU	0	0.009	0.000	28.552	-0.003	-0.003	0.000	0.000	0.000	0.000
203	A	204	VAL	0	-0.020	-0.008	22.920	-0.005	-0.005	0.000	0.000	0.000	0.000
204	A	205	ARG	1	0.946	0.968	25.871	-0.056	-0.056	0.000	0.000	0.000	0.000
205	A	206	GLU	-1	-0.885	-0.936	27.498	0.017	0.017	0.000	0.000	0.000	0.000
206	A	207	VAL	0	-0.031	-0.018	25.087	-0.005	-0.005	0.000	0.000	0.000	0.000
207	A	208	ILE	0	-0.022	-0.019	22.398	-0.007	-0.007	0.000	0.000	0.000	0.000
208	A	209	ASP	-1	-0.870	-0.932	25.874	0.023	0.023	0.000	0.000	0.000	0.000
209	A	210	ILE	0	-0.009	0.003	29.210	-0.004	-0.004	0.000	0.000	0.000	0.000
210	A	211	ILE	0	-0.037	-0.023	24.339	-0.005	-0.005	0.000	0.000	0.000	0.000
211	A	212	LYS	1	0.776	0.897	23.158	-0.013	-0.013	0.000	0.000	0.000	0.000
212	A	213	GLU	-1	-0.947	-0.961	28.295	0.004	0.004	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:SER)