FMO DATABASE

FMODB ID: R4M58

Calculation Name: 7LS2-A-Other547

Preferred Name:

Target Type:

Ligand Name: 2-methyl, 7-(3-methyl-pentane), guanosine-5'-monophosphate | (2~{r})-2-azanyl-4-[5-[(2~{s},3~{r},4~{s},5~{r})-3,4-bis(oxidanyl)-5-(phosphonooxymethyl)oxolan-2-yl]-3-methyl-2,6-bis(oxidanylidene)pyrimidin-1-yl]butanoic acid | guanosine-5'-diphosphate | n7-methyl-guanosine-5'-monophosphate | 7-propyl, guanosine-5'-monophosphate | 7-ethyl, guanosine-5'-monophosphate | 6-propyl, guanosine-5'-monophosphate | n(4)-acetylcytidine-5'-monophosphate | 6-ethyl, guanosine-5'-monophosphate | 2n-methylguanosine-5'-monophosphate | 6-methyl, guanosine-5'-monophosphate | 4-isopropyl, uridine-5'-monophosphate | 2'-methyl, 3-propyl, cytidine-5'-monophosphate | 6-hydro-1-methyladenosine-5'-monophosphate | n6-methyladenosine-5'-monophosphate | {3-[4-(2-amino-2-carboxy-ethyl)-1h-imidazol-2-yl]-1-carbamoyl-propyl}-trimethyl-ammonium | pseudouridine-5'-monophosphate | 5-methylcytidine-5'-monophosphate | 4-methyl, cytidine-5'-monophosphate | o2'-methylguanosine-5'-monophosphate | 3-methyluridine-5'-monophoshate | 3-methyl, cytidine-5'-monophosphate | o2'-methylycytidine-5'-monophosphate | o2'-methyluridine 5'-monophosphate | 2'-o-methyladenosine 5'-(dihydrogen phosphate) | n-methyl-lysine | magnesium ion | zinc ion

Ligand 3-letter code: MHG | B8N | GDP | G7M | P7G | E7G | B9B | 4AC | E6G | 2MG | B8W | I4U | B9H | 1MA | 6MZ | DDE | PSU | 5MC | B8T | OMG | UR3 | B8Q | OMC | OMU | A2M | MLZ | MG | ZN

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 7LS2

Chain ID: A

ChEMBL ID:

UniProt ID:

Base Structure: ElectronMicroscopy

Registration Date: 2025-10-06

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	206
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2239213.360943
FMO2-HF: Nuclear repulsion	2156634.359206
FMO2-HF: Total energy	-82579.001737
FMO2-MP2: Total energy	-82819.348741

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:5:VAL)

Summations of interaction energy for fragment #1(A:5:VAL)

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.
139.955	141.486	7.74	-4.394	-4.876	-0.044

Interaction energy analysis for fragmet #1(A:5:VAL)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.904 / q_NPA : 0.936

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	7	ARG	1	0.944	0.959	3.704	39.987	41.360	0.005	-0.463	-0.916	0.000
4	A	8	ASP	-1	-0.870	-0.935	1.682	-69.718	-70.559	7.729	-3.530	-3.357	-0.043
5	A	9	THR	0	0.010	0.002	3.579	11.904	12.903	0.006	-0.401	-0.603	-0.001
6	A	10	LEU	0	-0.069	-0.036	5.671	7.019	7.019	0.000	0.000	0.000	0.000
7	A	11	TYR	0	0.015	0.019	5.930	1.706	1.706	0.000	0.000	0.000	0.000
8	A	12	GLU	-1	-0.823	-0.917	8.316	-24.862	-24.862	0.000	0.000	0.000	0.000
9	A	13	ALA	0	-0.064	-0.021	10.251	2.716	2.716	0.000	0.000	0.000	0.000
10	A	14	VAL	0	-0.013	-0.013	12.276	2.118	2.118	0.000	0.000	0.000	0.000
11	A	15	ARG	1	0.992	1.001	13.378	19.212	19.212	0.000	0.000	0.000	0.000
12	A	16	GLU	-1	-0.886	-0.961	14.008	-17.497	-17.497	0.000	0.000	0.000	0.000
13	A	17	VAL	0	-0.055	-0.031	16.274	1.186	1.186	0.000	0.000	0.000	0.000
14	A	18	LEU	0	-0.047	-0.002	18.342	0.988	0.988	0.000	0.000	0.000	0.000
15	A	19	HIS	0	-0.063	-0.044	18.577	0.983	0.983	0.000	0.000	0.000	0.000
16	A	20	GLY	0	0.038	0.045	18.448	0.482	0.482	0.000	0.000	0.000	0.000
17	A	21	ASN	0	-0.038	-0.029	19.327	0.803	0.803	0.000	0.000	0.000	0.000
18	A	22	GLN	0	0.091	0.061	22.304	0.794	0.794	0.000	0.000	0.000	0.000
19	A	23	ARG	1	0.920	0.938	24.794	12.624	12.624	0.000	0.000	0.000	0.000
20	A	24	LYS	1	0.903	0.945	27.216	9.829	9.829	0.000	0.000	0.000	0.000
21	A	25	ARG	1	1.011	1.027	28.160	10.638	10.638	0.000	0.000	0.000	0.000
22	A	26	ARG	1	0.909	0.957	26.562	11.524	11.524	0.000	0.000	0.000	0.000
23	A	27	LYS	1	0.961	0.989	30.583	8.536	8.536	0.000	0.000	0.000	0.000
24	A	28	PHE	0	-0.024	-0.020	29.511	0.212	0.212	0.000	0.000	0.000	0.000
25	A	29	LEU	0	-0.010	-0.011	27.114	0.006	0.006	0.000	0.000	0.000	0.000
26	A	30	GLU	-1	-0.855	-0.942	24.297	-12.531	-12.531	0.000	0.000	0.000	0.000
27	A	31	THR	0	-0.032	-0.028	23.452	-0.223	-0.223	0.000	0.000	0.000	0.000
28	A	32	VAL	0	0.072	0.071	18.255	0.358	0.358	0.000	0.000	0.000	0.000
29	A	33	GLU	-1	-1.008	-0.999	21.242	-12.583	-12.583	0.000	0.000	0.000	0.000
30	A	34	LEU	0	-0.005	0.005	14.484	-0.363	-0.363	0.000	0.000	0.000	0.000
31	A	35	GLN	0	-0.008	-0.013	17.302	0.748	0.748	0.000	0.000	0.000	0.000
32	A	36	ILE	0	0.025	0.016	15.412	-1.004	-1.004	0.000	0.000	0.000	0.000
33	A	37	SER	0	0.014	0.000	16.225	1.143	1.143	0.000	0.000	0.000	0.000
34	A	38	LEU	0	0.012	0.013	17.408	-0.499	-0.499	0.000	0.000	0.000	0.000
35	A	39	LYS	1	0.929	0.979	16.918	14.741	14.741	0.000	0.000	0.000	0.000
36	A	40	ASN	0	0.046	0.003	19.768	-0.047	-0.047	0.000	0.000	0.000	0.000
37	A	41	TYR	0	0.031	0.037	23.064	0.153	0.153	0.000	0.000	0.000	0.000
38	A	42	ASP	-1	-0.778	-0.873	24.836	-10.288	-10.288	0.000	0.000	0.000	0.000
39	A	43	PRO	0	-0.009	-0.018	28.670	0.031	0.031	0.000	0.000	0.000	0.000
40	A	44	GLN	0	-0.001	-0.010	30.159	0.194	0.194	0.000	0.000	0.000	0.000
41	A	45	LYS	1	0.949	0.985	31.320	9.124	9.124	0.000	0.000	0.000	0.000
42	A	46	ASP	-1	-0.816	-0.903	32.185	-8.758	-8.758	0.000	0.000	0.000	0.000
43	A	47	LYS	1	0.834	0.897	27.762	10.079	10.079	0.000	0.000	0.000	0.000
44	A	48	ARG	1	0.891	0.946	28.111	9.159	9.159	0.000	0.000	0.000	0.000
45	A	49	PHE	0	0.080	0.043	23.973	0.147	0.147	0.000	0.000	0.000	0.000
46	A	50	SER	0	-0.026	-0.044	26.579	0.383	0.383	0.000	0.000	0.000	0.000
47	A	51	GLY	0	0.038	0.034	26.135	0.119	0.119	0.000	0.000	0.000	0.000
48	A	52	THR	0	-0.060	-0.035	26.394	-0.051	-0.051	0.000	0.000	0.000	0.000
49	A	53	VAL	0	-0.008	0.011	21.212	0.066	0.066	0.000	0.000	0.000	0.000
50	A	54	ARG	1	0.940	0.970	24.299	11.270	11.270	0.000	0.000	0.000	0.000
51	A	55	LEU	0	-0.020	-0.006	20.433	-0.658	-0.658	0.000	0.000	0.000	0.000
52	A	56	LYS	1	1.039	1.020	20.168	14.946	14.946	0.000	0.000	0.000	0.000
53	A	57	SER	0	-0.057	-0.038	20.465	0.304	0.304	0.000	0.000	0.000	0.000
54	A	58	THR	0	0.025	0.001	23.597	0.040	0.040	0.000	0.000	0.000	0.000
55	A	59	PRO	0	0.033	0.017	21.549	0.124	0.124	0.000	0.000	0.000	0.000
56	A	60	ARG	1	0.947	0.959	23.437	11.319	11.319	0.000	0.000	0.000	0.000
57	A	61	PRO	0	0.009	0.010	26.926	0.269	0.269	0.000	0.000	0.000	0.000
58	A	62	LYS	1	0.939	0.987	29.975	9.519	9.519	0.000	0.000	0.000	0.000
59	A	63	PHE	0	-0.034	-0.026	29.286	-0.137	-0.137	0.000	0.000	0.000	0.000
60	A	64	SER	0	-0.004	0.015	34.182	0.109	0.109	0.000	0.000	0.000	0.000
61	A	65	VAL	0	0.052	0.024	35.314	-0.168	-0.168	0.000	0.000	0.000	0.000
62	A	66	CYS	0	-0.031	-0.009	38.154	0.271	0.271	0.000	0.000	0.000	0.000
63	A	67	VAL	0	0.007	0.001	40.277	-0.161	-0.161	0.000	0.000	0.000	0.000
64	A	68	LEU	0	-0.026	-0.007	42.639	0.200	0.200	0.000	0.000	0.000	0.000
65	A	69	GLY	0	-0.005	-0.015	44.486	-0.153	-0.153	0.000	0.000	0.000	0.000
66	A	70	ASP	-1	-0.802	-0.879	46.596	-6.566	-6.566	0.000	0.000	0.000	0.000
67	A	71	GLN	0	0.055	0.027	49.242	-0.008	-0.008	0.000	0.000	0.000	0.000
68	A	72	GLN	0	-0.017	-0.026	48.964	0.022	0.022	0.000	0.000	0.000	0.000
69	A	73	HIS	1	0.881	0.940	45.138	6.882	6.882	0.000	0.000	0.000	0.000
70	A	74	CYS	0	-0.103	-0.047	47.551	-0.089	-0.089	0.000	0.000	0.000	0.000
71	A	75	ASP	-1	-0.828	-0.924	49.736	-6.367	-6.367	0.000	0.000	0.000	0.000
72	A	76	GLU	-1	-0.834	-0.914	44.704	-7.193	-7.193	0.000	0.000	0.000	0.000
73	A	77	ARG	1	0.821	0.896	44.538	6.699	6.699	0.000	0.000	0.000	0.000
74	A	78	LYS	1	0.879	0.951	45.258	6.534	6.534	0.000	0.000	0.000	0.000
75	A	79	ALA	0	0.068	0.041	45.378	-0.051	-0.051	0.000	0.000	0.000	0.000
76	A	80	VAL	0	-0.053	-0.023	39.436	-0.142	-0.142	0.000	0.000	0.000	0.000
77	A	81	ASP	-1	-0.894	-0.934	41.411	-7.430	-7.430	0.000	0.000	0.000	0.000
78	A	82	ILE	0	-0.081	-0.034	39.355	-0.098	-0.098	0.000	0.000	0.000	0.000
79	A	83	PRO	0	-0.049	-0.044	42.778	0.212	0.212	0.000	0.000	0.000	0.000
80	A	84	HIS	0	-0.012	-0.013	45.205	-0.227	-0.227	0.000	0.000	0.000	0.000
81	A	85	MET	0	-0.047	-0.007	46.777	0.126	0.126	0.000	0.000	0.000	0.000
82	A	86	ASP	-1	-0.739	-0.878	48.519	-6.113	-6.113	0.000	0.000	0.000	0.000
83	A	87	ILE	0	-0.001	-0.013	51.638	-0.028	-0.028	0.000	0.000	0.000	0.000
84	A	88	GLU	-1	-0.790	-0.902	53.752	-5.815	-5.815	0.000	0.000	0.000	0.000
85	A	89	ALA	0	0.036	0.028	51.865	0.035	0.035	0.000	0.000	0.000	0.000
86	A	90	LEU	0	-0.006	-0.012	48.511	-0.024	-0.024	0.000	0.000	0.000	0.000
87	A	91	LYS	1	0.883	0.933	52.407	5.863	5.863	0.000	0.000	0.000	0.000
88	A	92	LYS	1	0.905	0.955	55.470	5.711	5.711	0.000	0.000	0.000	0.000
89	A	93	LEU	0	0.059	0.023	50.761	0.018	0.018	0.000	0.000	0.000	0.000
90	A	94	ASN	0	-0.021	-0.009	53.000	-0.122	-0.122	0.000	0.000	0.000	0.000
91	A	95	LYS	1	0.933	0.964	53.955	5.404	5.404	0.000	0.000	0.000	0.000
92	A	96	ASN	0	0.070	0.044	53.583	-0.004	-0.004	0.000	0.000	0.000	0.000
93	A	97	LYS	1	0.927	0.978	51.224	5.987	5.987	0.000	0.000	0.000	0.000
94	A	98	LYS	1	0.918	0.934	49.292	6.124	6.124	0.000	0.000	0.000	0.000
95	A	99	LEU	0	0.045	0.016	48.355	-0.176	-0.176	0.000	0.000	0.000	0.000
96	A	100	VAL	0	0.084	0.044	47.349	-0.132	-0.132	0.000	0.000	0.000	0.000
97	A	101	LYS	1	0.908	0.978	44.610	6.499	6.499	0.000	0.000	0.000	0.000
98	A	102	LYS	1	0.916	0.955	43.534	6.601	6.601	0.000	0.000	0.000	0.000
99	A	103	LEU	0	0.034	0.022	43.887	-0.143	-0.143	0.000	0.000	0.000	0.000
100	A	104	ALA	0	0.075	0.030	41.560	-0.146	-0.146	0.000	0.000	0.000	0.000
101	A	105	LYS	1	0.866	0.924	39.376	7.498	7.498	0.000	0.000	0.000	0.000
102	A	106	LYS	1	0.923	0.965	38.892	7.416	7.416	0.000	0.000	0.000	0.000
103	A	107	TYR	0	0.022	-0.006	39.298	-0.053	-0.053	0.000	0.000	0.000	0.000
104	A	108	ASP	-1	-0.880	-0.923	34.652	-9.322	-9.322	0.000	0.000	0.000	0.000
105	A	109	ALA	0	0.013	0.019	34.019	0.040	0.040	0.000	0.000	0.000	0.000
106	A	110	PHE	0	-0.013	-0.014	36.172	0.220	0.220	0.000	0.000	0.000	0.000
107	A	111	LEU	0	0.043	0.023	37.828	-0.212	-0.212	0.000	0.000	0.000	0.000
108	A	112	ALA	0	0.017	0.000	40.010	0.206	0.206	0.000	0.000	0.000	0.000
109	A	113	SER	0	0.017	-0.027	42.314	-0.161	-0.161	0.000	0.000	0.000	0.000
110	A	114	GLU	-1	-0.835	-0.932	44.799	-6.603	-6.603	0.000	0.000	0.000	0.000
111	A	115	SER	0	0.033	0.034	46.136	0.107	0.107	0.000	0.000	0.000	0.000
112	A	116	LEU	0	0.017	0.003	47.565	0.092	0.092	0.000	0.000	0.000	0.000
113	A	117	ILE	0	-0.025	-0.008	42.537	0.030	0.030	0.000	0.000	0.000	0.000
114	A	118	LYS	1	0.894	0.946	46.892	6.475	6.475	0.000	0.000	0.000	0.000
115	A	119	GLN	0	-0.037	-0.008	50.251	0.058	0.058	0.000	0.000	0.000	0.000
116	A	120	ILE	0	0.044	0.012	46.340	0.079	0.079	0.000	0.000	0.000	0.000
117	A	121	PRO	0	-0.005	-0.019	48.133	0.046	0.046	0.000	0.000	0.000	0.000
118	A	122	ARG	1	0.953	0.993	49.797	5.760	5.760	0.000	0.000	0.000	0.000
119	A	123	ILE	0	0.030	0.004	52.386	0.089	0.089	0.000	0.000	0.000	0.000
120	A	124	LEU	0	-0.046	-0.010	48.988	-0.058	-0.058	0.000	0.000	0.000	0.000
121	A	125	GLY	0	0.048	0.019	46.675	-0.127	-0.127	0.000	0.000	0.000	0.000
122	A	126	PRO	0	0.026	0.008	46.410	-0.153	-0.153	0.000	0.000	0.000	0.000
123	A	127	GLY	0	-0.033	0.002	47.544	-0.046	-0.046	0.000	0.000	0.000	0.000
124	A	128	LEU	0	-0.051	-0.048	45.028	-0.029	-0.029	0.000	0.000	0.000	0.000
125	A	129	ASN	0	0.047	0.027	41.571	-0.290	-0.290	0.000	0.000	0.000	0.000
126	A	130	LYS	1	0.941	0.974	41.093	6.988	6.988	0.000	0.000	0.000	0.000
127	A	131	ALA	0	-0.026	-0.012	39.673	-0.121	-0.121	0.000	0.000	0.000	0.000
128	A	132	GLY	0	-0.012	-0.004	36.895	-0.244	-0.244	0.000	0.000	0.000	0.000
129	A	133	LYS	1	0.797	0.906	34.710	8.805	8.805	0.000	0.000	0.000	0.000
130	A	134	PHE	0	0.005	0.005	37.039	0.220	0.220	0.000	0.000	0.000	0.000
131	A	135	PRO	0	-0.021	-0.008	37.113	-0.220	-0.220	0.000	0.000	0.000	0.000
132	A	136	SER	0	0.005	0.019	34.648	0.062	0.062	0.000	0.000	0.000	0.000
133	A	137	LEU	0	0.007	0.006	37.180	0.216	0.216	0.000	0.000	0.000	0.000
134	A	138	LEU	0	0.021	0.009	38.290	-0.235	-0.235	0.000	0.000	0.000	0.000
135	A	139	THR	0	-0.037	-0.040	38.529	-0.185	-0.185	0.000	0.000	0.000	0.000
136	A	140	HIS	0	0.094	0.028	41.461	-0.102	-0.102	0.000	0.000	0.000	0.000
137	A	141	ASN	0	-0.021	-0.007	38.215	-0.052	-0.052	0.000	0.000	0.000	0.000
138	A	142	GLU	-1	-0.830	-0.898	41.096	-7.027	-7.027	0.000	0.000	0.000	0.000
139	A	143	ASN	0	0.055	0.037	37.616	-0.151	-0.151	0.000	0.000	0.000	0.000
140	A	144	MET	0	-0.021	-0.020	38.771	-0.102	-0.102	0.000	0.000	0.000	0.000
141	A	145	VAL	0	0.034	0.032	35.109	-0.051	-0.051	0.000	0.000	0.000	0.000
142	A	146	ALA	0	0.080	0.039	33.015	-0.241	-0.241	0.000	0.000	0.000	0.000
143	A	147	LYS	1	0.853	0.931	32.438	8.417	8.417	0.000	0.000	0.000	0.000
144	A	148	VAL	0	-0.020	-0.014	33.889	-0.090	-0.090	0.000	0.000	0.000	0.000
145	A	149	ASP	-1	-0.855	-0.914	30.228	-10.054	-10.054	0.000	0.000	0.000	0.000
146	A	150	GLU	-1	-0.881	-0.941	26.274	-12.256	-12.256	0.000	0.000	0.000	0.000
147	A	151	VAL	0	-0.033	-0.011	28.786	-0.184	-0.184	0.000	0.000	0.000	0.000
148	A	152	LYS	1	0.830	0.894	29.857	9.921	9.921	0.000	0.000	0.000	0.000
149	A	153	SER	0	-0.005	-0.006	24.802	-0.270	-0.270	0.000	0.000	0.000	0.000
150	A	154	THR	0	-0.027	0.004	25.293	-0.477	-0.477	0.000	0.000	0.000	0.000
151	A	155	ILE	0	-0.001	0.006	21.284	0.294	0.294	0.000	0.000	0.000	0.000
152	A	156	LYS	1	0.919	0.951	25.358	10.530	10.530	0.000	0.000	0.000	0.000
153	A	157	PHE	0	0.043	0.033	19.919	0.398	0.398	0.000	0.000	0.000	0.000
154	A	158	GLN	0	-0.044	-0.037	25.250	0.311	0.311	0.000	0.000	0.000	0.000
155	A	159	MET	0	-0.021	0.033	26.729	0.064	0.064	0.000	0.000	0.000	0.000
156	A	160	LYS	1	0.931	0.953	27.650	10.271	10.271	0.000	0.000	0.000	0.000
157	A	161	LYS	1	0.989	0.984	28.623	8.587	8.587	0.000	0.000	0.000	0.000
158	A	162	VAL	0	0.038	0.027	27.140	0.188	0.188	0.000	0.000	0.000	0.000
159	A	163	LEU	0	-0.009	0.004	23.250	-0.193	-0.193	0.000	0.000	0.000	0.000
160	A	164	CYS	0	-0.015	-0.022	21.857	-0.420	-0.420	0.000	0.000	0.000	0.000
161	A	165	LEU	0	-0.023	-0.004	20.788	0.667	0.667	0.000	0.000	0.000	0.000
162	A	166	ALA	0	0.031	0.026	20.871	-0.619	-0.619	0.000	0.000	0.000	0.000
163	A	167	VAL	0	-0.019	-0.018	19.339	0.417	0.417	0.000	0.000	0.000	0.000
164	A	168	ALA	0	0.046	0.025	21.180	-0.518	-0.518	0.000	0.000	0.000	0.000
165	A	169	VAL	0	-0.061	-0.030	18.318	0.344	0.344	0.000	0.000	0.000	0.000
166	A	170	GLY	0	0.106	0.038	19.175	-0.838	-0.838	0.000	0.000	0.000	0.000
167	A	171	HIS	0	-0.093	-0.073	20.156	0.957	0.957	0.000	0.000	0.000	0.000
168	A	172	VAL	0	0.025	0.023	20.412	-0.451	-0.451	0.000	0.000	0.000	0.000
169	A	173	LYS	1	0.925	0.972	21.214	11.162	11.162	0.000	0.000	0.000	0.000
170	A	174	MET	0	-0.052	-0.002	19.841	0.604	0.604	0.000	0.000	0.000	0.000
171	A	175	THR	0	0.020	-0.016	18.040	-0.169	-0.169	0.000	0.000	0.000	0.000
172	A	176	ASP	-1	-0.856	-0.921	13.550	-20.976	-20.976	0.000	0.000	0.000	0.000
173	A	177	ASP	-1	-0.881	-0.956	11.299	-25.962	-25.962	0.000	0.000	0.000	0.000
174	A	178	GLU	-1	-0.780	-0.862	13.086	-16.710	-16.710	0.000	0.000	0.000	0.000
175	A	179	LEU	0	-0.026	-0.004	15.594	0.288	0.288	0.000	0.000	0.000	0.000
176	A	180	VAL	0	-0.017	-0.016	9.960	-0.119	-0.119	0.000	0.000	0.000	0.000
177	A	181	TYR	0	0.002	0.016	11.374	-1.490	-1.490	0.000	0.000	0.000	0.000
178	A	182	ASN	0	-0.017	-0.024	12.807	0.592	0.592	0.000	0.000	0.000	0.000
179	A	183	ILE	0	-0.033	-0.007	11.438	0.870	0.870	0.000	0.000	0.000	0.000
180	A	184	HIS	0	0.027	0.028	9.941	-0.909	-0.909	0.000	0.000	0.000	0.000
181	A	185	LEU	0	-0.020	0.000	12.835	0.663	0.663	0.000	0.000	0.000	0.000
182	A	186	ALA	0	0.000	-0.004	15.896	0.959	0.959	0.000	0.000	0.000	0.000
183	A	187	VAL	0	-0.016	-0.018	12.991	0.897	0.897	0.000	0.000	0.000	0.000
184	A	188	ASN	0	0.013	-0.014	12.232	0.093	0.093	0.000	0.000	0.000	0.000
185	A	189	PHE	0	0.008	0.010	15.462	0.753	0.753	0.000	0.000	0.000	0.000
186	A	190	LEU	0	-0.020	-0.016	18.335	0.809	0.809	0.000	0.000	0.000	0.000
187	A	191	VAL	0	-0.053	-0.031	13.681	0.618	0.618	0.000	0.000	0.000	0.000
188	A	192	SER	0	0.011	0.002	17.008	0.156	0.156	0.000	0.000	0.000	0.000
189	A	193	LEU	0	-0.020	0.012	19.529	0.670	0.670	0.000	0.000	0.000	0.000
190	A	194	LEU	0	-0.025	-0.009	18.749	0.726	0.726	0.000	0.000	0.000	0.000
191	A	195	LYS	1	0.862	0.924	21.904	11.052	11.052	0.000	0.000	0.000	0.000
192	A	196	LYS	1	0.878	0.918	19.829	12.745	12.745	0.000	0.000	0.000	0.000
193	A	197	ASN	0	0.091	0.062	17.349	-0.128	-0.128	0.000	0.000	0.000	0.000
194	A	198	TRP	0	0.017	0.012	7.380	-0.122	-0.122	0.000	0.000	0.000	0.000
195	A	199	GLN	0	0.037	0.016	13.947	0.169	0.169	0.000	0.000	0.000	0.000
196	A	200	ASN	0	-0.056	-0.059	16.405	0.520	0.520	0.000	0.000	0.000	0.000
197	A	201	VAL	0	0.024	0.024	12.895	0.645	0.645	0.000	0.000	0.000	0.000
198	A	202	ARG	1	0.817	0.903	14.876	13.844	13.844	0.000	0.000	0.000	0.000
199	A	203	ALA	0	0.049	0.019	12.562	-0.456	-0.456	0.000	0.000	0.000	0.000
200	A	204	LEU	0	-0.026	0.004	9.429	1.053	1.053	0.000	0.000	0.000	0.000
201	A	205	TYR	0	0.033	0.010	11.936	-0.222	-0.222	0.000	0.000	0.000	0.000
202	A	206	ILE	0	0.026	0.001	11.481	-0.046	-0.046	0.000	0.000	0.000	0.000
203	A	207	LYS	1	0.954	0.979	14.959	16.729	16.729	0.000	0.000	0.000	0.000
204	A	208	SER	0	-0.003	0.018	17.527	0.593	0.593	0.000	0.000	0.000	0.000
205	A	209	THR	0	-0.053	-0.040	21.217	-0.252	-0.252	0.000	0.000	0.000	0.000
206	A	210	MET	-1	-0.846	-0.924	22.500	-13.537	-13.537	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:5:VAL)