FMO DATABASE

FMODB ID: QLJVY

Calculation Name: 3JCU-S-Other547

Preferred Name:

Target Type:

Ligand Name: chlorophyll a | chlorophyll b | pheophytin a | protoporphyrin ix containing fe | digalactosyl diacyl glycerol (dgdg) | 2,3-dimethyl-5-(3,7,11,15,19,23,27,31,35-nonamethyl-2,6,10,14,18,22,26,30,34-hexatriacontanonaenyl-2,5-cyclohexadiene-1,4-dione-2,3-dimethyl-5-solanesyl-1,4-benzoquinone | (3s,5r,6s,3's,5'r,6's)-5,6,5',6'-diepoxy-5,6,5',6'-tetrahydro-beta,beta-carotene-3,3'-diol | (1r,3r)-6-{(3e,5e,7e,9e,11e,13e,15e,17e)-18-[(1s,4r,6r)-4-hydroxy-2,2,6-trimethyl-7-oxabicyclo[4.1.0]hept-1-yl]-3,7,12,16-tetramethyloctadeca-1,3,5,7,9,11,13,15,17-nonaenylidene}-1,5,5-trimethylcyclohexane-1,3-diol | (3r,3'r,6s)-4,5-didehydro-5,6-dihydro-beta,beta-carotene-3,3'-diol | 1,2-di-o-acyl-3-o-[6-deoxy-6-sulfo-alpha-d-glucopyranosyl]-sn-glycerol | beta-carotene | 1,2-distearoyl-monogalactosyl-diglyceride | 1,2-dipalmitoyl-phosphatidyl-glycerole | ca-mn4-o5 cluster | bicarbonate ion | fe (ii) ion

Ligand 3-letter code: CLA | CHL | PHO | HEM | DGD | PL9 | XAT | NEX | LUT | SQD | BCR | LMG | LHG | OEX | BCT | FE2

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3JCU

Chain ID: S

ChEMBL ID:

UniProt ID: P12333

Base Structure: ElectronMicroscopy

Registration Date: 2025-10-05

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	214
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2084769.206257
FMO2-HF: Nuclear repulsion	2003831.456595
FMO2-HF: Total energy	-80937.749662
FMO2-MP2: Total energy	-81176.409223

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:23:LEU)

Summations of interaction energy for fragment #1(A:23:LEU)

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.
-144.368	-140.993	14.274	-3.004	-14.645	-0.14

Interaction energy analysis for fragmet #1(A:23:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.808 / q_NPA : 0.949

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	25	LYS	1	0.992	0.978	2.576	46.882	41.104	0.433	7.228	-1.883	-0.016
4	A	26	TRP	0	-0.071	-0.046	2.085	-0.134	0.697	3.919	-2.232	-2.517	-0.022
5	A	27	TYR	0	0.053	0.028	2.382	-8.827	-5.106	1.333	-2.223	-2.831	-0.025
6	A	28	GLY	0	0.048	0.032	4.871	0.622	0.635	-0.001	-0.002	-0.010	0.000
158	A	180	ASP	-1	-0.830	-0.953	2.519	-87.052	-82.413	4.432	-3.981	-5.090	-0.052
159	A	181	GLN	0	-0.034	-0.016	4.449	-3.027	-2.939	-0.001	-0.008	-0.079	0.000
162	A	184	LEU	0	-0.023	-0.026	1.788	-5.964	-6.166	4.161	-1.784	-2.176	-0.025
163	A	185	LEU	0	-0.050	-0.022	5.272	3.677	3.685	-0.001	0.000	-0.007	0.000
165	A	187	VAL	0	-0.003	-0.001	4.520	2.182	2.237	-0.001	-0.002	-0.052	0.000
7	A	29	PRO	0	0.021	-0.004	7.695	-0.190	-0.190	0.000	0.000	0.000	0.000
8	A	30	ASP	-1	-0.877	-0.932	7.377	-26.451	-26.451	0.000	0.000	0.000	0.000
9	A	31	ARG	1	0.714	0.867	6.299	23.444	23.444	0.000	0.000	0.000	0.000
10	A	32	ARG	1	0.889	0.939	7.013	33.970	33.970	0.000	0.000	0.000	0.000
11	A	33	ILE	0	0.086	0.045	9.111	-0.796	-0.796	0.000	0.000	0.000	0.000
12	A	34	PHE	0	-0.007	-0.014	12.451	0.410	0.410	0.000	0.000	0.000	0.000
13	A	35	LEU	0	-0.008	-0.014	15.241	0.844	0.844	0.000	0.000	0.000	0.000
14	A	36	PRO	0	-0.077	-0.020	13.133	0.252	0.252	0.000	0.000	0.000	0.000
15	A	37	ASP	-1	-0.801	-0.901	15.041	-20.393	-20.393	0.000	0.000	0.000	0.000
16	A	38	GLY	0	-0.040	-0.016	17.593	0.471	0.471	0.000	0.000	0.000	0.000
17	A	39	LEU	0	-0.058	-0.042	20.475	0.729	0.729	0.000	0.000	0.000	0.000
18	A	40	LEU	0	-0.051	-0.015	16.488	0.409	0.409	0.000	0.000	0.000	0.000
19	A	41	ASP	-1	-0.934	-0.975	19.492	-15.042	-15.042	0.000	0.000	0.000	0.000
20	A	42	ARG	1	0.833	0.921	12.319	20.988	20.988	0.000	0.000	0.000	0.000
21	A	43	ASP	-1	-0.873	-0.923	18.228	-12.947	-12.947	0.000	0.000	0.000	0.000
22	A	44	ASP	-1	-0.923	-0.981	16.805	-17.386	-17.386	0.000	0.000	0.000	0.000
23	A	45	ILE	0	-0.046	-0.017	20.511	0.225	0.225	0.000	0.000	0.000	0.000
24	A	46	PRO	0	-0.009	0.022	16.072	0.302	0.302	0.000	0.000	0.000	0.000
25	A	47	GLU	-1	-0.982	-1.000	16.524	-18.442	-18.442	0.000	0.000	0.000	0.000
26	A	48	TYR	0	-0.064	-0.054	18.677	1.041	1.041	0.000	0.000	0.000	0.000
27	A	49	LEU	0	-0.012	0.022	14.873	-0.307	-0.307	0.000	0.000	0.000	0.000
28	A	50	ASN	0	0.038	0.026	13.476	-1.095	-1.095	0.000	0.000	0.000	0.000
29	A	51	GLY	0	0.013	-0.002	9.510	-0.838	-0.838	0.000	0.000	0.000	0.000
30	A	52	GLU	-1	-0.937	-0.976	7.882	-35.968	-35.968	0.000	0.000	0.000	0.000
31	A	53	VAL	0	-0.037	-0.011	8.583	-1.577	-1.577	0.000	0.000	0.000	0.000
32	A	54	PRO	0	-0.031	-0.020	6.827	-2.770	-2.770	0.000	0.000	0.000	0.000
33	A	55	GLY	0	0.026	0.000	6.937	2.944	2.944	0.000	0.000	0.000	0.000
34	A	56	ASP	-1	-0.776	-0.863	8.751	-20.784	-20.784	0.000	0.000	0.000	0.000
35	A	57	TYR	-1	-0.904	-0.943	9.373	-32.556	-32.556	0.000	0.000	0.000	0.000
36	A	58	GLY	0	0.107	0.034	11.969	1.121	1.121	0.000	0.000	0.000	0.000
37	A	59	TYR	0	-0.082	-0.041	14.877	1.466	1.466	0.000	0.000	0.000	0.000
38	A	60	ASP	-1	-0.825	-0.933	16.918	-14.504	-14.504	0.000	0.000	0.000	0.000
39	A	61	PRO	0	-0.036	-0.009	19.876	0.405	0.405	0.000	0.000	0.000	0.000
40	A	62	PHE	0	-0.039	-0.022	22.693	0.673	0.673	0.000	0.000	0.000	0.000
41	A	63	GLY	0	-0.014	0.014	23.424	0.526	0.526	0.000	0.000	0.000	0.000
42	A	64	LEU	0	-0.112	-0.056	24.354	0.213	0.213	0.000	0.000	0.000	0.000
43	A	65	GLY	0	0.150	0.076	21.297	-0.093	-0.093	0.000	0.000	0.000	0.000
44	A	66	LYS	1	0.887	0.939	22.334	10.975	10.975	0.000	0.000	0.000	0.000
45	A	67	LYS	1	0.941	0.985	24.392	11.013	11.013	0.000	0.000	0.000	0.000
46	A	68	PRO	0	0.087	0.040	20.222	-0.302	-0.302	0.000	0.000	0.000	0.000
47	A	69	GLU	-1	-0.896	-0.956	20.248	-12.573	-12.573	0.000	0.000	0.000	0.000
48	A	70	ASP	-1	-0.894	-0.949	22.664	-11.792	-11.792	0.000	0.000	0.000	0.000
49	A	71	PHE	0	0.056	0.031	14.687	0.013	0.013	0.000	0.000	0.000	0.000
50	A	72	ALA	0	0.028	0.016	18.132	-0.620	-0.620	0.000	0.000	0.000	0.000
51	A	73	LYS	1	0.883	0.934	19.183	11.611	11.611	0.000	0.000	0.000	0.000
52	A	74	TYR	0	0.000	-0.010	20.649	0.297	0.297	0.000	0.000	0.000	0.000
53	A	75	GLN	0	0.023	0.016	13.551	-1.249	-1.249	0.000	0.000	0.000	0.000
54	A	76	ALA	0	0.011	0.006	17.567	-0.414	-0.414	0.000	0.000	0.000	0.000
55	A	77	PHE	0	-0.034	-0.030	19.699	0.222	0.222	0.000	0.000	0.000	0.000
56	A	78	GLU	-1	-0.822	-0.872	16.388	-18.781	-18.781	0.000	0.000	0.000	0.000
57	A	79	LEU	0	0.010	-0.004	14.138	-0.164	-0.164	0.000	0.000	0.000	0.000
58	A	80	ILE	0	-0.018	-0.007	17.515	0.186	0.186	0.000	0.000	0.000	0.000
59	A	81	HIS	0	0.014	-0.001	21.147	0.266	0.266	0.000	0.000	0.000	0.000
60	A	82	ALA	0	-0.012	0.005	17.000	0.205	0.205	0.000	0.000	0.000	0.000
61	A	83	ARG	1	0.855	0.898	16.188	17.968	17.968	0.000	0.000	0.000	0.000
62	A	84	TRP	0	0.018	-0.001	19.929	0.416	0.416	0.000	0.000	0.000	0.000
63	A	85	ALA	0	0.005	0.012	21.560	0.521	0.521	0.000	0.000	0.000	0.000
64	A	86	MET	0	-0.023	-0.007	16.495	-0.003	-0.003	0.000	0.000	0.000	0.000
65	A	87	LEU	0	-0.022	-0.001	21.705	0.425	0.425	0.000	0.000	0.000	0.000
66	A	88	GLY	0	0.014	0.013	24.769	0.498	0.498	0.000	0.000	0.000	0.000
67	A	89	ALA	0	0.056	0.006	23.674	0.443	0.443	0.000	0.000	0.000	0.000
68	A	90	ALA	0	-0.017	-0.008	24.352	0.318	0.318	0.000	0.000	0.000	0.000
69	A	91	GLY	0	-0.001	-0.004	26.173	0.415	0.415	0.000	0.000	0.000	0.000
70	A	92	CYS	0	-0.081	-0.052	29.016	0.518	0.518	0.000	0.000	0.000	0.000
71	A	93	VAL	0	0.002	0.010	27.360	0.280	0.280	0.000	0.000	0.000	0.000
72	A	94	ILE	0	-0.013	-0.011	28.030	0.280	0.280	0.000	0.000	0.000	0.000
73	A	95	PRO	0	-0.003	-0.004	30.591	0.227	0.227	0.000	0.000	0.000	0.000
74	A	96	GLU	-1	-0.708	-0.862	33.766	-9.002	-9.002	0.000	0.000	0.000	0.000
75	A	97	ALA	0	-0.051	-0.027	31.265	0.142	0.142	0.000	0.000	0.000	0.000
76	A	98	PHE	0	-0.063	-0.039	31.701	0.036	0.036	0.000	0.000	0.000	0.000
77	A	99	ASN	0	0.026	0.004	35.860	0.333	0.333	0.000	0.000	0.000	0.000
78	A	100	LYS	1	0.920	0.981	34.556	9.166	9.166	0.000	0.000	0.000	0.000
79	A	101	PHE	0	-0.078	-0.045	37.236	0.168	0.168	0.000	0.000	0.000	0.000
80	A	102	GLY	0	0.004	0.022	40.497	0.005	0.005	0.000	0.000	0.000	0.000
81	A	103	ALA	0	-0.005	0.000	40.239	-0.110	-0.110	0.000	0.000	0.000	0.000
82	A	104	ASN	0	-0.100	-0.045	35.614	0.081	0.081	0.000	0.000	0.000	0.000
83	A	105	CYS	0	0.045	-0.002	37.664	-0.237	-0.237	0.000	0.000	0.000	0.000
84	A	106	GLY	0	-0.003	0.034	40.134	0.090	0.090	0.000	0.000	0.000	0.000
85	A	107	PRO	0	0.036	-0.013	41.956	0.134	0.134	0.000	0.000	0.000	0.000
86	A	108	GLU	-1	-0.842	-0.931	41.623	-7.701	-7.701	0.000	0.000	0.000	0.000
87	A	109	ALA	0	-0.043	-0.024	36.668	-0.048	-0.048	0.000	0.000	0.000	0.000
88	A	110	VAL	0	0.030	0.025	36.490	-0.078	-0.078	0.000	0.000	0.000	0.000
89	A	111	TRP	0	0.034	0.017	32.766	0.215	0.215	0.000	0.000	0.000	0.000
90	A	112	PHE	0	-0.011	-0.002	35.440	0.149	0.149	0.000	0.000	0.000	0.000
91	A	113	LYS	1	0.925	0.962	37.270	7.895	7.895	0.000	0.000	0.000	0.000
92	A	114	THR	0	0.005	-0.001	36.293	0.163	0.163	0.000	0.000	0.000	0.000
93	A	115	GLY	0	-0.004	0.000	39.609	0.033	0.033	0.000	0.000	0.000	0.000
94	A	116	ALA	0	-0.019	-0.013	40.968	0.149	0.149	0.000	0.000	0.000	0.000
95	A	117	LEU	0	-0.033	0.001	40.972	0.161	0.161	0.000	0.000	0.000	0.000
96	A	118	LEU	0	-0.034	-0.016	41.536	0.135	0.135	0.000	0.000	0.000	0.000
97	A	119	LEU	0	-0.043	-0.005	45.796	0.024	0.024	0.000	0.000	0.000	0.000
98	A	120	ASP	-1	-0.955	-0.980	47.814	-6.299	-6.299	0.000	0.000	0.000	0.000
99	A	121	GLY	0	-0.012	-0.002	49.207	0.082	0.082	0.000	0.000	0.000	0.000
100	A	122	ASN	0	-0.039	-0.028	46.733	-0.086	-0.086	0.000	0.000	0.000	0.000
101	A	123	THR	0	0.064	0.031	40.882	-0.036	-0.036	0.000	0.000	0.000	0.000
102	A	124	LEU	0	-0.042	0.000	42.915	0.077	0.077	0.000	0.000	0.000	0.000
103	A	125	ASN	0	0.006	0.002	37.065	-0.120	-0.120	0.000	0.000	0.000	0.000
104	A	126	TYR	0	0.117	0.068	39.996	0.064	0.064	0.000	0.000	0.000	0.000
105	A	127	PHE	0	-0.043	-0.032	39.465	0.065	0.065	0.000	0.000	0.000	0.000
106	A	128	GLY	0	0.046	0.023	44.614	0.174	0.174	0.000	0.000	0.000	0.000
107	A	129	LYS	1	0.901	0.941	45.161	6.846	6.846	0.000	0.000	0.000	0.000
108	A	130	ASN	0	-0.019	-0.013	41.820	-0.131	-0.131	0.000	0.000	0.000	0.000
109	A	131	ILE	0	-0.035	-0.010	42.211	0.158	0.158	0.000	0.000	0.000	0.000
110	A	132	PRO	0	-0.048	-0.001	44.972	0.151	0.151	0.000	0.000	0.000	0.000
111	A	133	ILE	0	-0.020	-0.031	42.239	0.110	0.110	0.000	0.000	0.000	0.000
112	A	134	ASN	0	0.144	0.067	44.464	-0.192	-0.192	0.000	0.000	0.000	0.000
113	A	135	LEU	0	0.055	0.003	43.512	-0.090	-0.090	0.000	0.000	0.000	0.000
114	A	136	VAL	0	-0.029	-0.005	44.286	-0.081	-0.081	0.000	0.000	0.000	0.000
115	A	137	LEU	0	-0.015	-0.010	43.347	0.027	0.027	0.000	0.000	0.000	0.000
116	A	138	ALA	0	0.021	0.022	40.269	-0.156	-0.156	0.000	0.000	0.000	0.000
117	A	139	VAL	0	0.070	0.036	39.644	-0.179	-0.179	0.000	0.000	0.000	0.000
118	A	140	VAL	0	-0.024	-0.004	40.152	-0.119	-0.119	0.000	0.000	0.000	0.000
119	A	141	ALA	0	-0.001	-0.004	38.415	-0.122	-0.122	0.000	0.000	0.000	0.000
120	A	142	GLU	-1	-0.916	-0.957	35.598	-8.838	-8.838	0.000	0.000	0.000	0.000
121	A	143	VAL	0	-0.005	-0.014	35.579	-0.242	-0.242	0.000	0.000	0.000	0.000
122	A	144	VAL	0	-0.044	-0.022	37.124	-0.105	-0.105	0.000	0.000	0.000	0.000
123	A	145	LEU	0	-0.033	-0.018	34.026	-0.141	-0.141	0.000	0.000	0.000	0.000
124	A	146	LEU	0	0.003	0.012	29.238	-0.297	-0.297	0.000	0.000	0.000	0.000
125	A	147	GLY	0	0.036	0.011	31.988	-0.223	-0.223	0.000	0.000	0.000	0.000
126	A	148	GLY	0	0.013	0.003	33.929	-0.057	-0.057	0.000	0.000	0.000	0.000
127	A	149	ALA	0	-0.006	-0.011	29.468	-0.137	-0.137	0.000	0.000	0.000	0.000
128	A	150	GLU	-1	-0.877	-0.925	28.033	-11.641	-11.641	0.000	0.000	0.000	0.000
129	A	151	TYR	0	0.011	0.008	29.930	-0.143	-0.143	0.000	0.000	0.000	0.000
130	A	152	TYR	0	-0.025	0.005	29.921	0.126	0.126	0.000	0.000	0.000	0.000
131	A	153	ARG	1	0.832	0.902	24.549	12.005	12.005	0.000	0.000	0.000	0.000
132	A	154	ILE	0	-0.044	-0.020	26.673	-0.440	-0.440	0.000	0.000	0.000	0.000
133	A	155	THR	0	-0.073	-0.043	28.920	0.227	0.227	0.000	0.000	0.000	0.000
134	A	156	ASN	0	-0.038	-0.031	29.628	-0.480	-0.480	0.000	0.000	0.000	0.000
135	A	157	GLY	0	0.056	0.038	26.827	-0.127	-0.127	0.000	0.000	0.000	0.000
136	A	158	LEU	0	-0.104	-0.045	23.940	0.060	0.060	0.000	0.000	0.000	0.000
137	A	159	ASP	-1	-0.873	-0.935	20.015	-14.841	-14.841	0.000	0.000	0.000	0.000
138	A	160	PHE	0	0.004	-0.019	15.670	0.355	0.355	0.000	0.000	0.000	0.000
139	A	161	GLU	-1	-0.908	-0.956	20.076	-13.728	-13.728	0.000	0.000	0.000	0.000
140	A	162	ASP	-1	-0.898	-0.957	17.215	-17.197	-17.197	0.000	0.000	0.000	0.000
141	A	163	LYS	1	0.789	0.928	20.280	13.961	13.961	0.000	0.000	0.000	0.000
142	A	164	LEU	0	0.011	0.034	15.528	-0.470	-0.470	0.000	0.000	0.000	0.000
143	A	165	HIS	0	-0.074	-0.071	13.150	0.818	0.818	0.000	0.000	0.000	0.000
144	A	166	PRO	0	0.073	0.046	16.669	-0.531	-0.531	0.000	0.000	0.000	0.000
145	A	167	GLY	0	0.050	0.015	17.535	-1.068	-1.068	0.000	0.000	0.000	0.000
146	A	168	GLY	0	0.020	0.008	18.893	0.874	0.874	0.000	0.000	0.000	0.000
147	A	169	PRO	0	-0.015	-0.022	20.924	-0.257	-0.257	0.000	0.000	0.000	0.000
148	A	170	PHE	0	-0.031	-0.011	20.747	0.354	0.354	0.000	0.000	0.000	0.000
149	A	171	ASP	-1	-0.851	-0.928	16.053	-19.956	-19.956	0.000	0.000	0.000	0.000
150	A	172	PRO	0	-0.028	0.010	19.606	0.068	0.068	0.000	0.000	0.000	0.000
151	A	173	LEU	0	0.057	-0.012	20.027	0.110	0.110	0.000	0.000	0.000	0.000
152	A	174	GLY	0	-0.084	-0.018	16.703	-0.059	-0.059	0.000	0.000	0.000	0.000
153	A	175	LEU	0	-0.002	0.002	13.786	-1.214	-1.214	0.000	0.000	0.000	0.000
154	A	176	ALA	0	0.047	0.042	12.975	-1.899	-1.899	0.000	0.000	0.000	0.000
155	A	177	LYS	1	0.791	0.891	10.927	20.983	20.983	0.000	0.000	0.000	0.000
156	A	178	ASP	-1	-0.841	-0.904	9.135	-26.594	-26.594	0.000	0.000	0.000	0.000
157	A	179	PRO	0	-0.022	-0.027	5.202	0.550	0.550	0.000	0.000	0.000	0.000
160	A	182	ALA	0	0.107	0.061	7.510	-0.959	-0.959	0.000	0.000	0.000	0.000
161	A	183	ALA	0	-0.004	0.001	4.813	1.081	1.081	0.000	0.000	0.000	0.000
164	A	186	LYS	1	0.992	1.008	8.381	29.229	29.229	0.000	0.000	0.000	0.000
166	A	188	LYS	1	0.921	0.951	7.227	37.090	37.090	0.000	0.000	0.000	0.000
167	A	189	GLU	-1	-0.823	-0.874	9.849	-18.067	-18.067	0.000	0.000	0.000	0.000
168	A	190	ILE	0	0.044	0.024	10.112	1.740	1.740	0.000	0.000	0.000	0.000
169	A	191	LYS	1	0.828	0.923	8.633	31.147	31.147	0.000	0.000	0.000	0.000
170	A	192	ASN	0	-0.057	-0.047	12.436	2.497	2.497	0.000	0.000	0.000	0.000
171	A	193	GLY	0	0.065	0.025	15.354	1.296	1.296	0.000	0.000	0.000	0.000
172	A	194	ARG	1	0.799	0.857	12.167	23.114	23.114	0.000	0.000	0.000	0.000
173	A	195	LEU	0	-0.002	0.007	16.505	0.991	0.991	0.000	0.000	0.000	0.000
174	A	196	ALA	0	0.005	0.018	18.292	1.034	1.034	0.000	0.000	0.000	0.000
175	A	197	MET	0	0.003	-0.003	18.543	1.028	1.028	0.000	0.000	0.000	0.000
176	A	198	PHE	0	-0.027	-0.001	20.713	0.744	0.744	0.000	0.000	0.000	0.000
177	A	199	SER	0	-0.020	-0.027	21.985	0.696	0.696	0.000	0.000	0.000	0.000
178	A	200	MET	0	-0.019	0.003	24.314	0.572	0.572	0.000	0.000	0.000	0.000
179	A	201	PHE	0	0.004	0.007	25.636	0.562	0.562	0.000	0.000	0.000	0.000
180	A	202	ALA	0	0.011	0.002	26.525	0.501	0.501	0.000	0.000	0.000	0.000
181	A	203	PHE	0	-0.014	-0.024	26.773	0.417	0.417	0.000	0.000	0.000	0.000
182	A	204	PHE	0	-0.017	-0.012	28.830	0.385	0.385	0.000	0.000	0.000	0.000
183	A	205	ILE	0	0.015	0.012	30.758	0.380	0.380	0.000	0.000	0.000	0.000
184	A	206	GLN	0	0.011	-0.003	30.078	0.324	0.324	0.000	0.000	0.000	0.000
185	A	207	ALA	0	0.013	0.040	33.935	0.241	0.241	0.000	0.000	0.000	0.000
186	A	208	TYR	0	-0.078	-0.031	35.833	0.334	0.334	0.000	0.000	0.000	0.000
187	A	209	VAL	0	-0.028	-0.013	36.850	0.220	0.220	0.000	0.000	0.000	0.000
188	A	210	THR	0	0.009	-0.023	36.077	0.222	0.222	0.000	0.000	0.000	0.000
189	A	211	GLY	0	-0.008	0.007	39.145	0.216	0.216	0.000	0.000	0.000	0.000
190	A	212	GLN	0	-0.049	-0.031	38.023	0.120	0.120	0.000	0.000	0.000	0.000
191	A	213	GLY	0	0.015	0.008	35.251	-0.178	-0.178	0.000	0.000	0.000	0.000
192	A	214	PRO	0	-0.009	-0.003	30.157	0.057	0.057	0.000	0.000	0.000	0.000
193	A	215	VAL	0	-0.019	-0.014	31.290	-0.180	-0.180	0.000	0.000	0.000	0.000
194	A	216	GLU	-1	-0.890	-0.954	33.249	-8.267	-8.267	0.000	0.000	0.000	0.000
195	A	217	ASN	0	-0.037	-0.022	33.507	0.293	0.293	0.000	0.000	0.000	0.000
196	A	218	LEU	0	-0.031	-0.013	29.335	-0.007	-0.007	0.000	0.000	0.000	0.000
197	A	219	SER	0	-0.037	-0.031	32.943	0.004	0.004	0.000	0.000	0.000	0.000
198	A	220	ALA	0	0.002	0.011	36.184	0.164	0.164	0.000	0.000	0.000	0.000
199	A	221	HIS	0	0.041	0.017	32.171	0.213	0.213	0.000	0.000	0.000	0.000
200	A	222	LEU	0	-0.071	-0.052	31.494	-0.111	-0.111	0.000	0.000	0.000	0.000
201	A	223	SER	0	-0.082	-0.022	35.471	0.117	0.117	0.000	0.000	0.000	0.000
202	A	224	ASP	-1	-0.885	-0.930	39.134	-7.515	-7.515	0.000	0.000	0.000	0.000
203	A	225	PRO	0	0.002	0.015	34.641	0.014	0.014	0.000	0.000	0.000	0.000
204	A	226	PHE	0	-0.055	-0.040	36.211	-0.148	-0.148	0.000	0.000	0.000	0.000
205	A	227	GLY	0	-0.011	0.002	39.051	0.134	0.134	0.000	0.000	0.000	0.000
206	A	228	ASN	0	0.003	-0.008	39.274	0.045	0.045	0.000	0.000	0.000	0.000
207	A	229	ASN	0	0.035	0.020	35.162	-0.190	-0.190	0.000	0.000	0.000	0.000
208	A	230	LEU	0	0.031	0.020	33.236	0.191	0.191	0.000	0.000	0.000	0.000
209	A	231	LEU	0	-0.027	-0.026	35.819	0.143	0.143	0.000	0.000	0.000	0.000
210	A	232	THR	0	-0.072	-0.039	38.902	0.225	0.225	0.000	0.000	0.000	0.000
211	A	233	VAL	0	0.010	-0.002	38.620	0.142	0.142	0.000	0.000	0.000	0.000
212	A	234	ILE	0	-0.069	-0.026	39.443	0.055	0.055	0.000	0.000	0.000	0.000
213	A	235	GLY	0	-0.033	-0.015	41.388	0.117	0.117	0.000	0.000	0.000	0.000
214	A	236	GLY	-1	-0.963	-0.967	44.811	-6.545	-6.545	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:23:LEU)