CN109837259B - Thermophilic esterase crystal three-dimensional structure derived from marine bacteria and expression purification method - Google Patents
Thermophilic esterase crystal three-dimensional structure derived from marine bacteria and expression purification method Download PDFInfo
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Abstract
The invention belongs to the field of biotechnology, and particularly relates to a thermophilic esterase crystal three-dimensional structure derived from marine bacteria and an expression and purification method thereof. The thermophilic esterase AlinE4 contains 190 amino acids, the molecular weight is about 20.5 kDa, and the isoelectric point is about 6.8; in the expression strainEscherichia coli BL21 has high solubility expression and shows good heat resistance, alkali resistance, salt resistance and heavy metal resistance; the esterase AlinE4 has a three-dimensional structure obtained by an X-ray diffraction method, and the resolution reaches 1.18A. The structure consists of 5 beta sheets, 9 alpha helices and 23 10 -a helical composition; wherein the 13 th serine, the 162 th aspartic acid and the 165 th histidine form an enzymatic active center; the 13 th serine, the 50 th glycine and the 81 th asparagine form an oxygen ion channel. The three-dimensional structure of the esterase AlinE4 can have wide application prospects in the aspects of screening chiral prodrug, modifying substrate in industrial enzyme preparations and improving enzyme activity.
Description
Technical Field
The invention belongs to the technical field of biology, and particularly relates to a crystal structure of protein esterase from marine bacteria and an expression and purification method thereof.
Background
Esterases (esterases EC 3.1.1.1) are a class of hydrolases that are capable of decomposing lipids into acids and alcohols by chemical reactions. Esterases usually have a catalytic triangle consisting of three amino acid residues, serine, histidine and aspartic acid, as their active centers; among them, serine residues are often present in a conserved pentapeptide sequence of GXSXG. Most esterases do not need auxiliary factors for catalytic reaction, and have universality and certain three-dimensional structure specificity on reaction substrates, so that the esterases are more and more concerned as a biocatalyst. Nowadays, esterases play an increasingly important role as an environmentally friendly, economical and clean catalyst in the fields of food, paper manufacture, fine chemical synthesis and medical diagnostics. The esterase used in industry is mainly from different organisms, particularly from fungi and bacteria, and the esterase from microorganisms has the advantages of high yield, stable reaction, low toxicity of byproducts, simple molecular biological operation and the like.
Since the esterase derived from marine sources generally has excellent properties related to marine environment, such as temperature stability, salt tolerance, alkali tolerance, low temperature tolerance, excellent chiral selectivity and the like, screening of esterase with unique characteristics from marine microorganisms becomes an important direction for screening chiral prodrugs and developing novel industrial enzyme preparations. The invention obtains the protein crystal of esterase AlinE4 by using a crystallization method and analyzes the three-dimensional structure of the protein crystal. The AlinE4 crystal structure has wide application prospect in chiral prodrug screening, substrate modification in industrial enzyme preparations and enzyme activity improvement.
Disclosure of Invention
The invention aims to provide an expression and purification method of a protein esterase derived from marine bacteria and a crystal three-dimensional structure of the protein esterase.
The invention includes providing a strain derived from marine bacteriaAltererythrobacter indicus DSM 18604 T The esterase AlinE4 is genetically engineered to obtain a method for efficient expression, purification and crystallization in Escherichia coli, and a three-dimensional crystal structure of the 1 st to 190 th amino acids of the esterase AlinE4 and application thereof in the industry.
The invention firstly takes the marine bacteria fromAltererythrobacter indicus DSM 18604 T The esterase AlinE4 was genetically engineered, and its full-length gene was cloned into a vector of pSMT 3. The esterase AlinE4 amino acid sequence is shown as SEQ.ID.NO1, and the nucleic acid sequence is shown as SEQ.ID and NO 2.
The invention preferably uses a prokaryotic expression system of E.coli (but not excluding other expression systems, such as expression in other bacteria or other eukaryotic cells), and the above proteins are expressed as fusion proteins, and preferably His tags are selected to be expressed in a soluble form (but not excluding other tags, such as MBP or GST tags are also expressed in a soluble form).
The invention also provides a method for expressing and purifying the protein from marine bacteriaAltererythrobacter indicusDSM 18604 T The method of esterase AlinE4, comprising: construction of fusion wild typealine4The recombinant vector of the full-length gene is used for transforming escherichia coli so as to express the fusion protein AlinE4 with a label, the obtained protein is subjected to a specific method for identifying the specific label, preferably Ni affinity chromatography (the separation principle is that a buffer solution with low imidazole concentration is used for sampling, and a buffer solution with high imidazole concentration is used for eluting) to separate target protein, and then the high-purity protein of AlinE4 is obtained by a gel filtration chromatography method.
Wherein the upstream primer for amplifying the esterase whole gene is aline4F (5' -TCGC)GGATCCATGGGCGAATCGCG-3’（ SEQ. ID. NO3），BamHI) and downstream primer are aline4R (5' -TCCG)CTCGAGTCACTTCTTCGCAG-3’（SEQ. ID. NO4），XhoI) (ii) a The expression plasmid is pSMT3, the transformation method is a CaCl2 transformation method, the transformation strain is Escherichia coli DH5 alpha, and the expression strain is Escherichia coli BL21 (DE 3).
Wherein, the balance buffer solution of the Ni affinity chromatography is preferentially selected from: 50mM Tris (pH 8.0), 100-500mM NaCl,5% glycerol, 10mM imidazole, 2mM β -Me,0.2mM PMSF;
the Ni affinity chromatography elution buffer is preferably selected from the following: 50mM Tris, pH 8.0, 500mM NaCl,5% glycerol, 250mM imidazole, 2mM β -Me;
the buffer solution for gel filtration chromatography is preferably selected from: 20mM Tris (pH 7.5), 100mM NaCl,2mM DTT.
The invention also provides a method for crystallizing the esterase AlinE4, which comprises the following specific steps: the esterase AlinE4 was concentrated to a concentration of 5-30mg/ml, and crystallization was carried out by the pendant drop vapor diffusion method using a crystallization Kit (Crystal Screen Kit I/II, index, salt, PEG/Ion, etc. from Hampton Research, etc.) as the primary screening condition for Crystal growth. The temperature is 4-25 deg.C, preferably 18 deg.C.
Crystallization conditions are as follows: the crystallization is carried out by a hanging drop gas phase diffusion method, the volume ratio of the protein solution to the crystallization reagent in the crystallization drops is in a range from 3 to 1, the preferred volume ratio is 1. The crystal growth is carried out at 4 to 25 degrees celsius (preferably 18 degrees celsius).
The invention also provides crystals of the esterase alinE4 protein with good diffraction performance.
The invention also provides the three-dimensional structure of the esterase AlinE4, which describes the secondary structure composition, the peptide chain trend, the tissue pattern and the three-dimensional molecular structure of the esterase AlinE 4. Wherein, diffraction is carried out aiming at esterase AlinE4 protein to obtain crystal diffraction data of the esterase AlinE4 protein, so as to be derived from bacteriaPseudomonas aeruginosaThe homologous GDSL family esterase TesA (PDB ID:4 JGG) is used as a model for structural analysis, and the three-dimensional structure of the esterase AlinE4 protein is finally obtained.
In a particular embodiment, a crystalline three-dimensional structure of esterase AlinE4 is provided, said esterase AlinE4 comprising 190 amino acids, having a molecular weight of about 20.5 kDa, and having an isoelectric point of about 6.8; the atoms in the crystalline three-dimensional structure have at least 40% of the atomic coordinates set forth in table 1, or any structure having an average root variance from the three-dimensional coordinates of the atoms of the backbone carbon skeleton of at least 40% of the amino acid residues in that coordinate of less than or equal to 1.2 a.
The invention obtains the crystal three-dimensional structure of the preferred esterase AlinE4, the resolution is 1.2A, and the space group of the crystal structure is P4 2 2 1 2. The unit cell parameters are: a =79.783 a, b =79.783 a, c =61.010 a, α = β = γ =90.000 °.
The crystal structure of the esterase alinE4 or the foldable part thereof has a three-dimensional structure determined by the atomic coordinates (x, y, z) ± (1.0, 1.0, 1.0) listed in figures 1, 2 and 3.
In a particular embodimentIn embodiments, the three-dimensional structure of the esterase AlinE4 has a protein molecule within a crystallographically asymmetric unit. The structure consists of 5 beta sheets, 9 alpha helices and 23 10 And (4) spiral composition.
Wherein the 5 β sheets are centered and the 9 α helices surround the α 1 sheet. Wherein, beta sheet 1, the amino acid segment containing Arg5-Gly 11; α 0 helix 1, an amino acid segment comprising Ser13-Ala 16; alpha helix 2, an amino acid segment comprising Tyr26-His 37; beta sheet 2, an amino acid segment comprising Ala41-Gly 47; alpha helix 3, an amino acid segment comprising Thr53-Asp 65; beta sheet 3, an amino acid segment comprising Leu73-Glu 77; alpha helix 4, an amino acid segment containing Gly80-Leu 84; alpha helix 5, an amino acid segment containing Pro89-Arg 105; beta sheet 4, the amino acid segment comprising Ile110-Met 113; 3 10 Helix 1, an amino acid segment containing Pro119-Leu 121; alpha helix 6, an amino acid segment containing Ala123-Asp 130; alpha helix 7, an amino acid segment comprising Ile132-Lys 139; beta sheet 5, an amino acid segment comprising Lys143-Val 145; alpha helix 8, an amino acid segment comprising Phe148-Val 152; 3 10 Helix 3, an amino acid segment containing Pro156-Leu 158; alpha helix 9, an amino acid segment containing Ala168-Ala 185.
The invention also provides an action mechanism of the esterase AlinE4 for playing the hydrolysis function of the esterase. In the crystal structure of the esterase AlinE4, the 13 th serine (Ser 13), the 162 th aspartic acid (Asp 162) and the 165 th histidine (His 165) form a catalytic triad to form an active center. The active center is occupied by a cadmium ion as shown in fig. 3.
The crystal structure of the esterase AlinE4, the 13 th serine (Ser 13), the 50 th glycine (Gly 50) and the 81 th asparagine (Asn 81) form an oxygen ion channel.
The invention also provides application of the three-dimensional structure of the esterase AlinE4 in chiral prodrug screening, substrate modification in industrial enzyme preparations and enzyme activity improvement.
Drawings
FIG. 1 is a cartoon representation of the three-dimensional structure of the esterase AlinE4 monomer, alpha helix and 3 10 For screwsBlue, beta sheet with yellow label, and random coil in gray.
FIG. 2 is a schematic diagram of the surface charge distribution and active sites of esterase AlinE4, with electron cloud density level =1.0.
Fig. 3 is a schematic diagram of the interaction between active center cadmium ion and catalytic triad, and the electron cloud density level =1.0.
FIG. 4 shows the results of protein purification and crystal screening of the esterase AlinE 4. Wherein, on (A): a schematic of the results obtained with AlinE4 molecular sieves using Superdex 75/600 (GE, USA); the following: SDS-PAGE of the AlinE4 molecular sieve eluted sample, protein Marker in the left lane. (B) AlinE4 crystal pictures.
Detailed Description
The present invention will be further described with reference to the following examples.
The following is a more detailed description of the present invention in connection with specific preferred embodiments and it is not intended that the practice of the invention be limited to these descriptions. For those skilled in the art to which the invention pertains, several simple deductions or substitutions can be made without departing from the spirit of the invention, and all shall be considered as belonging to the protection scope of the invention.
Example 1 expression purification of esterase AlinE4
Derived from marine bacteriaAltererythrobacter indicus DSM 18604 T The amino acid sequence of the esterase AlinE4 is shown in SEQ.ID.NO1, and the nucleic acid sequence is shown in SEQ.ID and NO 2.
Esterase prepared by molecular cloning technologyaline4The full-length gene is cloned on a vector of pSMT3 and used for expressing fusion protein with 6 His fused at the amino terminal, the recombinant vector is transformed into escherichia coli BL21 (DE 3), and when the OD600 reaches 0.8 by shaking culture at 37 ℃, IPTG with the final concentration of 0.5 mM is added for induction expression, the expression conditions are as follows: shaking at 16 deg.C for 20h or 20 deg.C for 16h or 25 deg.C for 8h.
The constructed recombinant expression vector is transformed into escherichia coli BL21 (DE 3) to carry out soluble expression of esterase AlinE 4. Transferring the recombinant expression strain into LB liquid culture medium containing 50 ug/ml kanamycin and 34 ug/ml chloramphenicol as selective pressure, performing shake culture at 37 deg.C until OD600 reaches 0.8, adding IPTG with final concentration of 0.5 mM for induction expression, preferably under the following conditions: shaking and culturing at 16 deg.C for 20h. When OD600 reached 0.8, IPTG was added to a final concentration of 0.5 mM for induction of expression. The cells were cultured at 16 ℃ with shaking at 200rpm, and after 20 hours, the cells were collected by centrifugation and used for purification.
The expression bacteria collected by centrifugation were suspended in an appropriate amount of buffer (50 mM Tris (pH 8.0), 500mM NaCl,5% glycerol, 10mM imidazole, 2 mM. Beta. -Me,0.2mM PMSF), the cells were lysed using a low-temperature ultra-high-pressure cell disruption apparatus (Guangzhou focused Biotechnology Co., ltd.), and centrifuged at 18000rpm for 1 hour to remove precipitates and other particulate impurities. After binding the centrifuged supernatant to Ni-NTA affinity media, the media was washed with 50mM Tris (pH 8.0), 500mM NaCl,5% glycerol, 50mM imidazole, 2mM β -Me buffer to remove contaminating proteins. The protein of interest is finally eluted from the affinity medium with an eluent of 50mM Tris (pH 8.0), 500mM NaCl,5% glycerol, 250mM imidazole, 2mM beta-Me, and the eluent is concentrated with a 10 kDa cut-off concentration tube. The concentrated protein solution was further purified by gel filtration chromatography (superdex 75, 16/600) using 20mM Tris (pH 7.5), 100mM NaCl,2mM DTT as a buffer. The eluted target protein was concentrated to a concentration of 60mg/ml, stored at-80 ℃ and used for crystallization experiments.
EXAMPLE 2 crystallization of esterase AlinE4
The esterase AlinE4 expressed and purified as above was concentrated to a concentration of about 60mg/ml, and crystallized by the hanging drop gas phase diffusion method using a crystallization Kit (Crystal Screen Kit I/II, index, salt, PEG/Ion, etc. from Hampton Research et al) as a primary screening condition for Crystal growth. The present invention obtains initial crystals under a plurality of different crystallization reagent conditions. By post optimization adjustment, preferably 50mM cadmium sulfate, 100mM Hepes (pH 7.5), 1M sodium acetate buffer as crystal growth conditions, a set of X-ray diffraction data was collected with a resolution of 1.18 a.
Example 3 Collection of receipts and structural analysis of esterase AlinE4
The prepared crystal is frozen and stored in liquid nitrogen after being treated by 25 percent of glycerin as an antifreeze. Data collection for crystal X-ray diffraction was performed at the Shanghai illuminant (SSRF) biomacromolecule crystallography Beam line station (five lines six station BL17U 1). Data processing Using HKL2000, structural analysis to derive from bacteriaPseudomonas aeruginosaThe homologous GDSL family esterase TesA (PDB ID:4 JGG) is taken as a model, a molecular replacement method is adopted, a Refmac program is utilized, coot software is used for further correction, and finally the crystal structure of the esterase AlinE4 protein is obtained through analysis. One of ordinary skill in the art would know that either the atoms in the crystalline three-dimensional structure have atomic coordinates of at least 40% as listed in table 1, or the atomic structure coordinates of the backbone carbon backbone of at least 40% of the amino acids in the crystalline three-dimensional structure of the 3D protein have atomic coordinates having an average root variance less than or equal to 1.2 a from the coordinates in table 1, can be considered to have a raney structure with the 3D protein.
Specifically, the crystal three-dimensional structure of the esterase AlinE4 has two asymmetric molecules in one crystallography asymmetric unit. From 5 beta sheets, 9 alpha helices and 23 10 The helix composition, wherein, the 5 beta sheet in the center, the 9 alpha helix around the alpha 1 folding. Wherein, beta sheet 1, the amino acid segment containing Arg5-Gly 11; α 0 helix 1, an amino acid segment comprising Ser13-Ala 16; alpha helix 2, an amino acid segment comprising Tyr26-His 37; beta sheet 2, an amino acid segment comprising Ala41-Gly 47; alpha helix 3, an amino acid segment comprising Thr53-Asp 65; beta sheet 3, an amino acid segment comprising Leu73-Glu 77; alpha helix 4, an amino acid segment containing Gly80-Leu 84; alpha helix 5, an amino acid segment containing Pro89-Arg 105; beta sheet 4, the amino acid segment comprising Ile110-Met 113; 3 10 Helix 1, an amino acid segment containing Pro119-Leu 121; alpha helix 6, an amino acid segment containing Ala123-Asp 130; alpha helix 7, an amino acid segment comprising Ile132-Lys 139; beta sheet 5, an amino acid segment comprising Lys143-Val 145; alpha helix 8, an amino acid segment comprising Phe148-Val 152; 3 10 Helix 3, an amino acid segment containing Pro156-Leu 158; the alpha-helix 9 is arranged such that,i.e., the amino acid segment containing Ala168-Ala 185.
The atomic coordinate groups of the protease AlinE4 crystals are as follows (see table 1):
crystal space group: p4 2 2 1 2 ；
The unit cell parameters are: : a =79.783 a, b =79.783 a, c =61.010 a, α = β = γ =90.000 °;
I/σI：20.66 ；
Rwork/Rfree are respectively: 0.178 and 0.189;
resolution range (a): 48.46-1.18;
data integrity (%): 99.03.
TABLE 1
Atom 1N SER A0-25.136 6.782 8.343 1.00 13.15N
Atom 2 CA SER A0-24.109.5.938 8.933 1.00 14.44C
Atom 3C SER A0-24.369 5.715 10.411 1.00 13.02C
Atom 4O SER A0-25.061 6.500.043.00.12.87O
Atom 6 OG SER A0-22.450.888 7.441 1.00 16.45O
Atom 7N AMET A1-23.828 4.622.932 0.60.33N
Atom 8 CA AMET A1-23.950 4.306.339 0.60.93C
Atom 9C AMET A1-22.860 5.014 13.127 0.60.95C
Atom 10O AMET A1-21.779.5.316.607 0.60.57O
Atom 11 CB AMET A1-23.780 2.802.12.541 0.60.63C
Atom 12 CG AMET A1-24.842 1.983.858 0.60.18.90C
Atom 13 SD AMET A1-26.398 2.188 12.725 0.60.10S
Atom 14 CE AMET A1-26.119 1.125.136 0.60.17C
Atom 15N BMET A1-23.846 4.624 10.963.40.40N
Atom 16 CA BMET A1-24.059.313.367 0.40.02C
Atom 17C BMET A1-22.876.793.196 0.40.27C
Atom 18O BMET A1-21.725.4.729.753 0.40.88O
Atom 19 CB BMET A1-24.236 2.807 12.569.40.54C
Atom 21 SD BMET A1-25.777 0.516.444.40.65S
Atom 22 CE BMET A1-25.532 0.569.216.40.95C
Atom 23N GLY A2-23.165 5.293 14.385 1.00 12.68N
Atom 24 CA GLY A2-22.127 5.508 15.366 1.00 14.43C
Atom 25C GLY A2-21.852 6.972 15.653 1.00 12.05C
Atom 26O GLY A2-22.087.864 14.836 1.00.21O
Atom 27N GLU A3-21.270 7.186.16.828 1.00 12.79N
Atom 28 CA GLU A3-20.766 8.488 17.231.00 11.17C
Atom 29C GLU A3-19.627 8.920.314 1.00 10.90C
Atom 30O GLU A3-18.928 8.103.103.702.00.10.75O
Atom 31 CB GLU A3-20.262.8.446 18.674 1.00 13.18C
Atom 32 CG GLU A3-19.216.7.406 18.917 1.00 16.03C
Atom 33 CD GLU A3-19.799.185.19.575 1.00 25.79C
Atom 34 OE1 GLU A3-19.307 5.801 20.655.00.31.35O
Atom 35 OE2 GLU A3-20.764 5.619 19.019 1.00 25.45O
Atom 36N SER A4-19.448 10.231.232.1.00.83N
Atom 37 CA SER A4-18.447 10.807 15.354 1.00 11.13C
Atom 38C SER A4-17.035 10.540.865 1.00 11.57C
Atom 39O SER A4-16.801 10.366.366 17.068.00.12.43O
Atom 40 CB SER A4-18.679.311 15.259 1.00.73C
Atom 41 OG SER A4-19.938 12.582 14.669.00 11.07O
Atom 42N ARG A5-16.089.526.14.927.00.11.42N
Atom 43 CA ARG A5-14.668 10.414 15.229 1.00 11.52C
Atom 44C ARG A5-14.116.11.760.679.00.12.36C
Atom 45O ARG A5-14.306.12.781 15.009 1.00 15.39O
Atom 46 CB ARG A5-13.897.965 13.986.00 12.50C
Atom 47 CG ARG A5-14.543 8.836 13.189.00 12.46C
Atom 48 CD ARG A5-14.555 7.514.514.973.00 12.96C
Atom 49 NE ARG A5-13.252 7.198 14.553 1.00 12.81N
Atom 50 CZ ARG A5-12.238 6.679.865 1.00 13.25C
Atom 51 NH1 ARG A5-12.355 6.417 12.568 1.00 13.94N
Atom 52 NH2 ARG A5-11.084.443.14.477 1.00 15.37N
Atom 53N VAL A6-13.388.11.764 16.783.00 10.09N
Atom 54 CA VAL A6-12.930 13.013 17.375 1.00 9.75C
Atom 55C VAL A6-11.516 13.334 16.903 1.00 10.09C
Atom 56O VAL A6-10.593.12.526.068.00.10.20O
Atom 57 CB VAL A6-13.001 12.937.904.00 11.36C
Atom 58 CG1 VAL A6-12.447 14.208 19.528 1.00 11.71C
Atom 60N ILE A7-11.339 14.524.333.1.00 9.59N
Atom 62C ILE A7-9.731 16.304.532 1.00 8.22C
Atom 63O ILE A7-10.578 17.197.570.1.00 10.70O
Atom 64 CB ILE A7-10.034.180 14.312.00 9.15C
Atom 66 CG2 ILE A7-8.671 15.716.857.00 9.86C
Atom 68N LEU A8-8.526 16.423 17.092.00.8.82N
Atom 70C LEU A8-7.319 18.491 16.628 1.00 8.26C
Atom 71O LEU A8-6.324.18.004 16.089.00 10.08O
Atom 74 CD1 LEU A8-7.651 19.488 20.156.1.00.16C
Atom 76N ALA A9-7.781 19.705 16.332.00.8.28N
Atom 78C ALA A9-6.344 21.640 16.322.00.8.30C
Atom 79O ALA A9-6.948.594 16.808 1.00.9.31O
Atom 81N PHE A10-5.047.416.554 1.00.7.56N
Atom 83C PHE A10-3.337.23.106.748 1.00.07C
Atom 84O PHE A10-2.350.647 16.170.00.9.14O
Atom 86 CG PHE A10-2.834 21.846 19.604 1.00 7.78C
Atom 87 CD1 PHE A10-3.601 22.218 20.699.00.9.35C
Atom 88 CD2 PHE A10-1.461 22.069.645.1.00.05C
Atom 89 CE1 PHE A10-3.012 22.796.831 1.00 9.54C
Atom 91 CZ PHE A10-1.640 23.017 21.861 1.00.66C
Atom 92N GLY A11-3.658 24.395 16.706.00.8.30N
Atom 93 CA GLY A11-2.914 25.300.861 1.00.28C
Atom 94C GLY A11-3.099.26.755 16.204.00.7.97C
Atom 95O GLY A11-3.444 27.109.109.333.1.00 8.56O
Atom 96N ASP A12-2.840.27.598.205.00.9.02N
Atom 97 CA ASP A12-2.819 29.042.388.388 1.00.30C
Atom 98C ASP A12-3.929.29.699.572 1.00.96C
Atom 99O ASP A12-5.020 29.130.453.00 1.00 10.25O
Atom 100 CB ASP A12-1.420.621 15.119.00 9.85C
Atom 101 CG ASP A12-0.887.29.257 13.757.00 10.69C
Atom 102 OD1 ASP A12-1.707 29.077.825 1.00 10.57O
Atom 103 OD2 ASP A12.347.29.179 13.591 1.00 10.54O
Atom 104N ASER A13-3.676 30.882 14.009 0.52.62N
Atom 105 CA ASER A13-4.723 31.579.265 0.52.26C
Atom 106C ASER A13-5.175 30.818.12.025 0.52.74C
Atom 107O ASER A13-6.287 31.062 11.537 0.52.93O
Atom 108 CB ASER A13-4.266 32.986.876.52.16.09C
Atom 109 OG ASER A13-3.065.943.127 0.52.42O
Atom 110N BSER A13-3.668 30.884.009 0.48.66N
Atom 111 CA BSER A13-4.697.589.245.0.48.29C
Atom 112C BSER A13-5.200.30.767.068.48.72C
Atom 113O BSER A13-6.363 30.914 11.662 0.48.20O
Atom 114 CB BSER A13-4.164 32.930 12.737 0.48.13C
Atom 115 OG BSER A13-3.942 33.838 13.799.48.63O
Atom 116N LEU A14-4.348 29.911 11.497 1.00 10.58N
Atom 117 CA LEU A14-4.760 LEU 29.126 10.338 1.00 11.76C
Atom 118C LEU A14-5.799.076.692.1.00 10.98C
Atom 119O LEU A14-6.521 27.609.9.800.00.13.94O
Atom 120 CB LEU A14-3.556 28.458 9.682 1.00.48C
Atom 121 CG LEU A14-2.444 29.390 9.206 1.00 16.19C
Atom 122 CD1 LEU A14-1.297 28.584 8.603.00 16.99C
Atom 123 CD2 LEU A14-2.961 30.410.189.00 18.22C
Atom 124N PHE A15-5.868 27.661 11.956.00.9.59N
Atom 125 CA PHE A15-6.958 26.817 12.416 1.00 10.07C
Atom 126C PHE A15-8.080 27.620.055 1.00.19C
Atom 127O PHE A15-9.246 27.258 12.895.00 12.38O
Atom 128 CB PHE A15-6.449 25.769.412.412.00 10.09C
Atom 129 CG PHE A15-5.767.24.584 12.771 1.00.26C
Atom 130 CD1 PHE A15-5.569.24.506 11.395 1.00 10.69C
Atom 131 CD2 PHE A15-5.311 23.545 13.564 1.00 9.46C
Atom 132 CE1 PHE A15-4.941 23.397 10.831 1.00 11.45C
Atom 133 CE2 PHE A15-4.687.443 13.016.1.00 10.15C
Atom 134 CZ PHE A15-4.508 22.363 11.641 1.00 10.77C
Atom 135N ALA A16-7.760 28.716.759.00 11.29N
Atom 136 CA ALA A16-8.800 29.516 14.405 1.00 11.74C
Atom 137C ALA A16-9.748 30.157.13.399 1.00 14.30C
Atom 138O ALA A16-10.896.30.453.13.747.00.17.14O
Atom 139 CB ALA A16-8.176 ALA A30.599.284 1.00 12.72C
Atom 140N GLY A17-9.296, 30.397 12.171, 1.00 13.40N
Atom 141 CA GLY A17-10.141.31.030 11.175 1.00 14.78C
Atom 142C GLY A17-10.111.32.544 11.238.1.00 17.09C
Atom 143O GLY A17-11.139 33.199 11.031 1.00 16.87O
Atom 144N TYR A18-8.935 33.112.497 1.00 17.49N
Atom 145 CA TYR A18-8.805 34.557 11.632 1.00 17.26C
Atom 146C TYR A18-9.291 35.261.261.371 1.00 20.22C
Atom 147O TYR A18-8.893.34.910.9.255.00.19.20O
Atom 148 CB TYR A18-7.341 34.919 11.894.00 22.05C
Atom 149 CG TYR A18-7.062 36.401.401.768 1.00.28.04C
Atom 150 CD1 TYR A18-7.405 37.280.12.786.00.31.28C
Atom 151 CD2 TYR A18-6.469.921 10.628.00.28.39C
Atom 152 CE1 TYR A18-7.159 38.635 12.671 1.00 25.77C
Atom 153 CE2 TYR A18-6.219.38.274 10.504.1.00 33.60C
Atom 154 CZ TYR A18-6.563 39.125.11.528 1.00 32.23C
Atom 155 OH TYR A18-6.311 40.474.11.403.00.39.37O
Atom 156N GLY A19-10.148.36.267 10.556 1.00 18.60N
Atom 157 CA GLY A19-10.689.044.458 1.00.19.65C
Atom 158C GLY A19-11.837.398 8.723 1.00 19.43C
Atom 159O GLY A19-12.351 36.993.765 1.00.82O
Atoms 160N LEU A20-12.265 35.211.9.134.00 18.55N
Atom 161 CA LEU A20-13.314 34.485 8.437 1.00 20.13C
Atom 162C LEU A20-14.585 34.453.453.273 1.00 23.41C
Atom 163O LEU A20-14.575 34.701.483 1.00.25.09O
Atom 164 CB LEU A20-12.871 33.054.112.00.00C
Atom 165 CG LEU A20-11.585 32.949.298.1.00 15.79C
Atom 166 CD1 LEU A20-11.214.494 7.111.00.16.08C
Atoms 167 CD2 LEU A20-11.739 33.653 5.954 1.00 18.80C
Atom 168N ASP A21-15.689.34.142.602.00 25.57N
Atom 169 CA ASP A21-16.980.34.059.260.00 25.67C
Atom 170C ASP A21-17.167 32.673.868 1.00.22C
Atom 171O ASP A21-16.334 31.774 9.710 1.00 24.22O
Atom 172 CB ASP A21-18.100.34.424 8.288 1.00 33.33C
Atom 173 CG ASP A21-18.101.35.898.929.00.41.76C
Atom 174 OD1 ASP A21-17.477 36.693.666 1.00.48.45O
Atom 175 OD2 ASP A21-18.724 36.264.264 6.911 1.00 44.13O
Atom 176N LYS A22-18.279 32.501.576 1.00 26.79N
Atom 177 CA LYS A22-18.532 31.250.274 1.00.26C
Atom 178C LYS A22-18.669.105.105.281 1.00.64C
Atomic 179O LYS A22-19.364 30.220.267 1.00.36O
Atom 180 CB LYS A22-19.800.373 12.120.00 32.19C
Atom 181 CG LYS A22-19.903 30.352.247 1.00 41.27C
Atom 182 CD LYS A22-18.553 30.110.919 1.00 44.86C
Atom 183 CE LYS A22-18.120.301.14.767.00 56.10C
Atoms 184 NZ LYS A22-16.872 31.010 15.525 1.00 62.39N
Atom 185N GLY A23-17.985.29.003 10.568 1.00 20.94N
Atom 186 CA GLY A23-18.034.844 9.713.1.00 18.99C
Atom 187C GLY A23-17.086.864 8.534 1.00 14.68C
Atom 188O GLY A23-17.043.26.881 7.787.00.17.98O
Atom 189N GLU A24-16.317.938 8.346 1.00 15.50N
Atom 190 CA GLU A24-15.393 29.034.225.00.13.08C
Atom 191C GLU A24-13.964.621.621.568 1.00.12.66C
Atom 192O GLU A24-13.136 28.523 6.658 1.00 12.59O
Atom 193 CB GLU A24-15.385 30.461 6.670.00 17.05C
Atom 194 CG GLU A24-16.711 30.885.046.00 1.59C
Atom 195 CD GLU A24-16.694 32.310.520.00.22.67C
Atom 196 OE1 GLU A24-15.889.128.6.008 1.00 20.21O
Atom 197 OE2 GLU A24-17.488 32.613.613.607.00.25.96O
Atom 198N SER A25-13.652 28.365 8.838 1.00 12.48N
Atom 199 CA SER A25-12.286 28.003 9.194 1.00 10.79C
Atom 200C SER A25-11.922.26.639.630.1.00 10.99C
Atom 201O SER A25-12.778.812 8.305.00.11.17O
Atom 202 CB SER A25-12.118 27.946 10.713.713.00 14.60C
Atom 203 OG SER A25-12.770 26.810 11.263 1.00 13.45O
Atom 204N TYR A26-10.615 26.416 8.522 1.00 10.62N
Atom 205 CA TYR A26-10.101.25.133.050 1.00 10.38C
Atom 206C TYR A26-10.654 23.940 8.821 1.00 9.07C
Atom 207O TYR A26-11.108.22.978.175.00.9.46O
Atom 208 CB TYR A26-8.565 25.177 7.963.00.9.99C
Atom 209 CG TYR A26-7.961 23.841 7.609 1.00.56C
Atom 210 CD1 TYR A26-7.620.931 8.603.00.9.30C
Atom 211 CD2 TYR A26-7.738 23.487 6.289 1.00.29C
Atom 212 CE1 TYR A26-7.088.716 8.293 1.00.9.48C
Atom 213 CE2 TYR A26-7.202.263 5.969.00.9.46C
Atom 214 CZ TYR A26-6.873.21.376 6.972 1.00.8.83C
Atom 215 OH TYR A26-6.337 20.138.699.00.10.24O
Atom 216N PRO A27-10.654 23.918 10.164.164 1.00 8.87N
Atom 217 CA PRO A27-11.219.22.742 10.852 1.00.56C
Atom 218C PRO A27-12.687.22.505 10.523 1.00.14C
Atom 219O PRO A27-13.099.348 10.345.1.00.11.09O
Atom 220 CB PRO A27-10.959.043.335.1.00 10.70C
Atom 221 CG PRO A27-9.750 23.966.314 1.00 10.59C
Atom 222 CD PRO A27-10.011 24.844 11.117 1.00 9.67C
Atom 223N ALA A28-13.482.23.573 10.429 1.00 11.18N
Atom 224 CA ALA A28-14.901 23.411 10.122 1.00 12.41C
Atom 225C ALA A28-15.108.22.873.710.00.11.50C
Atom 226O ALA A28-15.932 21.977.490 1.00.12.28O
Atom 227 CB ALA A28-15.632 24.739.298.1.00 13.98C
Atom 228N LYS A29-14.363 23.400.736 1.00 9.97N
Atom 229 CA LYS A29-14.537 22.930 6.368 1.00 10.43C
Atoms 230C LYS A29-13.940 21.545 6.185.00 9.97C
Atom 231O LYS A29-14.454 20.743 5.394 1.00 11.07O
Atom 232 CB LYS A29-13.926 23.936 5.391 1.00 11.18C
Atom 233 CG LYS A29-14.739 25.225 5.256 1.00 12.80C
Atom 234 CD LYS A29-16.085.948.575 1.00 17.46C
Atom 235 CE LYS A29-16.924 26.205.394 1.00 19.90C
Atom 236 NZ LYS A29-16.437 27.080 3.284 1.00 18.49N
Atoms 237N LEU A30-12.859.21.240.6.913 1.00.91N
Atom 238 CA LEU A30-12.302 19.895.872 1.00.22C
Atom 239C LEU A30-13.304 18.879.405 1.00.9.75C
Atoms 240O LEU A30-13.454 17.789.6.845 1.00 10.03O
Atom 241 CB LEU A30-11.007 19.846 7.685 1.00.70C
Atom 242 CG LEU A30-10.344.18.485 7.881 1.00.82C
Atoms 243 CD1 LEU A30-9.897.897.897.560.00 10.43C
Atom 244 CD2 LEU A30-9.158 18.631 8.834 1.00 10.25C
Atom 245N GLU A31-13.996.19.220.490.1.00.73N
Atom 246 CA GLU A31-14.997 18.314 9.046.00 11.29C
Atom 247C GLU A31-16.031 17.941 7.990.00.25C
Atom 248O GLU A31-16.362 16.762 7.814.00 13.43O
Atom 249 CB GLU A31-15.661 18.972 10.255.1.00 13.29C
Atom 250 CG GLU A31-16.635 18.065.969.00 14.24C
Atom 251 CD GLU A31-17.212 18.697.224.00 13.81C
Atom 252 OE1 GLU A31-16.463 19.098.152.00 14.29O
Atom 253 OE2 GLU A31-18.448 18.798.296.1.00 19.44O
Atom 254N THR A32-16.528 18.935 7.255.00 11.26N
Atom 255 CA THR A32-17.510.18.651 6.216 1.00 13.69C
Atom 256C THR A32-16.908 17.805 5.103.00.12.96C
Atom 257O THR A32-17.541 16.851 4.628 1.00 12.69O
Atom 258 CB THR A32-18.066.959.660 1.00 14.30C
Atom 259 OG1 THR A32-18.711 20.680 6.714.00 19.11O
261N ALA A33-15.678 18.123.687.00.11.35N atom
Atom 262 CA ALA A33-15.044.406 3.584 1.00 11.34C
Atom 263C ALA A33-14.796.941 3.915 1.00.10.74C
Atom 264O ALA A33-14.853.084.021 1.00 11.89O
Atom 265 CB ALA A33-13.732 18.083 3.197 1.00 11.36C
Atom 266N LEU A34-14.534 15.622 5.184.184.00 9.80N
Atom 267 CA LEU A34-14.276 14.235.235 5.533 1.00 10.15C
Atom 268C LEU A34-15.486 13.334 5.296 1.00 9.87C
Atom 269O LEU A34-15.309 12.121.5.153.00.9.59O
Atom 270 CB LEU A34-13.795 14.144 6.981.00.38C
Atom 271 CG LEU A34-12.356 14.634 7.192 1.00 10.84C
Atom 272 CD1 LEU A34-12.015 14.669.668.1.00 11.24C
Atom 273 CD2 LEU A34-11.343 13.783.444 1.00 13.16C
Atom 274N ARG A35-16.699.898.254.00.10.18N
Atom 275 CA ARG A35-17.874 13.095.906.00.12.67C
Atom 276C ARG A35-17.678 12.388 3.574 1.00 13.88C
Atom 277O ARG A35-18.127.248 3.391.00.16.32O
Atom 278 CB ARG A35-19.120.13.979.840.1.00.32C
Atom 279 CG ARG A35-19.604 14.529 6.167 1.00 19.57C
Atom 281 NE ARG A35-20.868 16.575 6.784.00 33.65N
Atom 282 CZ ARG A35-21.670 17.615.615.585 1.00.12C
Atom 283 NH1 ARG A35-22.527 17.609 5.572 1.00 41.74N
Atom 284 NH2 ARG A35-21.617 18.659.400.00 46.45N
Atom 285N SER A36-16.982.036.641 1.00.12.10N
Atom 286 CA SER A36-16.747.460.1.325.00 13.80C
Atom 287C SER A36-15.702 11.362 1.359 1.00 13.62C
Atom 288O SER A36-15.495 10.691 0.338 1.00 17.30O
Atom 289 CB SER A36-16.336 13.563 0.346 1.00 16.82C
Atom 290 OG SER A36-17.394 14.495 0.177 1.00.01O
Atom 291N HIS A37-15.078.153 2.511 1.00 11.37N
Atom 292 CA HIS A37-14.122 10.068.700.00 12.81C
Atom 293C HIS A37-14.756 8.970 3.557 1.00.54C
Atom 294O HIS A37-14.055 8.117 4.085.00.14.49O
Atom 295 CB HIS A37-12.840 10.575 3.361 1.00 13.57C
Atom 296 CG HIS A37-12.075 11.536 2.515 1.00 13.44C
Atom 297 ND1 HIS A37-10.916 11.188 1.856 1.00 16.12N
Atom 298 CD2 HIS A37-12.325 12.824 2.186.00 14.64C
Atom 299 CE1 HIS A37-10.475 12.229 1.176 1.00 14.01C
Atom 300 NE2 HIS A37-11.310 13.233 1.356 1.00 15.55N
Atom 301N GLY A38-16.077.026 3.728 1.00 11.83N
Atom 302 CA GLY A38-16.771 8.069.569.00 13.01C
Atom 303C GLY A38-16.602 8.282 6.058.00.12.55C
Atoms 304O GLY A38-16.815 7.342 6.826 1.00 14.90O
Atom 305N ILE A39-16.243 9.493 6.497 1.00 11.73N
Atom 306 CA ILE A39-15.917 9.775 7.894.00 11.88C
Atom 307C ILE A39-16.861 10.840.424.00.11.16C
Atom 308O ILE A39-16.977.924 7.844 1.00 11.31O
Atom 309 CB ILE A39-14.456 10.246 8.047.00 11.31C
Atom 310 CG1 ILE A39-13.497 9.122.7.667 1.00 12.03C
Atom 311 CG2 ILE A39-14.191 10.749.477 1.00 13.02C
Atom 312 CD1 ILE A39-12.087.605.332.1.00 14.48C
Atom 313N ASN A40-17.510.542.9.557 1.00 11.25N
Atom 314 CA ASN A40-18.223 11.535 10.348 1.00 11.79C
Atom 315C ASN A40-17.297 11.927.493 1.00 11.71C
Atom 316O ASN A40-17.099.146.12.434.00.10.38O
Atom 317 CB ASN A40-19.527 10.962 10.899.00 13.35C
Atom 318 CG ASN A40-20.639.10.964.874 1.00 13.90C
Atom 319 OD1 ASN A40-20.834 11.945 9.157 1.00 20.53O
Atom 320 ND2 ASN A40-21.373 9.858 796.00 14.77N
Atom 321N ALA A41-16.728 13.126 11.409 1.00 11.85N
Atom 322 CA ALA A41-15.793.628 12.403.00 11.21C
Atom 323C ALA A41-16.415 14.779.179 1.00 13.36C
Atom 324O ALA A41-17.291 15.496 12.680 1.00 15.55O
Atom 325 CB ALA A41-14.503 14.109.729.00 16.15C
Atom 326N ARG A42-15.974.927.421 1.00 10.59N
Atom 327 CA ARG A42-16.175 16.132.132.209 1.00 10.99C
Atom 328C ARG A42-14.778.16.682.412 1.00 11.21C
Atom 329O ARG A42-13.955 16.054.091 1.00 11.68O
Atom 330 CB ARG A42-16.804 15.813 16.562 1.00 12.24C
Atom 331 CG ARG A42-16.941 17.032 17.442 1.00.06C
Atom 332 CD ARG A42-17.801 16.774 18.678 1.00 18.79C
Atom 333 NE ARG A42-17.168 15.945 19.708 1.00 17.21N
Atom 334 CZ ARG A42-16.253 16.379 20.574 1.00 20.51C
Atom 335 NH1 ARG A42-15.830 17.636 20.528 1.00 19.19N
Atom 336 NH2 ARG A42-15.768 15.555 21.497 1.00 17.67N
Atom 337N ILE A43-14.487 17.810 14.788.00 10.15N
Atom 338 CA ILE A43-13.153 18.381 14.867.00 10.86C
Atom 339C ILE A43-13.169 19.482.908 1.00 12.36C
Atom 340O ILE A43-13.877 20.488 15.761 1.00.14.83O
Atom 341 CB ILE A43-12.654 18.874 13.506 1.00 11.39C
Atom 342 CG1 ILE A43-12.703 17.717 12.504 1.00 11.46C
Atom 343 CG2 ILE A43-11.228 19.414 13.653 1.00 11.27C
Atom 344 CD1 ILE A43-12.003 17.998 11.183 1.00 11.61C
Atom 345N ILE A44-12.389 19.270 16.968.00.9.86N
Atom 346 CA ILE A44-12.194 20.251 18.027 1.00 10.61C
Atom 347C ILE A44-11.309 21.353 17.470.470 1.00 9.46C
Atom 348O ILE A44-10.146 21.113.17.116.00 11.41O
Atom 349 CB ILE A44-11.498 19.610 19.235 1.00 11.48C
Atom 350 CG1 ILE A44-12.210 18.355 19.728 1.00 13.63C
Atom 351 CG2 ILE A44-11.320 20.629 20.353 1.00 13.46C
Atom 352 CD1 ILE A44-11.257 17.423 20.455 1.00 14.90C
Atom 353N ASN A45-11.836 22.565 17.398 1.00 10.86N
Atom 354 CA ASN A45-11.035 23.682 16.912 1.00 9.72C
Atom 355C ASN A45-10.284 24.257 18.101 1.00 10.79C
Atom 356O ASN A45-10.818 25.066.865 1.00 13.36O
Atom 357 CB ASN A45-11.883 24.732 16.207 1.00 12.13C
Atom 358 CG ASN A45-11.028 25.733 15.468 1.00 11.80C
Atoms 359 OD1 ASN A45-9.875 25.965 15.856 1.00 13.53O
Atom 360 ND2 ASN A45-11.556 26.316.316.404 1.00 12.09N
Atom 361N ALA A46-9.039.811 18.267 1.00 10.20N
Atom 362 CA ALA A46-8.134 24.358 19.267 1.00 10.25C
Atom 363C ALA A46-7.113.25.288 18.629 1.00.04C
Atom 364O ALA A46-5.955 25.346.19.053.00.43O
Atom 365 CB ALA A46-7.478 23.251 20.088.00 11.08C
Atom 366N GLY A47-7.525.26.012 17.593.00.9.89N
Atom 367 CA GLY A47-6.692 27.059.050 1.00 10.26C
Atom 368C GLY A47-6.794.28.315.896.00.10.79C
Atom 369O GLY A47-7.877.717 18.332.00.12.90O
Atom 370N VAL A48-5.639 28.916 18.165.00 10.15N
Atom 371 CA VAL A48-5.574 30.165 18.909 1.00 11.29C
Atom 372C VAL A48-4.730.31.126.093.00.80C
Atom 373O VAL A48-3.548 30.862 17.839.00.10.86O
Atom 374 CB VAL A48-4.982.9829.983 20.315.00.11.83C
Atom 375 CG1 VAL A48-4.817 31.339 20.996.00 14.10C
Atom 376 CG2 VAL A48-5.881 29.078.138.1.00.13.07C
Atom 377N SER A49-5.324 32.239 17.685 1.00 11.85N
Atom 378 CA SER A49-4.607 33.195.16.857.00 13.79C
Atom 379C SER A49-3.393 33.721 17.611 1.00.73C
Atom 380O SER A49-3.472 34.038.800.1.00 15.81O
Atom 381 CB SER A49-5.536 34.340.16.465.00 15.44C
Atom 382 OG SER A49-6.521 33.866 15.556 1.00 19.05O
Atom 383N GLY A50-2.259 33.784.16.915 1.00 16.09N
Atom 384 CA GLY A50-1.031 34.276 17.504 1.00 17.30C
Atom 385C GLY A50-0.225.33.284 18.319 1.00.10C
Atom 386O GLY A50.868 33.643 18.781 1.00 15.63O
Atom 387N ASP A51-0.711 32.059.514.514 1.00 11.53N
Atom 388 CA ASP A51.030 31.084.308.308 1.00 10.34C
Atom 389C ASP A51.380.30.763.687.00.9.45C
Atom 390O ASP A51.461 30.355 17.530 1.00 10.15O
Atom 391 CB ASP A51-0.753 29.775 19.414 1.00 11.28C
Atom 392 CG ASP A51-1.389 29.561 20.771 1.00.58C
Atoms 393 OD1 ASP A51-1.572 30.539 21.534 1.00.07O
Atom 394 OD2 ASP A51-1.652 28.389 21.096.00 15.49O
Atom 395N THR A52.432 30.907 19.480.480.00.65N
Atom 396 CA THR A52.745.30.388 19.130 1.00 10.06C
Atom 397C THR A52.827 28.917 19.527 1.00.29C
Atom 398O THR A52.944 28.381 20.197 1.00.01O
Atom 399 CB THR A52.810.31.126.930 1.00 11.39C
Atom 401 CG2 THR A52.837.32.617.19.572.1.00 12.95C
Atom 402N THR A53.927.28.260.141.1.00.9.44N
Atom 403 CA THR A53.159.26.907 19.634 1.00 8.52C
Atom 404C THR A53.211.26.869.161.00.7.86C
Atom 405O THR A53.715.25.922.21.776 1.00 9.32O
Atom 406 CB THR A53.428 26.308.009 1.00 9.18C
Atom 407 OG1 THR A53.586 27.073.402.1.00.9.52O
Atom 408 CG2 THR A53.317.26.205.477 1.00.9.88C
Atom 409N ALA A54.812.27.887.795.00.9.82N
Atom 410 CA ALA A54.850.27.904 23.257 1.00.8.56C
Atom 411C ALA A54.448 28.036.837.00.8.45C
Atom 412O ALA A54.119 27.376 24.828 1.00.87O
Atom 413 CB ALA A54.741 29.036.775 1.00 10.02C
Atom 414N ALA A55.612.28.891.239 1.00 8.18N
Atom 415 CA ALA A55.235.003.23.717 1.00.53C
Atom 416C ALA A55.487 27.680 23.570.00.7.93C
Atom 417O ALA A55.728 27.275.24.462.00.9.32O
Atom 418 CB ALA A55.507 30.138.22.992.00.11.09C
Atom 419N GLY A56 1.696 26.982.22.452 1.00.96N
Atom 420 CA GLY A56.059.688 22.286 1.00 9.29C
Atom 421C GLY A56 1.530.24.686 23.318 1.00.08C
Atom 422O GLY A56 0.733 23.939.886.00.9.42O
Atom 423N LEU A57 2.837 24.659.23.581 1.00.9.10N
Atom 424 CA LEU A57.3.360 23.758 24.602.00.9.10C
Atom 425C LEU A57 2.769.24.068.972 1.00.8.84C
Atom 426O LEU A57.2.481 23.158.26.753 1.00.10.95O
Atom 427 CB LEU A57 4.885.23.841 24.623 1.00 9.77C
Atom 428 CG LEU A57.610.23.010 25.684 1.00.84C
Atom 429 CD1 LEU A57.276 21.531 25.537 1.00.12.43C
Atom 430 CD2 LEU A57.107.23.255.25.575 1.00.05C
Atom 431N GLN A58.557 25.350.26.259 1.00 8.54N
Atom 432 CA GLN A58.030 25.748 27.556 1.00 9.32C
Atom 433C GLN A58 0.616 25.237 27.780.00.9.41C
Atom 434O GLN A58.224 24.997.931 1.00 10.86O
Atom 435 CB GLN A58 2.049.266.266.663 1.00 10.43C
Atom 436 CG GLN A58.759.775 29.072 1.00 11.92C
Atom 437 CD GLN A58.907 27.494 30.022 1.00.61C
Atom 438 OE1 GLN A58.072 27.603.644 1.00 16.64O
Atom 439 NE2 GLN A58.589.131.31.252.1.00.19.37N
Atom 440N ARG A59-0.163.25.046.711 1.00.57N
Atoms 441 CA ARG A59-1.572 24.695 26.847.00 8.79C
Atom 442C ARG A59-1.923.23.281 26.409.00.9.71C
Atom 443O ARG A59-3.077.883.26.593.00.10.41O
Atoms 444 CB ARG A59-2.495 25.715 26.156.00.8.95C
Atom 445 CG ARG A59-2.385 25.744 24.654 1.00 10.27C
Atom 446 CD ARG A59-3.452 26.657 24.016 1.00 10.62C
Atom 447 NE ARG A59-3.141 26.816 22.600.00 10.32N
Atom 448 CZ ARG A59-3.847 26.298.21.599.00 10.89C
Atom 449 NH1 ARG A59-4.973.644 21.828 1.00 11.19N
Atom 450 NH2 ARG A59-3.421 26.456 20.358.1.00 10.77N
Atom 451N ILE A60-0.988.497 25.856 1.00.9.44N
Atom 452 CA ILE A60-1.393 21.213.25.275 1.00 9.33C
Atom 453C ILE A60-2.024 20.287 26.317.1.00.62C
Atom 454O ILE A60-3.042.639.049.00 9.97O
Atom 455 CB ILE A60-0.255 20.548 24.477 1.00.44C
Atom 456 CG1 ILE A60-0.737 19.221 23.867.00.9.97C
Atom 457 CG2 ILE A60.988.20.296 25.344.1.00 10.76C
Atom 458 CD1 ILE A60-1.840 19.348.799.00 11.01C
Atom 459N ALYS A61-1.433 20.201 27.510.44.90N
Atom 460 CA ALYS A61-2.001 19.326.529 0.44.03C
Atom 461C ALYS A61-3.396 19.783.28.937.44.02C
Atom 462O ALYS A61-4.313 18.963.064.44.96O
Atom 463 CB ALYS A61-1.077.266.29.740 0.44.66C
Atom 464 CG ALYS A61-1.587 18.384 30.852 0.44.06C
Atom 465 CD ALYS A61-0.653 18.412.047.44.32C
Atom 466 CE ALYS A61-1.393 18.047.324 0.44.99C
Atom 467 NZ ALYS A61-2.264 16.855 33.128.44.46N
Atom 468N BLYS A61-1.429 20.193 27.510.56.81N
Atom 469 CA BLYS A61-1.999 19.326 28.539 0.56.03C
Atom 470C BLYS A61-3.401 19.783.28.926 0.56.98C
Atom 471O BLYS A61-4.324.18.968.036.56.92O
Atom 472 CB BLYS A61-1.093.296.29.768 0.56.66C
Atom 473 CG BLYS A61 0.118 18.370 29.671 0.56.85C
Atom 474 CD BLYS A61.971 18.487 30.942.0.56.23C
Atom 475 CE BLYS A61.184.17.566.30.931 0.56.55C
Atom 476 NZ BLYS A61.808 16.130.001.56.18.26N
Atom 477N PHE A62-3.574 21.088.142.00.9.91N
Atom 478 CA PHE A62-4.887.615 29.507 1.00.9.45C
Atom 479C PHE A62-5.922 21.326.326 28.428 1.00 9.81C
Atom 480O PHE A62-7.055 20.934 28.729.00.85O
Atom 481 CB PHE A62-4.784.23.123.29.731 1.00.72C
Atom 482 CG PHE A62-6.093.773.773.090 1.00 10.80C
Atom 483 CD1 PHE A62-6.537 23.775 31.403.00 12.96C
Atom 484 CD2 PHE A62-6.888 24.364.128 1.00 14.10C
Atom 485 CE1 PHE A62-7.737 24.368 31.753 1.00 16.09C
Atom 486 CE2 PHE A62-8.100.24.959.480.1.00 16.73C
Atom 487 CZ PHE A62-8.524.953.30.791.00 16.87C
Atom 488N VAL A63-5.561 21.546 27.164.164 1.00 8.93N
Atom 489 CA VAL A63-6.502 21.302.26.071 1.00.8.06C
Atoms 490C VAL A63-6.906.19.833 26.041 1.00.94C
Atom 491O VAL A63-8.090 19.499 25.904 1.00 10.43O
Atom 492 CB VAL A63-5.899.771 24.731 1.00.72C
Atom 493 CG1 VAL A63-6.723 21.269 23.560.00 10.55C
Atom 494 CG2 VAL A63-5.802 23.288 24.698 1.00 10.01C
Atom 495N LEU A64-5.939.932 26.196.00.8.89N
Atom 496 CA LEU A64-6.264 17.507.26.196 1.00 10.17C
Atom 497C LEU A64-7.114.17.131 27.405.1.00.35C
Atom 498O LEU A64-8.107 16.404.27.275 1.00 10.95O
Atom 499 CB LEU A64-4.979.16.689.171.1.00.39C
Atom 500 CG LEU A64-4.228 16.777 24.842 1.00.68C
Atom 501 CD1 LEU A64-2.828 16.189 24.969.00 11.80C
Atom 502 CD2 LEU A64-5.010 16.083 23.714 1.00 10.27C
Atom 503N ASP A65-6.747.625 28.590.1.00.14N
Atom 504 CA ASP A65-7.493 17.316.810.1.00.07C
Atom 505C ASP A65-8.888 17.913 29.787.00.10.26C
Atom 506O ASP A65-9.752 17.470 30.556 1.00 13.17O
Atom 507 CB ASP A65-6.742 17.852 31.040 1.00 11.28C
Atom 508 CG ASP A65-5.459 17.100.339 1.00.11.59C
Atom 509 OD1 ASP A65-5.224 16.000 30.799.00 12.67O
Atom 510 OD2 ASP A65-4.671 17.612 32.153.00 13.55O
Atom 511N SER A66-9.123 18.925 28.955 1.00 10.73N
Atom 512 CA SER A66-10.435 19.545 28.868 1.00 11.21C
Atom 513C SER A66-11.407 18.757.011 1.00.68C
Atom 514O SER A66-12.601.19.080 28.018 1.00 15.16O
Atom 515 CB SER A66-10.328 20.965 28.308.00 12.52C
Atom 516 OG SER A66-9.645 21.800.219.1.00.88O
Atom 517N GLN A67-10.939.17.747.289 1.00.9.98N
Atom 518 CA GLN A67-11.770 17.065.303.00.11.63C
Atoms 519C GLN A67-12.642 16.009 26.966.00.12.79C
Atom 520O GLN A67-12.120.15.133.27.659.00.13.02O
Atom 521 CB GLN A67-10.884.16.381 25.272.00.54C
Atom 522 CG GLN A67-10.079.352.24.444 1.00.64C
Atom 523 CD GLN A67-10.925 18.500 23.943.00 12.22C
Atom 524 OE1 GLN A67-12.017 18.296 23.398 1.00 13.37O
Atom 525 NE2 GLN A67-10.437 19.715 24.121 1.00 12.68N
Atom 526N PRO A68-13.958 16.024 26.737 1.00 12.92N
Atoms 527 CA PRO A68-14.778.900.27.215.00 13.15C
Atom 528C PRO A68-14.457 13.613 26.495 1.00 12.46C
Atom 529O PRO A68-14.555 12.535 27.092.00 14.51O
Atom 530 CB PRO A68-16.217 15.353 26.927.00 16.97C
Atom 531 CG PRO A68-16.131 16.842 26.742 1.00 23.94C
Atom 532 CD PRO A68-14.769.097.26.152.00 13.67C
Atom 533N ASP A69-14.069.692 25.221 1.00 12.42N
Atom 534 CA ASP A69-13.718 12.523 24.432 1.00 12.04C
Atom 535C ASP A69-12.274 12.649.976.00 12.50C
Atom 536O ASP A69-11.894.657.370.1.00.69O
Atom 537 CB ASP A69-14.599.12.410 23.189 1.00 15.15C
Atom 538 CG ASP A69-16.065.302 23.518 1.00 17.65C
Atom 539 OD1 ASP A69-16.421 11.456 24.372 1.00 15.31O
Atom 540 OD2 ASP A69-16.853.064.909 1.00 19.72O
Atom 541N LYS A70-11.487 11.625 24.235 1.00 12.07N
Atom 542 CA LYS A70-10.081 11.657.874 1.00 12.05C
Atoms 543C LYS A70-9.934 11.742 22.357 1.00 11.82C
Atom 544O LYS A70-10.582 10.976.625 1.00 11.84O
Atom 545 CB LYS A70-9.418 10.380 24.367 1.00 14.87C
Atom 546 CG LYS A70-7.929.342 24.159 1.00 14.25C
Atom 547 CD LYS A70-7.356 9.055 24.727 1.00 18.79C
Atom 548 CE LYS A70-5.850.9.089 24.699.00 18.37C
Atom 549 NZ LYS A70-5.278 7.861 25.326 1.00 22.73N
Atom 550N PRO A71-9.094.637 21.847.00.9.83N
Atom 551 CA PRO A71-8.894.709 20.397 1.00.98C
Atom 552C PRO A71-8.369 11.402 19.838 1.00 10.31C
Atom 553O PRO A71-7.508 10.744 20.427 1.00 11.80O
Atom 554 CB PRO A71-7.865 13.831 20.244.00 12.09C
Atom 555 CG PRO A71-8.094.703 21.453.00.12.65C
Atom 556 CD PRO A71-8.394 13.719 22.559.00.12.02C
Atom 557N GLU A72-8.891.043.18.672 1.00 10.24N
Atom 558 CA GLU A72-8.434 9.879.940.1.00 10.61C
Atom 559C GLU A72-7.350 10.222.924 1.00 11.18C
Atom 560O GLU A72-6.694 9.321 16.396 1.00.33O
Atom 561 CB GLU A72-9.639.197.17.279.00 11.69C
Atom 562 CG GLU A72-10.689.764 18.310.00 13.22C
Atom 563 CD GLU A72-12.008 8.329 17.692.1.00 13.37C
Atom 564 OE1 GLU A72-12.998.091 17.799.00 16.14O
Atom 565 OE2 GLU A72-12.047.217 17.124.00 15.59O
Atom 566N LEU A73-7.127 11.508 16.687.00.10.91N
Atom 567 CA LEU A73-6.056.026 15.854 1.00.9.17C
Atoms 568C LEU A73-5.853.455 16.320.1.00.01C
Atom 569O LEU A73-6.829 14.148.615 1.00.9.64O
Atom 570 CB LEU A73-6.467 12.045 14.375 1.00 10.14C
Atom 571 CG LEU A73-5.540 12.777.402 1.00.9.36C
Atoms 572 CD1 LEU A73-4.197 12.079.294.1.00 10.03C
Atom 573 CD2 LEU A73-6.193 12.866 12.022 1.00 10.36C
Atom 574N ALA A74-4.597.882 16.391.1.00.52N
Atom 575 CA ALA A74-4.257 15.267 16.683 1.00.97C
Atom 576C ALA A74-3.519 15.829 15.481 1.00.41C
Atom 577O ALA A74-2.501 15.263 15.057.00.10.68O
Atom 578 CB ALA A74-3.362 15.378 17.917 1.00 10.09C
Atom 579N ILE A75-4.021 16.936 14.949.00 8.51N
Atom 580 CA ILE A75-3.365 17.661 13.869.00.8.79C
Atom 581C ILE A75-2.674 18.863 14.492.00.9.19C
Atom 582O ILE A75-3.330 19.704 15.111.00.10.02O
Atom 583 CB ILE A75-4.374 18.116.803.1.00.06C
Atom 584 CG1 ILE A75-5.253 16.956 12.311 1.00 10.57C
Atom 585 CG2 ILE A75-3.635 18.787.11.654 1.00.64C
Atom 586 CD1 ILE A75-6.384 17.389 11.375 1.00 10.50C
Atom 587N VAL A76-1.358 18.960 14.328 1.00.60N
Atom 588 CA VAL A76-0.562.994.14.989.00.8.68C
Atom 589C VAL A76-0.037.953.930.1.00.78C
Atom 590O VAL A76 0.686 20.541 13.012 1.00.44O
Atom 591 CB VAL A76 0.580.19.386 15.815 1.00.8.96C
Atom 592 CG1 VAL A76.449 20.482.482 16.411 1.00 10.63C
Atom 593 CG2 VAL A76 0.029.471 16.896.00 10.86C
Atom 594N GLU A77-0.376 22.236.236.080 1.00.60N
Atom 595 CA GLU A77-0.086.265.083 1.00.8.46C
Atom 596C GLU A77 0.438 24.492.13.827 1.00.65C
Atom 597O GLU A77-0.330 25.377 14.193 1.00 8.41O
Atom 598 CB GLU A77-1.365 23.573 12.312.00 10.15C
Atom 599 CG GLU A77-1.258 24.673.11.296 1.00 9.50C
Atom 601 OE1 GLU A77-0.892 26.992 11.539 1.00.9.35O
Atom 602 OE2 GLU A77-2.689.181.12.529 1.00 10.11O
Atom 603N LEU A78.748 24.529 14.072 1.00 8.49N
Atom 604 CA LEU A78.336 25.616 14.838 1.00 9.17C
Atom 605C LEU A78.734 25.889.314 1.00 9.27C
Atom 606O LEU A78.410 25.008 13.769.00 9.55O
Atom 607 CB LEU A78.426.25.295 16.330.1.00.9.32C
Atom 608 CG LEU A78.098.252.076.00.8.27C
Atom 609 CD1 LEU A78.344 24.738 18.487 1.00.70C
Atom 610 CD2 LEU A78.472 26.621.621.142.00.10.01C
Atom 611N GLY A79.179 27.119 14.550 1.00.52N
Atom 612 CA GLY A79.5.507 27.578 14.177 1.00 10.88C
Atom 613C GLY A79.5.491 28.812 13.310.00.10.33C
Atom 614O GLY A79.483 29.557 13.279 1.00.10.98O
Atom 615N GLY A80.383.29.066.615 1.00 9.68N
Atom 616 CA GLY A80.288 30.275 11.818 1.00 11.89C
Atom 617C GLY A80.507.31.537 12.631 1.00 12.65C
Atom 618O GLY A80.153.32.479.166 1.00 13.37O
Atom 619N ASN A81 3.990.573 13.858 1.00.09N
Atom 620 CA ASN A81.176 32.769.668 1.00 11.70C
Atom 621C ASN A81 5.601 32.895.186 1.00 12.66C
Atom 622O ASN A81 6.086.022 15.351 1.00 15.73O
Atom 623 CB ASN A81.128.32.850 15.774 1.00 12.10C
Atom 624 CG ASN A81.782.251 15.233 1.00 14.94C
Atom 625 OD1 ASN A81.632 34.310.621.621.00 22.82O
Atom 626 ND2 ASN A81 0.805 32.396 15.414 1.00 15.71N
Atom 627N ASP A82.292 31.776 15.425.00 9.41N
Atom 628 CA ASP A82.720.31.855 15.733.733 1.00 10.09C
Atom 629C ASP A82.472 32.516.589.00.12.69C
Atom 630O ASP A82.312.394.14.808 1.00 13.35O
Atom 631 CB ASP A82.313 30.468 16.021 1.00 10.09C
Atom 632 CG ASP A82.651 29.761 17.177 1.00 9.99C
Atom 633 OD1 ASP A82.403 29.656.656.17.168 1.00 10.99O
Atom 634 OD2 ASP A82.375 29.278 18.072 1.00 10.29O
Atom 635N LEU A83.181.32.100.353 1.00 13.31N
Atom 636 CA LEU A83 8.731 32.762 12.169 1.00 17.40C
Atom 637C LEU A83.8.465.34.259 12.199.1.00.23.03C
Atom 638O LEU A83.9.370.35.075.11.981.00.23.93O
Atom 639 CB LEU A83.8.023 32.219.10.935 1.00 20.59C
Atom 640 CG LEU A83.8.399 30.879.354.1.00 22.29C
Atom 641 CD1 LEU A83.7.444.30.537.217 1.00 25.28C
Atom 642 CD2 LEU A83.824.30.935.935.865 1.00.25.44C
Atom 643N LEU A84.206.34.637 12.417 1.00 20.62N
Atom 644 CA LEU A84 6.812.36.037.316.00 22.02C
Atom 645C LEU A84.470.36.893.387 1.00 24.11C
Atom 646O LEU A84 7.600.38.108.205.00.28.71O
Atom 647 CB LEU A84.287 36.154.12.387 1.00.79C
Atom 648 CG LEU A84.475.35.933 11.097.00.32.24C
Atom 649 CD1 LEU A84.042.34.849.10.175.00 30.33C
Atom 650 CD2 LEU A84.028 35.618 11.433.1.00.31.15C
Atom 651N ARG A85.881 36.288 14.495 1.00 20.85N
Atom 652 CA ARG A85.661 36.966.517 1.00 17.70C
Atom 653C ARG A85.166 36.811 15.310.00 20.87C
Atom 654O ARG A85.937.37.330 16.120.00 24.06O
Atom 655 CB ARG A85.261.36.467 16.910.00.21.09C
Atom 656 CG ARG A85.844 36.847.361 1.00.56C
Atom 657 CD ARG A85.525.36.174.692 1.00.13C
Atom 658 NE ARG A85.184.36.480 19.181.00.28.98N
Atom 659 CZ ARG A85.899.37.503 19.979.00.84C
Atom 660 NH1 ARG A85.651 37.706 20.379.00 37.12N
Atom 661 NH2 ARG A85.864 38.321 20.378 1.00 32.61N
Atom 662N GLY A86 10.598.36.123 14.250 1.00 18.68N
Atom 663 CA GLY A86.018 35.888 14.010 1.00 19.31C
Atom 664C GLY A86.713.35.021 15.037.00.12.51C
Atom 665O GLY A86.939.35.106 15.190.00.14.27O
Atom 666N LEU A87.11.966.34.179 15.737 1.00 10.70N
Atom 667 CA LEU A87.12.491 33.427 16.864 1.00 10.68C
Atom 668C LEU A87 13.321 32.236 16.395 1.00.32C
Atom 669O LEU A87 13.192 31.750 15.263 1.00 10.25O
Atom 670 CB LEU A87.11.351 32.914 17.739.00 11.29C
Atom 671 CG LEU A87.500.34.005 18.385 1.00.12.95C
Atom 672 CD1 LEU A87.9.387 33.358.19.212.00.15.16C
Atom 673 CD2 LEU A87.345.34.942.19.238.1.00 16.17C
Atom 674N SER A88.140.737 17.307 1.00 10.07N
Atom 675 CA SER A88.040 30.625.17.053.00.52C
Atom 676C SER A88.288 29.435.16.458 1.00 8.55C
Atom 677O SER A88.351 28.919 17.091 1.00.97O
Atom 678 CB SER A88.653 30.207.18.384.00.48C
Atom 679 OG SER A88.247 28.926 18.279.1.00.14O
Atom 680N PRO A89.704.28.926.15.298 1.00 9.51N
Atom 681 CA PRO A89.103 27.669.14.818.00.9.93C
Atom 682C PRO A89.400.26.493 15.726 1.00.9.72C
Atom 683O PRO A89.560.25.591 15.863.00.9.87O
Atom 684 CB PRO A89.731 27.478 13.433.1.00.11.02C
Atom 685 CG PRO A89.154 28.855 13.019 1.00 11.64C
Atom 686 CD PRO A89.594 29.533.14.287 1.00 10.96C
Atom 687N ALA A90.581 26.472 16.354.1.00 9.54N
Atom 688 CA ALA A90.915 25.372 17.250.00.10.50C
Atom 689C ALA A90.961 25.329.18.435.00.9.55C
Atomic 690O ALA A90.502.24.255.18.841 1.00 11.63O
Atom 691 CB ALA A90.365 25.503.503.716.1.00 13.08C
Atom 692N GLU A91 14.641 26.491 18.991.00 9.04N
Atom 693 CA GLU A91 13.702 26.523 20.103 1.00.8.72C
Atom 694C GLU A91.297 26.141.19.660 1.00.9.08C
Atom 695O GLU A91.568 25.499 20.419.00.94O
Atom 696 CB GLU A91.735.27.892 20.761 1.00 11.28C
Atom 697 CG GLU A91 15.094.28.141 21.390 1.00.11.06C
Atom 698 CD GLU A91 15.171 29.412.22.147 1.00 12.39C
Atom 699 OE1 GLU A91 14.131.30.038.22.422 1.00 16.61O
Atom 700 OE2 GLU A91 16.301.29.793.511 1.00 14.10O
Atom 701N ALA A92.896.26.530.441.1.00 9.49N
Atom 702 CA ALA A92.601.26.091 17.916 1.00.9.30C
Atom 703C ALA A92.548.24.570.17.819 1.00.9.17C
Atom 704O ALA A92.542.23.943.179 1.00 9.90O
Atom 705 CB ALA A92.341 26.734 16.550 1.00 10.34C
Atom 706N ARG A93.638 23.961.17.347.1.00 8.53N
Atom 707 CA ARG A93.717 22.505.277.1.00 9.91C
Atom 708C ARG A93.590.21.874 18.657.00.9.28C
Atom 709O ARG A93.899.20.862 18.825 1.00 9.51O
Atom 710 CB ARG A93.036.094.623 1.00.8.92C
Atom 711 CG ARG A93.176 20.599.383 1.00 11.36C
Atom 712 CD ARG A93.533 20.261 15.758 1.00 12.46C
Atom 713 NE ARG A93.606 20.760 16.602.00 14.00N
Atom 714 CZ ARG A93.611 21.527 16.186 1.00 15.26C
Atom 715 NH1 ARG A93.512.21.960.17.061 1.00 15.90N
Atom 716 NH2 ARG A93.726 21.855 14.906.00 14.85N
Atom 717N GLN A94.281 22.443 19.653 1.00 8.43N
Atom 718 CA GLN A94.207 21.919 21.015.1.00 9.28C
Atom 719C GLN A94.796.22.032 21.578 1.00.7.99C
Atom 720O GLN A94.297 21.101.22.217 1.00 9.30O
Atom 721 CB GLN A94 13.174 22.690 21.909 1.00 12.13C
Atom 722 CG GLN A94.637 22.5821.522 1.00.28C
Atom 723 CD GLN A94.15.456 23.788.992.1.00.30.86C
Atom 724 OE1 GLN A94.048.525 22.896.00.29.78O
Atom 725 NE2 GLN A94.617 23.991.21.373 1.00 29.07N
Atom 726N ASN A95.142.23.174.21.355 1.00 8.50N
Atom 727 CA ASN A95.784.23.358 21.859.00.9.02C
Atom 728C ASN A95.821 22.386 21.189 1.00 8.55C
Atom 729O ASN A95.008 21.734 21.861 1.00 9.61O
Atom 730 CB ASN A95.339 24.802 21.630.1.00 9.16C
Atom 731 CG ASN A95.118 25.799.452 1.00 9.64C
Atom 732 OD1 ASN A95.722 25.448 23.475 1.00 11.85O
Atom 733 ND2 ASN A95.099.27.053.024 1.00 10.74N
Atom 734N LEU A96.919 22.256.19.862 1.00.8.83N
Atom 735 CA LEU A96.082 21.289 19.161 1.00.8.50C
Atom 736C LEU A96.354.19.870 19.639.00.8.05C
Atom 737O LEU A96.427 19.058.739.00.9.48O
Atom 738 CB LEU A96.305.21.393 17.654 1.00.53C
Atom 739 CG LEU A96.541 22.531 16.983.00.10.62C
Atom 740 CD1 LEU A96.161.22.909.15.649.00 11.73C
Atom 741 CD2 LEU A96.5.069.185.16.804.1.00 12.67C
Atom 742N SER A97.621 19.555 19.946 1.00 9.90N
Atom 743 CA SER A97.945 18.231 20.231 20.470 1.00 10.34C
Atom 744C SER A97.8.171 17.956 21.753 1.00 9.28C
Atom 745O SER A97.675 16.845 21.960 1.00 10.32O
Atom 746 CB SER A97.448 18.122 20.741 1.00 10.69C
Atom 747 OG SER A97.196 18.155 19.547 1.00.13.21O
Atom 748N GLY A98.067.958 22.629 1.00.8.86N
Atom 749 CA GLY A98.317 18.775 23.861 1.00.9.80C
Atom 750C GLY A98.841 18.530.612.1.00.9.17C
Atom 751O GLY A98.5.212.17.732 24.311 1.00 10.04O
Atom 752N ILE A99.265 19.210.614 1.00 9.02N
Atom 753 CA ILE A99.866 18.971.22.258 1.00.9.84C
Atom 754C ILE A99.681 17.547 21.759.00.8.20C
Atom 755O ILE A99.767.16.830.188.1.00 10.00O
Atom 756 CB ILE A99.391.19.984.206.1.00.78C
Atom 757 CG1 ILE A99.3.426 21.397 21.778.00 10.08C
Atom 758 CG2 ILE A99.988.628.718.1.00.9.36C
Atom 759 CD1 ILE A99.332 22.479.727 1.00 10.20C
Atom 760N LEU A100.551 17.116.20.847.00.8.42N
Atom 761 CA LEU A100.395 15.787.20.271.1.00.03C
Atom 762C LEU A100.4.661 14.709 21.306.00 10.17C
Atom 763O LEU A100.027 13.648 21.272.00.11.61O
Atom 764 CB LEU A100.322.15.614.19.071 1.00.10.50C
Atom 765 CG LEU A100.119 16.634 17.944 1.00 11.10C
Atom 766 CD1 LEU A100.849.16.191.16.690 1.00 15.31C
Atom 767 CD2 LEU A100.642 16.904 17.640.1.00 14.47C
Atom 768N GLU A101 5.580 14.970 22.239 1.00 11.19N
Atom 769 CA GLU A101.5.864 14.004 23.290 1.00.30C
Atom 770C GLU A101.646 13.787.24.170.1.00 12.00C
Atom 771O GLU A101.373 12.657.591.1.00.16O
Atom 772 CB GLU A101.060 14.470 24.119.1.00 12.87C
Atom 773 CG GLU A101.379.092.491.00 18.99C
Atom 774 CD GLU A101.594 14.656.24.200.00.30.51C
Atom 775 OE1 GLU A101.443 15.275 25.279.1.00.65O
Atom 776 OE2 GLU A101.708 14.470.661 1.00 27.86O
Atom 777N GLU A102.909 14.853.853.474.00.11.20N
Atom 778 CA GLU A102 2.696.706 25.269 1.00 11.26C
Atom 779C GLU A102.638 13.902.24.520.00.11.09C
Atom 780O GLU A102 0.986.028 25.103 1.00.12.09O
Atom 781 CB GLU A102 2.169 16.085.643 1.00.11.82C
Atom 782 CG GLU A102 0.876.058.446 1.00.13.61C
Atom 783 CD GLU A102.012 15.407 27.817 1.00.38C
Atom 784 OE1 GLU A102 2.147.15.276 28.319 1.00.05O
Atom 785 OE2 GLU A102-0.027 15.024 28.399.1.00 16.09O
Atom 786N LEU A103.437 14.194 23.231.1.00 10.13N
Atom 787 CA LEU A103 0.494 13.408.22.439 1.00.9.90C
Atom 788C LEU A103.915 11.945 22.379.00 11.38C
Atom 789O LEU A103 0.078.045 22.519 1.00 11.96O
Atom 790 CB LEU A103 0.372 14.001 21.034.00 10.61C
Atom 791 CG LEU A103-0.292 15.381 21.010 1.00.94C
Atom 792 CD1 LEU A103-0.007 16.112.19.699.00 10.34C
Atoms 793 CD2 LEU A103-1.785.274.21.245.00 10.39C
Atom 794N GLN A104 2.211.11.689.181.1.00 11.66N
Atom 795 CA GLN A104.706 10.317.22.115.00 15.01C
Atom 796C GLN A104 2.522 9.601 23.445 1.00 16.30C
Atom 797O GLN A104 2.176 8.410 23.477 1.00.16.61O
Atom 798 CB GLN A104.182.10.341 21.734 1.00 19.40C
Atom 799 CG GLN A104 4.709 9.060 21.120.1.00 24.50C
Atom 801 OE1 GLN A104.008 9.672 21.293 1.00.60O
Atomic 802 NE2 GLN A104 6.301 8.905 19.304 1.00 29.23N
Atom 803N AARG A105.743 10.319 24.554 0.46.14N
Atom 804 CA AARG A105.556 9.767.894.46.15.11C
Atom 805C AARG A105.131.9.273 26.103.46.14.62C
Atom 806O AARG A105.903 8.331 26.874 0.46.95O
Atom 807 CB AARG A105.877 10.858 26.922 0.46 16.60C
Atom 808 CG AARG A105.452 10.382 28.245 0.46.19.73C
Atom 809 CD AARG A105 4.536 11.335 28.762 0.46.82C
Atom 810 NE AARG A105.195 12.752 28.614 0.46 15.19N
Atom 811 CZ AARG A105.5.070 13.695 28.266.46 15.08C
Atom 812 NH1AARG A105.335 13.372 28.033 0.46.44N
Atom 813 NH2AARG A105 4.686 14.959.156 0.46.44N
Atom 814N BARG A105.778.293 24.556 0.54.12N
Atom 815 CA BARG A105.551 9.681 25.858 0.54.02C
Atom 816C BARG A105.132.9.146.956 0.54.75C
Atom 817O BARG A105 0.907 8.041 26.467 0.54.24O
Atom 818 CB BARG A105.812 10.704 26.964.54.06C
Atom 819 CG BARG A105.790 10.140 28.369 0.54.91C
Atom 820 CD BARG A105.034.248.29.382 0.54.61C
Atom 821 NE BARG A105.900.12.164 29.463 0.54.10N
Atom 822 CZ BARG A105.791.11.919 30.151.54.36C
Atom 823 NH1BARG A105.667 10.786.830.54.20.13N
Atom 824 NH2BARG A105-0.194 12.805 30.165 0.54.39N
Atom 825N ARG A106 0.162.907 25.447 1.00 12.63N
Atom 826 CA ARG A106-1.239 9.525.513 1.00 12.23C
Atom 827C ARG A106-1.655 8.626 24.365 1.00 12.43C
Atom 828O ARG A106-2.843 8.320.24.241 1.00.12.72O
Atom 829 CB ARG A106-2.132.10.767.544 1.00 12.61C
Atom 830 CG ARG A106-1.768 11.727 26.664 1.00.30C
Atom 831 CD ARG A106-2.869.12.733 26.857.00 17.57C
Atom 832 NE ARG A106-2.466 13.794.767.00 14.22N
Atom 833 CZ ARG A106-3.301.14.457 28.554 1.00 12.21C
Atom 834 NH1 ARG A106-4.591 14.167 28.560.00 14.39N
Atom 835 NH2 ARG A106-2.832 15.401.401.347.1.00.13.95N
Atom 836N LYS A107-0.709 8.218.522 1.00 12.23N
Atom 837 CA LYS A107-0.981.7.333.22.392 1.00 13.11C
Atom 838C LYS A107-2.003 7.926 21.421 1.00 12.26C
Atom 839O LYS A107-2.853.218.877.00.14.87O
Atom 840 CB LYS A107-1.363 5.926 22.855 1.00 16.42C
Atom 841 CG LYS A107-0.285 5.304 23.731.00 1.19.72C
Atom 842 CD LYS A107-0.460.3.810 23.905 1.00 28.91C
Atom 843 CE LYS A107 0.818 3.178 24.435.00.97C
Atom 844 NZ LYS A107.060 1.837.831.1.00 47.46N
Atom 845N ILE A108-1.931 9.235 21.205 1.00 11.31N
Atom 846 CA ILE A108-2.783.930 20.243.00 10.76C
Atom 847C ILE A108-2.013 10.060 18.934 1.00 10.62C
Atom 848O ILE A108-0.937.684 18.921 1.00 11.18O
Atom 849 CB ILE A108-3.224 11.302 20.764 1.00 9.91C
Atom 850 CG1 ILE A108-4.076.123 22.021 1.00 10.88C
Atom 851 CG2 ILE A108-4.002 12.051 19.673.00 10.73C
Atom 852 CD1 ILE A108-4.349 12.407 22.769.00 11.68C
Atom 853N PRO A109-2.501 9.481 17.837.00.10.45N
Atom 854 CA PRO A109-1.825 9.643 16.548.00.11.39C
Atom 855C PRO A109-1.692 11.106.158.00.9.44C
Atom 856O PRO A109-2.553 11.934 16.460.1.00 10.00O
Atom 857 CB PRO A109-2.746 8.895.577.00 12.79C
Atom 858 CG PRO A109-3.482.7.896.429 1.00.09C
Atom 859 CD PRO A109-3.690 8.612.739.00.11.42C
Atom 860N ILE A110-0.625 11.403 15.418 1.00 10.57N
Atom 861 CA ILE A110-0.242 12.773.15.091 1.00 11.18C
Atom 862C ILE A110-0.175 12.948.577.00.9.33C
Atom 863O ILE A110.459 12.147 12.872 1.00 10.76O
Atomic 864 CB ILE A110.136 13.110.15.679.00.9.51C
Atom 865 CG1 ILE A110.140.946 17.201.00.12.23C
Atom 866 CG2 ILE A110.566 14.523 15.290 1.00 11.51C
Atom 867 CD1 ILE A110.2.534 12.869.778.00 12.28C
Atoms 868N LEU A111-0.770.14.033 13.092.00.9.31N
Atom 869 CA LEU A111-0.502.14.569.763.00.9.40C
Atom 870C LEU A111 0.100.15.959.946 1.00.8.05C
Atom 871O LEU A111-0.523 16.838 12.552 1.00.93O
Atom 872 CB LEU A111-1.785.14.654.654.934 1.00.88C
Atom 873 CG LEU A111-1.649.310.9.561 1.00 10.44C
Atom 874 CD1 LEU A111-0.680 14.544 8.681 1.00 14.31C
Atom 875 CD2 LEU A111-3.012 15.403.8.893.00.12.06C
Atom 876N LEU A112.300.16.163.421.1.00.8.59N
Atom 877 CA LEU A112.011 17.426.11.549 1.00.72C
Atom 878C LEU A112.847.18.230.265.00.8.78C
Atom 879O LEU A112.106 17.718 9.171 1.00 10.93O
Atom 880 CB LEU A112.491 17.132.782.1.00.12C
Atom 881 CG LEU A112.384 18.285 12.234.00.11.22C
Atom 882 CD1 LEU A112.936 18.867.564.00.11.69C
Atom 883 CD2 LEU A112.832 17.827 12.313 1.00.99C
Atom 884N MET A113.420 19.481 10.392 1.00.9.38N
Atom 885 CA MET A113.292 20.393 9.257 1.00 9.26C
Atom 886C MET A113.590 21.180.9.097.00.9.15C
Atom 887O MET A113.946 21.996.961.00.9.68O
Atom 888 CB MET A113 0.116.21.336.9.470.00.9.89C
Atom 889 CG MET A113-1.241 20.646 9.499 1.00.90C
Atom 890 SD MET A113-1.488 19.596 8.063 1.00 12.33S
Atom 891 CE MET A113-3.270 19.529 7.977.00.12.46C
Atom 892N GLY A114.311 20.919 8.010 1.00.15N
Atom 893 CA GLY A114.599.561 7.795.00.8.98C
Atom 894C GLY A114.444 23.031 7.449 1.00.24C
Atom 895O GLY A114.619 23.406.406.606 1.00.10.54O
Atom 896N MET A115.239 23.874 8.105.00.9.94N
Atom 897 CA MET A115.290 25.302.302.823 1.00 10.11C
Atom 898C MET A115.572 25.623.7.064.00.10.22C
Atom 899O MET A115.578 24.913 7.181 1.00 10.24O
Atom 900 CB MET A115.216.26.125 9.112 1.00 10.22C
Atom 901 CG MET A115.034.749.012 1.00 10.41C
Atom 902 SD MET A115.414 25.883.231.1.00 13.47S
Atom 903 CE MET A115.382 27.618 8.831 1.00 18.39C
Atom 904N ARG A116.530.26.689.6.269 1.00 10.34N
Atom 905 CA ARG A116.666 27.082 5.446 1.00 11.43C
Atom 906C ARG A116.984.28.553.553.652.1.00 12.19C
Atom 907O ARG A116.080 29.388.388.778.00.42O
Atom 908 CB ARG A116.390.26.828 3.966.00 12.51C
Atom 909 CG ARG A116.267 25.358 3.636 1.00 12.76C
Atom 910 CD ARG A116.621.24.672 3.669.00.12.47C
Atom 911 NE ARG A116.523 23.239 3.395 1.00 12.37N
Atom 912 CZ ARG A116.329 22.712.190.00 12.68C
Atom 913 NH1 ARG A116.225.23.497 1.123.00 15.78N
Atom 914 NH2 ARG A116.253 21.395 2.062 1.00 14.05N
Atom 915N ALA A117 9.274 28.860 5.691 1.00 12.61N
Atom 916 CA ALA A117 9.675 30.235 5.954 1.00 13.36C
Atom 917C ALA A117 9.718 31.025 4.650 1.00 16.59C
Atom 918O ALA A117 10.152.30.499 3.624 1.00 14.36O
Atom 919 CB ALA A117.11.063 30.263 6.587.00 14.84C
Atom 920N PRO A118.9.281 32.282 4.672 1.00 18.20N
Atom 921 CA PRO A118.9.443 33.145 3.506 1.00 18.07C
Atom 922C PRO A118.10.880 33.626 3.419 1.00 19.39C
Atom 923O PRO A118.636.33.529 4.395 1.00 18.97O
Atom 924 CB PRO A118 8.485 34.307 3.809 1.00 22.56C
Atom 925 CG PRO A118 8.522 34.415 5.282 1.00 25.38C
Atom 926 CD PRO A118 8.669.32.997.5.806 1.00 20.44C
Atom 927N PRO A119.302 34.146 2.267 1.00 16.33N
Atom 928 CA PRO A119 12.726 34.479.086.00 16.75C
Atom 929C PRO A119.223 35.673.889.00.20.20C
Atom 930O PRO A119 14.442 35.876.940 1.00 16.16O
Atom 931 CB PRO A119 12.834 34.749 0.580.00 19.41C
Atom 932 CG PRO A119.441 35.130.0.171 1.00 23.38C
Atom 933 CD PRO A119.541 34.285.014 1.00 22.66C
Atom 934N AASN A120.343 36.492 3.473 0.45 18.06N
Atom 935 CA AASN A120.820.711 4.121 0.45.98C
Atom 936C AASN A120.655 37.440.363 0.45.95C
Atom 937O AASN A120.328 38.355 5.850.45.64O
Atom 938 CB AASN A120.675 38.689.418 0.45.66C
Atom 939 CG AASN A120.627 38.111.5.347 0.45.16C
Atom 940 OD1AASN A120.925 37.712 6.473 0.45.19O
Atom 941 ND2AASN A120.382 38.084.886.45 22.32N
Atom 942N BASN A120.336.36.406 3.573 0.55.77N
Atom 943 CA BASN A120.717 37.671 4.205 0.55.66C
Atom 944C BASN A120.824 37.496 5.241.55.54C
Atom 945O BASN A120.739.323 5.320.55.53O
Atom 946 CB BASN A120.497 38.340.837.55.20.26C
Atom 947 CG BASN A120.780.39.763.282 0.55.12C
Atom 948 OD1BASN A120.268 40.586 4.504 0.55 22.84O
Atom 949 ND2BASN A120.475.40.060 6.540.0.55.57N
Atomic 950N ALEU A121.13.640.36.217 5.881 0.45.18.00N
Atomic 951 CA ALEU A121.499 35.867.998.45.18.88C
Atom 952C ALEU A121.15.847.35.310.6.559.45.41C
Atom 953O ALEU A121.652 34.951 7.422 0.45.19O
Atom 954 CB ALEU A121.776 34.915.7.962 0.45.21C
Atom 955 CG ALEU A121.811 35.680.8.880 0.45.26C
Atom 956 CD1ALEU A121.303.34.834 10.024 0.45.21C
Atom 957 CD2ALEU A121.475.36.939.417.45.40C
Atomic 958N BLEN BLEU A121.13.757.442.6.056.55.77N
Atom 959 CA BLEU A121.788.36.258 7.069.55.53C
Atomic 960C BLEU A121 16.090 35.703.509 0.55.53C
Atom 961O BLEU A121.17.083 35.664 7.243 0.55 16.85O
Atom 962 CB BLEU A121.302 35.357 8.208 0.55.57C
Atom 963 CG BLEU A121.952 35.678 8.840.0.55.55C
Atom 964 CD1BLEU A121.920 34.682 8.356 0.55.71C
Atom 965 CD2BLEU A121.069.640.10.346 0.55.34C
Atom 966N GLY A122.113.35.273 5.255.00 13.79N
Atom 967 CA GLY A122 17.355 34.799.4.676 1.00.03C
Atom 968C GLY A122 17.399 33.284 4.561 1.00 11.39C
Atom 969O GLY A122 16.690 32.553 5.255.00 11.72O
Atom 970N ALA A123 18.280.32.810 3.673.00.10.65N
Atom 971 CA ALA A123 18.359 31.382 3.374 1.00 10.25C
Atom 972C ALA A123.820.30.564 4.573 1.00.10.42C
Atom 973O ALA A123.18.357 29.436.4.773.00.10.52O
Atom 974 CB ALA A123.294 31.142 2.189 1.00 11.93C
Atom 975N LYS A124.19.760.086.360.00.9.27N
Atom 976 CA LYS A124.242 30.335.335.518.00.9.73C
Atom 977C LYS A124.107.30.043.494 1.00.97C
Atom 978O LYS A124.900.28.895.896.00.10.78O
Atom 979 CB LYS A124.374 31.096.200.00 10.90C
Atom 980 CG LYS A124.941 30.365 8.395 1.00 12.19C
Atom 981 CD LYS A124.173 31.084.935 1.00 14.79C
Atom 982 CE LYS A124.728 30.420 10.194 1.00 17.28C
Atom 983 NZ LYS A124.012 31.072 10.614 1.00 21.92N
Atom 984N TYR A125.18.351 31.074.871 1.00.9.44N
Atom 985 CA TYR A125 17.202 30.878.748 1.00.65C
Atom 986C TYR A125 16.156.29.989.082 1.00.8.12C
Atom 987O TYR A125.15.623 29.063 8.702.1.00 10.17O
Atom 988 CB TYR A125 16.600 32.235.9.120.00 10.63C
Atom 989 CG TYR A125.446 32.165 10.090 1.00 9.90C
Atom 990 CD1 TYR A125.177 31.738 9.695 1.00.12.25C
Atom 991 CD2 TYR A125.628 32.527 11.406 1.00 10.38C
Atom 992 CE1 TYR A125.13.138.665 10.607.00 12.54C
Atom 993 CE2 TYR A125.595 32.467 12.319 1.00 10.62C
Atom 994 CZ TYR A125.351 32.031 11.911 1.00.9.95C
Atom 995 OH TYR A125.12.284 31.972 12.782.1.00.99O
Atom 996N GLN A126.836 30.270.6.820 1.00 9.41N
Atom 997 CA GLN A126 14.759.545 6.151.00 10.22C
Atom 998C GLN A126 15.052 28.049.065.00 10.11C
Atom 999O GLN A126.178.27.217 6.342 1.00 9.95O
Atom 1001 CG GLN A126 13.733 29.258 3.826 1.00 11.57C
Atom 1002 CD GLN A126.662.28.413 2.988.00 13.05C
Atom 1003 OE1 GLN A126 15.691 28.895.506 1.00.13.10O
Atom 1004 NE2 GLN A126 14.314.27.145 2.812 1.00 13.07N
Atom 1005N ARG A127.274 27.682 5.682 1.00.51N
Atom 1006 CA ARG A127.606 26.265 5.619 1.00 10.45C
Atom 1007C ARG A127.493 25.623 6.990 1.00 9.80C
Atom 1008O ARG A127.999 24.497 7.121.1.00 10.64O
Atom 1009 CB ARG A127.028 26.076.107.1.00 12.33C
Atom 1010 CG ARG A127.183 26.265 3.601 1.00 14.70C
Atom 1011 CD ARG A127.618 25.981.153.153.00 18.99C
Atom 1012 NE ARG A127.572 26.904 3.759.00 16.32N
Atom 1013 CZ ARG A127.348 27.737 3.077.00 15.10C
Atom 1014 NH1 ARG A127.281 27.772 1.752 1.00 20.51N
Atom 1015 NH2 ARG A127.181 28.542.3.722.1.00 17.68N
Atom 1016N GLU A128.984.26.310.8.024 1.00.52N
Atom 1017 CA GLU A128.920 25.755.9.370.1.00.50C
Atom 1018C GLU A128.476 25.569.818.1.00.85C
Atom 1019O GLU A128.110.24.512 10.347.1.00 10.55O
Atom 1020 CB GLU A128 17.685 26.645 10.354 1.00 10.54C
Atom 1021 CG GLU A128.17.869.25.965 11.718.1.00 11.45C
Atom 1022 CD GLU A128.18.446 26.845 12.812 1.00 12.19C
Atom 1023 OE1 GLU A128 18.853.993.9912.557 1.00 12.56O
Atom 1024 OE2 GLU A128 18.470 26.369 13.967.00 13.07O
Atom 1025N APHE A129.648 26.599.623 0.65.02N
Atom 1026 CA APHE A129.13.252 26.510.027 0.65.9.27C
Atom 1027C APHE A129 12.534 25.394 9.281 0.65.98C
Atom 1028O APHE A129.844 24.565 9.886.65.9.91O
Atom 1029 CB APHE A129 12.545 27.841 9.776 0.65.21C
Atom 1030 CG APHE A129.096.27.797.128.0.65.35C
Atom 1031 CD1APHE A129 10.692 27.983.444 0.65.12.70C
Atom 1032 CD2APHE A129.134.27.507 9.164.0.65.20C
Atom 1033 CE1APHE A129.9.351 27.912.11.789.65.13.77C
Atom 1034 CE2APHE A129 8.792 27.428 9.503 0.65.37C
Atom 1035 CZ APHE A129.400.27.629 10.819 0.65.41C
Atom 1036N BPHE A129.631 26.580.606 0.35.21N
Atom 1037 CA BPHE A129.13.255.26.462.10.078.35.39C
Atom 1038C BPHE A129.12.469.25.427.9.277 0.35.18C
Atom 1039O BPHE A129 11.692 24.658 9.852 0.35.82O
Atom 1040 CB BPHE A129 12.552 27.823 10.110.35.75C
Atom 1041 CG BPHE A129.517 27.931 11.203 0.35.37C
Atom 1042 CD1BPHE A129.10.356.27.174.149 0.35.12.15C
Atom 1043 CD2BPHE A129.716 28.761 12.299 0.35.61C
Atom 1044 CE1BPHE A129.9.413 27.250.155.35.12.80C
Atom 1045 CE2BPHE A129.772 28.841 13.308.35.00C
Atom 1046 CZ BPHE A129.621 28.086.234.35.38C
Atom 1047N ASP A130.656 25.385 7.953.00 9.67N
Atom 1048 CA ASP A130.893.433 7.433.152.00.9.31C
Atom 1049C ASP A130.211.003.7.558.1.00 9.64C
Atom 1050O ASP A130.333 22.130.7.533 1.00 10.63O
Atom 1051 CB ASP A130.203 24.622 5.670.00 1.00 10.66C
Atom 1052 CG ASP A130.599.872.872 5.094.00.10.23C
Atom 1053 OD1 ASP A130.945 26.650.5.813 1.00 11.45O
Atom 1054 OD2 ASP A130.804.26.069.882 1.00 11.02O
Atom 1055N GLY A131.461 22.741.944 1.00.42N
Atom 1056 CA GLY A131.869.377 8.249 1.00.90C
Atom 1057C GLY A131.344.20.830.9.564 1.00.8.99C
Atom 1058O GLY A131.461 19.623 9.805 1.00.30O
Atom 1059N ILE A132.785.674 10.431.00.9.01N
Atom 1060 CA ILE A132.351 21.135.721.1.00 8.91C
Atom 1061C ILE A132.181 20.177 11.554 1.00 8.61C
Atom 1062O ILE A132.043.19.226.226.329 1.00.9.50O
Atom 1063 CB ILE A132.076.214 12.791.00 10.64C
Atom 1064 CG1 ILE A132.761 22.964.12.545 1.00 9.98C
Atom 1065 CG2 ILE A132.265 23.162 12.922.00 11.44C
Atom 1066 CD1 ILE A132.399 23.971.644 1.00 11.88C
Atom 1067N TYR A133 10.338 20.390 10.390.535 1.00.38N
Atom 1068 CA TYR A133 9.132.19.573 10.410.00.8.99C
Atom 1069C TYR A133.9.432 18.147 9.969.00.9.72C
Atom 1070O TYR A133 8.939.17.205.617 1.00 10.00O
Atom 1071 CB TYR A133 8.081 20.292 9.552 1.00 10.09C
Atom 1072 CG TYR A133.637 21.574 10.221.1.00.8.61C
Atom 1073 CD1 TYR A133 6.636 21.567.187.1.00 8.73C
Atom 1074 CD2 TYR A133 8.260 22.784.933 1.00 9.50C
Atom 1075 CE1 TYR A133.6.261 22.732 11.848 1.00.36C
Atom 1076 CE2 TYR A133 7.891.949.9410.574 1.00 9.41C
Atom 1077 CZ TYR A133 6.893 23.915 11.533.1.00 6.97C
Atom 1078 OH TYR A133 6.553 25.084.165.1.00.9.21O
Atom 1079N PRO A134 10.223 17.903 8.918 1.00 10.31N
Atom 1080 CA PRO A134 10.577.16.508 8.614 1.00.10C
Atom 1081C PRO A134.335 15.837.741.1.00.30C
Atom 1082O PRO A134.147.14.636.9.983.00.12.88O
Atom 1083 CB PRO A134.417 16.606.331.1.00 12.71C
Atom 1084 CG PRO A134.089.934 6.744 1.00 17.29C
Atom 1085 CD PRO A134.721 18.835.888 1.00 10.25C
Atom 1086N TYR A135 12.166 16.587.10.464 1.00 11.35N
Atom 1087 CA TYR A135.869.017 11.605.1.00 11.09C
Atom 1088C TYR A135.878.539 12.662 1.00 11.97C
Atom 1089O TYR A135.992 14.419.13.183 1.00 12.88O
Atom 1090 CB TYR A135 13.823 17.053.198 1.00 13.77C
Atom 1091 CG TYR A135 14.436 16.611 13.502.00 16.42C
Atom 1092 CD1 TYR A135.595 15.843.520.00 20.53C
Atom 1093 CD2 TYR A135.862 16.962 14.714.1.00 16.18C
Atom 1094 CE1 TYR A135.16.160.15.431 14.710.00.23.68C
Atom 1095 CE2 TYR A135.422 16.551 15.917 1.00 20.34C
Atom 1096 CZ TYR A135 15.569.787.899.00.21.31C
Atom 1097 OH TYR A135 16.129 15.378 17.086.00.28.56O
Atom 1098N LEU A136.906.16.387 13.010 1.00 10.06N
Atom 1099 CA LEU A136.940.16.026 14.047.00 11.32C
Atom 1100C LEU A136.062 14.861 13.616 1.00 10.52C
Atom 1101O LEU A136.734 13.992 14.434 1.00 12.06O
Atom 1102 CB LEU A136.059.229.229 14.370.1.00 12.27C
Atom 1103 CG LEU a 136.742, 18.388, 15.084.00, 12.04C
Atom 1104 CD1 LEU A136.934 19.670 14.891.00 13.51C
Atom 1105 CD2 LEU A136.930.18.063 16.566.1.00 17.38C
Atom 1106N ALA A137.8.626 14.851 12.353 1.00 11.12N
Atom 1107 CA ALA A137 7.772 13.765 11.889.00 12.57C
Atom 1108C ALA A137 8.488 12.429 11.997 1.00 12.90C
Atom 1109O ALA A137 7.896.432 12.428 1.00 14.69O
Atom 1110 CB ALA A137 7.327 14.031 10.454 1.00 14.44C
Atom 1111N AGLU A138.777.12.406 11.646 0.41.54N
Atom 1112 CA AGLU A138.569.181.11.702 0.41.16.43C
Atom 1113C AGLU A138.826 10.757.142 0.41 16.84C
Atom 1114O AGLU A138.779.564 13.465.0.41.77O
Atom 1115 CB AGLU A138.891.418 10.971.41.69C
Atom 1116 CG AGLU A138.871 10.258 10.989.41.55C
Atom 1117 CD AGLU A138.726 10.215.9.735 0.41.25.05C
Atom 1118 OE1AGLU A138.13.469.352.8.870 0.41.93O
Atom 1119 OE2AGLU A138.648 11.049.609 0.41.83O
Atom 1120N BGLU A138.762 12.379.608.11.608 0.59.58N
Atom 1121 CA BGLU A138.508 11.132.11.737 0.59.16.37C
Atom 1122C BGLU A138 10.677.760.13.201 0.59.16.57C
Atom 1123O BGLU A138.421 9.617 13.599.59.16.61O
Atom 1124 CB BGLU A138.875 11.258 BGLU A11.064.59.38C
Atom 1125 CG BGLU A138.550 9.915 10.915.766 0.59.62C
Atom 1126 CD BGLU A138.290 9.333.11.963 0.59.23.95C
Atom 1127 OE1BGLU A138.597.10.087.912 0.59.98O
Atom 1128 OE2BGLU A138.572 8.113.11.950 0.59.40O
Atom 1129N LYS A139.095.720.14.023 1.00 15.11N
Atom 1130 CA LYS A139 11.432 11.393 15.401.00 15.82C
Atom 1131C LYS A139 10.223 10.877.165 1.00 16.69C
Atom 1132O LYS A139.341.9.949.16.976.00.17.18O
Atom 1133 CB LYS A139 12.025 12.621 16.088.00 16.52C
Atom 1134 CG LYS A139 12.413 12.371 17.530.00 15.19C
Atom 1135 CD LYS A139 13.179 13.538 18.123.123 1.00 19.86C
Atom 1136 CE LYS A139 13.399 13.341 19.621 1.00 22.25C
Atom 1137 NZ LYS A139 14.277 14.404 20.179 1.00 29.14N
Atom 1138N TYR A140 9.047.446 15.911 1.00 13.85N
Atom 1139 CA TYR A140 7.856 11.127.682 1.00 15.64C
Atom 1140C TYR A140.877.10.237 15.932.1.00 16.63C
Atom 1141O TYR A140.735 10.085.377 1.00 17.69O
Atom 1142 CB TYR A140 7.198 12.407 17.208 1.00 16.90C
Atom 1143 CG TYR A140.096.081 18.213 1.00 15.04C
Atom 1144 CD1 TYR A140 8.223 12.573 19.493 1.00 17.92C
Atom 1145 CD2 TYR A140.8.877.169 17.860.1.00 14.61C
Atom 1146 CE1 TYR A140.9.075 13.155 20.407 1.00 17.89C
Atom 1147 CE2 TYR A140.9.731 14.761 18.767.00 15.54C
Atom 1148 CZ TYR A140.9.825 14.251 20.049.00 16.72C
Atom 1149 OH TYR A140.10.682 14.838 20.956 1.00 18.82O
Atom 1150N ASP A141.307 9.632 14.824 1.00 17.02N
Atom 1151 CA ASP A141.469.735 14.028 1.00.04C
Atom 1152C ASP A141 5.129.389 13.697.00.21.25C
Atom 1153O ASP A141.4.052 8.808 13.861 1.00.49O
Atom 1154 CB ASP A141.294 7.375 14.707 1.00 24.94C
Atom 1155 CG ASP A141 5.526 6.385 13.846 1.00 33.21C
Atom 1156 OD1 ASP A141 5.569.514 12.603.00 1.37.35O
Atom 1157 OD2 ASP A141.868 5.490 14.418 1.00 41.81O
Atom 1158N ALA A142.206.10.631 13.240.00.16.03N
Atom 1159 CA ALA A142 4.031 11.393 12.871 1.00 15.70C
Atom 1160C ALA A142.939.449 11.358.1.00.13.41C
Atom 1161O ALA A142.957.11.508.10.662.00.15.87O
Atom 1162 CB ALA A142 4.118 12.817 13.419.00 16.11C
Atom 1163N LYS A143.722 11.430.848 1.00 12.61N
Atom 1164 CA LYS A143.542.11.729.439 1.00.13.06C
Atom 1165C LYS A143 2.743 13.222.9.224.00 11.61C
Atom 1166O LYS A143 2.542 14.030 10.136 1.00 12.79O
Atom 1167 CB LYS A143.163.11.282 8.984.00.14.70C
Atom 1168 CG LYS A143.073.759.851.1.00 22.53C
Atom 1169 CD LYS A143-0.353 9.277 8.728 1.00 30.17C
Atom 1170 CE LYS A143-0.400.7.816.8.295 1.00 33.58C
Atom 1171 NZ LYS A143-0.563 6.898.456 1.00 34.04N
Atom 1172N LEU A144 3.175.13.585 8.021 1.00.12.27N
Atom 1173 CA LEU A144.3.557 14.959.723.1.00.86C
Atom 1174C LEU A144.888 15.403.6.433.1.00.11.68C
Atom 1175O LEU A144 2.968.709 5.412.1.00.65O
Atom 1176 CB LEU A144.075 15.080 7.558.1.00.11C
Atom 1177 CG LEU A144 5.590 16.441 7.087.00.11.86C
Atom 1178 CD1 LEU A144.395 17.504 8.162.1.00.57C
Atom 1179 CD2 LEU A144.055 16.340.6.705 1.00 16.97C
Atom 1180N VAL A145 2.237 16.561 6.473 1.00 10.10N
Atom 1181 CA VAL A145.930 17.329 5.273 1.00.10C
Atom 1182C VAL A145.104.18.277.5.061 1.00 10.39C
Atom 1183O VAL A145.296 19.187 5.879.00.10.07O
Atom 1184 CB VAL A145 0.617 18.108.421 1.00.33C
Atom 1185 CG1 VAL A145 0.447 19.100.279 1.00.12.84C
Atom 1186 CG2 VAL A145-0.579.151.5.482 1.00 13.61C
Atom 1187N PRO A146.940 18.070 4.044.00.10.26N
Atom 1188 CA PRO A146 5.200 18.824 3.996.00 10.89C
Atom 1189C PRO A146 5.006 20.325.953.00.10.27C
Atom 1190O PRO A146 5.771 21.062 4.585 1.00.10.24O
Atom 1191 CB PRO A146 5.887.18.292 2.729.00 13.22C
Atom 1192 CG PRO A146.327 16.916 2.565 1.00 16.38C
Atom 1193 CD PRO A146.888 17.008 3.024 1.00.12.89C
Atom 1194N PHE A147.991 20.809 3.237.00 10.60N
Atom 1195 CA PHE A147 3.806 22.248.027 1.00.10.68C
Atom 1196C PHE A147 2.306.22.519 3.125.00.9.65C
Atom 1197O PHE A147 1.577.457 2.130.00 10.23O
Atom 1198 CB PHE A147 4.405 22.666 1.684 1.00.15C
Atom 1199 CG PHE A147.365 24.159 1.393 1.00 12.32C
Atom 1201 CD2 PHE A147 4.735 24.616 0.141.1.00 15.16C
Atom 1202 CE1 PHE A147 3.948.453.2.019 1.00 15.04C
Atom 1203 CE2 PHE A147.712 25.972-0.167.00 15.64C
Atom 1204 CZ PHE A147 4.317.26.886.765 1.00 17.13C
Atom 1205N PHE A148.850.22.831 4.336.00.9.83N
Atom 1206 CA PHE A148 0.419 22.977.575 1.00 10.24C
Atom 1207C PHE A148-0.204.24.034.671 1.00 10.84C
Atom 1208O PHE A148-1.309.23.839.151.00.10.12O
Atom 1209 CB PHE A148 0.192 23.306.048.00 10.44C
Atom 1210 CG PHE A148-1.243 23.558 6.398 1.00 10.54C
Atom 1211 CD1 PHE A148-2.222.637 6.067.00 14.60C
Atom 1212 CD2 PHE A148-1.615 24.713.713 7.056.00 14.30C
Atom 1213 CE1 PHE A148-3.551 22.864 6.395 1.00 16.46C
Atom 1214 CE2 PHE A148-2.943 24.943.947.387 1.00 17.34C
Atom 1215 CZ PHE A148-3.907 24.014 7.049.00 16.59C
Atom 1216N LEU A149 0.475 25.157 3.470 1.00 9.60N
Atom 1217 CA LEU A149-0.088.251 2.679.00 10.22C
Atom 1218C LEU A149 0.236.26.155.190.1.00.10.27C
Atom 1219O LEU A149 0.023 27.133.0.460.00.11.08O
Atom 1220 CB LEU A149 0.370.27.606 3.226.1.00 10.11C
Atoms 1221 CG LEU A149-0.182.27.967.603.1.00.92C
Atom 1222 CD1 LEU A149 0.366 29.315 5.043.00.99C
Atom 1223 CD2 LEU A149-1.709 27.984.607.00 15.92C
Atom 1224N GLU A150.748 25.020 0.723 1.00 10.00N
Atom 1225 CA GLU A150 1.138.24.895-0.679.00.12.27C
Atoms 1226C GLU A150 0.020 25.295-1.633 1.00.86C
Atom 1227O GLU A150 0.272 25.948-2.653 1.00 12.01O
Atoms 1228 CB GLU A150 1.572 23.463-0.956 1.00.46C
Atom 1229 CG GLU A150.131.23.249-2.348 1.00 14.66C
Atom 1230 CD GLU A150 2.689.21.847-2.513 1.00 25.34C
Atomic 1231 OE1 GLU A150.058.893-2.007 1.00 30.31O
Atom 1232 OE2 GLU A150.755 21.699-3.147 1.00.34.85O
Atom 1233N ALA A151-1.218.911-1.331-1.00 10.51N
Atom 1234 CA ALA A151-2.289 25.127-2.297 1.00.11.45C
Atom 1235C ALA A151-2.663 26.592-2.460.00 12.64C
Atomic 1236O ALA A151-3.346 26.921-3.435.00.14.72O
Atom 1237 CB ALA A151-3.511 24.293-1.935 1.00 13.46C
Atoms 1238N VAL A152-2.241N 27.481-1.567.00N 11.90N
Atom 1239 CA VAL A152-2.456 28.911-1.765 1.00 13.11C
Atom 1240C VAL A152-1.171.653-2.086.00 13.74C
Atom 1241O VAL A152-1.207 30.880-2.277 1.00 14.66O
Atom 1242 CB VAL A152-3.213.29.561-0.593.00 12.93C
Atoms 1243 CG1 VAL A152-4.600.940-0.455 1.00 16.42C
Atom 1244 CG2 VAL A152-2.411 29.438 0.706 1.00 14.95C
Atomic 1245N ALA A153-0.048.936-2.224.00 16.69N
Atom 1246 CA ALA A153.262.29.573-2.335.00 22.91C
Atom 1247C ALA A153 1.354 30.460-3.566 1.00.50C
Atom 1248O ALA A153.012 31.507-3.539 1.00.30.21O
Atom 1249 CB ALA A153.353 28.502-2.375 1.00 24.30C
Atom 1250N ASP A154 0.720.30.049-4.660 1.00 19.76N
Atom 1251 CA ASP A154 0.766 30.794-5.909 1.00.53C
Atoms 1252C ASP A154-0.542.517-6.193 1.00.27C
Atoms 1253O ASP A154-0.833 31.830-7.351 1.00 18.88O
Atom 1254 CB ASP A154.122.867-7.073.00.23.91C
Atom 1255 CG ASP A154 2.500.256-6.931 1.00 40.79C
Atoms 1256 OD1 ASP A154.426.29.970-6.491 1.00.68O
Atoms 1257 OD2 ASP A154 2.656 28.059-7.259 1.00 51.68O
Atoms 1258N ARG A155-1.353.31.770-5.168 1.00 13.78N
Atom 1259 CA ARG A155-2.717 32.257-5.355 1.00 12.13C
Atom 1260C ARG A155-2.979.453-4.451 1.00 13.31C
Atoms 1261O ARG A155-3.694 33.348-3.450.00.84O
Atoms 1262 CB ARG A155-3.720.31.133-5.097.00 11.76C
Atoms 1263 CG ARG A155-3.695 30.013-6.122 1.00 11.87C
Atoms 1264 CD ARG A155-4.217 30.454-7.483 1.00 11.22C
Atom 1265 NE ARG A155-5.551 31.053-7.452 1.00 10.93N
Atom 1266 CZ ARG A155-6.688 30.388-7.628 1.00 10.40C
Atoms 1267 NH1 ARG A155-6.676 29.076-7.812 1.00 12.13N
Atoms 1268 NH2 ARG A155-7.846 31.034-7.620.00 10.93N
Atoms 1269N PRO A156-2.424.34.620-4.787.00 15.63N
Atom 1270 CA PRO A156-2.713 35.817-3.977.00 15.46C
Atoms 1271C PRO A156-4.189 36.160-3.918 1.00 14.67C
Atoms 1272O PRO A156-4.629 36.787-2.948.00 16.35O
Atom 1273 CB PRO A156-1.886.924-4.651 1.00 21.28C
Atom 1274 CG PRO A156-1.494 36.385-5.978.00 21.80C
Atom 1275 CD PRO A156-1.462, 34.894-5.869.00.16C
Atoms 1276N ASP A157-4.975.737-4.909 1.00 12.29N
Atom 1277 CA ASP A157-6.416.35.950-4.876.00 13.35C
Atoms 1278C ASP A157-7.124.35.116-3.813 1.00 13.08C
Atom 1279O ASP A157-8.303.35.370-3.535 1.00.70O
Atom 1280 CB ASP A157-7.034.683-6.248.1.00 12.70C
Atom 1281 CG ASP A157-6.724 34.296-6.787.00 12.73C
Atom 1282 OD1 ASP A157-5.655 33.726-6.454 1.00 13.07O
Atoms 1283 OD2 ASP A157-7.534 33.784-7.590.00 13.59O
Atoms 1284N LEU A158-6.429 34.154-3.196 1.00 11.11N
Atoms 1285 CA LEU A158-6.988.295-2.161.00.10.08C
Atoms 1286C LEU A158-6.438 33.629-0.787.00.12.24C
Atoms 1287O LEU A158-6.644 32.859.159 1.00 12.42O
Atoms 1288 CB LEU A158-6.715 31.827-2.484 1.00 11.43C
Atoms 1289 CG LEU A158-7.311.31.301-3.791.00 11.35C
Atom 1290 CD1 LEU A158-6.947.846-3.969.00 12.82C
Atom 1291 CD2 LEU A158-8.825 31.492-3.843.00 13.55C
Atom 1292N ILE A159-5.748 34.761-0.658.00 12.74N
Atom 1293 CA ILE A159-5.130.197.588 1.00.92C
Atom 1294C ILE A159-5.782 36.508 0.992.00 14.58C
Atom 1295O ILE A159-5.947.409 0.158.00 14.30O
Atom 1296 CB ILE A159-3.608 35.367 0.422 1.00 17.20C
Atom 1297 CG1 ILE A159-2.967.040 0.002 1.00 17.99C
Atom 1298 CG2 ILE A159-2.974.894.894.697.00 18.69C
Atom 1299 CD1 ILE A159-3.298 32.908 0.918 1.00 22.39C
Atom 1300N GLN A160-6.176 36.602 2.256 1.00 15.16N
Atom 1301 CA GLN A160-6.796.37.813 2.765 1.00 16.24C
Atom 1302C GLN A160-5.799.958 2.726 1.00.19.09C
Atom 1303O GLN A160-4.601.38.776 2.939.00 18.47O
Atom 1304 CB GLN A160-7.203 37.615 4.222.00 17.93C
Atom 1305 CG GLN A160-8.282 36.584 4.462 1.00 25.01C
Atom 1306 CD GLN A160-8.623 36.472 5.933 1.00 24.65C
Atom 1307 OE1 GLN A160-8.742. Sup.37.482.482.630.00.30.72O
Atom 1308 NE2 GLN A160-8.754 35.242 6.422 1.00 22.16N
Atom 1309N ALYS A161-6.309 40.139 2.409 0.69 20.65N
Atom 1310 CA ALYS A161-5.564 41.375 2.573 0.69 23.23C
Atom 1311C ALYS A161-5.808 41.845 4.000 0.69.37C
Atom 1312O ALYS A161-6.941 42.176 4.365 0.69 24.88O
Atom 1313 CB ALYS A161-6.057.414 1.571 0.69.96C
Atom 1314 CG ALYS A161-5.343 43.754 1.650 0.69.87C
Atom 1315 CD ALYS A161-3.832 43.580.721 0.69.00C
Atom 1316 CE ALYS A161-3.132 44.272 0.558 0.69 28.07C
Atoms 1317 NZ ALYS A161-2.883.333-0.572 0.69 30.55N
Atom 1318N BLYS A161-6.288 40.161 2.470 0.31.09N
Atom 1319 CA BLYS A161-5.438 41.347 2.546 0.31.43C
Atom 1320C BLYS A161-5.696.015.3.891.31.66C
Atom 1321O BLYS A161-6.722 42.670 4.086.31.86O
Atom 1322 CB BLYS A161-5.698A 42.294 1.384 0.31.27C
Atom 1323 CG BLYS A161-6.825 41.860 0.495 0.31.35C
Atom 1324 CD BLYS A161-7.570 43.059-0.021 0.31.49C
Atom 1325 CE BLYS A161-8.650.42.622-0.961.31.07C
Atom 1326 NZ BLYS A161-8.127.41.710-2.014 0.31.33N
Atom 1327N ASP A162-4.759.838 4.819 1.00 25.68N
Atom 1328 CA ASP A162-4.870 42.403.157 1.00.56C
Atom 1329C ASP A162-3.606 43.184.492 1.00 28.88C
Atom 1330O ASP A162-3.525.387 6.218 1.00 30.53O
Atoms 1331 CB ASP A162-5.160 41.313 7.199 1.00.07C
Atom 1332 CG ASP A162-4.432 40.013 6.911 1.00.75C
Atom 1333 OD1 ASP A162-3.217 40.053.630.00.29.09O
Atom 1334 OD2 ASP A162-5.076.942 6.964.00 30.35O
Atom 1335N HIS A163-2.615 42.515.515.057.00.24.24N
Atom 1336 CA HIS A163-1.373 43.202 7.360.00 26.59C
Atom 1337C HIS A163-0.698.43.639.077.00.27.71C
Atom 1338O HIS A163-0.655 42.917 5.095.00.11O
Atom 1339 CB HIS A163-0.401 42.314 8.128 1.00.48C
Atom 1340 CG HIS A163-0.892 41.879.473 1.00 33.67C
Atom 1341 ND1 HIS A163-0.381 42.381 10.652 1.00 32.55N
Atom 1342 CD2 HIS A163-1.822 40.961.824.00.36.61C
Atom 1343 CE1 HIS A163-0.989.800.671 1.00 36.69C
Atom 1344 NE2 HIS A163-1.864 40.933 11.196.00 40.61N
Atom 1345N VAL A164-0.154 44.835 6.104.00.26.44N
Atom 1346 CA VAL A164.571 45.399 4.968.00 27.88C
Atom 1347C VAL A164.853.45.997.5.534 1.00.26.09C
Atom 1348O VAL A164.848 47.126 6.038.00 32.33O
Atom 1349 CB VAL A164-0.254.46.448 4.205 1.00 27.23C
Atom 1350 CG1 VAL A164.610.47.196 3.192.1.00 24.79C
Atoms 1351 CG2 VAL A164-1.428 45.789.504 1.00 29.29C
Atom 1352N HIS A165 2.947.45.227 5.495 1.00 21.54N
Atom 1353 CA HIS A165.246 45.704.956 1.00 20.07C
Atom 1354C HIS A165.106.033.4.756 1.00 18.53C
Atom 1355O HIS A165.460.45.117 3.998.00 22.77O
Atom 1356 CB HIS A165.955 44.641 6.763.00 22.13C
Atom 1357 CG HIS A165.151.44.128.899.00.29.75C
Atom 1358 ND1 HIS A165.227 42.826 8.335.00.34.64N
Atom 1359 CD2 HIS A165.240.44.743 8.684 1.00.86C
Atom 1360 CE1 HIS A165.399 42.662.9.350.1.00 32.20C
Atom 1361 NES 2 HIS A165 2.797.811 9.583.00.27.61N
Atom 1362N PRO A166 5.510.281 4.567.00 13.92N
Atom 1363 CA PRO A166 6.410 47.594 3.451 1.00 13.35C
Atom 1364C PRO A166.773.46.929.611.1.00 11.56C
Atom 1365O PRO A166.8.297 46.796.719.00.14.08O
Atom 1366 CB PRO A166 6.533.49.123 3.514 1.00 12.32C
Atom 1367 CG PRO A166 5.312 49.567.308.1.00 20.34C
Atom 1368 CD PRO A166 5.088.480.5.313 1.00 16.34C
Atom 1369N THR A167.356.46.518.2.484 1.00 11.67N
Atom 1370 CA THR A167.771 46.157 2.457.1.00 11.58C
Atom 1371C THR A167.609 47.417 2.652 1.00 11.73C
Atom 1372O THR A167 10.089.533.2.710 1.00 11.44O
Atom 1373 CB THR A167.133.45.536 1.113.00 11.18C
Atom 1374 OG1 THR A167.946 46.538 0.115.00 11.10O
Atom 1375 CG2 THR A167.241.44.329 0.795.00 12.93C
Atom 1376N ALA A168.932 47.249 2.729.00.12.92N
Atom 1377 CA ALA A168.799.48.418 2.857.00 13.41C
Atom 1378C ALA A168.12.616 49.364.675 1.00 12.24C
Atom 1379O ALA A168.576 50.594 1.836 1.00 12.15O
Atom 1380 CB ALA A168 14.257 47.974.984.00 16.50C
Atom 1381N ARG A169 12.470 48.803.476 0.476 1.00.42N
Atom 1382 CA ARG A169 12.209.49.620-0.698 1.00 11.91C
Atom 1383C ARG A169 10.817 50.242-0.625 1.00 12.18C
Atom 1384O ARG A169.622 51.396-1.020 1.00 11.20O
Atom 1385 CB ARG A169 12.388.758-1.949.00 13.09C
Atom 1386 CG ARG A169 12.209 49.461-3.264 1.00 15.94C
Atom 1387 CD ARG A169 13.300.50.491-3.547 1.00.40C
Atom 1388 NE ARG A169 12.984.51.219-4.774 1.00.27.09N
Atom 1389 CZ ARG A169.993.52.102-4.874 1.00.13C
Atoms 1390 NH1 ARG A169.11.246.385-3.816.1.00 27.88N
Atom 1391 NH2 ARG A169.751 52.714-6.022 1.00.16N
Atoms 1392N GLY A170.9.841.49.493-0.104.00.10.43N
Atom 1393 CA GLY A170.522 50.065.112.00.10.60C
Atomic 1394C GLY A170.548.51.243.1.070 1.00.9.39C
Atom 1395O GLY A170.831.52.224.0.872 1.00.77O
Atom 1396N VAL A171.375 51.161 2.115.1.00 9.65N
Atom 1397 CA VAL A171.518.52.288 3.043.00.9.90C
Atom 1398C VAL A171.021 53.519 2.307.1.00 10.48C
Atom 1399O VAL A171.514.54.630.2.497 1.00.10.46O
Atom 1401 CG1 VAL A171 10.897.53.192.192.945 1.00 12.07C
Atom 1402 CG2 VAL A171.751 50.989.989.175.00.11.34C
Atom 1403N GLU A172.023 53.342.1.436.00.11.47N
Atom 1404 CA GLU A172.533.54.478 0.675 1.00 12.28C
Atom 1405C GLU A172.429 55.102-0.159 1.00 10.48C
Atom 1406O GLU A172.365.56.326-0.312.00.12.23O
Atom 1407 CB GLU A172.718 54.038-0.188 1.00 14.42C
Atom 1408 CG GLU A172.899.53.598.654.00.16.84C
Atom 1409 CD GLU A172.062 53.087-0.169 1.00 26.14C
Atom 1410 OE1 GLU A172.913 52.946-1.403.00.26.18O
Atom 1411 OE2 GLU A172.126.52.820 0.428 1.00.13O
Atom 1412N AGLU A173.543.54.273-0.714 0.53.10.74N
Atoms 1413 CA AGLU A173.405.54.797-1.461 0.53.17C
Atom 1414C AGLU A173.506.644-0.573 0.53.00C
Atom 1415O AGLU A173.054.721-0.975.53.11.21O
Atom 1416 CB AGLU A173.597.53.641-2.034.53.54C
Atom 1417 CG AGLU A173.231 AGLU A53.013-3.222 0.53.06C
Atoms 1418 CD AGLU A173.262.53.943-4.390 0.53.96C
Atom 1419 OE1AGLU A173.202 54.524-4.709 0.53.23O
Atom 1420 OE2AGLU A173.346.54.099-4.982.53.14O
Atom 1421N BGLU A173.546 54.264-0.705 0.47.76N
Atom 1422 CA BGLU A173.402.749-1.464 0.47.21C
Atom 1423C BGLU A173.482.55.604-0.595 0.47.06C
Atom 1424O BGLU A173.009 56.662-1.025 0.47.24O
Atom 1425 CB BGLU A173.655 53.537-2.022 0.47.45C
Atom 1426 CG BGLU A173.582 53.848-3.028 0.47.16C
Atom 1427 CD BGLU A173.142.54.386-4.314 0.47.86C
Atom 1428 OE1BGLU A173.294.54.041-4.673.47.58O
Atom 1429 OE2BGLU A173.424.55.163-4.972 0.47.24O
Atom 1430N LEU A174.222.55.161.638 1.00.8.92N
Atom 1431 CA LEU A174.376.55.927.550.00.9.69C
Atom 1432C LEU A174.042.57.233.1.939.00.9.85C
Atom 1433O LEU A174.377 58.267 2.043.00 10.58O
Atom 1434 CB LEU A174.099.120.2.815 1.00 10.61C
Atom 1435 CG LEU A174.334 53.818.2.629 1.00 10.63C
Atom 1436 CD1 LEU A174.259 53.073.957.00.17.31C
Atom 1437 CD2 LEU A174.944 54.091 2.094.00 11.93C
Atom 1438N VAL A175.354 57.190 2.173 1.00 9.05N
Atom 1439 CA VAL A175.088.402 2.527 1.00 10.08C
Atom 1440C VAL A175.009 59.418.394 1.00 9.91C
Atom 1441O VAL A175.767.60.610.1.617.1.00 11.49O
Atom 1442 CB VAL A175.540 58.050 2.906.1.00.82C
Atom 1443 CG1 VAL A175.383.59.302.302.024 1.00.12.59C
Atom 1444 CG2 VAL A175.568 57.281 4.209.00.11.17C
Atom 1445N ASER A176.187 58.963 0.152.69 10.53N
Atom 1446 CA ASER A176 9.134.890-0.974.69.11.61C
Atom 1447C ASER A176 7.760 60.525-1.109.0.69.72C
Atom 1448O ASER A176 7.651 61.691-1.514.69 12.63O
Atom 1449 CB ASER A176 9.532 59.179-2.268 0.69.09C
Atom 1450 OG ASER A176 10.893.799-2.215.69 13.20O
Atom 1451N BSER A176 9.184 58.956 0.152 0.31.67N
Atom 1452 CA BSER A176.134.866-0.989.31.69C
Atom 1453C BSER A176 7.761 60.503-1.143 0.31.80C
Atom 1454O BSER A176.655 61.646-1.604 0.31.12.75O
Atom 1455 CB BSER A176.537 59.135-2.274 0.31.15C
Atom 1456 OG BSER A176 8.542.58.211-2.685 0.31.49O
Atom 1457N ALA A177 6.700.794-0.753 1.00 10.41N
Atom 1458 CA ALA A177 5.350.313-0.903 1.00 10.06C
Atom 1459C ALA A177.913 61.217 0.241 1.00 11.06C
Atom 1460O ALA A177 3.998.024 0.054.00 13.49O
Atom 1461 CB ALA A177.4.357 59.156-1.008 1.00 12.58C
Atom 1462N THR A178.544.61.119.414.1.00.9.55N
Atom 1463 CA THR A178.057.807 2.606 1.00 10.26C
Atom 1464C THR A178.022 62.833 3.186.00.10.17C
Atom 1465O THR A178.632.63.557 4.115.00.10.56O
Atom 1466 CB THR A178.690 60.796.707 1.00.62C
Atom 1467 OG1 THR A178.846.60.036.068.00 10.59O
Atom 1468 CG2 THR A178.579.855 3.221.00 13.64C
Atom 1469N SER A179 7.258 62.927.681 1.00 10.72N
Atom 1470 CA SER A179 8.217 63.838 3.299 1.00 11.00C
Atom 1471C SER A179 7.792 65.291 3.150.1.00 10.57C
Atom 1472O SER A179 8.049.101.046.00.10.62O
Atom 1473 CB SER A179 9.607 63.638 2.709 1.00 10.83C
Atom 1474 OG SER A179 10.203 62.454 3.197 1.00 11.85O
Atom 1475N ASN A180.162.65.650.2.028 1.00.9.59N
Atom 1476 CA ASN A180.661 67.013 1.868 1.00 11.71C
Atom 1477C ASN A180.698 67.359.2.989.00 11.58C
Atom 1478O ASN A180.773.444.3.574 1.00 12.02O
Atom 1479 CB ASN A180.937.166 0.528 1.00 12.94C
Atom 1480 CG ASN A180.885.202-0.667 1.00 18.16C
Atom 1481 OD1 ASN A180.084.405-0.518.00 19.11O
Atom 1482 ND2 ASN A180.337.67.007-1.867.00 17.71N
Atom 1483N ALA A181 4.776 66.445 3.299 1.00 10.56N
Atom 1484 CA ALA A181 3.793.66.712 4.346 1.00.10.80C
Atom 1485C ALA A181.462.66.865 5.704.1.00.9.46C
Atom 1486O ALA A181 4.063 67.717 6.510.00 11.90O
Atom 1487 CB ALA A181 2.762 65.584 4.387 1.00 13.72C
Atom 1488N VAL A182.470 66.039.984.00.9.76N
Atom 1489 CA VAL A182.163.66.122.263 1.00 9.85C
Atom 1490C VAL A182.909 67.444 7.379.00.9.49C
Atom 1491O VAL A182.846.68.131.410.00.10.97O
Atom 1492 CB VAL A182.117 7.64.929.433.00.8.87C
Atom 1493 CG1 VAL A182.940 65.095.8.706 1.00 10.74C
Atom 1494 CG2 VAL A182.352.63.615 7.453.1.00.11.20C
Atom 1495N ALA A183.632 67.817 6.315.00.9.90N
Atom 1496 CA ALA A183 8.389 69.066.333.1.00 10.92C
Atom 1497C ALA A183 7.467 70.260.505.1.00.77C
Atom 1498O ALA A183.806 71.219.7.213 1.00 14.12O
Atom 1499 CB ALA A183 9.208.207.5.049.00.12.40C
Atom 1500N ALYS A184.281 70.205.890 0.50.99N
Atom 1501 CA ALYS A184.314 71.297 5.981 0.50.11C
Atom 1502C ALYS A184.667 71.372 7.358 0.50.29C
Atom 1503O ALYS A184.299 72.462.7.813 0.50.83O
Atom 1504 CB ALYS A184.251.71.131.890.0.50.81C
Atom 1505 CG ALYS A184.003 72.000 5.043.50.31C
Atom 1506 CD ALYS A184 2.104 71.894.815 0.50.85C
Atom 1507 CE ALYS A184 0.896.815 3.928 0.50.54C
Atom 1508 NZ ALYS A184 0.166 72.940 2.636 0.50.39N
Atom 1509N BLYS A184 6.296 70.231 5.871 0.50.98N
Atom 1510 CA BLYS A184.363 71.341 6.027 0.50.13C
Atom 1511C BLYS A184.799.71.395 7.441 0.50.20C
Atom 1512O BLYS A184.629 72.483 8.007 0.50.35O
Atom 1513 CB BLYS A184 4.238 71.241 4.998 0.50.74C
Atom 1514 CG BLYS A184.664 71.534 3.569.50.74C
Atom 1515 CD BLYS A184 3.472 71.510.626 0.50.49C
Atom 1516 CE BLYS A184.869.009 1.248 0.50.98C
Atom 1517 NZ BLYS A184.806 70.159 0.653 0.50.21N
Atomic 1518N ALA A185.4.514 70.232.8.031 1.00.70N
Atom 1519 CA ALA A185.921 70.203.203 9.362 1.00 11.70C
Atom 1520C ALA A185.893.70.641 10.452 1.00 11.67C
Atom 1521O ALA A185.447 71.071 11.525.00.12.84O
Atom 1522 CB ALA A185.386 68.804.9.671 1.00 12.03C
Atom 1523N LEU A186.194 70.503 10.231 1.00 11.76N
Atom 1524 CA LEU A186.180.70.901 11.227 1.00 11.46C
Atom 1525C LEU A186.317.72.416.416.204.00.12.36C
Atom 1526O LEU A186.673.72.975.10.160.00.13.46O
Atom 1527 CB LEU A186.8.523 70.271.271.882 1.00 12.42C
Atom 1528 CG LEU A186.690 70.599.599.821 1.00 12.97C
Atom 1529 CD1 LEU A186.475.998.998.219.1.00 13.01C
Atom 1530 CD2 LEU A186.003 70.118 11.216.216.00 15.31C
Atom 1531N PRO A187 7.052 73.118 12.310.1.00 12.88N
Atom 1532 CA PRO A187.197.74.581 12.290 1.00 14.93C
Atom 1533C PRO A187 8.616 74.993 11.927.00 15.61C
Atom 1534O PRO A187 9.589.74.334 12.293 1.00 16.27O
Atom 1535 CB PRO A187 6.850 74.989.725.1.00 17.96C
Atom 1536 CG PRO A187 5.965 73.904 14.225 1.00 17.16C
Atom 1537 CD PRO A187 6.492 72.638 13.590 1.00 12.98C
Atom 1538N ALA A188.728 76.099.200.00 20.65N
Atom 1539 CA ALA A188.032 76.589.10.765 1.00 23.44C
Atom 1540C ALA A188.825 77.167.11.933 1.00 24.88C
Atom 1541O ALA A188.315 77.286 13.048.00 27.41O
Atom 1542 CB ALA A188.9.864 77.632 9.667 1.00.70C
TER 1543 ALA A 188
Sequence listing
<110> university of Compound Dan
<120> thermophilic esterase crystal three-dimensional structure derived from marine bacteria and expression purification method
<130> 001
<160> 4
<170> SIPOSequenceListing 1.0
<210> 1
<211> 190
<212> PRT
<213> Artificial Sequence (Artificial Sequence)
<400> 1
Met Gly Glu Ser Arg Val Ile Leu Ala Phe Gly Asp Ser Leu Phe Ala
1 5 10 15
Gly Tyr Gly Leu Asp Lys Gly Glu Ser Tyr Pro Ala Lys Leu Glu Thr
20 25 30
Ala Leu Arg Ser His Gly Ile Asn Ala Arg Ile Ile Asn Ala Gly Val
35 40 45
Ser Gly Asp Thr Thr Ala Ala Gly Leu Gln Arg Ile Lys Phe Val Leu
50 55 60
Asp Ser Gln Pro Asp Lys Pro Glu Leu Ala Ile Val Glu Leu Gly Gly
65 70 75 80
Asn Asp Leu Leu Arg Gly Leu Ser Pro Ala Glu Ala Arg Gln Asn Leu
85 90 95
Ser Gly Ile Leu Glu Glu Leu Gln Arg Arg Lys Ile Pro Ile Leu Leu
100 105 110
Met Gly Met Arg Ala Pro Pro Asn Leu Gly Ala Lys Tyr Gln Arg Glu
115 120 125
Phe Asp Gly Ile Tyr Pro Tyr Leu Ala Glu Lys Tyr Asp Ala Lys Leu
130 135 140
Val Pro Phe Phe Leu Glu Ala Val Ala Asp Arg Pro Asp Leu Ile Gln
145 150 155 160
Lys Asp His Val His Pro Thr Ala Arg Gly Val Glu Glu Leu Val Ser
165 170 175
Ala Thr Ser Asn Ala Val Ala Lys Ala Leu Pro Ala Lys Lys
180 185 190
<210> 2
<211> 573
<212> DNA
<213> Artificial Sequence (Artificial Sequence)
<400> 2
atgggcgaat cgcgcgtgat tctcgccttc ggagacagcc tgtttgcagg ctatggcctt 60
gataaggggg agagctatcc ggcaaagctg gaaactgcgc tgcgcagcca tggcatcaat 120
gccagaatca ttaatgccgg cgtttcgggt gacaccactg cggcagggct gcagcgaatc 180
aaattcgtgc tggatagcca gccggacaag ccggaattgg ccatagtgga actgggcggg 240
aatgaccttt tacgcggcct ctcaccagcc gaagcgcggc agaacctcag cggaatcctc 300
gaagaattgc agaggcggaa aattccaatc ctgttgatgg gaatgcgagc gccgcccaat 360
ctaggggcaa aatatcagcg cgaatttgat gggatttatc cctatctggc cgaaaaatat 420
gacgccaagc tggtaccttt cttccttgag gccgtggcag atagacctga cctcattcag 480
aaggatcacg ttcaccccac tgcgcgcggt gtggaggaac tcgtgtctgc aacatcgaat 540
gcagttgcca aggcgctgcc tgcgaagaag tga 573
<210> 3
<211> 24
<212> DNA
<213> Artificial Sequence (Artificial Sequence)
<400> 3
tcgcggatcc atgggcgaat cgcg 24
<210> 4
<211> 24
<212> DNA
<213> Artificial Sequence (Artificial Sequence)
<400> 4
tccgctcgag tcacttcttc gcag 24
Claims (6)
1. A thermophilic esterase crystal derived from a marine bacterium which isAltererythrobacter indicus DSM 18604 T The thermophilic esterase is AlinE4 which contains 190 amino acids and has the molecular weight of 20.5 kDa; the amino acid sequence of the esterase AlinE4 is shown as SEQ ID NO. 1; the method is characterized in that:
the crystal has the three-dimensional structure with the atomic coordinates listed in table 1;
the resolution is 1.18A; wherein the crystal structure space group of the esterase AlinE4 is P4 2 2 1 2, one asymmetric unit contains one molecule; the unit cell parameters are: a =79.783 a, b =79.783 a, c =61.010 a, α = β = γ =90.000 °.
2. A crystal according to claim 1, characterized by 5 β sheets, 9 α helices and 23 α helices 10 -a helical composition;
the 5 beta sheet is located in the center, the 9 alpha helix around the alpha 1 folding; wherein, beta sheet 1, the amino acid segment containing Arg5-Gly 11; α 0 helix 1, an amino acid segment comprising Ser13-Ala 16; alpha helix 2, an amino acid segment comprising Tyr26-His 37; beta sheet 2, an amino acid segment comprising Ala41-Gly 47; alpha helix 3, an amino acid segment comprising Thr53-Asp 65; beta sheet 3, an amino acid segment comprising Leu73-Glu 77; alpha helix 4, an amino acid segment containing Gly80-Leu 84; alpha helix 5, an amino acid segment containing Pro89-Arg 105; beta sheet 4I.e., an amino acid segment comprising Ile110-Met 113; 3 10 Helix 1, an amino acid segment containing Pro119-Leu 121; alpha helix 6, an amino acid segment containing Ala123-Asp 130; alpha helix 7, an amino acid segment comprising Ile132-Lys 139; beta sheet 5, an amino acid segment comprising Lys143-Val 145; alpha helix 8, an amino acid segment comprising Phe148-Val 152; 3 10 Helix 3, an amino acid segment containing Pro156-Leu 158; alpha helix 9, an amino acid segment containing Ala168-Ala 185.
3. The thermophilic esterase crystal according to claim 1, characterized in that the catalytic triad active center is constituted by serine at position 13, aspartic acid at position 162 and histidine at position 165; the active center is occupied by a cadmium ion.
4. The thermophilic esterase crystal according to claim 1, characterized in that the oxygen ion channel is constituted by serine at position 13, glycine at position 50 and asparagine at position 81.
5. A marine bacteriumAltererythrobacter indicus DSM 18604 T The method for expressing and purifying the esterase AlinE4 is characterized by comprising the following specific steps of: construction of fusion with wild typealine4A recombinant vector of a full-length gene, which is transformed into escherichia coli so as to express a fusion protein AlinE4 with a label, the obtained protein is separated into target protein by a specific and specific label identification method, and then high-purity esterase AlinE4 protein is obtained by a gel filtration chromatography method; wherein, the amino acid sequence of the esterase AlinE4 is shown as SEQ ID NO. 1, and the nucleic acid sequence is shown as SEQ ID NO. 2.
6. A process for the crystallization of crystals of the esterase AlinE4 derived from marine bacteria according to claim 1, characterized by the specific steps of concentrating the protein AlinE4 to a concentration of 10-60 mg/ml, using 50mM cadmium sulfate, pH7.5 buffer of 100mM hepes,1m sodium acetate as primary screening conditions for crystal growth, and performing crystallization by hanging drop gas phase diffusion at a temperature of 4-25 ℃.
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Citations (3)
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|---|---|---|---|---|
| CN106589104A (en) * | 2016-12-25 | 2017-04-26 | 复旦大学 | Archease and expression and purification, crystal structure as well as application of Archease |
| CN106676082A (en) * | 2016-12-25 | 2017-05-17 | 复旦大学 | Psychrophilic protein enzyme E10, as well as expression purification, crystal structure and application thereof |
| CN106754820A (en) * | 2016-12-14 | 2017-05-31 | 复旦大学 | Albumen esterase E8 and its expression and purification, crystal structure and application |
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2019
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| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN106754820A (en) * | 2016-12-14 | 2017-05-31 | 复旦大学 | Albumen esterase E8 and its expression and purification, crystal structure and application |
| CN106589104A (en) * | 2016-12-25 | 2017-04-26 | 复旦大学 | Archease and expression and purification, crystal structure as well as application of Archease |
| CN106676082A (en) * | 2016-12-25 | 2017-05-17 | 复旦大学 | Psychrophilic protein enzyme E10, as well as expression purification, crystal structure and application thereof |
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| Title |
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| Chain A, SGNH-hydrolase family esterase,PDB: 7C2A_A;Li,Z. and Li,J.;《NCBI》;20200520;第1-2页 * |
| Structure-guided protein engineering increases enzymatic activities of the SGNH family esterases;Zhengyang Li等;《Biotechnol Biofuels》;20200615;第13卷(第107期);第1-14页 * |
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