Method of screening for antimicrobial agents

Abstract

[Object] To identify FFRPs which are prospective targets of antimicrobial agents, and by using the FFRPs, to provide a pharmaceutical agent and a novel method for screening for a pharmaceutical agent, in particular, an agent that acts against P. aeruginosa.

Description

TECHNICAL FIELD OF THE INVENTION

The present invention relates to a method of identifying proteins that can be used for searching for antimicrobial agents and to a method of screening for agents by targeting these proteins.

DESCRIPTION OF THE RELATED ART

Metabolism, growth, and environmental adaptation of many bacteria are regulated by a group of genes closely related with each other. The products of these genes, which are referred to as “feast/famine regulatory proteins (FFRPs)”, bind to promoter regions in genomic DNAs and efficiently regulate transcription of genes positioned downstream. The term “FFRPs” was proposed by the present inventors by referring to “feast/famine regulation”, an expression (Nonpatent Document 1) used to summarize the function of the leucine-responsive regulatory protein (Lrp) of Escherichia coli, a protein in this group. When sensing an increase in the nutrition outside through a high concentration of leucine, E. coli pauses its motility, initiates active transport of nutrients from outside, shifts its metabolism to a more heterotrophic mode, and initiates its growth, eventually changing its infectivity. Another E. coli protein, the asparagine synthesis C gene product (AsnC) senses an increase in the nutrition outside through high concentration of asparagine and regulates biosynthesis of asparagine and growth of the bacterium. The amino acid sequence of AsnC resembles that of Lrp, and thus AsnC too is classified into the group of FFRPs. E. coli has a third FFRP whose function is yet unknown.

Pseudomonas aeruginosa opportunistically infects people whose defensibility is weakened, i.e., those who are suffering from cancer, burn injuries, immune disorder, or the like, and causes serious diseases, such as sepsis and cystic fibrosis, sometimes leading to death of the patient. P. aeruginosa adopts abilities to resist various antibiotics and disinfectants. The multi-drug resistancy of P. aeruginosa has caused serious inside hospital infections not only in developing countries but also in advanced countries. In an attempt to unravel the infection mechanism of P. aeruginosa, the genomic sequence of its standard strain PAO1 has been determined and published under international collaboration (Nonpatent Document 2). However, to date, this has not lead to development of effective agents.

Whereas most other pathogenic bacteria are parasitic and can only survive inside their hosts, P. aeruginosa adapts to and grows in various environments, those in water and soil, and those inside plants and animal tissues, and so on. Bacteria of the species P. aeruginosa communicate with each other by transmitting signals and their characteristics change largely once the number of the bacteria reaches a certain threshold. This mechanism called “quorum sensing” is rarely found with other bacterial species and in some sense comparable with intercellular signaling inside multicellular organisms such as humans. It is likely that this remarkable environmental adaptability of the organism, together with its opportunistic infectivity (i.e. its ability to change depending on host susceptibly) and its multi-drug resistancy (i.e. its ability to change by responding to drugs), all are of the same type of abilities, and underneath all these lying is an efficient mechanism of regulating transcription of a number of genes in various ways.

The present inventors have identified eight FFRPs (Nonpatent Document 3), by using the genomic sequence of P. aeruginosa publicly available. No FFRP has been found coded in many parasitic pathogens, and this can be a reflection of the fact that these pathogens are dependent on nutrition present inside their hosts and do not regulate their metabolisms. In contrast, the number of FFRPs of P. aeruginosa, i.e., eight, is the largest among eubacteria so far examined, strongly suggesting involvement of these proteins in the efficient transcription regulatory mechanism of P. aeruginosa. So far, no evidence has been found to prove direct involvement of FFRPs in multi-drug resistance or opportunistic infectivity of the organism. Even so, FFRPs will regulate the metabolism of P. aeruginosa as does that of E. coli, and thus, regardless of the detailed function of FFRPs, FFRPs are potential targets for designing drugs that can terminate growth of P. aeruginosa or eradicate this organism.

[Nonpatent Document 1]

• Calvo, J. M., and Matthews, R. G., 1994, Microb. Rev., 58, pp. 466-490

[Nonpatent Document 2]

• Stover, C. K. et al., 2000, Nature, 401, pp. 959-964

[Nonpatent Document 3]

• Koike, H. et al., 2003, Proc. Japan. Acad., 79B, pp. 63-69

[Problems to be Solved by the Invention]

An object of the present invention is to identify the FFRPs which are potential targets while screening for antimicrobial agents and to provide a novel system for developing agents by using the identified target FFRPs, in particular, a novel method for developing agents acting against P. aeruginosa.

[Means for Solving the Problems]

The present inventors have identified eight FFRPs of P. aeruginosa and have completed a multiple alignment (FIG. 1) by comparing the amino acid sequences of the P. aeruginosa FFRPs with those of FFRPs from other bacteria, in particular by analyzing possibilities of these sequences to form a particular set of secondary structural elements. In addition, the present inventors have crystallized an archaeal FFRP (pot1216151) in complex with a ligand, and, by using the 3D coordinates determined thereof, have identified the geometries of the amino acid side chains which will interact with pharmaceutical agents. Based on these findings, the inventors have identified, in the eight FFRPs of P. aeruginosa, the positions and types of amino acid residues with which agents to be developed to act against P. aeruginosa will interact. Furthermore, in order to minimize potential interaction of agents to be developed with E. coli in human body, the phylogenetic relationship of the P. aeruginosa FFRPs with FFRPs of other bacteria has been analyzed thereby identifying FFRPs of P. aeruginosa closely related with E. coli Lrp.

The present invention provides a method of identifying a target protein for its use in screening for an antimicrobial agent, which comprises:

• 1) from the amino acid sequences of all open reading frames identified using the genomic sequence of a target bacterium, selecting amino acid sequences having homologies of 20% or higher to one of feast/famine regulatory proteins (FFRPs) having amino acid sequences set forth in SEQ ID NOS. 9 to 31;
• 2) from the amino acid sequences selected in step 1), excluding any amino acid sequence that does not match with a multiple alignment by forming the same secondary structural elements, the multiple alignment being shown in FIG. 1; and
• 3) identifying a protein, which has an amino acid sequence obtained through steps 1) and 2), as the target protein for its use in the screening for the antimicrobial agent.

The above-described method may further comprise the step of excluding any amino acid sequence phylogenetically related with one of the E. coli FFRPs having amino acid sequences set forth in SEQ ID NOS. 9 to 11, by a bootstrap value of 900/1,000 or higher.

In step 1), amino acid sequences having, for example, FASTA Z scores of 180 or higher to one of FFRPs having amino acid sequences set forth in SEQ ID NOS. 9 to 31 may be selected.

In step 2), for example, any amino acid sequence that is unlikely to form α helices in five regions 34 to 43, 59 to 66, 70 to 82, 126 to 135, and 170 to 180 or β strands in five regions 90 to 96, 109 to 117, 142 to 148, 154 to 160, and 193 to 205 is excluded from the amino acid sequences selected by step 1), wherein these positions are identified using the numbering scheme shown in the multiple alignment in FIG. 1.

The present invention provides also a method of screening for an antimicrobial agent, which comprises the step of selecting a chemical compound as a candidate of the agent, wherein the chemical compound is able to bind specifically to a protein identified by the method described above or to its assembly, thereby altering the three-dimensional structure or the assembly form of the protein.

In an embodiment, the above-described method becomes a method of screening for an antimicrobial agent acting against Pseudomonas aeruginosa, which comprises the step of selecting a chemical compound as a candidate of the antimicrobial agent, wherein said chemical compound is able to bind specifically to a target protein or its assembly, thereby altering the three-dimensional structure or the assembly form of the protein, wherein the target protein is either

• i) a protein having an amino acid sequence set forth in one of SEQ ID NOS. 1 to 8; or
• ii) a protein which is derived from Pseudomonas aeruginosa, related to an amino acid sequence set forth in one of SEQ ID NOS. 1 to 8 by deletion, substitution, or insertion of up to several amino acid residues, and is able to act as an FFRP.

In another embodiment, the above-described method becomes a method of screening for an antimicrobial agent acting against Pseudomonas aeruginosa, which comprises the step of selecting a chemical compound as a candidate of the antimicrobial agent, said chemical compound being able to bind specifically to a target protein having an amino acid sequence set forth in one of SEQ ID NOS. 1 to 8 or its assembly, thereby altering the three-dimensional structure or the assembly form of the target protein.

In yet another embodiment, the method may be a method of screening for an antimicrobial agent acting against Pseudomonas aeruginosa, which comprises the step of selecting a chemical compound as a candidate of the antimicrobial agent, said chemical compound being able to bind specifically to a target protein having an amino acid sequence set forth in one of SEQ ID NOS. 1 to 7 or its assembly, thereby altering the three-dimensional structure or the assembly form of the target protein.

In the screening method of the present invention, for example, the chemical compound may be selected on the basis of interaction between the chemical compound and at least one of thirty-two amino acid residues in the target protein, said thirty-two amino acid residues being found at positions 113, 116, 119, 120, 126, 144, 145, 147, 148, 149, 150, 152, 153, 154, 155, 166, 169, 173, 176, 177, 181, 183, 185, 193, 195, 196, 197, 198, 199, 200, 201, and 202, respectively, wherein these positions are identified using FIG. 1.

Alternatively, the chemical compound is selected on the basis of interaction between the chemical compound and at least one of eighteen amino acid residues in the target protein, said eighteen amino acid residues being found at positions 113, 126, 147, 148, 149, 150, 152, 153, 154, 155, 176, 177, 181, 196, 197, 198, 199, and 202, respectively, wherein these positions are identified using FIG. 1.

Alternatively, the chemical compound is selected on the basis of interaction between the chemical compound and at least one of seven amino acid residues in the target protein, said seven amino acid residues being found at positions 147, 154, 169, 181, 199, 200, and 201, respectively, wherein these positions are identified using FIG. 1.

Alternatively, the chemical compound is selected on the basis of interaction between the chemical compound and at least one of seven amino acid residues in the target protein, said seven amino acid residues being found at positions 147, 149, 154, 169, 173, 200, and 202, respectively, wherein these positions are identified using FIG. 1.

Alternatively, the chemical compound is selected on the basis of interaction between the chemical compound and at least one of twenty-eight amino acid residues in the target protein, said twenty-eight amino acid residues being found at positions 116, 119, 120, 126, 144, 145, 147, 148, 149, 150, 152, 153, 154, 166, 169, 173, 177, 181, 183, 185, 193, 195, 196, 197, 198, 199, 200, and 201, respectively, wherein these positions are identified using FIG. 1.

DESCRIPTION OF THE EMBODIMENTS

The present invention will now be described in detail.

1. Feast/Famine Regulatory Proteins (FFRPs)

In the present invention, the term “FFRPs” refers to proteins that regulate metabolism, growth, and infectivity of bacteria in response to changes in nutritional conditions outside. This term was derived from an expression, “feast/famine regulation”, used to summarize function of E. coli leucine-responsive regulatory protein (Lrp), a protein in this group. It has been identified that E. coli has three FFRPs: Lrp, AsnC, and a third FFRP of unknown function. FFRPs have been found in many other bacteria, such as those belonging to the genus Pyrococcus and the genus Sulfolobus.

FFRPs function by binding to promoter DNA regions positioned upstream of genes regulated by FFRPs, thereby activating or inactivating transcription of these genes. It is believed that association to or dissociation from promoter regions by FFRPs is regulated by the small molecules that reflect the nutritional conditions outside and that these small molecules introduce structural changes to the FFRPs, thereby affecting their abilities to bind to the promoter DNAs. The present invention relates to a method of screening for pharmaceutical agents that bind specifically to FFRPs thereby introducing structural changes, and thus able to regulate metabolism, growth, or infectivity of bacteria. In the present invention the term “antimicrobial agent” refers to “an agent interacting with a bacterium thereby regulating one of metabolism, growth, and infectivity of the bacterium and terminating its growth or eradicating the bacterium”. In particular, the present invention provides a method of screening for agents that can act against P. aeruginosa by targeting the P. aeruginosa FFRPs identified in this application.

2. Method of Identifying Target Proteins (FFRPs)

The present invention provides a method of identifying a target protein for its use in screening for an antimicrobial agent, which comprises the steps of:

• 1) from the amino acid sequences of all open reading frames identified using the genomic sequence of a target bacterium, selecting amino acid sequences having homologies of 20% or higher to one of feast/famine regulatory proteins (FFRPs) having amino acid sequences set forth in SEQ ID NOS. 9 to 31;
• 2) from the amino acid sequences selected in step 1), excluding any amino acid sequence that does not match with a multiple alignment by forming a particular set of secondary structural elements, the multiple alignment being shown in FIG. 1; and
• 3) identifying a protein, which has an amino acid sequence obtained through steps 1) and 2), as the target protein for use in the screening for the antimicrobial agent. 2.1. Homology Search

Step 1 is a step of selecting amino acid sequences homologous to those of known FFRPs by using information obtained from a genomic sequence. This step may be performed using a homology search program, such as BLAST, FASTA, PSI-BLAST, or SSEARCH. The threshold is preferably set to a relatively low level so that no FFRP is overlooked. For example, if FASTA program is used, a low Z score, such as approximately 180, can be used as a threshold.

2.2. Multiple Alignment

Step 2) is a step of excluding amino acid sequences that do not form the same set of secondary structural elements as those formed by known FFRPs by using the multiple alignment (FIG. 1) made by the present inventors.

The multiple alignment shown in FIG. 1 is an improvement of an initial version made using a program such as CLUSTALW, PAM, or MultAlin. In each set of positions equivalent between proteins, the number of positions occupied by the same type of amino acid residues has been maximized. In order to confirm that regions equivalent between different proteins will form the same secondary structural elements and the same 3D structures, the following requirements have been satisfied:

• • 1) inside regions predicted to form a-helices, hydrophobic residues should be best positioned in the same phases;
  • 2) inside regions predicted to form secondary structural elements, amino acid residues that might prevent formation of these elements should best be avoided;
  • 3) neither deletion nor insertion of amino acid residues will be found at the midst of regions predicted to form α helices;
  • 4) proline, glycine, and tryptophan should best occupy the same positions among the FFRPs.

Theoretical identification of proteins is a process of finding, in a genomic sequence, candidate blocks whose sequences resemble a referential amino acid sequence. If a threshold used for judging resemblance is fixed too high, no candidate will be qualified. If the threshold is fixed too low, all the candidates will be qualified. Selecting an appropriate threshold is thus important and this process of fixing the threshold largely depends on experience. In addition, it is also difficult to align more than two amino acid sequences by matching sets of residues with each other. Furthermore, resembling or not resembling between twenty types of amino acid residues depends on the context, i.e., the function expected for the position. For example, arginine and glutamic acid have opposite electron charges, and thus they are different. However, both are hydrophilic and are often positioned on the surface of a protein. Once the arginine side chain is neutralized by electrostatic interactions with another amino acid side chain, the “stem” composed of hydrocarbons will behave in ways similar to the side chains of hydrophobic amino acid residues such as leucine. The multiple alignment such as the one shown in FIG. 1 can be produced only on the basis of an accumulation of experiences and by applying high analytic skills.

Amino acid sequences that do not form the same set of secondary structures shown along the multiple alignment in FIG. 1 are thus excluded. Namely, amino acid sequences that are not expected to form α helices in five regions 34-43, 59-66, 70-82, 126-135, and 170-180, or β strands in five regions 90-96, 109-117, 142-148, 154-160, and 193-205 are excluded.

2.3. Phylogenetic Relation

Various types of similarities are found between proteins. For example, human hemoglobin and porcine hemoglobin have essentially the same function but have differences originated in speciation between humans and swine. Proteins related by such similarity are defined as orthologous to each other. Proteins orthologous to each other are essentially interchangeable. Until recently, porcine insulin was used to treat patients replacing human insulin. During the Second World War, even tuna insulin was used. On the other hand, the similarity found between human hemoglobin and human myoglobin is of a different type. Functions of these proteins have deviated from each other and the proteins are not interchangeable. Proteins related by such similarity are called to be paralogous to each other. The group of FFRPs is a mixture of proteins orthologous or paralogous to each other.

By comparing FFRPs of two or more bacterial species and by screening for chemical compounds acting against FFRPs shared by these species, the method of the present invention can be used in order to develop agents able to act against a desired wide variety of bacteria. Alternatively, by screening for an FFRP present in a particular bacterial species only, pharmaceutical agents specifically acting against the species can be developed. For example, in order to develop an agent not interactive with the human symbiont E. coli, the method of the present invention may include the step of excluding the amino acid sequences that closely resemble the amino acid sequences (SEQ ID NOS. 9 to 11) of E. coli FFRPs.

“Orthologous/paralogous” relationships between FFRPs can be identified by analyzing their phylogeny. Phylogeny can be analyzed by using commercially available software, such as that in the PHYLIP package, while keeping the alignment shown in FIG. 1 unchanged. Preferably, a threshold usable for excluding remote proteins is a bootstrap value of approximately 900/1,000 or higher.

A bootstrap value is a measure for evaluating homogeneity of data from which a conclusion is deduced. Here, this value defines the number of trials in which the same diversification at a node is concluded out of 1,000 trials, while effectively changing a weight given to each amino acid position used for determining similarity. A pair of proteins related by a bootstrap value close to 1,000 are concluded to be phylogenically close.

3. FFRPs from P. aeruginosa

By using the method of the present invention, eight FFRPs were identified as coded in the genome of the standard strain PAO1 of P. aeruginosa (Stover, C. K. et al., 2000, Nature 406, 959-964):

• Ps5047278 (SEQ ID NO. 1), Ps4445486 (SEQ ID NO. 2),
• Ps2472442 (SEQ ID NO. 3), Ps2291589 (SEQ ID NO. 4),
• Ps2220251 (SEQ ID NO. 5), Ps2914358 (SEQ ID NO. 6),
• Ps5372266 (SEQ ID NO. 7), and Ps5977610 (SEQ ID NO. 8).

As has been discussed earlier in this specification, P. aeruginosa easily mutates, thereby acquiring resistance to drugs. Therefore, these FFRPs determined using the genomic sequence of the standard strain PAO1 of P. aeruginosa may also be mutated. The present invention also concerns modified proteins having amino acid sequences mutated from those described above by deletion, substitution, or insertion of up to several amino acid residues, when the modified proteins retain their function as FFRPs.

In order to maintain the original 3D structure, the above-described deletion, substitution, or insertion should not affect formation of the five a helices or five β strands at the regions indicated in FIG. 1. It is preferable that no deletion, substitution, or insertion should occur at amino acid positions that will interact with the pharmaceutical agents, i.e., positions 113, 116, 119, 120, 126, 144, 145, 147, 148, 149, 150, 152, 153, 154, 155, 166, 169, 173, 176, 177, 181, 183, 185, 193, 195, 196, 197, 198, 199, 200, 201, and 202 shown in FIG. 1.

By analyzing phylogeny between FFRPs of P. aeruginosa and E. coli, for reasons it has been confirmed that Ps5977610 is an ortholog of E. coli Lrp, with the bootstrap value being higher than 900. Thus, Ps5977610 (SEQ ID NO. 8) should better not be used as the target for developing pharmaceutical agents to be administered to humans in order to minimize possible effects of the agents on the human symbiont E. coli.

4. Method of Screening for Antimicrobial Agents

A general expectation is that upon transcription regulation by FFRPs small molecules (i.e., ligands) signaling the nutritional conditions outside bind to FFRPS, and change the 3D structure of FFRPs thereby changing the abilities of the FFRPs to bind promoter DNA regions. In other words, a chemical compound able to alter the 3D structure or the assembly form of an FFRP can be used as an antimicrobial agent, which will affect, via modification of transcription regulation by the FFRP, metabolism, growth, or infectivity of the bacterium.

The present invention provides a method of screening for antimicrobial agents, which will bind to a target protein identified by the present invention or its assembly, thereby changing the 3D structure or the assembly form of the target protein, where the target protein and its assembly are the target FFRP and its assembly.

The screening method of the present invention may include either any known ligand-screening system for characterizing changes in the 3D structure or the assembly form of an FFRP upon adding a ligand candidate (e.g., gel filtration, sedimentation coefficient measurement, or the like), or a virtual screening method using a computer.

4.1 3D Structural Information

The structure of an Lrp-like protein (i.e. an FFRP) derived from Pyrococcus furiosus and crystallized in the absence of any ligand and the secondary structural composition of the protein have been reported (Philip M. Leonard, et al., 2001, The EMBO Journal, vol. 20, No. 5, pp. 990-997). With the quality of these data being poor (i.e. an R-factor of approximately 30% or higher at a resolution of approximately 3 Å), the conformations of amino acid side chains, which are important for screening for ligands have not been specified.

The present inventors have succeeded in crystallizing another FFRP (pot1216151) in complex with a ligand, the FFRP being one of the fourteen FFRPs derived from Pyrococcus sp. OT3 (a.k.a. Pyrococcus horikoshii or Pyrococcus shinkaii, Japan Collection of Microorganisms, JCM Registration No. 9974). The 3D structure of the FFRP-ligand complex has been determined at a high resolution using an X-ray diffraction method. To date, this is the single 3D structure of any FFRP determined in complex with a ligand. With the high quality, i.e., R-factor of 21% at a resolution of 1.8 Å, this is the single structure of any FFRP where the accurate positions of amino acid side chains interacting with a ligand are determined.

Table 1 shows the 3D coordinates of pot1216151 determined by the present inventors. These 3D coordinates, or a graphical representation or numerical information derived from the 3D coordinates can provide the 3D structural information necessary for searching for a ligand able to interact with an FFRP. Such 3D structural information includes information concerning both the monomer and its assembly, and also information concerning both the protein alone and the protein in complex with the ligand.

In the present invention, the information, in particular, concerning “the gaps” or “the hole” formed upon assembling of FFRP molecules is useful. Here, “gap” refers to an empty space created between a pair of FFRP monomers, between their atoms, or between their amino acid residues, and “hole” refers to a larger empty space formed at around the center of the assembly. Such information is important for characterizing binding to FFRPs of ligands to be screened.

By using the sequence alignment shown in FIG. 1, the 3D information obtained from Table 1 becomes applicable to other FFRPs. In particular, information concerning amino acid residues facing the “hole” or the “gaps” in the assembly, which are ligand-binding positions, is provided. In this way, the present inventors have specified thirty-two positions of bacterial FFRPs, these positions being potential targets of pharmaceutical agents: 113, 116, 119, 120, 126, 144, 145, 147, 148, 149, 150, 152, 153, 154, 155, 166, 169, 173, 176, 177, 181, 183, 185, 193, 195, 196, 197, 198, 199, 200, 201 and 202 (FIG. 3), wherein these positions are identified using FIG. 1.

Of the above-described positions, the following eighteen positions (FIG. 6) are the positions, in pot1216151, identified as interacting with two molecules of an unidentified assembly promotion factor: 113, 126, 147, 148, 149, 150, 152, 153, 154, 155, 176, 177, 181, 196, 197, 198, 199, and 202 shown in FIG. 1.

The following seven positions (FIG. 7) are the positions, in E. coli Lrp, identified to potentially interact with leucine: 147, 154, 169, 181, 199, 200, and 201 of FIG. 1.

The following seven positions (FIG. 9) are the positions, in pot1216151, identified to potentially interact with leucine: 147, 149, 154, 169, 173, 200, and 202 of FIG. 1.

The following twenty-eight positions (FIG. 12) are the positions, in pot1216151, identified as facing the “gaps”: 116, 119, 120, 126, 144, 145, 147, 148, 149, 150, 152, 153, 154, 166, 169, 173, 177, 181, 183, 185, 193, 195, 196, 197, 198, 199, 200, and 201 of FIG. 1.

4.2. Virtual Screening and Drug Designing

In the present invention, agents can be virtually screened by using the original 3D atomic coordinates determined as above or coordinates derived therefrom.

Upon the virtual screening, the 3D atomic coordinates shown in Table 1 are input to a computer thereby obtaining graphic representation or any type of numerical information. All the coordinates shown in Table 1 or any necessary part may be input, such as the part defining the “hole” or the “gaps”, or the part defining the five α helices and the five β helices. Examples of a program usable for analyzing the 3D structure include those collected in CCP4 package, and program O, X-plor, MolScript, Insight II, and Grasp. Examples of “graphic representation” include any forms to produce visual information such as ribbon diagrams, 3D models, or types of computer graphics. Examples of “numerical information” include any information composed of numbers, such as diameters of crystals and widths and depths of the hole and the gaps.

The information obtained as above is input to a virtual library of chemical compounds in order to search for compounds that are candidates of the pharmaceutical agents. Examples of the virtual library include, but are not limited to, those commercially available. For example, screening software such as DOCK-4 (Kunts), and a 3D structural database such as MDDR (Prous Science) can be used.

The graphic representation or the numerical information described above can be used not only for screening for candidates of pharmaceutical agents but also for modeling or designing of agents using computers. Modeling may be performed using software such as FRODO or O, designed for analyzing crystal structure, and designing may be performed using QUANTA, InsightII, or the like. For, example, a ligand able to fit into the hole or the gap can be designed by using software for molecular designing, such as QUANTA, by consulting with a computer graphics made using the atomic coordinates of the FFRP.

EXAMPLES

Although the present invention will now be described in detail by way of EXAMPLES and REFERENCE EXAMPLES, the present invention is not limited to these examples.

Example 1

Identification of P. aeruginosa FFRPs

All open reading frames (ORFs, each formally codes for 50 or more amino acid residues between the start and stop codons) found in the complete genomic sequence (Stover, C. K. et al., 2000, Nature 406, 959-964) of the standard strain (PAO1) of P. aeruginosa were identified and translated to amino acid sequences. ORFs of P. aeruginosa resembling the FFRPs of E. coli (genomic sequence of E. coli K strain: Blattner, F. R. et al., 1977, Science, 277, 1453-1474), or FFRPs of archaea, Pyrococcus sp. OT3 (JCM 9974) or Thermoplasma volcanium (these FFRPs listed in Suzuki, M et al., 2003, Proc. Japan Acad. 79B, pp. 92-98), were identified using the FASTA program (Peason, W. R., and Lipman, D. L., 1988, Proc. Natl. Acad. Sci. USA, 85, 2444-2448). A low Z score of approximately 180 was used as the threshold so that no FFRP was overlooked.

The amino acid sequences of the candidates of P. aeruginosa FFRPs identified as above and the amino acid sequences of FFRPs of the other bacteria were analyzed using the CLUSTALW program collected in the PHYLIP package (Thompson J. D. et al., 1994, Nucl. Acids Res., 22, 4673-4680), and a multiple alignment was made by correlating residues between different sequences with each other.

Two types of major improvements were made to this alignment. First, in each set of positions identified to be identical as many as possible should be occupied by the single type of amino acid residue (highlighted in bold at positions outside the α helices in FIG. 1). Second, identical regions in different FFRPs should form the same types of secondary structural elements (e.g., an α helix), so that these secondary structural elements formed in the same order will form essentially the same 3D structure. A program such as CLUSTALW is not usable for the latter type of improvement.

Importantly, it has been confirmed that inside the regions predicted to fold into α-helices, hydrophobic residues should be positioned by forming particular phasings: in an α helix, every 3.6 amino acid residues will face the same side, and thus hydrophobic residues arranged with this periodicity will stabilize a protein domain by interacting with other secondary structural elements. Also, amino acid residues that would prevent formation of particular types of second structural elements were best avoided from regions identified to form such elements. Deletion or insertion of amino acid residues was best avoided at the midst of the regions predicted to form secondary structural elements. The alignment was improved so that residues stereochemically atypical, such as proline, glycine, and tryptophan, were best occupying the same positions among the FFRPs.

Consequently, eight FFRPs of P. aeruginosa were identified, and a multiple alignment correlating their amino acid residues to those of FFRPs of other bacteria was finalized (FIG. 1).

Example 2

Identification of the Phylogenetic Relation Between FFRPs

Without changing the correlation between residues in the multiple alignment in FIG. 1 and by using the PHYLIP package, FIG. 2 was made showing similarities between FFRPs. In FIG. 2, two FFRPs related more closely are separated by a shorter distance, this distance being defined as the sum of partial distances measured from the node separating the two FFRPs to the respective FFRPS. For example, the protein related closest to E. coli Lrp is Ps5977610 from P. aeruginosa.

A bootstrap value was calculated for each node in FIG. 2. A bootstrap value is a measure for evaluating degree of homogeneity of data used to deduce a conclusion: a conclusion needs to be unbiased, supported by essentially the whole of the data set. This value defines the number of times the same diversification at a node is concluded out of, for example, 1,000 trials, while effectively changing the weight given to each of the amino acid positions used for the analysis. In extreme cases, some positions might be excluded from the analysis or only several positions might be selected. Phylogenetic relation indicated by a node in a model is more accurate when the bootstrap value approaches 1,000.

Bootstrap values calculated to nodes inside regions including the eight FFRPs of P. aeruginosa (highlighted red or blue in FIG. 2) were generally high, indicating higher reliability of the phylogenetic relations determined between these proteins. In particular, the bootstrap value calculated to the node separating E. coli Lrp and Ps5977610 was higher than 900/1,000, and the orthologous relationship between the two proteins was unambiguous. The closest to Ec0468065 of E. coli was Ps2220251 of P. aeruginosa, but the bootstrap value calculated to the node relating the two was not very high (FIG. 2). No P. aeruginosa FFRP was found resembling E. coli AsnC.

Example 3

Identification of Ligand-Binding Site

By using correlation of amino acid sequences between P. aeruginosa FFRPs and pot1216151 shown in FIG. 1 and by using findings obtained by analyzing the crystal coordinates of the archaeal FFRP, pot1216151 (see REFERENCE EXAMPLES and Patent Application No. 2001-384683), in total thirty-two amino acid positions were identified for each of the FFRPs from bacterial species as potential targets while developing a pharmaceutical agent (FIG. 3). The crystal structure of pot1216151 used for this identification is the only 3D structure of any FFRP determined to date in complex with a ligand. It is the single FFRP structure where the positions of the side chains of amino acid residues are determined precisely. The identification of these positions was carried out by four different approaches described below.

• i) In the crystal of pot1216151, each octamer was found in complex with two molecules of an unidentified assembly promotion factor (i.e., a ligand), this ligand having being absorbed from E. coli cells upon expression of the protein (see REFERENCE EXAMPLES and Patent Application No. 2001-384683). Related by a crystallographic symmetry, the two ligand molecules are binding to identical sites in the pot1216151 assembly (FIG. 4). The size of the ligand was similar to that of a medium amino acid, e.g., valine: a valine molecule was modeled by filling the electron density of each ligand molecule (FIG. 5). Eighteen amino acid residues whose at least one non-hydrogen atom was positioned within 6 Å from the modeled valine, when measured from carbon, oxygen, or nitrogen atoms in the valine (FIG. 6). It has been concluded that in general in FFRPs, the eighteen positions, i.e., 113, 126, 147, 148, 149, 150, 152, 153, 154, 155, 176, 177, 181, 196, 197, 198, 199, and 202, have potentials to interact with ligands, wherein these positions are identified using FIG. 1.
  • ii) Molecular genetic experiments using E. coli Lrp have shown that leucine-dependence of transcription regulation by Lrp was affected by mutation at each of seven positions (Platko, J. V., and Calvo, J. M., 1993, J. Bacteriol., 175, 1110-1117). These seven positions, in E. coli Lrp, are candidates which possibly interact with leucine. With the 3D structure of E. coli Lrp being unknown, residues of pot1216151, identified as occupying the equivalent positions (147, 154, 169, 181, 199, 200, and 201 in FIG. 1) were found surrounding the gap formed in the FFRP assembly (FIGS. 7 and 8). Among the seven residues of pot1216151, the side chain of Met (199) only was found facing away from the gap, facing into the protein domain, although its position was close to the gap. Of the remaining six residues, the main chain carboxyl group of Ala (201) and the side chains of Val (147), Asp (154), Leu (169), Arg (181), and Ile (200) were found facing the gap. It was concluded that with these seven positions generally in FFRPs, ligands interact potentially.
• iii) Leucine interacts not only with E. coli Lrp (Marasco, R. et al., 1994, J. Bacteriol., 176, 5197-5201) but also with pot1216151 (REFERENCE EXAMPLES and Patent Application No. 2001-384683), thereby disassembling these FFRPs. Up to two molecules of leucine binds to E. coli Lrp per gap (Marasco, R. et al., 1994, J. Bacteriol., 176, 5197-5201) formed between a pair of dimers. In order to analyze possible stereochemical changes induced upon interaction between leucine and pot1216151, two leucine molecules were modeled using a computer and added to the crystal structure of pot1216151 by fitting into the gaps formed between a pair of dimers. Each leucine molecule was modeled near the seven residues described above. As shown in FIG. 9, the two gaps are related by a pseudo two-fold symmetry, each gap potentially interacting with one molecule of leucine. Here, only one leucine molecule is shown in FIG. 9, by fitting into the lower gap. FIG. 9 is a view of the complex when looked through the direction indicated by the arrow in FIG. 10, showing only the two dimers closest to the arrow. The side chain of the leucine molecule was modeled extending from the vicinity of Val (147) through Leu (169) towards Ile (200), so that hydrophobic interactions will be formed. The amido group of leucine was modeled approaching Asp (154) of pot1216151, while the amido group of leucine approached Val (147), both forming chemical bonds. The overall complementality between the leucine molecule and the gap was found ideal; however the leucine molecule was positioned too close to Tyr (149), Asp (173), and Ile (202) of pot1216151, creating van der Waals conflicts. Thus, this complex will not be stable, but might dynamically change. At the five positions from which interactions were made without a conflict, E. coli Lrp and pot1216151 share the same or similar amino acid residues (FIG. 11). It was thus concluded that ligands potentially bind to the seven positions of FFRPs in general.
• iv) Using the 3D structure of pot1216151, twenty-eight amino acid positions were identified as forming the gaps between dimers. Equivalent positions in FFRPs in general are candidates potentially interacting with ligands. Namely, amino acid residues were identified as forming gaps when they were inaccessible by a probe of the radius 5.0 Å moving by contacting the surface of the assembly, but at least partially accessible by another probe of the radius 1.4 Å, when this accessible area was 5% or larger of the area exposed when the same type of amino acid residue was fully stretched between a pair of glycine residues. In the crystal structure, four gaps were formed unrelated by any crystallographic symmetry, and twenty-eight residues were identified as forming two or more of the four gaps (FIG. 12). These residues are found at 116, 119, 120, 126, 144, 145, 147, 148, 149, 150, 152, 153, 154, 166, 169, 173, 177, 181, 183, 185, 193, 195, 196, 197, 198, 199, 200, and 201 shown where these positions are identified using FIG. 1.

As the sum of identifications i) to iv), thirty-two positions are listed in FIG. 3. These positions are interpretable as forming two ligand-binding sites partially overlapping onto each other (*Typographical error existed here, noted by the translator). Of the positions listed in FIG. 3, when ten positions, 116, 119, 120, 144, 145, 166, 183, 185, 193, and 195, identified only in iv) but not in i)-iii) were removed, twenty-two positions shown in FIG. 13 remained. Of these, the E. coli unidentified assembly promotion factor binds around positions identified in i) only, or in both i) and iv), i.e., twelve positions on the left in FIG. 13. While, the disassembling factor, leucine, binds around four positions on the right in FIG. 13, identified in iv) and one or both of ii) and iii). At around the six positions in between, the two types of ligands might compete with each other for binding.

Example 4

Further Specifying Target P. aeruginosa FFRPs in Order to Prevent Possible Interaction of Pharmaceutical Agents to be Developed with E. coli

E. coli Lrp and P. aeruginosa Ps5977610 have very similar amino acid residues at positions important for interaction with ligands. The two amino acid sequences shown in FIG. 1 are similar to each other as a whole. These facts suggest that the two proteins are regulated in the same way by the same ligands including leucine. None of the P. aeruginosa FFRPs was found to be resembling E. coli AsnC. The protein most resembling E. coli Ec0468065 was Ps2225251, but the similarity between the two was not high. Of the other six P. aeruginosa FFRPs, Ps2914358 and Ps5372266 were found to be differentiated from all the three FFRPs of E. coli.

It has been discussed that, of the three a helices formed inside the N-terminal domain of an FFRP, the third helix is important for recognizing DNA bases, but that three positions of the third helix are unable to recognize DNA, since they are often occupied by hydrophobic residues, facing into the protein domain (Suzuki, M., et al., 2003, Proc. Japan Acad. 79B, 92-98). Based on the multiple alignment shown in FIG. 1, amino acid residues forming the third α helix of each P. aeruginosa FFRP were identified, and twelve positions potentially recognizing DNA bases were identified (FIG. 14). At these positions E. coli Lrp and P. aeruginosa Ps5977610 had very similar amino acid residues, suggesting that both will recognize the same DNA sequence. Ec0468065 and Ps2225251 were found sharing the same residues at four positions out of the twelve positions. Among the FFRPs of P. aeruginosa, Ps2914358 and Ps5372266 have differentiated farthest from the three E. coli FFRPs. No P. aeruginosa FFRP was found sharing three or more residues with E. coli AsnC at the same positions. These findings are consistent with the conclusion obtained by analyzing positions possibly interacting with ligands, and also with those drawn by comparing the whole amino acid sequences.

Reference Example 1

Crystallization of an FFRP

(1) Construction of a Vector for Expressing an FFRP

The following primers were synthesized in order to amplify a DNA fragment coding an FFRP (pot1216151) gene by PCR using the genomic DNA of Pyrococcus sp. OT3 (JCM 9974) as the template. PCR was carried out using the reaction solution, 20 μl, LA Tag (Takara Shuzo Co., Ltd.) and GeneAmp PCR system 9600 (Perkin Elmer): each cycle consisting of denaturation at 94° C., annealing at 55° C., and elongation at 72° C., and repeating this cycle 30 times.

The amplified DNA fragment was cleaved using restriction enzymes NdeI (Takara Shuzo Co., Ltd.) and BamHI (Takara Shuzo Co., Ltd.), and the fragment coding the gene was separated from the rest by electrophoresis using an agarose gel. The DNA fragment coding the FFRP (potl216151) gene was ligated with an expression vector, pET3 (Novagen), cleaved using restriction enzymes, NdeI and BamHI, thereby constructing an expression vector (pET3-LRPS01): 10 μl of the reaction solution, 660 mM Tris-HCl buffer (pH 7.6) containing 66 mM MgCl₂, 100 mM DTT, and 1 mM ATP, was kept at 16° C. overnight, in the presence of T4 DNA ligase (Takara Shuzo Co., Ltd.).

Primers:

(SEQ ID NO: 32)
Forward Strand:
5′-TGGTGATGACATATGGTGACGGCCTTTATCCTG-3′
(SEQ ID NO: 33)
Reverse Strand:
5′-GAACGGATCCATCAAATTGCTATCATAGTCGAGGTC-3′

(2) Expression of an FFRP using E. coli

The vector designed for expressing the FFRP (pot1216151) gene, pET3-LRPS01, was introduced into E. coli cells strain BL21 (DE3) (Novagen). The E. coli cells were cultured in 8 ml of the 2×YT medium containing 50 mg/ml ampicillin at 37° C. overnight, inoculated into 8 l of the same medium, and allowed to grow until the absorbance of the medium reached approximately 0.75 at 600 nm. Subsequently, 2 mM isopropylthiogalactoside (IPTG) was added to induce expression of the FFRP. After additional culture for 4 hours, cells were collected by centrifugation at 7,500 rpm for 5 minutes using a centrifuge (Beckman Avanti J-25).

(3) Purification of an FFRP (pot1216151)

The cells expressing the FFRP (pot1216151) were suspended into 250 ml of a 100 mM Tris-HCl buffer (pH 7.0) containing 1 mM EDTA, and treated using a French press (SLM). After centrifugation for 30 minutes at 4° C. at 25,000 rpm using a centrifuge (Beckman Avanti J-25) and a rotor (JA-25.5), the supernatant was collected and heated at 75° C. for 1 hour. After another centrifugation at 4° C. at 25,000 rpm for 30 minutes, the supernatant was dialyzed against a 30 mM Tris-HCl buffer (pH 7.0), and subjected to further purification: by twice repeating the following process, i.e., anion exchange column chromatography followed by gel filtration.

The supernatant was applied to an anion exchanger (1.6×18 cm, Resource Q, Pharmacia), in a column, equilibrated with 30 mM Tris-HCl buffer (pH 7.0), and the column was washed with the same buffer. Subsequently, the protein was eluted with a linear gradient, 0-2 M of NaCl in the buffer, with a flow rate of 2 ml/min, using FPLC column (Pharmacia). The solution eluted from the column was fractionated into fractions of 4 ml. By SDS electrophoresis, fractions containing the FFRP were identified and stored.

The stored protein solution was dialyzed against 100 mM Tris-HCl (pH 7.0) and subjected to gel filtration. The protein solution was applied to a gel column (2.6×60 cm, Superdex 75, Pharmacia) equilibrated with a 100 mM Tris-HCl buffer (pH 7.0), and eluted with the same buffer at a flow rate of 1 ml/min using the FPLC system (Pharmacia). The fractions obtained (2 ml each) were subjected to SDS electrophoresis, and those containing the FFRP were identified and stored. The above processes of anion exchange chromatography and gel filtration were alternately carried out two times to purify the FFRP until a single band was observed in an electrophoretogram.

(4) Crystallization of the FFRP (pot1216151)

The purified FFRP, 20 mg/ml, was dissolved in a 10 mM Tris-HCl buffer (pH 7.0) to prepare a sample for crystallization. The sample was crystallized on a 24-well crystallization plate (Hampton Research) by a vapor-diffusion method using a sitting-drop technique. Specifically, using a mixture of 4 μl of the sample and 4 μl of a reservoir solution (100 mM citrate buffer (pH 4.0) containing 10% by weight of PEG 6000 and 1.0 M lithium chloride) as the mother solution, the sample was allowed to be equilibrated with 0.8 ml of the reservoir solution by vapor diffusion at a constant temperature of 5° C. In approximately a week, six-sided pyramid crystals of about 0.2 mm were obtained.

Reference Example 2

Analysis of the 3D Structure of the FFRP

(1) X-Ray Diffraction Analysis

In order to determine the 3D structure by a heavy atom isomorphous replacement method, the FFRP (pot1216151) crystal obtained in REFERENCE EXAMPLE 1 was soaked in a preservative solution containing 10 mM platinocyanide (K₂[Pt(CN)₆]) or 0.1 mM gold chloride (K[AuCl₄]) at 5° C. for about 2 days.

Four sets i.e., two sets of FFRP original crystals and two sets of derivatives respectively derived from two heavy atoms (platinum and gold), were measured using two X-ray source: 1) a laboratory rotating anode X-ray source, and 2) a synchrotron radiation X-ray source.

1) Analysis Using a Laboratory Rotating Anode X-Ray Source

A set of original crystals of the FFRP (pot1216151) and two sets of derivatives from two heavy atoms (platinum and gold) were analyzed at room temperature by using the laboratory rotating anode X-ray source. Each set was placed in a quartz capillary (1.5 mm in diameter, produced by TOHO Co., Ltd.), and an excessive solution was removed. After both ends of the capillary were sealed with wax, the capillary was set in an X-ray diffractometer. The X-ray source (UltraX 18 produced by Rigaku Industrial Corporation) was operated with 50 kV and 100 mA, and diffraction data was recorded with a diffraction device (R-AXIS IV produced by Rigaku Industrial Corporation).

2) Analysis Using A Synchrotron Radiation X-Ray Source

In order to obtain data at a higher resolution, the original FFRP (pot1216151) crystal was measured in a frozen state by using the synchrotron radiation X-ray source. The synchrotron radiation X-ray source used was Hyogo-ken Beam Line BL24XU of photon factory SPring8. The crystal was immersed in a cryopreservation solution [20% (by weight) glycerol, 14% (by weight) PEG 6000, 1.0 M lithium chloride, and a 100 mM citrate buffer (pH 4.0)] for several minutes, mounted on a 0.2-mm mount loop (Cryoloop, produced by Hampton Research Corporation) for cryopreservation, and was frozen in liquid nitrogen (−196° C.). During the analysis, the temperature of the crystal was kept at −173° C. using a device designed to spray cold air to crystals (produced by Rigaku Industrial Co., Ltd.). Diffraction was recorded by a diffractometer (R-AXIS IV produced by Rigaku Industrial Co., Ltd.) using a synchrotron radiation X-ray having a wavelength of 0.834 Å.

(2) Data Analysis

The recorded diffraction was processed using a program designed for the diffractometer and the programs in the CCP4 package (Collaborative Computational Project, Number 4, Acta Crystallographica D50, 760-763, 1994). The space group of the crystals was identified as belonging to a space group P3₂21 or P3₁21, and the unit cell lengths were identified: a=b=96.3 Å, and c=97.1 Å. Based on these lengths, it was concluded that each asymmetric unit of these crystals contained three to six molecules of the FFRP.

(3) Building an Initial Model

The diffractions from the FFRP pot1216151 and the two heavy atom (platinum and gold) derivatives were integrated using programs in the CCP4 package, and used for the subsequent computational analysis. Positions of the heavy atoms in the derivatives were determined using difference Patterson maps. The gold and platinum derivatives, respectively, had two and three heavy metal atoms per asymmetric units. Numbers, positions, and occupancies of the heavy atoms were refined using the MLPHARE program in the CCP4 package. The overall figure of merit at this stage was calculated as 0.43 at 3.0 Å.

By using the phase obtained as above and by using the isomorphous replacement method, an electron density map was calculated. By examining the map, the phase was improved by the methods of solvent flattening and histogram matching, using the DM program in the CCP4 package. In the revised electron density map calculated using the improved phase, electron densities corresponding to right-handed α-helices were identified appropriately only when four molecules of the protein were assumed in each asymmetric unit and when these units were related by the space group P3₂21. A model was made by assembling four monomers (each consisting of 72 alanine residues), so that the model would best fit to the electron density map using program O (Jones T. A., Zou J. Y., Cowan S. W., and Kjeldgaard M., Improved methods for binding protein models in electron density maps and the location of errors in these models, Acta Crystallographica A47, 110-119, 1991).

(4) Refinement of the Model

The initial model was refined using the X-PLORE program (Brünger, A. X-PLORE v3.1 Manual (Yale University, New Haven, 1992)), so that the model would best satisfy both the diffraction data experimentally obtained and the standard geometric parameters (Engh and Huber) that were expected for protein 3D structures in general. The model was further refined using program O to correct the part of the model where large deviations from the electron density map were observed. Until this stage, the four monomers in the asymmetric unit were kept identical to each other. The R factor indicating the difference between the experimental data and the model was 39.1% at this stage.

In order to further refine the model, the high-resolution data obtained at SPring8 BL24XU were used. The aforementioned alanine model was refined using the X-PLORE program using data up to 3.0 Å, and other data up to 2.0 Å were incorporated while improving the phase using the wARP program (Perrakis, A., Sixma, T. K., Wilson, K. S., and Lamzin, V. S., wARP: Improvement and extension of crystallographic phases by weighted averaging multiple refined dummy atomic models, Acta Crystallographica D53, 448-455, 1997). Using the improved phase, a new electron density map was calculated, where electron densities of most of the atoms in the protein, including the atoms of side chains of the amino acid residues, were clearly identified. Based on this electron density map, another 3D structural model was made by including the amino acid side chains of the FFRP (pot1216151).

Further refinements were carried out at a resolution of 1.8 Å, by modeling solvent molecules so that there would match with electron densities that were clearly identified but not interpretable as any atoms in the protein, which will be discussed further in the following paragraph. At the final stage of refinement, the four monomers in the asymmetric unit were allowed to adopt non-identical 3D structures.

(5) Determination of the Final Model

The final model (FIG. 8) was assembled by four independent monomers of the FFRP (pot1216151). Each monomer comprises all the residues except for the first amino acid residue, i.e., methionine, at the N-terminal end. The R factor, evaluating the consistency between the experimental data (20-1.8 Å) and the final model, was calculated as 21.2%, indicating a high accuracy of the 3D model. The PROCHECK program in the CCP4 package was used to calculate a Ramachandran plot. In the plot, 98.5% of all the residues were found in energetically most stable regions. The average temperature factor (B-factor) was as small as 17.3, indicating that all the atoms were determined unambiguously, except for some side chains, which were positioned on the surface, and thus expected as possessing real flexibilities for movements.

Reference Example 3

Analysis of the FFRP by Gel Filtration

It has been reported that many FFRPs derived from microorganisms, including E. coli, form dimers or tetramers in solution. The FFRP expressed in E. coli was analyzed by gel filtration in order to estimate sizes of its assemblies in solution.

Specifically, the FFRP pot1216151 purified for the crystallization was diluted with a 50 mM Tris-HCl buffer (pH 7.0) containing 300 mM sodium chloride, yielding a concentration of approximately 100 μM. Gel filtration was carried out at a flow rate 1 ml/min (LC Module I plus System, Waters) using a matrix (Protein Pak 125, 7.8×300 mm, Waters) and the same buffer. Retention of the protein was recorded by measuring the UV absorption at 220 nm.

A multiple number of peaks were observed (FIG. 16, purification 1). In general upon gel filtration, assemblies of larger sizes will be retained for a shorter time. Accordingly, the first peak (peak 1 in FIG. 16) might correspond to an octamer, and other peaks retained longer should correspond to smaller assemblies. This protein forms a variety of assemblies up to an octamer depending on the condition. The function of the octamer may be different from those of smaller assemblies.

Example 4

Analysis of the 3D Coordinates of Atoms in the FFRP pot1216151

(1) The 3D Coordinates of Atoms in the FFRP

The atomic coordinates of the 3D structure of the FFRP pot1216151 determined are shown using the protein data bank (PDB) format (Table 1), describing the four independent monomers of the protein (A to D) in the asymmetric unit and 196 water molecules. Lines 1 to 7 of Table 1 specify the crystal symmetry to repeat the asymmetric unit, as is generally the case of any crystals. From line 8, eleven parameters (i)-(xi) described from left to right are: (i) serial numbers of the atoms (1 to 2,556); (ii) types of atoms, e.g., C, the carbon, further differentiated as, for example, CA, CB, indicating the positions inside the amino acid residues, also including information concerning chemical bonding; (iii) assignments of the atoms to 20 types of amino acid residues, using the 3 letter code, e.g., VAL for valine and HOH for the atoms belonging not to amino acid residues but to water molecules, and, in addition, their assignments to the four monomers (A to D) or to water molecule (W); (iv) amino acid residue numbers counted from the N terminus in each monomer, or numbers 1 to 196 for the water molecules; (v) the X coordinates in angstrom; (vi) the Y coordinates in angstrom; (vii) the Z coordinates in angstrom; (viii) occupancies (i.e., probabilities of the atoms occupying the given coordinates); (ix) isotropic temperature factors (i.e., measures of the flexibilities of atoms for thermal movements); (x) the atomic numbers defined by the periodic table (e.g., 6 for C, 7 for N, and 8 for 0); and (xi) types of the atoms, the same as in (ii) (e.g., C, O, and N).

The atoms are named according to the IUPAC-IUB nomenclature; however, in (ii), A, B, C, D, E, Z, and H were used (e.g., CA or CB) instead of α, β, γ, δ, ε, ζ, and η. The additional oxygen atoms present at the C termini were labeled as OXT (OT).

(2) Analysis of the 3D Coordinates

1) Formation of Assemblies of the FFRP pot1216151

By analyzing the data shown in Table 1, it was found that each monomer of the FFRP is composed of a four-stranded β sheet and two α-helices (FIG. 15). Each pair of monomers assembled into a dimer, by forming a single β-strand composed of eight strands, i.e., four strands from each monomer (FIG. 15). In the crystal, four such dimers further assembled to form a disk-like octamer (FIG. 3). The diameter of the octamer disk was approximately 60 Å and the thickness thereof was approximately 40 Å.

2) Characteristics of the 3D Structure of the FFRP pot1216151

In the central region of the disk-like octamer of the FFRP pot1216151, there exists a hole, the overall shape resembling a Japanese 50-yen coin. Four gaps, each formed between a pair of dimers, extend from this hole, thereby forming a space having a cross-like shape (FIG. 8). The shape of this space, and types and coordinates of amino acid side chains surrounding this space are the 3D structural information important for screening for ligands interacting with the FFPR.

The hole in the central region resembled a cylinder having a diameter of approximately 12 Å and a height of approximately 30 Å. The hole was large enough to accommodate two amino acid molecules. Eight sets of amino acid side chains respectively from eight FFRPs in the assembly, valine 9, glutamic acid 37, tyrosine 38, methionine 68, and serine 70, face this hole (here numbers, such as 9, 37, or 38, are those of amino acid residues, counted from the N terminus in each FFRP monomer (see Table 1). Also, residues 37, 38, and 68 are positioned on the border between the hole and the gaps.

Each of the four gaps formed between the pairs of the dimers is large enough to accommodate two amino acids, or able to do so by being expanded by the two amino acids. Each gap was surrounded by two sets of side chains of the two dimers, glutamic acid 15, valine 33, tyrosine 35, aspartic acid 39, leucine 49, aspartic acid 53, isoleucine 56, threonine 57, arginine 61, threonines 69 and 71, and isoleucines 73 and 75.

3) Application of the 3D Information to Screening for Ligands

If a ligand binds to the space extending from the hole to the gaps and if the ligand is completely complementary to part of the space and thus able to fit into, the ligand will stabilize the octamer thereby activating the functions of the FFRP as an octamer. However, if the ligand is larger than the space and binds there with a high constant, it will enlarge the space, thereby dissociating the octamer, terminating the functions of the FFRP as an octamer, and activating functions as smaller assemblies. Most likely, this space is where interaction with natural ligands will occur.

As has been described, graphical and/or numerical information of the FFRP obtained from the 3D coordinates shown in Table 1 defines the space extending from the hole to the gaps and specify the positions of atomic groups, hydrophobic or hydrophilic, facing the space. Thus, this information provides a useful platform for screening for ligands interacting with the FFRP.

Reference Example 5

The Position of a Natural Ligand Present in the Crystal of FFRP

(1) The Presence of a Natural Ligand in the Crystal of the FFRP pot1216151

The presence of a natural ligand in the crystal obtained in REFERENCE EXAMPLE 1 was confirmed as described below.

1) Purification of the FFRP (pot1216151) using a Method Different from what was Described in REFERENCE EXAMPLE 1

The protein was purified by a more rigorous method with additional uses of ammonium sulfate fractionation and hydrophobic column chromatography. Ammonium sulfate fractionation was carried out after the heat treatment and centrifugation. Namely, ammonium sulfate was added to the supernatant, yielding 40% saturation. The solution was centrifuged at 4° C. at 18,000 rpm for 15 minutes. Ammonium sulfate was further added to the supernatant, yielding 80% saturation. After the centrifugation at 4° C. at 18,000 rpm for 15 minutes, the sediment was dissolved in 30 ml of a 30 mM Tris-HCl buffer (pH 7.0) and dialyzed against a 30 mM Tris-HCl buffer (pH 7.0). Hydrophobic column chromatography was carried out after the anion exchange column chromatography and the gel filtration described in REFERENCE EXAMPLE 1. Namely, after the gel filtration, ammonium sulfate was added to the protein solution, yielding a concentration of 1.6 M, and applied to a column (1.6×18 cm), containing Butyl-Toyopearl 650 M (Tosoh) pre-equilibrated with 50 mM Tris-HCl buffer (pH 7.0) containing 1.5 M ammonium sulfate. The column was washed with the same buffer. Subsequently, the protein was eluted using a line, 1.5-0 M, gradient of ammonium sulfate in the buffer with a flow rate 2 ml/min: the FPLC column (Pharmacia) was used. Fractions, 4 ml each, were subjected to SDS electrophoresis and those identified as containing the FFRP were stored.

2) Changes Between Assembly Forms

Changes in apparent molecular weight of the FFRP (pot1216151) in the solution, i.e., changes in the assembly form, were confirmed (FIG. 16, purification 2) by electrophoresis. Compared with the method employed in REFERENCE EXAMPLE 1, in this method, the protein is exposed to the environments accelerating, in general, denaturation of proteins. This suggests that the ligand, which has been derived from E. coli and stabilized the assembly of the FFRP, dissociated from the FFRP after the rigorous purification, thereby failing to form an octamer. The analysis thus suggests that a natural ligand that stabilizes the assembly of the FFRP exists in the cells of E. coli and that the crystal obtained in REFERENCE EXAMPLE 1 was in complex with this natural ligand.

(2) The Position of the Natural Ligand in the Crystal of FFRP (pot1216151)

The final model showing the 3D structure of the FFRP (pot1216151) was re-examined to analyze non-protein regions (the regions interpreted to correspond with 196 water molecules) in further detail. Electron densities which likely possibly correspond to two molecules of the ligand were identified at two positions inside the gaps formed between the dimers (FIG. 4).

As has been discussed, what can be determined experimentally by X-ray diffraction analysis is an electron density map, and the 3D coordinates obtained best fitting the map are still a model. While a large number of water molecules are generally contained in crystals, it is extremely difficult to identify molecules as small as water in an electron density map. Of the atoms constituting a water molecule, the two hydrogen atoms diffract X-rays very poorly, and thus, in short, they are invisible by X-ray analysis. Consequently, in order to identity a water molecule, a point-like density of the oxygen atom isolated from any other density needs to be identified in the electron density map. In the present model, densities identified as corresponding to molecules other than FFRP molecules are first assumed as derived from 196 water molecules, i.e., 196 oxygen atoms in particular. If a natural ligand originated in E. coli cells is present in the crystal, one of such electron densities should correspond to that of the natural ligand.

In order to identify the electron density of the ligand, water molecules modeled to relatively low electron densities were removed. Of these, 66 were found inside the hole at the center of the octamer. This was necessary to remove distortion of the map caused by possible misidentification of these atoms. Starting with this model, the process of 3D structure refinement was repeated several times, and the difference between the model and the electron density map (hereafter referred to as the difference Fourier map) was computed, expecting that a density should emerge, corresponding to the ligand. At each cycle, high densities newly found in the difference Fourier map (at counter levels of three or higher) were examined thoroughly. To these densities, which were isolated or which were close enough to hydrophilic groups in the protein so that ionic/hydrogen bonding was possible, new water molecules were modeled. Finally, an electron density larger than that expected for a water molecule, was identified in each asymmetric unit. Since an octamer is composed of two such asymmetric units two such densities were found in the octamer (FIG. 4). These two densities were interpreted as those of two molecules of the ligand, each positioned inside the gap formed between a pair of dimers. Each electron density has a size equivalent with four or more water molecules, or equivalent with a single molecule of a medium sized amino acid such as valine or isoleucine.

Example 6

Interaction Between the FFRP and Natural Ligands in Solution

It has been confirmed that various amino acids and some other biomolecules (e.g., metabolic intermediates) can act as natural ligands on assemblies of the FFRP (pot1216151).

(1) Changes in Crystal Structure by Amino Acids

It has been known that the regularity inside a crystal might be affected, if the structure of the protein changes upon interaction with a ligand which is incorporated from outside the crystal, thereby depolarizing the crystal. Crystals of the FFRP (pot1216151) were soaked into solutions, each containing one of twenty amino acids at the same concentration 10 mM. With isoleucine, valine, methionine, and leucine, the crystals depolarized after several hours. With the other amino acids, no change was observed. It is important to note that the changes caused by the four amino acids to the 3D structure of the protein are not necessarily the same, and that it is possible that the other amino acids, although they showed no effect, had no ability to diffuse into the crystal.

(2) Analysis Using Gel Filtration

Changes in assemblies of the FFRP pot1216151 induced by interaction with amino acids and metabolic intermediates were analyzed in solution using gel filtration.

1) Experimental Procedure

Gel filtration was carried out at a flow rate 1 ml/min, using a matrix (Protein Pak 125, 7.8×300 mm, Waters) and a 50 mM Tris-HCl buffer (pH 7.0) containing 300 mM sodium chloride. Flow of the protein was monitored by measuring the UV absorbance at 220 nm (LC Module I plus system, Waters). The FFRP pot1216151 purified by method 2, i.e., the rigorous method, was dissolved in 50 mM Tris-HCl buffer (pH 7.0) containing 200 mM sodium chloride, and kept at −80° C. until it was diluted by 10-fold with a 50 mM Tris-HCl buffer (pH 7.0) containing 300 mM sodium chloride, and mixed with each potential ligand for at least 30 minutes at room temperature (about 25° C.). In the mixture, the monomer concentration of the FFRP was approximately 100 μM. While, the concentration of each-amino acid was 1 mM and that of 5 metabolic intermediates, i.e., malic acid, 2-oxoglutaric acid, oxaloacetic acid, pyruvic acid, and 3-phosphoglyceric acid, was 10 mM.

2) Results

In the sample containing isoleucine, the second peak increased. In the sample containing valine, the third peak increased (FIG. 17a). In samples containing other six amino acids, i.e., methionine, arginine, leucine, phenylalanine, alanine, and threonine, the fourth peak increased (FIG. 17b). None of the other twelve amino acids showed any significant effect. When one of the three metabolic intermediates, each containing four or more carbon atoms (i.e., malic acid, 2-oxoglutaric acid, and oxaloacetic acid) was mixed, the third peak increased (FIG. 17c). In contrast, no significant effect was observed with two other metabolic intermediates (i.e., pyruvic acid and 3-phosphoglyceric acid), each containing three carbon atoms.

Peaks associated with smaller retention time should correspond to assemblies of larger molecular weights. Thus it is concluded that isoleucine accelerates assembling of the protein, six other amino acids, i.e., methionine, arginine, leucine, phenylalanine, alanine, and threonine, accelerate disassembling of the protein, and valine and three metabolic intermediates (malic acid, 2-oxoglutaric acid, and oxaloacetic acid) have effects of stabilizing intermediate assemblies.

TABLE 1
3D atomic coordinates of the 3D structure of the FFRP
(pot1216151)
ORIGX1	1.000000	0.000000	0.000000	0.00000
ORIGX2	0.000000	1.000000	0.000000	0.00000
ORIGX3	0.000000	0.000000	1.000000	0.00000
CRYST1	96.345	96.345	97.056	90.00	90.00	120.00
SCALE1	0.010379	0.005993	0.000000	0.00000
SCALE2	0.000000	0.011985	0.000000	0.00000
SCALE3	0.000000	0.000000	0.010303	0.00000
ATOM	1	CB	VAL	A	2	−2.073	48.359	7.218	1.00	7.25	6	C
ATOM	2	CG1	VAL	A	2	−0.814	47.539	6.836	1.00	8.49	6	C
ATOM	3	CG2	VAL	A	2	−3.080	48.341	6.088	1.00	7.16	6	C
ATOM	4	C	VAL	A	2	−1.718	47.700	9.595	1.00	7.20	6	C
ATOM	5	O	VAL	A	2	−1.191	48.725	10.010	1.00	8.49	8	O
ATOM	6	N	VAL	A	2	−4.005	48.669	8.832	1.00	7.12	7	N
ATOM	7	CA	VAL	A	2	−2.752	47.840	8.490	1.00	7.39	6	C
ATOM	8	N	THR	A	3	−1.376	46.456	9.992	1.00	7.51	7	N
ATOM	9	CA	THR	A	3	−0.236	46.219	10.863	1.00	8.84	6	C
ATOM	10	CB	THR	A	3	−0.541	45.367	12.111	1.00	9.16	6	C
ATOM	11	OG1	THR	A	3	−1.620	46.010	12.820	1.00	9.25	8	O
ATOM	12	CG2	THR	A	3	0.616	45.208	13.110	1.00	8.76	6	C
ATOM	13	C	THR	A	3	0.836	45.449	10.073	1.00	6.50	6	C
ATOM	14	O	THR	A	3	0.454	44.528	9.380	1.00	4.22	8	O
ATOM	15	N	ALA	A	4	2.098	45.907	10.132	1.00	6.94	7	N
ATOM	16	CA	ALA	A	4	3.101	45.068	9.420	1.00	6.58	6	C
ATOM	17	CB	ALA	A	4	3.286	45.669	8.021	1.00	6.97	6	C
ATOM	18	C	ALA	A	4	4.402	45.022	10.211	1.00	7.80	6	C
ATOM	19	O	ALA	A	4	4.635	45.828	11.124	1.00	7.68	8	O
ATOM	20	N	PHE	A	5	5.272	44.058	9.877	1.00	5.61	7	N
ATOM	21	CA	PHE	A	5	6.561	44.001	10.554	1.00	7.24	6	C
ATOM	22	CB	PHE	A	5	6.806	42.707	11.355	1.00	6.59	6	C
ATOM	23	CG	PHE	A	5	5.969	42.618	12.605	1.00	7.48	6	C
ATOM	24	CD1	PHE	A	5	4.628	42.271	12.533	1.00	7.25	6	C
ATOM	25	CD2	PHE	A	5	6.511	42.995	13.830	1.00	8.05	6	C
ATOM	26	CE1	PHE	A	5	3.833	42.218	13.670	1.00	8.84	6	C
ATOM	27	CE2	PHE	A	5	5.734	42.907	14.983	1.00	6.40	6	C
ATOM	28	CZ	PHE	A	5	4.430	42.493	14.877	1.00	7.39	6	C
ATOM	29	C	PHE	A	5	7.648	44.035	9.432	1.00	7.62	6	C
ATOM	30	O	PHE	A	5	7.556	43.301	8.456	1.00	4.61	8	O
ATOM	31	N	ILE	A	6	8.535	45.005	9.654	1.00	7.29	7	N
ATOM	32	CA	ILE	A	6	9.625	45.211	8.729	1.00	7.19	6	C
ATOM	33	CB	ILE	A	6	9.692	46.692	8.314	1.00	5.96	6	C
ATOM	34	CG2	ILE	A	6	10.728	46.809	7.191	1.00	5.34	6	C
ATOM	35	CG1	ILE	A	6	8.337	47.188	7.774	1.00	7.13	6	C
ATOM	36	CD1	ILE	A	6	8.404	48.686	7.432	1.00	9.39	6	C
ATOM	37	C	ILE	A	6	10.957	44.758	9.348	1.00	6.37	6	C
ATOM	38	O	ILE	A	6	11.373	45.243	10.412	1.00	6.22	8	O
ATOM	39	N	LEU	A	7	11.568	43.783	8.725	1.00	7.34	7	N
ATOM	40	CA	LEU	A	7	12.832	43.204	9.137	1.00	9.69	6	C
ATOM	41	CB	LEU	A	7	12.897	41.701	8.927	1.00	12.76	6	C
ATOM	42	CG	LEU	A	7	11.781	40.816	9.451	1.00	17.25	6	C
ATOM	43	CD1	LEU	A	7	12.038	39.325	9.258	1.00	18.40	6	C
ATOM	44	CD2	LEU	A	7	11.550	41.078	10.922	1.00	17.00	6	C
ATOM	45	C	LEU	A	7	13.973	43.797	8.292	1.00	9.33	6	C
ATOM	46	O	LEU	A	7	13.711	44.012	7.118	1.00	7.50	8	O
ATOM	47	N	MET	A	8	15.012	44.351	8.930	1.00	9.25	7	N
ATOM	48	CA	MET	A	8	16.013	45.098	8.227	1.00	11.96	6	C
ATOM	49	CB	MET	A	8	15.954	46.584	8.663	1.00	13.86	6	C
ATOM	50	CG	MET	A	8	14.610	47.251	8.492	1.00	18.88	6	C
ATOM	51	SD	MET	A	8	14.490	48.890	9.189	1.00	16.93	16	S
ATOM	52	CE	MET	A	8	13.643	48.403	10.698	1.00	23.90	6	C
ATOM	53	C	MET	A	8	17.458	44.653	8.580	1.00	14.57	6	C
ATOM	54	O	MET	A	8	17.730	44.249	9.707	1.00	12.69	8	O
ATOM	55	N	VAL	A	9	18.357	44.743	7.615	1.00	13.97	7	N
ATOM	56	CA	VAL	A	9	19.787	44.503	7.800	1.00	14.26	6	C
ATOM	57	CB	VAL	A	9	20.417	43.674	6.668	1.00	16.26	6	C
ATOM	58	CG1	VAL	A	9	21.972	43.738	6.697	1.00	16.52	6	C
ATOM	59	CG2	VAL	A	9	19.994	42.242	6.760	1.00	14.67	6	C
ATOM	60	C	VAL	A	9	20.346	45.902	7.807	1.00	15.95	6	C
ATOM	61	O	VAL	A	9	19.933	46.661	6.900	1.00	20.59	8	O
ATOM	62	N	THR	A	10	21.152	46.424	8.712	1.00	15.01	7	N
ATOM	63	CA	THR	A	10	21.660	47.783	8.609	1.00	13.75	6	C
ATOM	64	CB	THR	A	10	21.540	48.675	9.859	1.00	13.36	6	C
ATOM	65	OG1	THR	A	10	22.194	48.066	11.001	1.00	11.93	8	O
ATOM	66	CG2	THR	A	10	20.070	48.913	10.248	1.00	13.19	6	C
ATOM	67	C	THR	A	10	23.190	47.710	8.376	1.00	15.09	6	C
ATOM	68	O	THR	A	10	23.728	46.650	8.648	1.00	15.54	8	O
ATOM	69	N	ALA	A	11	23.809	48.827	8.039	1.00	16.40	7	N
ATOM	70	CA	ALA	A	11	25.306	48.728	7.997	1.00	17.23	6	C
ATOM	71	CB	ALA	A	11	25.835	50.065	7.564	1.00	16.26	6	C
ATOM	72	C	ALA	A	11	25.722	48.352	9.413	1.00	17.14	6	C
ATOM	73	O	ALA	A	11	25.090	48.782	10.388	1.00	16.25	8	O
ATOM	74	N	ALA	A	12	26.758	47.550	9.599	1.00	17.62	7	N
ATOM	75	CA	ALA	A	12	27.170	47.140	10.952	1.00	17.18	6	C
ATOM	76	CB	ALA	A	12	28.389	46.228	10.790	1.00	18.07	6	C
ATOM	77	C	ALA	A	12	27.431	48.312	11.870	1.00	16.00	6	C
ATOM	78	O	ALA	A	12	28.132	49.260	11.528	1.00	14.87	8	O
ATOM	79	N	GLY	A	13	26.855	48.330	13.093	1.00	14.71	7	N
ATOM	80	CA	GLY	A	13	27.171	49.433	14.022	1.00	14.32	6	C
ATOM	81	C	GLY	A	13	26.236	50.639	13.929	1.00	15.21	6	C
ATOM	82	O	GLY	A	13	26.360	51.575	14.690	1.00	15.60	8	O
ATOM	83	N	LYS	A	14	25.288	50.635	13.004	1.00	15.71	7	N
ATOM	84	CA	LYS	A	14	24.320	51.724	12.873	1.00	16.25	6	C
ATOM	85	CB	LYS	A	14	24.207	52.109	11.375	1.00	17.80	6	C
ATOM	86	CG	LYS	A	14	25.566	52.622	10.845	1.00	21.86	6	C
ATOM	87	CD	LYS	A	14	25.885	53.964	11.484	1.00	21.55	6	C
ATOM	88	CE	LYS	A	14	27.300	54.385	11.090	1.00	24.44	6	C
ATOM	89	NZ	LYS	A	14	27.432	55.819	11.485	1.00	25.93	7	N
ATOM	90	C	LYS	A	14	22.920	51.288	13.302	1.00	14.39	6	C
ATOM	91	O	LYS	A	14	22.013	52.111	13.269	1.00	15.68	8	O
ATOM	92	N	GLU	A	15	22.738	50.034	13.653	1.00	13.01	7	N
ATOM	93	CA	GLU	A	15	21.393	49.571	14.001	1.00	15.99	6	C
ATOM	94	CB	GLU	A	15	21.452	48.127	14.521	1.00	17.36	6	C
ATOM	95	CG	GLU	A	15	22.248	48.147	15.825	1.00	25.39	6	C
ATOM	96	CD	GLU	A	15	22.807	46.808	16.246	1.00	31.23	6	C
ATOM	97	OE1	GLU	A	15	22.135	45.923	15.626	1.00	35.29	8	O
ATOM	98	OE2	GLU	A	15	23.723	46.692	17.119	1.00	30.70	8	O
ATOM	99	C	GLU	A	15	20.705	50.444	15.061	1.00	15.48	6	C
ATOM	100	O	GLU	A	15	19.530	50.761	14.944	1.00	12.54	8	O
ATOM	101	N	ARG	A	16	21.415	50.780	16.143	1.00	16.35	7	N
ATOM	102	CA	ARG	A	16	20.787	51.555	17.210	1.00	19.56	6	C
ATOM	103	CB	ARG	A	16	21.667	51.542	18.462	1.00	23.74	6	C
ATOM	104	CG	ARG	A	16	21.326	52.436	19.616	1.00	29.54	6	C
ATOM	105	CD	ARG	A	16	21.727	53.910	19.477	1.00	35.88	6	C
ATOM	106	NE	ARG	A	16	21.060	54.702	20.540	1.00	41.43	7	N
ATOM	107	CZ	ARG	A	16	21.427	54.741	21.819	1.00	43.05	6	C
ATOM	108	NH1	ARG	A	16	22.488	54.052	22.253	1.00	45.29	7	N
ATOM	109	NH2	ARG	A	16	20.720	55.492	22.656	1.00	44.30	7	N
ATOM	110	C	ARG	A	16	20.424	52.947	16.752	1.00	18.28	6	C
ATOM	111	O	ARG	A	16	19.346	53.412	17.143	1.00	16.68	8	O
ATOM	112	N	GLU	A	17	21.313	53.637	16.018	1.00	16.79	7	N
ATOM	113	CA	GLU	A	17	20.956	54.980	15.563	1.00	15.83	6	C
ATOM	114	CB	GLU	A	17	22.123	55.767	15.012	1.00	18.26	6	C
ATOM	115	CG	GLU	A	17	22.870	55.079	13.891	1.00	21.97	6	C
ATOM	116	CD	GLU	A	17	22.345	55.501	12.538	1.00	25.19	6	C
ATOM	117	OE1	GLU	A	17	21.453	56.393	12.521	1.00	26.12	8	O
ATOM	118	OE2	GLU	A	17	22.822	54.970	11.512	1.00	27.57	8	O
ATOM	119	C	GLU	A	17	19.819	54.887	14.538	1.00	14.37	6	C
ATOM	120	O	GLU	A	17	18.952	55.773	14.540	1.00	12.63	8	O
ATOM	121	N	VAL	A	18	19.744	53.871	13.711	1.00	11.94	7	N
ATOM	122	CA	VAL	A	18	18.618	53.738	12.799	1.00	12.82	6	C
ATOM	123	CB	VAL	A	18	18.806	52.622	11.773	1.00	13.64	6	C
ATOM	124	CG1	VAL	A	18	17.503	52.290	11.014	1.00	10.60	6	C
ATOM	125	CG2	VAL	A	18	19.882	53.077	10.757	1.00	13.42	6	C
ATOM	126	C	VAL	A	18	17.359	53.493	13.631	1.00	14.02	6	C
ATOM	127	O	VAL	A	18	16.319	54.112	13.357	1.00	14.65	8	O
ATOM	128	N	MET	A	19	17.442	52.601	14.594	1.00	13.17	7	N
ATOM	129	CA	MET	A	19	16.271	52.267	15.425	1.00	13.50	6	C
ATOM	130	CB	MET	A	19	16.681	51.279	16.512	1.00	14.15	6	C
ATOM	131	CG	MET	A	19	15.459	50.893	17.328	1.00	15.47	6	C
ATOM	132	SD	MET	A	19	15.745	49.773	18.610	1.00	16.28	16	S
ATOM	133	CE	MET	A	19	16.553	50.600	19.921	1.00	18.98	6	C
ATOM	134	C	MET	A	19	15.711	53.484	16.132	1.00	14.53	6	C
ATOM	135	O	MET	A	19	14.486	53.703	16.175	1.00	13.43	8	O
ATOM	136	N	GLU	A	20	16.611	54.320	16.649	1.00	14.59	7	N
ATOM	137	CA	GLU	A	20	16.163	55.531	17.322	1.00	18.00	6	C
ATOM	138	CB	GLU	A	20	17.306	56.289	18.025	1.00	20.38	6	C
ATOM	139	CG	GLU	A	20	17.844	55.506	19.220	1.00	23.46	6	C
ATOM	140	CD	GLU	A	20	16.821	55.001	20.202	1.00	27.70	6	C
ATOM	141	OE1	GLU	A	20	15.771	55.673	20.405	1.00	31.74	8	O
ATOM	142	OE2	GLU	A	20	17.017	53.914	20.797	1.00	29.38	8	O
ATOM	143	C	GLU	A	20	15.420	56.452	16.373	1.00	17.62	6	C
ATOM	144	O	GLU	A	20	14.387	56.983	16.753	1.00	17.09	8	O
ATOM	145	N	LYS	A	21	15.914	56.708	15.172	1.00	16.59	7	N
ATOM	146	CA	LYS	A	21	15.260	57.495	14.164	1.00	15.48	6	C
ATOM	147	CB	LYS	A	21	16.106	57.424	12.866	1.00	15.60	6	C
ATOM	148	CG	LYS	A	21	17.132	58.542	12.743	1.00	19.35	6	C
ATOM	149	CD	LYS	A	21	18.166	58.319	11.668	1.00	20.39	6	C
ATOM	150	CE	LYS	A	21	19.434	59.162	11.914	1.00	23.18	6	C
ATOM	151	NZ	LYS	A	21	20.429	58.883	10.813	1.00	21.66	7	N
ATOM	152	C	LYS	A	21	13.879	56.889	13.850	1.00	14.96	6	C
ATOM	153	O	LYS	A	21	12.905	57.633	13.658	1.00	15.15	8	O
ATOM	154	N	LEU	A	22	13.759	55.566	13.682	1.00	10.45	7	N
ATOM	155	CA	LEU	A	22	12.469	54.967	13.372	1.00	11.33	6	C
ATOM	156	CB	LEU	A	22	12.651	53.463	13.095	1.00	11.29	6	C
ATOM	157	CG	LEU	A	22	13.490	53.153	11.855	1.00	12.08	6	C
ATOM	158	CD1	LEU	A	22	13.725	51.647	11.748	1.00	14.54	6	C
ATOM	159	CD2	LEU	A	22	12.857	53.652	10.579	1.00	11.38	6	C
ATOM	160	C	LEU	A	22	11.460	55.109	14.514	1.00	11.56	6	C
ATOM	161	O	LEU	A	22	10.270	55.364	14.275	1.00	10.86	8	O
ATOM	162	N	LEU	A	23	11.918	54.921	15.746	1.00	13.00	7	N
ATOM	163	CA	LEU	A	23	11.054	55.014	16.917	1.00	16.61	6	C
ATOM	164	CB	LEU	A	23	11.801	54.718	18.209	1.00	16.55	6	C
ATOM	165	CG	LEU	A	23	11.858	53.264	18.610	1.00	18.39	6	C
ATOM	166	CD1	LEU	A	23	12.928	53.050	19.675	1.00	16.32	6	C
ATOM	167	CD2	LEU	A	23	10.501	52.804	19.142	1.00	17.70	6	C
ATOM	168	C	LEU	A	23	10.404	56.393	17.064	1.00	15.89	6	C
ATOM	169	O	LEU	A	23	9.282	56.440	17.556	1.00	17.60	8	O
ATOM	170	N	ALA	A	24	10.998	57.440	16.551	1.00	16.01	7	N
ATOM	171	CA	ALA	A	24	10.422	58.773	16.532	1.00	18.43	6	C
ATOM	172	CB	ALA	A	24	11.533	59.775	16.231	1.00	16.56	6	C
ATOM	173	C	ALA	A	24	9.330	58.951	15.481	1.00	18.75	6	C
ATOM	174	O	ALA	A	24	8.778	60.058	15.427	1.00	19.41	8	O
ATOM	175	N	MET	A	25	9.188	58.039	14.512	1.00	15.42	7	N
ATOM	176	CA	MET	A	25	8.189	58.202	13.466	1.00	15.12	6	C
ATOM	177	CB	MET	A	25	8.570	57.409	12.208	1.00	14.61	6	C
ATOM	178	CG	MET	A	25	9.787	57.989	11.504	1.00	16.53	6	C
ATOM	179	SD	MET	A	25	10.471	56.816	10.317	1.00	15.91	16	S
ATOM	180	CE	MET	A	25	12.118	57.576	10.131	1.00	18.16	6	C
ATOM	181	C	MET	A	25	6.845	57.715	13.992	1.00	15.09	6	C
ATOM	182	O	MET	A	25	6.801	56.666	14.654	1.00	15.91	8	O
ATOM	183	N	PRO	A	26	5.757	58.441	13.743	1.00	14.86	7	N
ATOM	184	CD	PRO	A	26	5.755	59.703	12.955	1.00	14.19	6	C
ATOM	185	CA	PRO	A	26	4.455	58.083	14.242	1.00	14.29	6	C
ATOM	186	CB	PRO	A	26	3.504	59.246	13.796	1.00	15.81	6	C
ATOM	187	CG	PRO	A	26	4.265	59.970	12.737	1.00	16.25	6	C
ATOM	188	C	PRO	A	26	3.900	56.773	13.810	1.00	13.72	6	C
ATOM	189	O	PRO	A	26	3.192	56.130	14.625	1.00	14.68	8	O
ATOM	190	N	GLU	A	27	4.291	56.227	12.645	1.00	13.34	7	N
ATOM	191	CA	GLU	A	27	3.806	54.923	12.235	1.00	13.47	6	C
ATOM	192	CB	GLU	A	27	4.091	54.625	10.760	1.00	17.16	6	C
ATOM	193	CG	GLU	A	27	3.995	55.541	9.606	1.00	21.17	6	C
ATOM	194	CD	GLU	A	27	4.560	56.955	9.586	1.00	23.93	6	C
ATOM	195	OE1	GLU	A	27	5.418	57.453	10.335	1.00	20.18	8	O
ATOM	196	OE2	GLU	A	27	4.072	57.616	8.610	1.00	25.99	8	O
ATOM	197	C	GLU	A	27	4.444	53.764	13.004	1.00	10.60	6	C
ATOM	198	O	GLU	A	27	3.954	52.644	13.011	1.00	7.90	8	O
ATOM	199	N	VAL	A	28	5.617	53.989	13.561	1.00	9.98	7	N
ATOM	200	CA	VAL	A	28	6.394	52.946	14.202	1.00	8.91	6	C
ATOM	201	CB	VAL	A	28	7.896	53.306	14.215	1.00	8.00	6	C
ATOM	202	CG1	VAL	A	28	8.683	52.277	15.029	1.00	6.92	6	C
ATOM	203	CG2	VAL	A	28	8.442	53.420	12.791	1.00	6.99	6	C
ATOM	204	C	VAL	A	28	5.878	52.729	15.620	1.00	10.15	6	C
ATOM	205	O	VAL	A	28	5.925	53.618	16.428	1.00	10.34	8	O
ATOM	206	N	LYS	A	29	5.411	51.543	15.933	1.00	10.04	7	N
ATOM	207	CA	LYS	A	29	4.865	51.238	17.225	1.00	12.44	6	C
ATOM	208	CB	LYS	A	29	3.643	50.303	17.106	1.00	13.57	6	C
ATOM	209	CG	LYS	A	29	2.432	50.906	16.421	1.00	14.50	6	C
ATOM	210	CD	LYS	A	29	2.302	52.410	16.610	1.00	15.93	6	C
ATOM	211	CE	LYS	A	29	1.142	52.994	15.832	1.00	20.88	6	C
ATOM	212	NZ	LYS	A	29	1.224	54.497	15.684	1.00	22.58	7	N
ATOM	213	C	LYS	A	29	5.891	50.550	18.129	1.00	12.91	6	C
ATOM	214	O	LYS	A	29	5.769	50.754	19.332	1.00	11.55	8	O
ATOM	215	N	GLU	A	30	6.810	49.746	17.592	1.00	10.53	7	N
ATOM	216	CA	GLU	A	30	7.785	49.053	18.424	1.00	11.26	6	C
ATOM	217	CB	GLU	A	30	7.350	47.633	18.831	1.00	13.54	6	C
ATOM	218	CG	GLU	A	30	6.072	47.456	19.598	1.00	16.71	6	C
ATOM	219	CD	GLU	A	30	5.654	46.018	19.905	1.00	18.00	6	C
ATOM	220	OE1	GLU	A	30	4.403	45.814	19.971	1.00	17.65	8	O
ATOM	221	OE2	GLU	A	30	6.554	45.183	20.077	1.00	15.08	8	O
ATOM	222	C	GLU	A	30	9.025	48.844	17.522	1.00	8.70	6	C
ATOM	223	O	GLU	A	30	8.821	48.760	16.305	1.00	6.20	8	O
ATOM	224	N	ALA	A	31	10.198	48.728	18.108	1.00	8.38	7	N
ATOM	225	CA	ALA	A	31	11.417	48.529	17.293	1.00	5.18	6	C
ATOM	226	CB	ALA	A	31	11.894	49.862	16.752	1.00	7.29	6	C
ATOM	227	C	ALA	A	31	12.462	47.902	18.163	1.00	9.36	6	C
ATOM	228	O	ALA	A	31	12.517	48.224	19.344	1.00	9.20	8	O
ATOM	229	N	TYR	A	32	13.162	46.872	17.670	1.00	6.49	7	N
ATOM	230	CA	TYR	A	32	14.166	46.191	18.428	1.00	8.44	6	C
ATOM	231	CB	TYR	A	32	13.698	44.827	18.938	1.00	6.51	6	C
ATOM	232	CG	TYR	A	32	12.632	44.881	20.030	1.00	7.98	6	C
ATOM	233	CD1	TYR	A	32	12.981	44.818	21.371	1.00	9.50	6	C
ATOM	234	CE1	TYR	A	32	12.017	44.881	22.369	1.00	12.01	6	C
ATOM	235	CD2	TYR	A	32	11.293	45.016	19.698	1.00	8.48	6	C
ATOM	236	CE2	TYR	A	32	10.324	45.079	20.666	1.00	9.99	6	C
ATOM	237	CZ	TYR	A	32	10.685	44.997	21.998	1.00	11.97	6	C
ATOM	238	OH	TYR	A	32	9.698	45.024	22.951	1.00	12.74	8	O
ATOM	239	C	TYR	A	32	15.396	45.801	17.567	1.00	8.57	6	C
ATOM	240	O	TYR	A	32	15.211	45.300	16.462	1.00	7.72	8	O
ATOM	241	N	VAL	A	33	16.568	45.985	18.158	1.00	7.80	7	N
ATOM	242	CA	VAL	A	33	17.785	45.424	17.605	1.00	6.39	6	C
ATOM	243	CB	VAL	A	33	19.048	46.137	18.150	1.00	8.75	6	C
ATOM	244	CG1	VAL	A	33	20.273	45.355	17.658	1.00	8.40	6	C
ATOM	245	CG2	VAL	A	33	19.021	47.589	17.720	1.00	7.33	6	C
ATOM	246	C	VAL	A	33	17.812	43.939	17.896	1.00	5.76	6	C
ATOM	247	O	VAL	A	33	17.615	43.509	19.054	1.00	7.13	8	O
ATOM	248	N	VAL	A	34	18.079	43.073	16.894	1.00	4.78	7	N
ATOM	249	CA	VAL	A	34	18.004	41.632	17.161	1.00	6.41	6	C
ATOM	250	CB	VAL	A	34	16.731	41.014	16.512	1.00	6.60	6	C
ATOM	251	CG1	VAL	A	34	15.430	41.454	17.214	1.00	5.42	6	C
ATOM	252	CG2	VAL	A	34	16.583	41.384	15.032	1.00	6.47	6	C
ATOM	253	C	VAL	A	34	19.219	40.873	16.622	1.00	8.92	6	C
ATOM	254	O	VAL	A	34	19.953	41.359	15.772	1.00	10.44	8	O
ATOM	255	N	TYR	A	35	19.405	39.621	16.980	1.00	10.34	7	N
ATOM	256	CA	TYR	A	35	20.429	38.735	16.482	1.00	10.98	6	C
ATOM	257	CB	TYR	A	35	20.884	37.774	17.543	1.00	11.65	6	C
ATOM	258	CG	TYR	A	35	21.645	38.403	18.665	1.00	14.04	6	C
ATOM	259	CD1	TYR	A	35	22.970	38.793	18.465	1.00	17.64	6	C
ATOM	260	CE1	TYR	A	35	23.712	39.294	19.521	1.00	18.93	6	C
ATOM	261	CD2	TYR	A	35	21.070	38.581	19.905	1.00	15.53	6	C
ATOM	262	CE2	TYR	A	35	21.807	39.100	20.951	1.00	16.48	6	C
ATOM	263	CZ	TYR	A	35	23.122	39.436	20.762	1.00	19.05	6	C
ATOM	264	OH	TYR	A	35	23.870	39.944	21.812	1.00	20.64	8	O
ATOM	265	C	TYR	A	35	19.815	37.881	15.371	1.00	11.75	6	C
ATOM	266	O	TYR	A	35	18.624	37.596	15.481	1.00	14.45	8	O
ATOM	267	N	GLY	A	36	20.585	37.514	14.415	1.00	12.14	7	N
ATOM	268	CA	GLY	A	36	20.085	36.727	13.250	1.00	15.97	6	C
ATOM	269	C	GLY	A	36	20.689	37.429	12.036	1.00	16.50	6	C
ATOM	270	O	GLY	A	36	21.418	38.441	12.153	1.00	21.32	8	O
ATOM	271	N	GLU	A	37	20.171	37.205	10.883	1.00	20.97	7	N
ATOM	272	CA	GLU	A	37	20.478	37.746	9.563	1.00	24.00	6	C
ATOM	273	CB	GLU	A	37	19.730	36.869	8.521	1.00	28.29	6	C
ATOM	274	CG	GLU	A	37	19.992	37.381	7.113	1.00	31.96	6	C
ATOM	275	CD	GLU	A	37	19.034	36.898	6.059	1.00	35.65	6	C
ATOM	276	OE1	GLU	A	37	18.268	35.905	6.213	1.00	37.44	8	O
ATOM	277	OE2	GLU	A	37	19.114	37.582	5.011	1.00	38.02	8	O
ATOM	278	C	GLU	A	37	19.912	39.147	9.418	1.00	23.50	6	C
ATOM	279	O	GLU	A	37	20.409	40.033	8.717	1.00	24.72	8	O
ATOM	280	N	TYR	A	38	18.815	39.382	10.151	1.00	21.31	7	N
ATOM	281	CA	TYR	A	38	18.292	40.761	10.215	1.00	18.05	6	C
ATOM	282	CB	TYR	A	38	16.758	40.730	10.202	1.00	18.36	6	C
ATOM	283	CG	TYR	A	38	16.285	40.221	8.856	1.00	21.89	6	C
ATOM	284	CD1	TYR	A	38	16.438	41.026	7.736	1.00	23.00	6	C
ATOM	285	CE1	TYR	A	38	15.971	40.590	6.514	1.00	25.96	6	C
ATOM	286	CD2	TYR	A	38	15.624	39.002	8.750	1.00	24.51	6	C
ATOM	287	CE2	TYR	A	38	15.160	38.565	7.520	1.00	26.07	6	C
ATOM	288	CZ	TYR	A	38	15.410	39.342	6.414	1.00	25.27	6	C
ATOM	289	OH	TYR	A	38	14.955	38.933	5.173	1.00	29.39	8	O
ATOM	290	C	TYR	A	38	18.810	41.336	11.545	1.00	15.22	6	C
ATOM	291	O	TYR	A	38	18.883	40.635	12.546	1.00	16.00	8	O
ATOM	292	N	ASP	A	39	18.955	42.613	11.599	1.00	14.06	7	N
ATOM	293	CA	ASP	A	39	19.565	43.412	12.643	1.00	13.19	6	C
ATOM	294	CB	ASP	A	39	20.378	44.510	11.873	1.00	11.78	6	C
ATOM	295	CG	ASP	A	39	21.527	43.891	11.130	1.00	13.09	6	C
ATOM	296	OD1	ASP	A	39	21.795	42.747	11.415	1.00	12.32	8	O
ATOM	297	OD2	ASP	A	39	22.173	44.518	10.302	1.00	16.95	8	O
ATOM	298	C	ASP	A	39	18.532	44.178	13.447	1.00	10.56	6	C
ATOM	299	O	ASP	A	39	18.763	44.513	14.618	1.00	8.22	8	O
ATOM	300	N	LEU	A	40	17.434	44.496	12.735	1.00	9.46	7	N
ATOM	301	CA	LEU	A	40	16.344	45.250	13.355	1.00	9.22	6	C
ATOM	302	CB	LEU	A	40	16.246	46.683	12.865	1.00	12.49	6	C
ATOM	303	CG	LEU	A	40	17.180	47.814	13.176	1.00	14.92	6	C
ATOM	304	CD1	LEU	A	40	16.680	49.055	12.461	1.00	15.41	6	C
ATOM	305	CD2	LEU	A	40	17.274	48.049	14.672	1.00	17.24	6	C
ATOM	306	C	LEU	A	40	14.966	44.704	12.880	1.00	8.69	6	C
ATOM	307	O	LEU	A	40	14.829	44.337	11.705	1.00	6.37	8	O
ATOM	308	N	ILE	A	41	14.001	44.818	13.778	1.00	7.55	7	N
ATOM	309	CA	ILE	A	41	12.598	44.417	13.498	1.00	8.63	6	C
ATOM	310	CB	ILE	A	41	12.087	43.119	14.076	1.00	9.76	6	C
ATOM	311	CG2	ILE	A	41	12.326	42.903	15.566	1.00	11.62	6	C
ATOM	312	CG1	ILE	A	41	10.575	42.937	13.807	1.00	10.77	6	C
ATOM	313	CD1	ILE	A	41	10.193	41.468	13.867	1.00	13.08	6	C
ATOM	314	C	ILE	A	41	11.750	45.593	13.967	1.00	10.12	6	C
ATOM	315	O	ILE	A	41	12.005	46.153	15.053	1.00	7.54	8	O
ATOM	316	N	VAL	A	42	10.953	46.090	13.043	1.00	8.66	7	N
ATOM	317	CA	VAL	A	42	10.139	47.268	13.395	1.00	10.64	6	C
ATOM	318	CB	VAL	A	42	10.656	48.463	12.600	1.00	14.70	6	C
ATOM	319	CG1	VAL	A	42	9.705	49.597	12.514	1.00	14.15	6	C
ATOM	320	CG2	VAL	A	42	11.929	49.038	13.295	1.00	17.64	6	C
ATOM	321	C	VAL	A	42	8.676	46.957	13.114	1.00	9.69	6	C
ATOM	322	O	VAL	A	42	8.404	46.277	12.123	1.00	9.29	8	O
ATOM	323	N	LYS	A	43	7.785	47.249	14.067	1.00	9.12	7	N
ATOM	324	CA	LYS	A	43	6.352	47.043	13.919	1.00	7.52	6	C
ATOM	325	CB	LYS	A	43	5.757	46.570	15.274	1.00	8.78	6	C
ATOM	326	CG	LYS	A	43	4.246	46.290	15.145	1.00	12.03	6	C
ATOM	327	CD	LYS	A	43	3.692	45.912	16.541	1.00	11.71	6	C
ATOM	328	CE	LYS	A	43	2.200	45.790	16.524	1.00	13.09	6	C
ATOM	329	NZ	LYS	A	43	1.593	45.210	17.748	1.00	11.39	7	N
ATOM	330	C	LYS	A	43	5.697	48.367	13.564	1.00	7.31	6	C
ATOM	331	O	LYS	A	43	5.845	49.413	14.216	1.00	6.38	8	O
ATOM	332	N	VAL	A	44	4.971	48.402	12.451	1.00	6.74	7	N
ATOM	333	CA	VAL	A	44	4.336	49.585	11.930	1.00	7.54	6	C
ATOM	334	CB	VAL	A	44	4.898	50.065	10.573	1.00	11.01	6	C
ATOM	335	CG1	VAL	A	44	6.434	50.232	10.650	1.00	12.68	6	C
ATOM	336	CG2	VAL	A	44	4.541	49.098	9.469	1.00	10.39	6	C
ATOM	337	C	VAL	A	44	2.825	49.371	11.758	1.00	9.21	6	C
ATOM	338	O	VAL	A	44	2.292	48.264	11.561	1.00	8.93	8	O
ATOM	339	N	GLU	A	45	2.134	50.493	11.957	1.00	10.36	7	N
ATOM	340	CA	GLU	A	45	0.665	50.496	11.858	1.00	12.06	6	C
ATOM	341	CB	GLU	A	45	0.004	50.496	13.238	1.00	12.25	6	C
ATOM	342	CG	GLU	A	45	0.012	49.086	13.798	1.00	15.23	6	C
ATOM	343	CD	GLU	A	45	−0.408	48.927	15.233	1.00	18.39	6	C
ATOM	344	OE1	GLU	A	45	−0.169	47.876	15.848	1.00	21.70	8	O
ATOM	345	OE2	GLU	A	45	−1.021	49.852	15.769	1.00	21.18	8	O
ATOM	346	C	GLU	A	45	0.236	51.698	11.047	1.00	10.21	6	C
ATOM	347	O	GLU	A	45	0.783	52.780	11.208	1.00	10.74	8	O
ATOM	348	N	THR	A	46	−0.422	51.431	9.912	1.00	10.02	7	N
ATOM	349	CA	THR	A	46	−0.794	52.546	9.056	1.00	10.52	6	C
ATOM	350	CB	THR	A	46	−0.030	52.589	7.701	1.00	12.10	6	C
ATOM	351	OG1	THR	A	46	−0.280	51.395	6.931	1.00	9.65	8	O
ATOM	352	CG2	THR	A	46	1.482	52.648	7.918	1.00	14.04	6	C
ATOM	353	C	THR	A	46	−2.297	52.431	8.783	1.00	10.40	6	C
ATOM	354	O	THR	A	46	−2.889	51.353	8.880	1.00	6.84	8	O
ATOM	355	N	ASP	A	47	−2.838	53.524	8.240	1.00	10.42	7	N
ATOM	356	CA	ASP	A	47	−4.298	53.427	7.930	1.00	13.28	6	C
ATOM	357	CB	ASP	A	47	−4.956	54.763	7.696	1.00	17.79	6	C
ATOM	358	CG	ASP	A	47	−4.912	55.703	8.873	1.00	22.85	6	C
ATOM	359	OD1	ASP	A	47	−5.187	55.282	10.024	1.00	24.70	8	O
ATOM	360	OD2	ASP	A	47	−4.546	56.871	8.607	1.00	26.41	8	O
ATOM	361	C	ASP	A	47	−4.556	52.525	6.736	1.00	12.26	6	C
ATOM	362	O	ASP	A	47	−5.638	51.891	6.708	1.00	9.75	8	O
ATOM	363	N	THR	A	48	−3.726	52.630	5.681	1.00	10.33	7	N
ATOM	364	CA	THR	A	48	−3.998	51.918	4.451	1.00	10.32	6	C
ATOM	365	CB	THR	A	48	−4.553	52.795	3.306	1.00	12.96	6	C
ATOM	366	OG1	THR	A	48	−3.520	53.774	3.020	1.00	11.60	8	O
ATOM	367	CG2	THR	A	48	−5.883	53.503	3.608	1.00	15.12	6	C
ATOM	368	C	THR	A	48	−2.701	51.285	3.893	1.00	11.08	6	C
ATOM	369	O	THR	A	48	−1.596	51.629	4.290	1.00	10.17	8	O
ATOM	370	N	LEU	A	49	−2.831	50.326	3.009	1.00	11.90	7	N
ATOM	371	CA	LEU	A	49	−1.700	49.679	2.357	1.00	13.32	6	C
ATOM	372	CB	LEU	A	49	−2.134	48.604	1.395	1.00	14.57	6	C
ATOM	373	CG	LEU	A	49	−1.094	47.810	0.623	1.00	17.35	6	C
ATOM	374	CD1	LEU	A	49	−0.056	47.181	1.546	1.00	15.04	6	C
ATOM	375	CD2	LEU	A	49	−1.808	46.682	−0.141	1.00	17.00	6	C
ATOM	376	C	LEU	A	49	−0.852	50.701	1.596	1.00	14.01	6	C
ATOM	377	O	LEU	A	49	0.391	50.684	1.581	1.00	13.28	8	O
ATOM	378	N	LYS	A	50	−1.512	51.662	0.995	1.00	14.48	7	N
ATOM	379	CA	LYS	A	50	−0.901	52.771	0.305	1.00	17.54	6	C
ATOM	380	CB	LYS	A	50	−2.009	53.660	−0.266	1.00	21.43	6	C
ATOM	381	CG	LYS	A	50	−1.525	54.829	−1.120	1.00	27.31	6	C
ATOM	382	CD	LYS	A	50	−2.665	55.246	−2.068	1.00	30.92	6	C
ATOM	383	CE	LYS	A	50	−2.165	55.936	−3.327	1.00	35.13	6	C
ATOM	384	NZ	LYS	A	50	−1.681	55.003	−4.385	1.00	37.07	7	N
ATOM	385	C	LYS	A	50	−0.042	53.546	1.285	1.00	15.32	6	C
ATOM	386	O	LYS	A	50	1.063	53.914	0.938	1.00	14.61	8	O
ATOM	387	N	ASP	A	51	−0.491	53.838	2.496	1.00	14.52	7	N
ATOM	388	CA	ASP	A	51	0.314	54.507	3.504	1.00	13.63	6	C
ATOM	389	CB	ASP	A	51	−0.439	54.839	4.775	1.00	16.05	6	C
ATOM	390	CG	ASP	A	51	−1.564	55.875	4.586	1.00	19.66	6	C
ATOM	391	OD1	ASP	A	51	−1.389	56.778	3.763	1.00	18.33	8	O
ATOM	392	OD2	ASP	A	51	−2.609	55.712	5.280	1.00	20.80	8	O
ATOM	393	C	ASP	A	51	1.563	53.630	3.824	1.00	12.48	6	C
ATOM	394	O	ASP	A	51	2.638	54.196	4.026	1.00	10.69	8	O
ATOM	395	N	LEU	A	52	1.429	52.318	3.906	1.00	10.26	7	N
ATOM	396	CA	LEU	A	52	2.587	51.461	4.209	1.00	10.76	6	C
ATOM	397	CB	LEU	A	52	2.161	50.001	4.439	1.00	8.04	6	C
ATOM	398	CG	LEU	A	52	3.303	48.994	4.717	1.00	8.93	6	C
ATOM	399	CD1	LEU	A	52	4.036	49.344	5.991	1.00	8.54	6	C
ATOM	400	CD2	LEU	A	52	2.727	47.582	4.789	1.00	6.69	6	C
ATOM	401	C	LEU	A	52	3.609	51.536	3.086	1.00	10.23	6	C
ATOM	402	O	LEU	A	52	4.803	51.700	3.307	1.00	10.81	8	O
ATOM	403	N	ASP	A	53	3.139	51.505	1.847	1.00	12.35	7	N
ATOM	404	CA	ASP	A	53	3.945	51.675	0.658	1.00	14.81	6	C
ATOM	405	CB	ASP	A	53	3.000	51.762	−0.539	1.00	16.01	6	C
ATOM	406	CG	ASP	A	53	2.380	50.470	−0.981	1.00	16.50	6	C
ATOM	407	OD1	ASP	A	53	2.487	49.314	−0.542	1.00	16.66	8	O
ATOM	408	OD2	ASP	A	53	1.600	50.652	−1.934	1.00	19.89	8	O
ATOM	409	C	ASP	A	53	4.760	52.960	0.728	1.00	16.37	6	C
ATOM	410	O	ASP	A	53	5.984	52.976	0.478	1.00	13.89	8	O
ATOM	411	N	GLN	A	54	4.067	54.021	1.166	1.00	16.03	7	N
ATOM	412	CA	GLN	A	54	4.736	55.341	1.262	1.00	17.59	6	C
ATOM	413	CB	GLN	A	54	3.640	56.376	1.250	1.00	22.16	6	C
ATOM	414	CG	GLN	A	54	3.822	57.848	1.338	1.00	30.35	6	C
ATOM	415	CD	GLN	A	54	2.485	58.612	1.418	1.00	35.56	6	C
ATOM	416	OE1	GLN	A	54	1.366	58.133	1.134	1.00	37.13	8	O
ATOM	417	NE2	GLN	A	54	2.602	59.867	1.844	1.00	36.35	7	N
ATOM	418	C	GLN	A	54	5.722	55.402	2.394	1.00	15.60	6	C
ATOM	419	O	GLN	A	54	6.791	56.008	2.287	1.00	16.58	8	O
ATOM	420	N	PHE	A	55	5.539	54.709	3.507	1.00	14.54	7	N
ATOM	421	CA	PHE	A	55	6.508	54.584	4.590	1.00	12.24	6	C
ATOM	422	CB	PHE	A	55	5.901	53.747	5.733	1.00	12.77	6	C
ATOM	423	CG	PHE	A	55	6.785	53.705	6.955	1.00	11.74	6	C
ATOM	424	CD1	PHE	A	55	6.962	54.849	7.699	1.00	13.70	6	C
ATOM	425	CD2	PHE	A	55	7.483	52.560	7.281	1.00	11.58	6	C
ATOM	426	CE1	PHE	A	55	7.786	54.861	8.806	1.00	11.72	6	C
ATOM	427	CE2	PHE	A	55	8.345	52.564	8.372	1.00	13.77	6	C
ATOM	428	CZ	PHE	A	55	8.485	53.705	9.134	1.00	13.93	6	C
ATOM	429	C	PHE	A	55	7.793	53.901	4.107	1.00	11.18	6	C
ATOM	430	O	PHE	A	55	8.914	54.384	4.344	1.00	11.64	8	O
ATOM	431	N	ILE	A	56	7.694	52.778	3.413	1.00	9.30	7	N
ATOM	432	CA	ILE	A	56	8.772	52.040	2.820	1.00	10.44	6	C
ATOM	433	CB	ILE	A	56	8.350	50.766	2.043	1.00	12.03	6	C
ATOM	434	CG2	ILE	A	56	9.595	50.037	1.526	1.00	11.62	6	C
ATOM	435	CG1	ILE	A	56	7.507	49.761	2.823	1.00	13.57	6	C
ATOM	436	CD1	ILE	A	56	8.161	49.397	4.141	1.00	16.82	6	C
ATOM	437	C	ILE	A	56	9.521	52.936	1.813	1.00	10.94	6	C
ATOM	438	O	ILE	A	56	10.737	53.141	2.008	1.00	10.83	8	O
ATOM	439	N	THR	A	57	8.820	53.526	0.843	1.00	10.32	7	N
ATOM	440	CA	THR	A	57	9.547	54.292	−0.177	1.00	15.45	6	C
ATOM	441	CB	THR	A	57	8.786	54.444	−1.513	1.00	15.05	6	C
ATOM	442	OG1	THR	A	57	7.636	55.254	−1.248	1.00	17.59	8	O
ATOM	443	CG2	THR	A	57	8.341	53.042	−1.938	1.00	15.90	6	C
ATOM	444	C	THR	A	57	10.046	55.637	0.282	1.00	18.09	6	C
ATOM	445	O	THR	A	57	11.145	56.074	−0.104	1.00	17.72	8	O
ATOM	446	N	GLU	A	58	9.248	56.355	1.064	1.00	18.70	7	N
ATOM	447	CA	GLU	A	58	9.648	57.717	1.436	1.00	21.41	6	C
ATOM	448	CB	GLU	A	58	8.422	58.659	1.495	1.00	23.68	6	C
ATOM	449	CG	GLU	A	58	7.668	58.633	0.164	1.00	28.38	6	C
ATOM	450	CD	GLU	A	58	8.510	58.884	−1.083	1.00	32.18	6	C
ATOM	451	OE1	GLU	A	58	9.164	59.955	−1.157	1.00	34.50	8	O
ATOM	452	OE2	GLU	A	58	8.542	58.044	−2.033	1.00	31.90	8	O
ATOM	453	C	GLU	A	58	10.458	57.767	2.715	1.00	20.49	6	C
ATOM	454	O	GLU	A	58	11.158	58.771	2.852	1.00	19.41	8	O
ATOM	455	N	LYS	A	59	10.333	56.793	3.610	1.00	17.03	7	N
ATOM	456	CA	LYS	A	59	11.082	56.882	4.860	1.00	18.11	6	C
ATOM	457	CB	LYS	A	59	10.157	56.735	6.085	1.00	20.27	6	C
ATOM	458	CG	LYS	A	59	9.242	57.974	6.156	1.00	25.90	6	C
ATOM	459	CD	LYS	A	59	8.467	58.103	7.454	1.00	31.51	6	C
ATOM	460	CE	LYS	A	59	7.799	59.461	7.620	1.00	33.05	6	C
ATOM	461	NZ	LYS	A	59	6.928	59.580	8.833	1.00	33.55	7	N
ATOM	462	C	LYS	A	59	12.227	55.877	4.872	1.00	16.26	6	C
ATOM	463	O	LYS	A	59	13.411	56.261	4.886	1.00	14.64	8	O
ATOM	464	N	ILE	A	60	11.861	54.602	4.787	1.00	13.46	7	N
ATOM	465	CA	ILE	A	60	12.891	53.543	4.870	1.00	12.61	6	C
ATOM	466	CB	ILE	A	60	12.205	52.176	4.758	1.00	12.63	6	C
ATOM	467	CG2	ILE	A	60	13.152	50.999	4.855	1.00	14.47	6	C
ATOM	468	CG1	ILE	A	60	11.078	52.045	5.811	1.00	13.49	6	C
ATOM	469	CD1	ILE	A	60	11.557	52.160	7.226	1.00	15.68	6	C
ATOM	470	C	ILE	A	60	13.933	53.683	3.769	1.00	12.10	6	C
ATOM	471	O	ILE	A	60	15.130	53.686	4.030	1.00	11.15	8	O
ATOM	472	N	ARG	A	61	13.477	53.685	2.531	1.00	11.05	7	N
ATOM	473	CA	ARG	A	61	14.398	53.702	1.390	1.00	14.35	6	C
ATOM	474	CB	ARG	A	61	13.613	53.280	0.121	1.00	12.92	6	C
ATOM	475	CG	ARG	A	61	13.408	51.765	0.293	1.00	15.09	6	C
ATOM	476	CD	ARG	A	61	12.740	51.100	−0.894	1.00	14.74	6	C
ATOM	477	NE	ARG	A	61	12.694	49.638	−0.750	1.00	10.39	7	N
ATOM	478	CZ	ARG	A	61	12.155	48.865	−1.683	1.00	10.84	6	C
ATOM	479	NH1	ARG	A	61	11.705	49.379	−2.843	1.00	8.51	7	N
ATOM	480	NH2	ARG	A	61	12.149	47.541	−1.520	1.00	7.77	7	N
ATOM	481	C	ARG	A	61	15.230	54.952	1.199	1.00	12.68	6	C
ATOM	482	O	ARG	A	61	16.126	54.985	0.379	1.00	12.57	8	O
ATOM	483	N	LYS	A	62	14.965	56.045	1.874	1.00	11.92	7	N
ATOM	484	CA	LYS	A	62	15.767	57.215	1.937	1.00	15.99	6	C
ATOM	485	CB	LYS	A	62	14.866	58.469	2.069	1.00	18.60	6	C
ATOM	486	CG	LYS	A	62	14.165	58.660	0.733	1.00	21.84	6	C
ATOM	487	CD	LYS	A	62	13.529	60.019	0.531	1.00	25.52	6	C
ATOM	488	CE	LYS	A	62	12.694	59.946	−0.762	1.00	25.02	6	C
ATOM	489	NZ	LYS	A	62	12.156	61.305	−1.045	1.00	27.48	7	N
ATOM	490	C	LYS	A	62	16.820	57.155	3.057	1.00	17.44	6	C
ATOM	491	O	LYS	A	62	17.554	58.146	3.135	1.00	17.35	8	O
ATOM	492	N	MET	A	63	16.892	56.117	3.867	1.00	14.00	7	N
ATOM	493	CA	MET	A	63	17.923	56.000	4.889	1.00	16.24	6	C
ATOM	494	CB	MET	A	63	17.312	55.433	6.183	1.00	17.88	6	C
ATOM	495	CG	MET	A	63	16.270	56.338	6.811	1.00	21.60	6	C
ATOM	496	SD	MET	A	63	15.470	55.691	8.306	1.00	20.40	16	S
ATOM	497	CE	MET	A	63	14.362	54.509	7.598	1.00	24.10	6	C
ATOM	498	C	MET	A	63	19.041	55.086	4.400	1.00	14.86	6	C
ATOM	499	O	MET	A	63	18.889	53.879	4.279	1.00	11.39	8	O
ATOM	500	N	PRO	A	64	20.235	55.621	4.123	1.00	16.04	7	N
ATOM	501	CD	PRO	A	64	20.544	57.076	4.204	1.00	16.05	6	C
ATOM	502	CA	PRO	A	64	21.320	54.831	3.549	1.00	16.25	6	C
ATOM	503	CB	PRO	A	64	22.349	55.886	3.119	1.00	17.65	6	C
ATOM	504	CG	PRO	A	64	22.041	57.059	4.001	1.00	18.37	6	C
ATOM	505	CG	PRO	A	64	21.892	53.725	4.391	1.00	16.20	6	C
ATOM	506	O	PRO	A	64	22.415	52.724	3.846	1.00	17.51	8	O
ATOM	507	N	GLU	A	65	21.774	53.746	5.713	1.00	16.16	7	N
ATOM	508	CA	GLU	A	65	22.214	52.697	6.620	1.00	19.24	6	C
ATOM	509	CB	GLU	A	65	22.275	53.230	8.060	1.00	21.22	6	C
ATOM	510	CG	GLU	A	65	22.899	54.616	8.078	1.00	25.48	6	C
ATOM	511	CD	GLU	A	65	21.970	55.758	7.731	1.00	30.11	6	C
ATOM	512	OE1	GLU	A	65	20.719	55.794	7.576	1.00	26.69	8	O
ATOM	513	OE2	GLU	A	65	22.562	56.925	7.697	1.00	35.08	8	O
ATOM	514	C	GLU	A	65	21.322	51.462	6.576	1.00	18.67	6	C
ATOM	515	O	GLU	A	65	21.812	50.337	6.859	1.00	17.95	8	O
ATOM	516	N	ILE	A	66	20.094	51.634	6.036	1.00	15.76	7	N
ATOM	517	CA	ILE	A	66	19.264	50.426	5.886	1.00	15.12	6	C
ATOM	518	CB	ILE	A	66	17.761	50.790	6.040	1.00	15.29	6	C
ATOM	519	CG2	ILE	A	66	16.985	49.503	5.763	1.00	17.90	6	C
ATOM	520	CG1	ILE	A	66	17.536	51.382	7.403	1.00	15.51	6	C
ATOM	521	CD1	ILE	A	66	16.130	51.794	7.783	1.00	18.15	6	C
ATOM	522	C	ILE	A	66	19.547	49.790	4.557	1.00	15.35	6	C
ATOM	523	O	ILE	A	66	19.500	50.521	3.558	1.00	16.62	8	O
ATOM	524	N	GLN	A	67	19.964	48.553	4.453	1.00	17.21	7	N
ATOM	525	CA	GLN	A	67	20.439	47.860	3.282	1.00	19.06	6	C
ATOM	526	CB	GLN	A	67	21.783	47.155	3.681	1.00	22.67	6	C
ATOM	527	CG	GLN	A	67	22.821	48.236	4.024	1.00	27.17	6	C
ATOM	528	CD	GLN	A	67	24.172	47.665	4.393	1.00	29.47	6	C
ATOM	529	OE1	GLN	A	67	25.008	48.411	4.916	1.00	30.95	8	O
ATOM	530	NE2	GLN	A	67	24.408	46.398	4.137	1.00	28.71	7	N
ATOM	531	C	GLN	A	67	19.599	45.747	2.673	1.00	20.41	6	C
ATOM	532	O	GLN	A	67	19.769	46.389	1.495	1.00	21.52	8	O
ATOM	533	N	MET	A	68	18.877	45.948	3.425	1.00	18.04	7	N
ATOM	534	CA	MET	A	68	17.961	44.941	2.966	1.00	16.99	6	C
ATOM	535	CB	MET	A	68	18.584	43.560	2.923	1.00	19.00	6	C
ATOM	536	CG	MET	A	68	18.006	42.708	1.809	1.00	25.20	6	C
ATOM	537	SD	MET	A	68	18.507	40.980	1.906	1.00	32.29	16	S
ATOM	538	CE	MET	A	68	20.191	41.033	1.269	1.00	31.84	6	C
ATOM	539	C	MET	A	68	16.753	44.876	3.930	1.00	14.82	6	C
ATOM	540	O	MET	A	68	16.955	44.821	5.156	1.00	9.54	8	O
ATOM	541	N	THR	A	69	15.567	44.888	3.325	1.00	10.34	7	N
ATOM	542	CA	THR	A	69	14.343	44.824	4.099	1.00	11.13	6	C
ATOM	543	CB	THR	A	69	13.513	46.151	4.085	1.00	11.22	6	C
ATOM	544	OG1	THR	A	69	13.145	46.401	2.740	1.00	11.52	8	O
ATOM	545	CG2	THR	A	69	14.291	47.328	4.617	1.00	10.08	6	C
ATOM	546	C	THR	A	69	13.428	43.733	3.590	1.00	12.72	6	C
ATOM	547	O	THR	A	69	13.574	43.310	2.431	1.00	12.83	8	O
ATOM	548	N	SER	A	70	12.650	43.124	4.475	1.00	10.14	7	N
ATOM	549	CA	SER	A	70	11.693	42.093	4.182	1.00	8.64	6	C
ATOM	550	CB	SER	A	70	12.094	40.688	4.647	1.00	8.17	6	C
ATOM	551	OG	SER	A	70	11.039	39.830	4.251	1.00	11.27	8	O
ATOM	552	C	SER	A	70	10.464	42.513	5.055	1.00	12.16	6	C
ATOM	553	O	SER	A	70	10.659	42.602	6.288	1.00	9.70	8	O
ATOM	554	N	THR	A	71	9.352	42.753	4.380	1.00	10.49	7	N
ATOM	555	CA	THR	A	71	8.153	43.198	5.110	1.00	11.09	6	C
ATOM	556	CB	THR	A	71	7.587	44.481	4.499	1.00	11.77	6	C
ATOM	557	OG1	THR	A	71	8.593	45.476	4.690	1.00	10.42	8	O
ATOM	558	CG2	THR	A	71	6.295	45.014	5.189	1.00	13.37	6	C
ATOM	559	C	THR	A	71	7.092	42.123	5.214	1.00	10.51	6	C
ATOM	560	O	THR	A	71	6.771	41.472	4.217	1.00	10.60	8	O
ATOM	561	N	MET	A	72	6.591	41.918	6.423	1.00	8.76	7	N
ATOM	562	CA	MET	A	72	5.484	40.937	6.575	1.00	11.11	6	C
ATOM	563	CB	MET	A	72	5.816	39.916	7.651	1.00	13.22	6	C
ATOM	564	CG	MET	A	72	6.324	38.626	6.987	1.00	21.65	6	C
ATOM	565	SD	MET	A	72	7.682	37.932	7.913	1.00	27.13	16	S
ATOM	566	CE	MET	A	72	9.041	38.835	7.191	1.00	25.46	6	C
ATOM	567	C	MET	A	72	4.216	41.662	7.019	1.00	10.65	6	C
ATOM	568	O	MET	A	72	4.247	42.322	8.052	1.00	8.92	8	O
ATOM	569	N	ILE	A	73	3.140	41.593	6.255	1.00	10.57	7	N
ATOM	570	CA	ILE	A	73	1.905	42.309	6.581	1.00	8.83	6	C
ATOM	571	CB	ILE	A	73	1.359	42.913	5.279	1.00	8.76	6	C
ATOM	572	CG2	ILE	A	73	0.061	43.700	5.504	1.00	7.15	6	C
ATOM	573	CG1	ILE	A	73	2.472	43.768	4.604	1.00	8.63	6	C
ATOM	574	CD1	ILE	A	73	2.028	44.206	3.186	1.00	8.44	6	C
ATOM	575	C	ILE	A	73	0.877	41.401	7.223	1.00	10.71	6	C
ATOM	576	O	ILE	A	73	0.582	40.281	6.799	1.00	12.18	8	O
ATOM	577	N	ALA	A	74	0.305	41.845	8.320	1.00	11.15	7	N
ATOM	578	CA	ALA	A	74	−0.650	41.052	9.086	1.00	11.38	6	C
ATOM	579	CB	ALA	A	74	−0.976	41.637	10.453	1.00	8.81	6	C
ATOM	580	C	ALA	A	74	−1.900	40.883	8.226	1.00	13.75	6	C
ATOM	581	O	ALA	A	74	−2.334	41.884	7.674	1.00	9.08	8	O
ATOM	582	N	ILE	A	75	−2.464	39.673	8.299	1.00	14.79	7	N
ATOM	583	CA	ILE	A	75	−3.640	39.439	7.473	1.00	20.01	6	C
ATOM	584	CB	ILE	A	75	−3.364	38.627	6.190	1.00	20.01	6	C
ATOM	585	CG2	ILE	A	75	−2.744	39.438	5.070	1.00	20.74	6	C
ATOM	586	CG1	ILE	A	75	−2.502	37.432	6.567	1.00	21.65	6	C
ATOM	587	CD1	ILE	A	75	−2.352	36.330	5.553	1.00	23.37	6	C
ATOM	588	C	ILE	A	75	−4.656	38.685	8.333	1.00	21.16	6	C
ATOM	589	O	ILE	A	75	−4.293	38.301	9.452	1.00	19.96	8	O
ATOM	590	OT	ILE	A	75	−5.709	38.325	7.766	1.00	24.56	8	O
ATOM	591	CB	VAL	B	2	15.203	36.576	27.110	1.00	10.81	6	C
ATOM	592	CG1	VAL	B	2	15.489	36.311	25.630	1.00	10.60	6	C
ATOM	593	CG2	VAL	B	2	16.487	36.270	27.887	1.00	9.64	6	C
ATOM	594	C	VAL	B	2	13.491	38.209	26.316	1.00	9.81	6	C
ATOM	595	O	VAL	B	2	12.467	37.543	26.535	1.00	8.96	8	O
ATOM	596	N	VAL	B	2	14.395	38.441	28.691	1.00	10.90	7	N
ATOM	597	CA	VAL	B	2	14.702	38.012	27.247	1.00	9.65	6	C
ATOM	598	N	THR	B	3	13.641	39.006	25.278	1.00	8.35	7	N
ATOM	599	CA	THR	B	3	12.571	39.256	24.318	1.00	7.94	6	C
ATOM	600	CB	THR	B	3	12.241	40.729	24.045	1.00	8.58	6	C
ATOM	601	OG1	THR	B	3	11.836	41.393	25.244	1.00	8.95	8	O
ATOM	602	CG2	THR	B	3	11.075	40.881	23.044	1.00	6.74	6	C
ATOM	603	C	THR	B	3	13.026	38.662	22.981	1.00	10.25	6	C
ATOM	604	O	THR	B	3	14.248	38.762	22.725	1.00	6.93	8	O
ATOM	605	N	ALA	B	4	12.186	37.851	22.328	1.00	7.68	7	N
ATOM	606	CA	ALA	B	4	12.535	37.308	21.033	1.00	8.07	6	C
ATOM	607	CB	ALA	B	4	13.073	35.859	21.152	1.00	5.87	6	C
ATOM	608	C	ALA	B	4	11.315	37.351	20.096	1.00	9.20	6	C
ATOM	609	O	ALA	B	4	10.154	37.299	20.559	1.00	9.29	8	O
ATOM	610	N	PHE	B	5	11.596	37.401	18.802	1.00	6.28	7	N
ATOM	611	CA	PHE	B	5	10.592	37.272	17.760	1.00	8.35	6	C
ATOM	612	CB	PHE	B	5	10.612	38.420	16.752	1.00	6.55	6	C
ATOM	613	CG	PHE	B	5	10.185	39.729	17.409	1.00	7.88	6	C
ATOM	614	CD1	PHE	B	5	11.087	40.520	18.080	1.00	6.54	6	C
ATOM	615	CD2	PHE	B	5	8.853	40.140	17.310	1.00	8.11	6	C
ATOM	616	CE1	PHE	B	5	10.653	41.713	18.654	1.00	8.22	6	C
ATOM	617	CE2	PHE	B	5	8.436	41.346	17.873	1.00	7.71	6	C
ATOM	618	CZ	PHE	B	5	9.335	42.140	18.531	1.00	7.27	6	C
ATOM	619	C	PHE	B	5	10.793	35.963	16.987	1.00	7.00	6	C
ATOM	620	O	PHE	B	5	11.904	35.640	16.514	1.00	6.91	8	O
ATOM	621	N	ILE	B	6	9.771	35.121	16.971	1.00	7.10	7	N
ATOM	622	CA	ILE	B	6	9.898	33.824	16.270	1.00	7.30	6	C
ATOM	623	CB	ILE	B	6	9.190	32.706	17.057	1.00	7.52	6	C
ATOM	624	CG2	ILE	B	6	9.353	31.396	16.284	1.00	6.04	6	C
ATOM	625	CG1	ILE	B	6	9.708	32.559	18.504	1.00	6.96	6	C
ATOM	626	CD1	ILE	B	6	8.811	31.481	19.176	1.00	12.29	6	C
ATOM	627	C	ILE	B	6	9.210	33.940	14.917	1.00	10.08	6	C
ATOM	628	O	ILE	B	6	7.991	34.222	14.923	1.00	10.99	8	O
ATOM	629	N	LEU	B	7	9.882	33.668	13.819	1.00	11.51	7	N
ATOM	630	CA	LEU	B	7	9.237	33.678	12.492	1.00	12.43	6	C
ATOM	631	CB	LEU	B	7	10.173	34.267	11.447	1.00	12.72	6	C
ATOM	632	CG	LEU	B	7	10.630	35.703	11.722	1.00	17.00	6	C
ATOM	633	CD1	LEU	B	7	11.870	36.078	10.883	1.00	17.22	6	C
ATOM	634	CD2	LEU	B	7	9.485	36.665	11.508	1.00	18.19	6	C
ATOM	635	C	LEU	B	7	8.919	32.224	12.235	1.00	14.19	6	C
ATOM	636	O	LEU	B	7	9.746	31.328	12.500	1.00	13.47	8	O
ATOM	637	N	MET	B	8	7.688	31.875	11.846	1.00	13.99	7	N
ATOM	638	CA	MET	B	8	7.306	30.486	11.708	1.00	13.46	6	C
ATOM	639	CB	MET	B	8	6.368	30.028	12.835	1.00	16.11	6	C
ATOM	640	CG	MET	B	8	6.691	30.264	14.271	1.00	18.68	6	C
ATOM	641	SD	MET	B	8	5.428	29.803	15.535	1.00	20.37	16	S
ATOM	642	CE	MET	B	8	4.118	29.468	14.437	1.00	17.84	6	C
ATOM	643	C	MET	B	8	6.609	30.158	10.390	1.00	15.90	6	C
ATOM	644	O	MET	B	8	5.832	30.941	9.852	1.00	14.92	8	O
ATOM	645	N	VAL	B	9	6.857	28.937	9.914	1.00	16.65	7	N
ATOM	646	CA	VAL	B	9	6.126	28.443	8.730	1.00	16.44	6	C
ATOM	647	CB	VAL	B	9	7.072	27.868	7.674	1.00	17.96	6	C
ATOM	648	CG1	VAL	B	9	6.361	27.078	6.558	1.00	16.89	6	C
ATOM	649	CG2	VAL	B	9	7.856	29.021	7.048	1.00	17.27	6	C
ATOM	650	C	VAL	B	9	5.258	27.333	9.285	1.00	17.36	6	C
ATOM	651	O	VAL	B	9	5.868	26.512	9.992	1.00	18.71	8	O
ATOM	652	N	THR	B	10	3.947	27.306	9.086	1.00	16.83	7	N
ATOM	653	CA	THR	B	10	3.149	26.199	9.609	1.00	16.97	6	C
ATOM	654	CB	THR	B	10	1.860	26.674	10.313	1.00	17.72	6	C
ATOM	655	OG1	THR	B	10	1.014	27.388	9.376	1.00	16.78	8	O
ATOM	656	CG2	THR	B	10	2.219	27.659	11.422	1.00	15.85	6	C
ATOM	657	C	THR	B	10	2.690	25.289	8.460	1.00	18.72	6	C
ATOM	658	O	THR	B	10	2.941	25.560	7.279	1.00	19.05	8	O
ATOM	659	N	ALA	B	11	2.101	24.137	8.755	1.00	20.00	7	N
ATOM	660	CA	ALA	B	11	1.480	23.354	7.657	1.00	20.04	6	C
ATOM	661	CB	ALA	B	11	0.916	22.098	8.243	1.00	20.18	6	C
ATOM	662	C	ALA	B	11	0.384	24.233	7.072	1.00	22.64	6	C
ATOM	663	O	ALA	B	11	−0.259	24.987	7.818	1.00	22.86	8	O
ATOM	664	N	ALA	B	12	0.184	24.225	5.759	1.00	24.51	7	N
ATOM	665	CA	ALA	B	12	−0.856	25.096	5.158	1.00	24.49	6	C
ATOM	666	CB	ALA	B	12	−0.865	24.883	3.649	1.00	23.68	6	C
ATOM	667	C	ALA	B	12	−2.233	24.886	5.770	1.00	22.73	6	C
ATOM	668	O	ALA	B	12	−2.587	23.826	6.290	1.00	22.75	8	O
ATOM	669	N	GLY	B	13	−2.983	25.998	5.943	1.00	23.23	7	N
ATOM	670	CA	GLY	B	13	−4.307	25.962	6.557	1.00	20.92	6	C
ATOM	671	C	GLY	B	13	−4.310	25.750	8.059	1.00	22.76	6	C
ATOM	672	O	GLY	B	13	−5.358	25.433	8.643	1.00	23.11	8	O
ATOM	673	N	LYS	B	14	−3.158	25.825	8.750	1.00	20.91	7	N
ATOM	674	CA	LYS	B	14	−3.162	25.571	10.173	1.00	20.15	6	C
ATOM	675	CB	LYS	B	14	−2.198	24.425	10.520	1.00	21.56	6	C
ATOM	676	CG	LYS	B	14	−2.514	23.101	9.799	1.00	23.27	6	C
ATOM	677	CD	LYS	B	14	−3.830	22.532	10.369	1.00	25.36	6	C
ATOM	678	CE	LYS	B	14	−4.059	21.130	9.715	1.00	27.62	6	C
ATOM	679	NZ	LYS	B	14	−5.327	20.576	10.272	1.00	29.04	7	N
ATOM	680	C	LYS	B	14	−2.790	26.865	10.903	1.00	18.58	6	C
ATOM	681	O	LYS	B	14	−2.848	26.865	12.120	1.00	18.56	8	O
ATOM	682	N	GLU	B	15	−2.503	27.914	10.171	1.00	19.78	7	N
ATOM	683	CA	GLU	B	15	−1.978	29.156	10.731	1.00	21.26	6	C
ATOM	684	CB	GLU	B	15	−1.998	30.269	9.681	1.00	22.71	6	C
ATOM	685	CG	GLU	B	15	−0.900	30.330	8.665	1.00	25.31	6	C
ATOM	686	CD	GLU	B	15	−1.205	29.466	7.441	1.00	28.76	6	C
ATOM	687	OE1	GLU	B	15	−2.177	28.683	7.478	1.00	29.58	8	O
ATOM	688	OE2	GLU	B	15	−0.430	29.519	6.444	1.00	29.72	8	O
ATOM	689	C	GLU	B	15	−2.786	29.696	11.894	1.00	21.72	6	C
ATOM	690	O	GLU	B	15	−2.302	29.933	13.001	1.00	21.00	8	O
ATOM	691	N	ARG	B	16	−4.093	29.876	11.651	1.00	22.71	7	N
ATOM	692	CA	ARG	B	16	−5.022	30.366	12.661	1.00	22.83	6	C
ATOM	693	CB	ARG	B	16	−6.422	30.552	12.073	1.00	26.64	6	C
ATOM	694	CG	ARG	B	16	−6.635	31.630	11.048	1.00	30.52	6	C
ATOM	695	CD	ARG	B	16	−6.555	33.048	11.602	1.00	35.34	6	C
ATOM	696	NE	ARG	B	16	−6.384	33.959	10.475	1.00	39.66	7	N
ATOM	697	CZ	ARG	B	16	−6.162	35.258	10.382	1.00	41.31	6	C
ATOM	698	NH1	ARG	B	16	−6.070	36.144	11.364	1.00	42.11	7	N
ATOM	699	NH2	ARG	B	16	−6.050	35.658	9.104	1.00	41.95	7	N
ATOM	700	C	ARG	B	16	−5.125	29.436	13.851	1.00	21.36	6	C
ATOM	701	O	ARG	B	16	−5.111	29.904	15.001	1.00	21.13	8	O
ATOM	702	N	GLU	B	17	−5.120	28.107	13.675	1.00	19.62	7	N
ATOM	703	CA	GLU	B	17	−5.244	27.313	14.924	1.00	19.14	6	C
ATOM	704	CB	GLU	B	17	−5.774	25.898	14.657	1.00	22.22	6	C
ATOM	705	CG	GLU	B	17	−4.832	25.235	13.662	1.00	26.79	6	C
ATOM	706	CD	GLU	B	17	−4.940	23.734	13.633	1.00	31.06	6	C
ATOM	707	OE1	GLU	B	17	−6.094	23.198	13.654	1.00	33.97	8	O
ATOM	708	OE2	GLU	B	17	−3.794	23.223	13.550	1.00	32.92	8	O
ATOM	709	C	GLU	B	17	−3.922	27.312	15.672	1.00	16.82	6	C
ATOM	710	O	GLU	B	17	−3.902	27.254	16.914	1.00	16.12	8	O
ATOM	711	N	VAL	B	18	−2.801	27.360	14.949	1.00	16.92	7	N
ATOM	712	CA	VAL	B	18	−1.508	27.472	15.634	1.00	16.56	6	C
ATOM	713	CB	VAL	B	18	−0.319	27.395	14.663	1.00	16.85	6	C
ATOM	714	CG1	VAL	B	18	1.050	27.672	15.311	1.00	16.29	6	C
ATOM	715	CG2	VAL	B	18	−0.228	25.929	14.201	1.00	16.98	6	C
ATOM	716	C	VAL	B	18	−1.548	28.791	16.416	1.00	14.71	6	C
ATOM	717	O	VAL	B	18	−1.156	28.849	17.560	1.00	13.81	8	O
ATOM	718	N	MET	B	19	−1.977	29.869	15.764	1.00	15.18	7	N
ATOM	719	CA	MET	B	19	−2.023	31.157	16.469	1.00	16.64	6	C
ATOM	720	CB	MET	B	19	−2.587	32.281	15.598	1.00	17.04	6	C
ATOM	721	CG	MET	B	19	−2.598	33.599	16.417	1.00	20.44	6	C
ATOM	722	SD	MET	B	19	−2.923	34.981	15.256	1.00	23.31	16	S
ATOM	723	CE	MET	B	19	−1.290	34.646	14.586	1.00	24.64	6	C
ATOM	724	C	MET	B	19	−2.802	31.103	17.757	1.00	16.32	6	C
ATOM	725	O	MET	B	19	−2.336	31.571	18.803	1.00	13.62	8	O
ATOM	726	N	GLU	B	20	−3.983	30.445	17.736	1.00	18.19	7	N
ATOM	727	CA	GLU	B	20	−4.773	30.394	18.973	1.00	17.75	6	C
ATOM	728	CB	GLU	B	20	−6.220	29.959	18.669	1.00	20.39	6	C
ATOM	729	CG	GLU	B	20	−6.902	30.808	17.607	1.00	22.11	6	C
ATOM	730	CD	GLU	B	20	−6.977	32.322	17.735	1.00	25.01	6	C
ATOM	731	OE1	GLU	B	20	−7.101	32.971	18.786	1.00	22.59	8	O
ATOM	732	OE2	GLU	B	20	−6.869	33.012	16.673	1.00	27.61	8	O
ATOM	733	C	GLU	B	20	−4.070	29.571	20.027	1.00	17.39	6	C
ATOM	734	O	GLU	B	20	−4.083	30.001	21.202	1.00	15.65	8	O
ATOM	735	N	LYS	B	21	−3.400	28.447	19.654	1.00	15.60	7	N
ATOM	736	CA	LYS	B	21	−2.647	27.767	20.701	1.00	14.17	6	C
ATOM	737	CB	LYS	B	21	−1.968	26.465	20.239	1.00	17.22	6	C
ATOM	738	CG	LYS	B	21	−3.009	25.422	19.806	1.00	20.24	6	C
ATOM	739	CD	LYS	B	21	−2.479	24.019	19.721	1.00	20.81	6	C
ATOM	740	CE	LYS	B	21	−3.531	23.001	19.287	1.00	23.49	6	C
ATOM	741	NZ	LYS	B	21	−3.546	22.690	17.821	1.00	24.31	7	N
ATOM	742	C	LYS	B	21	−1.559	28.704	21.255	1.00	12.69	6	C
ATOM	743	O	LYS	B	21	−1.277	28.673	22.450	1.00	9.62	8	O
ATOM	744	N	LEU	B	22	−0.810	29.387	20.376	1.00	12.07	7	N
ATOM	745	CA	LEU	B	22	0.286	30.235	20.919	1.00	10.01	6	C
ATOM	746	CB	LEU	B	22	0.994	30.891	19.717	1.00	10.07	6	C
ATOM	747	CG	LEU	B	22	1.765	29.929	18.772	1.00	11.87	6	C
ATOM	748	CD1	LEU	B	22	2.156	30.691	17.484	1.00	10.37	6	C
ATOM	749	CD2	LEU	B	22	2.966	29.369	19.452	1.00	9.92	6	C
ATOM	750	C	LEU	B	22	−0.229	31.325	21.840	1.00	10.76	6	C
ATOM	751	O	LEU	B	22	0.328	31.647	22.890	1.00	11.14	8	O
ATOM	752	N	LEU	B	23	−1.358	31.960	21.525	1.00	9.40	7	N
ATOM	753	CA	LEU	B	23	−1.921	33.024	22.345	1.00	11.73	6	C
ATOM	754	CB	LEU	B	23	−3.079	33.727	21.621	1.00	11.69	6	C
ATOM	755	CG	LEU	B	23	−2.745	34.512	20.356	1.00	11.81	6	C
ATOM	756	CD1	LEU	B	23	−4.016	34.922	19.616	1.00	11.79	6	C
ATOM	757	CD2	LEU	B	23	−1.938	35.790	20.695	1.00	12.26	6	C
ATOM	758	C	LEU	B	23	−2.357	32.553	23.727	1.00	13.43	6	C
ATOM	759	O	LEU	B	23	−2.425	33.433	24.579	1.00	13.81	8	O
ATOM	760	N	ALA	B	24	−2.580	31.252	23.978	1.00	14.24	7	N
ATOM	761	CA	ALA	B	24	−2.824	30.782	25.339	1.00	15.64	6	C
ATOM	762	CB	ALA	B	24	−3.502	29.408	25.345	1.00	15.75	6	C
ATOM	763	C	ALA	B	24	−1.514	30.588	26.104	1.00	16.64	6	C
ATOM	764	O	ALA	B	24	−1.600	30.289	27.290	1.00	17.40	8	O
ATOM	765	N	MET	B	25	−0.349	30.681	25.462	1.00	14.70	7	N
ATOM	766	CA	MET	B	25	0.901	30.516	26.249	1.00	15.45	6	C
ATOM	767	CB	MET	B	25	2.001	29.980	25.331	1.00	14.21	6	C
ATOM	768	CG	MET	B	25	1.578	28.734	24.564	1.00	15.72	6	C
ATOM	769	SD	MET	B	25	2.874	28.259	23.361	1.00	15.01	16	S
ATOM	770	CE	MET	B	25	2.028	26.880	22.566	1.00	14.16	6	C
ATOM	771	C	MET	B	25	1.267	31.832	26.875	1.00	13.99	6	C
ATOM	772	O	MET	B	25	1.300	32.872	26.197	1.00	13.82	8	O
ATOM	773	N	PRO	B	26	1.573	31.882	28.180	1.00	15.20	7	N
ATOM	774	CD	PRO	B	26	1.680	30.670	29.044	1.00	15.96	6	C
ATOM	775	CA	PRO	B	26	1.948	33.094	28.857	1.00	14.72	6	C
ATOM	776	CB	PRO	B	26	2.160	32.681	30.320	1.00	15.60	6	C
ATOM	777	CG	PRO	B	26	2.374	31.223	30.279	1.00	15.14	6	C
ATOM	778	C	PRO	B	26	3.255	33.744	28.338	1.00	14.07	6	C
ATOM	779	O	PRO	B	26	3.350	34.960	28.438	1.00	13.92	8	O
ATOM	780	N	GLU	B	27	4.170	33.002	27.747	1.00	11.08	7	N
ATOM	781	CA	GLU	B	27	5.391	33.603	27.183	1.00	13.20	6	C
ATOM	782	CB	GLU	B	27	6.371	32.491	26.747	1.00	13.28	6	C
ATOM	783	CG	GLU	B	27	6.822	31.666	27.944	1.00	16.85	6	C
ATOM	784	CD	GLU	B	27	6.036	30.398	28.231	1.00	18.72	6	C
ATOM	785	OE1	GLU	B	27	4.890	30.149	27.819	1.00	18.84	8	O
ATOM	786	OE2	GLU	B	27	6.595	29.540	28.940	1.00	19.28	8	O
ATOM	787	C	GLU	B	27	5.057	34.427	25.939	1.00	11.33	6	C
ATOM	788	O	GLU	B	27	5.821	35.259	25.512	1.00	11.54	8	O
ATOM	789	N	VAL	B	28	3.990	34.102	25.231	1.00	10.97	7	N
ATOM	790	CA	VAL	B	28	3.634	34.767	23.972	1.00	10.37	6	C
ATOM	791	CB	VAL	B	28	2.695	33.897	23.121	1.00	10.11	6	C
ATOM	792	CG1	VAL	B	28	2.226	34.564	21.814	1.00	7.99	6	C
ATOM	793	CG2	VAL	B	28	3.397	32.551	22.912	1.00	7.50	6	C
ATOM	794	C	VAL	B	28	2.948	36.083	24.254	1.00	11.91	6	C
ATOM	795	O	VAL	B	28	1.843	36.130	24.822	1.00	13.08	8	O
ATOM	796	N	LYS	B	29	3.565	37.163	23.832	1.00	10.47	7	N
ATOM	797	CA	LYS	B	29	3.011	38.482	24.072	1.00	10.88	6	C
ATOM	798	CB	LYS	B	29	4.110	39.487	24.379	1.00	11.16	5	C
ATOM	799	CG	LYS	B	29	5.048	38.925	25.483	1.00	12.65	6	C
ATOM	800	CD	LYS	B	29	4.298	38.989	26.830	1.00	16.71	6	C
ATOM	801	CE	LYS	B	29	4.738	37.821	27.706	1.00	19.48	6	C
ATOM	802	NZ	LYS	B	29	4.388	38.062	29.136	1.00	23.26	7	N
ATOM	803	C	LYS	B	29	2.264	38.986	22.859	1.00	11.85	6	C
ATOM	804	O	LYS	B	29	1.369	39.856	23.035	1.00	11.08	8	O
ATOM	805	N	GLU	B	30	2.695	38.590	21.651	1.00	9.93	7	N
ATOM	806	CA	GLU	B	30	1.998	39.086	20.459	1.00	9.60	6	C
ATOM	807	CB	GLU	B	30	2.546	40.384	19.899	1.00	13.47	6	C
ATOM	808	CG	GLU	B	30	2.577	41.628	20.771	1.00	11.99	6	C
ATOM	809	CD	GLU	B	30	3.193	42.838	20.116	1.00	13.20	6	C
ATOM	810	OE1	GLU	B	30	3.579	43.769	20.856	1.00	11.60	8	O
ATOM	811	OE2	GLU	B	30	3.107	42.989	18.886	1.00	13.89	8	O
ATOM	812	C	GLU	B	30	2.104	37.967	19.437	1.00	11.24	6	C
ATOM	813	O	GLU	B	30	3.137	37.255	19.467	1.00	9.55	8	O
ATOM	814	N	ALA	B	31	1.076	37.818	18.606	1.00	9.40	7	N
ATOM	815	CA	ALA	B	31	1.198	36.803	17.543	1.00	8.70	6	C
ATOM	816	CB	ALA	B	31	0.698	35.429	17.973	1.00	7.99	6	C
ATOM	817	C	ALA	B	31	0.357	37.314	16.390	1.00	9.99	6	C
ATOM	818	O	ALA	B	31	−0.761	37.841	16.609	1.00	10.67	8	O
ATOM	819	N	TYR	B	32	0.854	37.192	15.160	1.00	7.33	7	N
ATOM	820	CA	TYR	B	32	0.119	37.639	14.013	1.00	7.98	6	C
ATOM	821	CB	TYR	B	32	0.604	38.961	13.443	1.00	6.68	6	C
ATOM	822	CG	TYR	B	32	0.423	40.157	14.312	1.00	8.26	6	C
ATOM	823	CD1	TYR	B	32	−0.728	40.934	14.064	1.00	8.39	6	C
ATOM	824	CE1	TYR	B	32	−0.914	42.086	14.840	1.00	9.14	6	C
ATOM	825	CD2	TYR	B	32	1.304	40.489	15.344	1.00	6.70	6	C
ATOM	826	CE2	TYR	B	32	1.089	41.623	16.105	1.00	7.28	6	C
ATOM	827	CZ	TYR	B	32	−0.020	42.387	15.849	1.00	8.06	6	C
ATOM	828	OH	TYR	B	32	−0.272	43.545	16.575	1.00	11.13	8	O
ATOM	829	C	TYR	B	32	0.359	36.711	12.791	1.00	9.26	6	C
ATOM	830	O	TYR	B	32	1.455	36.211	12.595	1.00	7.38	8	O
ATOM	831	N	VAL	B	33	−0.774	36.442	12.119	1.00	7.76	7	N
ATOM	832	CA	VAL	B	33	−0.738	35.690	10.887	1.00	8.25	6	C
ATOM	833	CB	VAL	B	33	−2.103	35.103	10.485	1.00	9.77	6	C
ATOM	834	CG1	VAL	B	33	−1.928	34.416	9.141	1.00	9.20	6	C
ATOM	835	CG2	VAL	B	33	−2.588	34.125	11.538	1.00	10.44	6	C
ATOM	836	C	VAL	B	33	−0.313	36.695	9.830	1.00	6.92	6	C
ATOM	837	O	VAL	B	33	−0.847	37.804	9.767	1.00	8.47	8	O
ATOM	838	N	VAL	B	34	0.698	36.343	9.020	1.00	8.02	7	N
ATOM	839	CA	VAL	B	34	1.176	37.342	8.101	1.00	8.86	6	C
ATOM	840	CB	VAL	B	34	2.565	37.938	8.440	1.00	8.81	6	C
ATOM	841	CG1	VAL	B	34	2.493	38.825	9.666	1.00	8.55	6	C
ATOM	842	CG2	VAL	B	34	3.567	36.787	8.612	1.00	8.06	6	C
ATOM	843	C	VAL	B	34	1.265	36.792	6.688	1.00	11.20	6	C
ATOM	844	O	VAL	B	34	1.427	35.613	6.470	1.00	13.52	8	O
ATOM	845	N	TYR	B	35	1.323	37.793	5.807	1.00	13.07	7	N
ATOM	846	CA	TYR	B	35	1.667	37.464	4.421	1.00	15.59	6	C
ATOM	847	CB	TYR	B	35	0.814	38.417	3.594	1.00	17.52	6	C
ATOM	848	CG	TYR	B	35	1.217	38.209	2.156	1.00	21.88	6	C
ATOM	849	CD1	TYR	B	35	0.716	37.086	1.532	1.00	25.26	6	C
ATOM	850	CE1	TYR	B	35	1.050	36.814	0.212	1.00	28.20	6	C
ATOM	851	CD2	TYR	B	35	2.102	39.034	1.521	1.00	24.78	6	C
ATOM	852	CE2	TYR	B	35	2.530	38.731	0.240	1.00	26.74	6	C
ATOM	853	CZ	TYR	B	35	1.938	37.685	−0.398	1.00	28.56	6	C
ATOM	854	OH	TYR	B	35	2.277	37.427	−1.709	1.00	33.78	8	O
ATOM	855	C	TYR	B	35	3.152	37.824	4.207	1.00	16.52	6	C
ATOM	856	O	TYR	B	35	3.517	38.932	4.657	1.00	18.14	8	O
ATOM	857	N	GLY	B	36	3.904	37.025	3.511	1.00	15.07	7	N
ATOM	858	CA	GLY	B	36	5.297	37.441	3.214	1.00	18.36	6	C
ATOM	859	C	GLY	B	36	6.143	36.151	3.231	1.00	19.05	6	C
ATOM	860	O	GLY	B	36	5.557	35.061	3.058	1.00	16.65	8	O
ATOM	861	N	GLU	B	37	7.434	36.257	3.609	1.00	21.01	7	N
ATOM	862	CA	GLU	B	37	8.152	34.953	3.595	1.00	23.51	6	C
ATOM	863	CB	GLU	B	37	9.663	35.177	3.504	1.00	28.70	6	C
ATOM	864	CG	GLU	B	37	10.269	35.983	4.630	1.00	32.35	6	C
ATOM	865	CD	GLU	B	37	11.798	35.903	4.612	1.00	36.24	6	C
ATOM	866	OE1	GLU	B	37	12.437	36.685	5.372	1.00	35.75	8	O
ATOM	867	OE2	GLU	B	37	12.317	35.044	3.847	1.00	37.65	8	O
ATOM	868	C	GLU	B	37	7.845	33.981	4.714	1.00	23.07	6	C
ATOM	869	O	GLU	B	37	8.259	32.834	4.540	1.00	23.02	8	O
ATOM	870	N	TYR	B	38	7.232	34.337	5.840	1.00	21.40	7	N
ATOM	871	CA	TYR	B	38	6.879	33.361	6.889	1.00	19.67	6	C
ATOM	872	CB	TYR	B	38	7.610	33.823	8.162	1.00	20.72	6	C
ATOM	873	CG	TYR	B	38	9.064	33.414	8.146	1.00	23.64	6	C
ATOM	874	CD1	TYR	B	38	9.401	32.089	8.412	1.00	25.30	6	C
ATOM	875	CE1	TYR	B	38	10.714	31.666	8.416	1.00	26.52	6	C
ATOM	876	CD2	TYR	B	38	10.090	34.313	7.871	1.00	25.13	6	C
ATOM	877	CE2	TYR	B	38	11.410	33.895	7.884	1.00	25.61	6	C
ATOM	878	CZ	TYR	B	38	11.710	32.591	8.145	1.00	27.23	6	C
ATOM	879	OH	TYR	B	38	13.035	32.149	8.152	1.00	29.72	8	O
ATOM	880	C	TYR	B	38	5.376	33.329	7.149	1.00	17.30	6	C
ATOM	881	O	TYR	B	38	4.744	34.238	6.603	1.00	16.96	8	O
ATOM	882	N	ASP	B	39	4.742	32.399	7.856	1.00	16.10	7	N
ATOM	883	CA	ASP	B	39	3.318	32.359	8.062	1.00	15.22	6	C
ATOM	884	CB	ASP	B	39	2.879	30.893	8.284	1.00	17.21	6	C
ATOM	885	CG	ASP	B	39	2.939	30.170	6.935	1.00	19.01	6	C
ATOM	886	OD1	ASP	B	39	2.735	30.787	5.869	1.00	19.17	8	O
ATOM	887	OD2	ASP	B	39	3.263	28.976	7.028	1.00	20.31	8	O
ATOM	888	C	ASP	B	39	2.815	33.108	9.297	1.00	15.48	6	C
ATOM	889	O	ASP	B	39	1.726	33.694	9.290	1.00	13.65	8	O
ATOM	890	N	LEU	B	40	3.590	33.064	10.383	1.00	13.35	7	N
ATOM	891	CA	LEU	B	40	3.266	33.717	11.639	1.00	12.10	6	C
ATOM	892	CB	LEU	B	40	2.872	32.708	12.724	1.00	13.67	6	C
ATOM	893	CG	LEU	B	40	1.601	31.893	12.552	1.00	17.69	6	C
ATOM	894	CD1	LEU	B	40	1.329	30.939	13.715	1.00	20.32	6	C
ATOM	895	CD2	LEU	B	40	0.394	32.825	12.479	1.00	20.29	6	C
ATOM	896	C	LEU	B	40	4.471	34.470	12.223	1.00	11.17	6	C
ATOM	897	O	LEU	B	40	5.646	34.118	11.961	1.00	10.75	8	O
ATOM	898	N	ILE	B	41	4.237	35.543	12.943	1.00	8.24	7	N
ATOM	899	CA	ILE	B	41	5.339	36.230	13.626	1.00	9.66	6	C
ATOM	900	CB	ILE	B	41	5.712	37.587	13.108	1.00	12.11	6	C
ATOM	901	CG2	ILE	B	41	4.557	38.563	13.016	1.00	15.03	6	C
ATOM	902	CG1	ILE	B	41	6.735	38.248	14.096	1.00	13.84	6	C
ATOM	903	CD1	ILE	B	41	7.691	39.105	13.319	1.00	15.84	6	C
ATOM	904	C	ILE	B	41	4.851	36.269	15.074	1.00	10.80	6	C
ATOM	905	O	ILE	B	41	3.678	36.570	15.329	1.00	9.87	8	O
ATOM	906	N	VAL	B	42	5.666	35.853	16.019	1.00	9.90	7	N
ATOM	907	CA	VAL	B	42	5.269	35.779	17.415	1.00	8.61	6	C
ATOM	908	CB	VAL	B	42	5.231	34.269	17.758	1.00	11.63	6	C
ATOM	909	CG1	VAL	B	42	4.728	33.994	19.179	1.00	11.77	6	C
ATOM	910	CG2	VAL	B	42	4.389	33.446	16.776	1.00	11.85	6	C
ATOM	911	C	VAL	B	42	6.265	36.480	18.307	1.00	9.85	6	C
ATOM	912	O	VAL	B	42	7.476	36.173	18.143	1.00	9.17	8	O
ATOM	913	N	LYS	B	43	5.811	37.419	19.136	1.00	7.78	7	N
ATOM	914	CA	LYS	B	43	6.740	38.088	20.055	1.00	7.65	6	C
ATOM	915	CB	LYS	B	43	6.282	39.519	20.345	1.00	9.86	6	C
ATOM	916	CG	LYS	B	43	7.306	40.251	21.245	1.00	10.71	6	C
ATOM	917	CD	LYS	B	43	6.614	41.604	21.531	1.00	9.74	6	C
ATOM	918	CE	LYS	B	43	7.585	42.476	22.315	1.00	10.47	6	C
ATOM	919	NZ	LYS	B	43	6.920	43.783	22.618	1.00	6.81	7	N
ATOM	920	C	LYS	B	43	6.694	37.349	21.396	1.00	9.77	6	C
ATOM	921	O	LYS	B	43	5.585	37.200	21.979	1.00	8.09	8	O
ATOM	922	N	VAL	B	44	7.840	36.891	21.897	1.00	8.63	7	N
ATOM	923	CA	VAL	B	44	7.818	36.118	23.143	1.00	8.80	6	C
ATOM	924	CB	VAL	B	44	8.104	34.612	22.973	1.00	10.38	6	C
ATOM	925	CG1	VAL	B	44	7.208	33.936	21.922	1.00	8.21	6	C
ATOM	926	CG2	VAL	B	44	9.563	34.281	22.597	1.00	9.95	6	C
ATOM	927	C	VAL	B	44	8.782	36.742	24.138	1.00	9.71	6	C
ATOM	928	O	VAL	B	44	9.699	37.510	23.750	1.00	5.89	8	O
ATOM	929	N	GLU	B	45	8.479	36.528	25.418	1.00	10.09	7	N
ATOM	930	CA	GLU	B	45	9.296	37.043	26.518	1.00	13.68	6	C
ATOM	931	CB	GLU	B	45	8.689	38.315	27.137	1.00	14.51	6	C
ATOM	932	CG	GLU	B	45	8.798	39.552	26.269	1.00	18.31	6	C
ATOM	933	CD	GLU	B	45	8.037	40.752	26.792	1.00	21.50	6	C
ATOM	934	OE1	GLU	B	45	7.964	41.733	26.010	1.00	22.57	8	O
ATOM	935	OE2	GLU	B	45	7.590	40.680	27.967	1.00	20.85	8	O
ATOM	936	C	GLU	B	45	9.424	35.985	27.622	1.00	15.23	6	C
ATOM	937	O	GLU	B	45	8.491	35.243	27.941	1.00	12.79	8	O
ATOM	938	N	THR	B	46	10.617	35.776	28.144	1.00	15.49	7	N
ATOM	939	CA	THR	B	46	10.988	34.815	29.157	1.00	15.12	6	C
ATOM	940	CB	THR	B	46	11.682	33.534	28.689	1.00	16.31	6	C
ATOM	941	OG1	THR	B	46	12.959	33.763	28.010	1.00	15.78	8	O
ATOM	942	CG2	THR	B	46	10.833	32.730	27.693	1.00	17.84	6	C
ATOM	943	C	THR	B	46	11.930	35.522	30.142	1.00	17.32	6	C
ATOM	944	O	THR	B	46	12.524	36.584	29.858	1.00	16.70	8	O
ATOM	945	N	ASP	B	47	12.010	34.957	31.363	1.00	17.97	7	N
ATOM	946	CA	ASP	B	47	12.845	35.635	32.353	1.00	20.36	6	C
ATOM	947	CB	ASP	B	47	12.598	35.223	33.813	1.00	25.58	6	C
ATOM	948	CG	ASP	B	47	12.664	33.736	34.035	1.00	29.81	6	C
ATOM	949	OD1	ASP	B	47	12.448	33.010	33.027	1.00	31.62	8	O
ATOM	950	OD2	ASP	B	47	12.956	33.250	35.162	1.00	32.24	8	O
ATOM	951	C	ASP	B	47	14.301	35.373	31.978	1.00	16.72	6	C
ATOM	952	O	ASP	B	47	15.112	36.307	32.039	1.00	17.65	8	O
ATOM	953	N	THR	B	48	14.620	34.173	31.551	1.00	15.74	7	N
ATOM	954	CA	THR	B	48	16.043	33.987	31.213	1.00	16.40	6	C
ATOM	955	CB	THR	B	48	16.770	33.069	32.215	1.00	15.67	6	C
ATOM	956	OG1	THR	B	48	16.288	31.739	31.991	1.00	16.49	8	O
ATOM	957	CG2	THR	B	48	16.605	33.444	33.691	1.00	17.54	6	C
ATOM	958	C	THR	B	48	16.231	33.405	29.817	1.00	15.74	6	C
ATOM	959	O	THR	B	48	15.286	32.952	29.210	1.00	16.51	8	O
ATOM	960	N	LEU	B	49	17.488	33.424	29.331	1.00	14.22	7	N
ATOM	961	CA	LEU	B	49	17.828	32.808	28.078	1.00	12.99	6	C
ATOM	962	CB	LEU	B	49	19.309	33.047	27.731	1.00	13.45	6	C
ATOM	963	CG	LEU	B	49	19.772	32.442	26.399	1.00	12.86	6	C
ATOM	964	CD1	LEU	B	49	18.885	32.972	25.269	1.00	12.52	6	C
ATOM	965	CD2	LEU	B	49	21.248	32.799	26.176	1.00	12.69	6	C
ATOM	966	C	LEU	B	49	17.641	31.314	28.138	1.00	14.59	6	C
ATOM	967	O	LEU	B	49	17.102	30.681	27.223	1.00	15.53	8	O
ATOM	968	N	LYS	B	50	17.970	30.682	29.262	1.00	16.17	7	N
ATOM	969	CA	LYS	B	50	17.720	29.246	29.381	1.00	19.48	6	C
ATOM	970	CB	LYS	B	50	18.193	28.727	30.758	1.00	22.06	6	C
ATOM	971	CG	LYS	B	50	19.650	28.768	31.070	1.00	27.90	6	C
ATOM	972	CD	LYS	B	50	20.542	27.872	30.226	1.00	30.91	6	C
ATOM	973	CE	LYS	B	50	21.605	27.205	31.107	1.00	34.16	6	C
ATOM	974	NZ	LYS	B	50	22.915	27.924	31.080	1.00	35.27	7	N
ATOM	975	C	LYS	B	50	16.214	28.924	29.306	1.00	14.90	6	C
ATOM	976	O	LYS	B	50	15.819	27.823	28.917	1.00	14.68	8	O
ATOM	977	N	ASP	B	51	15.380	29.793	29.876	1.00	17.81	7	N
ATOM	978	CA	ASP	B	51	13.908	29.507	29.814	1.00	17.69	6	C
ATOM	979	CB	ASP	B	51	13.219	30.482	30.729	1.00	19.51	6	C
ATOM	980	CG	ASP	B	51	13.360	30.134	32.206	1.00	20.72	6	C
ATOM	981	OD1	ASP	B	51	13.708	29.003	32.574	1.00	21.31	8	O
ATOM	982	OD2	ASP	B	51	13.092	31.053	32.984	1.00	20.55	8	O
ATOM	983	C	ASP	B	51	13.371	29.632	28.398	1.00	16.44	6	C
ATOM	984	O	ASP	B	51	12.715	28.703	27.890	1.00	17.42	8	O
ATOM	985	N	LEU	B	52	13.941	30.582	27.633	1.00	15.23	7	N
ATOM	986	CA	LEU	B	52	13.645	30.699	26.207	1.00	13.82	6	C
ATOM	987	CB	LEU	B	52	14.396	31.920	25.587	1.00	14.63	6	C
ATOM	988	CG	LEU	B	52	14.076	32.194	24.117	1.00	15.53	6	C
ATOM	989	CD1	LEU	B	52	12.710	32.945	24.006	1.00	14.67	6	C
ATOM	990	CD2	LEU	B	52	15.158	32.974	23.399	1.00	13.85	6	C
ATOM	991	C	LEU	B	52	14.079	29.449	25.476	1.00	14.79	6	C
ATOM	992	O	LEU	B	52	13.369	28.870	24.658	1.00	14.97	8	O
ATOM	993	N	ASP	B	53	15.306	28.967	25.785	1.00	14.38	7	N
ATOM	994	CA	ASP	B	53	15.821	27.759	25.148	1.00	16.61	6	C
ATOM	995	CB	ASP	B	53	17.158	27.294	25.758	1.00	16.33	6	C
ATOM	996	CG	ASP	B	53	18.329	28.180	25.461	1.00	17.82	6	C
ATOM	997	OD1	ASP	B	53	18.339	29.043	24.561	1.00	16.77	8	O
ATOM	998	OD2	ASP	B	53	19.340	28.168	26.224	1.00	21.96	8	O
ATOM	999	C	ASP	B	53	14.800	26.626	25.231	1.00	16.88	6	C
ATOM	1000	O	ASP	B	53	14.575	25.898	24.270	1.00	16.79	8	O
ATOM	1001	N	GLN	B	54	14.351	26.352	26.437	1.00	19.65	7	N
ATOM	1002	CA	GLN	B	54	13.406	25.269	26.733	1.00	23.28	6	C
ATOM	1003	CB	GLN	B	54	13.240	25.185	28.249	1.00	26.46	6	C
ATOM	1004	CG	GLN	B	54	12.272	24.200	28.879	1.00	32.94	6	C
ATOM	1005	CD	GLN	B	54	12.330	24.433	30.398	1.00	37.85	6	C
ATOM	1006	OE1	GLN	B	54	11.846	25.474	30.887	1.00	39.47	8	O
ATOM	1007	NE2	GLN	B	54	12.945	23.515	31.160	1.00	38.13	7	N
ATOM	1008	C	GLN	B	54	12.051	25.545	26.083	1.00	21.13	6	C
ATOM	1009	O	GLN	B	54	11.499	24.633	25.489	1.00	23.10	8	O
ATOM	1010	N	PHE	B	55	11.558	26.769	26.135	1.00	20.48	7	N
ATOM	1011	CA	PHE	B	55	10.290	27.164	25.514	1.00	17.72	6	C
ATOM	1012	CB	PHE	B	55	9.979	28.639	25.834	1.00	17.24	6	C
ATOM	1013	CG	PHE	B	55	8.715	29.086	25.132	1.00	17.59	6	C
ATOM	1014	CD1	PHE	B	55	7.479	28.564	25.536	1.00	16.74	6	C
ATOM	1015	CD2	PHE	B	55	8.753	29.980	24.075	1.00	16.08	6	C
ATOM	1016	CE1	PHE	B	55	6.317	28.943	24.873	1.00	15.53	6	C
ATOM	1017	CE2	PHE	B	55	7.594	30.392	23.472	1.00	15.86	6	C
ATOM	1018	CZ	PHE	B	55	6.369	29.852	23.853	1.00	16.04	6	C
ATOM	1019	C	PHE	B	55	10.271	26.871	24.028	1.00	17.99	6	C
ATOM	1020	O	PHE	B	55	9.434	26.131	23.471	1.00	14.83	8	O
ATOM	1021	N	ILE	B	56	11.365	27.316	23.361	1.00	16.17	7	N
ATOM	1022	CA	ILE	B	56	11.462	27.092	21.932	1.00	17.08	6	C
ATOM	1023	CB	ILE	B	56	12.504	28.050	21.294	1.00	17.13	6	C
ATOM	1024	CG2	ILE	B	56	12.639	27.710	19.833	1.00	17.70	6	C
ATOM	1025	CG1	ILE	B	56	11.991	29.470	21.490	1.00	18.12	6	C
ATOM	1026	CD1	ILE	B	56	12.819	30.561	20.895	1.00	22.50	6	C
ATOM	1027	C	ILE	B	56	11.776	25.645	21.585	1.00	17.95	6	C
ATOM	1028	O	ILE	B	56	11.122	25.106	20.683	1.00	17.47	8	O
ATOM	1029	N	THR	B	57	12.732	24.990	22.239	1.00	18.22	7	N
ATOM	1030	CA	THR	B	57	13.053	23.632	21.790	1.00	20.69	6	C
ATOM	1031	CB	THR	B	57	14.411	23.126	22.315	1.00	20.99	6	C
ATOM	1032	OG1	THR	B	57	14.470	23.336	23.722	1.00	23.13	8	O
ATOM	1033	CG2	THR	B	57	15.565	23.877	21.657	1.00	21.52	6	C
ATOM	1034	C	THR	B	57	11.986	22.615	22.194	1.00	22.22	6	C
ATOM	1035	O	THR	B	57	11.712	21.730	21.385	1.00	21.32	8	O
ATOM	1036	N	GLU	B	58	11.456	22.829	23.392	1.00	23.89	7	N
ATOM	1037	CA	GLU	B	58	10.513	21.872	23.941	1.00	28.94	6	C
ATOM	1038	CB	GLU	B	58	10.777	21.648	25.449	1.00	30.54	6	C
ATOM	1039	CG	GLU	B	58	12.155	21.058	25.706	1.00	33.21	6	C
ATOM	1040	CD	GLU	B	58	12.442	19.835	24.844	1.00	36.23	6	C
ATOM	1041	OE1	GLU	B	58	11.537	18.989	24.608	1.00	36.52	8	O
ATOM	1042	OE2	GLU	B	58	13.596	19.742	24.361	1.00	36.20	8	O
ATOM	1043	C	GLU	B	58	9.052	22.194	23.689	1.00	27.95	6	C
ATOM	1044	O	GLU	B	58	8.347	21.187	23.496	1.00	30.27	8	O
ATOM	1045	N	LYS	B	59	8.594	23.432	23.616	1.00	20.94	7	N
ATOM	1046	CA	LYS	B	59	7.178	23.648	23.327	1.00	25.11	6	C
ATOM	1047	CB	LYS	B	59	6.578	24.692	24.255	1.00	27.02	6	C
ATOM	1048	CG	LYS	B	59	6.244	24.161	25.639	1.00	30.90	6	C
ATOM	1049	CD	LYS	B	59	5.624	25.236	26.549	1.00	34.58	6	C
ATOM	1050	CE	LYS	B	59	5.699	24.798	28.020	1.00	34.94	6	C
ATOM	1051	NZ	LYS	B	59	5.725	25.944	28.972	1.00	36.11	7	N
ATOM	1052	C	LYS	B	59	6.911	24.004	21.857	1.00	23.87	6	C
ATOM	1053	O	LYS	B	59	6.423	23.147	21.109	1.00	23.36	8	O
ATOM	1054	N	ILE	B	60	7.548	25.056	21.351	1.00	19.85	7	N
ATOM	1055	CA	ILE	B	60	7.274	25.554	20.003	1.00	17.05	6	C
ATOM	1056	CB	ILE	B	60	8.007	26.905	19.765	1.00	15.53	6	C
ATOM	1057	CG2	ILE	B	60	7.825	27.435	18.363	1.00	13.69	6	C
ATOM	1058	CG1	ILE	B	60	7.481	27.986	20.736	1.00	16.51	6	C
ATOM	1059	CD1	ILE	B	60	5.991	28.251	20.476	1.00	15.98	6	C
ATOM	1060	C	ILE	B	60	7.609	24.563	18.917	1.00	17.34	6	C
ATOM	1061	O	ILE	B	60	6.772	24.162	18.130	1.00	14.52	8	O
ATOM	1062	N	ARG	B	61	8.875	24.103	18.890	1.00	18.70	7	N
ATOM	1063	CA	ARG	B	61	9.371	23.212	17.852	1.00	20.52	6	C
ATOM	1064	CB	ARG	B	61	10.920	23.301	17.802	1.00	20.89	6	C
ATOM	1065	CG	ARG	B	61	11.306	24.662	17.216	1.00	21.37	6	C
ATOM	1066	CD	ARG	B	61	12.788	24.911	17.048	1.00	21.93	6	C
ATOM	1067	NE	ARG	B	61	13.411	24.028	16.080	1.00	21.23	7	N
ATOM	1068	CZ	ARG	B	61	13.511	24.024	14.776	1.00	18.33	6	C
ATOM	1069	NH1	ARG	B	61	12.968	24.992	14.081	1.00	18.18	7	N
ATOM	1070	NH2	ARG	B	61	14.210	23.051	14.197	1.00	22.37	7	N
ATOM	1071	C	ARG	B	61	8.849	21.789	17.877	1.00	20.48	6	C
ATOM	1072	O	ARG	B	61	8.872	21.139	16.823	1.00	19.46	8	O
ATOM	1073	N	LYS	B	62	8.189	21.397	18.948	1.00	19.89	7	N
ATOM	1074	CA	LYS	B	62	7.486	20.126	19.010	1.00	22.12	6	C
ATOM	1075	CB	LYS	B	62	7.564	19.510	20.415	1.00	22.87	6	C
ATOM	1076	CG	LYS	B	62	8.998	19.480	20.908	1.00	25.05	6	C
ATOM	1077	CD	LYS	B	62	9.842	18.467	20.132	1.00	26.73	6	C
ATOM	1078	CE	LYS	B	62	11.164	18.267	20.879	1.00	28.67	6	C
ATOM	1079	NZ	LYS	B	62	11.865	17.052	20.376	1.00	29.88	7	N
ATOM	1080	C	LYS	B	62	6.018	20.266	18.653	1.00	22.89	6	C
ATOM	1081	O	LYS	B	62	5.371	19.221	18.738	1.00	24.68	8	O
ATOM	1082	N	MET	B	63	5.493	21.455	18.346	1.00	22.05	7	N
ATOM	1083	CA	MET	B	63	4.085	21.535	17.935	1.00	21.24	6	C
ATOM	1084	CB	MET	B	63	3.596	22.986	17.770	1.00	21.67	6	C
ATOM	1085	CG	MET	B	63	3.515	23.697	19.108	1.00	24.24	6	C
ATOM	1086	SD	MET	B	63	2.958	25.403	19.105	1.00	25.86	16	S
ATOM	1087	CE	MET	B	63	1.266	25.330	18.546	1.00	22.54	6	C
ATOM	1088	C	MET	B	63	3.994	20.877	16.578	1.00	20.21	6	C
ATOM	1089	O	MET	B	63	4.679	21.365	15.693	1.00	19.21	8	O
ATOM	1090	N	PRO	B	64	3.013	20.020	16.328	1.00	20.66	7	N
ATOM	1091	CD	PRO	B	64	2.171	19.423	17.400	1.00	21.16	6	C
ATOM	1092	CA	PRO	B	64	3.009	19.225	15.113	1.00	20.71	6	C
ATOM	1093	CB	PRO	B	64	1.914	18.185	15.357	1.00	22.37	6	C
ATOM	1094	CG	PRO	B	64	1.645	18.137	16.824	1.00	20.69	6	C
ATOM	1095	C	PRO	B	64	2.817	20.011	13.840	1.00	20.17	6	C
ATOM	1096	O	PRO	B	64	3.344	19.668	12.765	1.00	19.17	8	O
ATOM	1097	N	GLU	B	65	2.077	21.113	13.928	1.00	18.92	7	N
ATOM	1098	CA	GLU	B	65	1.808	21.925	12.750	1.00	20.82	6	C
ATOM	1099	CB	GLU	B	65	0.451	22.625	12.962	1.00	23.06	6	C
ATOM	1100	CG	GLU	B	65	−0.570	21.732	13.649	1.00	24.65	6	C
ATOM	1101	CD	GLU	B	65	−0.701	22.037	15.135	1.00	28.89	6	C
ATOM	1102	OE1	GLU	B	65	0.281	21.999	15.947	1.00	26.57	8	O
ATOM	1103	OE2	GLU	B	65	−1.900	22.338	15.495	1.00	30.49	8	O
ATOM	1104	C	GLU	B	65	2.866	22.965	12.446	1.00	20.76	6	C
ATOM	1105	O	GLU	B	65	2.822	23.524	11.345	1.00	23.34	8	O
ATOM	1106	N	ILE	B	66	3.880	23.130	13.292	1.00	19.85	7	N
ATOM	1107	CA	ILE	B	66	4.988	24.066	12.991	1.00	18.23	6	C
ATOM	1108	CB	ILE	B	66	5.574	24.580	14.324	1.00	18.27	6	C
ATOM	1109	CG2	ILE	B	66	6.951	25.202	14.145	1.00	18.20	6	C
ATOM	1110	CG1	ILE	B	66	4.502	25.528	14.888	1.00	18.67	6	C
ATOM	1111	CD1	ILE	B	66	4.911	26.360	16.092	1.00	19.78	6	C
ATOM	1112	C	ILE	B	66	6.023	23.331	12.155	1.00	19.56	6	C
ATOM	1113	O	ILE	B	66	6.493	22.275	12.616	1.00	18.62	8	O
ATOM	1114	N	GLN	B	67	6.373	23.821	10.957	1.00	18.63	7	N
ATOM	1115	CA	GLN	B	67	7.296	23.106	10.117	1.00	19.98	6	C
ATOM	1116	CB	GLN	B	67	6.901	23.271	8.625	1.00	21.88	6	C
ATOM	1117	CG	GLN	B	67	5.496	22.762	8.421	1.00	26.02	6	C
ATOM	1118	CD	GLN	B	67	5.042	22.459	7.026	1.00	28.55	6	C
ATOM	1119	OE1	GLN	B	67	4.361	21.434	6.858	1.00	31.69	8	O
ATOM	1120	NE2	GLN	B	67	5.284	23.306	6.034	1.00	29.80	7	N
ATOM	1121	C	GLN	B	67	8.706	23.681	10.243	1.00	21.32	6	C
ATOM	1122	O	GLN	B	67	9.715	23.099	9.843	1.00	20.33	8	O
ATOM	1123	N	MET	B	68	8.749	24.966	10.583	1.00	21.16	7	N
ATOM	1124	CA	MET	B	68	10.009	25.693	10.650	1.00	20.94	6	C
ATOM	1125	CB	MET	B	68	10.295	26.285	9.262	1.00	24.01	6	C
ATOM	1126	CG	MET	B	68	10.902	25.394	8.237	1.00	30.45	6	C
ATOM	1127	SD	MET	B	68	11.853	26.281	7.020	1.00	38.87	16	S
ATOM	1128	CE	MET	B	68	10.602	26.712	5.822	1.00	35.81	6	C
ATOM	1129	C	MET	B	68	9.911	26.899	11.558	1.00	17.78	6	C
ATOM	1130	O	MET	B	68	8.870	27.576	11.556	1.00	16.20	8	O
ATOM	1131	N	THR	B	69	10.977	27.268	12.235	1.00	15.58	7	N
ATOM	1132	CA	THR	B	69	11.017	28.506	13.025	1.00	12.38	6	C
ATOM	1133	CB	THR	B	69	10.793	28.278	14.527	1.00	13.97	6	C
ATOM	1134	OG1	THR	B	69	11.853	27.497	15.116	1.00	14.07	8	O
ATOM	1135	CG2	THR	B	69	9.458	27.596	14.822	1.00	11.50	6	C
ATOM	1136	C	THR	B	69	12.360	29.171	12.790	1.00	14.55	6	C
ATOM	1137	O	THR	B	69	13.364	28.457	12.587	1.00	13.00	8	O
ATOM	1138	N	SER	B	70	12.431	30.484	12.926	1.00	11.76	7	N
ATOM	1139	CA	SER	B	70	13.653	31.254	12.816	1.00	11.23	6	C
ATOM	1140	CB	SER	B	70	13.770	31.802	11.403	1.00	10.94	6	C
ATOM	1141	OG	SER	B	70	14.807	32.763	11.395	1.00	13.40	8	O
ATOM	1142	C	SER	B	70	13.467	32.327	13.909	1.00	13.08	6	C
ATOM	1143	O	SER	B	70	12.493	33.086	13.794	1.00	11.11	8	O
ATOM	1144	N	THR	B	71	14.234	32.225	15.001	1.00	9.49	7	N
ATOM	1145	CA	THR	B	71	14.004	33.081	16.152	1.00	9.27	6	C
ATOM	1146	CB	THR	B	71	14.023	32.166	17.406	1.00	11.05	6	C
ATOM	1147	OG1	THR	B	71	12.964	31.212	17.347	1.00	10.77	8	O
ATOM	1148	CG2	THR	B	71	13.880	33.018	18.664	1.00	12.37	6	C
ATOM	1149	C	THR	B	71	15.047	34.188	16.282	1.00	8.22	6	C
ATOM	1150	O	THR	B	71	16.249	33.931	16.119	1.00	10.11	8	O
ATOM	1151	N	MET	B	72	14.635	35.405	16.449	1.00	6.69	7	N
ATOM	1152	CA	MET	B	72	15.517	36.547	16.585	1.00	7.80	6	C
ATOM	1153	CB	MET	B	72	15.111	37.662	15.627	1.00	10.55	6	C
ATOM	1154	CG	MET	B	72	15.251	37.183	14.165	1.00	16.67	6	C
ATOM	1155	SD	MET	B	72	14.478	38.386	13.048	1.00	20.04	16	S
ATOM	1156	CE	MET	B	72	14.819	37.455	11.545	1.00	23.19	6	C
ATOM	1157	C	MET	B	72	15.467	37.079	18.005	1.00	7.77	6	C
ATOM	1158	O	MET	B	72	14.442	37.688	18.349	1.00	7.18	8	O
ATOM	1159	N	ILE	B	73	16.559	36.867	18.744	1.00	6.41	7	N
ATOM	1160	CA	ILE	B	73	16.580	37.347	20.117	1.00	8.84	6	C
ATOM	1161	CB	ILE	B	73	17.656	36.575	20.926	1.00	7.95	6	C
ATOM	1162	CG2	ILE	B	73	17.878	37.273	22.301	1.00	9.41	6	C
ATOM	1163	CG1	ILE	B	73	17.217	35.102	21.017	1.00	8.05	6	C
ATOM	1164	CD1	ILE	B	73	18.284	34.103	21.467	1.00	11.03	6	C
ATOM	1165	C	ILE	B	73	16.774	38.842	20.097	1.00	11.08	6	C
ATOM	1166	O	ILE	B	73	17.663	39.307	19.357	1.00	12.77	8	O
ATOM	1167	N	ALA	B	74	16.112	39.633	20.955	1.00	11.74	7	N
ATOM	1168	CA	ALA	B	74	16.349	41.049	21.012	1.00	11.91	6	C
ATOM	1169	CB	ALA	B	74	15.190	41.968	21.481	1.00	11.66	6	C
ATOM	1170	C	ALA	B	74	17.560	41.357	21.904	1.00	14.51	6	C
ATOM	1171	O	ALA	B	74	17.794	40.714	22.942	1.00	11.20	8	O
ATOM	1172	N	ILE	B	75	18.109	42.519	21.630	1.00	17.53	7	N
ATOM	1173	CA	ILE	B	75	19.305	43.071	22.262	1.00	24.22	6	C
ATOM	1174	CB	ILE	B	75	20.071	43.938	21.234	1.00	25.52	6	C
ATOM	1175	CG2	ILE	B	75	20.752	45.181	21.763	1.00	27.56	6	C
ATOM	1176	CG1	ILE	B	75	21.106	43.078	20.489	1.00	25.82	6	C
ATOM	1177	CD1	ILE	B	75	22.210	42.628	21.402	1.00	28.79	6	C
ATOM	1178	C	ILE	B	75	18.913	43.902	23.470	1.00	27.45	6	C
ATOM	1179	O	ILE	B	75	17.779	44.405	23.469	1.00	29.37	8	O
ATOM	1180	OT	ILE	B	75	19.762	44.028	24.395	1.00	31.78	8	O
ATOM	1181	CB	VAL	C	2	39.332	19.443	4.171	1.00	13.51	6	C
ATOM	1182	CG1	VAL	C	2	38.145	20.355	3.825	1.00	13.69	6	C
ATOM	1183	CG2	VAL	C	2	40.295	19.357	2.968	1.00	11.61	6	C
ATOM	1184	C	VAL	C	2	39.163	20.233	6.562	1.00	13.74	6	C
ATOM	1185	O	VAL	C	2	38.668	19.280	7.202	1.00	13.05	8	O
ATOM	1186	N	VAL	C	2	41.199	18.998	5.711	1.00	13.50	7	N
ATOM	1187	CA	VAL	C	2	40.102	19.970	5.380	1.00	13.12	6	C
ATOM	1188	N	THR	C	3	39.031	21.486	6.942	1.00	13.22	7	N
ATOM	1189	CA	THR	C	3	38.168	21.900	8.039	1.00	14.11	6	C
ATOM	1190	CB	THR	C	3	38.833	22.798	9.084	1.00	12.14	6	C
ATOM	1191	OG1	THR	C	3	39.931	22.193	9.744	1.00	12.53	8	O
ATOM	1192	CG2	THR	C	3	37.829	23.094	10.246	1.00	10.76	6	C
ATOM	1193	C	THR	C	3	36.960	22.646	7.426	1.00	13.61	6	C
ATOM	1194	O	THR	C	3	37.202	23.489	6.563	1.00	12.66	8	O
ATOM	1195	N	ALA	C	4	35.746	22.325	7.836	1.00	11.41	7	N
ATOM	1196	CA	ALA	C	4	34.586	22.976	7.285	1.00	11.20	6	C
ATOM	1197	CB	ALA	C	4	33.979	22.223	6.107	1.00	8.89	6	C
ATOM	1198	C	ALA	C	4	33.477	23.136	8.345	1.00	11.12	6	C
ATOM	1199	O	ALA	C	4	33.347	22.322	9.266	1.00	10.90	8	O
ATOM	1200	N	PHE	C	5	32.693	24.214	8.185	1.00	9.67	7	N
ATOM	1201	CA	PHE	C	5	31.550	24.453	9.036	1.00	9.21	6	C
ATOM	1202	CB	PHE	C	5	31.422	25.860	9.633	1.00	9.50	6	C
ATOM	1203	CG	PHE	C	5	32.397	26.100	10.752	1.00	10.21	6	C
ATOM	1204	CD1	PHE	C	5	33.702	26.499	10.428	1.00	8.38	6	C
ATOM	1205	CD2	PHE	C	5	32.076	25.900	12.080	1.00	9.76	6	C
ATOM	1206	CE1	PHE	C	5	34.665	26.663	11.392	1.00	10.44	6	C
ATOM	1207	CE2	PHE	C	5	33.051	26.086	13.050	1.00	8.18	6	C
ATOM	1208	CZ	PHE	C	5	34.318	26.446	12.727	1.00	9.99	6	C
ATOM	1209	C	PHE	C	5	30.312	24.105	8.196	1.00	11.44	6	C
ATOM	1210	O	PHE	C	5	30.128	24.588	7.060	1.00	13.44	8	O
ATOM	1211	N	ILE	C	6	29.458	23.243	8.739	1.00	9.23	7	N
ATOM	1212	CA	ILE	C	6	28.227	22.977	7.980	1.00	10.67	6	C
ATOM	1213	CB	ILE	C	6	28.075	21.453	7.793	1.00	12.19	6	C
ATOM	1214	CG2	ILE	C	6	26.744	21.189	7.118	1.00	11.24	6	C
ATOM	1215	CG1	ILE	C	6	29.268	20.837	7.020	1.00	12.66	6	C
ATOM	1216	CD1	ILE	C	6	29.037	19.318	6.949	1.00	12.74	6	C
ATOM	1217	C	ILE	C	6	27.055	23.571	8.739	1.00	9.95	6	C
ATOM	1218	O	ILE	C	6	26.932	23.245	9.922	1.00	7.94	8	O
ATOM	1219	N	LEU	C	7	26.275	24.443	8.129	1.00	10.46	7	N
ATOM	1220	CA	LEU	C	7	25.123	25.054	8.768	1.00	11.52	6	C
ATOM	1221	CB	LEU	C	7	24.963	26.522	8.306	1.00	14.75	6	C
ATOM	1222	CG	LEU	C	7	26.163	27.363	8.764	1.00	16.86	6	C
ATOM	1223	CD1	LEU	C	7	25.971	28.807	8.310	1.00	19.73	6	C
ATOM	1224	CD2	LEU	C	7	26.301	27.276	10.262	1.00	17.56	6	C
ATOM	1225	C	LEU	C	7	23.887	24.324	8.262	1.00	13.74	6	C
ATOM	1226	O	LEU	C	7	23.864	24.231	7.024	1.00	15.75	8	O
ATOM	1227	N	MET	C	8	22.967	23.861	9.073	1.00	12.28	7	N
ATOM	1228	CA	MET	C	8	21.871	23.050	8.619	1.00	15.30	6	C
ATOM	1229	CB	MET	C	8	22.064	21.613	9.116	1.00	16.92	6	C
ATOM	1230	CG	MET	C	8	23.275	20.809	8.666	1.00	18.76	6	C
ATOM	1231	SD	MET	C	8	23.600	19.314	9.582	1.00	20.83	16	S
ATOM	1232	CE	MET	C	8	24.791	19.921	10.776	1.00	24.28	6	C
ATOM	1233	C	MET	C	8	20.510	23.492	9.187	1.00	17.65	6	C
ATOM	1234	O	MET	C	8	20.409	23.926	10.346	1.00	16.91	8	O
ATOM	1235	N	VAL	C	9	19.496	23.240	8.362	1.00	19.14	7	N
ATOM	1236	CA	VAL	C	9	18.083	23.374	8.761	1.00	19.28	6	C
ATOM	1237	CB	VAL	C	9	17.168	23.967	7.718	1.00	19.18	6	C
ATOM	1238	CG1	VAL	C	9	15.697	23.905	8.170	1.00	19.22	6	C
ATOM	1239	CG2	VAL	C	9	17.579	25.418	7.540	1.00	19.16	6	C
ATOM	1240	C	VAL	C	9	17.598	21.966	9.060	1.00	19.88	6	C
ATOM	1241	O	VAL	C	9	18.106	21.035	8.414	1.00	23.28	8	O
ATOM	1242	N	THR	C	10	16.890	21.717	10.155	1.00	19.30	7	N
ATOM	1243	CA	THR	C	10	16.411	20.364	10.393	1.00	17.92	6	C
ATOM	1244	CB	THR	C	10	16.843	19.661	11.672	1.00	16.38	6	C
ATOM	1245	OG1	THR	C	10	16.133	20.315	12.741	1.00	18.11	8	O
ATOM	1246	CG2	THR	C	10	18.340	19.783	11.879	1.00	18.62	6	C
ATOM	1247	C	THR	C	10	14.873	20.411	10.478	1.00	19.30	6	C
ATOM	1248	O	THR	C	10	14.321	21.487	10.541	1.00	18.20	8	O
ATOM	1249	N	ALA	C	11	14.222	19.244	10.430	1.00	19.87	7	N
ATOM	1250	CA	ALA	C	11	12.729	19.379	10.557	1.00	21.46	6	C
ATOM	1251	CB	ALA	C	11	12.177	17.984	10.450	1.00	20.40	6	C
ATOM	1252	C	ALA	C	11	12.554	20.024	11.947	1.00	22.53	6	C
ATOM	1253	O	ALA	C	11	13.387	19.737	12.828	1.00	20.28	8	O
ATOM	1254	N	ALA	C	12	11.570	20.893	12.172	1.00	22.83	7	N
ATOM	1255	CA	ALA	C	12	11.388	21.485	13.491	1.00	21.67	6	C
ATOM	1256	CB	ALA	C	12	10.050	22.226	13.511	1.00	21.82	6	C
ATOM	1257	C	ALA	C	12	11.279	20.386	14.546	1.00	22.13	6	C
ATOM	1258	O	ALA	C	12	10.431	19.494	14.387	1.00	21.92	8	O
ATOM	1259	N	GLY	C	13	12.059	20.441	15.634	1.00	21.75	7	N
ATOM	1260	CA	GLY	C	13	11.867	19.456	16.708	1.00	20.46	6	C
ATOM	1261	C	GLY	C	13	12.824	18.291	16.688	1.00	20.35	6	C
ATOM	1262	O	GLY	C	13	12.994	17.498	17.614	1.00	21.82	8	O
ATOM	1263	N	LYS	C	14	13.508	18.073	15.581	1.00	21.21	7	N
ATOM	1264	CA	LYS	C	14	14.496	17.032	15.406	1.00	20.28	6	C
ATOM	1265	CB	LYS	C	14	14.312	16.435	13.999	1.00	22.02	6	C
ATOM	1266	CG	LYS	C	14	12.877	15.929	13.752	1.00	23.94	6	C
ATOM	1267	CD	LYS	C	14	12.495	14.817	14.711	1.00	24.03	6	C
ATOM	1268	CE	LYS	C	14	11.142	14.233	14.252	1.00	27.62	6	C
ATOM	1269	NZ	LYS	C	14	10.815	13.033	15.090	1.00	29.36	7	N
ATOM	1270	C	LYS	C	14	15.931	17.544	15.561	1.00	20.24	6	C
ATOM	1271	O	LYS	C	14	16.810	16.665	15.603	1.00	20.05	8	O
ATOM	1272	N	GLU	C	15	16.201	18.853	15.711	1.00	17.96	7	N
ATOM	1273	CA	GLU	C	15	17.600	19.258	15.842	1.00	17.39	6	C
ATOM	1274	CB	GLU	C	15	17.723	20.771	16.040	1.00	18.15	6	C
ATOM	1275	CG	GLU	C	15	16.929	21.378	17.155	1.00	21.05	6	C
ATOM	1276	CD	GLU	C	15	15.446	21.691	16.877	1.00	23.06	6	C
ATOM	1277	OE1	GLU	C	15	14.902	22.458	17.720	1.00	22.27	8	O
ATOM	1278	OE2	GLU	C	15	14.811	21.237	15.899	1.00	19.49	8	O
ATOM	1279	C	GLU	C	15	18.439	18.541	16.875	1.00	17.98	6	C
ATOM	1280	O	GLU	C	15	19.633	18.251	16.612	1.00	17.01	8	O
ATOM	1281	N	ARG	C	16	17.951	18.262	18.084	1.00	19.93	7	N
ATOM	1282	CA	ARG	C	16	18.758	17.602	19.095	1.00	23.34	6	C
ATOM	1283	CB	ARG	C	16	18.142	17.638	20.485	1.00	26.49	6	C
ATOM	1284	CG	ARG	C	16	18.577	18.836	21.313	1.00	32.57	6	C
ATOM	1285	CD	ARG	C	16	17.739	18.911	22.588	1.00	36.19	6	C
ATOM	1286	NE	ARG	C	16	17.646	20.313	23.027	1.00	40.59	7	N
ATOM	1287	CZ	ARG	C	16	16.894	20.698	24.064	1.00	43.15	6	C
ATOM	1288	NH1	ARG	C	16	16.218	19.820	24.813	1.00	45.02	7	N
ATOM	1289	NH2	ARG	C	16	16.882	21.992	24.344	1.00	43.41	7	N
ATOM	1290	C	ARG	C	16	19.121	16.155	18.749	1.00	23.41	6	C
ATOM	1291	O	ARG	C	16	20.244	15.713	19.020	1.00	24.50	8	O
ATOM	1292	N	GLU	C	17	18.196	15.378	18.198	1.00	22.54	7	N
ATOM	1293	CA	GLU	C	17	18.534	13.994	17.878	1.00	22.99	6	C
ATOM	1294	CB	GLU	C	17	17.267	13.167	17.843	1.00	23.42	6	C
ATOM	1295	CG	GLU	C	17	16.247	13.469	16.765	1.00	26.37	6	C
ATOM	1296	CD	GLU	C	17	16.705	12.793	15.478	1.00	29.84	6	C
ATOM	1297	OE1	GLU	C	17	17.540	11.856	15.651	1.00	30.85	8	O
ATOM	1298	OE2	GLU	C	17	16.264	13.213	14.403	1.00	30.82	8	O
ATOM	1299	C	GLU	C	17	19.392	13.983	16.617	1.00	21.91	6	C
ATOM	1300	O	GLU	C	17	20.201	13.066	16.406	1.00	23.15	8	O
ATOM	1301	N	VAL	C	18	19.222	14.931	15.686	1.00	20.55	7	N
ATOM	1302	CA	VAL	C	18	20.142	14.929	14.546	1.00	18.68	6	C
ATOM	1303	CB	VAL	C	18	19.763	16.002	13.524	1.00	18.86	6	C
ATOM	1304	CG1	VAL	C	18	20.916	16.280	12.556	1.00	17.78	6	C
ATOM	1305	CG2	VAL	C	18	18.534	15.567	12.751	1.00	17.95	6	C
ATOM	1306	C	VAL	C	18	21.529	15.200	15.104	1.00	18.89	6	C
ATOM	1307	O	VAL	C	18	22.532	14.523	14.868	1.00	20.52	8	O
ATOM	1308	N	MET	C	19	21.637	16.181	15.993	1.00	18.99	7	N
ATOM	1309	CA	MET	C	19	22.925	16.541	16.559	1.00	19.72	6	C
ATOM	1310	CB	MET	C	19	22.769	17.748	17.479	1.00	19.34	6	C
ATOM	1311	CG	MET	C	19	24.112	18.134	18.123	1.00	19.03	6	C
ATOM	1312	SD	MET	C	19	23.905	19.552	19.172	1.00	19.97	16	S
ATOM	1313	CE	MET	C	19	22.982	18.859	20.519	1.00	21.11	6	C
ATOM	1314	C	MET	C	19	23.606	15.412	17.319	1.00	20.76	6	C
ATOM	1315	O	MET	C	19	24.841	15.407	17.408	1.00	20.12	8	O
ATOM	1316	N	GLU	C	20	22.856	14.570	18.009	1.00	21.72	7	N
ATOM	1317	CA	GLU	C	20	23.500	13.493	18.805	1.00	22.57	6	C
ATOM	1318	CB	GLU	C	20	22.492	12.946	19.823	1.00	23.97	6	C
ATOM	1319	CG	GLU	C	20	22.242	13.984	20.941	1.00	26.93	6	C
ATOM	1320	CD	GLU	C	20	23.506	14.388	21.687	1.00	28.95	6	C
ATOM	1321	OE1	GLU	C	20	24.338	13.471	21.927	1.00	29.90	8	O
ATOM	1322	OE2	GLU	C	20	23.742	15.589	22.041	1.00	29.95	8	O
ATOM	1323	C	GLU	C	20	24.055	12.461	17.840	1.00	21.95	6	C
ATOM	1324	O	GLU	C	20	25.107	11.816	18.043	1.00	23.26	8	O
ATOM	1325	N	LYS	C	21	23.317	12.251	16.749	1.00	19.49	7	N
ATOM	1326	CA	LYS	C	21	23.826	11.337	15.739	1.00	19.77	6	C
ATOM	1327	CB	LYS	C	21	22.813	11.186	14.594	1.00	19.76	6	C
ATOM	1328	CG	LYS	C	21	21.640	10.325	15.093	1.00	21.20	6	C
ATOM	1329	CD	LYS	C	21	20.679	10.149	13.933	1.00	22.36	6	C
ATOM	1330	CE	LYS	C	21	19.385	9.482	14.443	1.00	24.72	6	C
ATOM	1331	NZ	LYS	C	21	18.396	9.485	13.330	1.00	25.52	7	N
ATOM	1332	C	LYS	C	21	25.117	11.882	15.155	1.00	20.89	6	C
ATOM	1333	O	LYS	C	21	26.020	11.102	14.816	1.00	22.01	8	O
ATOM	1334	N	LEU	C	22	25.168	13.196	14.848	1.00	20.08	7	N
ATOM	1335	CA	LEU	C	22	26.349	13.828	14.265	1.00	17.68	6	C
ATOM	1336	CB	LEU	C	22	26.026	15.282	13.809	1.00	17.13	6	C
ATOM	1337	CG	LEU	C	22	25.157	15.440	12.582	1.00	17.15	6	C
ATOM	1338	CD1	LEU	C	22	24.528	16.851	12.515	1.00	19.16	6	C
ATOM	1339	CD2	LEU	C	22	25.864	15.262	11.272	1.00	18.59	6	C
ATOM	1340	C	LEU	C	22	27.497	13.777	15.240	1.00	18.53	6	C
ATOM	1341	O	LEU	C	22	28.660	13.456	14.925	1.00	18.17	8	O
ATOM	1342	N	LEU	C	23	27.270	14.064	16.528	1.00	19.42	7	N
ATOM	1343	CA	LEU	C	23	28.369	13.962	17.481	1.00	19.76	6	C
ATOM	1344	CB	LEU	C	23	27.928	14.386	18.870	1.00	19.18	6	C
ATOM	1345	CG	LEU	C	23	27.619	15.872	18.970	1.00	19.72	6	C
ATOM	1346	CD1	LEU	C	23	26.733	16.088	20.201	1.00	19.30	6	C
ATOM	1347	CD2	LEU	C	23	28.940	16.627	19.057	1.00	20.29	6	C
ATOM	1348	C	LEU	C	23	28.921	12.547	17.596	1.00	20.32	6	C
ATOM	1349	O	LEU	C	23	29.996	12.403	18.217	1.00	24.12	8	O
ATOM	1350	N	ALA	C	24	28.288	11.498	17.091	1.00	21.26	7	N
ATOM	1351	CA	ALA	C	24	28.945	10.187	17.254	1.00	23.37	6	C
ATOM	1352	CB	ALA	C	24	27.913	9.105	17.455	1.00	22.08	6	C
ATOM	1353	C	ALA	C	24	29.909	9.985	16.096	1.00	23.91	6	C
ATOM	1354	O	ALA	C	24	30.794	9.135	16.181	1.00	26.64	8	O
ATOM	1355	N	MET	C	25	29.831	10.763	15.018	1.00	22.85	7	N
ATOM	1356	CA	MET	C	25	30.719	10.545	13.862	1.00	19.77	6	C
ATOM	1357	CB	MET	C	25	30.066	11.120	12.615	1.00	20.26	6	C
ATOM	1358	CG	MET	C	25	28.610	10.697	12.416	1.00	18.66	6	C
ATOM	1359	SD	MET	C	25	27.853	11.632	11.049	1.00	20.09	16	S
ATOM	1360	CE	MET	C	25	26.186	10.959	11.067	1.00	18.76	6	C
ATOM	1361	C	MET	C	25	32.084	11.124	14.126	1.00	20.66	6	C
ATOM	1362	O	MET	C	25	32.191	12.215	14.649	1.00	20.74	8	O
ATOM	1363	N	PRO	C	26	33.161	10.396	13.787	1.00	19.82	7	N
ATOM	1364	CD	PRO	C	26	33.098	9.044	13.168	1.00	20.83	6	C
ATOM	1365	CA	PRO	C	26	34.498	10.816	14.024	1.00	19.76	6	C
ATOM	1366	CB	PRO	C	26	35.376	9.630	13.588	1.00	19.77	6	C
ATOM	1367	CG	PRO	C	26	34.515	8.779	12.738	1.00	20.30	6	C
ATOM	1368	C	PRO	C	26	34.873	12.109	13.315	1.00	17.68	6	C
ATOM	1369	O	PRO	C	26	35.713	12.838	13.852	1.00	17.43	8	O
ATOM	1370	N	GLU	C	27	34.287	12.423	12.176	1.00	17.43	7	N
ATOM	1371	CA	GLU	C	27	34.610	13.635	11.418	1.00	16.36	6	C
ATOM	1372	CB	GLU	C	27	33.964	13.666	10.045	1.00	18.01	6	C
ATOM	1373	CG	GLU	C	27	33.994	12.573	9.040	1.00	21.06	6	C
ATOM	1374	CD	GLU	C	27	33.460	11.209	9.439	1.00	24.48	6	C
ATOM	1375	OE1	GLU	C	27	32.905	10.975	10.544	1.00	22.13	8	O
ATOM	1376	OE2	GLU	C	27	33.612	10.328	8.548	1.00	26.95	8	O
ATOM	1377	C	GLU	C	27	34.072	14.894	12.132	1.00	15.77	6	C
ATOM	1378	O	GLU	C	27	34.608	16.018	12.001	1.00	13.07	8	O
ATOM	1379	N	VAL	C	28	32.985	14.693	12.889	1.00	14.39	7	N
ATOM	1380	CA	VAL	C	28	32.385	15.833	13.582	1.00	14.23	6	C
ATOM	1381	CB	VAL	C	28	30.911	15.621	13.946	1.00	13.36	6	C
ATOM	1382	CG1	VAL	C	28	30.347	16.905	14.607	1.00	13.52	6	C
ATOM	1383	CG2	VAL	C	28	30.089	15.300	12.718	1.00	11.93	6	C
ATOM	1384	C	VAL	C	28	33.224	16.259	14.766	1.00	14.33	6	C
ATOM	1385	O	VAL	C	28	33.347	15.476	15.722	1.00	15.29	8	O
ATOM	1386	N	LYS	C	29	33.694	17.504	14.806	1.00	13.37	7	N
ATOM	1387	CA	LYS	C	29	34.438	17.954	15.988	1.00	13.98	6	C
ATOM	1388	CB	LYS	C	29	35.625	18.884	15.662	1.00	13.92	6	C
ATOM	1389	CG	LYS	C	29	36.534	18.189	14.630	1.00	16.47	6	C
ATOM	1390	CD	LYS	C	29	36.875	16.761	15.038	1.00	16.96	6	C
ATOM	1391	CE	LYS	C	29	38.221	16.374	14.398	1.00	22.04	6	C
ATOM	1392	NZ	LYS	C	29	38.262	14.911	14.030	1.00	24.30	7	N
ATOM	1393	C	LYS	C	29	33.640	18.713	17.033	1.00	14.44	6	C
ATOM	1394	O	LYS	C	29	34.018	18.680	18.202	1.00	12.53	8	O
ATOM	1395	N	GLU	C	30	32.583	19.419	16.575	1.00	13.94	7	N
ATOM	1396	CA	GLU	C	30	31.766	20.156	17.551	1.00	13.46	6	C
ATOM	1397	CB	GLU	C	30	32.435	21.389	18.153	1.00	14.91	6	C
ATOM	1398	CG	GLU	C	30	32.868	22.376	17.121	1.00	17.59	6	C
ATOM	1399	CD	GLU	C	30	33.308	23.755	17.492	1.00	18.48	6	C
ATOM	1400	OE1	GLU	C	30	33.818	24.439	16.555	1.00	19.49	8	O
ATOM	1401	OE2	GLU	C	30	33.093	24.296	18.587	1.00	18.98	8	O
ATOM	1402	C	GLU	C	30	30.423	20.378	16.853	1.00	12.44	6	C
ATOM	1403	O	GLU	C	30	30.303	20.285	15.629	1.00	10.96	8	O
ATOM	1404	N	ALA	C	31	29.366	20.505	17.626	1.00	11.16	7	N
ATOM	1405	CA	ALA	C	31	28.021	20.599	17.048	1.00	10.93	6	C
ATOM	1406	CB	ALA	C	31	27.428	19.201	16.822	1.00	10.63	6	C
ATOM	1407	C	ALA	C	31	27.190	21.315	18.113	1.00	10.97	6	C
ATOM	1408	O	ALA	C	31	27.360	21.054	19.316	1.00	9.38	8	O
ATOM	1409	N	TYR	C	32	26.391	22.275	17.649	1.00	9.53	7	N
ATOM	1410	CA	TYR	C	32	25.530	23.025	18.552	1.00	8.67	6	C
ATOM	1411	CB	TYR	C	32	26.086	24.395	18.891	1.00	9.25	6	C
ATOM	1412	CG	TYR	C	32	27.408	24.481	19.615	1.00	10.08	6	C
ATOM	1413	CD1	TYR	C	32	27.357	24.671	20.988	1.00	11.88	6	C
ATOM	1414	CE1	TYR	C	32	28.503	24.740	21.794	1.00	12.28	6	C
ATOM	1415	CD2	TYR	C	32	28.646	24.324	18.992	1.00	10.95	6	C
ATOM	1416	CE2	TYR	C	32	29.799	24.403	19.764	1.00	11.49	6	C
ATOM	1417	CZ	TYR	C	32	29.709	24.623	21.121	1.00	12.94	6	C
ATOM	1418	OH	TYR	C	32	30.827	24.777	21.921	1.00	15.26	8	O
ATOM	1419	C	TYR	C	32	24.204	23.305	17.843	1.00	10.59	6	C
ATOM	1420	O	TYR	C	32	24.121	23.444	16.603	1.00	10.55	8	O
ATOM	1421	N	VAL	C	33	23.162	23.336	18.661	1.00	9.72	7	N
ATOM	1422	CA	VAL	C	33	21.851	23.736	18.161	1.00	9.11	6	C
ATOM	1423	CB	VAL	C	33	20.683	23.161	18.968	1.00	9.44	6	C
ATOM	1424	CG1	VAL	C	33	19.379	23.787	18.505	1.00	11.05	6	C
ATOM	1425	CG2	VAL	C	33	20.646	21.639	18.742	1.00	9.65	6	C
ATOM	1426	C	VAL	C	33	21.845	25.259	18.352	1.00	8.78	6	C
ATOM	1427	O	VAL	C	33	22.349	25.739	19.368	1.00	11.19	8	O
ATOM	1428	N	VAL	C	34	21.478	26.012	17.342	1.00	8.87	7	N
ATOM	1429	CA	VAL	C	34	21.543	27.472	17.359	1.00	7.42	6	C
ATOM	1430	CB	VAL	C	34	22.674	27.896	16.409	1.00	7.82	6	C
ATOM	1431	CG1	VAL	C	34	24.065	27.329	16.849	1.00	6.17	6	C
ATOM	1432	CG2	VAL	C	34	22.466	27.457	14.933	1.00	5.87	6	C
ATOM	1433	C	VAL	C	34	20.225	28.140	16.954	1.00	9.54	6	C
ATOM	1434	O	VAL	C	34	19.395	27.580	16.223	1.00	8.27	8	O
ATOM	1435	N	TYR	C	35	20.027	29.392	17.383	1.00	10.13	7	N
ATOM	1436	CA	TYR	C	35	18.976	30.284	16.947	1.00	11.95	6	C
ATOM	1437	CB	TYR	C	35	18.775	31.483	17.876	1.00	12.68	6	C
ATOM	1438	CG	TYR	C	35	18.185	31.039	19.195	1.00	17.52	6	C
ATOM	1439	CD1	TYR	C	35	16.816	31.015	19.360	1.00	18.77	6	C
ATOM	1440	CE1	TYR	C	35	16.271	30.631	20.564	1.00	18.30	6	C
ATOM	1441	CD2	TYR	C	35	18.994	30.662	20.262	1.00	17.66	6	C
ATOM	1442	CE2	TYR	C	35	18.444	30.266	21.460	1.00	18.18	6	C
ATOM	1443	CZ	TYR	C	35	17.067	30.261	21.601	1.00	18.43	6	C
ATOM	1444	OH	TYR	C	35	16.493	29.868	22.789	1.00	18.93	8	O
ATOM	1445	C	TYR	C	35	19.300	30.955	15.604	1.00	12.91	6	C
ATOM	1446	O	TYR	C	35	20.482	31.218	15.319	1.00	12.84	8	O
ATOM	1447	N	GLY	C	36	18.299	31.196	14.782	1.00	14.24	7	N
ATOM	1448	CA	GLY	C	36	18.520	31.859	13.478	1.00	12.60	6	C
ATOM	1449	C	GLY	C	36	17.864	31.056	12.389	1.00	14.26	6	C
ATOM	1450	O	GLY	C	36	17.106	30.079	12.649	1.00	18.80	8	O
ATOM	1451	N	GLU	C	37	18.194	31.299	11.145	1.00	18.17	7	N
ATOM	1452	CA	GLU	C	37	17.633	30.564	10.002	1.00	23.09	6	C
ATOM	1453	CB	GLU	C	37	18.169	31.203	8.714	1.00	27.51	6	C
ATOM	1454	CG	GLU	C	37	17.650	30.595	7.407	1.00	32.04	6	C
ATOM	1455	CD	GLU	C	37	18.546	31.061	6.256	1.00	35.48	6	C
ATOM	1456	OE1	GLU	C	37	19.323	30.257	5.686	1.00	37.55	8	O
ATOM	1457	OE2	GLU	C	37	18.521	32.254	5.909	1.00	36.51	8	O
ATOM	1458	C	GLU	C	37	18.066	29.104	10.001	1.00	23.63	6	C
ATOM	1459	O	GLU	C	37	17.322	28.198	9.618	1.00	23.98	8	O
ATOM	1460	N	TYR	C	38	19.316	28.847	10.403	1.00	21.56	7	N
ATOM	1461	CA	TYR	C	38	19.836	27.509	10.574	1.00	19.52	6	C
ATOM	1462	CB	TYR	C	38	21.368	27.543	10.441	1.00	22.39	6	C
ATOM	1463	CG	TYR	C	38	21.703	28.026	9.039	1.00	24.37	6	C
ATOM	1464	CD1	TYR	C	38	21.292	27.258	7.969	1.00	25.06	6	C
ATOM	1465	CE1	TYR	C	38	21.584	27.690	6.693	1.00	28.43	6	C
ATOM	1466	CD2	TYR	C	38	22.404	29.209	8.861	1.00	25.04	6	C
ATOM	1467	CE2	TYR	C	38	22.726	29.599	7.572	1.00	27.79	6	C
ATOM	1468	CZ	TYR	C	38	22.292	28.843	6.501	1.00	27.61	6	C
ATOM	1469	OH	THR	C	38	22.596	29.243	5.230	1.00	31.14	8	O
ATOM	1470	C	THR	C	38	19.568	27.040	12.010	1.00	17.33	6	C
ATOM	1471	O	THR	C	38	19.308	27.808	12.915	1.00	18.03	8	O
ATOM	1472	N	ASP	C	39	19.479	25.752	12.164	1.00	15.50	7	N
ATOM	1473	CA	ASP	C	39	19.069	25.122	13.403	1.00	16.04	6	C
ATOM	1474	CB	ASP	C	39	18.092	24.006	13.020	1.00	14.43	6	C
ATOM	1475	CG	ASP	C	39	16.840	24.566	12.407	1.00	16.60	6	C
ATOM	1476	OD1	ASP	C	39	16.453	25.687	12.752	1.00	15.98	8	O
ATOM	1477	OD2	ASP	C	39	16.250	23.864	11.558	1.00	20.27	8	O
ATOM	1478	C	ASP	C	39	20.282	24.495	14.086	1.00	13.53	6	C
ATOM	1479	O	ASP	C	39	20.326	24.344	15.307	1.00	14.94	8	O
ATOM	1480	N	LEU	C	40	21.232	24.154	13.194	1.00	12.61	7	N
ATOM	1481	CA	LEU	C	40	22.439	23.489	13.689	1.00	13.53	6	C
ATOM	1482	CB	LEU	C	40	22.190	22.022	13.285	1.00	15.55	6	C
ATOM	1483	CG	LEU	C	40	22.710	20.831	14.001	1.00	19.18	6	C
ATOM	1484	CD1	LEU	C	40	22.457	20.879	15.503	1.00	19.65	6	C
ATOM	1485	CD2	LEU	C	40	21.942	19.557	13.514	1.00	18.15	6	C
ATOM	1486	C	LEU	C	40	23.716	23.928	12.995	1.00	11.96	6	C
ATOM	1487	O	LEU	C	40	23.749	24.157	11.769	1.00	10.54	8	O
ATOM	1488	N	ILE	C	41	24.785	23.932	13.784	1.00	11.74	7	N
ATOM	1489	CA	ILE	C	41	26.123	24.205	13.183	1.00	11.84	6	C
ATOM	1490	CB	ILE	C	41	26.679	25.588	13.482	1.00	12.75	6	C
ATOM	1491	CG2	ILE	C	41	26.699	25.790	14.971	1.00	13.88	6	C
ATOM	1492	CG1	ILE	C	41	28.120	25.681	12.875	1.00	13.00	6	C
ATOM	1493	CD1	ILE	C	41	28.527	27.134	12.744	1.00	14.55	6	C
ATOM	1494	C	ILE	C	41	27.072	23.118	13.664	1.00	10.85	6	C
ATOM	1495	O	ILE	C	41	27.076	22.742	14.846	1.00	10.67	8	O
ATOM	1496	N	VAL	C	42	27.801	22.553	12.699	1.00	10.11	7	N
ATOM	1497	CA	VAL	C	42	28.738	21.454	12.964	1.00	11.25	6	C
ATOM	1498	CB	VAL	C	42	28.087	20.228	12.232	1.00	14.86	6	C
ATOM	1499	CG1	VAL	C	42	28.985	19.118	11.842	1.00	13.65	6	C
ATOM	1500	CG2	VAL	C	42	26.998	19.628	13.169	1.00	15.56	6	C
ATOM	1501	C	VAL	C	42	30.084	21.759	12.362	1.00	11.05	6	C
ATOM	1502	O	VAL	C	42	30.168	22.412	11.300	1.00	11.42	8	O
ATOM	1503	N	LYS	C	43	31.164	21.525	13.084	1.00	11.17	7	N
ATOM	1504	CA	LYS	C	43	32.510	21.655	12.560	1.00	10.83	6	C
ATOM	1505	CB	LYS	C	43	33.423	22.361	13.542	1.00	10.74	6	C
ATOM	1506	CG	LYS	C	43	34.834	22.632	12.996	1.00	12.24	6	C
ATOM	1507	CD	LYS	C	43	35.626	22.992	14.268	1.00	15.84	6	C
ATOM	1508	CE	LYS	C	43	37.101	23.230	14.123	1.00	15.74	6	C
ATOM	1509	NZ	LYS	C	43	37.562	23.826	15.456	1.00	14.56	7	N
ATOM	1510	C	LYS	C	43	33.051	20.251	12.241	1.00	11.80	6	C
ATOM	1511	O	LYS	C	43	33.135	19.345	13.083	1.00	10.83	8	O
ATOM	1512	N	VAL	C	44	33.453	20.042	10.989	1.00	11.36	7	N
ATOM	1513	CA	VAL	C	44	33.934	18.777	10.453	1.00	11.94	6	C
ATOM	1514	CB	VAL	C	44	32.975	18.306	9.341	1.00	13.11	6	C
ATOM	1515	CG1	VAL	C	44	33.430	17.009	8.657	1.00	16.19	6	C
ATOM	1516	CG2	VAL	C	44	31.583	17.978	9.900	1.00	13.88	6	C
ATOM	1517	C	VAL	C	44	35.387	18.934	10.004	1.00	13.35	6	C
ATOM	1518	O	VAL	C	44	35.899	20.015	9.598	1.00	13.28	8	O
ATOM	1519	N	GLU	C	45	36.207	17.906	10.191	1.00	14.07	7	N
ATOM	1520	CA	GLU	C	45	37.622	17.831	9.808	1.00	14.76	6	C
ATOM	1521	CB	GLU	C	45	38.680	18.063	10.878	1.00	16.30	6	C
ATOM	1522	CG	GLU	C	45	38.631	19.447	11.511	1.00	19.96	6	C
ATOM	1523	CD	GLU	C	45	39.528	19.670	12.698	1.00	22.48	6	C
ATOM	1524	OE1	GLU	C	45	39.541	20.843	13.173	1.00	25.62	8	O
ATOM	1525	OE2	GLU	C	45	40.204	18.732	13.168	1.00	22.11	8	O
ATOM	1526	C	GLU	C	45	37.840	16.458	9.161	1.00	16.36	6	C
ATOM	1527	O	GLU	C	45	37.106	15.509	9.540	1.00	15.71	8	O
ATOM	1528	N	THR	C	46	38.215	16.526	7.857	1.00	16.74	7	N
ATOM	1529	CA	THR	C	46	38.348	15.349	7.020	1.00	16.32	6	C
ATOM	1530	CB	THR	C	46	37.338	15.094	5.916	1.00	17.33	6	C
ATOM	1531	CG1	THR	C	46	37.480	16.090	4.875	1.00	17.34	8	O
ATOM	1532	CG2	THR	C	46	35.887	15.114	6.379	1.00	18.83	6	C
ATOM	1533	C	THR	C	46	39.742	15.413	6.391	1.00	16.88	6	C
ATOM	1534	O	THR	C	46	40.446	16.425	6.502	1.00	16.93	8	O
ATOM	1535	N	ASP	C	47	40.290	14.231	6.023	1.00	19.87	7	N
ATOM	1536	CA	ASP	C	47	41.700	14.317	5.576	1.00	21.73	6	C
ATOM	1537	CB	ASP	C	47	42.426	12.954	5.586	1.00	26.37	6	C
ATOM	1538	CG	ASP	C	47	41.716	12.020	4.630	1.00	29.72	6	C
ATOM	1539	OD1	ASP	C	47	40.591	12.393	4.229	1.00	31.09	8	O
ATOM	1540	OD2	ASP	C	47	42.171	10.932	4.213	1.00	33.95	8	O
ATOM	1541	C	ASP	C	47	41.738	14.992	4.194	1.00	19.55	6	C
ATOM	1542	O	ASP	C	47	42.634	15.814	4.039	1.00	20.55	8	O
ATOM	1543	N	THR	C	48	40.768	14.797	3.313	1.00	17.36	7	N
ATOM	1544	CA	THR	C	48	40.777	15.364	1.972	1.00	16.80	6	C
ATOM	1545	CB	THR	C	48	40.998	14.279	0.889	1.00	17.66	6	C
ATOM	1546	OG1	THR	C	48	39.843	13.418	0.841	1.00	19.76	8	O
ATOM	1547	CG2	THR	C	48	42.226	13.399	1.066	1.00	18.46	6	C
ATOM	1548	C	THR	C	48	39.390	15.962	1.645	1.00	17.80	6	C
ATOM	1549	O	THR	C	48	38.410	15.767	2.371	1.00	17.96	8	O
ATOM	1550	N	LEU	C	49	39.276	16.693	0.539	1.00	17.38	7	N
ATOM	1551	CA	LEU	C	49	38.041	17.313	0.104	1.00	17.64	6	C
ATOM	1552	CB	LEU	C	49	38.373	18.361	−0.982	1.00	18.40	6	C
ATOM	1553	CG	LEU	C	49	37.081	19.124	−1.386	1.00	19.66	6	C
ATOM	1554	CD1	LEU	C	49	36.587	19.885	−0.153	1.00	18.61	6	C
ATOM	1555	CD2	LEU	C	49	37.331	20.095	−2.523	1.00	20.55	6	C
ATOM	1556	C	LEU	C	49	37.073	16.254	−0.415	1.00	19.38	6	C
ATOM	1557	O	LEU	C	49	35.854	16.268	−0.227	1.00	17.37	8	O
ATOM	1558	N	LYS	C	50	37.667	15.245	−1.085	1.00	19.62	7	N
ATOM	1559	CA	LYS	C	50	36.914	14.069	−1.516	1.00	22.17	6	C
ATOM	1560	CB	LYS	C	50	37.782	13.055	−2.251	1.00	25.37	6	C
ATOM	1561	CG	LYS	C	50	37.245	11.638	−2.416	1.00	29.73	6	C
ATOM	1562	CD	LYS	C	50	38.410	10.633	−2.435	1.00	32.69	6	C
ATOM	1563	CE	LYS	C	50	38.020	9.201	−2.769	1.00	34.00	6	C
ATOM	1564	NZ	LYS	C	50	38.205	8.880	−4.230	1.00	36.40	7	N
ATOM	1565	C	LYS	C	50	36.286	13.404	−0.280	1.00	19.70	6	C
ATOM	1566	O	LYS	C	50	35.097	13.147	−0.311	1.00	18.54	8	O
ATOM	1567	N	ASP	C	51	37.028	13.195	0.810	1.00	20.24	7	N
ATOM	1568	CA	ASP	C	51	36.392	12.664	2.031	1.00	19.47	6	C
ATOM	1569	CB	ASP	C	51	37.475	12.383	3.087	1.00	20.84	6	C
ATOM	1570	CG	ASP	C	51	38.327	11.194	2.601	1.00	22.11	6	C
ATOM	1571	OD1	ASP	C	51	37.801	10.426	1.779	1.00	22.72	8	O
ATOM	1572	OD2	ASP	C	51	39.478	11.066	3.025	1.00	20.72	8	O
ATOM	1573	C	ASP	C	51	35.320	13.573	2.580	1.00	19.16	6	C
ATOM	1574	O	ASP	C	51	34.292	13.068	3.019	1.00	21.04	8	O
ATOM	1575	N	LEU	C	52	35.448	14.912	2.479	1.00	18.94	7	N
ATOM	1576	CA	LEU	C	52	34.381	15.799	2.945	1.00	15.62	6	C
ATOM	1577	CB	LEU	C	52	34.813	17.271	2.792	1.00	15.17	6	C
ATOM	1578	CG	LEU	C	52	33.760	18.354	3.078	1.00	12.83	6	C
ATOM	1579	CD1	LEU	C	52	33.238	18.194	4.507	1.00	14.01	6	C
ATOM	1580	CD2	LEU	C	52	34.453	19.713	2.883	1.00	13.45	6	C
ATOM	1581	C	LEU	C	52	33.132	15.606	2.142	1.00	16.81	6	C
ATOM	1582	O	LEU	C	52	32.026	15.503	2.644	1.00	16.79	8	O
ATOM	1583	N	ASP	C	53	33.296	15.652	0.811	1.00	20.54	7	N
ATOM	1584	CA	ASP	C	53	32.156	15.528	−0.100	1.00	23.66	6	C
ATOM	1585	CB	ASP	C	53	32.600	15.643	−1.558	1.00	24.36	6	C
ATOM	1586	CG	ASP	C	53	31.433	15.675	−2.527	1.00	27.18	6	C
ATOM	1587	OD1	ASP	C	53	30.847	14.603	−2.831	1.00	28.04	8	O
ATOM	1588	OD2	ASP	C	53	31.048	16.750	−3.064	1.00	28.27	8	O
ATOM	1589	C	ASP	C	53	31.465	14.198	0.183	1.00	24.54	6	C
ATOM	1590	O	ASP	C	53	30.237	14.171	0.266	1.00	27.34	8	O
ATOM	1591	N	GLN	C	54	32.212	13.126	0.480	1.00	25.41	7	N
ATOM	1592	CA	GLN	C	54	31.528	11.856	0.704	1.00	27.72	6	C
ATOM	1593	CB	GLN	C	54	32.540	10.726	0.543	1.00	29.95	6	C
ATOM	1594	CG	GLN	C	54	31.771	9.421	0.229	1.00	35.88	6	C
ATOM	1595	CD	GLN	C	54	32.776	8.260	0.234	1.00	38.59	6	C
ATOM	1596	OE1	GLN	C	54	33.997	8.535	0.208	1.00	40.18	8	O
ATOM	1597	NE2	GLN	C	54	32.222	7.057	0.258	1.00	38.68	7	N
ATOM	1598	C	GLN	C	54	30.861	11.758	2.073	1.00	26.83	6	C
ATOM	1599	O	GLN	C	54	29.910	10.973	2.244	1.00	27.40	8	O
ATOM	1600	N	PHE	C	55	31.350	12.565	3.019	1.00	23.70	7	N
ATOM	1601	CA	PHE	C	55	30.710	12.620	4.348	1.00	21.86	6	C
ATOM	1602	CB	PHE	C	55	31.702	13.193	5.357	1.00	19.93	6	C
ATOM	1603	CG	PHE	C	55	30.987	13.609	6.614	1.00	20.88	6	C
ATOM	1604	CD1	PHE	C	55	30.884	12.742	7.683	1.00	19.06	6	C
ATOM	1605	CD2	PHE	C	55	30.394	14.873	6.690	1.00	19.80	6	C
ATOM	1606	CE1	PHE	C	55	30.209	13.115	8.823	1.00	17.49	6	C
ATOM	1607	CE2	PHE	C	55	29.715	15.249	7.830	1.00	20.56	6	C
ATOM	1608	CZ	PHE	C	55	29.643	14.352	8.895	1.00	19.05	6	C
ATOM	1609	C	PHE	C	55	29.387	13.339	4.235	1.00	21.61	6	C
ATOM	1610	O	PHE	C	55	28.353	12.900	4.766	1.00	22.20	8	O
ATOM	1611	N	ILE	C	56	29.352	14.429	3.454	1.00	21.99	7	N
ATOM	1612	CA	ILE	C	56	28.092	15.134	3.220	1.00	22.47	6	C
ATOM	1613	CB	ILE	C	56	28.328	16.386	2.337	1.00	22.35	6	C
ATOM	1614	CG2	ILE	C	56	27.039	16.904	1.709	1.00	21.09	6	C
ATOM	1615	CG1	ILE	C	56	29.004	17.487	3.171	1.00	21.32	6	C
ATOM	1616	CD1	ILE	C	56	29.601	18.543	2.264	1.00	24.85	6	C
ATOM	1617	C	ILE	C	56	27.044	14.280	2.523	1.00	24.70	6	C
ATOM	1618	O	ILE	C	56	25.851	14.393	2.839	1.00	26.85	8	O
ATOM	1619	N	THR	C	57	27.403	13.577	1.446	1.00	26.48	7	N
ATOM	1620	CA	THR	C	57	26.407	12.847	0.667	1.00	27.16	6	C
ATOM	1621	CB	THR	C	57	27.007	12.425	−0.687	1.00	27.37	6	C
ATOM	1622	OG1	THR	C	57	28.236	11.757	−0.326	1.00	30.53	8	O
ATOM	1623	CG2	THR	C	57	27.367	13.571	−1.616	1.00	25.93	6	C
ATOM	1624	C	THR	C	57	25.977	11.580	1.383	1.00	29.79	6	C
ATOM	1625	O	THR	C	57	24.792	11.181	1.373	1.00	32.61	8	O
ATOM	1626	N	GLU	C	58	26.951	10.884	1.965	1.00	30.00	7	N
ATOM	1627	CA	GLU	C	58	26.591	9.627	2.622	1.00	31.50	6	C
ATOM	1628	CB	GLU	C	58	27.826	8.747	2.774	1.00	33.53	6	C
ATOM	1629	CG	GLU	C	58	28.512	8.540	1.428	1.00	36.71	6	C
ATOM	1630	CD	GLU	C	58	27.648	8.445	0.182	1.00	39.49	6	C
ATOM	1631	OE1	GLU	C	58	26.556	7.813	0.197	1.00	39.86	8	O
ATOM	1632	OE2	GLU	C	58	28.074	8.990	−0.885	1.00	40.22	8	O
ATOM	1633	C	GLU	C	58	25.848	9.921	3.911	1.00	31.88	6	C
ATOM	1634	O	GLU	C	58	24.713	9.432	4.067	1.00	32.24	8	O
ATOM	1635	N	LYS	C	59	26.476	10.754	4.754	1.00	31.30	7	N
ATOM	1636	CA	LYS	C	59	25.833	11.012	6.046	1.00	29.92	6	C
ATOM	1637	CB	LYS	C	59	26.896	11.140	7.160	1.00	30.17	6	C
ATOM	1638	CG	LYS	C	59	28.102	10.256	6.978	1.00	31.15	6	C
ATOM	1639	CD	LYS	C	59	28.432	9.440	8.232	1.00	34.64	6	C
ATOM	1640	CE	LYS	C	59	29.922	9.072	8.262	1.00	35.28	6	C
ATOM	1641	NZ	LYS	C	59	30.375	8.487	9.562	1.00	35.48	7	N
ATOM	1642	C	LYS	C	59	24.914	12.203	6.056	1.00	28.84	6	C
ATOM	1643	O	LYS	C	59	23.891	12.075	6.757	1.00	32.65	8	O
ATOM	1644	N	ILE	C	60	25.105	13.337	5.401	1.00	27.08	7	N
ATOM	1645	CA	ILE	C	60	24.205	14.461	5.598	1.00	24.04	6	C
ATOM	1646	CB	ILE	C	60	24.917	15.824	5.491	1.00	22.38	6	C
ATOM	1647	CG2	ILE	C	60	23.980	17.028	5.513	1.00	22.26	6	C
ATOM	1648	CG1	ILE	C	60	25.945	15.987	6.614	1.00	22.82	6	C
ATOM	1649	CD1	ILE	C	60	25.479	15.800	8.043	1.00	22.99	6	C
ATOM	1650	C	ILE	C	60	22.982	14.420	4.717	1.00	26.78	6	C
ATOM	1651	O	ILE	C	60	21.885	14.876	5.126	1.00	27.54	8	O
ATOM	1652	N	ARG	C	61	23.097	13.874	3.518	1.00	27.90	7	N
ATOM	1653	CA	ARG	C	61	21.922	13.822	2.639	1.00	28.63	6	C
ATOM	1654	CB	ARG	C	61	22.337	14.115	1.194	1.00	28.99	6	C
ATOM	1655	CG	ARG	C	61	22.193	15.571	0.776	1.00	29.41	6	C
ATOM	1656	CD	ARG	C	61	23.149	15.907	−0.362	1.00	30.77	6	C
ATOM	1657	NE	ARG	C	61	23.058	17.293	−0.839	1.00	30.00	7	N
ATOM	1658	CZ	ARG	C	61	23.823	17.717	−1.861	1.00	31.73	6	C
ATOM	1659	NH1	ARG	C	61	24.650	16.865	−2.519	1.00	30.90	7	N
ATOM	1660	NH2	ARG	C	61	23.747	18.977	−2.334	1.00	31.15	7	N
ATOM	1661	C	ARG	C	61	21.144	12.525	2.785	1.00	29.56	6	C
ATOM	1662	O	ARG	C	61	20.054	12.488	2.195	1.00	32.69	8	O
ATOM	1663	N	LYS	C	62	21.507	11.519	3.565	1.00	28.81	7	N
ATOM	1664	CA	LYS	C	62	20.703	10.354	3.850	1.00	28.73	6	C
ATOM	1665	CB	LYS	C	62	21.495	9.038	3.876	1.00	29.41	6	C
ATOM	1666	CG	LYS	C	62	21.713	8.469	2.472	1.00	30.20	6	C
ATOM	1667	CD	LYS	C	62	22.852	7.434	2.430	1.00	32.21	6	C
ATOM	1668	CE	LYS	C	62	23.356	7.366	0.974	1.00	32.81	6	C
ATOM	1669	NZ	LYS	C	62	24.510	6.429	0.843	1.00	33.64	7	N
ATOM	1670	C	LYS	C	62	20.038	10.515	5.230	1.00	30.02	6	C
ATOM	1671	O	LYS	C	62	19.651	9.527	5.885	1.00	32.12	8	O
ATOM	1672	N	MET	C	63	20.177	11.713	5.823	1.00	28.76	7	N
ATOM	1673	CA	MET	C	63	19.493	11.980	7.098	1.00	26.81	6	C
ATOM	1674	CB	MET	C	63	20.435	12.737	8.034	1.00	27.75	6	C
ATOM	1675	CG	MET	C	63	20.688	11.900	9.255	1.00	28.92	6	C
ATOM	1676	SD	MET	C	63	21.342	12.751	10.713	1.00	34.47	16	S
ATOM	1677	CE	MET	C	63	23.079	12.594	10.294	1.00	29.00	6	C
ATOM	1678	C	MET	C	63	18.231	12.718	6.738	1.00	25.17	6	C
ATOM	1679	O	MET	C	63	18.220	13.864	6.271	1.00	27.77	8	O
ATOM	1680	N	PRO	C	64	17.097	12.006	6.766	1.00	23.96	7	N
ATOM	1681	CD	PRO	C	64	16.986	10.619	7.289	1.00	24.17	6	C
ATOM	1682	CA	PRO	C	64	15.808	12.538	6.355	1.00	24.05	6	C
ATOM	1683	CB	PRO	C	64	14.878	11.345	6.357	1.00	24.26	6	C
ATOM	1684	CG	PRO	C	64	15.491	10.380	7.310	1.00	24.02	6	C
ATOM	1685	C	PRO	C	64	15.351	13.693	7.238	1.00	23.26	6	C
ATOM	1686	O	PRO	C	64	14.634	14.599	6.786	1.00	23.48	8	O
ATOM	1687	N	GLU	C	65	15.894	13.773	8.458	1.00	23.82	7	N
ATOM	1688	CA	GLU	C	65	15.503	14.946	9.287	1.00	25.38	6	C
ATOM	1689	CB	GLU	C	65	15.737	14.529	10.742	1.00	26.46	6	C
ATOM	1690	CG	GLU	C	65	14.861	13.328	11.046	1.00	29.88	6	C
ATOM	1691	CD	GLU	C	65	15.581	12.403	11.996	1.00	33.43	6	C
ATOM	1692	OE1	GLU	C	65	14.905	11.607	12.707	1.00	36.06	8	O
ATOM	1693	OE2	GLU	C	65	16.826	12.495	12.168	1.00	34.58	8	O
ATOM	1694	C	GLU	C	65	16.224	16.228	8.933	1.00	25.09	6	C
ATOM	1695	O	GLU	C	65	15.716	17.320	9.257	1.00	25.89	8	O
ATOM	1696	N	ILE	C	66	17.369	16.098	8.233	1.00	23.79	7	N
ATOM	1697	CA	ILE	C	66	18.156	17.256	7.814	1.00	22.74	6	C
ATOM	1698	CB	ILE	C	66	19.635	16.857	7.670	1.00	22.13	6	C
ATOM	1699	CG2	ILE	C	66	20.468	17.984	7.086	1.00	22.33	6	C
ATOM	1700	CG1	ILE	C	66	20.165	16.412	9.012	1.00	20.58	6	C
ATOM	1701	CD1	ILE	C	66	21.611	15.995	9.067	1.00	23.30	6	C
ATOM	1702	C	ILE	C	66	17.578	17.729	6.511	1.00	24.00	6	C
ATOM	1703	O	ILE	C	66	17.301	16.854	5.665	1.00	26.96	8	O
ATOM	1704	N	GLN	C	67	17.361	19.007	6.283	1.00	25.25	7	N
ATOM	1705	CA	GLN	C	67	16.593	19.488	5.154	1.00	25.62	6	C
ATOM	1706	CB	GLN	C	67	15.371	20.251	5.750	1.00	27.64	6	C
ATOM	1707	CG	GLN	C	67	14.314	19.213	6.197	1.00	30.98	6	C
ATOM	1708	CD	GLN	C	67	13.082	19.895	6.738	1.00	32.31	6	C
ATOM	1709	OE1	GLN	C	67	12.934	21.113	6.514	1.00	35.41	8	O
ATOM	1710	NE2	GLN	C	67	12.264	19.145	7.471	1.00	33.33	7	N
ATOM	1711	C	GLN	C	67	17.276	20.434	4.200	1.00	28.28	6	C
ATOM	1712	O	GLN	C	67	16.880	20.489	3.003	1.00	30.74	8	O
ATOM	1713	N	MET	C	68	18.156	21.310	4.658	1.00	27.47	7	N
ATOM	1714	CA	MET	C	68	18.862	22.263	3.802	1.00	24.68	6	C
ATOM	1715	CB	MET	C	68	18.008	23.515	3.700	1.00	26.70	6	C
ATOM	1716	CG	MET	C	68	18.697	24.745	3.118	1.00	31.25	6	C
ATOM	1717	SD	MET	C	68	17.815	26.277	3.584	1.00	38.51	16	S
ATOM	1718	CE	MET	C	68	19.212	27.404	3.757	1.00	35.34	6	C
ATOM	1719	C	MET	C	68	20.189	22.645	4.477	1.00	23.75	6	C
ATOM	1720	O	MET	C	68	20.099	23.063	5.644	1.00	19.66	8	O
ATOM	1721	N	THR	C	69	21.313	22.411	3.789	1.00	21.36	7	N
ATOM	1722	CA	THR	C	69	22.618	22.639	4.357	1.00	19.81	6	C
ATOM	1723	CB	THR	C	69	23.404	21.315	4.525	1.00	20.43	6	C
ATOM	1724	OG1	THR	C	69	24.167	21.019	3.362	1.00	22.61	8	O
ATOM	1725	CG2	THR	C	69	22.506	20.131	4.834	1.00	17.73	6	C
ATOM	1726	C	THR	C	69	23.490	23.637	3.618	1.00	18.75	6	C
ATOM	1727	O	THR	C	69	23.440	23.819	2.409	1.00	20.19	8	O
ATOM	1728	N	SER	C	70	24.295	24.391	4.359	1.00	16.80	7	N
ATOM	1729	CA	SER	C	70	25.258	25.283	3.740	1.00	17.93	6	C
ATOM	1730	CB	SER	C	70	24.713	26.687	3.927	1.00	17.55	6	C
ATOM	1731	OG	SER	C	70	25.650	27.578	3.348	1.00	22.26	8	O
ATOM	1732	C	SER	C	70	26.657	24.999	4.302	1.00	17.09	6	C
ATOM	1733	O	SER	C	70	26.847	25.050	5.520	1.00	17.01	8	O
ATOM	1734	N	THR	C	71	27.600	24.667	3.423	1.00	14.94	7	N
ATOM	1735	CA	THR	C	71	28.959	24.328	3.889	1.00	15.34	6	C
ATOM	1736	CB	THR	C	71	29.491	23.036	3.200	1.00	15.88	6	C
ATOM	1737	OG1	THR	C	71	28.576	21.980	3.539	1.00	15.96	8	O
ATOM	1738	CG2	THR	C	71	30.856	22.573	3.655	1.00	16.01	6	C
ATOM	1739	C	THR	C	71	29.906	25.472	3.588	1.00	14.07	6	C
ATOM	1740	O	THR	C	71	29.908	26.005	2.467	1.00	13.13	8	O
ATOM	1741	N	MET	C	72	30.733	25.786	4.576	1.00	12.04	7	N
ATOM	1742	CA	MET	C	72	31.806	26.752	4.438	1.00	12.02	6	C
ATOM	1743	CB	MET	C	72	31.612	27.963	5.351	1.00	11.60	6	C
ATOM	1744	CG	MET	C	72	30.249	28.638	5.153	1.00	17.54	6	C
ATOM	1745	SD	MET	C	72	29.862	29.742	6.517	1.00	18.74	16	S
ATOM	1746	CE	MET	C	72	28.292	30.398	6.028	1.00	21.26	6	C
ATOM	1747	C	MET	C	72	33.168	26.143	4.823	1.00	11.23	6	C
ATOM	1748	O	MET	C	72	33.471	25.902	6.015	1.00	8.34	8	O
ATOM	1749	N	ILE	C	73	33.996	25.961	3.813	1.00	10.73	7	N
ATOM	1750	CA	ILE	C	73	35.331	25.404	4.056	1.00	10.84	6	C
ATOM	1751	CB	ILE	C	73	35.953	24.995	2.723	1.00	13.41	6	C
ATOM	1752	CG2	ILE	C	73	37.443	24.649	2.885	1.00	12.03	6	C
ATOM	1753	CG1	ILE	C	73	35.105	23.853	2.157	1.00	14.14	6	C
ATOM	1754	CD1	ILE	C	73	35.758	23.179	0.954	1.00	16.09	6	C
ATOM	1755	C	ILE	C	73	36.203	26.456	4.725	1.00	13.62	6	C
ATOM	1756	O	ILE	C	73	36.216	27.633	4.359	1.00	13.19	8	O
ATOM	1757	N	ALA	C	74	36.934	26.033	5.735	1.00	14.74	7	N
ATOM	1758	CA	ALA	C	74	37.896	26.893	6.398	1.00	18.25	6	C
ATOM	1759	CB	ALA	C	74	37.993	26.485	7.858	1.00	18.16	6	C
ATOM	1760	C	ALA	C	74	39.226	26.939	5.669	1.00	22.37	6	C
ATOM	1761	O	ALA	C	74	39.598	26.057	4.867	1.00	24.32	8	O
ATOM	1762	N	ILE	C	75	39.770	28.140	5.533	1.00	24.13	7	N
ATOM	1763	CA	ILE	C	75	41.072	28.446	4.996	1.00	26.43	6	C
ATOM	1764	CB	ILE	C	75	41.185	29.580	3.977	1.00	25.92	6	C
ATOM	1765	CG2	ILE	C	75	42.611	29.746	3.459	1.00	25.06	6	C
ATOM	1766	CG1	ILE	C	75	40.232	29.433	2.812	1.00	25.87	6	C
ATOM	1767	CD1	ILE	C	75	39.600	30.788	2.473	1.00	25.99	6	C
ATOM	1768	C	ILE	C	75	41.832	28.964	6.239	1.00	29.95	6	C
ATOM	1769	O	ILE	C	75	41.645	28.455	7.393	1.00	29.32	8	O
ATOM	1770	OT	ILE	C	75	42.313	30.128	6.106	1.00	33.07	8	O
ATOM	1771	CB	VAL	D	2	25.991	33.212	26.292	1.00	10.82	6	C
ATOM	1772	CG1	VAL	D	2	25.191	33.260	24.963	1.00	10.54	6	C
ATOM	1773	CG2	VAL	D	2	24.998	33.476	27.435	1.00	11.04	6	C
ATOM	1774	C	VAL	D	2	27.631	31.627	25.373	1.00	9.57	6	C
ATOM	1775	O	VAL	D	2	28.621	32.340	25.380	1.00	12.23	8	O
ATOM	1776	N	VAL	D	2	27.227	31.645	27.864	1.00	11.94	7	N
ATOM	1777	CA	VAL	D	2	26.629	31.841	26.486	1.00	10.20	6	C
ATOM	1778	N	THR	D	3	27.387	30.772	24.418	1.00	10.51	7	N
ATOM	1779	CA	THR	D	3	28.201	30.539	23.233	1.00	12.03	6	C
ATOM	1780	CB	THR	D	3	28.465	29.034	23.075	1.00	12.43	6	C
ATOM	1781	OG1	THR	D	3	29.142	28.582	24.249	1.00	13.41	8	O
ATOM	1782	CG2	THR	D	3	29.325	28.600	21.892	1.00	9.36	6	C
ATOM	1783	C	THR	D	3	27.453	31.041	21.984	1.00	10.73	6	C
ATOM	1784	O	THR	D	3	26.224	30.920	21.844	1.00	8.60	8	O
ATOM	1785	N	ALA	D	4	28.180	31.725	21.110	1.00	8.65	7	N
ATOM	1786	CA	ALA	D	4	27.522	32.150	19.858	1.00	7.98	6	C
ATOM	1787	CB	ALA	D	4	27.122	33.625	20.025	1.00	6.69	6	C
ATOM	1788	C	ALA	D	4	28.519	31.981	18.712	1.00	8.86	6	C
ATOM	1789	O	ALA	D	4	29.734	32.022	18.997	1.00	6.46	8	O
ATOM	1790	N	PHE	D	5	28.015	31.833	17.488	1.00	6.65	7	N
ATOM	1791	CA	PHE	D	5	28.883	31.817	16.321	1.00	6.21	6	C
ATOM	1792	CB	PHE	D	5	28.691	30.573	15.466	1.00	6.58	6	C
ATOM	1793	CG	PHE	D	5	29.300	29.326	16.045	1.00	6.64	6	C
ATOM	1794	CD1	PHE	D	5	28.596	28.550	16.929	1.00	8.03	6	C
ATOM	1795	CD2	PHE	D	5	30.594	28.964	15.709	1.00	8.47	6	C
ATOM	1796	CE1	PHE	D	5	29.137	27.383	17.485	1.00	8.72	6	C
ATOM	1797	CE2	PHE	D	5	31.157	27.771	16.245	1.00	9.33	6	C
ATOM	1798	CZ	PHE	D	5	30.417	27.024	17.108	1.00	9.51	6	C
ATOM	1799	C	PHE	D	5	28.529	33.046	15.478	1.00	8.92	6	C
ATOM	1800	O	PHE	D	5	27.347	33.369	15.226	1.00	7.43	8	O
ATOM	1801	N	ILE	D	6	29.571	33.778	15.043	1.00	6.33	7	N
ATOM	1802	CA	ILE	D	6	29.321	35.020	14.346	1.00	5.35	6	C
ATOM	1803	CB	ILE	D	6	29.968	36.242	14.991	1.00	7.05	6	C
ATOM	1804	CG2	ILE	D	6	29.512	37.544	14.306	1.00	6.83	6	C
ATOM	1805	CG1	ILE	D	6	29.682	36.312	16.498	1.00	9.71	6	C
ATOM	1806	CD1	ILE	D	6	30.583	37.312	17.230	1.00	10.38	6	C
ATOM	1807	C	ILE	D	6	29.965	34.952	12.940	1.00	7.08	6	C
ATOM	1808	O	ILE	D	6	31.167	34.685	12.840	1.00	6.63	8	O
ATOM	1809	N	LEU	D	7	29.158	35.223	11.940	1.00	6.66	7	N
ATOM	1810	CA	LEU	D	7	29.569	35.267	10.534	1.00	8.26	6	C
ATOM	1811	CB	LEU	D	7	28.490	34.694	9.625	1.00	9.39	6	C
ATOM	1812	CG	LEU	D	7	28.278	33.182	9.719	1.00	12.12	6	C
ATOM	1813	CD1	LEU	D	7	26.964	32.819	9.001	1.00	12.30	6	C
ATOM	1814	CD2	LEU	D	7	29.452	32.442	9.113	1.00	12.62	6	C
ATOM	1815	C	LEU	D	7	29.753	36.727	10.173	1.00	9.44	6	C
ATOM	1816	O	LEU	D	7	28.969	37.612	10.588	1.00	8.72	8	O
ATOM	1817	N	MET	D	8	30.883	37.069	9.557	1.00	7.27	7	N
ATOM	1818	CA	MET	D	8	31.248	38.430	9.267	1.00	7.95	6	C
ATOM	1819	CB	MET	D	8	32.497	38.770	10.154	1.00	9.16	6	C
ATOM	1820	CG	MET	D	8	32.240	38.575	11.637	1.00	12.23	6	C
ATOM	1821	SD	MET	D	8	33.642	39.025	12.668	1.00	9.99	16	S
ATOM	1822	CE	MET	D	8	33.323	38.190	14.198	1.00	15.38	6	C
ATOM	1823	C	MET	D	8	31.695	38.640	7.819	1.00	9.51	6	C
ATOM	1824	O	MET	D	8	32.466	37.818	7.278	1.00	7.50	8	O
ATOM	1825	N	VAL	D	9	31.387	39.829	7.340	1.00	8.02	7	N
ATOM	1826	CA	VAL	D	9	31.905	40.303	6.047	1.00	10.82	6	C
ATOM	1827	CB	VAL	D	9	30.854	40.707	5.000	1.00	11.20	6	C
ATOM	1828	CG1	VAL	D	9	31.500	41.169	3.666	1.00	11.05	6	C
ATOM	1829	CG2	VAL	D	9	29.940	39.525	4.650	1.00	10.58	6	C
ATOM	1830	C	VAL	D	9	32.812	41.482	6.401	1.00	10.74	6	C
ATOM	1831	O	VAL	D	9	32.330	42.332	7.162	1.00	11.16	8	O
ATOM	1832	N	THR	D	10	34.049	41.503	5.908	1.00	8.55	7	N
ATOM	1833	CA	THR	D	10	34.950	42.605	6.235	1.00	9.63	6	C
ATOM	1834	CB	THR	D	10	36.316	42.145	6.788	1.00	7.41	6	C
ATOM	1835	OG1	THR	D	10	37.064	41.489	5.731	1.00	7.90	8	O
ATOM	1836	CG2	THR	D	10	36.134	41.119	7.892	1.00	6.20	6	C
ATOM	1837	C	THR	D	10	35.214	43.436	4.976	1.00	10.07	6	C
ATOM	1838	O	THR	D	10	34.887	42.902	3.935	1.00	5.93	8	O
ATOM	1839	N	ALA	D	11	35.781	44.632	5.043	1.00	8.15	7	N
ATOM	1840	CA	ALA	D	11	36.193	45.341	3.862	1.00	10.45	6	C
ATOM	1841	CB	ALA	D	11	36.773	46.737	4.229	1.00	9.59	6	C
ATOM	1842	C	ALA	D	11	37.261	44.555	3.115	1.00	11.75	6	C
ATOM	1843	O	ALA	D	11	38.008	43.789	3.744	1.00	11.01	8	O
ATOM	1844	N	ALA	D	12	37.428	44.805	1.813	1.00	11.13	7	N
ATOM	1845	CA	ALA	D	12	38.439	44.106	1.030	1.00	11.80	6	C
ATOM	1846	CB	ALA	D	12	38.456	44.611	−0.421	1.00	11.09	6	C
ATOM	1847	C	ALA	D	12	39.838	44.330	1.596	1.00	10.46	6	C
ATOM	1848	O	ALA	D	12	40.159	45.459	1.986	1.00	8.93	8	O
ATOM	1849	N	GLY	D	13	40.632	43.273	1.670	1.00	11.63	7	N
ATOM	1850	CA	GLY	D	13	42.018	43.352	2.113	1.00	9.40	6	C
ATOM	1851	C	GLY	D	13	42.048	43.563	3.634	1.00	10.22	6	C
ATOM	1852	O	GLY	D	13	43.122	43.919	4.107	1.00	7.69	8	O
ATOM	1853	N	LYS	D	14	40.965	43.319	4.365	1.00	8.00	7	N
ATOM	1854	CA	LYS	D	14	41.015	43.549	5.807	1.00	10.05	6	C
ATOM	1855	CB	LYS	D	14	39.991	44.631	6.218	1.00	11.34	6	C
ATOM	1856	CG	LYS	D	14	40.323	46.070	5.765	1.00	13.42	6	C
ATOM	1857	CD	LYS	D	14	41.685	46.502	6.343	1.00	15.94	6	C
ATOM	1858	CE	LYS	D	14	41.973	47.965	6.014	1.00	17.06	6	C
ATOM	1859	NZ	LYS	D	14	43.258	48.433	6.607	1.00	15.63	7	N
ATOM	1860	C	LYS	D	14	40.739	42.306	6.612	1.00	8.73	6	C
ATOM	1861	O	LYS	D	14	40.729	42.391	7.849	1.00	8.72	8	O
ATOM	1862	N	GLU	D	15	40.392	41.175	5.995	1.00	8.24	7	N
ATOM	1863	CA	GLU	D	15	40.019	40.018	6.817	1.00	11.30	6	C
ATOM	1864	CB	GLU	D	15	39.552	38.840	6.006	1.00	12.74	6	C
ATOM	1865	CG	GLU	D	15	40.569	38.210	5.063	1.00	13.46	6	C
ATOM	1866	CD	GLU	D	15	39.892	37.220	4.102	1.00	15.23	6	C
ATOM	1867	OE1	GLU	D	15	38.702	36.868	4.120	1.00	10.38	8	O
ATOM	1868	OE2	GLU	D	15	40.658	36.700	3.250	1.00	17.69	8	O
ATOM	1869	C	GLU	D	15	41.152	39.617	7.758	1.00	11.05	6	C
ATOM	1870	O	GLU	D	15	40.864	39.297	8.907	1.00	11.86	8	O
ATOM	1871	N	ARG	D	16	42.382	39.633	7.311	1.00	11.96	7	N
ATOM	1872	CA	ARG	D	16	43.472	39.262	8.208	1.00	14.89	6	C
ATOM	1873	CB	ARG	D	16	44.805	39.220	7.437	1.00	17.84	6	C
ATOM	1874	CG	ARG	D	16	45.966	39.007	8.388	1.00	25.50	6	C
ATOM	1875	CD	ARG	D	16	47.263	38.621	7.649	1.00	31.98	6	C
ATOM	1876	NE	ARG	D	16	48.220	38.168	8.650	1.00	37.59	7	N
ATOM	1877	CZ	ARG	D	16	49.449	37.704	8.576	1.00	40.87	6	C
ATOM	1878	NH1	ARG	D	16	50.073	37.573	7.404	1.00	43.35	7	N
ATOM	1879	NH2	ARG	D	16	50.078	37.359	9.694	1.00	41.61	7	N
ATOM	1880	C	ARG	D	16	43.580	40.265	9.363	1.00	11.57	6	C
ATOM	1881	O	ARG	D	16	43.846	39.856	10.471	1.00	7.54	8	O
ATOM	1882	N	GLU	D	17	43.509	41.574	9.058	1.00	8.70	7	N
ATOM	1883	CA	GLU	D	17	43.520	42.590	10.104	1.00	11.16	6	C
ATOM	1884	CB	GLU	D	17	43.356	43.975	9.464	1.00	10.95	6	C
ATOM	1885	CG	GLU	D	17	43.321	45.161	10.442	1.00	11.37	6	C
ATOM	1886	CD	GLU	D	17	43.336	46.423	9.614	1.00	14.08	6	C
ATOM	1887	OE1	GLU	D	17	44.230	46.626	8.769	1.00	11.49	8	O
ATOM	1888	OE2	GLU	D	17	42.391	47.252	9.756	1.00	14.65	8	O
ATOM	1889	C	GLU	D	17	42.415	42.345	11.131	1.00	10.84	6	C
ATOM	1890	O	GLU	D	17	42.610	42.536	12.360	1.00	9.09	8	O
ATOM	1891	N	VAL	D	18	41.222	41.917	10.678	1.00	9.00	7	N
ATOM	1892	CA	VAL	D	18	40.148	41.641	11.625	1.00	9.27	6	C
ATOM	1893	CB	VAL	D	18	38.804	41.488	10.876	1.00	9.98	6	C
ATOM	1894	CG1	VAL	D	18	37.657	41.058	11.792	1.00	9.93	6	C
ATOM	1895	CG2	VAL	D	18	38.445	42.837	10.240	1.00	8.46	6	C
ATOM	1896	C	VAL	D	18	40.467	40.420	12.475	1.00	8.32	6	C
ATOM	1897	O	VAL	D	18	40.313	40.366	13.706	1.00	6.46	8	O
ATOM	1898	N	MET	D	19	40.966	39.375	11.776	1.00	5.78	7	N
ATOM	1899	CA	MET	D	19	41.370	38.173	12.470	1.00	7.84	6	C
ATOM	1900	CB	MET	D	19	42.012	37.108	11.544	1.00	7.18	6	C
ATOM	1901	CG	MET	D	19	40.955	36.423	10.674	1.00	10.79	6	C
ATOM	1902	SD	MET	D	19	40.066	35.123	11.568	1.00	9.43	16	S
ATOM	1903	CE	MET	D	19	41.320	33.849	11.585	1.00	13.35	6	C
ATOM	1904	C	MET	D	19	42.380	38.513	13.580	1.00	8.79	6	C
ATOM	1905	O	MET	D	19	42.398	37.821	14.587	1.00	6.86	8	O
ATOM	1906	N	GLU	D	20	43.327	39.417	13.289	1.00	8.74	7	N
ATOM	1907	CA	GLU	D	20	44.322	39.799	14.331	1.00	12.83	6	C
ATOM	1908	CB	GLU	D	20	45.435	40.642	13.699	1.00	11.30	6	C
ATOM	1909	CG	GLU	D	20	46.357	39.657	12.930	1.00	13.63	6	C
ATOM	1910	CD	GLU	D	20	47.519	40.364	12.253	1.00	17.21	6	C
ATOM	1911	OE1	GLU	D	20	47.597	41.620	12.258	1.00	17.52	8	O
ATOM	1912	OE2	GLU	D	20	48.352	39.656	11.622	1.00	17.62	8	O
ATOM	1913	C	GLU	D	20	43.639	40.472	15.520	1.00	12.42	6	C
ATOM	1914	O	GLU	D	20	43.980	40.207	16.673	1.00	13.73	8	O
ATOM	1915	N	LYS	D	21	42.617	41.275	15.271	1.00	10.66	7	N
ATOM	1916	CA	LYS	D	21	41.854	41.867	16.365	1.00	11.11	6	C
ATOM	1917	CB	LYS	D	21	40.878	42.958	15.892	1.00	10.31	6	C
ATOM	1918	CG	LYS	D	21	41.568	44.254	15.563	1.00	11.75	6	C
ATOM	1919	CD	LYS	D	21	40.551	45.276	15.062	1.00	12.69	6	C
ATOM	1920	CE	LYS	D	21	41.190	46.632	14.741	1.00	14.75	6	C
ATOM	1921	NZ	LYS	D	21	40.107	47.556	14.250	1.00	12.59	7	N
ATOM	1922	C	LYS	D	21	41.115	40.792	17.136	1.00	8.78	6	C
ATOM	1923	O	LYS	D	21	41.229	40.694	18.372	1.00	10.75	8	O
ATOM	1924	N	LEU	D	22	40.465	39.846	16.472	1.00	10.46	7	N
ATOM	1925	CA	LEU	D	22	39.667	38.802	17.134	1.00	8.87	6	C
ATOM	1926	CB	LEU	D	22	38.920	37.980	16.061	1.00	8.01	6	C
ATOM	1927	CG	LEU	D	22	37.883	38.808	15.271	1.00	10.13	6	C
ATOM	1928	CD1	LEU	D	22	37.464	38.033	14.021	1.00	9.62	6	C
ATOM	1929	CD2	LEU	D	22	36.664	39.137	16.170	1.00	8.70	6	C
ATOM	1930	C	LEU	D	22	40.536	37.837	17.936	1.00	10.00	6	C
ATOM	1931	O	LEU	D	22	40.171	37.498	19.077	1.00	7.47	8	O
ATOM	1932	N	LEU	D	23	41.707	37.413	17.394	1.00	7.02	7	N
ATOM	1933	CA	LEU	D	23	42.521	36.497	18.203	1.00	10.23	6	C
ATOM	1934	CB	LEU	D	23	43.459	35.688	17.309	1.00	11.12	6	C
ATOM	1935	CG	LEU	D	23	42.767	34.912	16.180	1.00	13.04	6	C
ATOM	1936	CD1	LEU	D	23	43.728	34.528	15.057	1.00	11.71	6	C
ATOM	1937	CD2	LEU	D	23	42.107	33.666	16.753	1.00	12.37	6	C
ATOM	1938	C	LEU	D	23	43.234	37.115	19.399	1.00	10.47	6	C
ATOM	1939	O	LEU	D	23	43.943	36.413	20.157	1.00	10.67	8	O
ATOM	1940	N	ALA	D	24	43.032	38.376	19.741	1.00	8.71	7	N
ATOM	1941	CA	ALA	D	24	43.504	39.013	20.928	1.00	10.88	6	C
ATOM	1942	CB	ALA	D	24	44.146	40.395	20.663	1.00	10.61	6	C
ATOM	1943	C	ALA	D	24	42.298	39.250	21.861	1.00	12.75	6	C
ATOM	1944	O	ALA	D	24	42.581	39.689	22.961	1.00	11.80	8	O
ATOM	1945	N	MET	D	25	41.070	38.842	21.482	1.00	10.78	7	N
ATOM	1946	CA	MET	D	25	39.984	39.163	22.443	1.00	12.47	6	C
ATOM	1947	CB	MET	D	25	38.724	39.513	21.657	1.00	11.87	6	C
ATOM	1948	CG	MET	D	25	38.837	40.708	20.724	1.00	9.43	6	C
ATOM	1949	SD	MET	D	25	37.279	40.909	19.751	1.00	7.93	16	S
ATOM	1950	CE	MET	D	25	37.656	42.472	18.986	1.00	8.17	6	C
ATOM	1951	C	MET	D	25	39.756	37.981	23.364	1.00	10.74	6	C
ATOM	1952	O	MET	D	25	39.689	36.838	22.907	1.00	10.38	8	O
ATOM	1953	N	PRO	D	26	39.638	38.173	24.662	1.00	10.43	7	N
ATOM	1954	CD	PRO	D	26	39.570	39.495	25.327	1.00	11.37	6	C
ATOM	1955	CA	PRO	D	26	39.297	37.068	25.552	1.00	10.14	6	C
ATOM	1956	CB	PRO	D	26	38.977	37.760	26.908	1.00	11.47	6	C
ATOM	1957	CG	PRO	D	26	39.571	39.129	26.804	1.00	13.17	6	C
ATOM	1958	C	PRO	D	26	38.094	36.224	25.147	1.00	8.78	6	C
ATOM	1959	O	PRO	D	26	38.113	34.961	25.329	1.00	7.44	8	O
ATOM	1960	N	GLU	D	27	37.067	36.856	24.599	1.00	7.06	7	N
ATOM	1961	CA	GLU	D	27	35.809	36.171	24.302	1.00	9.61	6	C
ATOM	1962	CB	GLU	D	27	34.693	37.232	24.074	1.00	10.96	6	C
ATOM	1963	CG	GLU	D	27	34.496	38.142	25.290	1.00	13.96	6	C
ATOM	1964	CD	GLU	D	27	35.375	39.387	25.273	1.00	15.97	6	C
ATOM	1965	OE1	GLU	D	27	36.379	39.456	24.532	1.00	13.92	8	O
ATOM	1966	OE2	GLU	D	27	34.937	40.411	25.876	1.00	16.96	8	O
ATOM	1967	C	GLU	D	27	35.818	35.290	23.070	1.00	8.19	6	C
ATOM	1968	O	GLU	D	27	35.104	34.293	23.034	1.00	6.20	8	O
ATOM	1969	N	VAL	D	28	36.862	35.512	22.223	1.00	8.44	7	N
ATOM	1970	CA	VAL	D	28	36.933	34.688	20.998	1.00	7.24	6	C
ATOM	1971	CB	VAL	D	28	37.735	35.371	19.882	1.00	3.76	6	C
ATOM	1972	CG1	VAL	D	28	38.115	34.476	18.758	1.00	3.75	6	C
ATOM	1973	CG2	VAL	D	28	36.991	36.648	19.370	1.00	3.95	6	C
ATOM	1974	C	VAL	D	28	37.547	33.354	21.308	1.00	9.27	6	C
ATOM	1975	O	VAL	D	28	38.709	33.330	21.734	1.00	9.19	8	O
ATOM	1976	N	LYS	D	29	36.868	32.228	21.065	1.00	9.77	7	N
ATOM	1977	CA	LYS	D	29	37.439	30.911	21.290	1.00	10.82	6	C
ATOM	1978	CB	LYS	D	29	36.354	29.989	21.860	1.00	12.93	6	C
ATOM	1979	CG	LYS	D	29	35.708	30.606	23.097	1.00	15.22	6	C
ATOM	1980	CD	LYS	D	29	36.573	30.622	24.356	1.00	16.50	6	C
ATOM	1981	CE	LYS	D	29	36.919	32.063	24.674	1.00	18.62	6	C
ATOM	1982	NZ	LYS	D	29	37.533	32.336	26.009	1.00	20.84	7	N
ATOM	1983	C	LYS	D	29	38.023	30.242	20.062	1.00	11.20	6	C
ATOM	1984	O	LYS	D	29	38.928	29.399	20.213	1.00	10.74	8	O
ATOM	1985	N	GLU	D	30	37.527	30.591	18.876	1.00	10.26	7	N
ATOM	1986	CA	GLU	D	30	38.068	30.038	17.625	1.00	10.81	6	C
ATOM	1987	CB	GLU	D	30	37.655	28.615	17.277	1.00	13.90	6	C
ATOM	1988	CG	GLU	D	30	36.198	28.375	16.965	1.00	18.66	6	C
ATOM	1989	CD	GLU	D	30	35.861	26.876	16.789	1.00	20.56	6	C
ATOM	1990	OE1	GLU	D	30	36.678	26.028	16.448	1.00	17.38	8	O
ATOM	1991	OE2	GLU	D	30	34.684	26.508	16.956	1.00	21.70	8	O
ATOM	1992	C	GLU	D	30	37.675	31.011	16.512	1.00	10.06	6	C
ATOM	1993	O	GLU	D	30	36.609	31.646	16.617	1.00	7.37	8	O
ATOM	1994	N	ALA	D	31	38.502	31.177	15.507	1.00	8.02	7	N
ATOM	1995	CA	ALA	D	31	38.200	32.119	14.421	1.00	7.12	6	C
ATOM	1996	CB	ALA	D	31	38.807	33.489	14.683	1.00	8.42	6	C
ATOM	1997	C	ALA	D	31	38.745	31.565	13.117	1.00	8.88	6	C
ATOM	1998	O	ALA	D	31	39.884	31.020	13.144	1.00	8.65	8	O
ATOM	1999	N	TYR	D	32	37.999	31.613	12.001	1.00	5.43	7	N
ATOM	2000	CA	TYR	D	32	38.546	31.045	10.796	1.00	6.36	6	C
ATOM	2001	CB	TYR	D	32	37.990	29.674	10.391	1.00	8.15	6	C
ATOM	2002	CG	TYR	D	32	38.426	28.515	11.256	1.00	10.64	6	C
ATOM	2003	CD1	TYR	D	32	39.545	27.765	10.930	1.00	13.77	6	C
ATOM	2004	CE1	TYR	D	32	39.920	26.682	11.711	1.00	15.51	6	C
ATOM	2005	CD2	TYR	D	32	37.754	28.227	12.419	1.00	11.24	6	C
ATOM	2006	CE2	TYR	D	32	38.115	27.173	13.217	1.00	12.74	6	C
ATOM	2007	CZ	TYR	D	32	39.201	26.419	12.861	1.00	14.10	6	C
ATOM	2008	OH	TYR	D	32	39.533	25.377	13.684	1.00	16.30	8	O
ATOM	2009	C	TYR	D	32	38.154	31.873	9.560	1.00	7.98	6	C
ATOM	2010	O	TYR	D	32	37.040	32.416	9.586	1.00	7.94	8	O
ATOM	2011	N	VAL	D	33	39.074	31.877	8.611	1.00	6.38	7	N
ATOM	2012	CA	VAL	D	33	38.758	32.536	7.348	1.00	7.52	6	C
ATOM	2013	CB	VAL	D	33	39.981	32.990	6.536	1.00	8.07	6	C
ATOM	2014	CG1	VAL	D	33	39.567	33.517	5.162	1.00	6.28	6	C
ATOM	2015	CG2	VAL	D	33	40.723	34.076	7.330	1.00	7.68	6	C
ATOM	2016	C	VAL	D	33	37.968	31.475	6.595	1.00	7.23	6	C
ATOM	2017	O	VAL	D	33	38.398	30.299	6.681	1.00	10.00	8	O
ATOM	2018	N	VAL	D	34	36.784	31.773	6.055	1.00	6.32	7	N
ATOM	2019	CA	VAL	D	34	36.024	30.715	5.372	1.00	6.20	6	C
ATOM	2020	CB	VAL	D	34	34.708	30.380	6.088	1.00	8.45	6	C
ATOM	2021	CG1	VAL	D	34	34.870	29.568	7.387	1.00	8.52	6	C
ATOM	2022	CG2	VAL	D	34	33.920	31.673	6.419	1.00	8.05	6	C
ATOM	2023	C	VAL	D	34	35.687	31.195	3.959	1.00	8.31	6	C
ATOM	2024	O	VAL	D	34	35.649	32.430	3.697	1.00	8.44	8	O
ATOM	2025	N	TYR	D	35	35.506	30.287	3.043	1.00	7.60	7	N
ATOM	2026	CA	TYR	D	35	35.035	30.540	1.693	1.00	10.70	6	C
ATOM	2027	CB	TYR	D	35	34.992	29.145	0.966	1.00	13.94	6	C
ATOM	2028	CG	TYR	D	35	36.287	28.648	0.406	1.00	19.41	6	C
ATOM	2029	CD1	TYR	D	35	36.500	28.632	−0.976	1.00	21.68	6	C
ATOM	2030	CE1	TYR	D	35	37.708	28.179	−1.499	1.00	23.69	6	C
ATOM	2031	CD2	TYR	D	35	37.334	28.196	1.232	1.00	21.93	6	C
ATOM	2032	CE2	TYR	D	35	38.533	27.739	0.695	1.00	21.21	6	C
ATOM	2033	CZ	TYR	D	35	38.714	27.728	−0.672	1.00	23.19	6	C
ATOM	2034	OH	TYR	D	35	39.907	27.295	−1.250	1.00	23.55	8	O
ATOM	2035	C	TYR	D	35	33.570	31.004	1.702	1.00	9.18	6	C
ATOM	2036	O	TYR	D	35	32.887	30.788	2.719	1.00	7.05	8	O
ATOM	2037	N	GLY	D	36	33.114	31.550	0.583	1.00	9.23	7	N
ATOM	2038	CA	GLY	D	36	31.703	31.882	0.420	1.00	8.59	6	C
ATOM	2039	C	GLY	D	36	31.335	33.330	0.669	1.00	10.03	6	C
ATOM	2040	O	GLY	D	36	32.197	34.227	0.709	1.00	8.03	8	O
ATOM	2041	N	GLU	D	37	30.038	33.530	0.994	1.00	9.60	7	N
ATOM	2042	CA	GLU	D	37	29.553	34.874	1.190	1.00	13.84	6	C
ATOM	2043	CB	GLU	D	37	28.042	34.888	1.222	1.00	20.20	6	C
ATOM	2044	CG	GLU	D	37	27.302	34.244	2.338	1.00	26.34	6	C
ATOM	2045	CD	GLU	D	37	25.826	34.649	2.298	1.00	29.65	6	C
ATOM	2046	OE1	GLU	D	37	24.966	33.760	2.335	1.00	33.05	8	O
ATOM	2047	OE2	GLU	D	37	25.505	35.844	2.279	1.00	32.09	8	O
ATOM	2048	C	GLU	D	37	30.156	35.589	2.393	1.00	13.26	6	C
ATOM	2049	O	GLU	D	37	30.257	36.818	2.316	1.00	11.83	8	O
ATOM	2050	N	TYR	D	38	30.463	34.895	3.458	1.00	11.24	7	N
ATOM	2051	CA	TYR	D	38	31.113	35.525	4.609	1.00	13.22	6	C
ATOM	2052	CB	TYR	D	38	30.602	34.920	5.924	1.00	14.41	6	C
ATOM	2053	CG	TYR	D	38	29.125	35.241	6.086	1.00	17.44	6	C
ATOM	2054	CD1	TYR	D	38	28.751	36.473	6.607	1.00	19.66	6	C
ATOM	2055	CE1	TYR	D	38	27.404	36.793	6.741	1.00	22.87	6	C
ATOM	2056	CD2	TYR	D	38	28.164	34.332	5.690	1.00	19.08	6	C
ATOM	2057	CE2	TYR	D	38	26.806	34.627	5.817	1.00	21.26	6	C
ATOM	2058	CZ	TYR	D	38	26.460	35.851	6.360	1.00	23.15	6	C
ATOM	2059	OH	TYR	D	38	25.146	36.171	6.515	1.00	25.72	8	O
ATOM	2060	C	TYR	D	38	32.632	35.321	4.547	1.00	12.41	6	C
ATOM	2061	O	TYR	D	38	33.089	34.307	4.013	1.00	8.37	8	O
ATOM	2062	N	ASP	D	39	33.400	36.289	5.061	1.00	11.84	7	N
ATOM	2063	CA	ASP	D	39	34.846	36.127	5.064	1.00	10.07	6	C
ATOM	2064	CB	ASP	D	39	35.517	37.526	5.140	1.00	12.25	6	C
ATOM	2065	CG	ASP	D	39	35.115	38.291	3.866	1.00	12.99	6	C
ATOM	2066	OD1	ASP	D	39	35.289	37.666	2.802	1.00	11.90	8	O
ATOM	2067	OD2	ASP	D	39	34.602	39.408	3.976	1.00	12.15	8	O
ATOM	2068	C	ASP	D	39	35.285	35.299	6.253	1.00	8.98	6	C
ATOM	2069	O	ASP	D	39	36.213	34.516	6.139	1.00	9.58	8	O
ATOM	2070	N	LEU	D	40	34.658	35.524	7.416	1.00	5.50	7	N
ATOM	2071	CA	LEU	D	40	35.088	34.829	8.633	1.00	7.68	6	C
ATOM	2072	CB	LEU	D	40	35.715	35.942	9.546	1.00	8.52	6	C
ATOM	2073	CG	LEU	D	40	36.837	36.793	9.009	1.00	14.09	6	C
ATOM	2074	CD1	LEU	D	40	37.168	37.996	9.919	1.00	13.28	6	C
ATOM	2075	CD2	LEU	D	40	38.110	35.938	8.801	1.00	14.05	6	C
ATOM	2076	C	LEU	D	40	33.952	34.236	9.461	1.00	7.29	6	C
ATOM	2077	O	LEU	D	40	32.834	34.770	9.431	1.00	7.50	8	O
ATOM	2078	N	ILE	D	41	34.225	33.291	10.308	1.00	6.52	7	N
ATOM	2079	CA	ILE	D	41	33.347	32.659	11.251	1.00	8.65	6	C
ATOM	2080	CB	ILE	D	41	32.757	31.294	10.866	1.00	7.09	6	C
ATOM	2081	CG2	ILE	D	41	33.763	30.136	10.738	1.00	7.76	6	C
ATOM	2082	CG1	ILE	D	41	31.714	30.864	11.933	1.00	7.44	6	C
ATOM	2083	CD1	ILE	D	41	30.882	29.692	11.430	1.00	8.47	6	C
ATOM	2084	C	ILE	D	41	34.095	32.701	12.586	1.00	10.10	6	C
ATOM	2085	O	ILE	D	41	35.293	32.408	12.685	1.00	9.03	8	O
ATOM	2086	N	VAL	D	42	33.391	33.059	13.669	1.00	10.09	7	N
ATOM	2087	CA	VAL	D	42	34.073	33.170	14.978	1.00	10.73	6	C
ATOM	2088	CB	VAL	D	42	34.404	34.614	15.388	1.00	13.00	6	C
ATOM	2089	CG1	VAL	D	42	33.245	35.362	16.063	1.00	14.99	6	C
ATOM	2090	CG2	VAL	D	42	35.471	34.830	16.425	1.00	12.34	6	C
ATOM	2091	C	VAL	D	42	33.159	32.540	16.008	1.00	9.22	6	C
ATOM	2092	O	VAL	D	42	31.939	32.782	15.940	1.00	9.43	8	O
ATOM	2093	N	LYS	D	43	33.739	31.804	16.934	1.00	6.57	7	N
ATOM	2094	CA	LYS	D	43	32.976	31.281	18.049	1.00	7.49	6	C
ATOM	2095	CB	LYS	D	43	33.242	29.814	18.298	1.00	8.66	6	C
ATOM	2096	CG	LYS	D	43	32.509	29.240	19.502	1.00	10.98	6	C
ATOM	2097	CD	LYS	D	43	32.987	27.756	19.527	1.00	12.07	6	C
ATOM	2098	CE	LYS	D	43	32.765	27.099	20.873	1.00	14.03	6	C
ATOM	2099	NZ	LYS	D	43	33.327	25.695	20.768	1.00	12.83	7	N
ATOM	2100	C	LYS	D	43	33.370	32.072	19.277	1.00	7.78	6	C
ATOM	2101	O	LYS	D	43	34.586	32.291	19.497	1.00	8.73	8	O
ATOM	2102	N	VAL	D	44	32.387	32.621	19.972	1.00	8.73	7	N
ATOM	2103	CA	VAL	D	44	32.629	33.468	21.129	1.00	7.44	6	C
ATOM	2104	CB	VAL	D	44	32.310	34.941	20.905	1.00	8.98	6	C
ATOM	2105	CG1	VAL	D	44	33.072	35.522	19.705	1.00	7.87	6	C
ATOM	2106	CG2	VAL	D	44	30.806	35.154	20.649	1.00	8.94	6	C
ATOM	2107	C	VAL	D	44	31.798	32.956	22.304	1.00	9.01	6	C
ATOM	2108	O	VAL	D	44	30.837	32.209	22.117	1.00	9.60	8	O
ATOM	2109	N	GLU	D	45	32.254	33.197	23.525	1.00	9.31	7	N
ATOM	2110	CA	GLU	D	45	31.678	32.770	24.753	1.00	12.52	6	C
ATOM	2111	CB	GLU	D	45	32.392	31.581	25.436	1.00	14.38	6	C
ATOM	2112	CG	GLU	D	45	32.127	30.265	24.685	1.00	18.54	6	C
ATOM	2113	CD	GLU	D	45	32.979	29.114	25.184	1.00	22.44	6	C
ATOM	2114	OE1	GLU	D	45	33.025	28.070	24.514	1.00	23.21	8	O
ATOM	2115	OE2	GLU	D	45	33.613	29.221	26.263	1.00	23.95	8	O
ATOM	2116	C	GLU	D	45	31.715	33.963	25.718	1.00	13.18	6	C
ATOM	2117	O	GLU	D	45	32.691	34.687	25.785	1.00	10.66	8	O
ATOM	2118	N	THR	D	46	30.602	34.241	26.380	1.00	13.36	7	N
ATOM	2119	CA	THR	D	46	30.527	35.298	27.381	1.00	13.78	6	C
ATOM	2120	CB	THR	D	46	29.805	36.570	26.915	1.00	15.75	6	C
ATOM	2121	OG1	THR	D	46	28.450	36.171	26.648	1.00	14.48	8	O
ATOM	2122	CG2	THR	D	46	30.488	37.200	25.710	1.00	15.69	6	C
ATOM	2123	C	THR	D	46	29.791	34.679	28.574	1.00	14.47	6	C
ATOM	2124	O	THR	D	46	29.069	33.663	28.418	1.00	13.33	8	O
ATOM	2125	N	ASP	D	47	29.938	35.295	29.735	1.00	13.95	7	N
ATOM	2126	CA	ASP	D	47	29.336	34.725	30.929	1.00	16.99	6	C
ATOM	2127	CB	ASP	D	47	29.734	35.409	32.247	1.00	22.34	6	C
ATOM	2128	CG	ASP	D	47	31.173	35.190	32.639	1.00	27.62	6	C
ATOM	2129	OD1	ASP	D	47	31.825	34.359	31.947	1.00	31.21	8	O
ATOM	2130	OD2	ASP	D	47	31.713	35.782	33.605	1.00	30.67	8	O
ATOM	2131	C	ASP	D	47	27.819	34.864	30.828	1.00	14.12	6	C
ATOM	2132	O	ASP	D	47	27.153	33.940	31.227	1.00	15.12	8	O
ATOM	2133	N	THR	D	48	27.297	35.969	30.327	1.00	11.97	7	N
ATOM	2134	CA	THR	D	48	25.875	36.189	30.244	1.00	13.15	6	C
ATOM	2135	CB	THR	D	48	25.373	37.236	31.240	1.00	13.15	6	C
ATOM	2136	OG1	THR	D	48	26.017	38.511	30.973	1.00	15.41	8	O
ATOM	2137	CG2	THR	D	48	25.612	36.804	32.692	1.00	14.04	6	C
ATOM	2138	C	THR	D	48	25.446	36.742	28.877	1.00	14.57	6	C
ATOM	2139	O	THR	D	48	26.291	37.155	28.065	1.00	12.38	8	O
ATOM	2140	N	LEU	D	49	24.125	36.733	28.685	1.00	11.23	7	N
ATOM	2141	CA	LEU	D	49	23.583	37.284	27.437	1.00	13.73	6	C
ATOM	2142	CB	LEU	D	49	22.065	37.080	27.339	1.00	12.51	6	C
ATOM	2143	CG	LEU	D	49	21.364	37.558	26.069	1.00	14.18	6	C
ATOM	2144	CD1	LEU	D	49	22.014	37.002	24.817	1.00	11.03	6	C
ATOM	2145	CD2	LEU	D	49	19.881	37.088	26.143	1.00	13.29	6	C
ATOM	2146	C	LEU	D	49	23.855	38.778	27.338	1.00	13.40	6	C
ATOM	2147	O	LEU	D	49	24.102	39.374	26.296	1.00	13.30	8	O
ATOM	2148	N	LYS	D	50	23.652	39.471	28.462	1.00	13.92	7	N
ATOM	2149	CA	LYS	D	50	23.916	40.892	28.544	1.00	16.34	6	C
ATOM	2150	CB	LYS	D	50	23.691	41.327	30.019	1.00	20.47	6	C
ATOM	2151	CG	LYS	D	50	23.302	42.793	30.072	1.00	26.88	6	C
ATOM	2152	CD	LYS	D	50	24.075	43.538	31.151	1.00	31.08	6	C
ATOM	2153	CE	LYS	D	50	23.804	45.046	31.108	1.00	32.48	6	C
ATOM	2154	NZ	LYS	D	50	23.836	45.593	32.509	1.00	34.98	7	N
ATOM	2155	C	LYS	D	50	25.348	41.230	28.148	1.00	13.33	6	C
ATOM	2156	O	LYS	D	50	25.614	42.240	27.468	1.00	13.39	8	O
ATOM	2157	N	ASP	D	51	26.299	40.411	28.563	1.00	12.48	7	N
ATOM	2158	CA	ASP	D	51	27.692	40.626	28.146	1.00	15.10	6	C
ATOM	2159	CB	ASP	D	51	28.663	39.759	28.947	1.00	16.35	6	C
ATOM	2160	CG	ASP	D	51	28.728	40.315	30.377	1.00	18.78	6	C
ATOM	2161	OD1	ASP	D	51	28.465	41.527	30.553	1.00	19.84	8	O
ATOM	2162	OD2	ASP	D	51	29.036	39.468	31.217	1.00	19.28	8	O
ATOM	2163	C	ASP	D	51	27.868	40.329	26.659	1.00	12.69	6	C
ATOM	2164	O	ASP	D	51	28.701	40.979	26.028	1.00	14.63	8	O
ATOM	2165	N	LEU	D	52	27.187	39.306	26.139	1.00	11.08	7	N
ATOM	2166	CA	LEU	D	52	27.246	39.107	24.685	1.00	10.83	6	C
ATOM	2167	CB	LEU	D	52	26.456	37.864	24.267	1.00	10.10	6	C
ATOM	2168	CG	LEU	D	52	26.605	37.462	22.793	1.00	9.50	6	C
ATOM	2169	CD1	LEU	D	52	28.001	36.865	22.523	1.00	9.81	6	C
ATOM	2170	CD2	LEU	D	52	25.529	36.464	22.405	1.00	7.72	6	C
ATOM	2171	C	LEU	D	52	26.704	40.331	23.976	1.00	12.03	6	C
ATOM	2172	O	LEU	D	52	27.289	40.837	22.985	1.00	10.16	8	O
ATOM	2173	N	ASP	D	53	25.546	40.859	24.479	1.00	11.64	7	N
ATOM	2174	CA	ASP	D	53	24.983	42.043	23.860	1.00	12.95	6	C
ATOM	2175	CB	ASP	D	53	23.750	42.582	24.595	1.00	14.34	6	C
ATOM	2176	CG	ASP	D	53	22.563	41.630	24.609	1.00	15.63	6	C
ATOM	2177	OD1	ASP	D	53	22.449	40.684	23.791	1.00	15.62	8	O
ATOM	2178	OD2	ASP	D	53	21.691	41.824	25.492	1.00	16.34	8	O
ATOM	2179	C	ASP	D	53	26.040	43.147	23.688	1.00	15.69	6	C
ATOM	2180	O	ASP	D	53	26.150	43.779	22.627	1.00	13.41	8	O
ATOM	2181	N	GLN	D	54	26.714	43.454	24.782	1.00	15.39	7	N
ATOM	2182	CA	GLN	D	54	27.750	44.490	24.826	1.00	19.04	6	C
ATOM	2183	CB	GLN	D	54	28.196	44.595	26.286	1.00	21.11	6	C
ATOM	2184	CG	GLN	D	54	28.911	45.886	26.619	1.00	30.34	6	C
ATOM	2185	CD	GLN	D	54	29.355	45.897	28.070	1.00	35.43	6	C
ATOM	2186	OE1	GLN	D	54	29.038	45.001	28.873	1.00	38.74	8	O
ATOM	2187	NE2	GLN	D	54	30.131	46.936	28.390	1.00	37.61	7	N
ATOM	2188	C	GLN	D	54	28.943	44.195	23.929	1.00	13.99	6	C
ATOM	2189	O	GLN	D	54	29.388	45.028	23.162	1.00	12.65	8	O
ATOM	2190	N	PHE	D	55	29.447	42.978	23.978	1.00	15.43	7	N
ATOM	2191	CA	PHE	D	55	30.586	42.554	23.134	1.00	13.50	6	C
ATOM	2192	CB	PHE	D	55	30.897	41.093	23.483	1.00	12.42	6	C
ATOM	2193	CG	PHE	D	55	32.002	40.549	22.602	1.00	11.54	6	C
ATOM	2194	CD1	PHE	D	55	33.319	41.015	22.767	1.00	9.95	6	C
ATOM	2195	CD2	PHE	D	55	31.713	39.571	21.668	1.00	9.64	6	C
ATOM	2196	CE1	PHE	D	55	34.292	40.453	21.936	1.00	12.19	6	C
ATOM	2197	CE2	PHE	D	55	32.705	39.010	20.874	1.00	10.13	6	C
ATOM	2198	CZ	PHE	D	55	34.002	39.465	21.026	1.00	9.99	6	C
ATOM	2199	C	PHE	D	55	30.255	42.714	21.653	1.00	13.58	6	C
ATOM	2200	O	PHE	D	55	30.888	43.510	20.915	1.00	10.92	8	O
ATOM	2201	N	ILE	D	56	29.107	42.119	21.255	1.00	10.76	7	N
ATOM	2202	CA	ILE	D	56	28.785	42.189	19.830	1.00	11.96	6	C
ATOM	2203	CB	ILE	D	56	27.579	41.278	19.498	1.00	13.95	6	C
ATOM	2204	CG2	ILE	D	56	27.096	41.404	18.056	1.00	12.24	6	C
ATOM	2205	CG1	ILE	D	56	28.011	39.898	19.947	1.00	14.49	6	C
ATOM	2206	CD1	ILE	D	56	28.161	38.777	19.011	1.00	18.97	6	C
ATOM	2207	C	ILE	D	56	28.491	43.582	19.349	1.00	13.51	6	C
ATOM	2208	O	ILE	D	56	28.926	43.983	18.256	1.00	13.02	8	O
ATOM	2209	N	THR	D	57	27.710	44.341	20.110	1.00	15.60	7	N
ATOM	2210	CA	THR	D	57	27.326	45.675	19.621	1.00	17.80	6	C
ATOM	2211	CB	THR	D	57	26.048	46.210	20.297	1.00	19.23	6	C
ATOM	2212	OG1	THR	D	57	26.180	46.125	21.711	1.00	22.03	8	O
ATOM	2213	CG2	THR	D	57	24.810	45.352	20.028	1.00	20.73	6	C
ATOM	2214	C	THR	D	57	28.518	46.636	19.744	1.00	20.35	6	C
ATOM	2215	O	THR	D	57	28.824	47.295	18.729	1.00	22.00	8	O
ATOM	2216	N	GLU	D	58	29.389	46.530	20.744	1.00	20.17	7	N
ATOM	2217	CA	GLU	D	58	30.510	47.426	20.876	1.00	23.72	6	C
ATOM	2218	CB	GLU	D	58	30.773	47.819	22.355	1.00	27.15	6	C
ATOM	2219	CG	GLU	D	58	29.557	48.536	22.967	1.00	30.14	6	C
ATOM	2220	CD	GLU	D	58	29.380	49.919	22.337	1.00	33.67	6	C
ATOM	2221	OE1	GLU	D	58	30.396	50.630	22.041	1.00	35.18	8	O
ATOM	2222	OE2	GLU	D	58	28.204	50.285	22.109	1.00	34.26	8	O
ATOM	2223	C	GLU	D	58	31.818	46.930	20.286	1.00	22.92	6	C
ATOM	2224	O	GLU	D	58	32.507	47.785	19.723	1.00	22.33	8	O
ATOM	2225	N	LYS	D	59	32.204	45.660	20.404	1.00	20.11	7	N
ATOM	2226	CA	LYS	D	59	33.473	45.223	19.873	1.00	20.10	6	C
ATOM	2227	CB	LYS	D	59	34.111	44.113	20.719	1.00	21.48	6	C
ATOM	2228	CG	LYS	D	59	34.207	44.513	22.199	1.00	27.96	6	C
ATOM	2229	CD	LYS	D	59	35.424	45.373	22.500	1.00	30.31	6	C
ATOM	2230	CE	LYS	D	59	35.427	45.865	23.946	1.00	32.73	6	C
ATOM	2231	NZ	LYS	D	59	35.737	47.347	24.028	1.00	34.31	7	N
ATOM	2232	C	LYS	D	59	33.396	44.694	18.438	1.00	19.09	6	C
ATOM	2233	O	LYS	D	59	34.445	44.621	17.756	1.00	19.41	8	O
ATOM	2234	N	ILE	D	60	32.263	44.090	18.091	1.00	13.82	7	N
ATOM	2235	CA	ILE	D	60	32.200	43.489	16.762	1.00	12.95	6	C
ATOM	2236	CB	ILE	D	60	31.556	42.118	16.849	1.00	12.02	6	C
ATOM	2237	CG2	ILE	D	60	31.412	41.544	15.429	1.00	11.69	6	C
ATOM	2238	CG1	ILE	D	60	32.335	41.135	17.750	1.00	12.06	6	C
ATOM	2239	CD1	ILE	D	60	33.810	41.039	17.546	1.00	12.30	6	C
ATOM	2240	C	ILE	D	60	31.545	44.412	15.729	1.00	14.62	6	C
ATOM	2241	O	ILE	D	60	32.126	44.822	14.727	1.00	10.09	8	O
ATOM	2242	N	ARG	D	61	30.278	44.774	15.969	1.00	14.65	7	N
ATOM	2243	CA	ARG	D	61	29.523	45.610	15.045	1.00	16.07	6	C
ATOM	2244	CB	ARG	D	61	28.038	45.579	15.500	1.00	16.92	6	C
ATOM	2245	CG	ARG	D	61	27.363	44.212	15.262	1.00	17.47	6	C
ATOM	2246	CD	ARG	D	61	25.893	44.275	15.640	1.00	22.16	6	C
ATOM	2247	NE	ARG	D	61	25.086	43.063	15.705	1.00	20.80	7	N
ATOM	2248	CZ	ARG	D	61	23.799	42.867	15.496	1.00	20.73	6	C
ATOM	2249	NH1	ARG	D	61	22.940	43.817	15.183	1.00	21.08	7	N
ATOM	2250	NH2	ARG	D	61	23.194	41.692	15.674	1.00	19.70	7	N
ATOM	2251	C	ARG	D	61	30.081	47.007	14.834	1.00	15.30	6	C
ATOM	2252	O	ARG	D	61	29.919	47.548	13.729	1.00	12.83	8	O
ATOM	2253	N	LYS	D	62	30.862	47.581	15.726	1.00	13.69	7	N
ATOM	2254	CA	LYS	D	62	31.537	48.845	15.612	1.00	16.28	6	C
ATOM	2255	CB	LYS	D	62	31.355	49.671	16.910	1.00	19.57	6	C
ATOM	2256	CG	LYS	D	62	29.965	50.343	16.732	1.00	21.09	6	C
ATOM	2257	CD	LYS	D	62	29.347	50.574	18.073	1.00	24.81	6	C
ATOM	2258	CE	LYS	D	62	28.160	51.539	17.965	1.00	26.49	6	C
ATOM	2259	NZ	LYS	D	62	27.744	51.698	19.399	1.00	32.17	7	N
ATOM	2260	C	LYS	D	62	32.991	48.777	15.185	1.00	15.48	6	C
ATOM	2261	O	LYS	D	62	33.619	49.794	14.910	1.00	13.01	8	O
ATOM	2262	N	MET	D	63	33.483	47.575	14.930	1.00	13.64	7	N
ATOM	2263	CA	MET	D	63	34.840	47.469	14.347	1.00	14.05	6	C
ATOM	2264	CB	MET	D	63	35.250	46.002	14.371	1.00	14.96	6	C
ATOM	2265	CG	MET	D	63	36.702	45.765	13.995	1.00	17.59	6	C
ATOM	2266	SD	MET	D	63	37.077	44.017	13.778	1.00	16.00	16	S
ATOM	2267	CE	MET	D	63	36.816	43.394	15.447	1.00	16.24	6	C
ATOM	2268	C	MET	D	63	34.798	48.084	12.950	1.00	12.08	6	C
ATOM	2269	O	MET	D	63	33.998	47.740	12.079	1.00	8.64	8	O
ATOM	2270	N	PRO	D	64	35.692	49.011	12.624	1.00	12.28	7	N
ATOM	2271	CD	PRO	D	64	36.723	49.571	13.578	1.00	13.06	6	C
ATOM	2272	CA	PRO	D	64	35.610	49.760	11.398	1.00	11.60	6	C
ATOM	2273	CB	PRO	D	64	36.749	50.767	11.450	1.00	14.09	6	C
ATOM	2274	CG	PRO	D	64	37.175	50.838	12.874	1.00	14.47	6	C
ATOM	2275	C	PRO	D	64	35.697	48.907	10.137	1.00	11.66	6	C
ATOM	2276	O	PRO	D	64	35.144	49.337	9.117	1.00	9.20	8	O
ATOM	2277	N	GLU	D	65	36.518	47.855	10.133	1.00	7.96	7	N
ATOM	2278	CA	GLU	D	65	36.670	46.978	8.990	1.00	10.89	6	C
ATOM	2279	CB	GLU	D	65	37.858	46.024	9.221	1.00	13.55	6	C
ATOM	2280	CG	GLU	D	65	39.187	46.824	9.538	1.00	13.78	6	C
ATOM	2281	CD	GLU	D	65	39.461	46.983	11.033	1.00	16.55	6	C
ATOM	2282	OE1	GLU	D	65	38.484	47.049	11.844	1.00	12.89	8	O
ATOM	2283	OE2	GLU	D	65	40.649	47.099	11.496	1.00	15.86	8	O
ATOM	2284	C	GLU	D	65	35.406	46.138	8.682	1.00	11.19	6	C
ATOM	2285	O	GLU	D	65	35.350	45.423	7.680	1.00	7.50	8	O
ATOM	2286	N	ILE	D	66	34.519	45.952	9.674	1.00	10.12	7	N
ATOM	2287	CA	ILE	D	66	33.361	45.070	9.550	1.00	11.60	6	C
ATOM	2288	CB	ILE	D	66	32.970	44.480	10.918	1.00	13.04	6	C
ATOM	2289	CG2	ILE	D	66	31.591	43.825	10.916	1.00	13.13	6	C
ATOM	2290	CG1	ILE	D	66	34.098	43.486	11.300	1.00	13.41	6	C
ATOM	2291	CD1	ILE	D	66	33.797	42.450	12.339	1.00	16.26	6	C
ATOM	2292	C	ILE	D	66	32.247	45.760	8.785	1.00	12.88	6	C
ATOM	2293	O	ILE	D	66	31.842	46.893	9.084	1.00	11.94	8	O
ATOM	2294	N	GLN	D	67	31.690	45.048	7.820	1.00	13.32	7	N
ATOM	2295	CA	GLN	D	67	30.565	45.570	7.031	1.00	13.81	6	C
ATOM	2296	CB	GLN	D	67	30.876	45.313	5.537	1.00	17.32	6	C
ATOM	2297	CG	GLN	D	67	32.065	46.094	5.003	1.00	20.78	6	C
ATOM	2298	CD	GLN	D	67	32.258	45.972	3.503	1.00	25.96	6	C
ATOM	2299	OE1	GLN	D	67	32.984	46.769	2.874	1.00	26.83	8	O
ATOM	2300	NE2	GLN	D	67	31.666	44.957	2.880	1.00	26.96	7	N
ATOM	2301	C	GLN	D	67	29.249	44.883	7.366	1.00	14.11	6	C
ATOM	2302	O	GLN	D	67	28.204	45.520	7.260	1.00	12.99	8	O
ATOM	2303	N	MET	D	68	29.234	43.596	7.687	1.00	13.17	7	N
ATOM	2304	CA	MET	D	68	27.975	42.918	8.012	1.00	14.61	6	C
ATOM	2305	CB	MET	D	68	27.292	42.526	6.707	1.00	17.39	6	C
ATOM	2306	CG	MET	D	68	27.455	41.040	6.441	1.00	26.39	6	C
ATOM	2307	SD	MET	D	68	25.983	40.112	6.946	1.00	28.95	16	S
ATOM	2308	CE	MET	D	68	25.089	40.321	5.379	1.00	31.95	6	C
ATOM	2309	C	MET	D	68	28.269	41.745	8.924	1.00	12.16	6	C
ATOM	2310	O	MET	D	68	29.374	41.163	8.887	1.00	8.95	8	O
ATOM	2311	N	THR	D	69	27.352	41.409	9.826	1.00	10.00	7	N
ATOM	2312	CA	THR	D	69	27.548	40.286	10.750	1.00	9.18	6	C
ATOM	2313	CB	THR	D	69	27.973	40.679	12.180	1.00	10.80	6	C
ATOM	2314	OG1	THR	D	69	26.965	41.517	12.738	1.00	10.14	8	O
ATOM	2315	CG2	THR	D	69	29.266	41.533	12.207	1.00	8.79	6	C
ATOM	2316	C	THR	D	69	26.209	39.551	10.885	1.00	10.48	6	C
ATOM	2317	O	THR	D	69	25.177	40.204	10.825	1.00	9.21	8	O
ATOM	2318	N	SER	D	70	26.237	38.260	11.134	1.00	8.78	7	N
ATOM	2319	CA	SER	D	70	25.036	37.493	11.456	1.00	11.09	6	C
ATOM	2320	CB	SER	D	70	24.662	36.702	10.189	1.00	12.33	6	C
ATOM	2321	OG	SER	D	70	23.493	35.994	10.510	1.00	13.28	8	O
ATOM	2322	C	SER	D	70	25.401	36.622	12.648	1.00	12.05	6	C
ATOM	2323	O	SER	D	70	26.397	35.870	12.567	1.00	12.32	8	O
ATOM	2324	N	THR	D	71	24.700	36.673	13.769	1.00	10.51	7	N
ATOM	2325	CA	THR	D	71	25.097	35.890	14.952	1.00	9.85	6	C
ATOM	2326	CB	THR	D	71	25.203	36.844	16.156	1.00	11.18	6	C
ATOM	2327	OG1	THR	D	71	26.203	37.821	15.911	1.00	8.76	8	O
ATOM	2328	CG2	THR	D	71	25.517	36.186	17.508	1.00	12.67	6	C
ATOM	2329	C	THR	D	71	24.120	34.795	15.261	1.00	8.82	6	C
ATOM	2330	O	THR	D	71	22.916	35.051	15.240	1.00	9.45	8	O
ATOM	2331	N	MET	D	72	24.629	33.588	15.474	1.00	6.60	7	N
ATOM	2332	CA	MET	D	72	23.854	32.463	15.846	1.00	7.67	6	C
ATOM	2333	CB	MET	D	72	24.175	31.262	14.930	1.00	9.49	6	C
ATOM	2334	CG	MET	D	72	23.687	31.559	13.500	1.00	14.91	6	C
ATOM	2335	SD	MET	D	72	24.478	30.502	12.269	1.00	15.37	16	S
ATOM	2336	CE	MET	D	72	26.144	31.123	12.202	1.00	17.36	6	C
ATOM	2337	C	MET	D	72	24.124	32.078	17.306	1.00	7.83	6	C
ATOM	2338	O	MET	D	72	25.184	31.458	17.566	1.00	8.05	8	O
ATOM	2339	N	ILE	D	73	23.212	32.379	18.186	1.00	8.09	7	N
ATOM	2340	CA	ILE	D	73	23.332	32.016	19.610	1.00	8.99	6	C
ATOM	2341	CB	ILE	D	73	22.410	32.880	20.471	1.00	9.51	6	C
ATOM	2342	CG2	ILE	D	73	22.288	32.354	21.920	1.00	11.36	6	C
ATOM	2343	CG1	ILE	D	73	22.973	34.315	20.535	1.00	11.16	6	C
ATOM	2344	CD1	ILE	D	73	21.936	35.363	20.896	1.00	11.78	6	C
ATOM	2345	C	ILE	D	73	23.038	30.542	19.775	1.00	11.33	6	C
ATOM	2346	O	ILE	D	73	22.036	30.000	19.267	1.00	11.92	8	O
ATOM	2347	N	ALA	D	74	23.949	29.824	20.414	1.00	12.81	7	N
ATOM	2348	CA	ALA	D	74	23.809	28.415	20.674	1.00	16.28	6	C
ATOM	2349	CB	ALA	D	74	25.122	27.728	21.084	1.00	17.94	6	C
ATOM	2350	C	ALA	D	74	22.875	28.195	21.886	1.00	18.40	6	C
ATOM	2351	O	ALA	D	74	22.936	28.914	22.879	1.00	16.19	8	O
ATOM	2352	N	ILE	D	75	22.208	27.070	21.826	1.00	20.41	7	N
ATOM	2353	CA	ILE	D	75	21.496	26.531	22.968	1.00	24.59	6	C
ATOM	2354	CB	ILE	D	75	20.391	25.581	22.489	1.00	25.97	6	C
ATOM	2355	CG2	ILE	D	75	20.115	24.427	23.439	1.00	26.43	6	C
ATOM	2356	CG1	ILE	D	75	19.126	26.385	22.194	1.00	24.83	6	C
ATOM	2357	CD1	ILE	D	75	19.021	26.717	20.709	1.00	27.91	6	C
ATOM	2358	C	ILE	D	75	22.520	25.792	23.826	1.00	27.53	6	C
ATOM	2359	O	ILE	D	75	23.522	25.173	23.340	1.00	29.12	8	O
ATOM	2360	OT	ILE	D	75	22.263	25.858	25.044	1.00	29.73	8	O
ATOM	2361	O	HOH	W	1	10.122	48.309	2.632	1.00	71.67	8	O
ATOM	2362	O	HOH	W	2	43.515	40.335	4.275	1.00	2.02	8	O
ATOM	2363	O	HOH	W	3	25.096	40.046	14.391	1.00	4.72	8	O
ATOM	2364	O	HOH	W	4	14.309	48.257	1.287	1.00	11.98	8	O
ATOM	2365	O	HOH	W	5	39.903	40.707	3.072	1.00	4.59	8	O
ATOM	2366	O	HOH	W	6	13.993	28.927	16.050	1.00	8.16	8	O
ATOM	2367	O	HOH	W	7	−2.824	44.331	8.615	1.00	6.77	8	O
ATOM	2368	O	HOH	W	8	46.758	44.137	12.543	1.00	9.80	8	O
ATOM	2369	O	HOH	W	9	22.057	38.363	30.808	1.00	10.53	8	O
ATOM	2370	O	HOH	W	10	41.588	30.809	8.960	1.00	14.97	8	O
ATOM	2371	O	HOH	W	11	32.061	36.737	−0.438	1.00	13.10	8	O
ATOM	2372	O	HOH	W	12	25.621	43.699	12.042	1.00	12.21	8	O
ATOM	2373	O	HOH	W	13	41.643	43.045	19.819	1.00	12.14	8	O
ATOM	2374	O	HOH	W	14	18.598	35.090	17.431	1.00	7.05	8	O
ATOM	2375	O	HOH	W	15	35.642	46.870	0.589	1.00	14.25	8	O
ATOM	2376	O	HOH	W	16	−2.309	45.120	15.349	1.00	5.19	8	O
ATOM	2377	O	HOH	W	17	21.148	34.153	17.144	1.00	9.28	8	O
ATOM	2378	O	HOH	W	18	10.042	49.433	21.052	1.00	16.66	8	O
ATOM	2379	O	HOH	W	19	24.907	43.442	9.509	1.00	8.06	8	O
ATOM	2380	O	HOH	W	20	40.340	29.254	22.526	1.00	15.14	8	O
ATOM	2381	O	HOH	W	21	24.110	53.078	16.016	1.00	13.14	8	O
ATOM	2382	O	HOH	W	22	30.704	31.905	3.919	1.00	15.56	8	O
ATOM	2383	O	HOH	W	23	16.095	40.414	25.005	1.00	19.01	8	O
ATOM	2384	O	HOH	W	24	−4.341	51.429	0.089	1.00	10.32	8	O
ATOM	2385	O	HOH	W	25	34.577	38.997	0.926	1.00	10.61	8	O
ATOM	2386	O	HOH	W	26	31.432	48.786	11.676	1.00	11.01	8	O
ATOM	2387	O	HOH	W	27	32.097	37.715	29.475	1.00	10.30	8	O
ATOM	2388	O	HOH	W	28	−2.898	39.485	16.073	1.00	12.22	8	O
ATOM	2389	O	HOH	W	29	22.459	34.856	30.472	1.00	17.04	8	O
ATOM	2390	O	HOH	W	30	−10.084	35.455	15.693	1.00	11.27	8	O
ATOM	2391	O	HOH	W	31	44.404	44.372	13.687	1.00	7.67	8	O
ATOM	2392	O	HOH	W	32	30.987	42.125	27.230	1.00	18.75	8	O
ATOM	2393	O	HOH	W	33	24.805	29.509	24.797	1.00	10.67	8	O
ATOM	2394	O	HOH	W	34	13.345	25.150	11.364	1.00	12.88	8	O
ATOM	2395	O	HOH	W	35	44.404	42.640	6.498	1.00	6.66	8	O
ATOM	2396	O	HOH	W	36	13.422	56.153	−1.749	1.00	15.97	8	O
ATOM	2397	O	HOH	W	37	19.476	35.360	30.724	1.00	11.73	8	O
ATOM	2398	O	HOH	W	38	9.109	42.563	1.635	1.00	6.86	8	O
ATOM	2399	O	HOH	W	39	40.432	23.485	5.437	1.00	12.80	8	O
ATOM	2400	O	HOH	W	40	42.096	30.240	11.776	1.00	14.42	8	O
ATOM	2401	O	HOH	W	41	42.873	37.972	25.858	1.00	11.47	8	O
ATOM	2402	O	HOH	W	42	9.770	32.553	31.637	1.00	15.13	8	O
ATOM	2403	O	HOH	W	43	−6.902	49.549	6.190	1.00	9.47	8	O
ATOM	2404	O	HOH	W	44	28.555	30.858	2.221	1.00	13.41	8	O
ATOM	2405	O	HOH	W	45	−1.387	38.899	22.433	1.00	11.37	8	O
ATOM	2406	O	HOH	W	46	37.404	40.600	2.609	1.00	14.02	8	O
ATOM	2407	O	HOH	W	47	22.531	31.795	29.779	1.00	17.69	8	O
ATOM	2408	O	HOH	W	48	23.048	38.797	14.218	1.00	14.69	8	O
ATOM	2409	O	HOH	W	49	17.943	35.402	10.729	1.00	20.01	8	O
ATOM	2410	O	HOH	W	50	5.174	54.657	−2.822	1.00	17.90	8	O
ATOM	2411	O	HOH	W	51	13.246	20.750	19.283	1.00	29.29	8	O
ATOM	2412	O	HOH	W	52	48.032	37.211	11.489	1.00	16.87	8	O
ATOM	2413	O	HOH	W	53	30.209	20.178	20.611	1.00	18.81	8	O
ATOM	2414	O	HOH	W	54	23.513	22.824	21.491	1.00	20.26	8	O
ATOM	2415	O	HOH	W	55	21.561	29.530	25.223	1.00	20.52	8	O
ATOM	2416	O	HOH	W	56	42.111	36.443	28.208	1.00	19.47	8	O
ATOM	2417	O	HOH	W	57	40.876	29.661	15.978	1.00	16.06	8	O
ATOM	2418	O	HOH	W	58	16.494	34.453	13.028	1.00	25.55	8	O
ATOM	2419	O	HOH	W	59	−0.857	46.408	17.858	1.00	16.37	8	O
ATOM	2420	O	HOH	W	60	32.821	25.971	0.795	1.00	16.71	8	O
ATOM	2421	O	HOH	W	61	45.627	45.117	6.519	1.00	18.94	8	O
ATOM	2422	O	HOH	W	62	21.976	40.997	13.661	1.00	17.37	8	O
ATOM	2423	O	HOH	W	63	15.836	30.099	15.388	1.00	15.61	8	O
ATOM	2424	O	HOH	W	64	30.469	26.207	24.253	1.00	22.51	8	O
ATOM	2425	O	HOH	W	65	16.718	46.859	20.929	1.00	14.88	8	O
ATOM	2426	O	HOH	W	66	10.425	43.686	25.115	1.00	19.64	8	O
ATOM	2427	O	HOH	W	67	21.112	30.369	11.432	1.00	24.23	8	O
ATOM	2428	O	HOH	W	68	17.191	27.886	14.604	1.00	16.40	8	O
ATOM	2429	O	HOH	W	69	−1.313	55.974	8.469	1.00	20.48	8	O
ATOM	2430	O	HOH	W	70	−5.616	49.292	2.546	1.00	14.23	8	O
ATOM	2431	O	HOH	W	71	18.410	59.447	0.811	1.00	16.23	8	O
ATOM	2432	O	HOH	W	72	4.679	43.284	24.130	1.00	26.97	8	O
ATOM	2433	O	HOH	W	73	28.210	48.003	7.105	1.00	25.13	8	O
ATOM	2434	O	HOH	W	74	24.472	50.097	17.032	1.00	18.43	8	O
ATOM	2435	O	HOH	W	75	44.769	47.165	4.712	1.00	20.42	8	O
ATOM	2436	O	HOH	W	76	20.456	33.034	10.801	1.00	21.21	8	O
ATOM	2437	O	HOH	W	77	27.096	24.676	0.583	1.00	16.78	8	O
ATOM	2438	O	HOH	W	78	45.463	43.772	2.754	1.00	19.58	8	O
ATOM	2439	O	HOH	W	79	36.902	42.152	24.314	1.00	19.89	8	O
ATOM	2440	O	HOH	W	80	25.028	31.904	31.035	1.00	25.70	8	O
ATOM	2441	O	HOH	W	81	19.951	31.779	31.151	1.00	20.25	8	O
ATOM	2442	O	HOH	W	82	2.821	56.599	5.110	1.00	24.51	8	O
ATOM	2443	O	HOH	W	83	0.240	38.318	26.532	1.00	20.61	8	O
ATOM	2444	O	HOH	W	84	−5.501	28.962	8.643	1.00	25.67	8	O
ATOM	2445	O	HOH	W	85	15.080	16.024	18.827	1.00	23.79	8	O
ATOM	2446	O	HOH	W	86	17.453	52.249	2.615	1.00	24.26	8	O
ATOM	2447	O	HOH	W	87	10.408	41.106	29.551	1.00	25.17	8	O
ATOM	2448	O	HOH	W	88	−1.008	36.087	24.249	1.00	22.03	8	O
ATOM	2449	O	HOH	W	89	28.715	28.420	1.496	1.00	33.15	8	O
ATOM	2450	O	HOH	W	90	26.479	48.310	17.176	1.00	14.80	8	O
ATOM	2451	O	HOH	W	91	4.544	21.028	22.060	1.00	23.39	8	O
ATOM	2452	O	HOH	W	92	7.062	20.090	15.336	1.00	17.95	8	O
ATOM	2453	O	HOH	W	93	−8.087	52.015	8.198	1.00	13.31	8	O
ATOM	2454	O	HOH	W	94	13.718	42.096	26.908	1.00	15.23	8	O
ATOM	2455	O	HOH	W	95	−5.925	31.260	22.875	1.00	18.50	8	O
ATOM	2456	O	HOH	W	96	2.262	47.977	19.728	1.00	22.03	8	O
ATOM	2457	O	HOH	W	97	39.222	48.045	1.791	1.00	23.00	8	O
ATOM	2458	O	HOH	W	98	13.202	60.207	12.694	1.00	18.82	8	O
ATOM	2459	O	HOH	W	99	35.592	47.975	18.124	1.00	21.60	8	O
ATOM	2460	O	HOH	W	100	32.405	49.718	9.091	1.00	23.23	8	O
ATOM	2461	O	HOH	W	101	32.530	40.013	27.354	1.00	26.88	8	O
ATOM	2462	O	HOH	W	102	15.214	19.032	19.403	1.00	31.35	8	O
ATOM	2463	O	HOH	W	103	29.693	49.421	9.197	1.00	18.95	8	O
ATOM	2464	O	HOH	W	104	34.770	34.970	27.712	1.00	36.84	8	O
ATOM	2465	O	HOH	W	105	13.525	57.916	19.061	1.00	24.00	8	O
ATOM	2466	O	HOH	W	106	22.201	34.397	12.453	1.00	27.96	8	O
ATOM	2467	O	HOH	W	107	35.580	49.792	6.450	1.00	17.81	8	O
ATOM	2468	O	HOH	W	108	28.722	38.669	0.882	1.00	28.33	8	O
ATOM	2469	O	HOH	W	109	−1.552	26.414	23.825	1.00	25.54	8	O
ATOM	2470	O	HOH	W	110	6.586	43.932	26.846	1.00	30.40	8	O
ATOM	2471	O	HOH	W	111	26.222	21.733	1.726	1.00	27.89	8	O
ATOM	2472	O	HOH	W	112	38.816	11.853	6.953	1.00	31.38	8	O
ATOM	2473	O	HOH	W	113	40.804	10.936	−0.338	1.00	43.84	8	O
ATOM	2474	O	HOH	W	114	14.465	23.160	5.012	1.00	35.94	8	O
ATOM	2475	O	HOH	W	115	29.274	51.396	12.634	1.00	31.23	8	O
ATOM	2476	O	HOH	W	116	36.111	26.053	21.704	1.00	27.88	8	O
ATOM	2477	O	HOH	W	117	48.720	40.919	8.861	1.00	27.14	8	O
ATOM	2478	O	HOH	W	118	16.857	35.240	8.265	1.00	29.17	8	O
ATOM	2479	O	HOH	W	119	40.272	15.140	−2.430	1.00	28.86	8	O
ATOM	2480	O	HOH	W	120	8.464	39.395	3.469	1.00	26.29	8	O
ATOM	2481	O	HOH	W	121	24.991	50.953	19.868	1.00	38.39	8	O
ATOM	2482	O	HOH	W	122	32.494	43.852	25.475	1.00	20.94	8	O
ATOM	2483	O	HOH	W	123	42.907	20.569	5.948	1.00	20.98	8	O
ATOM	2484	O	HOH	W	124	11.409	60.427	−4.212	1.00	22.37	8	O
ATOM	2485	O	HOH	W	125	41.932	17.910	−0.484	1.00	24.91	8	O
ATOM	2486	O	HOH	W	126	−6.114	27.302	10.662	1.00	25.66	8	O
ATOM	2487	O	HOH	W	127	26.137	21.371	21.978	1.00	29.82	8	O
ATOM	2488	O	HOH	W	128	8.216	61.214	10.723	1.00	30.53	8	O
ATOM	2489	O	HOH	W	129	26.118	11.522	20.391	1.00	26.63	8	O
ATOM	2490	O	HOH	W	130	38.986	15.328	−4.568	1.00	35.28	8	O
ATOM	2491	O	HOH	W	131	32.545	51.686	12.997	1.00	34.45	8	O
ATOM	2492	O	HOH	W	132	10.691	28.090	29.628	1.00	23.73	8	O
ATOM	2493	O	HOH	W	133	42.534	51.095	7.222	1.00	27.35	8	O
ATOM	2494	O	HOH	W	134	24.319	44.661	27.426	1.00	29.68	8	O
ATOM	2495	O	HOH	W	135	27.184	27.908	26.119	1.00	29.01	8	O
ATOM	2496	O	HOH	W	136	12.482	23.286	9.718	1.00	25.90	8	O
ATOM	2497	O	HOH	W	137	13.725	58.650	6.382	1.00	30.09	8	O
ATOM	2498	O	HOH	W	138	16.824	30.085	33.861	1.00	29.63	8	O
ATOM	2499	O	HOH	W	139	25.538	40.408	32.871	1.00	25.50	8	O
ATOM	2500	O	HOH	W	140	−4.601	42.598	6.460	1.00	28.50	8	O
ATOM	2501	O	HOH	W	141	−4.314	55.800	1.473	1.00	23.98	8	O
ATOM	2502	O	HOH	W	142	4.180	40.729	2.968	1.00	38.79	8	O
ATOM	2503	O	HOH	W	143	2.880	34.275	3.975	1.00	35.32	8	O
ATOM	2504	O	HOH	W	144	22.685	41.116	9.871	1.00	37.58	8	O
ATOM	2505	O	HOH	W	145	5.911	42.222	1.293	1.00	38.18	8	O
ATOM	2506	O	HOH	W	146	−0.037	32.781	6.946	1.00	36.95	8	O
ATOM	2507	O	HOH	W	147	9.637	20.349	10.139	1.00	25.04	8	O
ATOM	2508	O	HOH	W	148	28.382	43.815	3.179	1.00	43.71	8	O
ATOM	2509	O	HOH	W	149	22.090	59.094	6.799	1.00	36.67	8	O
ATOM	2510	O	HOH	W	150	10.612	40.037	0.986	1.00	30.45	8	O
ATOM	2511	O	HOH	W	151	33.822	49.094	4.672	1.00	31.89	8	O
ATOM	2512	O	HOH	W	152	10.343	15.118	17.380	1.00	41.68	8	O
ATOM	2513	O	HOH	W	153	17.037	38.046	31.684	1.00	36.09	8	O
ATOM	2514	O	HOH	W	154	−4.211	57.650	5.730	1.00	37.59	8	O
ATOM	2515	O	HOH	W	155	10.360	30.679	5.056	1.00	35.82	8	O
ATOM	2516	O	HOH	W	156	9.319	30.377	30.150	1.00	45.13	8	O
ATOM	2517	O	HOH	W	157	32.537	46.738	25.670	1.00	42.21	8	O
ATOM	2518	O	HOH	W	158	−7.040	33.392	21.564	1.00	29.97	8	O
ATOM	2519	O	HOH	W	159	25.487	57.687	13.423	1.00	56.41	8	O
ATOM	2520	O	HOH	W	160	22.390	27.493	27.703	1.00	51.26	8	O
ATOM	2521	O	HOH	W	161	−1.944	32.594	29.002	1.00	35.60	8	O
ATOM	2522	O	HOH	W	162	19.494	57.986	15.703	1.00	27.66	8	O
ATOM	2523	O	HOH	W	163	4.218	34.783	−0.031	1.00	37.95	8	O
ATOM	2524	O	HOH	W	164	10.878	61.676	2.439	1.00	40.13	8	O
ATOM	2525	O	HOH	W	165	32.378	32.684	29.566	1.00	39.10	8	O
ATOM	2526	O	HOH	W	166	40.742	27.829	18.701	1.00	32.58	8	O
ATOM	2527	O	HOH	W	167	15.407	53.314	22.674	1.00	35.33	8	O
ATOM	2528	O	HOH	W	168	24.525	50.894	4.209	1.00	30.85	8	O
ATOM	2529	O	HOH	W	169	24.227	47.558	13.850	1.00	13.12	8	O
ATOM	2530	O	HOH	W	170	19.469	40.382	25.052	1.00	14.83	8	O
ATOM	2531	O	HOH	W	171	25.449	45.435	13.288	1.00	34.42	8	O
ATOM	2532	O	HOH	W	172	36.869	45.896	18.115	1.00	21.20	8	O
ATOM	2533	O	HOH	W	173	12.012	28.477	9.138	1.00	29.45	8	O
ATOM	2534	O	HOH	W	174	16.359	41.479	3.585	1.00	38.60	8	O
ATOM	2535	O	HOH	W	175	34.326	31.763	−2.161	1.00	2.02	8	O
ATOM	2536	O	HOH	W	176	17.655	52.366	−0.174	1.00	22.73	8	O
ATOM	2537	O	HOH	W	177	14.404	48.517	21.739	1.00	25.45	8	O
ATOM	2538	O	HOH	W	178	43.749	32.200	8.020	1.00	29.02	8	O
ATOM	2539	O	HOH	W	179	15.592	26.829	16.174	1.00	48.16	8	O
ATOM	2540	O	HOH	W	180	10.525	56.368	−4.081	1.00	30.23	8	O
ATOM	2541	O	HOH	W	181	8.713	25.942	28.348	1.00	25.77	8	O
ATOM	2542	O	HOH	W	182	29.737	7.237	11.850	1.00	33.68	8	O
ATOM	2543	O	HOH	W	183	21.164	33.439	7.966	1.00	38.28	8	O
ATOM	2544	O	HOH	W	184	24.119	46.149	24.377	1.00	37.23	8	O
ATOM	2545	O	HOH	W	185	21.753	56.692	10.121	1.00	33.11	8	O
ATOM	2546	O	HOH	W	186	17.585	38.448	12.402	1.00	39.35	8	O
ATOM	2547	O	HOH	W	187	−2.754	38.361	11.916	1.00	44.68	8	O
ATOM	2548	O	HOH	W	188	16.639	27.328	18.235	1.00	24.46	8	O
ATOM	2549	O	HOH	W	189	14.615	34.256	8.534	1.00	41.84	8	O
ATOM	2550	O	HOH	W	190	14.514	43.801	25.157	1.00	33.67	8	O
ATOM	2551	O	HOH	W	191	26.469	30.002	3.866	1.00	53.62	8	O
ATOM	2552	O	HOH	W	192	3.416	28.107	4.131	1.00	47.37	8	O
ATOM	2553	O	HOH	W	193	15.414	27.531	11.247	1.00	40.29	8	O
ATOM	2554	O	HOH	W	194	24.628	58.221	6.032	1.00	37.02	8	O
ATOM	2555	O	HOH	W	195	−1.971	51.690	17.147	1.00	35.28	8	O
ATOM	2556	O	HOH	W	196	16.659	23.680	26.303	1.00	37.61	8	O
END

[Advantages]

By using the present invention, it becomes possible to identify accurately and efficiently FFRPs regulating metabolism, growth, and infectivity of bacteria. Targeting the identified FFRPs, antimicrobial agents can be searched by using a known ligand screening method, or by a virtual screening method using 3D structure information.

Sequence Listing

• <110> National Institute of Advanced Industrial Science and Technology(AIST)
• <120> Method of Screening for Antimicrobial Agents
• <130> 334-03166
• <140>
• <141>
• <160> 33
• <170> PatentIn Ver. 2.1
• <210> 1
• <211> 157
• <212> PRT
• <213> Pseudomonas aeruginosa
• <220>
• <223> Inventor: Suzuki, Masashi; Koike, Hideaki

FIG. 1 shows correlation between amino acid sequences of different FFRPs (i.e., a multiple alignment) coded in the genomes of various bacteria. Hydrophobic phase inside α-helices are marked with asterisks (*), with types of residues, isoleucine, valine, leucine, and methionine in these phases highlighted in bold. Outside the α-helices at each position, the type of residues most frequently found is highlighted in bold.

[FIG. 2]

FIG. 2 is a diagram showing phylogenetic relations between FFRPs.

In this diagram, nodes characterized with bootstrap values of 500 or higher are colored in red. Nodes characterized with smaller bootstrap values, 350 or higher but less than 500, are indicated by closed circles colored in black. Four demi-FFRPs are colored in green, and the two subgroups together covering the eight P. aeruginosa FFRPs are colored in red and blue, respectively.

[FIG. 3]

FIG. 3 shows the thirty-two amino acid positions where pharmaceutical agents will bind. In this figure along the line, “(iii) Modeling of leucine binding”, residues producing conflicts (X) or no conflict (O) when leucine is modeled to fit pot1216151 are indicated.

[FIG. 4]

FIG. 4 show a wire model of the crystal structure of an FFRP (pot1216151) derived from an archaeon (Pyrococcus OT3). In this figure, the electron densities of two molecules of an unidentified ligand derived from E. coli are colored in red.

[FIG. 5]

FIG. 5 shows an enlargement of the electron density of the ligand shown in FIG. 4, to which a valine molecule is best fit. In this figure, the valine molecule is represented by a wire model, and the atoms are differentiated: oxygen (red), nitrogen (blue), and carbon (yellow). Hydrogen atoms are omitted.

[FIG. 6]

FIG. 6 shows residues of pot1216151 positioned within 6 Å from the unidentified assembly promotion factor derived from E. coli, and residues of other FFRP molecules occupying the identical positions. Residues found in E. coli Lrp but not found in EcO468065 at the same positions are colored in red, residues found in Ec0468065 but not found in E. coli Lrp at the same positions are colored in blue, and residues found in both at the same positions are colored in green.

[FIG. 7]

FIG. 7 shows positions potentially important for leucine-binding by E. coli Lrp, and the residues of archaeal FFRPs found at the same positions. In this figure, residues found in E. coli Lrp but not found in Ec0468065 at the same positions are colored in red, residues found in Ec0468065 but not found in E. coli Lrp are colored in blue, and residues found in both are colored in green.

[FIG. 8]

FIG. 8 shows a ribbon diagram of the crystal structure of pot1216151 with coloring seven positions important for leucine-binding by E. coli Lrp in blue.

[FIG. 9]

FIG. 9 shows a ribbon diagram of leucine (yellow) binding to pot1216151. FIG. 9 shows a view looked along the arrow shown in FIG. 10: two dimers closest to the arrow and a leucine molecule are shown. In the upper half of this model, positions the same as those colored in blue in FIG. 8 are highlighted in the same color, i.e., in blue. Meanwhile, residues forming the gap between the two dimers are highlighted in green. In the lower half of this model, residues contacting the modeled leucine molecule with no conflict are colored in blue, and three other residues positioned conflicting with the leucine molecule are colored in red.

[FIG. 10]

FIG. 10 is a ribbon diagram of a model of leucine-binding to pot1216151.

[FIG. 11]

FIG. 11 shows residues of pot1216151 positioned close to the leucine molecule modeled to fit the protein, and residues of other FFRP molecules occupying the same positions as those in pot1216151. In this figure, residues found in E. coli Lrp but not found in Ec0468065 at the same positions are colored in red, residues found in Ec0468065 but not found in E. coli Lrp at the same positions are colored in blue, and residues found in both at the same positions are colored in green.

[FIG. 12]

FIG. 12 shows residues of pot1216151 whose side chains are facing the gaps formed between the dimers, and residues of other FFRPs occupying the same positions. In this figure, residues found in E. coli Lrp but not found in Ec0468065 at the same positions are colored in red, residues found in Ec0468065 but not found in E. coli Lrp at the same positions are colored in blue, and residues found in both at the same positions are colored in green.

[FIG. 13]

FIG. 13 shows a partial rearrangement of the thirty-two positions shown in FIG. 3.

[FIG. 14]

FIG. 14 shows positions of FFRPs identified as important for DNA recognition. In this figure, residues found in E. coli Lrp but not found in Ec0468065 at the same positions are colored in red, residues found in Ec0468065 but not found in E. coli Lrp at the same positions are colored in blue, and residues found in both at the same positions are colored in green.

[FIG. 15]

FIG. 15 shows a ribbon diagram of the 3D structure of a dimer of the FFRP (pot1216151) in two views.

[FIG. 16]

FIG. 16 shows profiles of gel filtration of the FFRP pot1216151 purified using different methods: mild (black, purification 1) and rigorous (red, purification 2).

[FIG. 17]

FIG. 17 shows profiles of gel filtration of the FFRP pot1216151. In this diagram, profiles shown are those obtained in the absence (black) or presence of chemical compounds: amino acids (a, b) and other metabolic intermediates (c), malic acid (red), 2-oxoglutaric acid (green), and oxaloacetic acid (blue).

Claims

1. A method of identifying a target protein for its use in screening for an antimicrobial agent, which comprises the steps of: 1) from the amino acid sequences of all open reading frames identified using the genomic sequence of a target bacterium, selecting amino acid sequences having homologies of 20% or higher to one of feast/famine regulatory proteins (FFRPs) having amino acid sequences set forth in SEQ ID NOS. 9 to 31; and 2) from the amino acid sequences selected in step 1), excluding any amino acid sequence that does not match with a multiple alignment by forming the same secondary structural elements, the multiple alignment being shown in FIG. 1; and 3) identifying a protein, which has an amino acid sequence obtained through steps 1) and 2), as the target protein for its use in the screening for the antimicrobial agent.

2. The method according to claim 1, further comprising the step of excluding any amino acid sequence phylogenetically related with one of E. coli FFRPs having amino acid sequences set forth in SEQ ID NOS. 9 to 11, by a bootstrap value of 900/1,000 or higher.

3. The method according to claim 1 or 2, wherein, in step 1), from the amino acid sequences of all open reading frames identified using the genomic sequence of the target bacterium, amino acid sequences having FASTA Z scores of 180 or higher to one of FFRPs having amino acid sequences set forth in SEQ ID NOS. 9 to 31 are selected.

4. The method according to any one of claims 1 to 3, wherein, in step 2), any amino acid sequence that is unlikely to form α helices in five regions 34 to 43, 59 to 66, 70 to 82, 126 to 135, and 170 to 180 or β strands in five regions 90 to 96, 109 to 117, 142 to 148, 154 to 160, and 193 to 205 is excluded from the amino acid sequences selected by step 1), wherein these positions are identified using the numbering scheme shown in the multiple alignment in FIG. 1.

5. A method of screening for an antimicrobial agent, which comprises the step of selecting a chemical compound as a candidate of the agent, wherein the chemical compound is able to bind specifically to a protein identified by the method according to any one of claims 1 to 4 or to its assembly, thereby altering the three-dimensional structure or the assembly form of the protein.

6. A method of screening for an antimicrobial agent acting against Pseudomonas aeruginosa, which comprises the step of selecting a chemical compound as a candidate of the antimicrobial agent, wherein said chemical compound is able to bind specifically to a target protein or its assembly, thereby altering the three-dimensional structure or the assembly form of the protein, wherein the target protein is either i) a protein having an amino acid sequence set forth in one of SEQ ID NOS. 1 to 8; or ii) a protein which is derived from Pseudomonas aeruginosa, which is related to an amino acid sequence set forth in one of SEQ ID NOS. 1 to 8 by deletion, substitution, or insertion of up to several amino acid residues, and which is able to act as an FFRP.

7. A method of screening for an antimicrobial agent acting against Pseudomonas aeruginosa, which comprises the step of selecting a chemical compound as a candidate of the antimicrobial agent, said chemical compound being able to bind specifically to a target protein having an amino acid sequence set forth in one of SEQ ID NOS. 1 to 8 or able to bind to its assembly, thereby altering the three-dimensional structure or the assembly form of the target protein.

8. A method of screening for an antimicrobial agent acting against Pseudomonas aeruginosa, which comprises the step of selecting a chemical compound as a candidate of the antimicrobial agent, said chemical compound being able to bind specifically to a target protein having an amino acid sequence set forth in one of SEQ ID NOS. 1 to 7 or its assembly, thereby altering the three-dimensional structure or the assembly form of the target protein.

9. The method according to any one of claims 5 to 8, wherein the chemical compound is selected on the basis of interaction between the chemical compound and at least one of thirty-two amino acid residues in the target protein, said thirty-two amino acid residues being found at positions 113, 116, 119, 120, 126, 144, 145, 147, 148, 149, 150, 152, 153, 154, 155, 166, 169, 173, 176, 177, 181, 183, 185, 193, 195, 196, 197, 198, 199, 200, 201, and 202, respectively, wherein these positions are identified using the numbering scheme shown in the multiple alignment in FIG. 1.

10. The method according to any one of claims 5 to 8, wherein the chemical compound is selected on the basis of interaction between the chemical compound and at least one of eighteen amino acid residues in the target protein, said eighteen amino acid residues being found at positions 113, 126, 147, 148, 149, 150, 152, 153, 154, 155, 176, 177, 181, 196, 197, 198, 199, and 202, respectively, wherein these positions are identified using the numbering scheme shown in the multiple alignment in FIG. 1.

11. The method according to any one of claims 5 to 8, wherein the chemical compound is selected on the basis of interaction between the chemical compound and at least one of seven amino acid residues in the target protein, said seven amino acid residues being found at positions 147, 154, 169, 181, 199, 200, and 201, respectively, wherein these positions are identified using the numbering scheme shown in the multiple alignment in FIG. 1.

12. The method according to any one of claims 5 to 8, wherein the chemical compound is selected on the basis of interaction between the chemical compound and at least one of seven amino acid residues in the target protein, said seven amino acid residues being found at positions 147, 149, 154, 169, 173, 200, and 202, respectively, wherein these positions are identified using the numbering scheme shown in the multiple alignment in FIG. 1.

13. The method according to any one of claims 5 to 8, wherein the chemical compound is selected on the basis of interaction between the chemical compound and at least one of twenty-eight amino acid residues in the target protein, said twenty-eight amino acid residues being found at positions 116, 119, 120, 126, 144, 145, 147, 148, 149, 150, 152, 153, 154, 166, 169, 173, 177, 181, 183, 185, 193, 195, 196, 197, 198, 199, 200, and 201, respectively, wherein these positions are identified using the numbering scheme shown in the multiple alignment in FIG. 1.