Carcinoembryonic antigen cell adhesion molecule 1 (CEACAM1) structure and uses thereof in drug identification and screening

BACKGROUND OF THE INVENTION

[0003] This present CEACAM1 is a member of the carcinoembryonic antigen (CEA) family. Isoforms of murine CEACAM1 serve as receptors for mouse hepatitis virus (MHV), a murine coronavirus.

[0004] Carcinoembryonic antigen (CEA; CD66e) was initially discovered as a tumor antigen (Gold and Freedman, 1965). A large group of related glycoproteins is now called the CEA family within the Ig superfamily (IgSF). These anchored or secreted glycoproteins are expressed by epithelial cells, leukocytes, endothelial cells and placenta (Hammarstrom, 1999). In humans, the CEA family contains 29 genes or pseudogenes. The revised nomenclature of this family of glycoproteins was recently summarized (Beauchemin et al., 1999). The CEA family consists of the CEACAM (CEA-related cell adhesion molecule) and PSG (pregnancy-specific glycoprotein) subfamilies whose proteins share many common structural features (Hammarstrom, 1999).

[0005] CEACAM1 (CD66a) is the most highly conserved member of the CEA family. Most species have only one CEACAM1 gene, but mice have two closely related genes called CEACAM1 and CEACAM2 (Beauchemin et al., 1999, Nedellec et al. 1994). CEACAM1 has many important biological functions. It is a potent vascular endothelial growth factor (Ergun et al., 2000) and a growth inhibitor in tumor cells (Izzi et al., 1999); plays a key role in differentiation of mammary glands (Huang et al., 1999); is an early marker of T cell activation; and modulates the functions of T lymphocytes (Morales et al., 1999; Nakajima et al., 2002). Human CEACAM 1 is one of several human CEACAM proteins that serve as receptors for virulent strains of Neisseria gonorrhoeae, Neisseria meningitidis, and Hemophilus influenzae (Bos et al., 1999; Virji et al., 2000; Virji et al., 1999).

[0006] In mice four isoforms of CEACAM1 generated by alternative mRNA splicing have either 2 [D1,D4] or 4 [D1-D4] Ig-like domains on cell surface, a transmembrane segment and either short or a long cytoplasmic tail (Beauchemin et al., 1999). The long tail contains a modified ITIM (immunoreceptor tyrosine based inhibition motif)-like motif. Tyrosine phosphorylation of this motif is associated with signaling (Huber et al., 1999), but the natural ligands for the ecto-domain and the modulation of gene expression by CEACAM1 signaling are not well understood.

[0007] All four isoforms of murine CEACAM1a as well as murine CEACAM2 can serve as receptors for mouse hepatitis virus (MHV) strain A59 (MHV-A59) when the recombinant murine proteins are expressed at high levels in a hamster cell line (BHK) (Dveksler et al., 1993a; Dveksler et al., 1991; Nedellec et al., 1994). MHVs are large, enveloped, positive-stranded RNA viruses in the Coronaviridae family in the order Nidovirales. Various MHV strains cause diarrhea, hepatitis, respiratory, neurological and immunological disorders in mice. Infection is initiated by binding of the 180 kDa spike glycoprotein (S) on the viral envelope to a CEACAM glycoprotein on a murine cell membrane. Most inbred mouse strains are highly susceptible to MHV infection, but SJL/J mice are highly resistant. Susceptible strains are homozygous for the CEACAM1a allele that encodes the principal MHV receptor, while SJL/J mice are homozygous for the CEACAM1b allele. CEACAM1b proteins have weaker MHV binding and receptor activities than CEACAM1a proteins (Ohtsuka et al., 1996; Rao et al., 1997; Wessner et al., 1998).

[0008] What is known about the family of CEACAM1a proteins is that MHV strains utilize the murine CEACAM1a proteins as receptors (Compton, S. R. (1994); Dveksler (1991), Dveksler et al. (1993)). The spike (S) glycoprotein of MHV attaches to the N domain (D1) of CEACAM1a (Dveksler, et al., 1993, Williams, et al.,(1998). Mutational analysis showed that the virus MHV, binds to the C-C′ loop of domain 1 of the CEACAM1a protein (Rao, et al. (1997), Wessner, et al. (1998)). However, extensive N-linked glycosylation has precluded crystallization of any CEA proteins for structural analysis. A need continues to exist in the art defining the basic structure of this important family of proteins, as to do so would permit the development of a broad spectrum of therapeutic agents for viral, bacterial, immunological and carcinogenic pathologies.

SUMMARY OF THE INVENTION

[0009] The present invention, in a general and overall sense, relates to the identification of a uniquely crystalline structure of a biologically important molecule that to this time had been precluded by the extensive glycosylation inherent in the native CEA antigen. The structure of the biologically active CC′ loop of the N-terminal domain (domain 1) could not have been predicted based on a comparison of its linear amino acid sequence with that of any other known structure of any other protein in the database. The identification of this structure may be used in the selection and screening of agents for use in treatment of viral, bacterial, immunological diseases, malignancies and abnormal blood vessel growth. The crystal structure of soluble murine sCEACAM1a[1,4], is composed of two Ig-like domains. This protein has virus neutralizing activity. Its N-terminal domain has a uniquely folded CC′ loop that encompasses key virus-binding residues, these are KGNTTAIDKE (SEQ ID NO: 3). This is the first atomic structure of any member of the CEA family, and provides a prototypic architecture for functional identification of all other CEA family members. The structural basis of virus receptor activities of murine CEACAM1 proteins, binding of Neisseria to human CEACAM1, and other homophilic and heterophilic interactions of CEA family members is disclosed in the present invention. This structural information is also presented as embodiments of the invention that provides a method for screening molecules potentially useful as therapeutic agents in treating pathology where receptor interactions of this nature is important in the disease state.

[0010] In some embodiments, the invention provides a crystal structure of a soluble ecto-domain of an isoform of murine CEACAM1a that compress domains 1 and 4, (designated msCEACAM1a[1,4] hereafter) and has MHV neutralizing activity. The relationship of the structure of the msCEACAM1a[1,4] glycoprotein to its MHV binding and neutralizing activities is examined and described here. Based on the structure of msCEACAM1a[1,4], the invention in yet another aspect provides a model of human CEA family members. The models of two N-terminal domains of human CEACAM1, CEA and CEACAM6 provide particular embodiments of the invention. Based on the models of CEA and CEACAM6, a strategy of antibody development as well as other types of molecules capable of binding or inhibiting binding to the antigen is presented. The biological use of these structures in a pharmaceutical is disclosed.

[0011] The following terms, if appearing herein, shall have the definitions set out below.

[0012] The term “fragment”, as applied herein to a peptide, refers to at least 7 contiguous amino acids, preferably about 14 to 16, 20, 25, 30 or 36 contiguous amino acids, or up to more than 40 or 203 to 250 to 1500 contiguous amino acids in length. Such peptides can be produced by well-known methods to those skilled in the art, such as, for example, by proteolytic cleavage, genetic engineering or chemical synthesis.

[0013] The term “domain” refers to a compact, independently folded tertiary structural unit, usually consisting of 50-200 amino acid residues within a protein. A protein can have more than one domains to perform its function.

[0014] Unless defined otherwise, the scientific and technological terms and nomenclature used herein have the same meaning as commonly understood by a person of ordinary skill to which the invention pertains. Generally, the procedures for cell cultures, infection, molecular biology methods and the like are common methods used in the art. Such standard techniques can be found in reference manuals such as for example J. Sambrook, D. W. Russell, Third Edition. (2001, Molecular Cloning—A Laboratory Manual, Cold Spring Harbor Laboratories), and Ausubel et al. (1994. Current protocols in Molecular Biology, Wiley, New York).

[0015] As used herein, “nucleic acid molecule”, refers to a polymer of nucleotides. Non-limiting examples thereof include DNA (e.g. genomic DNA, cDNA), RNA molecules (e.g. mRNA) and chimeras thereof. The nucleic acid molecule can be obtained by cloning techniques or synthesized. DNA can be double-stranded or single-stranded (coding strand or non-coding strand [antisense]). RNA can be single-stranded or double-stranded, or partially double stranded.

[0016] The term “DNA segment” is used herein to refer to a DNA molecule comprising a linear stretch or sequence of nucleotides. This sequence when read in accordance with the genetic code, can encode a linear stretch or sequence of amino acids which can be referred to as a polypeptide, protein, protein fragment and the like.

[0017] As used herein, “oligonucleotides” or “oligos” define a molecule having two or more nucleotides (ribo or deoxyribonucleotides). The size of the oligo will be dictated by the particular situation and ultimately by the particular use thereof and adapted accordingly by the person of ordinary skill. An oligonucleotide can be synthetised chemically or derived by cloning according to well known methods.

[0018] The nucleic acid (e.g. DNA or RNA) for practicing the present inventions may be obtained according to well known methods.

[0019] The term “DNA” molecule or sequence refers to a molecule generally comprised of the deoxyribonucleotides adenine (A), guanine (G), thymine (T), and/or cytosine (C), which in a double-stranded form, can comprise or include a “regulatory element”, as the term is defined herein. “DNA” can be found in linear DNA molecules or fragments, viruses, plasmids, vectors, chromosomes or synthetically derived DNA. As used herein, particular double-stranded DNA sequences may be described according to the normal convention of giving only the sequence in the 5′ to 3′ direction. The same applies to single stranded DNA sequences. As well known in the art, DNA can also be found as circular molecules.

[0020] “Nucleic acid hybridization” refers generally to the hybridization of two single stranded nucleic acid molecules having complementary base sequences, which under appropriate conditions will form a thermodynamically favored double-stranded structure. Examples of hybridization conditions can be found in the two laboratory manuals referred above (Sambrook and Russell, (2001), and Ausubel et al. (2001) and are well known in the art. In the case of a hybridization to a nitrocellulose filter, as for example in the well known Southern blotting procedure, a nitrocellulose filter can be incubated overnight at 65° C. with a labelled probe in a solution containing 50% formamide, high salt (5×SSC or 5 x SSPE), 5× Denhardt's solution, 1% SDS, and 100 μg/ml denatured carrrier DNA (e.g. salmon sperm DNA). The non-specifically binding probe can then be washed off the filter by several washes in 0.2×SSC/0.1% SDS at a temperature which is selected in view of the desired stringency: room temperature (low stringency), 42° C. (moderate stringency) or 65° C. (high stringency). The selected temperature is based on the melting temperature (Tm) of the DNA hybrid. Of course, RNA-DNA hybrids can also be formed and detected. In such cases, the conditions of hybridization and washing can be adapted according to well known methods by the person of ordinary skill. Stringent conditions will be preferably used (Sambrook and Russell, (2001)).

[0021] Probes of the invention can be utilized with naturally occurring sugar-phosphate backbones as well as modified backbones including phosphorothioates, dithionates, alkyl phosphonates and nucleotides and the like. Modified sugar-phosphate backbones are generally taught by Miller, (1998) and Moran (1997). Probes of the invention can be constructed of either ribonucleic acid (RNA) or deoxyribonucleic acid (DNA).

[0022] The types of detection methods in which probes can be used include Southern blots (DNA detection), dot or slot blots (DNA, RNA), and Northern blots (RNA detection). Although less preferred, labelled proteins could also be used to detect a particular nucleic acid sequence to which it binds. Other detection methods include kits containing probes on a dipstick setup and the like.

[0023] Probes can be labelled according to numerous well known methods (Sambrook and Russell (2001)). Non-limiting examples of labels include 3H, 14C, 32P, and 35S. Non-limiting examples of detectable markers include ligands, fluorophores, chemiluminescent agents, enzymes, and antibodies. Other detectable markers for use with probes, which can enable an increase in sensitivity of the method of the invention, include biotin and radionucleotides. It will become evident to the person of ordinary skill that the choice of a particular label dictates the manner in which it is bound to the probe.

[0024] As commonly known, radioactive nucleotides can be incorporated into probes of the invention by several methods. Non-limiting examples thereof include kinasing the 5′ ends of the probes using gamma 32P ATP and polynucleotide kinase, using the Klenow fragement of Pol 1 of E. coli in the presence of radioactive dNTP (e.g. uniformly labelled DNA probe using random oligonucleotide primers in low-melt gels), using the SP6/T7 system to transcribe a DNA segment in the presence of one or more radioactive NTP, and the like.

[0025] As used herein, a “primer” defines an oligonucleotide which is capable of annealing to a target sequence, thereby creating a double stranded region which can serve as an initiation point for DNA synthesis under suitable conditions. In a particularly preferred embodiment, the primer is a single stranded DNA molecule.

[0026] Amplification of a selected, or target, nucleic acid sequence may be carried out by a number of suitable methods. Numerous amplification techniques have been described and can be readily adapted to suit particular needs of a person of ordinary skill. Non-limiting examples of amplification techniques include polymerase chain reaction (PCR), ligase chain reaction (LCR), strand displacement amplification (SDA), transcription-based amplification, the Qβ replicase system and NASBA (Sambrook and Russell, 2001, supra). Preferably, amplification will be carried out using PCR.

[0027] Polymerase chain reaction (PCR) is carried out in accordance with known techniques. See, e.g., U.S. Pat. Nos. 4,683,195; 4,683,202; 4,800,159; and 4,965,188 (the disclosures of all three U.S. Patents are incorporated herein by reference). In general, PCR involves, a treatment of a nucleic acid sample (e.g., in the presence of a heat stable DNA polymerase) under hybridizing conditions, with one oligonucleotide primer for each strand of the specific sequence to be detected. An extension product of each primer which is synthesized is complementary to each of the two nucleic acid strands, with the primers sufficiently complementary to each strand of the specific sequence to hybridize therewith. The extension product synthesized from each primer can also serve as a template for further synthesis of extension products using the same primers. Following a sufficient number of rounds of synthesis of extension products, the sample is analysed to assess whether the sequence or sequences to be detected are present. Detection of the amplified sequence may be carried out by visualization following EtBr staining of the DNA following gel electrophores, or using a detectable label in accordance with known techniques, and the like.

[0028] Ligase chain reaction (LCR) is carried out in accordance with known techniques (Weiss, 1991, Science 254:1292). Adaptation of the protocol to meet the desired needs can be carried out by a person of ordinary skill. Strand displacement amplification (SDA) is also carried out in accordance with known techniques or adaptations thereof to meet the particular needs.

[0029] As used herein, the term “gene” is well known in the art and relates to a nucleic acid sequence defining a single protein or polypeptide. A “structural gene” defines a DNA sequence which is transcribed into RNA and translated into a protein having a specific amino acid sequence thereby giving rise to a specific polypeptide or protein. It will be readily recognized by the person of ordinary skill, that the nucleic acid sequence of the present invention can be incorporated into any one of numerous established kit formats which are well known in the art.

[0030] A “heterologous” (e.g. a heterologous gene) region of a DNA molecule is a subsegment of DNA within a larger segment that is not found in association therewith in nature. The term “heterologous” can be similarly used to define two polypeptide segments not joined together in nature. Non-limiting examples of heterologous genes include reporter genes such as luciferase, chloramphenicol acetyl transferase, beta-galactosidase, and the like which can be juxtaposed or joined to heterologous control regions or to heterologous polypeptides.

[0031] The term “vector” is commonly known in the art and defines a plasmid DNA, phage DNA, viral DNA and the like, which can serve as a DNA vehicle into which DNA of the present invention can be cloned. Numerous types of vectors exist and are well known in the art.

[0032] The term “expression” defines the process by which a gene is transcribed into one or more mRNAs (transcription), the mRNA is then being translated (translation) into one polypeptide (or protein) or more.

[0033] The terminology “expression vector” defines a vector or vehicle as described above but designed to enable the expression of an inserted sequence following transformation into a host. The cloned gene (inserted sequence) is usually placed under the control of control element sequences such as promoter sequences. The placing of a cloned gene under such control sequences is often referred to as being operably linked to control elements or sequences.

[0034] Operably linked sequences may also include two segments that are transcribed onto the same RNA transcript. Thus, two sequences, such as a promoter and a “reporter sequence” are operably linked if transcription commencing in the promoter will produce an RNA transcript of the reporter sequence. In order to be “operably linked” it is not necessary that two sequences be immediately adjacent to one another.

[0035] Expression control sequences will vary depending on whether the vector is designed to express the operably linked gene in a prokaryotic or eukaryotic host or both (shuttle vectors) and can additionally contain transcriptional elements such as enhancer elements, termination sequences, tissue-specificity elements, and/or translational initiation and termination sites.

[0036] Prokaryotic expression systems are useful for the preparation of large quantities of the protein encoded by the DNA sequence of interest. This protein can be purified according to standard protocols that take advantage of the intrinsic properties thereof, such as size and charge (e.g. SDS gel electrophoresis, gel filtration, centrifugation, ion exchange chromatography, reverse phase chromatography, etc.). In addition, the protein of interest can be purified via affinity chromatography, for example, using polyclonal or monoclonal antibodies or nickel affinity chromatography.

[0037] The DNA construct can be a vector comprising a promoter that is operably linked to an oligonucleotide sequence, which is in turn, operably linked to a heterologous gene, such as the gene for the luciferase reporter molecule. “Promoter” refers to a DNA regulatory region capable of binding directly or indirectly to RNA polymerase in a cell and and initiating transcription of a downstream (3′ direction) coding sequence. For purposes of the present invention, the promoter is bound at its 3′ terminus by the transcription initiation site and extends upstream (5′ direction) to include the minimum number of bases or elements necessary to initiate transcription at levels detectable above background. Within the promoter will be found a transcription initiation site (conveniently defined by mapping with S1 nuclease), as well as protein binding domains (cosensus sequences) responsible for the binding of RNA polymerase. Eukaryotic promoters will often, but not always, contain “TATA” boxes and “CCAT” boxes. Prokaryotic promoters contain −10 and −35 consensus sequences, which serve to initiate transcription and the transcript products contain Shine-Dalgarno sequences, which serve as ribosome binding references during translation initiation.

[0038] As used herein, the designation “functional derivative”, the context of a functional derivative denotes, in the context of a functional derivative of a sequence whether a nucleic acid or amino acid sequence, a molecule that retains a biological activity (either function or structural) that is substantially similar to that of the original sequence (e.g. acting as receptor for viral infection). This functional derivative or equivalent may be a natural derivative or may be prepared synthetically. Such derivatives include amino acid sequences having substitutions, deletions, or additions of one or more amino acids, provided that the biological activity of the protein is conserved. The same applies to derivatives of nucleic acid sequences which can have substitutions, deletions, or additions of one or more nucleotides, provided that the biological activity of the sequence is generally maintained. When relating to a protein sequence, the substituting amino acid has chemico-physical properties which are similar to those of the substituted amino acid. The similar chemico-physical properties include similarities in charge, bulkiness, hydrophobicity, hydrophilicity and the like. The term “functional derivatives” is intended to include “fragments”, “segments”, “variants”, “analogs”, or “chemical derivatives” of the subject matter of the present invention.

[0039] As well-known in the art, a conservative mutation or substitution of an amino acid refers to mutation or substitution which maintains: 1) the structure of the backbone of the polypeptide (e.g. a beta sheet or alpha-helical structure); 2) the charge or hydrophobicity of the amino acid; or 3) the bulkiness of the side chain. More specifically, the well-known terminologies “hydrophilic residues” relate to serine, threonine, glutamine or asparagine. “Hydrophobic residues” refer to leucine, isoleucine, alanine, methionine, valine or proline. “Positive charged residues” refer to lysine, arginine or histidine. “Negatively charged residues” refer to aspartic acid or glutamic acid. Residues having “bulky side chains” refer to phenylalanine, tryptophan or tyrosine.

[0040] The term “variant” refers herein to a protein or nucleic acid molecule which is substantially similar in structure and biological activity to the protein, peptide, or nucleic acid described in the present invention.

[0041] The term “allele” defines an alternative form of a gene that occupies a given locus on a chromosome. Non-limiting examples thereof are exemplified with murine CEACAM1a and CEACAM1b.

[0042] As commonly known, a “mutation” is a detectable change in the genetic material which can be transmitted to a daughter cell. A mutation can be, for example, a detectable change in one or more deoxyribonucleotide or amino acid. For example, nucleotides or amino acids can be added, deleted, substituted for, inverted, or transposed to a new position. Spontaneous mutations and experimentally induced mutations exist. The result of a mutations of nucleic acid or amino acid molecule is a mutant molecule. A mutant polypeptide can be encoded from this mutant nucleic acid molecule.

[0043] It shall be understood that an in vitro assay may be used to demonstrate the utility of the particular molecule being examined as a useful therapeutic in vivo. For example, cellular extracts from an animal or purified animal testing extract of cells such as T-cells can be prepared and used as representative vitro to demonstrate the functionality and utility of the molecule as immunomolulatory molecule. An in vitro assay could be used to compare the infectious potential of infectious agents on extracts prepared from animal tissue in this same manner.

[0044] As used herein in the recitation “indicator cells” refers to cells that express, in one particular embodiment, the CEACAM1 glycoprotein or domains thereof which interact with a viral protein or other cellular protein which is directly or indirectly involved in infection by the virus or other molecular interactions of CEACAM 1, and wherein an interaction between these proteins or interacting domains thereof is coupled to an identifiable or selectable phenotype or characteristic such that it provides an assessment of the interaction between same. Such indicator cells can be used in the screening assays of the present invention. In certain embodiments, the indicator cells have been engineered so as to express a chosen derivative, fragmnent, homologue, or mutant of these interacting domains. The cells can be yeast cells or preferably higher eukaryotic cells such as mammalian cells (WO 96/41169).

[0045] A host cell or indicator cell has been “transfected” by exogenous or heterologous DNA (e.g. a DNA construct) when such DNA has been introduced inside the cell. The transfecting DNA may or may not be integrated (covalently linked) into chromosomal DNA making up the genome of the cell. In prokaryotes, yeast, and mammalian cells for example, the transfecting DNA may be maintained on an episomal cell element, such as a plasmid. With respect to eukaryotic cells, a stably transfected cell is one in which the transfecting DNA has become integrated into a chromosome so that it is inherited by daughter cells through chromosome replication. This stability is demonstrated by the ability of the eukaryotic cell to establish cell lines or clones comprised of a population of daughter cells containing the transfecting DNA. Transfection methods are well known in the art (Sambrook and Russell (2001), Ausubel et al., (1994)).

1C C′ loop, human CEACAM1 (10 a a) D1K-G-E-R-V-D-G-N-R-QSEQ ID NO: 11 10

[0046]

2

D1 loop, human CEACAM1 (1-107 aa)

1
Q-L-T-T-E-S-M-P-F-N-V-A-E-G-K-E-V-L-L-L-V-H-N-L-P
25
SEQ ID NO: 2

26
Q-Q-L-F-G-Y-S-W-V-K-G-E-R-V-D-G-N-R-Q-I-V-G-Y-A-I
50

51
G-T-Q-Q-A-T-P-G-P-A-N-S-G-R-E-T-I-Y-P-N-A-S-L-L-I
75

76
Q-N-V-T-Q-N-D-T-G-F-Y-T-L-Q-V-I-K-S-D-L-V-N-E-E-A
100

101
T-G-Q-F-H-V-Y
107

BRIEF DESCRIPTION OF THE FIGURES

[0047]
FIG. 1. Stereo view of the ribbon drawing of msCEACAM1a [1,4] which contains two Ig-like domains. The CC′-loop in the N-terminal domain (D1) which is involved in binding of MHV and other ligands is marked by an arrow. The predicted key virus-binding residue Ile41 on the CC′ loop is shown in ball-and-stick style. The FG loop of D1, another biologically important element is also shown. The carbohydrate moieties are drawn in ball-and-stick style. The glycan at Asn70 that is conserved in the whole CEA family is labeled. The figure was prepared using MOLSCRIPT ®(Krulis, 1991).

[0048]
FIG. 2(A)-2(C). Superposition of D1 of msCEACAM1a[1,4], CD2, CD4 and Bence-Jones protein REI. Each molecule is shown in Cat trace, with msCEACAM1a in a thick solid line (SEQ ID NO: 4), CD2 in a thin dashed line (SEQ ID NO: 5), CD4 in a solid line (SEQ ID NO: 6) and REI in a thick dashed line (SEQ ID NO: 7), respectively. The uniquely convoluted conformation of the CC′ loop in msCEACAM1a[1,4] is striking. The sequence alignment of the CC′ loop regions of these four molecules are also shown using the same code (SEQ ID NOS 4-7, respectively in the order of appearance). (2B) Stereo view of the exposed residues on the CFG face of D1 of msCEACAM1a[1,4]. The CaLtrace of the CC′ loop is highlighted. Displayed sidechains and carbohydrates are drawn in ball-and-stick style. (2C) Electrostatic potential surface representation of the same view as (B). FIGS. 2A and B were prepared with MOLSCRIPT ® (Krulis, 1991), and 2C, with GRASP®) (Nicholls et al., 1991).

[0049]
FIG. 3. A comparative view of structures of several virus receptors, including msCEACAM1a, receptor for murine coronavirus MHV; ICAM1, receptor for the major group of rhinoviruses; CD4, primary receptor for HIV; and CD46, receptor for measles virus. Shown here are only their N-terminal domains. Their key virus-binding motifs with uniquely topological features are also highlighted.

[0050]
FIG. 4. Sequence alignment of D1 and D4 of murine CEACAM1 with corresponding domains of human CEA family members. Residues invariant throughout all sequences shown are in bold italics, courier (serif), whereas physico-chemically conserved residues (with no more than two exceptions) are bold monospace (sans serif). The β-strands are shown underlined. (4A) D1 of murine CEACAM1a (SEQ ID NO: 8) is aligned with D1 of murine CEACAM1b (SEQ ID NO: 2) (upper panel), as well as the human CEA members found in the SWISSPROT database (lower panel) (SEQ ID NOS 10-24, respectively in the order of appearance). (4B) D4 of murine CEACAM1a (SEQ ID NO: 26) is aligned with D2 of the same molecule (upper panel) (SEQ ID NO: 25). This marks potential N-glycosylation sites. These sequences are compared with the A1 (SEQ ID NO: 27), A2 (SEQ ID NO: 28), A3 (SEQ ID NO: 29) and B1 (SEQ ID NO: 30), B2 (SEQ ID NO: 31), B3 (SEQ ID NO: 32) domains of human CEA, the gene product of CEACAM5 (lower panel).

[0051]
FIG. 5. Topology diagram for D1 of msCEACAM1a with β-strands shown as arrows. The diagram is coded according to the degree of variability in sequence of N-terminal domain for all available mammalian CEA molecules. The variability was measured using Shannon's entropy value (H) (Stewart et al., 1997). The least variable, or most conserved, residues (H<1) are shown as a dotted region, whereas the most variable ones (H>2) are depicted as an angled hatched region. Those residues in between (1<H<2) are depicted in a squared region. The difference in the degree of sequence conservation between the ABED and CFG faces is evident. On the ABED face, the glycan at Asn 70 and the shielded hydrophobic residues are marked.

[0052]
FIGS. 6A and B. Backbone worm representation of the “parallel” interaction between the dyad-related msCEACAM1a[1,4] molecules seen in the crystal structure, prepared with GRASP® (Nicholls et al., 1991). (6A) Two monomers are related by a crystallographic 2-fold axis, and are shown in a bold hatched line and a open hatched line, respectively. Carboydrates are drawn in ball-and-stick style. (6B) Stereo picture of the close-up view across the dimer interface. Those sidechain involved in interactions are shown in ball-and -stick style.

[0053]
FIG. 7 is the surface representation of the model, in which the glycan-protected areas for CEA is a cross-hatched area, labeled (I). The area shielded by glycans on CEACAM6 but not on CEA is labeled (II). The white areas are exposed and they contain the potential Mabs epitopes that recognize both CEA and CEACAM 6.

DETAILED DESCRIPTION OF THE PREFERRED EMBODIMENTS

[0054] The present invention is illustrated in further detail by the following non-limiting examples. Although the following descriptions are directed to preferred embodiments, namely a molecular model useful for designing compounds that modulate the interaction between the novel structure of the CC′ loop of the carcinoembryonic antigen cell adhesion molecule and other molecules (e.g. antibodies, proteins, peptides or other small molecules), as well as the various compounds that will satisfy this criteria, it should be understood that this description is illustrated only and is not intended to limit the scope of the invention.

[0055] The amino acid residues described herein are preferred to be in the “L” isomeric form. However, residues in the “D” isomeric form can be substituted for any L-amino acid residue, as long as the desired fractional property of immunoglobulin-binding is retained by the polypeptide. NH2 refers to the free amino group present at the amino terminus of a polypeptide. COOH refers to the free carboxy group present at the carboxy terminus of a polypeptide. In keeping with standard polypeptide nomenclature, J. Biol. Chem., 243:3552-59 (1969), abbreviations for amino acid residues are shown in the following Table of Correspondence:

3TABLE OF CORRESPONDENCESYMBOL1-Letter3-LetterAMINO ACIDYTyrtyrosineGGlyglycineFPhephenylalanineMMetmethionineAAlaalanineSSerserineIIleisoleucineLLeuleucineTThrthreonineVValvalinePProprolineKLyslysineHHishistidineQGlnglutamineEGluglutamic acidWTrptryptophanRArgarginineDAspaspartic acidNAsnasparagineCCyscysteine

[0056] It should be noted that all amino-acid residue sequences are represented herein by formulae whose left and right orientation is in the conventional direction of amino-terminus to carboxy-terminus. Furthermore, it should be noted that a dash at the beginning or end of an amino acid residue sequence indicates a peptide bond to a further sequence of one or more amino-acid residues. The above Table is presented to correlate the three-letter and one-letter notations which may appear alternately herein.

[0057] A number of articles review computer modeling of drugs interactive with specific proteins, such as Rotivinen (1988); Ripka (1988); McKinaly and Rossmann (1989); Perry and Davies (1989); Lewis and Dean (1989); and with respect to a model receptor for nucleic acid components, Askew, et al. (1989). Other computer programs that screen and graphically depict chemicals are available from companies such as BioDesign, Inc. (Pasadena, Calif.), Allelix, Inc. (Mississauga, Ontario, Canada), and Hypercube, Inc. (Cambridge, Ontario).

[0058] Although described above with reference to design and generation of compounds which could alter binding, one could also screen libraries of known compounds, including natural products or synthetic chemicals, and biologically active materials, including proteins, for compounds which are inhibitors or activators.

[0059] Compounds identified via assays such as those described herein may be useful, for example, for treating any of the conditions disclosed herein that depend upon biological interactions of CEACAM1 or structurally related proteins. Assays for testing the efficacy of compounds identified in the cellular screen can be tested in animal model systems for such conditions. Such animal models may be used as test substrates for the identification of drugs, pharmaceuticals, therapies and interventions which may be effective in treating such conditions. For example, animal models may be exposed to a compound suspected of exhibiting an ability to ameliorate a condition mediated by CEACAM1 or related proteins at a sufficient concentration and for a time sufficient to elicit such an amelioration of condition-associated symptoms in the exposed animals. The response of the animals to the exposure may be monitored by assessing the reversal of symptoms associated with the condition, such as an autoimmune condition or a delayed hypersensitivity response to an antigen, or by assessing prevention of infection with a virus or bacterium that depends upon binding to CEACAM1 or structurally related proteins on host cell membranes. With regard to intervention, any treatments that are based on the homologous human sequence and structure which reverse any aspect of such symptoms in an animal model system should be considered as candidates for human therapeutic intervention, in this manner, homologous drugs to examine in humans would be prepared. Dosages of test agents may be determined by deriving dose-response curves, in accordance with standard practice.

[0060] According to still another aspect of the invention, low molecular weight compounds that inhibit the interaction between CEACAM1 or structurally related proteins, peptides or other biologically important molecules, to and their natural ligands in the body, or to proteins of bacteria or viruses that use these molecules as receptors are provided. These compounds can be used to modulate the interaction, or can be used as lead compounds for the design of better compounds using the above-described computer-based rational drug design methods.

[0061] As also described in U.S. Pat. No. 5,908,609, exemplary library compounds include, but are not limited to, peptides such as, for example, soluble peptides, including but not limited to members of random peptide libraries; (see, e.g., Lam, K. S. et al., (1991); Houghten, R. et al., (1991)), and combinatorial chemistry-derived molecular libraries made of D-and/or L-configuration amino acids, phosphopeptides (including but not limited to, members of random or partially degenerate, directed phosphopeptide libraries; (see, e.g., Songyang, Z. et al., (1993)); antibodies (including, but not limited to, polyclonal, monoclonal, humanized, anti-idiotypic, chimeric or single chain antibodies, and Fab, F(ab), sub. 2 and Fab expression library fragments, and epitope-binding fragments thereof), and small organic or inorganic molecules. Other compounds which can be screened in accordance with the invention include but are not limited to small organic molecules that are able to gain entry into an appropriate cell and affect the interaction of CEACAM1 (or structurally related proteins in the CEA family) with its natural ligands in vivo or with bacteria or viruses. For example, the compounds of the invention that can be designed to satisfy the foregoing criteria include polypeptides and peptide mimetics. The peptide mimetic can be a hybrid molecule which includes both amino acid and non-amino acid components, e.g., the mimic can include amino acid components for the positively charged and negatively charged regions and non-amino acid (e.g., piperidine) having the same approximate size and dimension of a hydrophobic amino acid (e.g., phenylalanine) as the hydrophobic component.

[0062] In certain embodiments, the screening assay is designed to identify agents which modulate the interaction of the CEACAM1 or structurally related protein with the viral spike glycoprotein or a bacterial adhesion molecule or outer membrane protein (referred to in the art as a heterophilic interaction) and not interfere with homophilic interactions (e.g., CEACAM1 binding to another CEACAM1 or structurally related molecule). In this manner, agents can be selected which advantageously affect only the interaction of CEACAM1 or structurally related proteins with bacteria or viruses, without adversely affecting other natural cellular functions of these polypeptides. In these and other embodiments, the assays optionally involve the step of introducing the compound into an animal model of a condition mediated by the interaction of CEACAM1 or structurally related proteins and pathogenic bacteria or viruses and determining whether the compound prevents infection or alleviates the symptoms of the condition. At the same time, the natural cellular functions of CEACAM1 in cell adhesion, immune interactions, angiogenesis, etc. would be assayed to assure that these were normal, i.e., within pharmacological acceptable levels.

[0063] In general, the assay can be of any type, provided that the assay is capable of detecting the interaction of a CEACAM1 or structurally related protein and a natural ligand. Preferably, the assay is a binding assay (e.g., an adhesion assay)which detects adhesion between the CEACAM1 or structurally related protein and the domain or polypeptide of the natural ligand that binds to CEACAM1 or related protein. Exemplary adhesion assays are described in the Examples. In general, such assays can be performed using cell-free or cell-based systems, e.g., the polypeptide components can be isolated or can be expressed on the surface of a cell. Additionally, or alternatively, the assay can be a signaling assay which detects signaling events following interaction of the ligand or domain of the ligand and the CEACAM1 (or related ) protein or the ligand-binding domain of CEACAM1. In such instances, the signaling assay typically is a cell-based assay in which the CEACAM1 protein is expressed on a cell. In a cell signaling assay, a down-stream effect (e.g., a change in cytokine expression, enhanced expression of another gene) or altered expression of a receptor due to CEACAM1 binding to the ligand or the CEACAM1-binding domain of the ligand is detected, rather than detecting only the adhesion of these molecules to one another.

[0064] Regardless of the particular type of assay, in some embodiments, the assays of the invention may utilize an isolated ligand for CEACAM1, unless the assay further involves the selection of a molecular library, which takes into account the information presented herein with respect to the approximate size and charge characteristics of prospective modulators of the interaction. In the latter instances, the CC′ loop of CEACAM1 or a domain of its natural ligand that binds to the CC′ loop of CEACAM1 may form part of a synthesized or recombinant polypeptide that may or may not be complexed to a marker polypeptide or molecule. The assays of the invention may utilize CEACAM1 protein which is complete or, alternatively, which contains a CEACAM1 N-terminal domain (e.g., at least an isolated domain but not the entire 4 domain anchored CEACAM1 polypeptide sequence). The protein or peptide may be used in isolated form (e.g., immobilized to a solid support or as a soluble fusion protein as described in the examples) or expressed on the surface of a cell (e.g., an epithelial cell, an endothelial cell, or other cell genetically engineered to express the CEACAM1). The ligand polypeptide that binds to the CC′ loop of CEACAM1 (such as a viral spike glycoprotein, or bacterial outer membrane protein, or homophilic binding domain of CEACAM1, or a monoclonal antibody) likewise may be used in isolated form or expressed on the surface of a cell.

[0065] As used herein in reference to a peptide, the term “isolated” refers to a cloned expression product of an oligonucleotide; a peptide which is isolated following cleavage from a larger polypeptide; or a peptide that is synthesized, e.g., using solution and/or solid phase peptide synthesis methods as disclosed in, for example, U.S. Pat. No. 5,120,830, the entire contents of which are incorporated herein by reference. Accordingly, the phrase “isolated peptides” embraces peptide fragments of CEACAM1 or its ligands as well as functionally equivalent peptide analogs of the foregoing peptide fragments. As used herein, the term “peptide analog” refers to a peptide which shares a common structural feature with the molecule to which it is deemed to be an analog. A “functionally equivalent” peptide analog is a peptide analog which further shares a common functional activity with the molecule to which it is deemed an analog. Alternatively, the binding partners in the adhesion assays can be the particular ligands and receptors which mediate intercellular adhesion. For example, the binding of a lymphocyte, macrophage, polymorphonuclear cell or dendritic cell to an epithelial or endothelial cell may be mediated via the specific interaction of CEACAM1 and CEACAM1(on the epithelial cell). Accordingly, adhesion assays can be performed in which the binding partners are: (1) interacting cells (e.g. a lymphocyte and an epithelial cell, or a lymphocyte and a dendritic cell); (2) a cell expressing a ligand (e.g. an lymphocyte expressing CEACAM1 or a structurally related protein) and an isolated receptor (e.g. soluble recombinant CEACAM1) for the ligand; (3) an isolated ligand and a cell expressing the receptor for the ligand; and (4) an isolated ligand and its isolated receptor (e.g. soluble CEACAM1a[1,4] and MHV viral spike protein).

[0066] Thus, a high throughput screening assay for selecting pharmaceutical lead compounds can be performed. In one embodiment, the screening assay as a method of selecting pharmaceutical lead compounds will comprise the following steps: (1) immobilizing CEACAM1 onto a surface of a microtiter well having a plurality of wells, (2) adding an aliquot of a molecular library containing library members selected in accordance with methods of the invention 3) adding cells expressing a ligand for CEACAM1 (e.g. lymphocytes) to the wells and (4) incubating the well components are allowed to incubate for a period of time that is sufficient for the cells to bind to immobilized CEACAM1. Preferably, the cells (or soluble CEACAM1-binding protein or peptide) are labeled (e.g., preincubated with Cr 51 or a fluorescent dye) prior to their addition to the microtiter well. Following the incubation period, washing the wells to remove non-adherent cells and the signal attributable to the label on the remaining attached lymphocytes is determined. A positive control (e.g., a cell type that is known to bind to CEACAM1) on the same microtiter plate is used to establish maximal adhesion value. A negative control (e.g., soluble CEACAM1 added to the microtiter well) on the same microtiter plate is used to establish maximal levels of inhibition of adhesion.

[0067] The screening methods of the invention provide useful information for the rational drug design of novel agents which are, for example, capable of modulating an immune system response, or blocking viral or bacterial infection. In addition to the above-noted computer model programs, exemplary procedures for rational drug design are provided in Saragovi, H. er al., (1992); Haber E. (1983)(:1967); and Connolly Y., (1991) (“Computer-Assisted Rational Drug Design”: pp 587-616), the contents of which are incorporated herein by reference.

[0068] Thus, knowledge of the structure (primary, secondary or tertiary) of naturally occurring ligands and receptors can be used to rationally choose or design molecules which will bind with either the ligand or receptor. In particular, knowledge of the binding regions of ligands and receptors can be used to rationally choose or design compounds which are more potent than the naturally occurring ligands in eliciting their normal response or which are competitive inhibitors of the ligand-receptor interaction.

[0069] Once rationally chosen or designed and selected, the library members may be altered, e.g., in primary sequence, to produce new and different peptides. These fragments may be produced by site-directed mutagenesis or may be synthesized in vitro. These new fragments may then be tested for their ability to bind to the receptor or ligand and, by varying their primary sequences and observing the effects, peptides with increased binding or inhibitory ability can be produced. For example, improved compounds which modulate the interaction of a cell adhesion assay can be made by making conservative amino acid substitutes in peptides (e.g., Formula I) that are designed to fit in the active site defined by the docking model disclosed herein. As used herein, “conservative amino acid substitution” refers to an amino acid substitution which does not substantially alter the relative physico-chemical characteristics of the peptide in which the amino acid substitution is made.

[0070] It will be appreciated by those skilled in the art that various modifications of the foregoing peptide analogs can be made without departing from the essential nature of the invention. Accordingly, it is intended that peptides which include conservative substitutions and couples proteins in which a peptide of the invention is coupled to a solid support (such as a polymeric bead), a carrier molecule (such as keyhole limpet hemocyanin), a toxin (such as ricin) or a reporter group (such as radiolabel or other tag), also are embraced within the teachings of the invention.

[0071] The screening assays of the invention are useful for identifying pharmaceutical lead compounds in molecular libraries. A “molecular library” refers to a collection of structurally-diverse molecules. Molecular libraries can be chemically-synthesized or recombinantly produced. As used herein, a “molecular library member” refers to a molecule that is contained within the molecular library. Accordingly, “screening” refers to the process by which library molecules are tested for the ability to modulate (i.e., inhibit or enhance) interaction between a CEACAM1 or structurally related protein and a naturally occurring ligand, or a viral protein or bacterial protein or an antibody specific for CEACAM1, particularly the biologically active CC′ loop which has the unique structure described herein. As used herein, a “pharmaceutical lead compound” refers to a molecule example. Screening assays are useful for assessing the ability of a library molecule to inhibit the binding of a CEACAM1 ligand (or an polypeptide derived from CEACAM1 or structurally related protein) to a natural ligand.

[0072] Libraries of structurally diverse molecules can be prepared using chemical and/or recombinant technology. Such libraries for screening include recombinantly produced libraries of fusion proteins. An exemplary recombinantly produced library is prepared by ligating fragments of CEACAM1 or related protein into, for example, the pGEX2T vector (Pharmacia, Piscataway, N.H.). This vector contains the carboxy terminus of glutathion S-transfersse (GST) from Schistosoma japonicum. Use of the GST-containing vector facilitates purification of GST-polypeptide fusion proteins from bacterial lysates by affinity chromatography on glutathione sepherose. After elution from the affinity column, the fusion proteins are tested for activity by, for example, subjecting the fusion protein to the screening assays disclosed herein. Fusion proteins which inhibit binding between CEACAM1 expressing cells are selected as pharmaceutical lead compounds and/or to facilitate further characterization of the portion of the lead compound which blocks homophilic binding.

[0073] The methods of the invention are useful for identifying novel compounds that are capable of modulating a mucosal immune response in vivo. Accordingly, the invention further provides a pharmaceutical preparation for modulating a mucosal immune response in a subject is provided. The composition includes a pharmaceutically acceptable carrier and an agent that inhibits interaction (e.g., adhesion) between CC′ loops of CEACAM1 molecules. In particularly preferred embodiments, the agent inhibits homophlic adhesion between CEACAM1-expressing cells. The agent (e.g., the above-described peptide) is present in a therapeutically effective amount for treating the immune response or treating or preventing viral or bacterial infection. Thus, in a related aspect, the invention also provides a method for modulating the mucosal immune response of a subject. The method involves administering to the subject a pharmaceutical composition comprising the above-described agents for inhibiting adhesion between CEACAM1-expressing cells. In addition, the same compounds can be tested for the ability to inhibit or treat bacterial or viral infections of microbes that use CEACAM1 as receptors.

[0074] In general, the therapeutically effective amount is between about 1 mg and about 100 mg/kg. The preferred amount can be determined by one of ordinary skill in the art in accordance with standard practice for determining optimum dosage levels of the agent. The compounds are formulated into a pharmaceutical composition by combination with an appropriate pharmaceutically acceptable carrier. For example, the compounds may be used in the form of their pharmaceutically acceptable salts, or may be used alone or in appropriate association, as well as in combination with other pharmaceutically active compounds. The compounds may be formulated into preparations in solid, semisolid liquid, or gaseous form such as tablets, capsules, powders, granules, ointments, solutions, suppositories, inhalants and injections, in usual ways for oral, parenteral, or surgical administration. Exemplary pharmaceutically acceptable carriers are described in U.S. 5,211,657, the entire contents of which patent are incorporated herein by reference. The invention also includes locally administering the composition as an implant.

[0075] In order for this invention to be fully understood, the following examples are set forth. These examples are for the illustrative purpose only and not to be seen as limiting the scope of this invention.

EXAMPLE 1

Protein Expression and Purification

[0076] Nucleotide sequences encoding the first 236 amino acids of murine CEACAM1a[1,4] including the natural 34 aa long signal sequence were amplified by PCR using an oligonucleotide that added an XbaI site in frame at the 3′ end. This DNA was ligated in frame into a previously described construct encoding a thrombin cleavage peptide followed by six histidine residues and a stop codon (Zelus et al., 1998), and inserted into the pShuttle CMV vector (He et al., 1998). This construct was inserted into the pAd-Easy adenovirus vector, and adenoviruses that contained the cDNA were plaque purified and amplified in 293 cells as previously described (He et al., 1998). Lec-CHO cells stably transfected with CAR, the Coxsackie/adenovirus receptor were transduced with the CEACAM1a[1,4]-containing adenovirus. The soluble, his-tagged murine CEACAM1a[ 1,4] protein from the supernatant medium was purified by nickel affinity chromatography on a Pharmacia HiTrap chelating column, and eluted with imidazole. Fractions containing the protein were identified by immunoblotting with polyclonal rabbit antibody directed against murine CEACAM1a, and the pooled fractions were dialyzed against 25 mM Tris buffer, pH 9.0, with 5% glycerol. The protein was further purified by ion exchange chromatography on a HQ20 (Poros) column and eluted in a sodium chloride gradient. Fractions containing the protein were pooled, dialyzed against 25 mM TRIS pH (7.6), 150 MM NaCl, 5% glycerol, and stored at −80° C. The purity of the proteins was determined by silver staining of SDS-PAGE gels and by Western blotting with anti-CEACAM1a antibody. The medium of 40 T150 flasks of adenovirus transduced lec-, CAR+CHO cells yielded approximately 0.5 to 1 mg of purified msCEACAM1a[1,4] protein.

EXAMPLE 2

Crystallization and X-ray Data Collection

[0077] Single crystals of msCEACAM1a[1,4] were grown from a crystallization buffer containing 10% PEG 8000, 0.2 M magnesium acetate and 0.1 M cacodylate at pH 6.4 using the vapor-diffusion hanging drop method. For data collection at cryogenic temperature, the crystals were treated with a cryoprotectant solution (25% glycerol, 10% PEG 8000 and 0.1 M cacodylate), then frozen and stored in liquid nitrogen. Platinum derivatives were prepared by soaking the crystals overnight in the same cryo-protectant solution containing 0.5 mM K2PtBr4.

[0078] X-ray diffraction data were collected from pre-frozen crystals at APS SBC 19ID in Argonne National Laboratories at a temperature of 100° K. A native crystal diffracted to a resolution of 3.32 Å, with one molecule in one asymmetric unit. A multi-wavelength anomalous diffraction (MAD) data set of the platinum derivative was obtained to a resolution of 3.85 Å. All the raw data were indexed and reduced with HKL2000 (Otwinowski and Minor, 1997)(Table I).

EXAMPLE 3

[0079] Structure Determination and Refinement

[0080] The msCEACAM1a[1,4] structure was solved using the MAD phases in combination with molecular replacement (MR). Using programs in the CCP4 suite (CCP4, 1994), one Pt binding site was identified in one asymmetric unit in both difference and anomalous difference Patterson maps. Heavy atom parameters were refined at 4 Å resolution with the program MLPHARE in CCP4 suite, and an additional platinum site was identified. Phase extension was performed using the native data set to 3.32 Å by solvent flattening and histogram matching with DM. The resulting phases were used to carry out a phased molecular replacement with ROTPTF on the Bronx X-ray server for the two separate domains. The N-terminal domains of CD2 (PDB code 1HNF) and human Fc-γ receptor III (PDB code 1E4J) were used as search models for the D1 and D4 domains of msCEACAM1a[1,4], respectively. The model was traced with XtalView (http://www.scripts.edu/pub/dem-web) on the basis of the MAD phases, using the MR solutions as a guideline.

[0081] After cycles of model building using program 0 (Jones et al., 1991) and refinement, the final model was refined at 3.32 Å resolution to an Rfree factor of 32.9% and Rwork of 29.5% (Table I) using the Xplor (Brunger, 1992). At 1.5σ contour level (σ=0.125 e/Å3) in 2Fo-Fc map, there was continuous density for the main chain backbone. The final model contains 203 residues (from Glu1 to Thr203) and a total of 6 sugar residues associated with four of the five potential glycosylation sites. There was no visible electron density beyond residue Thr203 where more than a dozen residues including a his-tag are present in the expression construct. These C-terminal residues are apparently disordered. The current model also includes a total of 26 water molecules. Some of the densities assigned to solvent molecules around the end of glycans might be from partially disordered branched sugar residues.

4TABLE 1Data Collection, Structure determination and RefinementData CollectionData setPt peak¶Pt-inflections¶Pt-remote¶NativeSpace groupP3121Unit Cell (Å)a,b = 111.85, c = 66.34a,b = 111.26, c = 65.64X-ray sourceAPSWavelength (Å)1.07151.07181.05341.100Resolution (Å)20-3.8520-3.8520-3.8530-3.32Observations491795038945774123640(uniquely)(8681)¶(8645)¶(8566)¶(7127)I/σ overall16.0 (3.1)*15.2 (3.3)*13.2 (2.3)*17.3 (37)*Completeness (%)99.2 (91.8)*99.6 (96.3)*97.6 (82.9)*99.7 (100.0)*RMerge (%) 7.5 (45.4)* 6.9 (42.3)* 8.0 (55.4)* 7.3 (37.1)*Structure DeterminationFigure of Merit0.49Phasing power1.921.861.79RCullis (anomalous)0.820.840.88RCullis (isomorpous)0.600.610.61Structure RefinementResolution (Å)15-3.32Number of work/test reflections6144/754Nonhydrogen protein/carbohydrate/solvent atoms1692/81/26RWork/RFree (%)29.5/32.9Bond length(Å)/angle(°) rms deviation from ideal geometry0.011/2.325Ramachandran statistics (%)68.5/23.4/8.2/0Favourable/Additional/Generous/ForbiddenProtein atoms average B value (Å2), Mainchain/Sidechain55.12/64.15¶Bijvoet pairs are both counted, *(Last resolution bin)

EXAMPLE 4

Molecular structure of msCEACAM1a[1,4]

[0082] The msCEACAM1a[1,4] protein analyzed contains the 202 extracellular amino acids of the naturally expressed CEACAM1a[1,4] protein plus a six histidine-tag connected to the carboxy-terminus by a thrombin cleavage peptide. This soluble murine CEACAM1a[1,4] protein has strong virus neutralization activity at 37 ° C., pH 7.2, and readily induces an irreversible conformational change in the MHV-A59 spike glycoprotein under these conditions (Zelus et al., 1998).

[0083]
FIG. 1 shows the ribbon diagram of the molecular structure of soluble murine msCEACAM1a [1,4]. The two Ig-like domains of msCEACAM1a[1,4] are arranged in tandem. When the membrane proximal domain (D4) was oriented vertically as if it were perpendicular to the cell membrane, the virus-binding domain (D1) had a bending angle of about 60° from the vertical, with its A′GFCC′C″ β sheet (called CFG face hereafter) facing upwards, away from the cell membrane (FIG. 1). The rotation angle between D1 and D4 is about 170°, which places the CFG face of D4 on the opposite side of the molecule from the CFG face of D1, Other IgSF proteins on the cell surface have this orientation (Wang and Springer, 1998). Although there are five potential N-linked glycosylation sites on this protein, the crystal structure showed that only four of these sites are utilized: three in D1, and one in D4. One or more sugar moieties were clearly seen at each of these sites (FIG. 1), but no electron density was visible to indicate the presence of a possible glycan at Asn161 in the Asn-Asn-Ser motif in the DE loop of D4. The only observed glycan in D4 is at Asn119 (FIG. 1) near the bottom of the molecule, pointing downward toward the cell membrane. This glycan may play a role in holding the rod-like molecule erect on the membrane as shown for CD2 (Jones et al., 1992), ICAM-2 (Casasnovas et al., 1997), and CD4 (Wu et al., 1997).

[0084] The N-terminal domain (D1) of msCEACAM1a[1,4] belongs to the V set Ig-like fold. Within the IgSF, the CEA family and the CD2 family are unique in that their N-terminal domains lack the inter-sheet disulfide bond between β strands B and F that is conserved in the N-terminal domains of other IgSF members. In the DALI search for structures homologous to D1 of msCEACAM1a[1,4] using the web site (http://www2.ebi.ac.uk/dali/), D1 of CD2 was one of the top hits. There are, however, three important structural elements that distinguish D1 of msCEACAM1a[1,4] from CD2-D1. One striking feature of D1 of msCEACAM1a[1,4] is its uniquely structured, prominently protruding CC′ loop (highlighted in FIG. 1) that points upwards. The unique and intricate structure of the CC′ loop will be described in detail below. D1 of msCEACAM1a[1,4], like other V set Ig-like folds, retains a salt bridge between an arginine (Arg64) at the beginning of the D strand and an aspartate (Asp82) at the beginning of the F strand. This salt bridge may help to strengthen the interactions between the two anti-parallel β sheets of D1. By contrast, CD2-D1 does not have a salt bridge between the D sheets (Jones et al., 1992). Another difference between the D1s of msCEACAM1a[1,4] and CD2 is found at the A-A′ kink. As a structural hallmark in both V set and I set Ig folds, the A strand in one sheet runs midway through the domain, and then crosses over to join the opposite sheet, becoming the A′ strand. This may stabilize the membrane-distal domain that is usually the site for ligand binding (Wang and Springer, 1998). The amino acid at the kink position is usually a cis-proline. In D1 of msCEACAM1a[1,4], the A′ strand is significantly shorter than that of most other Ig-like molecules, whereas D1 of CD2 and some other CD2 family members have a relatively long A′ strand with no A strand at all. These features might reflect differences in the biological functions of CD2 and CEACAM1a.

[0085] Structural analysis shows that the C-terminal domain (D4) of msCEACAM1a[1,4] falls into the I1 set category (Harpaz and Chothia, 1994; Wang and Springer, 1998), rather than the C2 set as widely thought. Compared to the I set Ig-like domains of most other IgSF members, D4 of msCEACAM1a[1,4] has an unusually long CD loop of 10 residues (amino acids 146-155). The long CD loop in D4 of msCEACAM1a[1,4] is probably quite stable because it has a β-turn at each end (including the 2 residue C′ strand) and Leu152 and Leu152 in the middle of the loop point inward, joining the molecule's hydrophobic core.

[0086] msCEACAM1a[1,4] has a linker between D1 and D4. The last residue of D1 is His107, and the A strand of the following domain D4 starts at Phe114. The peptide segment in between does not appear to have mainchain-mainchain hydrogen bonds to the D4 domain. No significant interactions were observed between D1 and D4. The surface buried area between these two domains is 530 Å2, with a 1.7 Å probe. These observations indicate that the D1-D4 junction of msCEACAM1a[1,4] is quite flexible.

EXAMPLE 5

The unique CC′ loop of the N-terminal Domain Is an MHV-binding Site

[0087] Both the spike glycoprotein of MHV virions and MAb-CC1, a monoclonal antibody to murine CEACAM1a that blocks the binding of the virus to the receptor, were shown to bind to D1 of murine CEACAM1a (Dveksler et al., 1993b). Mutational analyses of murine CEACAM1a show that the peptide segments between amino acids 38 and 43 (Rao et al., 1997) or between amino acids 34 and 52 (Wessner et al., 1998) are involved in binding to the MHV spike glycoprotein, in virus receptor activity and binding of MAb-CC1. The structure for msCEACAM1a[1,4] defined in the present invention shows that this virus binding region is in the CC′ loop and the C′ strand.

[0088] Compared to the N-terminal domains of other IgSF members, D1 of msCEACAM1a[1,4] has an unusual CC′ loop, as marked in FIG. 1. This structure could not have been predicted based on the knowledge of the amino acid sequence in this region. FIG. 2A shows an overlay onto D1 of msCEACAM1a[1,4] of the N-terminal domains of three other representative IgSF proteins, CD2 (Jones et al., 1992), CD4 (Wang et al., 1990), and Bence-Jones protein REI (Epp et al., 1975), a typical variable domain of an antibody. The N-terminal domains of both CD2 and CD4 have shorter CC′ loops than that of msCEACAM1a[1,4] and REI. Although the CC′ loops of D1 of REI and msCEACAM1a[l,4] are the same length, that of REI is only slightly curved, while the CC′ loop of msCEACAM1a[1,4] remarkably folds back onto the CFG face.

[0089] The convoluted conformation of the CC′ loop in D1 of msCEACAM1a[1,4] is unique among IgSF molecules. The loop, from Lys35 to Glu44, is well structured (FIG. 2B) and probably maintained in a rigid conformation. Within the C terminal portion of the loop (residues 40 to 44), two mainchain hydrogen bonds form one and a half turns of a 310 helix. On the N-terminus of the CC′ loop, Thr38 forms a hydrogen bond with the carbonyl oxygen of Lys35. The mid portion of the CC′ loop makes close contact with the CFG face in two ways (FIG. 2B). Particularly interesting is the packing of two consecutive planar peptide groups on the loop, Thr39-Ala40 and Ala40-Ile41, against the aromatic ring of Tyr34 on the C strand. In addition, a bidentate hydrogen bond from the side-chain of Glu44 to side-chains of this Tyr34 and Arg47 helps to hold the aromatic ring in place for its interactions with the peptide groups. An additional hydrogen bond between the sidechains of Thr39 and Arg96 would also hold the CC′ loop toward the β sheet. Although a tyrosine equivalent to Tyr34 is conserved in the variable domains of most antibody light chains, nevertheless the CC′ loop in antibodies assumes a β hairpin structure (see REI in FIG. 2A) probably because the conserved Pro-Gly sequence motif of antibodies (FIG. 2A) favors a sharp turn at the tip of the loop. This might prevent the CC′ loop of REI from assuming a convoluted conformation like that seen in D1 of msCEACAM1a[1,4].

[0090] In D1 of msCEACAM1a[1,4], the consequence of the folding back of the highly structured CC′ loop against the CFG face is to cause the sidechain of Ile41 at the center of the loop to be prominently exposed, pointing away from the membrane (FIGS. 1 and 2A). Mutational evidence suggests that the Thr38-Thr39-Ala40O-Ile41 sequence motif in murine CEACAM1a[1,4] is important for binding to the MHV spike glycoprotein (Wessner et al., 1998). Two glycans, one at Asn37 and the other at Asn55, flank this important virus-binding motif (FIGS. 1 and 2B), which might help delineate the region for viral spike glycoprotein docking. Based on the structural data presented here, Ile41 is considered to be the energetic “hot spot” for binding to the MHV spike. A widely accepted model for the interaction of cell surface receptors with their ligands is that a central hydrophobic contact provides the major binding energy, while surrounding hydrophilic interactions contribute the specificity of binding (Clackson and Wells, 1995). This also appears to be the case for receptor/virus interactions as shown for binding of gp120 glycoprotein of HIV-1 to CD4 (Kwong et al., 1998). FIGS. 2B and 2C show a view looking from above down upon the CFG face of D1 of msCEACAM1a[1,4] which is likely to be the surface accessible to the MHV virus spike protein. The protruding hydrophobic Ile41 is surrounded by a number of surface-exposed charged residues, including Asp42, Glu44, Arg47, Asp89, Glu93, and Arg97. Ile41 might insert into a hypothetical hydrophobic pocket in the viral spike glycoprotein, and charged residues that surround the pocket could stabilize the MHV binding interaction and contribute to virus binding specificity. No structures are yet available for any coronavirus spike glycoproteins. Strains of MHV that differ in virulence and tissue tropism show considerable variation in the amino acid sequences of their S glycoproteins, yet all MHV strains tested can use murine CEACAM1a as a receptor. The observation that there is no single anti-S MAb that blocks infection by all strains of MHV (Talbot and Buchmeier, 1985) supports the idea that murine CEACAM1a may bind to a conserved pocket in S that is not accessible to antibody. The protruding Ile41 and the charged residues that surround it on the surface of the virus receptor are targets for further mutational analyses.

[0091] Cell adhesion molecules might be particularly suitable candidates for virus binding because their physiologic ligand/receptor binding affinities are very low, and adhesion is an avidity driven process. Uniquely exposed surface features of the cell adhesion molecules are selected for virus binding. FIG. 3 compares the virus-binding domain of msCEACAM1a[1,4] with those of several other virus receptors with the key virus-binding elements highlighted. The projecting Ile41 on the unique CC′ loop of D1 of msCEACAM1a[1,4] is the key topological feature for MHV binding. In CD4, the key HIV gp 120-binding Phe43 is located at the protruding ridge-like C′C″ corner of D1 (Wang et al., 1990). This structural element inserts into a recess in the surface of HIV gp 120 (Kwong et al., 1998). Compared to most IgSF members, ICAM-1, the receptor for the major group of rhinoviruses, has a uniquely tapering tip that inserts into the narrow “canyon” on the rhinovirus surface where the conserved receptor-binding epitopes lie hidden from immune recognition (Kolatkar et al., 1999). The measles virus receptor CD46 belongs to the complement control protein (CCP) superfamily. The center of the virus-binding epitope of CD46 is a well-structured, protruding DD′ loop consisting of a small group of hydrophobic residues with the key Pro39 extending furthest out (FIG. 3) (Casasnovas et al., 1999). Thus, uniquely protruding hydrophobic residues on cell adhesion molecules might be prime targets for virus binding.

EXAMPLE 6

MHV receptor activities of murine CEACAM isoforms, chimeras and mutants

[0092] The various natural isoforms of the murine CEACAM1a, CEACAM1b and CEACAM2 glycoproteins differ markedly in their virus binding, neutralization and virus receptor activities (Dveksler et al., 1993a; Gallagher, 1997; Ohtsuka et al., 1996; Zelus et al., 1998). A series of soluble or anchored mutant murine CEACAM proteins with various point mutations, deletions, or domain exchanges with other CEA-related glycoproteins has been tested for virus binding and receptor activities (Rao et al., 1997; Wessner et al., 1998). Several observations were made. MHV-A59 and soluble spike protein bound better to D1 of murine CEACAM1a from MHV susceptible mice than to CEACAM1b from MHV-resistant mice. Soluble murine CEACAM1b[1-4] had 4 to 10 fold less virus neutralization activity for MHV-A59 than msCEACAM1a[1-4]. The msCEACAM1b[1-4] failed to neutralize the neurotropic JHM strain of MHV, and msCEACAM1b[1,4] failed to neutralize either MHV-A59 or MHV-JHM(Zelus et al., 1998). While the naturally occurring 2 domain CEACAM1a[1,4] isoform neutralized MHV-A59 nearly as well as the 4 domain isoform CEACAM1a[1-4], a carboxyl terminal deletion protein consisting of D1 and D2 (CEACAM1a[1,2]) had only minimal MHV-A59-neutralizing activity. Thus, there is virus strain specificity in the interactions of MHV with various CEACAM1 proteins, and regions of CEACAM1 outside of the virus-binding domain (D1) can affect virus-receptor activity.

[0093] The amino acid sequences of murine CEACAM1a and CEACAM1b differ, principally in the N-terminal, virus-binding domain (Dveksler et al., 1993a). The lengths of the 1a and 1b proteins are the same, and all of the structurally important residues are the same or similar. The overall folding of murine CEACAM1b isoforms is therefore believed to be the same as or similar to that of the corresponding CEACAM1a isoforms. FIG. 4A (upper panel) shows the sequence alignment of D1 from murine CEACAM1a and CEACAM1b with β strands underlined. The most extensive differences between CEACAM1a and 1b are in the peptide segment from the virus-binding CC′ loop to the end of the C″ strand. In D1 of CEACAM1b, residue Ile41 is replaced by a threonine, which may account for its low virus binding activity relative to CEACAM1a.

[0094] Without the important Ile41, the question explored was why can murine CEACAM1b[1-4] serve as an MHV receptor. Comparison of the sequences in the CC′ loop region of D1 of CEACAM1a and 1b (FIG. 4A, upper panel) reveals two differences worthy of particular attention. Both Ile41 (Thr41 in CEACAM1b) and Thr39 (Val in CEACAM1b) are prominently exposed in the CC′ loop (FIG. 2B). In CEACAM1b, Pro38 replaces Thr38 of CEACAM1a and may change the conformation of the CC′ loop in CEACAM1b so that the projecting Val39 might serve as a virus-binding hotspot as Ile41 does for CEACAM1a, though to a lesser extent. Moreover, CEACAM1b lacks the glycosylation site at Asn37 of CEACAM1a due to the replacement of the N37TT sequence motif in CEACAM1a with N37PV. These differences in amino acid sequence and glycosylation probably also affect how spike proteins from various MHV strains dock on the different CEACAM receptor proteins, resulting in differences in receptor utilization, tissue tropism and virulence among the virus strains.

[0095] The carboxy-terminal deletion mutant msCEACAM1a[1,2] has very little virus neutralization activity, while the soluble form of the naturally occurring murine CEACAM1a[1,4] isoform neutralizes virus as well as the msCEACAM1a[1-4] isoform (Zelus et al., 1998). Analysis of the sequence alignment of domains 2 (D2) and 4 (D4) of CEACAM1 a reveals two major differences (FIG. 4B, upper panel). The BC loop of D2 is two residues longer than that of D4, and D2 has four more potential N-glycosylation sites than D4 (marked with * in FIG. 4B). The longer BC loop of D2 and the possible glycan attached to Asn192 at the beginning of the G strand of D2 may both restrict inter-domain flexibility between D1 and D2 in msCEACAM1a[1,2] in comparison to the junction between D1 and D4 in msCEACAM1a[1,4]. Moreover, the present invention model building suggests that there is a hydrogen bond between His 107 of D1 and Asn141 of D2, while no such hydrogen bond is possible at this site in the junction of D1 and D4. All of these structural differences could cause the D1-D2 junction to be less flexible than the highly flexible junction between D1 and D4 revealed by X-ray crystallography. In CEACAM1a[1,2] on the cell membrane, the limited flexibility at the D1-D2 junction might make it more difficult for a virus to attach. The four domain isoform CEACAM1a[1-4] has two more interdomain junctions than the truncated CEACAM1a[1,2] protein, and may therefore be more flexible.

EXAMPLE 7

Predicted Structures of CEA Family Members and Conservation of Glycan-Shielded Surface Hydrophobic Patch in the N-terminal Domain

[0096] CEA family members are all composed of several Ig-like domains in tandem. Following the N-terminal domain, two similar types of domains, called A and B, alternate along the chain. For example, CEA (CD66e), encoded by the CEACAM5 gene, has the N-A1-B1-A2-B2-A3-B3 domain structure (Hammarstrom, 1999).

[0097] Blast search (http://www.ncbi.nlm.nih.gov/BLAST/) of D1 of murine CEACAM1a found sequences of N-terminal domains of all mammalian CEA members. Five residues appear to be absolutely conserved: Trp33, Arg64, Leu73, Asp82 and Tyr86 (FIG. 4A, lower panel). No significant deletions or insertions were found in D1 of human CEA-related proteins, except for a few cases in which the length of the C′C″ loop varied slightly. Like D1 of murine CEACAM1a, the N-terminal domains of all members of the CEA family shown in FIG. 4A can be classified as V set Ig-like fold (Bates et al., 1992). This is determined by these key conserved structural features (Chothia et al., 1998): Pro8 at the A-A′ kink point; Trp33 on the C strand that acts as the center of a hydrophobic core; a salt bridge between Arg64 and Asp82; and the tyrosine-corner motif (Hemmingsen et al., 1994) D*G*Y86 at the beginning of the F strand.

[0098] One of the newly recognized, highly conserved structural features of msCEACAM1a[1,4] that appears to be unique to CEA family members (listed in FIG. 4A) is the glycosylation site at Asn70, on the opposite side of D1 from the proposed virus-binding surface (FIG. 1). In the crystal structure of msCEACAM1a[1,4], the glycan at Asn70 is better ordered than other glycans. Beneath the presumably large glycan at Asn7O lies a group of hydrophobic residues, including Val7 and Pro8 of the A strand, Leu18 and Leu20 of the B strand, Leu74 of the E strand, and probably also Tyr68 and Ile66 of the D strand. The area covers about 650 Å2. The glycan at Asn70 appears to stabilize the protein by preventing the exposure of this large surface hydrophobic patch. Most of these protected amino acid residues are either invariant (Pro8 and Leu18) or very conserved (Leu20, Tyr68 and Leu74) among CEA proteins (FIG. 4A). This is the first example of a three-dimensional structure consisting of a large, glycan-shielded surface hydrophobic patch that is conserved in a protein family. This structural feature is believed to have biological significance in the CEA family.

[0099] To assess the pattern of sequence conservation for all members of the mammalian CEA family in the SWISSPROT database, the variability in sequence using Shannon's entropy (Stewart et al., 1997) was calculated. FIG. 5 shows a topology diagram of D1 of msCEACAM1a[1,4] coded to indicate the relative degree of conservation of residues calculated for 42 CEA family members. A striking difference was discovered in the extent of amino acid conservation between the two faces of D1 among CEA family members. The ABED face containing the glycan-shielded hydrophobic patch is much more conserved than the CFG face. The CFG faces of the N-terminal domains of IgSF proteins are frequently used for cell surface recognition (Stuart and Jones, 1995; Wang and Springer, 1998). The variability in this face among CEA members is considered to be used for binding specificities.

[0100] In the lower panel of FIG. 4B, the sequences of the six A and B type domains of the human CEA protein are aligned with D2 and D4 of murine CEACAM1a. The three A type domains of human CEA, and probably the A domains of other CEA members as well, are structurally very homologous to D4 of murine CEACAM1a, an II set of Ig-fold. The B type domains of human CEA appear to have no D strand, but probably a C′ strand that directly connects to the E strand, as observed for 12 set of Ig-fold (Wang and Springer, 1998). Both I1 and I2 sets differ from the C set by having the A-A′ kink, and they are distinct from the V set in not having the C″ strand (Wang and Springer, 1998). In summary, data suggest that the general architecture of all CEA family members consists of a V set N-terminal domain followed by alternating I1and I2 set Ig-like domains.

EXAMPLE 8

The CC′ and FG Loops of the N-terminal Domains of Various CEA Family Members Play a Role in the Mediation of Biologically Important Molecular Interactions

[0101] The structure of murine CEACAM1a can be used to elucidate other molecular interactions of CEA family members including bacterial binding, immunomodulation, and homophilic and heterophilic adhesion.

[0102] Certain human CEA family members are subverted as receptors for bacterial pathogens including Hemophilus influenzae, Neisseria meningitidis and Neisseria gonorrhoeae. The N-terminal domains of many human CEA members are recognized by multiple Opa (opacity-associated) proteins on the surface of pathogenic strains of Neisseria (Bos et al., 1999; Virji et al., 1999). Homologue scanning mutagenesis revealed that Phe29, Ser32 and Gly4l (and to a lesser extent Gln44) of CEA (CD66e) are required for maximal Opa protein binding activity (Bos et al., 1999). Tyr34 and Ile91 (and to a lesser extent Val39 and Gln89) of human CEACAM1 (CD66a) are critical residues for most Opa protein interactions (Virji et al., 1999). Since the N-terminal domains of CEA and human CEACAM1 are the same length as that of murine CEACAM1 a (FIG. 4A), FIG. 2B was used to show that the Neisseria-binding residues on CEA and human CEACAM1 are on the C strand through the CC′ loop and on the F strand. Val39 and Gly41 of human CEACAM1 and CEA, respectively (corresponding to Thr39 and Ile41 in msCEACAM1a[1,4], FIG. 2B) are on the tip of the CC′ loop. If the CC′ loops of CEA and CEACAM1 were as flat as that of the Bence-Jones protein REI (FIG. 2A), then Val39 and Gly41 would not be close enough to other important Opa-binding residues to form an integrated binding site. This may explain why the Y34A mutation of human CEACAM1 abrogated binding of the majority of Opa proteins (Virji et al., 1999), since the aromatic ring of this conserved Tyr34 is the key to maintaining the convoluted structure of the CC′ loop as shown for msCEACAM1a[1,4]. Thus, the CC′ loops of CEA and human CEACAM1 probably assume a convoluted conformation like that of msCEACAM1a[1,4]. The second point is that the area around Phe29 of CEA and Ile91 of human CEACAM1 (corresponding to Gly29 and Thr91 in msCEACAM1a[1,4], FIG. 2B) is highly hydrophobic and might be an important determinant of binding energy. Knowing the structure of msCEACAM1a[1,4] makes it possible to rationally design mutations to elucidate the molecular basis of the specific interactions between bacterial Opa proteins and CEA members on human cell membranes. Based on the CEACAM1 structure, it is possible to design small molecules that can interfere with binding of ligands to the biologically important CC′ loop of CEACAM1 or related CEA family members.

EXAMPLE 9

Molecular Mechanism of PSG's Function in Pregnancy

[0103] The pregnancy-specific glycoprotein (PSG) subfamily of the CEA family appears to be essential for a successful pregnancy, although the functions of PSGs are not yet fully understood. PSGs may attenuate the mother's immune response to her semi-allogeneic fetus (Hammarstrom, 1999). The N-terminal domains of most human PSGs, but not baboon or rodent PSGs, contain an Arg-Gly-Asp (RGD) motif. The RGD motif is known to be associated with integrin binding and mediates a wide variety of cell adhesion events. For example, in human fibronectin (FN), an integrin-binding RGD motif is located on a type I′ turn at the tip of a protruded FG loop of the 10th FN domain (Leahy et al., 1996). FIG. 4A shows that in D1 of the human PSGs the RGD motifs are aligned at the very tip of the FG loop (highlighted in violet in FIG. 1). The corresponding sequence in msCEACAM1a[1,4] is Glu92-Asn93-Tyr94 (FIG. 4A), which assumes a type II β turn. Those PSG proteins with an RGD motif can slightly change the conformation at the tip of the FG loop to adopt a type II′ turn more suitable for integrin binding. The heterophilic binding of soluble PSGs to integrins might cause local immunosuppression in the uterus by shielding the integrins on cell membranes (Hammarstrom, 1999). In other species, PSGs lacking the RGD motif may still use one acidic residue (Glu or Asp) in the protruding FG loop (Zhou and Hammarstrom, 2001) to bind integrin, as demonstrated for leukocyte integrin ligands (Wang and Springer, 1998) and E-cadherin (Taraszka et al., 2000).

[0104] Knowing the molecular mechanism of PSG's function will be used in drug design for pregnancy-associated problems.

EXAMPLE 10

The CC′ Loop of Domain 1 of CEACAM1 May Also Mediate Homophilic Cell Adhesion

[0105] CEA family members can mediate intercellular adhesion in vitro and in vivo through binding interactions that involve the N-terminal domain (Hammarstrom, 1999). Mutational analyses of the N-terminal domain (D1) of human CEACAM1 and CEA showed that residues on the CFG face, and especially residues on the CC′ loop of D1 are directly engaged in homophilic cell adhesion. Mutations V39A and D40A in the CC′ loop abolished homophilic adhesion of human CEACAM1.

[0106] To study mechanisms for homophilic binding of msCEACAM1a[1,4], the molecular interactions observed in the crystal lattice of msCEACAM1a[1,4] were examined. Two major contact areas between symmetry-related molecules were found, one through D1 by a 2-fold axis, and the other through D4 by a 3-fold axis. The D1 -D1 contact seems most interesting. FIG. 6 shows how the CC′ and FG loops in D1 s of two dyad-related molecules made contact in the crystal structure of msCEACAM1a[1,4]. Hydrophilic interactions appear to dominate the adhesive interface, like that between CD2 and CD58 (Wang et al., 1999). However, the D1-D1 contact seen in FIG. 6 is quite different from the anti-parallel “hand-shaking” mode of CD2/CD58 interactions via their relatively flat CFG faces. For several reasons, the more “parallel” mode of homophilic D1-D1 contact seen between msCEACAM1a proteins are considered by the present inventors to be of physiological significance. First, as discussed above, the uniquely convoluted conformation of the CC′ loop of msCEACAM1a[1,4] is likely to be similar for human CEA members. The fact that Y34A, but not Y34F, mutation abrogated homophilic adhesion of CEA (Taheri et al., 2000) shows the importance of the hydrophobic aromatic ring for maintaining the structure of the convoluted CC′ loop. A convoluted, protruding CC′ loop would likely prevent CEA molecules from adopting the “hand-shaking” type of adhesion seen between CD2 and CD58. FIG. 6B shows that Val39 of one human CEACAM1 molecule (corresponding to Thr39 in msCEACAM1a[1,4]) might have hydrophobic contact with Val39 from its symmetry-mate, while Asp40 of CEA (corresponding to Ala40 of msCEACAM1a[1,4], FIG. 6B) might potentially form a salt bridge with Arg38 from the symmetry-mate. This may explain why mutations V39A and D40A in CEACAM1 disrupt homophilic cell adhesion.

[0107] The “parallel” mode of adhesion could occur between molecules on the same cell or opposing cells. The numerous inter-domain junctions of long CEA members may render them flexible enough to permit a trans-interaction between opposing cells using this “parallel” mode. CHO cells transfected with human CEACAM1-1s, which has only the D1 domain as its extra-cellular portion, showed negligible adhesion despite a high level of protein. Not enough flexibility in this short molecule prohibited this “parallel” mode of binding. Further crystallographic studies and mutational analysis are needed to characterize cis- or trans-adhesion mechanisms between CEA family members.

EXAMPLE 11

Extrapolating the Murine CEACAM1 Structure Onto Human Homologues Using Molecular Modelling

[0108] The X-ray structure of msCEACAM1a[1,4] can be used as a template for the reconstruction of the three-dimensional structure of human homologues of the CEA family. The sequence homology between mouse CEACAM1a[ 1,4] and its homologues is high. For example, the sequence identity of the N-terminal domains (D1) between msCEACAM1a and human CEACAM1 is greater than 30%, which allows building of models of human CEA family members as benchmarks for structure based drug design. In addition, the molecular architecture of the murine and human homologues is highly similar. Most human homologues have a similar number of residues, especially in D1, in which the ABDE beta sheet is highly conserved. Like msCEACAM[1,4], of all human homologues D1 lack a disulfide bridge typical for most Ig domains, and the murine and human homologues share a salt bridge that keeps the two beta sheets together.

[0109] The models of the two N-terminal domains of human homologues (CEACAM1, CEACAM5 and CEACAM6) were constructed through substitution of the residues in the msCEACAM[1,4] structure by their counterparts found in the respective human sequence. The resulting model is subjected to energy minimization to improve the atomic contacts and obtain a chemically sensible model. The homology modelling can be done with programs such as Modeller (A. Fiser, R. K. Do & A. Sali Protein Science 9. 1753-1773, 2000).

EXAMPLE 12

Monoclonal Antibody Mapping of CEA Molecules

[0110] With the structure of msCEACAM1a[1,4] available, and given the high degree of sequence and structure homology between D1 of mouse CEACAM1a and human CEA family members, a model of the first two domains (N-A1) of human CEA (gene product of CEACAM5) and NCA was constructed by simply making amino acid replacements on msCEACAM1a[1,4] for CEA. Since sequences of CEA and CEACAM6 are 90% and 84% identical in their N-terminal domain and A and B type domains (Hefta, et al.), the model could also be used for human CEACAM1 (BGP) and CEACAM6 (NCA) with minor changes. GOLD Mabs are known to have their epitopes on protein, but not on carbohydrates (Hammarstrom, et al., (1989). Glycosylation sites on CEA and CEACAM6 were used to delineate the possible epitope area, by assuming that residues located within 6A from the glycosylation sites are excluded from access by any antibody. FIG. 7 is the surface representation of the model, in which the glycan-protected areas for CEA is a cross-hatched area, labeled (I). The area shielded by glycans on CEACAM6 but not on CEA is labeled (II). The white areas are exposed and they contain the potential Mabs epitopes that recognize both CEA and CEACAM 6. The white areas are exposed and they contain are the potential Mabs epitopes that recognize both CEA and CEACAM6 except for a few residues substitution between these two molecules, which could differ in some cases. The large white area on the N-terminal domain is on the CFG face, on which many of GOLD 5 Mabs bind. These Mabs cross-react with CEACAM6 (Murakami, et al. (1995)). On the Al domain of CEA/CEACAM6, the area labeled (III) contains the large and protruded CD loop whereas the area labeled (IV) contains the A-A′ strands plus part of the G strand. These are likely to be the locations of epitopes of cross-reacting Mabs in the GOLD 4 group, which bind to A1-B1 domains (Murakami, et al., (1995)). The area labeled (II) is most interesting. This is the region spanning the BC and FG loops of domain A1 which is covered by glycans that only exist in CEACAM6. A region like this should be a good candidate to develop CEA-specific Mabs that do not recogize CEACAM6. Further modeling efforts are needed to aid the development of site-specific anti-CEA monoclonal antibodies for future medical use may be created using this modeling approach.

EXAMPLE 13

Drug Screening for Anti-Viral, Anti-Inflammatory and Anti-Cancer Agents

[0111] The present example is provided to demonstrate the utility of the present invention for the selection and screening of a variety of candidate substances for anti-viral, anti-bacterial, anti-inflammatory, immunomodulatory and anti-cancer activity.

[0112] The target control molecule that will be used is the soluble carcinoembryonic antigen (CEACAM1a[1,4]), described herein. The agent that will be used to quantify binding activity of a candidate substance, and against which the relative acceptability of a candidate substance will be determined, will be, by way of example, a monoclonal antibody. One such monoclonal antibody, CC1, antibody to the CC′ loop of mouse CEACAM1a is described in Wessner at al. (1998) which reference is specifically incorporated herein by reference. In general, substances (i.e., a candidate substance) that are capable of a binding specifically to the CC′ loop of mouse CEACAM1 having the unique conformational characteristics identified here with an binding affinity in the range of 104 to 1010 will be selected for use as potentially suitable anti-viral, anti-inflammatory immunomodulatory, and/or anti-cancer agents.

[0113] It should be understood that other monoclonal and polyclonal antibodies, or other types of molecules, that posseses the same or relatively the same binding affinity for the novel structure of the CC′ loop of mouse or human CEACAM1 protein as described here may also be used in the practice of the method for selecting candidate substances suitable for the uses described here.

[0114] It is expected that the disclosed method will be useful in identifying agents that may be used in the treatment and therapy of humans using the identified functional domain of CEACAM1 identified here as the CC′ loop because of the high degree of structural similarity that the present investigators have inferred from mutational data as existing between the sequenced CC′ region of mouse and human CEACAM1a. This region possesses about 10 amino acids in the mouse and the human sequences which are compared below, along with the amino acids that stabilize the uniquely structure of the CC′ loop:

[0115] Mouse CC′ region—-K G N T T A I D K E-(SEQ ID NO: 3)

[0116] Important amino acids that stabilize the structure of the CC′ loop:

[0117] Y34, E44, R47, R96 and possibly D89

[0118] Human CC′ region—-K G E R V D G N RQ-(SEQ ID NO: [2]1)

[0119] Amino acids that likely stabilize the structure of the CC′ loop:

[0120] Y34, Q44, G47, and Q89

[0121] It is envisioned that the unique convoluted structure of this CC′ loop will be used to develop an algorithm that will provide a three-dimensional (3-D) blueprint of structure against which candidate substances can be identified and compared as likely to attach to the functional CC′ loop of D1. This will then be incorporated into a software program wherein the calculation and identification of likely suitable candidate substances can be screened automatically and at a relatively rapid rate. Software programs currently available in the art for the purpose of drug screening and selection may be found at http://www.small-molecule-drug-discovery.com/high_screening.html.

[0122] The identified candidate substances that have binding activity for CEACAM1 as identified here, are also intended as part of the present invention. As a further step, and in some embodiments, the selected candidate substances may then be examined in an in vitro assay, such as for ability to bind CEACAM1 protein. Specificity of binding will be tested by using CEACAM1 proteins from different species, and other related glycoproteins in the CEA family.

[0123] Alternatively, the candidate substance can be tested for the ability to block the binding of a monoclonal antibody such as anti-CEACAM1 Mab-CC1 or the MHV viral spike glycoprotein (S) or a homophilic region of CEACAM1 to the functional domain CC′ of the CEACAM1 protein.

[0124] In yet another approach, the candidate substance may be tested for its ability to block the binding of MHV to mCEACAM1a, or for the ability to block the homophilic interaction of mCEACAM1a.

EXAMPLE 14

Pharmaceutical Preparations for Modulation of Diseases Related to Angiogenesis and Tumor Inhibition and Immune Response

[0125] The molecules of the present invention may be selected to provide a pharmacologically active preparation that will provide interference with aberrant angiogenesis, tumor metastasis inhibition, or other functions such as immunomodulation or virus or bacterial infection (Najajime et al., 2002). Because MAb-CC1 in the circulation inhibits delayed type hypersensitivity in vivo (and blocks MHV virus binding to CEACAM1 on murine cells), and virus binds by the CC′ loop, the CC′ loop is an important biological molecule needed for delayed type hypersensitivity in vivo. Inhibiting/blocking this loop on D1 may prevent delayed type hypersensitivity or other immune mediated damage. This could be used in allergic reactions, autoimmune disorders etc. The other application for pharmacological uses focuses on the angiogenesis activity of CEACAM1.

EXAMPLE 15

Drug Screening for Anti-Viral, Anti-Inflammatory and Anti-Cancer Agents

[0126] The administration to infant mice by the intranasal and intraperitoneal routes of monoclonal antibody MAb-CC1 (directed toward the CC′ loop of murine CEACAM1a) prevents infection and death of the animals following MHV inoculation (Smith, A. L et al. (1991). Therefore a candidate substance selected according to the present method that is targeted to the CC′ loop of murine CEACAM1a, the receptor for MHV, will be employed to block, prevent or treat MHV infection of mice in vivo.

[0127] After the previous in vitro tests described above have shown that a candidate CEACAM1a targeted substance can specifically block the binding of murine coronavirus MHV or its spike glycoprotein (S) to the CC′ loop in the N-terminal domain of murine CEACAM1a, it will be determined whether the substance is toxic to a variety of murine cells in vitro. If it is not toxic, it then will determine whether it is toxic when administered to mice by the intranasal, intravenous or intra-peritoneal routes at doses in the range of the observed pharmacologic effect in vitro. If the drug candidate is not toxic in vivo, administration of the candidate substance to mice before inoculation with MHV by the intranasal or the intraperitoneal routes, or at different times after the virus inoculation. It will then determine whether the candidate substance will block or reduce virus infection in vivo by measuring viral titer in treated vs. control animals in various target tissues such as liver, intestine and spleen. It will then be determined whether the substance modulates the immune response to viral infection by comparing the anti-viral antibody titers from treated vs. untreated animals, as well as by comparing the virus-specific cell-mediated immune responses from treated vs. untreated animals. Comparison of the histopathology, severity of clinical disease and lethal dose50 in the treated vs. untreated animals will also be conducted.

[0128] These methods of using identified candidate substances are of value in preventing or treating MHV infection of mice. MHV is one of the most devastating infections in laboratory mouse colonies because most inbred mouse strains are highly susceptible to MHV which can modulate their immune responses, and cause serious disease or death (S Compton, S Barthold and AL Smith, Lab. Animal Sci. 43:15-28 (1993). When precious inbred mice become infected with MHV, the colony is sometimes entirely euthanized in order to stop the spread of the virus. The animals have to be re-derived by Ceasarian section and breeding. This causes major economic problems for mouse breeders and university labs that use inbred mouse strains. Sometimes 40,000 mice are destroyed to stop the spread of MHV in a single colony. Thus a preventive or therapeutic agent for these kinds of murine dieseases and infecttions are of great potential value in lab animal husbandry.

EXAMPLE 16

Model Coordinates for CEACAM1a Angiten

[0129] Attached are the coordinates for human CEACAM1, CEACAM5 and CEACAM6 obtained through homology modeling based on the msCEACAM1a[1,4] structure and the respective human sequences. Each model consists of the N and the A1 domain. Further modeling of other human homologues could be done by the person of ordinary skill provided the disclosure of the present invention identifying the crystal structure of the CC′ loop of CEACAM and/or msCEACAM1a[1,4].

[0130] The following tables set forth the coordinates (X,Y and Z) of the particular CEACAM molecule indicated:

[0131] Table 2—Full coordinate set of domains N and Al of human CEACAM6 (homology model) (1574 Atoms, 203 Amino Acids

[0132] Table 3—Full coordinate set of domains N and Al of human CEACAM 5 (homology model)(1606 atoms, 203 amino acids)

[0133] Table 4—Full coordinate set of domains N and Al of human CEACAM1 (homology model) (1587 atoms, 203 amino acids)

[0134] Table 5—Full coordinate set of D1 of human CEACAM1a (homolology model)

[0135] Table 6—Full coordinate set of D1 D4 of murine CEACAM1a

[0136] Table 7—Coordinate set of CC′ loop of D1 of murine CEACAM1a (partial sequence of #5, corresponding to amino acid positions 35 through 45 (atoms positions 264 through 343)

5TABLE 2Full coordinate of domains N and A1 of human CEACAM6(homology model) 1574 Atoms, 203 amino acids)ANumATypeRTypeRNumXYZ1NLYS17.62028.81940.4442CALYS17.90527.38740.2503CBLYS16.95126.55341.1044CGLYS15.91527.46941.7475CDLYS14.70326.77242.3656CELYS13.49127.69842.5027NZLYS12.28826.93842.9098CLYS17.72526.99438.8359OLYS16.81926.22938.51610NLEU28.63927.50237.98411CALEU29.10326.82736.81012CBLEU210.06625.69637.21413CGLEU210.66724.87736.06214CD2LEU210.89623.42036.49515CD1LEU211.93725.54635.51416CLEU27.95126.25336.03217OLEU27.69425.05136.09118NTHR37.23327.08835.25419CATHR36.43726.47834.23720CBTHR34.96326.34334.53321OG1THR34.43327.56435.01622CG2THR34.76825.22835.56423CTHR36.48027.29333.00424OTHR37.52227.69032.47925NILE45.26227.47832.49626CAILE44.92827.36131.12927CBILE43.44127.07331.07028CG2ILE42.83727.65432.36129CG1ILE42.73227.53529.78830CD1ILE41.21727.55129.96631CILE45.32528.63430.47732OILE45.76129.58631.11933NGLU55.22828.66829.15334CAGLU55.42229.89728.48535CBGLU56.81230.02127.84236CGGLU57.15431.45727.46637CDGLU58.43131.40326.65838OE1GLU59.23630.45426.85539OE2GLU58.62032.33625.83540CGLU54.41729.85627.40741OGLU53.65128.89827.28742NSER64.38730.89126.56943CASER63.76530.54825.34644CBSER62.22230.41125.42045OGSER61.52831.43824.73146CSER64.24731.49324.32047OSER64.67032.61224.61148NTHR74.28730.98123.07949CATHR75.04231.58422.02850CBTHR76.32530.83521.85451OG1THR76.02629.59821.21552CG2THR76.95230.53423.23753CTHR74.22931.40420.76354OTHR73.46330.44620.68055NPRO84.30932.20519.72956CAPRO84.81133.55219.69557CDPRO83.66231.82118.48858CBPRO84.73634.00118.22159CGPRO84.18932.79217.43160CPRO83.95734.43620.55861OPRO82.74434.44720.36362NPHE94.52935.21221.49563CAPHE93.65836.15022.14764CBPHE94.21436.76223.43465CGPHE95.67836.53323.45366CD1PHE96.51337.19822.58367CD2PHE96.19735.63524.35668CE1PHE97.86836.97022.60569CE2PHE97.55035.40724.37770CZPHE98.38236.07223.51071CPHE93.39237.27221.21472OPHE94.25137.67620.43873NASN102.16437.79921.27274CAASN101.66538.66520.26775CBASN102.59539.85119.95776CGASN102.57940.72821.20777OD1ASN103.58040.92421.88978ND2ASN101.36641.23321.54379CASN101.44937.81019.07480OASN102.37437.18718.55581NVAL110.17737.72318.65182CAVAL11−0.18136.73817.68283CBVAL11−0.98635.61818.28684CG1VAL11−0.90134.42117.32885CG2VAL11−0.41435.36919.70286CVAL11−1.04537.41216.67887OVAL11−1.84438.28117.02388NALA12−0.91537.02415.40289CAALA12−1.72737.66514.41690CBALA12−1.01637.84513.07391CALA12−2.91436.80414.17492OALA12−3.04235.72114.73493NGLU13−3.81937.28813.31294CAGLU13−4.96236.52612.92995CBGLU13−6.08337.43412.42096CGGLU13−7.44237.20313.06097CDGLU13−8.45437.73312.07198OE1GLU13−9.35438.49512.51599OE2GLU13−8.32537.38410.869100CGLU13−4.53135.68011.774101OGLU13−3.76036.12210.924102NGLY14−5.02034.42911.705103CAGLY14−4.65333.58210.604104CGLY14−3.28033.04410.868105OGLY14−2.67632.39010.019106NLYS15−2.73533.30412.069107CALYS15−1.45732.72712.349108CBLYS15−0.34933.77212.551109CGLYS15−0.30334.73711.360110CDLYS150.97235.57711.231111CELYS151.88835.13310.090112NZLYS152.89534.19510.623113CLYS15−1.61631.90813.584114OLYS15−2.57432.06714.340115NGLU16−0.67530.96613.788116CAGLU16−0.82130.01114.840117CBGLU16−0.14628.65114.570118CGGLU16−0.83327.77013.527119CDGLU160.05626.56113.285120OE1GLU16−0.48625.42413.251121OE2GLU161.29226.76013.132122CGLU16−0.14830.53416.061123OGLU160.31131.67216.111124NVAL17−0.09529.65817.082125CAVAL170.54729.89518.339126CBVAL17−0.38530.39519.393127CG1VAL170.38430.50120.724128CG2VAL17−1.01931.71018.916129CVAL170.94928.55118.811130OVAL170.30827.55418.485131NLEU182.02428.47519.611132CALEU182.20327.23620.295133CBLEU183.53126.49820.034134CGLEU183.85525.45421.130135CD2LEU185.32325.00221.059136CD1LEU182.88624.26321.131137CLEU182.18427.55421.739138OLEU182.70828.57522.182139NLEU191.57126.67222.528140CALEU191.65926.90723.925141CBLEU190.35326.60224.665142CGLEU19−0.69827.72724.483143CD2LEU19−0.66328.30723.060144CD1LEU19−0.56528.78625.585145CLEU192.75426.02824.411146OLEU192.77224.83224.123147NLEU203.73726.61025.120148CALEU204.89125.84325.475149CBLEU206.19926.63225.257150CGLEU207.43325.83624.781151CD2LEU208.72326.68124.847152CD1LEU207.20125.27623.371153CLEU204.78125.60426.935154OLEU204.64126.55627.698155NALA214.86824.34027.374156CAALA215.12224.17628.767157CBALA214.38522.99529.407158CALA216.56723.87328.824159OALA217.06623.12527.989160NHIS227.30924.44729.775161CAHIS228.66724.03429.806162ND1HIS2210.58726.72428.707163CGHIS229.61026.34029.597164CBHIS229.62825.07030.376165NE2HIS229.07628.34928.739166CD2HIS228.69027.34429.599167CE1HIS2210.21827.93328.227168CHIS228.70122.86730.704169OHIS227.92821.93030.528170NASN239.59522.90031.701171CAASN239.87721.73432.479172CDASN2311.15421.87933.304173CGASN2312.28522.40532.420174OD1ASN2312.17023.41131.719175ND2ASN2313.44821.70532.482176CASN238.75221.54833.435177OASN238.08922.50333.833178NLEU248.51720.28733.839179CALEU247.38119.95834.643180CDLEU247.20020.85235.887181CGLEU248.33220.66636.915182CD2LEU248.99619.29536.739183CD1LEU247.84120.87638.349184CLEU246.16520.08233.793185OLEU245.86621.20133.373186NPRO255.43719.02733.465187CAPRO255.90817.65933.501188CDPRO254.90319.21832.126189CBPRO256.72017.54532.212190CGPRO255.83518.36031.226191CPRO256.50116.97834.707192OPRO256.69117.58035.761193NGLN266.76815.66634.528194CAGLN267.44214.76835.431195CBGLN268.10415.41236.655196CGGLN267.77014.63737.932197CDGLN267.54615.63239.054198OE1GLN268.03915.41940.159199NE2GLN266.78816.73138.780200CGLN266.41913.82435.976201OGLN265.36714.27636.429202NASN276.75812.50235.929203CAASN275.90411.33736.018204CBASN276.41410.18336.902205CGASN276.6208.97635.985206OD1ASN277.6028.24036.069207ND2ASN275.6508.77535.053208CASN274.56011.69836.508209OASN274.22411.51337.677210NARG283.75612.24435.587211CAARG282.43512.62235.934212CBARG281.97713.86335.158213CGARG283.06514.93935.087214CDARG282.88415.91933.928215NEARG282.54217.25534.494216CZARG282.00518.19833.705217NH1ARG281.69919.44434.191218NH2ARG281.76017.92332.373219CARG281.58411.46535.553220OARG282.03910.32235.513221NILE290.30611.71035.253222CAILE29−0.38810.58034.747223CBILE29−1.2609.86735.740224CG2ILE29−2.56410.66035.918225CG1ILE29−1.4938.42835.259226CD1ILE29−2.5987.68936.021227CILE29−1.23311.04333.619228OILE29−1.50110.28132.696229NGLY30−1.67812.31333.644230CAGLY30−2.50912.76232.570231CGLY30−2.73314.22132.737232OGLY30−2.95314.72533.836233NTYR31−2.66714.94431.612234CATYR31−2.86416.35031.711235CBTYR31−1.82117.18630.958236CGTYR31−0.74416.30930.393237CD1TYR31−0.72216.10829.029238CD2TYR310.22215.70031.164239CE1TYR310.23515.33428.438240CE2TYR311.18514.92630.573241CZTYR311.19514.74929.221242OHTYR312.19513.95228.649243CTYR31−4.19816.66231.122244OTYR31−4.86215.78730.572245NSER32−4.62517.93331.248246CASER32−5.79618.45730.608247CBSER32−6.94918.69031.606248OGSER32−8.02519.37530.976249CSER32−5.39019.81430.131250OSER32−4.55820.47230.751251NTRP33−5.95220.28029.007252CATRP33−5.71321.65028.668253CBTRP33−5.15621.87427.250254CGTRP33−3.70122.23927.275255CD2TRP33−3.20523.53527.632256CD1TRP33−2.61221.45827.047257NE1TRP33−1.46422.17327.279258CE2TRP33−1.81223.45627.637259CE3TRP33−3.86124.69027.954260CZ2TRP33−1.04624.53027.962261CZ3TRP33−3.08525.77628.266262CH2TRP33−1.71125.70128.274263CTRP33−7.03522.32528.707264OTRP33−8.02421.77928.223265NTYR34−7.09623.52529.302266CATYR34−8.37924.12229.478267CBTYR34−8.70624.40730.947268CGTYR34−9.26223.14131.506269CD1TYR34−8.70422.57732.634270CD2TYR34−10.33122.52430.900271CE1TYR34−9.21921.41233.151272CE2TYR34−10.84621.35331.425273CZTYR34−10.28320.79632.548274OHTYR34−10.80519.59633.086275CTYR34−8.39525.41028.743276OTYR34−7.66125.59227.768277NLYS35−9.27826.32129.190278CALYS35−9.40527.60328.578279CBLYS35−10.08827.55327.203280CGLYS35−10.51428.92926.699281CDLYS35−11.81628.93225.895282CELYS35−12.40630.32925.767283NZLYS35−12.29830.80624.369284CLYS35−10.32828.38429.445285OLYS35−11.49328.02129.592286NGLY36−9.84129.50330.012287CAGLY36−10.74630.46830.573288CGLY36−10.68430.40532.066289OGLY36−11.57530.89832.753290NGLU37−9.61129.81132.614291CAGLU37−9.39229.82334.032292CBGLU37−9.64931.20234.685293CGGLU37−9.45331.23036.206294CDGLU37−9.91432.59336.684295OE1GLU37−9.79832.88137.905296OE2GLU37−10.39033.36635.814297CGLU37−10.28528.82034.684298OGLU37−9.83428.04135.522299NARG38−11.57928.82534.327300CAARG38−12.54227.99534.986301CBARG38−13.91528.09134.316302CGARG38−14.95627.13434.870303CDARG38−16.26527.22434.094304NEARG38−17.32127.67635.055305CZARG38−18.63427.65634.660306NH1ARG38−19.63227.77835.587307NH2ARG38−18.92827.45933.349308CARG38−12.07226.58134.921309OARG38−11.72326.08933.852310NVAL39−11.99525.91136.090311CAVAL39−11.35624.62936.203312CBVAL39−10.62024.53337.522313CG1VAL39−9.86823.20137.613314CG2VAL39−9.68125.74437.595315CVAL39−12.41823.55736.100316OVAL39−12.42122.57336.838317NASP40−13.34523.74235.142318CAASP40−14.33122.74634.831319CBASP40−15.71823.34134.488320CGASP40−16.83522.72935.328321OD1ASP40−18.01323.02134.994322OD2ASP40−16.53321.98536.299323CASP40−13.84022.06533.587324OASP40−12.97822.58732.877325NGLY41−14.38920.86533.306326CAGLY41−14.07620.14032.112327CGLY41−15.27420.25531.244328OGLY41−15.42419.53130.261329NASN42−16.13721.20931.627330CAASN42−17.18221.79430.845331CBASN42−17.67723.04931.598332CGASN42−18.75723.86330.898333OD1ASN42−18.94323.83529.684334ND2ASN42−19.50524.63331.732335CASN42−16.53322.18329.551336OASN42−16.92021.74528.469337NSER43−15.47823.00629.621338CASER43−14.70223.20328.442339CBSER43−14.12924.60828.322340OGSER43−13.38124.69727.115341CSER43−13.53722.29228.564342OSER43−12.40422.75028.704343NLEU44−13.78520.96828.533344CALEU44−12.66620.08528.500345CBLEU44−12.92418.63328.926346CGLEU44−11.58817.87229.023347CD2LEU44−11.71416.62029.910348CD1LEU44−10.46118.83929.421349CLEU44−12.18820.04827.099350OLEU44−12.89819.63726.180351NILE45−10.94620.52026.926352CAILE45−10.30720.50625.659353CBILE45−9.27221.59125.542354CG2ILE45−8.70721.59424.110355CG1ILE45−9.90022.92325.974356CD1ILE45−9.46124.12925.140357CILE45−9.65219.16725.549358OILE45−10.25718.22525.044359NVAL46−8.40119.04126.031360CAVAL46−7.60717.91125.638361CBVAL46−6.24218.30925.163362CG1VAL46−5.74217.27724.133363CG2VAL46−6.37019.73224.586364CVAL46−7.43316.98226.792365OVAL46−8.17417.03727.774366NGLY47−6.44316.07326.678367CAGLY47−6.26615.06727.678368CGLY47−5.20114.13727.197369OGLY47−5.41412.93227.052370NTYR48−3.99514.68026.964371CATYR48−2.92813.78026.685372CBTYR48−1.61114.47926.283373CGTYR48−0.70013.37525.888374CD1TYR480.16612.82826.803375CD2TYR48−0.73712.88724.604376CE1TYR480.99711.79426.429377CE2TYR480.08611.85724.219378CZTYR480.94911.31525.140379OHTYR481.79410.25424.743380CTYR48−2.73612.98827.931381OTYR48−2.44313.53528.991382NVAL49−2.94311.67227.806383CAVAL49−2.93710.71028.867384CBVAL49−3.9539.67028.471385CG1VAL49−3.7878.37729.262386CG2VAL49−5.35310.28528.586387CVAL49−1.54310.12728.935388OVAL49−1.0299.63727.929389NILE50−0.86310.18230.110390CAILE500.4649.61030.109391CBILE501.51310.30630.962392CG2ILE501.5849.63532.349393CG1ILE502.85910.34630.197394CD1ILE504.04510.80731.038395CILE500.3408.20730.603396OILE50−0.5397.91031.413397NGLY511.2187.31130.112398CAGLY511.1685.91630.442399CGLY510.9725.17929.156400OGLY511.5755.49428.120401NTHR520.0714.17429.216402CATHR52−0.6303.86128.018403CBTHR52−1.8853.09728.226404OG1THR52−2.9033.63127.382405CG2THR52−2.3023.20929.699406CTHR52−1.0265.18427.504407OTHR52−1.6525.98228.195408NGLN53−0.5435.48726.299409CAGLN53−0.6666.82625.861410CBGLN530.4657.27824.938411CGGLN531.8297.23025.619412CDGLN532.8777.42824.527413OE1GLN534.0717.42324.817414NE2GLN532.4157.63123.269415CGLN53−1.9116.90125.071416OGLN53−2.6755.93924.953417NGLN54−2.1268.09924.524418CAGLN54−3.3228.38123.827419CBGLN54−4.5817.86924.548420CGGLN54−5.8037.54523.681421CDGLN54−6.7636.79524.602422OE1GLN54−7.8696.44024.191423NE2GLN54−6.3176.52525.855424CGLN54−3.3859.84723.867425OGLN54−2.38310.54424.018426NALA55−4.61110.32023.732427CAALA55−4.96411.67823.836428CBALA55−4.29912.58922.795429CALA55−6.38111.54723.491430OALA55−6.80810.51722.966431NTHR56−7.16612.54823.867432CATHR56−8.52512.19624.021433CBTHR56−8.68011.12725.065434OG1THR56−10.04810.86825.330435CG2THR56−7.94911.56326.341436CTHR56−9.12913.43824.512437OTHR56−8.43314.25725.105438NPRO57−10.38613.61724.283439CAPRO57−10.84014.94824.446440CDPRO57−10.90613.10823.022441CBPRO57−10.75315.55823.064442CGPRO57−10.92514.35322.102443CPRO57−12.27714.75424.709444OPRO57−12.69013.66425.104445NGLY58−13.04415.78924.354446CAGLY58−14.41715.61824.081447CGLY58−14.98216.96323.754448OGLY58−15.12717.36522.609449NPRO59−15.35517.61024.822450CAPRO59−16.53418.43824.829451CDPRO59−14.98217.10826.133452CBPRO59−16.90218.64126.295453CGPRO59−15.97217.70127.113454CPRO59−16.38419.73024.072455OPRO59−17.35120.48823.955456NALA60−15.17420.05323.589457CAALA60−14.94821.44023.352458CBALA60−13.95622.04224.364459CALA60−14.37621.60021.978460OALA60−14.20820.62821.243461NTYR61−14.08422.85821.589462CATYR61−13.61023.12820.271463CBTYR61−13.22624.60220.021464CGTYR61−14.08125.27118.987465CD1TYR61−15.32624.79218.644466CD2TYR61−13.63326.40518.341467CE1TYR61−16.09125.44217.697468CE2TYR61−14.39827.05117.398469CZTYR61−15.64126.57617.060470OHTYR61−16.42027.24416.084471CTYR61−12.37422.32220.061472OTYR61−11.46622.30220.890473NSER62−12.32221.65618.897474CASER62−11.13221.01118.452475CBSER62−11.33819.53518.129476OGSER62−10.96218.72819.229477CSER62−10.81921.61617.147478OSER62−10.09720.99516.364479NGLY63−11.40322.81416.910480CAGLY63−11.50723.43815.618481CGLY63−10.20123.28514.938482OGLY63−10.11322.65613.879483NARG64−9.14623.79315.599484CAARG64−7.82823.35115.288485CBARG64−7.19724.07714.086486CGARG64−7.96225.33013.656487CDARG64−8.22926.32714.787488NEARG64−9.59026.90114.538489CZARG64−10.20527.66015.488490NH1ARG64−9.54327.97616.636561CD1LEU73−4.10121.90524.208562CLEU73−0.64423.88221.888563OLEU73−0.70325.10022.054564NLEU74−0.54123.32420.666565CALEU74−0.57724.15019.501566CBLEU74−0.27423.37518.201567CGLEU74−0.80824.04216.911568CD2LED74−0.66623.13315.669569CD1LEU74−0.15825.40716.695570CLEU74−1.97224.63319.399571OLEU74−2.90223.92619.782572NILE75−2.15725.86018.887573CAILE75−3.51226.24518.647574CBILE75−4.12827.12819.700575CG2ILE75−3.08928.17520.123576CG1ILE75−5.45627.71619.186577CD1ILE75−6.17328.58720.215578CILE75−3.57726.94117.331579OILE75−2.92427.96117.098580NGLN76−4.37326.34916.421581CAGLN76−4.44626.79815.067582CBGLN76−4.68725.65714.062583CGGLN76−3.91424.38814.388584CDGLN76−4.04423.48313.175585OE1GLN76−5.03923.54112.453586NE2GLN76−3.01122.63412.947587CGLN76−5.61527.70614.935588OGLN76−6.29827.98315.924589NASN77−5.82828.16613.676590CAASN77−6.48829.38713.266591CBASN77−7.43629.20312.072592CGASN77−6.56928.67310.938593OD1ASN77−7.05428.00710.025594ND2ASN77−5.23728.95711.000595CASN77−7.19630.04514.405596OASN77−8.42230.11614.467597NVAL78−6.38430.54015.358598CAVAL78−6.87431.02816.616599CBVAL78−5.75031.51017.501600CG1VAL78−4.73032.26016.638601CG2VAL78−6.32932.34118.654602CVAL78−7.79532.17516.361603OVAL78−8.95232.15216.776604NTHR79−7.28033.20715.664605CATHR79−7.88734.50815.528606CBTHR79−9.10934.60514.652607OG1THR79−10.14033.76815.153608CG2THR79−8.75434.23713.202609CTHR79−8.29935.07716.839610OTHR79−8.04534.51817.903611NGLN80−8.92736.26316.743612CAGLN80−9.27837.11517.839613CBGLN80−9.96638.41617.379614CGGLN80−11.10438.83218.311615CDGLN80−11.89739.95617.666616OE1GLN80−12.97940.25918.160617NE2GLN80−11.36840.58916.585618CGLN80−10.25236.41118.719619OGLN80−10.23936.61719.933620NASN81−11.12735.58318.117621CAASN81−12.18034.96518.867622CBASN81−13.01433.95318.057623CGASN81−14.27834.63617.541624OD1ASN81−15.23633.95717.174625ND2ASN81−14.30335.99917.501626CASN81−11.58534.25720.048627OASN81−12.12834.34321.145628NASP82−10.43933.56719.879629CAASP82−9.92632.75220.948630CBASP82−9.21031.46220.480491NH2ARG64−11.48728.09215.294492CARG64−6.98723.60016.495493OARG64−6.62724.73216.803494NGLU65−6.65722.51317.214495CAGLU65−5.67422.58418.246496CBGLU65−6.21123.12819.585497CGGLU65−6.53724.62419.586498CDGLU65−8.04024.77819.615499OE1GLU65−8.75323.74619.495500OE2GLU65−8.48425.94619.766501CGLU65−5.21721.17618.451502OGLU65−5.93020.23918.103503NTHR66−3.99021.00018.983504CATHR66−3.45719.69619.247505CBTHR66−2.59419.17918.129506OG1THR66−3.33719.17916.925507CG2THR66−2.13417.73818.442508CTHR66−2.59219.83720.464509OTHR66−2.30920.94220.917510NILE67−2.16218.71521.066511CAILE67−1.37718.85222.260512CBILE67−2.03018.25623.485513CG2ILE67−1.76216.74123.470514CG1ILE67−1.52318.97324.744515CD1ILE67−1.64718.10825.988516CILE67−0.08518.12122.033517OILE670.07717.37221.068518NTYR680.89518.35322.922519CATYR682.17517.73322.802520CBTYR683.30518.75922.632521CGTYR683.39118.96321.166522CD1TYR684.36518.32220.436523CD2TYR682.48819.78020.528524CE1TYR684.44318.50219.074525CE2TYR682.55519.97019.174526CZTYR683.53619.33218.451527OHTYR683.61019.52817.056528CTYR682.44316.98924.073529OTYR682.04217.42825.146530NPRO693.11915.87723.982531CAPRO693.37115.07025.143532CDPRO693.12515.10522.753533CBPRO694.10713.84324.610534CGPRO693.62513.69623.148535CPRO694.13715.82426.193536OPRO694.09515.43027.358537NASN704.85916.89625.815538CAASN705.63917.60426.791539CBASN706.89818.29026.230540CGASN706.45219.15725.076541OD1ASN706.23418.67823.961542ND2ASN706.30120.47925.348543CASN704.76818.68227.345544OASN705.19819.47228.186545NALA713.50418.71726.889546CAALA712.50319.60927.386547CBALA712.49919.72528.914548CALA712.69620.95826.773549OALA712.68121.98327.459550NSER722.83420.97625.433551CASER722.62022.15924.653552CBSER723.55322.29323.432553OGSER724.67823.09823.731554CSER721.26222.00024.063555OSER720.85820.87023.809556NLEU730.52423.10523.803557CALEU73−0.68822.94123.047558CBLEU73−1.98623.24323.817559CGLEU73−3.23022.61323.158560CD2LEU73−4.02123.61622.299631CGASP82−10.22830.41120.064632OD1ASP82−10.59029.54620.908633OD2ASP82−10.64630.44318.880634CASP82−8.94733.51121.791635OASP82−8.31432.91522.663636NTHR83−8.78634.82821.561637CATHR83−7.83235.57322.332638CBTHR83−7.82937.04222.008639OG1THR83−6.51037.57022.024640CG2THR83−8.70637.77623.037641CTHR83−8.20435.39823.769642OTHR83−9.33935.03824.069643NGLY84−7.25735.60824.707644CAGLY84−7.62635.51726.094645CGLY84−6.83934.44026.784646OGLY84−5.69934.13726.433647NPHE85−7.46333.86227.832648CAPHE85−6.82532.99328.788649CBPHE85−7.60132.86730.124650CGPHE85−6.64832.46931.200651CD1PHE85−5.34832.91331.193652CD2PHE85−7.07031.68232.257653CE1PHE85−4.47132.53232.196654CE2PHE85−6.19831.29533.255655CZPHE85−4.88931.70033.203656CPHE85−6.77931.60928.260657OPHE85−7.60731.20427.445658NTYR86−5.81730.83028.784659CATYR86−5.92629.39728.775660CBTYR86−5.31428.68127.558661CGTYR86−6.15129.05426.385662CD1TYR86−5.79430.11925.587663CD2TYR86−7.29928.35126.090664CE1TYR86−6.57230.47124.505665CE2TYR86−8.08328.68725.011666CZTYR86−7.71229.75424.220667OHTYR86−8.51830.10723.115668CTYR86−5.17628.91829.958669OTYR86−4.21929.55130.408670NTHR87−5.60427.78030.514671CATHR87−4.89427.33831.666672CBTHR87−5.69727.36032.923673OG1THR87−4.84527.29334.059674CG2THR87−6.61626.12432.911675CTHR87−4.59925.91231.445676OTHR87−4.95525.33430.419677NLEU88−3.93625.30432.430678CALEU88−3.72923.91532.232679CBLEU88−2.27423.58831.867680CGLEU88−1.97822.08131.671681CD2LEU88−0.67521.67332.376682CD1LEU88−2.03021.70030.187683CLEU88−4.07623.25533.520684OLEU88−3.80323.79934.588685NGLN89−4.71422.06833.448686CAGLN89−4.87821.33034.660687CBGLN89−6.32721.09535.073688CGGLN89−6.42120.53936.492689CDGLN89−7.81819.97336.711690OE1GLN89−8.00119.01437.458691NE2GLN89−8.81520.56236.010692CGLN89−4.22419.99434.486693OGLN89−4.19819.44433.393694NVAL90−3.67219.42335.571695CAVAL90−3.01518.16235.446696CBVAL90−1.56418.29635.068697CG1VAL90−0.85316.92835.162698CG2VAL90−1.46919.04733.713699CVAL90−3.06517.52036.814700OVAL90−3.10218.19737.847701NILE91−3.10016.16936.789702CAILE91−3.31115.30237.917703CBILE91−4.47714.36037.757704CG2ILE91−4.62813.58439.088705CG1ILE91−5.73715.07637.252706CD1ILE91−5.67615.56335.796707CILE91−2.19214.32637.890708OILE91−1.95413.67636.875709NLYS92−1.53714.10639.030710CALYS92−1.02812.77839.161711CBLYS920.49212.72339.353712CGLYS921.06014.14339.448713CDLYS922.54914.26339.113714CELYS922.95515.63538.568715NZLYS923.72116.38739.588716CLYS92−1.71712.27540.373717OLYS92−2.11713.08541.204718NSER93−1.93710.95240.455719CASER93−2.68210.42341.553720CBSER93−2.9398.92341.388721OGSER93−4.1948.58541.954722CSER93−1.85510.63142.783723OSER93−1.0409.77843.133724NASP94−2.03011.79943.449725CAASP94−1.14612.18244.512726CBASP940.33311.85244.251727CGASP940.72511.07645.493728OD1ASP941.44110.04645.379729OD2ASP940.29011.52846.585730CASP94−1.23813.66044.803731OASP94−1.20814.06145.966732NLEU95−1.34614.52243.770733CALEU95−1.59115.91044.067734CBLEU95−0.33716.71144.489735CGLEU95−0.51417.72545.662736CD2LEU95−1.10717.05146.915737CD1LEU95−1.27119.00545.253738CLEU95−2.14116.53742.819739OLEU95−1.68516.25141.712740NVAL96−3.16417.40042.957741CAVAL96−3.70118.03341.792742CBVAL96−5.14218.43041.903743CG1VAL96−6.01917.28741.368744CG2VAL96−5.44218.84943.350745CVAL96−2.94419.29841.647746OVAL96−2.69020.01042.619747NASN97−2.55319.61340.404748CAASN97−1.97020.88840.170749CBASN97−0.62620.82339.429750CGASN970.38720.33040.445751OD1ASN971.53020.03840.096752ND2ASN97−0.03220.26441.734753CASN97−2.91121.58939.264754OASN97−3.47420.98738.349755NGLU98−3.08822.89939.480756CAGLU98−3.45223.69138.355757CBGLU98−4.46324.81438.648758CGGLU98−4.92225.57437.394759CDGLU98−6.32925.13437.023760OE1GLU98−6.67925.15935.814761OE2GLU98−7.08124.79237.974762CGLU98−2.18424.34237.966763OGLU98−1.27223.69937.455764NGLU99−2.11925.65638.250765CAGLU99−1.05226.53437.901766CBGLU990.11726.60138.885767CGGLU991.03327.73738.443768CDGLU992.34127.68539.205769OE1GLU992.51326.80740.100770OE2GLU993.20628.53638.879771CGLU99−0.47226.20736.563772OGLU990.36025.31436.405773NALA100−0.87227.01335.571774CAALA100−0.39126.94034.232775CBALA100−1.01825.76533.466776CALA100−0.88328.20333.611777OALA100−1.96628.23833.034778NTHR101−0.13129.30233.789779CATHR101−0.64430.60933.487780CBTHR101−0.26931.60834.549781OG1THR101−0.83531.18135.771782CG2THR101−0.78733.02134.212783CTHR101−0.06631.04232.179784OTHR1010.88530.44231.684785NGLY102−0.63332.09431.567786CAGLY102−0.10632.57430.329787CGLY102−1.27033.10429.569788OGLY102−2.25732.40029.357789NGLN103−1.19634.37829.148790CAGLN103−2.26534.91028.358791CBGLN103−2.92536.13629.007792CGGLN103−4.13036.70528.255793CDGLN103−4.49837.97828.991794OE1GLN103−5.45438.69328.693795NE2GLN103−3.67038.28630.025796CGLN103−1.64535.36427.081797OGLN103−0.42935.50726.986798NPHE104−2.47535.59126.044799CAPHE104−1.94336.20224.868800CBPHE104−1.22735.23523.897801CGPHE104−2.16934.19923.377802CD1PHE104−2.90633.41824.234803CD2PHE104−2.30333.97822.018804CE1PHE104−3.75632.45323.748805CE2PHE104−3.15333.01421.522806CZPHE104−3.88032.24322.391807CPHE104−3.08636.84924.164808OPHE104−4.24536.53624.421809NHIS105−2.78437.81923.285810CAHIS105−3.82938.57822.669811ND1HIS105−4.81040.66924.965812CGHIS105−3.63840.50024.268813CBHIS105−3.59840.08622.819814NE2HIS105−3.16341.09726.388815CD2HIS105−2.63240.75925.149816CE1HIS105−4.46741.03026.230817CHIS105−3.79238.20121.223818OHIS105−3.14137.22020.869819NVAL106−4.48338.95520.339820CAVAL106−4.36338.71118.923821CBVAL106−5.38437.76318.369822CG1VAL106−6.75738.20018.899823CG2VAL106−5.33337.79616.833824CVAL106−4.61440.00218.227825OVAL106−5.53840.73518.577826NTYR107−3.79240.32317.213827CATYR107−4.02741.57216.568828CBTYR107−2.84542.54816.743829CGTYR107−2.69342.75418.238830CD1TYR107−1.73242.07718.964831CD2TYR107−3.51943.61718.936832CE1TYR107−1.60942.24020.330833CE2TYR107−3.41743.79520.300834CZTYR107−2.43143.12420.997835OHTYR107−2.31443.29822.387836CTYR107−4.29341.28415.120837OTYR107−3.65440.45714.482838NPRO108−5.29441.99914.648839CAPRO108−5.73742.05313.279840CDPRO108−5.87143.06415.448841CBPRO108−7.08442.76913.320842CGPRO108−7.13943.50114.687843CPRO108−4.76742.89712.513844OPRO108−4.12943.73813.143845NGLU109−4.63442.71811.176846CAGLU109−3.55243.32010.423847CBGLU109−3.48442.8498.968848CGGLU109−3.49441.3188.836849CDGLU109−4.93840.8358.829850OE1GLU109−5.30740.1019.782851OE2GLU109−5.67441.2137.883852CGLU109−3.68144.81710.430853OGLU109−4.43245.37311.227854NLEU110−2.94345.5399.545855CALEU110−3.02646.9769.640856CBLEU110−2.01747.65010.584857CGLEU110−2.25849.17210.584858CD2LEU110−0.94849.96310.470859CD1LEU110−3.16549.61011.741860CLEU110−2.84247.6718.317861OLEU110−1.73847.8657.809862NPRO111−3.96448.0947.808863CAPRO111−4.10948.7856.547864CDPRO111−5.22247.7788.447865CBPRO111−5.60548.9106.305866CGPRO111−6.30048.0997.412867CPRO111−3.50350.1576.564868OPRO111−3.17750.6547.642869NLYS112−3.38450.7865.373870CALYS112−2.61751.9935.253871CBLYS112−2.12852.3053.826872CGLYS112−1.22053.5333.800873CDLYS112−0.45353.7242.490874CELYS1120.60754.8322.569875NZLYS1121.85254.2893.159876CLYS112−3.41353.1865.678877OLYS112−4.55553.4205.285878NPRO113−2.71053.9486.486879CAPRO113−3.07655.2746.907880CDPRO113−1.67753.3467.311881CBPRO113−2.11855.6288.055882CGPRO113−1.47054.2958.497883CPRO113−2.96756.2875.795884OPRO113−2.12756.1204.910885NSER114−3.79457.3565.867886CASER114−3.60658.5515.088887CBSER114−4.72958.8094.084888OGSER114−4.45960.0033.359889CSER114−3.60959.7186.035890OSER114−4.18159.6407.118891NILE115−2.96560.8475.637892CAILE115−3.04662.0576.426893CBILE115−1.74062.5576.990894CG2ILE115−0.78162.8215.820895CG1ILE115−2.00363.8107.860896CD1ILE115−0.74664.5888.247897CILE115−3.54763.1675.542898OILE115−3.20863.2394.365899NSER116−4.38564.0616.105900CASER116−4.94365.1655.374901CBSER116−6.46765.3135.590902OGSER116−6.92366.5915.162903CSER116−4.32366.3985.940904OSER116−4.68366.8247.036905NSER117−3.36167.0055.220906CASER117−2.80668.2405.684907CBSER117−1.34368.4755.262908OGSER117−1.02069.8495.405909CSER117−3.60569.3605.093910OSER117−4.17669.2444.010911NASN118−3.65970.5005.798912CAASN118−4.32771.6215.208913CBASN118−5.50572.1436.067914CGASN118−6.45272.9715.207915OD1ASN118−7.07673.9145.687916ND2ASN118−6.55572.6073.901917CASN118−3.31772.7175.048918OASN118−2.88173.3226.025919NASN119−2.92273.0073.787920CAASN119−2.16874.1813.448921CBASN119−2.61775.4314.242922CGASN119−2.05076.6873.586923OD1ASN119−1.27976.6052.633924ND2ASN119−2.38677.8874.137925CASN119−0.69773.9353.642926OASN119−0.25973.4894.701927NSER1200.10274.2192.589928CASER1201.50973.9272.599929CBSER1201.94473.1381.355930OGSER1203.02172.2821.695931CSER1202.26875.2282.605932OSER1203.16875.4403.421933NASN1211.86276.1771.721934CAASN1212.15377.5861.908935CBASN1211.28878.5120.994936CGASN1211.95278.943−0.311937OD1ASN1212.09780.143−0.566938ND2ASN1212.32877.953−1.166939CASN1211.76577.9143.317940OASN1210.98477.1943.929941NPRO1222.26978.9913.869942CAPRO1222.09379.3575.261943CDPRO1223.01379.9513.084944CBPRO1222.66380.7775.394945CGPRO1223.39081.0844.051946CPRO1220.61779.2835.633947OPRO122−0.20179.2944.718948NVAL1230.20879.1846.918949CAVAL1230.88778.8828.152950CBVAL1230.98377.4258.414951CG1VAL123−0.47076.9438.541952CG2VAL1231.82276.7337.326953CVAL1232.23779.4848.259954OVAL1233.26378.8118.297955NGLU1242.26180.8168.367956CAGLU1243.54281.3888.517957CBGLU1243.55482.8858.384958CGGLU1242.41183.4577.629959CDGLU1242.76684.9207.710960OE1GLU1242.84885.5526.621961OE2GLU1242.93485.4148.857962CGLU1243.97481.1599.918963OGLU1243.32580.45710.682964NASP1255.08881.80710.295965CAASP1255.50481.80911.658966CBASP1256.68382.74611.906967CGASP1257.88881.99911.366968OD1ASP1259.02482.53111.470969OD2ASP1257.69780.88010.817970CASP1254.35082.25412.481971OASP1253.89583.39712.375972NLYS1263.85281.30113.296973CALYS1262.92281.50314.373974CBLYS1262.77382.96814.820975CGLYS1262.85083.23716.328976CDLYS1262.70584.72416.637977CELYS1261.31785.11917.133978NZLYS1261.37385.46118.569979CLYS1261.54781.01614.018980OLYS1260.66281.08014.871981NASP1271.32480.49212.789982CAASP1270.04179.90312.493983CBASP127−0.33079.87011.002984CGASP127−0.56581.30710.576985OD1ASP127−0.71482.18411.469986OD2ASP127−0.60581.5549.343987CASP1270.03078.48112.944988OASP1270.76078.09813.855989NALA128−0.85477.64912.352990CAALA128−1.00076.35612.958991CBALA128−2.14076.23913.990992CALA128−1.26375.31311.938993OALA128−2.27375.32711.237994NVAL129−0.35874.32811.878995CAVAL129−0.65873.15011.142996CBVAL1290.52272.23910.974997CG1VAL1290.64971.8609.493998CG2VAL1291.76172.92611.575999CVAL129−1.63672.43111.9941000OVAL129−1.80472.75713.1731001NALA130−2.30271.43311.3911002CAALA130−2.99070.40512.0941003CBALA130−4.48570.68912.3471004CALA130−2.89869.24511.1671005OALA130−3.72469.07210.2721006NPHE131−1.84468.43111.3231007CAPHE131−1.75567.30710.4501008CBPHE131−0.33866.70710.3421009CGPHE1310.53267.6479.5621010CD1PHE1310.31667.8498.2201011CD2PHE1311.58268.32310.1541012CE1PHE1311.10068.7107.4861013CE2PHE1312.37269.1879.4221014CZPHE1312.13469.3898.0881015CPHE131−2.61466.26311.0691016OPHE131−2.28565.74412.1351017NTHR132−3.75265.93310.4231018CATHR132−4.57864.88510.9541019CBTHR132−6.03565.21111.0471020OG1THR132−6.40865.33212.4211021CG2THR132−6.83564.08410.3591022CTHR132−4.46463.67910.0781023OTHR132−4.55263.7598.8511024NCYS133−4.26362.51210.7251025CACYS133−4.14361.22910.1071026CBCYS133−3.33060.26010.9891027SGCYS133−2.96858.66510.2021028CCYS133−5.53360.70910.0081029OCYS133−6.45161.33110.5461030NGLU134−5.71959.5689.3061031CAGLU134−6.97958.8649.3051032CBGLU134−8.00659.3038.2411033CGGLU134−8.38660.7838.2231034CDGLU134−8.87561.0566.7921035OE1GLU134−10.08961.3506.6261036OE2GLU134−8.05060.9525.8451037CGLU134−6.74157.4248.9741038OGLU134−6.15157.0797.9541039NPRO135−7.24356.5779.8181040CAPRO135−7.05055.1699.6351041CDPRO135−7.07756.94011.2021042CBPRO135−6.08354.73510.7251043CGPRO135−6.05355.91111.7301044CPRO135−8.39554.5929.9341045OPRO135−9.25655.31510.4331046NGLU136−8.64753.3029.6701047CAGLU136−10.01152.9749.9551048CBGLU136−10.82452.6708.6821049CGGLU136−12.22253.3118.6291050CDGLU136−12.43054.1997.3911051OE1GLU136−13.08655.2557.5991052OE2GLU136−11.97053.8776.2581053CGLU136−10.07851.79510.8811054OGLU136−11.14351.20511.0631055NVAL137−8.93951.44011.5161056CAVAL137−8.88250.30612.3981057CBVAL137−7.51049.74212.5781058CG1VAL137−7.59548.22612.4231059CG2VAL137−6.55450.41411.5871060CVAL137−9.30450.70013.7861061OVAL137−10.09551.62613.9641062NGLN138−8.76449.97314.7961063CAGLN138−8.84250.29916.1941064CBGLN138−10.24050.05816.8141065CGGLN138−10.72148.60716.9521066CDGLN138−11.95548.62017.8691067OE1GLN138−11.90749.16418.9721068NE2GLN138−13.07247.99617.4151069CGLN138−7.79849.44316.8581070OGLN138−7.24448.54816.2261071NASN139−7.48549.70718.1381072CAASN139−6.30349.20718.7831073CBASN139−6.29847.70419.0841074CGASN139−5.41547.53220.3091075OD1ASN139−4.84346.47620.5691076ND2ASN139−5.27848.64421.0801077CASN139−5.10449.56217.9691078OASN139−4.13248.81817.8661079NTHR140−5.15550.76817.3991080CATHR140−4.04351.45816.8511081CBTHR140−4.50752.74416.2601082OG1THR140−4.93753.61617.2881083CG2THR140−5.67852.41315.3181084CTHR140−3.16951.79018.0091085OTHR140−3.66351.96319.1251086NTHR141−1.84951.91217.7711087CATHR141−1.12152.86018.5611088CBTHR141−0.35352.32519.7211089OG1THR1410.76653.17219.9361090CG2THR1410.10150.88619.4571091CTHR141−0.17253.57017.6651092OTHR1410.50352.97416.8241093NTYR142−0.18554.90417.8001094CATYR1420.04255.73216.6641095CBTYR142−1.14856.67116.4491096CGTYR142−0.78257.65315.4151097CD1TYR142−0.54757.24714.1181098CD2TYR142−0.70958.98115.7311099CE1TYR142−0.20158.15713.1571100CE2TYR142−0.35859.91214.7931101CZTYR142−0.11659.50013.4921102OHTYR1420.23160.43012.5151103CTYR1421.24056.55616.9891104OTYR1421.32457.15418.0411105NLEU1432.21356.61316.0391106CALEU1433.31257.49216.2751107CBLEU1434.67156.78116.2671108CGLEU1435.08856.30817.6671109CD2LEU1435.57354.85817.6661110CD1LEU1433.96356.52518.6911111CLEU1433.30758.51215.1961112OLEU1432.57358.39114.2201113NTRP1444.11459.57815.3721114CATRP1444.13360.68814.4501115CBTRP1443.71362.00715.1341116CGTRP1442.24062.35015.0261117CD2TRP1441.65662.77613.7951118CD1TRP1441.24062.37715.9621119NE1TRP1440.06762.80815.3841120CE2TRP1440.31363.05914.0481121CE3TRP1442.19662.93112.5601122CZ2TRP144−0.50863.51713.0571123CZ3TRP1441.36763.36311.5531124CH2TRP1440.04363.66111.8051125CTRP1445.56660.85814.0321126OTRP1446.46760.60514.8261127NTRP1455.84561.29612.7821128CATRP1457.23961.46312.4781129CBTRP1457.89360.22911.8091130CGTRP1457.52958.83312.3081131CD2TRP1457.83658.26113.6011132CD1TRP1456.89057.85211.6151133NE1TRP1456.78156.71312.3721134CE2TRP1457.35156.95013.6001135CE3TRP1458.49158.76514.6901136CZ2TRP1457.51256.13814.6851137CZ3TRP1458.61657.95815.7981138CH2TRP1458.13156.66715.8011139CTRP1457.43962.63411.5521140OTRP1456.47663.22211.0551141NVAL1468.73062.99811.3281142CAVAL1469.11464.10610.4901143CBVAL1469.32265.39211.2351144CG1VAL14610.07666.36310.3091145CG2VAL1467.97465.93511.7401146CVAL14610.45563.8289.8521147OVAL14611.44563.59610.5421148NASN14710.50963.9098.5071149CAASN14711.67463.8447.6691150CBASN14712.91164.5568.2381151CGASN14712.81666.0127.8031152OD1ASN14713.40166.8818.4451153ND2ASN14712.06666.2836.7031154CASN14711.97562.4117.4581155OASN14712.85562.0556.6671156NGLY14811.22361.5638.1761157CAGLY14811.51060.1738.2141158CGLY14812.19659.8859.5031159OGLY14812.95058.9209.5871160NGLN14911.97660.69910.5541161CAGLN14912.66860.32711.7541162CBGLN14914.19260.47011.6341163CGGLN14914.98559.40212.3801164CDGLN14916.43259.86612.3851165OE1GLN14916.75361.04712.4871166NE2GLN14917.35358.88112.2761167CGLN14912.27761.24312.8581168OGLN14912.32562.45712.6761169NSER15011.92460.61114.0201170CASER15011.45060.99815.3431171CBSER15012.51360.81416.4301172OGSER15011.97460.09217.5311173CSER15010.97062.40015.4941174OSER15011.43063.31614.8321175NLEU15110.04962.64316.4441176CALEU1519.86664.00816.8081177CBLEU1518.63964.78616.3081178CGLEU1518.98366.26716.0571179CD2LEU1518.03367.26216.7581180CD1LEU1519.04666.53014.5481181CLEU1519.47363.95718.2091182OLEU1518.27063.96718.4361183NPRO15210.46164.02619.0821184CAPRO15210.32965.02920.0991185CDPRO15211.76664.22218.4761186CBPRO15210.82066.29919.4141187CGPRO15211.94665.74718.5031188CPRO1528.99365.16520.7131189OPRO1528.67264.42421.6481190NVAL1538.17666.08420.1621191CAVAL1537.20266.87720.8711192CBVAL1536.44066.29322.0661193CG1VAL1535.63667.41522.7641194CG2VAL1535.55465.11021.6851195CVAL1537.92268.00821.4931196OVAL1538.92067.82222.1751197NSER1547.42069.22621.3311198CASER1547.91870.23022.2171199CBSER1548.76271.33121.5391200OGSER1549.74070.79420.6641201CSER1546.70170.92222.6601202OSER1545.65170.73522.0421203NPRO1556.83771.72523.6841204CAPRO1555.77372.51324.2231205CDPRO1557.96771.62924.5851206CBPRO1556.49873.53825.1031207CGPRO1557.74272.75625.6091208CPRO1554.82573.05923.1841209OPRO1553.62872.77823.2541210NARG1565.33173.80922.1931211CAARG1564.51374.44021.1881212CBARG1565.30775.07020.0401213CGARG1566.56974.29119.6841214CDARG1567.37374.98318.5821215NEARG1568.07773.95117.7671216CZARG1568.35174.21116.4491217NH1ARG1567.89175.37015.8941218NH2ARG1569.08373.34115.6941219CARG1563.49973.49620.5911220OARG1562.37873.92320.3291221NLEU1573.82272.20920.3291222CALEU1572.83771.45019.5861223CBLEU1573.33070.16918.8891224CGLEU1574.51770.37617.9371225CD2LEU1574.53269.32516.8101226CD1LEU1575.82770.41918.7451227CLEU1571.70071.02920.4551228OLEU1571.27071.76021.3471229NGLN1581.13769.83520.1511230CAGLN158−0.05769.31320.7691231CBGLN158−1.13270.37321.0971232CGGLN158−2.41669.79021.7191233CDGLN158−3.57070.77621.5741234OE1GLN158−4.59870.66122.2451235NE2GLN158−3.40471.77420.6641236CGLN158−0.70368.39419.7731237OGLN158−0.78668.71618.5941238NLEU159−1.17867.21720.2121239CALEU159−1.99966.39719.3601240CBLEU159−1.28265.16518.7721241CGLEU159−0.47964.38119.8351242CD2LEU1590.99864.83219.8381243CD1LEU159−0.66462.85619.6941244CLEU159−3.05165.85120.2571245OLEU159−2.79565.60121.4321246NSER160−4.27565.64319.7451247CASER160−5.24565.09520.6431248CBSER160−6.44866.02820.9321249OGSER160−6.99566.51119.7161250CSER160−5.76463.84520.0151251OSER160−5.16963.32519.0701252NASN161−6.90063.35020.5491253CAASN161−7.73662.38719.8761254CBASN161−8.45962.95218.6431255CGASN161−9.90763.25118.9701256OD1ASN161−10.68263.52918.0571257ND2ASN161−10.28163.17020.2741258CASN161−6.91761.26419.3521259OASN161−6.65461.20818.1481260NGLY162−6.51860.34020.2451261CAGLY162−5.76159.17019.9091262CGLY162−4.64759.56418.9871263OGLY162−4.48458.97517.9171264NASN163−3.85060.58419.3671265CAASN163−2.66660.95118.6101266CBASN163−1.63759.81818.4221267CGASN163−0.79359.59419.6601268OD1ASN1630.43259.64819.5841269ND2ASN163−1.46959.36920.8061270CASN163−3.03661.25017.1951271OASN163−2.14961.33016.3331272NMET164−4.31661.36016.8581273CAMET164−4.62961.31015.4681274CBMET164−6.14161.09115.2851275CGMET164−6.78361.66514.0291276SDMET164−8.49061.06113.8601277CEMET164−8.74161.71712.1931278CMET164−4.21462.62714.9271279OMET164−3.11862.80014.3981280NTHR165−5.09063.60815.1441281CATHR165−4.79365.00615.1061282CBTHR165−5.78065.76015.9321283OG1THR165−5.92465.09217.1711284CG2THR165−7.11865.74715.1821285CTHR165−3.46965.26115.7371286OTHR165−3.05664.60416.6931287NLEU166−2.79066.28315.2091288CALEU166−1.71166.91315.8951289CBLEU166−0.35866.26815.5931290CGLEU1660.81167.24815.6741291CD2LEU1661.94066.72014.7791292CD1LEU1661.23167.58117.1191293CLEU166−1.67968.28915.3341294OLEU166−1.76968.47714.1211295NTHR167−1.62369.29716.2091296CATHR167−1.78970.64115.7701297CBTHR167−2.93471.32016.4551298OG1THR167−2.65472.69816.6491299CG2THR167−3.14170.62617.8081300CTHR167−0.53971.36416.1411301OTHR167−0.16471.41817.3111302NLEU1680.15471.94115.1401303CALEU1681.33272.68815.4541304CBLEU1682.46372.53614.4221305CGLEU1683.76573.24314.8641306CD2LEU1684.87673.10913.8041307CD1LEU1684.17072.80016.2811308CLEU1680.94474.12615.4451309OLEU1680.66174.68814.3911310NLEU1690.92774.76716.6321311CALEU1690.80176.19416.7191312CBLEU169−0.65476.67616.8041313CGLEU169−0.78478.16817.1671314CD2LEU169−1.91978.39818.1761315CD1LEU169−0.96179.04015.9141316CLEU1691.41576.56018.0231317OLEU1691.12275.92719.0331318NSER1702.28577.58818.0701319CASER1702.75878.30716.9221320CBSER1703.55979.56317.3191321OGSER1704.42779.95216.2611322CSER1703.67177.38416.1701323OSER1704.32676.51816.7511324NVAL1713.72577.52714.8341325CAVAL1714.68176.76114.0941326CBVAL1714.10676.25212.7971327CG1VAL1713.43077.43212.0711328CG2VAL1715.16675.52211.9561329CVAL1715.82877.70413.8591330OVAL1715.73478.87614.2091331NLYS1726.96677.23713.3031332CALYS1728.01378.19613.0411333CBLYS1728.87478.52714.3161334CGLYS17210.37178.13414.4391335CDLYS17210.65677.03415.4701336CELYS17212.14076.83315.8381337NZLYS17213.03377.69715.0221338CLYS1728.76177.71811.8171339OLYS1728.16377.07810.9561340NARG17310.06678.04011.6711341CAARG17310.81377.73010.4881342CBARG17311.92678.74710.2301343CGARG17313.21178.35310.9491344CDARG17314.43979.11310.4571345NEARG17315.28679.41911.6391346CZARG17315.68280.70211.8811347NH1ARG17315.27381.69511.0241348NH2ARG17316.46981.00312.9461349CARG17311.50076.41210.6901350OARG17312.14375.8869.7801351NASN17411.38275.84411.9051352CAASN17412.03774.60012.1991353CBASN17411.89774.17213.6801354CGASN17412.93873.10714.0571355OD1ASN17412.83372.50615.1241356ND2ASN17413.95772.87113.1931357CASN17411.37573.54811.3661358OASN17411.97272.52211.0461359NASP17510.09973.77511.0111360CAASP1759.25572.71910.5371361CBASP1757.77872.99610.8191362CGASP1757.65273.00112.3351363OD1ASP1757.43074.09312.9171364OD2ASP1757.80071.90712.9441365CASP1759.41272.4989.0641366OASP1758.59571.8088.4541367NALA17610.46473.0658.4471368CAALA17610.62572.9207.0271369CBALA17611.74073.8146.4361370CALA17611.00671.4956.7641371OALA17612.18871.1636.7331372NGLY17710.01070.6026.5641373CAGLY17710.33769.2176.3561374CGLY1779.11568.4765.8951375OGLY1778.07769.0675.5941376NSER1789.21367.1325.8131377CASER1788.07866.3545.3921378CBSER1788.34165.4884.1431379OGSER1787.11465.0593.5741380CSER1787.73565.4186.4941381OSER1788.59764.7106.9931382NTYR1796.46265.3866.9141383CATYR1796.14064.6508.0941384CBTYR1795.27865.4749.0771385CGTYR1796.02966.6859.5611386CD1TYR1795.50367.42010.6071387CD2TYR1797.22767.0929.0111388CE1TYR1796.14868.53611.0851389CE2TYR1797.88168.2089.4841390CZTYR1797.34368.93010.5201391OHTYR1798.03070.06710.9871392CTYR1795.35663.4477.6681393OTYR1794.37863.5606.9301394NGLU1805.77962.2508.1211395CAGLU1805.07061.0627.7681396CBGLU1805.97059.8217.6321397CGGLU1805.27758.6456.0401398CDGLU1805.88958.4205.5581399OE1GLU1807.12258.1765.4801400OE2GLU1805.13258.4874.5561401CGLU1804.07460.8048.8481402OGLU1803.92961.6079.7741403NCYS1813.35959.6698.7501404CACYS1812.60759.1669.8531405CBCYS1811.08159.2409.6461406SGCYS1810.32057.6529.2351407CCYS1813.03357.7459.9691408OCYS1813.77557.2649.1151409NGLU1822.61057.04611.0411410CAGLU1822.77355.62611.1451411CBGLU1824.18255.14111.5971412CGGLU1824.54853.74711.0611413CDGLU1825.45952.99612.0371414OE1GLU1826.06353.63212.9431415OE2GLU1825.55751.75211.8731416CGLU1821.81755.21512.2031417OGLU1821.76855.80813.2791418NILE1831.01654.18111.9171419CAILE1830.31953.54712.9881420CBILE183−1.11453.21612.6341421CG2ILE183−1.72952.37713.7701422CG1ILE183−1.88654.51712.3211423CD1ILE183−2.95054.38511.2341424CILE1831.11052.29113.2181425OILE1831.94451.93112.3881426NGLN1840.91851.62314.3731427CAGLN1841.75750.49714.6241428CBGLN1842.85550.77315.6591429CGGLN1844.13549.98215.3781430CDGLN1845.12750.17416.5281431OE1GLN1844.75450.29417.6931432NE2GLN1846.43750.19916.1841433CGLN1840.91449.36415.1071434OGLN1840.12448.81414.3461435NASN1851.08948.98316.3971436CAASN1850.53647.79917.0041437CBASN185−0.87547.38916.4591438CGASN185−0.90646.15415.5551439OD1ASN185−1.08945.03416.0201440ND2ASN185−0.81446.34914.2141441CASN1851.57946.72216.8731442OASN1852.53046.91916.1161443NPRO1861.48845.61917.5891444CAPRO1862.58944.69717.7221445CDPRO1860.56445.50518.7031446CBPRO1862.06243.56418.5981447CGPRO1860.98244.23519.4781448CPRO1863.12744.28216.3901449OPRO1862.33843.88115.5351450NALA1874.45744.43816.2091451CAALA1875.07344.85914.9811452CBALA1876.58044.53914.9051453CALA1874.40444.23513.7981454OALA1874.53643.03813.5391455NSER1883.66945.08813.0541456CASER1883.02944.77911.8131457CBSER1881.85943.78011.9421458OGSER1881.09143.75310.7461459CSER1882.44546.09011.3941460OSER1881.24246.32811.5241461NALA1893.30047.01010.9101462CAALA1892.77848.30810.6241463CBALA1893.41649.42511.4561464CALA1893.04248.6149.1891465OALA1893.89847.9968.5541466NASN1902.28149.5968.6631467CAASN1902.57750.2297.4151468CBASN1901.40350.1536.4071469CGASN1901.38448.7685.7441470OD1ASN1900.62347.8806.1111471ND2ASN1902.26048.5824.7241472CASN1902.83751.6747.7451473OASN1903.19252.0018.8791474NARG1912.70152.6056.7751475CAARG1912.88553.9957.1241476CBARG1914.25054.5896.7151477CGARG1915.45953.9037.3281478CDARG1916.76454.2926.6411479NEARG1917.85253.5687.3631480CZARG1918.93554.2657.8181481NH1ARG1919.06355.5937.5601482NH2ARG1919.88953.5978.5421483CARG1911.85454.8036.4081484OARG1910.70854.3926.2891485NSER1922.24055.9945.9151486CASER1921.28056.7835.1921487CBSER1920.52457.8236.0451488OGSER1921.35458.9446.2901489CSER1921.97457.5614.1231490OSER1923.07557.2233.6831491NASP1931.29058.6323.6551492CAASP1931.74759.3812.5271493CBASP1930.68559.6791.4361494CGASP193−0.38160.6411.9821495OD1ASP193−1.12361.2101.1361496OD2ASP193−0.48560.8313.2231497CASP1932.28460.6822.9941498OASP1931.95861.2064.0561499NPRO1943.18561.1392.1761500CAPRO1944.16662.0562.6721501CDPRO1943.73060.2451.1781502CBPRO1945.51261.6332.0861503CGPRO1945.24960.2781.4101504CPRO1943.78763.4402.2951505OPRO1944.03763.8291.1531506NVAL1953.17264.2063.2241507CAVAL1952.81165.5622.9071508CBVAL1951.60066.0313.6631509CG1VAL1950.55064.9303.5321510CG2VAL1951.99866.3355.1111511CVAL1953.98766.4123.2781512OVAL1954.71366.1054.2241513NTHR1964.26567.4902.5121514CATHR1965.49368.1892.7921515CBTHR1966.40168.3451.6041516OG1THR1967.53369.1311.9741517CG2THR1965.62569.0370.4831518CTHR1965.14869.5623.2291519OTHR1964.24370.1992.6931520NLEU1975.88870.0824.2171521CALEU1975.66871.4554.4981522CBLEU1975.08771.7265.8891523CGLEU1973.58672.0155.7861524CD2LEU1972.96972.2927.1621525CD1LEU1972.84370.9005.0421526CLEU1976.95172.1824.3871527OLEU1977.92671.9185.0911528NASN1986.95373.1653.4801529CAASN1987.87274.2383.6281530CBASN1988.53274.6952.3151531CGASN1989.13873.4651.6421532OD1ASN19810.12272.8972.1131533ND2ASN1988.51473.0350.5251534CASN1987.04275.3764.1371535OASN1985.81275.3124.1491536NVAL1997.69476.4544.6011537CAVAL1996.94777.5195.1921538CBVAL1997.22477.6796.6671539CG1VAL1998.15776.5467.1241540CG2VAL1997.88979.0366.9131541CVAL1997.38878.7634.5061542OVAL1998.55078.8814.1331543NLEU2006.48279.7414.3161544CALEU2006.94881.0523.9731545CBLEU2006.21781.7662.8131546CGLEU2006.82883.1492.4901547CD2LEU2005.82484.0861.7881548CD1LEU2008.16782.9731.7411549CLEU2006.69181.8935.1731550OLEU2005.89881.5366.0421551NTYR2017.36383.0545.2331552CATYR2017.17483.9826.3001553CBTYR2018.48784.6586.7421554CGTYR2019.63384.1425.9351555CD1TYR20110.19584.9594.9851556CD2TYR20110.14482.8776.0911557CE1TYR20111.25884.5284.2281558CE2TYR20111.21082.4385.3391559CZTYR20111.77083.2724.3991560OHTYR20112.86582.8073.6351561CTYR2016.30485.0895.8001562OTYR2015.87885.1014.6431563NGLY2026.07586.0676.6981564CAGLY2025.74287.3966.3171565CGLY2026.47988.2547.3021566OGLY2025.87488.7668.2421567NPRO2037.76988.4217.1041568CAPRO2038.63289.1497.9981569CDPRO2038.50587.7176.0641570CBPRO20310.06988.9087.5601571CGPRO20310.00387.8536.4411572CPRO2038.35990.6137.9331573OPRO2037.25191.0808.2991574OXTPRO2039.31291.3337.526

[0137]

6

TABLE 3

Full coodinate set of domains N and A1 of human CECAM5

(homology model) (1606 atoms, 203 amino acids)

ANum
AType
RType
RNum
X
Y
Z

1
N
LYS
1
7.719
28.906
40.374

2
CA
LYS
1
7.851
27.446
40.229

3
CB
LYS
1
6.809
26.734
41.091

4
CG
LYS
1
5.441
27.413
41.027

5
CD
LYS
1
4.491
26.971
42.148

6
CE
LYS
1
3.141
27.698
42.179

7
NZ
LYS
1
2.197
26.990
43.074

8
C
LYS
1
7.678
26.990
38.826

9
O
LYS
1
6.752
26.240
38.523

10
N
LEU
2
8.629
27.425
37.973

11
CA
LEU
2
9.051
26.761
36.779

12
CB
LEU
2
10.019
25.616
37.140

13
CG
LEU
2
10.513
24.754
35.969

14
CD2
LEU
2
10.784
23.313
36.435

15
CD1
LEU
2
11.710
25.411
35.264

16
C
LEU
2
7.868
26.210
36.040

17
O
LEU
2
7.587
25.014
36.119

18
N
THR
3
7.156
27.055
35.272

19
CA
THR
3
6.338
26.446
34.274

20
CB
THR
3
4.867
26.351
34.590

21
OG1
THR
3
4.354
27.606
34.995

22
CG2
THR
3
4.679
25.323
35.708

23
C
THR
3
6.420
27.222
33.016

24
O
THR
3
7.485
27.542
32.485

25
N
ILE
4
5.220
27.467
32.495

26
CA
ILE
4
4.898
27.380
31.122

27
CB
ILE
4
3.414
27.094
31.056

28
CG2
ILE
4
2.817
27.645
32.362

29
CG1
ILE
4
2.706
27.582
29.785

30
CD1
ILE
4
1.190
27.556
29.964

31
C
ILE
4
5.299
28.670
30.501

32
O
ILE
4
5.731
29.607
31.167

33
N
GLU
5
5.207
28.727
29.174

34
CA
GLU
5
5.406
29.948
28.488

35
CB
GLU
5
6.776
30.023
27.796

36
CG
GLU
5
7.271
31.453
27.633

37
CD
GLU
5
8.469
31.398
26.712

38
OE1
GLU
5
9.340
30.506
26.885

39
OE2
GLU
5
8.525
32.280
25.814

40
C
GLU
5
4.375
29.904
27.433

41
O
GLU
5
3.556
28.985
27.383

42
N
SER
6
4.390
30.887
26.534

43
CA
SER
6
3.762
30.536
25.315

44
CB
SER
6
2.220
30.413
25.400

45
OG
SER
6
1.532
31.447
24.712

46
C
SER
6
4.248
31.483
24.282

47
O
SER
6
4.588
32.634
24.557

48
N
THR
7
4.391
30.949
23.058

49
CA
THR
7
5.185
31.571
22.043

50
CB
THR
7
6.530
30.916
21.987

51
OG1
THR
7
6.451
29.758
21.164

52
CG2
THR
7
6.933
30.480
23.410

53
C
THR
7
4.485
31.307
20.728

54
O
THR
7
3.950
30.213
20.561

55
N
PRO
8
4.423
32.174
19.737

56
CA
PRO
8
4.856
33.548
19.726

57
CD
PRO
8
3.905
31.742
18.448

58
CB
PRO
8
4.784
34.016
18.262

59
CG
PRO
8
4.386
32.779
17.430

60
C
PRO
8
3.967
34.410
20.576

61
O
PRO
8
2.756
34.386
20.370

62
N
PHE
9
4.517
35.217
21.502

63
CA
PHE
9
3.636
36.141
22.162

64
CB
PHE
9
4.197
36.770
23.438

65
CG
PHE
9
5.659
36.531
23.446

66
CD1
PHE
9
6.498
37.206
22.587

67
CD2
PHE
9
6.175
35.607
24.324

68
CE1
PHE
9
7.851
36.969
22.600

69
CE2
PHE
9
7.527
35.370
24.338

70
CZ
PHE
9
8.361
36.044
23.480

71
C
PHE
9
3.351
37.259
21.232

72
O
PHE
9
4.192
37.642
20.427

73
N
ASN
10
2.133
37.812
21.329

74
CA
ASN
10
1.614
38.674
20.328

75
CB
ASN
10
2.538
39.860
20.000

76
CG
ASN
10
2.564
40.745
21.243

77
OD1
ASN
10
3.586
40.930
21.897

78
ND2
ASN
10
1.372
41.285
21.600

79
C
ASN
10
1.397
37.814
19.137

80
O
ASN
10
2.324
37.199
18.612

81
N
VAL
11
0.130
37.708
18.714

82
CA
VAL
11
−0.190
36.730
17.724

83
CB
VAL
11
−0.948
35.575
18.295

84
CG1
VAL
11
−1.005
34.472
17.231

85
CG2
VAL
11
−0.295
35.190
19.634

86
C
VAL
11
−1.071
37.388
16.724

87
O
VAL
11
−1.905
38.221
17.071

88
N
ALA
12
−0.909
37.024
15.442

89
CA
ALA
12
−1.746
37.630
14.455

90
CB
ALA
12
−1.049
37.835
13.107

91
C
ALA
12
−2.899
36.724
14.214

92
O
ALA
12
−2.978
35.630
14.760

93
N
GLU
13
−3.828
37.182
13.360

94
CA
GLU
13
−4.929
36.381
12.938

95
CB
GLU
13
−6.067
37.242
12.386

96
CG
GLU
13
−7.406
37.104
13.096

97
CD
GLU
13
−8.426
37.618
12.105

98
OE1
GLU
13
−9.337
38.373
12.545

99
OE2
GLU
13
−8.293
37.268
10.905

100
C
GLU
13
−4.438
35.561
11.785

101
O
GLU
13
−3.721
36.063
10.922

102
N
GLY
14
−4.824
34.273
11.726

103
CA
GLY
14
−4.468
33.488
10.576

104
C
GLY
14
−3.074
32.980
10.767

105
O
GLY
14
−2.526
32.273
9.920

106
N
LYS
15
−2.451
33.327
11.904

107
CA
LYS
15
−1.197
32.718
12.217

108
CB
LYS
15
−0.051
33.735
12.269

109
CG
LYS
15
−0.119
34.632
11.029

110
CD
LYS
15
0.993
35.679
10.902

111
CE
LYS
15
2.131
35.267
9.963

112
NZ
LYS
15
2.956
34.221
10.607

113
C
LYS
15
−1.391
32.076
13.547

114
O
LYS
15
−2.304
32.432
14.292

115
N
GLU
16
−0.565
31.062
13.858

116
CA
GLU
16
−0.885
30.231
14.973

117
CB
GLU
16
−0.468
28.759
14.821

118
CG
GLU
16
−0.855
28.083
13.509

119
CD
GLU
16
0.055
26.879
13.339

120
OE1
GLU
16
−0.468
25.736
13.272

121
OE2
GLU
16
1.295
27.094
13.279

122
C
GLU
16
−0.106
30.692
16.151

123
O
GLU
16
0.360
31.825
16.221

124
N
VAL
17
0.040
29.750
17.100

125
CA
VAL
17
0.901
29.883
18.234

126
CB
VAL
17
0.168
30.218
19.485

127
CG1
VAL
17
0.938
31.330
20.220

128
CG2
VAL
17
−1.281
30.575
19.115

129
C
VAL
17
1.425
28.531
18.506

130
O
VAL
17
1.137
27.562
17.804

131
N
LEU
18
2.194
28.440
19.598

132
CA
LEU
18
2.312
27.209
20.293

133
CB
LEU
18
3.640
26.468
20.079

134
CG
LEU
18
3.893
25.416
21.171

135
CD2
LEU
18
5.356
24.945
21.148

136
CD1
LEU
18
2.881
24.263
21.105

137
C
LEU
18
2.260
27.578
21.730

138
O
LEU
18
2.724
28.648
22.126

139
N
LEU
19
1.677
26.706
22.551

140
CA
LEU
19
1.716
26.993
23.941

141
CB
LEU
19
0.403
26.655
24.656

142
CG
LEU
19
−0.680
27.738
24.442

143
CD2
LEU
19
−0.640
28.282
23.002

144
CD1
LEU
19
−0.585
28.822
25.521

145
C
LEU
19
2.805
26.150
24.477

146
O
LEU
19
2.745
24.919
24.382

147
N
LEU
20
3.856
26.783
25.021

148
CA
LEU
20
4.993
26.013
25.422

149
CB
LEU
20
6.326
26.772
25.259

150
CG
LEU
20
7.534
25.943
24.767

151
CD2
LEU
20
8.836
26.766
24.803

152
CD1
LEU
20
7.278
25.353
23.369

153
C
LEU
20
4.841
25.737
26.873

154
O
LEU
20
4.677
26.668
27.660

155
N
VAL
21
4.936
24.462
27.288

156
CA
VAL
21
5.238
24.258
28.671

157
CB
VAL
21
4.507
23.108
29.315

158
CG1
VAL
21
5.350
22.512
30.458

159
CG2
VAL
21
3.139
23.628
29.800

160
C
VAL
21
6.694
23.965
28.679

161
O
VAL
21
7.215
23.442
27.698

162
N
HIS
22
7.397
24.321
29.761

163
CA
HIS
22
8.786
24.010
29.781

164
ND1
HIS
22
9.333
26.496
28.441

165
CG
HIS
22
9.558
26.351
29.789

166
CB
HIS
22
9.645
25.048
30.483

167
NE2
HIS
22
9.498
28.548
29.294

168
CD2
HIS
22
9.653
27.612
30.296

169
CE1
HIS
22
9.307
27.836
28.202

170
C
HIS
22
8.920
22.793
30.582

171
O
HIS
22
8.305
21.766
30.305

172
N
ASN
23
9.748
22.904
31.629

173
CA
ASN
23
10.006
21.784
32.467

174
CB
ASN
23
11.195
22.015
33.403

175
CG
ASN
23
12.353
22.416
32.510

176
OD1
ASN
23
12.364
23.492
31.918

177
ND2
ASN
23
13.354
21.506
32.387

178
C
ASN
23
8.801
21.518
33.302

179
O
ASN
23
8.148
22.426
33.818

180
N
LEU
24
8.508
20.219
33.461

181
CA
LEU
24
7.461
19.763
34.313

182
CB
LEU
24
7.266
20.563
35.614

183
CG
LEU
24
8.471
20.531
36.586

184
CD2
LEU
24
9.273
19.225
36.501

185
CD1
LEU
24
8.009
20.850
38.021

186
C
LEU
24
6.178
19.720
33.563

187
O
LEU
24
5.755
20.754
33.046

188
N
PRO
25
5.492
18.615
33.419

189
CA
PRO
25
6.024
17.290
33.582

190
CD
PRO
25
4.799
18.618
32.147

191
CB
PRO
25
6.666
17.029
32.228

192
CG
PRO
25
5.643
17.676
31.251

193
C
PRO
25
6.732
16.752
34.802

194
O
PRO
25
7.442
17.427
35.540

195
N
GLN
26
6.552
15.451
35.055

196
CA
GLN
26
7.306
14.839
36.100

197
CB
GLN
26
7.191
15.526
37.471

198
CG
GLN
26
8.493
15.518
38.270

199
CD
GLN
26
8.277
16.292
39.569

200
OE1
GLN
26
8.593
15.744
40.622

201
NE2
GLN
26
7.767
17.553
39.529

202
C
GLN
26
6.699
13.501
36.286

203
O
GLN
26
6.592
13.016
37.410

204
N
HIS
27
6.271
12.876
35.172

205
CA
HIS
27
5.746
11.550
35.271

206
ND1
HIS
27
6.880
8.446
34.776

207
CG
HIS
27
6.598
9.177
35.914

208
CB
HIS
27
6.747
10.661
36.032

209
NE2
HIS
27
6.350
6.985
36.369

210
CD2
HIS
27
6.263
8.281
36.864

211
CE1
HIS
27
6.719
7.141
35.109

212
C
HIS
27
4.449
11.684
36.019

213
O
HIS
27
4.406
11.513
37.237

214
N
LEU
28
3.362
12.053
35.294

215
CA
LEU
28
2.137
12.488
35.925

216
CB
LEU
28
1.429
13.680
35.242

217
CG
LEU
28
1.843
15.128
35.603

218
CD2
LEU
28
3.206
15.527
35.022

219
CD1
LEU
28
1.751
15.391
37.104

220
C
LEU
28
1.135
11.398
35.752

221
O
LEU
28
1.389
10.229
36.038

222
N
PHE
29
−0.056
11.813
35.284

223
CA
PHE
29
−1.120
10.941
34.905

224
CB
PHE
29
−2.180
10.728
35.999

225
CG
PHE
29
−3.017
9.531
35.649

226
CD1
PHE
29
−3.363
8.646
36.641

227
CD2
PHE
29
−3.470
9.300
34.370

228
CE1
PHE
29
−4.115
7.537
36.341

229
CE2
PHE
29
−4.226
8.197
34.061

230
CZ
PHE
29
−4.545
7.306
35.058

231
C
PHE
29
−1.812
11.629
33.772

232
O
PHE
29
−1.558
11.322
32.609

233
N
GLY
30
−2.725
12.571
34.083

234
CA
GLY
30
−3.558
13.104
33.048

235
C
GLY
30
−3.063
14.471
32.693

236
O
GLY
30
−2.619
15.252
33.535

237
N
TYR
31
−3.140
14.817
31.401

238
CA
TYR
31
−2.867
16.188
31.120

239
CB
TYR
31
−2.000
16.431
29.876

240
CG
TYR
31
−0.769
15.562
29.727

241
CD1
TYR
31
0.219
16.026
28.890

242
CD2
TYR
31
−0.558
14.350
30.345

243
CE1
TYR
31
1.370
15.319
28.662

244
CE2
TYR
31
0.606
13.619
30.130

245
CZ
TYR
31
1.569
14.108
29.281

246
OH
TYR
31
2.771
13.397
29.034

247
C
TYR
31
−4.204
16.843
30.881

248
O
TYR
31
−5.221
16.382
31.405

249
N
SER
32
−4.220
17.929
30.067

250
CA
SER
32
−5.404
18.590
29.575

251
CB
SER
32
−6.637
18.522
30.497

252
OG
SER
32
−7.790
18.998
29.815

253
C
SER
32
−5.091
20.047
29.385

254
O
SER
32
−4.146
20.569
29.977

255
N
TRP
33
−5.889
20.742
28.541

256
CA
TRP
33
−5.884
22.181
28.518

257
CB
TRP
33
−5.461
22.830
27.199

258
CG
TRP
33
−3.975
22.934
27.032

259
CD2
TRP
33
−3.130
23.860
27.742

260
CD1
TRP
33
−3.157
22.181
26.246

261
NE1
TRP
33
−1.852
22.575
26.424

262
CE2
TRP
33
−1.821
23.605
27.349

263
CE3
TRP
33
−3.421
24.840
28.640

264
CZ2
TRP
33
−0.778
24.335
27.863

265
CZ3
TRP
33
−2.378
25.578
29.161

266
CH2
TRP
33
−1.073
25.322
28.777

267
C
TRP
33
−7.293
22.626
28.715

268
O
TRP
33
−8.236
21.906
28.386

269
N
TYR
34
−7.470
23.837
29.268

270
CA
TYR
34
−8.808
24.294
29.477

271
CB
TYR
34
−9.114
24.572
30.958

272
CG
TYR
34
−9.200
23.225
31.580

273
CD1
TYR
34
−8.092
22.664
32.159

274
CD2
TYR
34
−10.362
22.504
31.566

275
CE1
TYR
34
−8.149
21.410
32.723

276
CE2
TYR
34
−10.436
21.250
32.126

277
CZ
TYR
34
−9.319
20.705
32.707

278
OH
TYR
34
−9.377
19.417
33.283

279
C
TYR
34
−8.973
25.556
28.713

280
O
TYR
34
−8.646
25.627
27.532

281
N
LYS
35
−9.513
26.588
29.382

282
CA
LYS
35
−9.691
27.840
28.725

283
CB
LYS
35
−10.549
27.741
27.456

284
CG
LYS
35
−10.981
29.102
26.904

285
CD
LYS
35
−11.233
29.098
25.395

286
CE
LYS
35
−11.504
30.491
24.810

287
NZ
LYS
35
−12.737
30.467
23.993

288
C
LYS
35
−10.401
28.746
29.668

289
O
LYS
35
−11.552
28.522
30.027

290
N
GLY
36
−9.731
29.830
30.077

291
CA
GLY
36
−10.439
30.860
30.769

292
C
GLY
36
−10.621
30.450
32.188

293
O
GLY
36
−11.690
30.641
32.759

294
N
GLU
37
−9.558
29.915
32.807

295
CA
GLU
37
−9.452
29.961
34.236

296
CB
GLU
37
−10.051
31.257
34.851

297
CG
GLU
37
−9.611
31.529
36.290

298
CD
GLU
37
−10.258
32.831
36.731

299
OE1
GLU
37
−10.177
33.163
37.949

300
OE2
GLU
37
−10.861
33.507
35.858

301
C
GLU
37
−10.179
28.788
34.779

302
O
GLU
37
−9.554
27.860
35.289

303
N
ARG
38
−11.518
28.853
34.647

304
CA
ARG
38
−12.481
27.903
35.102

305
CB
ARG
38
−13.756
27.956
34.270

306
CG
ARG
38
−14.995
27.473
35.005

307
CD
ARG
38
−16.249
28.264
34.634

308
NE
ARG
38
−17.400
27.579
35.298

309
CZ
ARG
38
−18.435
27.078
34.556

310
NH1
ARG
38
−19.407
26.336
35.156

311
NH2
ARG
38
−18.476
27.296
33.213

312
C
ARG
38
−11.902
26.542
34.972

313
O
ARG
38
−11.222
26.228
33.994

314
N
VAL
39
−12.079
25.712
36.009

315
CA
VAL
39
−11.295
24.521
36.063

316
CB
VAL
39
−10.553
24.438
37.376

317
CG1
VAL
39
−9.800
23.109
37.476

318
CG2
VAL
39
−9.608
25.649
37.419

319
C
VAL
39
−12.234
23.384
35.852

320
O
VAL
39
−11.866
22.211
35.905

321
N
ASP
40
−13.490
23.723
35.512

322
CA
ASP
40
−14.369
22.729
34.972

323
CB
ASP
40
−15.738
23.260
34.507

324
CG
ASP
40
−16.828
22.975
35.530

325
OD1
ASP
40
−17.988
23.384
35.260

326
OD2
ASP
40
−16.539
22.373
36.595

327
C
ASP
40
−13.717
22.196
33.735

328
O
ASP
40
−12.725
22.740
33.248

329
N
GLY
41
−14.310
21.124
33.186

330
CA
GLY
41
−14.070
20.709
31.847

331
C
GLY
41
−15.419
20.721
31.221

332
O
GLY
41
−15.694
19.949
30.298

333
N
ASN
42
−16.284
21.603
31.763

334
CA
ASN
42
−17.509
22.027
31.156

335
CB
ASN
42
−17.882
23.429
31.655

336
CG
ASN
42
−19.385
23.645
31.645

337
OD1
ASN
42
−19.989
24.062
30.664

338
ND2
ASN
42
−20.000
23.396
32.826

339
C
ASN
42
−17.177
22.150
29.716

340
O
ASN
42
−17.755
21.488
28.854

341
N
ARG
43
−16.125
22.944
29.459

342
CA
ARG
43
−15.396
22.778
28.251

343
CB
ARG
43
−15.167
24.088
27.473

344
CG
ARG
43
−16.125
24.322
26.291

345
CD
ARG
43
−16.800
23.049
25.766

346
NE
ARG
43
−18.278
23.258
25.720

347
CZ
ARG
43
−18.880
24.090
24.821

348
NH1
ARG
43
−20.230
23.989
24.629

349
NH2
ARG
43
−18.154
24.999
24.107

350
C
ARG
43
−14.066
22.244
28.662

351
O
ARG
43
−13.178
22.986
29.074

352
N
GLN
44
−13.904
20.912
28.547

353
CA
GLN
44
−12.596
20.335
28.529

354
CB
GLN
44
−12.472
18.930
29.162

355
CG
GLN
44
−11.057
18.343
29.031

356
CD
GLN
44
−10.957
17.047
29.833

357
OE1
GLN
44
−10.677
17.045
31.037

358
NE2
GLN
44
−11.170
15.894
29.148

359
C
GLN
44
−12.243
20.199
27.087

360
O
GLN
44
−13.030
19.697
26.281

361
N
ILE
45
−11.030
20.685
26.756

362
CA
ILE
45
−10.515
20.589
25.429

363
CB
ILE
45
−9.363
21.505
25.173

364
CG2
ILE
45
−8.943
21.341
23.693

365
CG1
ILE
45
−9.715
22.928
25.614

366
CD1
ILE
45
−10.508
23.725
24.578

367
C
ILE
45
−9.919
19.248
25.352

368
O
ILE
45
−10.516
18.297
24.853

369
N
ILE
46
−8.680
19.176
25.854

370
CA
ILE
46
−7.699
18.254
25.372

371
CB
ILE
46
−6.516
19.040
24.847

372
CG2
ILE
46
−6.593
20.414
25.527

373
CG1
ILE
46
−5.141
18.373
25.000

374
CD1
ILE
46
−4.148
19.217
25.806

375
C
ILE
46
−7.316
17.365
26.511

376
O
ILE
46
−7.729
17.594
27.644

377
N
GLY
47
−6.540
16.297
26.250

378
CA
GLY
47
−6.033
15.577
27.382

379
C
GLY
47
−5.301
14.373
26.904

380
O
GLY
47
−5.776
13.248
27.041

381
N
TYR
48
−4.095
14.588
26.355

382
CA
TYR
48
−3.188
13.500
26.194

383
CB
TYR
48
−1.829
14.024
25.688

384
CG
TYR
48
−0.740
13.008
25.796

385
CD1
TYR
48
−0.042
12.877
26.977

386
CD2
TYR
48
−0.419
12.203
24.719

387
CE1
TYR
48
0.960
11.956
27.083

388
CE2
TYR
48
0.594
11.276
24.828

389
CZ
TYR
48
1.275
11.165
26.016

390
OH
TYR
48
2.315
10.231
26.164

391
C
TYR
48
−3.054
12.901
27.561

392
O
TYR
48
−3.286
13.570
28.574

393
N
VAL
49
−2.728
11.600
27.610

394
CA
VAL
49
−2.791
10.785
28.789

395
CB
VAL
49
−3.659
9.579
28.537

396
CG1
VAL
49
−3.734
8.740
29.820

397
CG2
VAL
49
−5.015
10.031
27.946

398
C
VAL
49
−1.402
10.253
28.972

399
O
VAL
49
−0.806
9.761
28.017

400
N
ILE
50
−0.803
10.318
30.172

401
CA
ILE
50
0.506
9.738
30.149

402
CB
ILE
50
1.517
10.415
31.029

403
CG2
ILE
50
1.313
10.066
32.518

404
CG1
ILE
50
2.916
10.112
30.472

405
CD1
ILE
50
3.893
11.267
30.638

406
C
ILE
50
0.374
8.309
30.550

407
O
ILE
50
−0.661
7.910
31.078

408
N
GLY
51
1.419
7.496
30.283

409
CA
GLY
51
1.374
6.094
30.588

410
C
GLY
51
0.998
5.386
29.328

411
O
GLY
51
1.574
5.642
28.268

412
N
THR
52
0.012
4.462
29.407

413
CA
THR
52
−0.538
3.959
28.185

414
CB
THR
52
−1.699
3.003
28.313

415
OG1
THR
52
−2.386
2.890
27.070

416
CG2
THR
52
−2.645
3.511
29.407

417
C
THR
52
−1.019
5.175
27.500

418
O
THR
52
−1.973
5.825
27.926

419
N
GLN
53
−0.304
5.554
26.441

420
CA
GLN
53
−0.474
6.876
25.940

421
CB
GLN
53
0.777
7.409
25.241

422
CG
GLN
53
2.065
7.273
26.041

423
CD
GLN
53
3.176
7.794
25.145

424
OE1
GLN
53
4.148
8.342
25.657

425
NE2
GLN
53
3.044
7.644
23.798

426
C
GLN
53
−1.550
6.826
24.921

427
O
GLN
53
−1.925
5.766
24.425

428
N
GLN
54
−2.084
8.006
24.600

429
CA
GLN
54
−3.267
8.106
23.827

430
CB
GLN
54
−4.337
7.090
24.292

431
CG
GLN
54
−5.798
7.534
24.351

432
CD
GLN
54
−6.631
6.282
24.102

433
OE1
GLN
54
−7.828
6.272
24.382

434
NE2
GLN
54
−6.003
5.204
23.547

435
C
GLN
54
−3.681
9.486
24.139

436
O
GLN
54
−3.045
10.144
24.957

437
N
ALA
55
−4.731
9.980
23.480

438
CA
ALA
55
−5.233
11.241
23.895

439
CB
ALA
55
−4.719
12.434
23.076

440
C
ALA
55
−6.679
11.126
23.678

441
O
ALA
55
−7.139
10.316
22.878

442
N
THR
56
−7.450
11.924
24.417

443
CA
THR
56
−8.844
11.843
24.199

444
CB
THR
56
−9.468
10.781
25.060

445
OG1
THR
56
−10.885
10.863
25.001

446
CG2
THR
56
−8.977
10.956
26.500

447
C
THR
56
−9.352
13.197
24.536

448
O
THR
56
−9.126
13.713
25.627

449
N
PRO
57
−10.009
13.824
23.618

450
CA
PRO
57
−10.504
15.141
23.833

451
CD
PRO
57
−10.444
13.243
22.361

452
CB
PRO
57
−11.009
15.642
22.493

453
CG
PRO
57
−10.926
14.444
21.524

454
C
PRO
57
−11.677
15.013
24.719

455
O
PRO
57
−11.837
13.988
25.379

456
N
GLY
58
−12.583
15.985
24.607

457
CA
GLY
58
−13.892
15.562
24.249

458
C
GLY
58
−14.574
16.748
23.658

459
O
GLY
58
−14.795
16.843
22.453

460
N
PRO
59
−14.970
17.613
24.537

461
CA
PRO
59
−16.211
18.267
24.255

462
CD
PRO
59
−14.781
17.352
25.948

463
CB
PRO
59
−16.980
18.335
25.576

464
CG
PRO
59
−16.177
17.495
26.572

465
C
PRO
59
−15.992
19.610
23.670

466
O
PRO
59
−16.962
20.223
23.230

467
N
ALA
60
−14.772
20.146
23.709

468
CA
ALA
60
−14.675
21.558
23.517

469
CB
ALA
60
−13.802
22.262
24.574

470
C
ALA
60
−14.074
21.831
22.183

471
O
ALA
60
−13.905
20.916
21.378

472
N
TYR
61
−13.767
23.120
21.916

473
CA
TYR
61
−13.358
23.500
20.593

474
CB
TYR
61
−13.036
24.986
20.415

475
CG
TYR
61
−13.922
25.541
19.333

476
CD1
TYR
61
−14.819
24.718
18.683

477
CD2
TYR
61
−13.860
26.861
18.944

478
CE1
TYR
61
−15.636
25.221
17.696

479
CE2
TYR
61
−14.672
27.377
17.955

480
CZ
TYR
61
−15.566
26.541
17.337

481
OH
TYR
61
−16.402
27.059
16.322

482
C
TYR
61
−12.143
22.717
20.279

483
O
TYR
61
−11.122
22.775
20.968

484
N
SER
62
−12.275
21.911
19.220

485
CA
SER
62
−11.235
21.040
18.797

486
CB
SER
62
−11.539
19.572
19.126

487
OG
SER
62
−10.354
18.785
19.095

488
C
SER
62
−11.247
21.184
17.325

489
O
SER
62
−11.267
20.209
16.579

490
N
GLY
63
−11.272
22.452
16.882

491
CA
GLY
63
−11.314
22.771
15.492

492
C
GLY
63
−9.907
22.787
15.017

493
O
GLY
63
−9.597
22.303
13.930

494
N
ARG
64
−8.998
23.354
15.826

495
CA
ARG
64
−7.643
23.306
15.383

496
CB
ARG
64
−7.302
24.362
14.324

497
CG
ARG
64
−8.503
25.211
13.925

498
CD
ARG
64
−8.355
26.687
14.299

499
NE
ARG
64
−9.721
27.254
14.413

500
CZ
ARG
64
−10.274
27.433
15.654

501
NH1
ARG
64
−9.535
27.196
16.765

502
NH2
ARG
64
−11.578
27.838
15.762

503
C
ARG
64
−6.757
23.529
16.556

504
O
ARG
64
−6.195
24.609
16.724

505
N
GLU
65
−6.591
22.487
17.387

506
CA
GLU
65
−5.559
22.529
18.371

507
CB
GLU
65
−6.013
23.127
19.711

508
CG
GLU
65
−6.478
24.583
19.539

509
CD
GLU
65
−7.387
24.950
20.697

510
OE1
GLU
65
−8.127
24.041
21.165

511
OE2
GLU
65
−7.341
26.124
21.150

512
C
GLU
65
−5.110
21.125
18.562

513
O
GLU
65
−5.672
20.196
17.987

514
N
ILE
66
−4.038
20.939
19.349

515
CA
ILE
66
−3.394
19.671
19.346

516
CB
ILE
66
−2.404
19.552
18.218

517
CG2
ILE
66
−1.675
18.200
18.308

518
CG1
ILE
66
−3.121
19.747
16.876

519
CD1
ILE
66
−2.147
19.793
15.697

520
C
ILE
66
−2.655
19.565
20.642

521
O
ILE
66
−2.362
20.564
21.296

522
N
ILE
67
−2.348
18.326
21.053

523
CA
ILE
67
−1.613
18.133
22.256

524
CB
ILE
67
−2.118
16.958
23.049

525
CG2
ILE
67
−2.316
15.793
22.062

526
CG1
ILE
67
−1.231
16.627
24.270

527
CD1
ILE
67
−0.957
17.852
25.153

528
C
ILE
67
−0.198
17.885
21.869

529
O
ILE
67
0.110
17.562
20.722

530
N
TYR
68
0.700
18.071
22.848

531
CA
TYR
68
2.056
17.642
22.752

532
CB
TYR
68
3.077
18.790
22.764

533
CG
TYR
68
3.094
19.298
21.375

534
CD1
TYR
68
4.056
18.852
20.501

535
CD2
TYR
68
2.133
20.186
20.952

536
CE1
TYR
68
4.092
19.298
19.204

537
CE2
TYR
68
2.169
20.631
19.655

538
CZ
TYR
68
3.139
20.195
18.786

539
OH
TYR
68
3.155
20.671
17.462

540
C
TYR
68
2.340
16.855
23.975

541
O
TYR
68
2.003
17.249
25.087

542
N
PRO
69
2.982
15.742
23.796

543
CA
PRO
69
3.351
14.882
24.878

544
CD
PRO
69
2.957
15.059
22.508

545
CB
PRO
69
4.119
13.728
24.220

546
CG
PRO
69
3.591
13.679
22.771

547
C
PRO
69
4.145
15.629
25.916

548
O
PRO
69
4.104
15.249
27.084

549
N
ASN
70
4.878
16.687
25.534

550
CA
ASN
70
5.619
17.408
26.530

551
CB
ASN
70
6.900
18.073
25.991

552
CG
ASN
70
6.661
18.462
24.544

553
OD1
ASN
70
7.480
18.152
23.679

554
ND2
ASN
70
5.529
19.168
24.266

555
C
ASN
70
4.718
18.483
27.053

556
O
ASN
70
5.168
19.560
27.437

557
N
ALA
71
3.406
18.183
27.095

558
CA
ALA
71
2.390
19.057
27.620

559
CB
ALA
71
2.360
19.107
29.157

560
C
ALA
71
2.562
20.443
27.083

561
O
ALA
71
2.860
21.388
27.817

562
N
SER
72
2.334
20.587
25.764

563
CA
SER
72
2.188
21.856
25.111

564
CB
SER
72
3.389
22.237
24.219

565
OG
SER
72
4.387
22.911
24.977

566
C
SER
72
1.010
21.695
24.193

567
O
SER
72
0.763
20.596
23.696

568
N
LEU
73
0.242
22.778
23.954

569
CA
LEU
73
−0.879
22.699
23.052

570
CB
LEU
73
−2.179
23.278
23.686

571
CG
LEU
73
−3.456
23.390
22.803

572
CD2
LEU
73
−4.212
24.686
23.145

573
CD1
LEU
73
−4.379
22.166
22.939

574
C
LEU
73
−0.515
23.523
21.859

575
O
LEU
73
0.049
24.605
22.009

576
N
LEU
74
−0.813
23.051
20.634

577
CA
LEU
74
−0.753
23.987
19.556

578
CB
LEU
74
−0.459
23.377
18.167

579
CG
LEU
74
−0.369
24.407
17.009

580
CD2
LEU
74
−0.948
23.849
15.698

581
CD1
LEU
74
1.063
24.937
16.824

582
C
LEU
74
−2.117
24.539
19.488

583
O
LEU
74
−3.078
23.842
19.808

584
N
ILE
75
−2.246
25.803
19.071

585
CA
ILE
75
−3.554
26.214
18.683

586
CB
ILE
75
−4.171
27.263
19.568

587
CG2
ILE
75
−3.053
28.151
20.117

588
CG1
ILE
75
−5.267
28.025
18.803

589
CD1
ILE
75
−5.831
29.221
19.571

590
C
ILE
75
−3.414
26.763
17.308

591
O
ILE
75
−2.697
27.739
17.083

592
N
GLN
76
−4.090
26.117
16.348

593
CA
GLN
76
−4.018
26.609
15.010

594
CB
GLN
76
−4.523
25.614
13.949

595
CG
GLN
76
−4.362
24.151
14.349

596
CD
GLN
76
−4.521
23.334
13.072

597
OE1
GLN
76
−5.516
22.639
12.888

598
NE2
GLN
76
−3.514
23.429
12.164

599
C
GLN
76
−4.863
27.830
14.955

600
O
GLN
76
−5.039
28.504
15.968

601
N
ASN
77
−5.373
28.156
13.750

602
CA
ASN
77
−5.716
29.507
13.419

603
CB
ASN
77
−6.312
29.693
12.014

604
CG
ASN
77
−5.504
28.832
11.058

605
OD1
ASN
77
−5.818
27.657
10.868

606
ND2
ASN
77
−4.454
29.419
10.426

607
C
ASN
77
−6.688
30.001
14.423

608
O
ASN
77
−7.542
29.257
14.900

609
N
ILE
78
−6.515
31.264
14.828

610
CA
ILE
78
−7.064
31.677
16.076

611
CB
ILE
78
−6.009
32.356
16.891

612
CG2
ILE
78
−6.669
33.043
18.090

613
CG1
ILE
78
−4.926
31.329
17.274

614
CD1
ILE
78
−3.507
31.901
17.321

615
C
ILE
78
−8.169
32.652
15.811

616
O
ILE
78
−9.342
32.364
16.037

617
N
ILE
79
−7.796
33.851
15.342

618
CA
ILE
79
−8.635
35.014
15.352

619
CB
ILE
79
−9.868
34.983
14.482

620
CG2
ILE
79
−9.814
33.762
13.558

621
CG1
ILE
79
−11.142
35.046
15.350

622
CD1
ILE
79
−12.423
35.382
14.575

623
C
ILE
79
−9.060
35.324
16.753

624
O
ILE
79
−9.075
34.467
17.642

625
N
GLN
80
−9.393
36.616
16.960

626
CA
GLN
80
−9.561
37.230
18.243

627
CB
GLN
80
−10.009
38.698
18.136

628
CG
GLN
80
−11.449
38.940
18.593

629
CD
GLN
80
−11.999
40.144
17.839

630
OE1
GLN
80
−13.138
40.522
18.082

631
NE2
GLN
80
−11.185
40.762
16.940

632
C
GLN
80
−10.574
36.479
19.034

633
O
GLN
80
−10.653
36.642
20.251

634
N
ASN
81
−11.381
35.636
18.361

635
CA
ASN
81
−12.413
34.888
19.028

636
CB
ASN
81
−13.069
33.831
18.112

637
CG
ASN
81
−14.495
34.266
17.791

638
OD1
ASN
81
−15.215
33.606
17.048

639
ND2
ASN
81
−14.919
35.418
18.365

640
C
ASN
81
−11.769
34.152
20.162

641
O
ASN
81
−12.185
34.271
21.312

642
N
ASP
82
−10.719
33.373
19.859

643
CA
ASP
82
−10.147
32.481
20.820

644
CB
ASP
82
−9.376
31.358
20.114

645
CG
ASP
82
−10.396
30.646
19.234

646
OD1
ASP
82
−11.363
30.057
19.794

647
OD2
ASP
82
−10.226
30.689
17.989

648
C
ASP
82
−9.190
33.210
21.715

649
O
ASP
82
−8.625
32.610
22.627

650
N
THR
83
−8.979
34.523
21.500

651
CA
THR
83
−8.001
35.201
22.298

652
CB
THR
83
−7.825
36.650
21.953

653
OG1
THR
83
−6.445
36.950
21.792

654
CG2
THR
83
−8.422
37.513
23.078

655
C
THR
83
−8.447
35.135
23.721

656
O
THR
63
−9.637
34.995
24.005

657
N
GLY
84
−7.491
35.239
24.664

658
CA
GLY
84
−7.883
35.251
26.036

659
C
GLY
84
−7.006
34.320
26.782

660
O
GLY
84
−5.853
34.086
26.430

661
N
PHE
85
−7.555
33.774
27.872

662
CA
PHE
85
−6.809
33.009
28.826

663
CB
PHE
85
−7.482
33.093
30.213

664
CG
PHE
85
−6.716
32.415
31.303

665
CD1
PHE
85
−5.416
32.718
31.625

666
CD2
PHE
85
−7.346
31.443
32.022

667
CE1
PHE
85
−4.762
32.035
32.639

668
CE2
PHE
85
−6.724
30.755
33.045

669
CZ
PHE
85
−5.420
31.054
33.355

670
C
PHE
85
−6.836
31.585
28.363

671
O
PHE
85
−7.721
31.158
27.617

672
N
TYR
86
−5.848
30.803
28.816

673
CA
TYR
86
−5.996
29.388
28.853

674
CB
TYR
86
−5.371
28.653
27.649

675
CG
TYR
86
−6.118
28.960
26.383

676
CD1
TYR
86
−5.478
29.586
25.342

677
CD2
TYR
86
−7.440
28.607
26.201

678
CE1
TYR
86
−6.134
29.870
24.162

679
CE2
TYR
86
−8.094
28.892
25.022

680
CZ
TYR
86
−7.457
29.523
23.986

681
OH
TYR
86
−8.142
29.801
22.786

682
C
TYR
86
−5.278
28.974
30.094

683
O
TYR
86
−4.324
29.622
30.529

684
N
THE
87
−5.756
27.888
30.719

685
CA
THR
87
−5.156
27.393
31.919

686
CB
THR
87
−6.115
27.319
33.062

687
OG1
THR
87
−5.475
26.800
34.222

688
CG2
THR
87
−7.248
26.378
32.631

689
C
THR
87
−4.799
25.979
31.626

690
O
THR
87
−5.218
25.434
30.608

691
N
LEU
88
−4.026
25.331
32.508

692
CA
LEU
88
−3.703
23.972
32.208

693
CB
LEU
88
−2.288
23.815
31.629

694
CG
LEU
88
−1.877
22.361
31.382

695
CD2
LEU
88
−0.623
21.994
32.195

696
CD1
LEU
88
−1.744
22.064
29.872

697
C
LEU
88
−3.785
23.225
33.487

698
O
LEU
88
−3.594
23.805
34.556

699
N
HIS
89
−4.126
21.927
33.407

700
CA
HIS
89
−4.428
21.216
34.607

701
ND1
HIS
89
−5.704
22.580
37.047

702
CG
HIS
89
−6.295
21.582
36.309

703
CB
HIS
89
−5.932
21.198
34.917

704
NE2
HIS
89
−7.242
21.638
38.349

705
CD2
HIS
89
−7.234
21.024
37.116

706
CE1
HIS
89
−6.308
22.569
38.266

707
C
HIS
89
−3.959
19.817
34.393

708
O
HIS
89
−3.901
19.313
33.266

709
N
VAL
90
−3.522
19.175
35.490

710
CA
VAL
90
−2.777
17.963
35.335

711
CB
VAL
90
−1.288
18.186
35.243

712
CG1
VAL
90
−0.749
17.563
33.944

713
CG2
VAL
90
−1.042
19.696
35.361

714
C
VAL
90
−3.016
17.151
36.550

715
O
VAL
90
−2.721
17.611
37.646

716
N
ILE
91
−3.542
15.925
36.405

717
CA
ILE
91
−3.611
15.036
37.528

718
CB
ILE
91
−4.501
13.849
37.243

719
CG2
ILE
91
−4.710
13.022
38.539

720
CG1
ILE
91
−5.814
14.367
36.605

721
CD1
ILE
91
−6.140
13.815
35.203

722
C
ILE
91
−2.230
14.496
37.765

723
O
ILE
91
−1.325
14.625
36.941

724
N
LYS
92
−2.043
13.884
38.942

725
CA
LYS
92
−1.495
12.574
39.052

726
CB
LYS
92
0.002
12.440
39.429

727
CG
LYS
92
0.904
13.670
39.306

728
CD
LYS
92
2.314
13.457
39.896

729
CE
LYS
92
3.380
14.448
39.396

730
NZ
LYS
92
4.055
15.075
40.566

731
C
LYS
92
−2.193
11.998
40.217

732
O
LYS
92
−2.948
12.698
40.882

733
N
SER
93
−1.963
10.710
40.519

734
CA
SER
93
−2.577
10.255
41.717

735
CB
SER
93
−2.798
8.733
41.755

736
OG
SER
93
−4.180
8.448
41.608

737
C
SER
93
−1.657
10.607
42.832

738
O
SER
93
−0.859
9.777
43.263

739
N
ASP
94
−1.737
11.855
43.337

740
CA
ASP
94
−1.038
12.125
44.564

741
CB
ASP
94
0.464
11.801
44.538

742
CG
ASP
94
0.740
11.161
45.890

743
OD1
ASP
94
1.220
9.992
45.909

744
OD2
ASP
94
0.441
11.818
46.922

745
C
ASP
94
−1.176
13.563
44.940

746
O
ASP
94
−1.147
13.906
46.121

747
N
LEU
95
−1.321
14.455
43.949

748
CA
LEU
95
−1.713
15.794
44.231

749
CB
LEU
95
−0.567
16.711
44.694

750
CG
LEU
95
−0.988
17.819
45.698

751
CD2
LEU
95
−1.637
17.222
46.956

752
CD1
LEU
95
−1.829
18.926
45.038

753
C
LEU
95
−2.130
16.299
42.913

754
O
LEU
95
−1.542
15.937
41.896

755
N
VAL
96
−3.177
17.117
42.876

756
CA
VAL
96
−3.505
17.607
41.595

757
CB
VAL
96
−4.978
17.649
41.406

758
CG1
VAL
96
−5.286
17.203
39.972

759
CG2
VAL
96
−5.602
16.701
42.452

760
C
VAL
96
−2.893
18.953
41.524

761
O
VAL
96
−2.832
19.689
42.511

762
N
ASN
97
−2.345
19.297
40.352

763
CA
ASN
97
−1.682
20.552
40.286

764
CB
ASN
97
−0.226
20.463
39.824

765
CG
ASN
97
0.563
20.538
41.111

766
OD1
ASN
97
1.685
21.034
41.155

767
ND2
ASN
97
−0.081
20.058
42.209

768
C
ASN
97
−2.422
21.354
39.287

769
O
ASN
97
−3.246
20.819
38.546

770
N
GLU
98
−2.162
22.668
39.243

771
CA
GLU
98
−2.777
23.418
38.196

772
CB
GLU
98
−3.904
24.358
38.662

773
CG
GLU
98
−4.365
25.273
37.517

774
CD
GLU
98
−5.864
25.548
37.595

775
OE1
GLU
98
−6.442
25.943
36.550

776
OE2
GLU
98
−6.446
25.393
38.709

777
C
GLU
98
−1.715
24.278
37.656

778
O
GLU
98
−1.142
23.968
36.610

779
N
GLU
99
−1.445
25.367
38.409

780
CA
GLU
99
−0.702
26.542
38.074

781
CB
GLU
99
0.542
26.788
38.916

782
CG
GLU
99
1.320
27.911
38.247

783
CD
GLU
99
2.633
28.034
38.977

784
OE1
GLU
99
3.147
26.980
39.440

785
OE2
GLU
99
3.137
29.186
39.093

786
C
GLU
99
−0.249
26.535
36.656

787
O
GLU
99
0.602
25.750
36.245

788
N
ALA
100
−0.841
27.454
35.886

789
CA
ALA
100
−0.682
27.394
34.480

790
CB
ALA
100
−1.503
26.256
33.855

791
C
ALA
100
−1.253
28.669
33.984

792
O
ALA
100
−2.342
28.693
33.413

793
N
THR
101
−0.542
29.784
34.218

794
CA
THR
101
−1.001
31.041
33.727

795
CB
THR
101
−0.699
32.158
34.680

796
OG1
THR
101
−1.041
31.734
35.990

797
CG2
THR
101
−1.506
33.415
34.303

798
C
THR
101
−0.318
31.283
32.421

799
O
THR
101
0.668
30.622
32.094

800
N
GLY
102
−0.846
32.217
31.615

801
CA
GLY
102
−0.335
32.374
30.283

802
C
GLY
102
−1.485
32.838
29.451

803
O
GLY
102
−2.486
32.144
29.291

804
N
GLN
103
−1.357
34.058
28.903

805
CA
GLN
103
−2.394
34.611
28.097

806
CB
GLN
103
−3.087
35.797
28.792

807
CG
GLN
103
−4.049
36.626
27.942

808
CD
GLN
103
−4.555
37.749
28.841

809
OE1
GLN
103
−5.495
38.470
28.509

810
NE2
GLN
103
−3.908
37.906
30.024

811
C
GLN
103
−1.705
35.127
26.884

812
O
GLN
103
−0.477
35.166
26.830

813
N
PHE
104
−2.474
35.540
25.865

814
CA
PHE
104
−1.868
36.247
24.781

815
CB
PHE
104
−1.306
35.337
23.673

816
CG
PHE
104
−2.423
34.461
23.239

817
CD1
PHE
104
−2.635
33.255
23.871

818
CD2
PHE
104
−3.280
34.834
22.223

819
CE1
PHE
104
−3.657
32.422
23.482

820
CE2
PHE
104
−4.302
33.996
21.839

821
CZ
PHE
104
−4.501
32.797
22.472

822
C
PHE
104
−2.944
37.087
24.185

823
O
PHE
104
−4.071
37.115
24.676

824
N
ARG
105
−2.623
37.806
23.100

825
CA
ARG
105
−3.641
38.575
22.463

826
CB
ARG
105
−3.438
40.089
22.635

827
CG
ARG
105
−3.582
40.516
24.098

828
CD
ARG
105
−2.503
41.485
24.573

829
NE
ARG
105
−3.003
42.070
25.847

830
CZ
ARG
105
−2.314
43.078
26.457

831
NH1
ARG
105
−2.706
43.477
27.701

832
NH2
ARG
105
−1.243
43.654
25.845

833
C
ARG
105
−3.599
38.231
21.013

834
O
ARG
105
−2.685
37.544
20.556

835
N
VAL
106
−4.614
38.674
20.251

836
CA
VAL
106
−4.529
38.444
18.845

837
CB
VAL
106
−5.655
37.653
18.289

838
CG1
VAL
106
−6.925
38.471
18.583

839
CG2
VAL
106
−5.389
37.414
16.788

840
C
VAL
106
−4.654
39.763
18.184

841
O
VAL
106
−5.299
40.681
18.698

842
N
TYR
107
−4.019
39.890
17.017

843
CA
TYR
107
−4.062
41.174
16.427

844
CB
TYR
107
−2.740
41.935
16.635

845
CG
TYR
107
−2.624
42.209
18.121

846
CD1
TYR
107
−1.740
41.509
18.921

847
CD2
TYR
107
−3.389
43.172
18.742

848
CE1
TYR
107
−1.639
41.782
20.280

849
CE2
TYR
107
−3.294
43.438
20.088

850
CZ
TYR
107
−2.396
42.749
20.878

851
OH
TYR
107
−2.278
43.023
22.259

852
C
TYR
107
−4.376
41.021
14.961

853
O
TYR
107
−4.153
39.992
14.332

854
N
PRO
108
−4.968
42.095
14.492

855
CA
PRO
108
−5.712
42.110
13.262

856
CD
PRO
108
−5.555
43.024
15.449

857
CB
PRO
108
−7.114
42.627
13.578

858
CG
PRO
108
−7.016
43.207
15.010

859
C
PRO
108
−5.071
43.114
12.348

860
O
PRO
108
−5.262
44.295
12.621

861
N
GLU
109
−4.342
42.665
11.303

862
CA
GLU
109
−3.538
43.411
10.358

863
CB
GLU
109
−3.599
42.809
8.944

864
CG
GLU
109
−3.634
41.279
8.941

865
CD
GLU
109
−5.058
40.813
9.202

866
OE1
GLU
109
−5.207
39.863
10.008

867
OE2
GLU
109
−6.020
41.386
8.609

868
C
GLU
109
−3.902
44.862
10.241

869
O
GLU
109
−5.071
45.245
10.284

870
N
LEU
110
−2.886
45.733
10.044

871
CA
LEU
110
−3.172
47.139
10.113

872
CB
LEU
110
−2.340
47.913
11.157

873
CG
LEU
110
−2.457
49.441
10.958

874
CD2
LEU
110
−1.150
50.137
11.358

875
CD1
LEU
110
−3.724
50.034
11.606

876
C
LEU
110
−2.950
47.832
8.795

877
O
LEU
110
−1.862
47.881
8.212

878
N
PRO
111
−4.049
48.424
8.404

879
CA
PRO
111
−4.240
49.147
7.174

880
CD
PRO
111
−5.283
48.142
9.107

881
CB
PRO
111
−5.665
49.696
7.258

882
CG
PRO
111
−6.393
48.836
8.309

883
C
PRO
111
−3.236
50.252
7.004

884
O
PRO
111
−2.340
50.372
7.836

885
N
LYS
112
−3.365
51.061
5.933

886
CA
LYS
112
−2.493
52.188
5.757

887
CB
LYS
112
−1.986
52.355
4.312

888
CG
LYS
112
−0.931
53.449
4.153

889
CD
LYS
112
−0.515
53.718
2.706

890
CE
LYS
112
0.409
54.931
2.584

891
NZ
LYS
112
1.242
54.825
1.365

892
C
LYS
112
−3.281
53.402
6.087

893
O
LYS
112
−4.421
53.537
5.636

894
N
PRO
113
−2.731
54.296
6.867

895
CA
PRO
113
−3.368
55.540
7.180

896
CD
PRO
113
−1.526
54.065
7.634

897
CB
PRO
113
−2.642
56.125
8.393

898
CG
PRO
113
−1.607
55.067
8.810

899
C
PRO
113
−3.216
56.431
5.991

900
O
PRO
113
−2.464
56.090
5.075

901
N
SER
114
−3.914
57.580
5.998

902
CA
SER
114
−3.648
58.574
5.006

903
CB
SER
114
−4.575
58.491
3.779

904
OG
SER
114
−3.962
59.107
2.655

905
C
SER
114
−3.867
59.873
5.701

906
O
SER
114
−4.841
60.023
6.438

907
N
ILE
115
−2.930
60.820
5.520

908
CA
ILE
115
−2.909
61.986
6.338

909
CB
ILE
115
−1.541
62.255
6.870

910
CG2
ILE
115
−0.622
62.544
5.675

911
CG1
ILE
115
−1.570
63.380
7.914

912
CD1
ILE
115
−0.283
64.194
7.924

913
C
ILE
115
−3.307
63.143
5.496

914
O
ILE
115
−3.022
63.186
4.299

915
N
SER
116
−4.004
64.120
6.108

916
CA
SER
116
−4.337
65.309
5.392

917
CB
SER
116
−5.856
65.530
5.240

918
OG
SER
116
−6.131
66.570
4.311

919
C
SER
116
−3.775
66.452
6.175

920
O
SER
116
−3.793
66.459
7.405

921
N
SER
117
−3.251
67.463
5.469

922
CA
SER
117
−2.979
68.702
6.123

923
CB
SER
117
−1.490
69.078
6.160

924
OG
SER
117
−1.371
70.466
6.432

925
C
SER
117
−3.660
69.737
5.305

926
O
SER
117
−3.889
69.556
4.106

927
N
ASN
118
−4.009
70.870
5.934

928
CA
ASN
118
−4.515
71.924
5.117

929
CB
ASN
118
−5.792
72.585
5.668

930
CG
ASN
118
−6.728
72.663
4.474

931
OD1
ASN
118
−7.889
73.063
4.559

932
ND2
ASN
118
−6.183
72.242
3.297

933
C
ASN
118
−3.456
72.965
4.980

934
O
ASN
118
−2.807
73.313
5.965

935
N
ASN
119
−3.287
73.472
3.737

936
CA
ASN
119
−2.389
74.541
3.429

937
CB
ASN
119
−2.715
75.826
4.228

938
CG
ASN
119
−2.726
77.026
3.295

939
OD1
ASN
119
−2.356
76.927
2.128

940
ND2
ASN
119
−3.176
78.191
3.829

941
C
ASN
119
−0.997
74.113
3.768

942
O
ASN
119
−0.631
74.004
4.936

943
N
SER
120
−0.159
73.891
2.741

944
CA
SER
120
1.227
73.629
3.003

945
CB
SER
120
1.825
72.593
2.051

946
OG
SER
120
3.225
72.475
2.275

947
C
SER
120
1.948
74.913
2.774

948
O
SER
120
2.777
75.327
3.587

949
N
LYS
121
1.577
75.573
1.658

950
CA
LYS
121
1.900
76.952
1.469

951
CB
LYS
121
1.066
77.630
0.367

952
CG
LYS
121
1.773
78.770
−0.370

953
CD
LYS
121
0.868
79.960
−0.696

954
CE
LYS
121
1.473
81.316
−0.302

955
NZ
LYS
121
0.577
82.421
−0.734

956
C
LYS
121
1.549
77.590
2.769

957
O
LYS
121
0.451
77.395
3.272

958
N
PRO
122
2.514
78.312
3.271

959
CA
PRO
122
2.601
78.806
4.614

960
CD
PRO
122
3.550
78.850
2.416

961
CB
PRO
122
3.212
80.190
4.494

962
CG
PRO
122
3.927
80.177
3.092

963
C
PRO
122
1.331
78.803
5.411

964
O
PRO
122
0.380
79.494
5.046

965
N
VAL
123
1.309
78.079
6.542

966
CA
VAL
123
1.025
78.686
7.794

967
CB
VAL
123
0.918
77.661
8.842

968
CG1
VAL
123
−0.536
77.201
8.825

969
CG2
VAL
123
1.926
76.562
8.478

970
C
VAL
123
2.224
79.525
8.043

971
O
VAL
123
3.352
79.047
7.967

972
N
GLU
124
2.020
80.832
8.307

973
CA
GLU
124
3.172
81.669
8.449

974
CB
GLU
124
2.866
83.178
8.333

975
CG
GLU
124
2.144
83.456
7.014

976
CD
GLU
124
1.160
84.561
7.251

977
OE1
GLU
124
0.895
85.315
6.274

978
OE2
GLU
124
0.654
84.665
8.393

979
C
GLU
124
3.820
81.344
9.748

980
O
GLU
124
3.520
80.320
10.369

981
N
ASP
125
4.776
82.179
10.166

982
CA
ASP
125
5.386
81.820
11.393

983
CB
ASP
125
6.713
82.547
11.677

984
CG
ASP
125
7.789
81.467
11.750

985
OD1
ASP
125
8.740
81.622
12.568

986
OD2
ASP
125
7.669
80.458
11.019

987
C
ASP
125
4.388
82.158
12.437

988
O
ASP
125
3.532
83.027
12.260

989
N
LYS
126
4.462
81.416
13.553

990
CA
LYS
126
3.446
81.443
14.550

991
CB
LYS
126
3.443
82.732
15.392

992
CG
LYS
126
2.727
82.602
16.746

993
CD
LYS
126
2.985
83.784
17.695

994
CE
LYS
126
2.001
84.953
17.522

995
NZ
LYS
126
1.545
85.469
18.836

996
C
LYS
126
2.121
81.301
13.875

997
O
LYS
126
1.168
82.022
14.171

998
N
ASP
127
2.020
80.313
12.971

999
CA
ASP
127
0.746
79.869
12.493

1000
CB
ASP
127
0.560
80.109
10.992

1001
CG
ASP
127
0.011
81.545
10.862

1002
OD1
ASP
127
−0.563
82.048
11.870

1003
OD2
ASP
127
0.117
82.170
9.778

1004
C
ASP
127
0.664
78.416
12.832

1005
O
ASP
127
1.359
77.966
13.734

1006
N
ALA
128
−0.223
77.632
12.194

1007
CA
ALA
128
−0.518
76.456
12.959

1008
CB
ALA
128
−1.633
76.694
13.985

1009
C
ALA
128
−1.017
75.351
12.091

1010
O
ALA
128
−2.223
75.223
11.876

1011
N
VAL
129
−0.107
74.471
11.630

1012
CA
VAL
129
−0.585
73.258
11.035

1013
CB
VAL
129
0.487
72.264
10.671

1014
CG1
VAL
129
0.137
71.566
9.354

1015
CG2
VAL
129
1.834
72.984
10.601

1016
C
VAL
129
−1.396
72.547
12.062

1017
O
VAL
129
−1.086
72.590
13.251

1018
N
ALA
130
−2.434
71.831
11.609

1019
CA
ALA
130
−2.852
70.689
12.357

1020
CB
ALA
130
−4.210
70.865
13.051

1021
C
ALA
130
−3.004
69.607
11.344

1022
O
ALA
130
−3.902
69.657
10.500

1023
N
PHE
131
−2.098
68.609
11.388

1024
CA
PHE
131
−2.210
67.510
10.483

1025
CB
PHE
131
−0.927
66.670
10.393

1026
CG
PHE
131
0.150
67.498
9.785

1027
CD1
PHE
131
−0.096
68.269
8.671

1028
CD2
PHE
131
1.413
67.503
10.333

1029
CE1
PHE
131
0.903
69.016
8.104

1030
CE2
PHE
131
2.416
68.258
9.772

1031
CZ
PHE
131
2.162
69.014
8.660

1032
C
PHE
131
−3.290
66.634
11.039

1033
O
PHE
131
−3.893
66.975
12.055

1034
N
THR
132
−3.553
65.488
10.379

1035
CA
THR
132
−4.426
64.478
10.913

1036
CB
THR
132
−5.887
64.814
10.857

1037
OG1
THR
132
−6.196
65.869
11.747

1038
CG2
THR
132
−6.686
63.559
11.250

1039
C
THR
132
−4.286
63.268
10.049

1040
O
THR
132
−4.485
63.347
8.838

1041
N
CYS
133
−3.948
62.115
10.665

1042
CA
CYS
133
−3.904
60.858
9.966

1043
CB
CYS
133
−3.066
59.799
10.718

1044
SG
CYS
133
−3.858
58.174
10.804

1045
C
CYS
133
−5.322
60.376
9.928

1046
O
CYS
133
−6.132
60.760
10.772

1047
N
GLU
134
−5.673
59.538
8.927

1048
CA
GLU
134
−6.973
58.931
8.968

1049
CB
GLU
134
−7.988
59.407
7.926

1050
CG
GLU
134
−8.135
60.915
7.792

1051
CD
GLU
134
−9.074
61.140
6.629

1052
OE1
GLU
134
−9.334
62.317
6.282

1053
OE2
GLU
134
−9.552
60.116
6.072

1054
C
GLU
134
−6.801
57.471
8.701

1055
O
GLU
134
−6.000
57.037
7.872

1056
N
PRO
135
−7.574
56.725
9.423

1057
CA
PRO
135
−7.161
55.379
9.658

1058
CD
PRO
135
−7.949
57.348
10.676

1059
CB
PRO
135
−6.511
55.397
11.029

1060
CG
PRO
135
−7.040
56.679
11.718

1061
C
PRO
135
−8.398
54.557
9.743

1062
O
PRO
135
−9.482
55.108
9.918

1063
N
GLU
136
−8.278
53.225
9.669

1064
CA
GLU
136
−9.500
52.514
9.885

1065
CB
GLU
136
−10.291
52.250
8.585

1066
CG
GLU
136
−11.765
52.668
8.709

1067
CD
GLU
136
−12.384
53.025
7.348

1068
OE1
GLU
136
−13.604
53.344
7.358

1069
OE2
GLU
136
−11.688
52.979
6.298

1070
C
GLU
136
−9.201
51.228
10.568

1071
O
GLU
136
−9.016
50.196
9.921

1072
N
THR
137
−9.160
51.265
11.920

1073
CA
THR
137
−8.949
50.086
12.708

1074
CB
THR
137
−7.682
49.395
12.342

1075
OG1
THR
137
−7.336
48.461
13.353

1076
CG2
THR
137
−6.608
50.494
12.200

1077
C
THR
137
−8.798
50.523
14.140

1078
O
THR
137
−8.491
51.679
14.433

1079
N
GLN
138
−9.033
49.590
15.080

1080
CA
GLN
138
−8.922
49.938
16.470

1081
CB
GLN
138
−10.246
49.820
17.258

1082
CG
GLN
138
−10.970
48.484
17.085

1083
CD
GLN
138
−12.367
48.683
17.665

1084
OE1
GLN
138
−12.664
49.800
18.079

1085
NE2
GLN
138
−13.209
47.617
17.736

1086
C
GLN
138
−7.920
49.035
17.111

1087
O
GLN
138
−7.519
48.013
16.550

1088
N
ASP
139
−7.500
49.432
18.327

1089
CA
ASP
139
−6.446
48.866
19.120

1090
CB
ASP
139
−6.452
47.330
19.191

1091
CG
ASP
139
−5.896
46.965
20.574

1092
OD1
ASP
139
−5.276
45.877
20.685

1093
OD2
ASP
139
−6.063
47.771
21.536

1094
C
ASP
139
−5.138
49.347
18.586

1095
O
ASP
139
−4.139
48.619
18.584

1096
N
ALA
140
−5.115
50.609
18.123

1097
CA
ALA
140
−3.955
51.134
17.472

1098
CB
ALA
140
−4.276
52.156
16.364

1099
C
ALA
140
−3.102
51.851
18.470

1100
O
ALA
140
−3.370
51.842
19.671

1101
N
THR
141
−2.037
52.492
17.953

1102
CA
THR
141
−1.035
53.172
18.721

1103
CB
THR
141
−0.133
52.205
19.425

1104
OG1
THR
141
1.118
52.792
19.740

1105
CG2
THR
141
0.065
50.984
18.512

1106
C
THR
141
−0.231
53.952
17.728

1107
O
THR
141
0.731
53.440
17.149

1108
N
TYR
142
−0.648
55.208
17.494

1109
CA
TYR
142
−0.183
56.022
16.404

1110
CB
TYR
142
−1.165
57.173
16.119

1111
CG
TYR
142
−0.717
58.109
15.030

1112
CD1
TYR
142
−0.637
57.703
13.712

1113
CD2
TYR
142
−0.389
59.415
15.347

1114
CE1
TYR
142
−0.234
58.609
12.760

1115
CE2
TYR
142
0.014
60.324
14.396

1116
CZ
TYR
142
0.095
59.910
13.086

1117
OH
TYR
142
0.506
60.799
12.070

1118
C
TYR
142
1.117
56.644
16.808

1119
O
TYR
142
1.378
56.888
17.987

1120
N
LEU
143
1.989
56.941
15.823

1121
CA
LEU
143
3.055
57.837
16.143

1122
CB
LEU
143
4.433
57.177
16.360

1123
CG
LEU
143
4.746
57.012
17.860

1124
CD2
LEU
143
6.259
56.943
18.119

1125
CD1
LEU
143
3.969
55.842
18.481

1126
C
LEU
143
3.185
58.846
15.039

1127
O
LEU
143
2.655
58.664
13.944

1128
N
TRP
144
3.879
59.964
15.325

1129
CA
TRP
144
4.060
61.028
14.371

1130
CB
TRP
144
3.721
62.410
14.974

1131
CG
TRP
144
2.260
62.807
14.961

1132
CD2
TRP
144
1.584
63.287
13.793

1133
CD1
TRP
144
1.327
62.792
15.964

1134
NE1
TRP
144
0.112
63.218
15.477

1135
CE2
TRP
144
0.257
63.528
14.143

1136
CE3
TRP
144
2.039
63.501
12.518

1137
CZ2
TRP
144
−0.643
63.985
13.223

1138
CZ3
TRP
144
1.133
63.979
11.601

1139
CH2
TRP
144
−0.182
64.214
11.942

1140
C
TRP
144
5.517
61.023
13.996

1141
O
TRP
144
6.347
60.580
14.789

1142
N
TRP
145
5.888
61.501
12.781

1143
CA
TRP
145
7.281
61.476
12.393

1144
CB
TRP
145
7.675
60.261
11.518

1145
CG
TRP
145
7.338
58.887
12.069

1146
CD2
TRP
145
7.875
58.354
13.288

1147
CD1
TRP
145
6.529
57.918
11.556

1148
NE1
TRP
145
6.521
56.815
12.376

1149
CE2
TRP
145
7.345
57.072
13.452

1150
CE3
TRP
145
8.733
58.887
14.199

1151
CZ2
TRP
145
7.675
56.309
14.532

1152
CZ3
TRP
145
9.063
58.116
15.294

1153
CH2
TRP
145
8.539
56.851
15.457

1154
C
TRP
145
7.597
62.682
11.556

1155
O
TRP
145
6.693
63.350
11.056

1156
N
VAL
146
8.908
62.992
11.385

1157
CA
VAL
146
9.323
64.139
10.626

1158
CB
VAL
146
9.649
65.359
11.443

1159
CG1
VAL
146
9.919
66.511
10.460

1160
CG2
VAL
146
8.519
65.641
12.441

1161
C
VAL
146
10.599
63.814
9.914

1162
O
VAL
146
11.601
63.461
10.535

1163
N
ASN
147
10.586
63.959
8.578

1164
CA
ASN
147
11.746
63.685
7.778

1165
CB
ASN
147
12.902
64.687
7.963

1166
CG
ASN
147
12.796
65.750
6.875

1167
OD1
ASN
147
13.633
66.645
6.769

1168
ND2
ASN
147
11.740
65.644
6.030

1169
C
ASN
147
12.262
62.334
8.122

1170
O
ASN
147
13.466
62.085
8.068

1171
N
ASN
148
11.343
61.414
8.452

1172
CA
ASN
148
11.727
60.052
8.619

1173
CB
ASN
148
12.484
59.489
7.414

1174
CG
ASN
148
12.508
57.979
7.548

1175
OD1
ASN
148
13.260
57.304
6.850

1176
ND2
ASN
148
11.685
57.433
8.477

1177
C
ASN
148
12.646
59.979
9.776

1178
O
ASN
148
13.570
59.168
9.788

1179
N
GLN
149
12.395
60.812
10.804

1180
CA
GLN
149
12.975
60.475
12.070

1181
CB
GLN
149
14.480
60.809
12.234

1182
CG
GLN
149
15.313
59.535
12.486

1183
CD
GLN
149
16.812
59.691
12.189

1184
OE1
GLN
149
17.313
60.680
11.664

1185
NE2
GLN
149
17.560
58.636
12.584

1186
C
GLN
149
12.157
61.090
13.154

1187
O
GLN
149
11.014
61.479
12.929

1188
N
SER
150
12.685
61.119
14.388

1189
CA
SER
150
11.738
61.139
15.458

1190
CB
SER
150
12.320
60.824
16.832

1191
OG
SER
150
11.271
60.552
17.750

1192
C
SER
150
11.164
62.506
15.559

1193
O
SER
150
11.556
63.399
14.804

1194
N
LEU
151
10.186
62.694
16.464

1195
CA
LEU
151
9.900
64.048
16.751

1196
CB
LEU
151
8.535
64.615
16.341

1197
CG
LEU
151
8.640
66.156
16.461

1198
CD2
LEU
151
7.410
66.880
17.049

1199
CD1
LEU
151
9.155
66.740
15.140

1200
C
LEU
151
9.788
64.119
18.210

1201
O
LEU
151
8.660
63.899
18.660

1202
N
PRO
152
10.888
64.445
18.911

1203
CA
PRO
152
10.779
65.395
19.997

1204
CD
PRO
152
12.133
64.690
18.191

1205
CB
PRO
152
11.364
66.682
19.442

1206
CG
PRO
152
12.512
66.136
18.558

1207
C
PRO
152
9.419
65.483
20.654

1208
O
PRO
152
9.121
64.618
21.481

1209
N
VAL
153
8.557
66.441
20.256

1210
CA
VAL
153
7.418
66.894
21.019

1211
CB
VAL
153
6.960
66.110
22.223

1212
CG1
VAL
153
5.911
66.956
22.969

1213
CG2
VAL
153
6.428
64.730
21.824

1214
C
VAL
153
7.876
68.155
21.639

1215
O
VAL
153
8.935
68.195
22.260

1216
N
SER
154
7.128
69.245
21.491

1217
CA
SER
154
7.696
70.378
22.124

1218
CB
SER
154
8.600
71.198
21.198

1219
OG
SER
154
9.074
70.387
20.139

1220
C
SER
154
6.542
71.220
22.520

1221
O
SER
154
5.432
70.984
22.036

1222
N
PRO
155
6.765
72.150
23.394

1223
CA
PRO
155
5.644
72.723
24.066

1224
CD
PRO
155
7.921
72.063
24.291

1225
CB
PRO
155
6.220
73.559
25.196

1226
CG
PRO
155
7.501
72.815
25.573

1227
C
PRO
155
4.731
73.462
23.138

1228
O
PRO
155
3.722
73.970
23.625

1229
N
ARG
156
5.016
73.528
21.817

1230
CA
ARG
156
4.089
74.154
20.920

1231
CB
ARG
156
4.751
74.960
19.792

1232
CG
ARG
156
6.174
74.492
19.518

1233
CD
ARG
156
6.810
75.111
18.277

1234
NE
ARG
156
7.830
74.139
17.797

1235
CZ
ARG
156
8.375
74.276
16.549

1236
NH1
ARG
156
8.045
75.361
15.791

1237
NH2
ARG
156
9.233
73.327
16.065

1238
C
ARG
156
3.238
73.119
20.247

1239
O
ARG
156
2.238
73.481
19.617

1240
N
LEU
157
3.580
71.811
20.351

1241
CA
LEU
157
2.705
70.846
19.730

1242
CB
LEU
157
3.411
69.552
19.249

1243
CG
LEU
157
4.457
69.808
18.146

1244
CD2
LEU
157
4.706
68.568
17.256

1245
CD1
LEU
157
5.754
70.378
18.734

1246
C
LEU
157
1.605
70.477
20.676

1247
O
LEU
157
1.613
70.833
21.857

1248
N
GLN
158
0.599
69.774
20.134

1249
CA
GLN
158
−0.585
69.475
20.872

1250
CB
GLN
158
−1.544
70.689
20.933

1251
CG
GLN
158
−2.269
70.909
22.270

1252
CD
GLN
158
−3.467
71.845
22.070

1253
OE1
GLN
158
−4.613
71.452
22.289

1254
NE2
GLN
158
−3.200
73.117
21.655

1255
C
GLN
158
−1.272
68.426
20.067

1256
O
GLN
158
−1.800
68.711
18.995

1257
N
LEU
159
−1.277
67.166
20.521

1258
CA
LEU
159
−2.049
66.261
19.727

1259
CB
LEU
159
−1.301
65.015
19.214

1260
CG
LEU
159
−0.351
64.364
20.224

1261
CD2
LEU
159
1.039
65.003
20.199

1262
CD1
LEU
159
−0.299
62.854
19.997

1263
C
LEU
159
−3.202
65.803
20.553

1264
O
LEU
159
−3.299
66.088
21.749

1265
N
SER
160
−4.149
65.105
19.909

1266
CA
SER
160
−5.311
64.719
20.646

1267
CB
SER
160
−6.337
65.853
20.773

1268
OG
SER
160
−6.286
66.665
19.610

1269
C
SER
160
−5.959
63.628
19.881

1270
O
SER
160
−5.486
63.242
18.813

1271
N
ASN
161
−7.076
63.100
20.404

1272
CA
ASN
161
−7.843
62.205
19.594

1273
CB
ASN
161
−8.216
62.821
18.229

1274
CG
ASN
161
−9.727
62.933
18.077

1275
OD1
ASN
161
−10.229
62.999
16.954

1276
ND2
ASN
161
−10.476
62.955
19.212

1277
C
ASN
161
−7.043
60.969
19.326

1278
O
ASN
161
−7.053
60.458
18.205

1279
N
GLY
162
−6.357
60.442
20.358

1280
CA
GLY
162
−5.710
59.172
20.224

1281
C
GLY
162
−4.395
59.386
19.558

1282
O
GLY
162
−3.627
58.433
19.421

1283
N
ASN
163
−4.118
60.641
19.133

1284
CA
ASN
163
−2.968
61.028
18.344

1285
CB
ASN
163
−1.855
59.994
18.080

1286
CG
ASN
163
−1.029
59.665
19.302

1287
OD1
ASN
163
0.110
59.234
19.132

1288
ND2
ASN
163
−1.571
59.843
20.533

1289
C
ASN
163
−3.440
61.158
16.959

1290
O
ASN
163
−2.684
60.879
16.031

1291
N
ARG
164
−4.705
61.504
16.748

1292
CA
ARG
164
−5.079
61.336
15.389

1293
CB
ARG
164
−6.596
61.254
15.283

1294
CG
ARG
164
−7.141
61.085
13.880

1295
CD
ARG
164
−8.661
61.165
13.915

1296
NE
ARG
164
−9.113
61.390
12.535

1297
CZ
ARG
164
−10.380
61.018
12.188

1298
NH1
ARG
164
−10.801
61.206
10.907

1299
NH2
ARG
164
−11.202
60.472
13.126

1300
C
ARG
164
−4.579
62.573
14.719

1301
O
ARG
164
−3.568
62.580
14.019

1302
N
THR
165
−5.304
63.667
14.994

1303
CA
THR
165
−4.976
65.030
14.703

1304
CB
THR
165
−6.031
65.909
15.270

1305
OG1
THR
165
−6.329
65.444
16.581

1306
CG2
THR
165
−7.274
65.844
14.369

1307
C
THR
165
−3.732
65.390
15.467

1308
O
THR
165
−3.537
64.935
16.594

1309
N
LEU
166
−2.876
66.242
14.863

1310
CA
LEU
166
−1.746
66.824
15.541

1311
CB
LEU
166
−0.409
66.390
14.907

1312
CG
LEU
166
0.855
67.085
15.435

1313
CD2
LEU
166
1.914
67.124
14.318

1314
CD1
LEU
166
1.349
66.470
16.755

1315
C
LEU
166
−1.884
68.305
15.326

1316
O
LEU
166
−2.175
68.742
14.213

1317
N
THR
167
−1.730
69.133
16.376

1318
CA
THR
167
−1.967
70.533
16.157

1319
CB
THR
167
−3.245
71.072
16.782

1320
OG1
THR
167
−3.441
72.408
16.371

1321
CG2
THR
167
−3.209
70.956
18.317

1322
C
THR
167
−0.776
71.301
16.655

1323
O
THR
167
−0.570
71.478
17.852

1324
N
LEU
168
0.068
71.764
15.717

1325
CA
LEU
168
1.255
72.476
16.095

1326
CB
LEU
168
2.485
72.191
15.216

1327
CG
LEU
168
3.613
73.237
15.333

1328
CD2
LEU
168
4.753
72.927
14.350

1329
CD1
LEU
168
4.102
73.431
16.786

1330
C
LEU
168
0.973
73.927
15.955

1331
O
LEU
168
0.405
74.383
14.960

1332
N
PHE
169
1.387
74.697
16.979

1333
CA
PHE
169
1.237
76.108
16.890

1334
CB
PHE
169
−0.211
76.515
16.574

1335
CG
PHE
169
−0.626
77.786
17.222

1336
CD1
PHE
169
0.069
78.961
17.075

1337
CD2
PHE
169
−1.766
77.774
17.993

1338
CE1
PHE
169
−0.357
80.111
17.702

1339
CE2
PHE
169
−2.201
78.916
18.622

1340
CZ
PHE
169
−1.498
80.082
18.478

1341
C
PHE
169
1.675
76.644
18.207

1342
O
PHE
169
1.176
76.259
19.265

1343
N
ASN
170
2.677
77.535
18.154

1344
CA
ASN
170
3.002
78.149
16.905

1345
CB
ASN
170
3.641
79.543
17.058

1346
CG
ASN
170
4.567
79.460
18.253

1347
OD1
ASN
170
4.244
79.994
19.315

1348
ND2
ASN
170
5.720
78.755
18.099

1349
C
ASN
170
4.007
77.300
16.198

1350
O
ASN
170
4.511
76.304
16.718

1351
N
VAL
171
4.318
77.686
14.957

1352
CA
VAL
171
5.109
76.877
14.098

1353
CB
VAL
171
4.280
76.359
12.933

1354
CG1
VAL
171
3.884
77.547
12.035

1355
CG2
VAL
171
5.002
75.200
12.220

1356
C
VAL
171
6.184
77.802
13.617

1357
O
VAL
171
6.036
79.013
13.738

1358
N
THR
172
7.309
77.292
13.094

1359
CA
THR
172
8.309
78.234
12.711

1360
CB
THR
172
9.403
78.422
13.740

1361
OG1
THR
172
10.212
79.535
13.402

1362
CG2
THR
172
10.261
77.142
13.877

1363
C
THR
172
8.890
77.797
11.395

1364
O
THR
172
8.171
77.290
10.535

1365
N
ARG
173
10.205
77.999
11.200

1366
CA
ARG
173
10.874
77.547
10.015

1367
CB
ARG
173
12.027
78.468
9.639

1368
CG
ARG
173
13.007
78.691
10.791

1369
CD
ARG
173
13.982
79.796
10.412

1370
NE
ARG
173
14.983
80.022
11.496

1371
CZ
ARG
173
16.214
80.477
11.135

1372
NH1
ARG
173
16.557
80.496
9.811

1373
NH2
ARG
173
17.086
80.957
12.072

1374
C
ARG
173
11.479
76.203
10.288

1375
O
ARG
173
12.012
75.552
9.390

1376
N
ASN
174
11.444
75.733
11.543

1377
CA
ASN
174
12.118
74.486
11.748

1378
CB
ASN
174
12.306
74.112
13.228

1379
CG
ASN
174
13.654
73.391
13.350

1380
OD1
ASN
174
13.942
72.747
14.356

1381
ND2
ASN
174
14.511
73.542
12.308

1382
C
ASN
174
11.278
73.430
11.107

1383
O
ASN
174
11.779
72.391
10.685

1384
N
ASP
175
9.957
73.684
11.019

1385
CA
ASP
175
9.030
72.666
10.622

1386
CB
ASP
175
7.630
72.841
11.248

1387
CG
ASP
175
7.817
72.957
12.755

1388
OD1
ASP
175
7.175
73.835
13.390

1389
OD2
ASP
175
8.628
72.159
13.295

1390
C
ASP
175
8.880
72.708
9.130

1391
O
ASP
175
7.767
72.647
8.612

1392
N
THR
176
10.012
72.774
8.398

1393
CA
THR
176
9.955
72.501
6.991

1394
CB
THR
176
10.818
73.403
6.156

1395
OG1
THR
176
11.144
72.761
4.940

1396
CG2
THR
176
12.097
73.728
6.948

1397
C
THR
176
10.465
71.111
6.792

1398
O
THR
176
11.669
70.869
6.779

1399
N
ALA
177
9.535
70.154
6.619

1400
CA
ALA
177
9.889
68.805
6.298

1401
CB
ALA
177
10.546
68.041
7.460

1402
C
ALA
177
8.616
68.103
5.995

1403
O
ALA
177
7.546
68.522
6.432

1404
N
SER
178
8.690
67.011
5.213

1405
CA
SER
178
7.520
66.219
5.019

1406
CB
SER
178
7.707
65.075
4.005

1407
OG
SER
178
6.537
64.274
3.933

1408
C
SER
178
7.245
65.616
6.344

1409
O
SER
178
8.132
65.022
6.951

1410
N
TYR
179
6.013
65.762
6.855

1411
CA
TYR
179
5.740
65.085
8.085

1412
CB
TYR
179
4.984
65.943
9.123

1413
CG
TYR
179
5.927
66.937
9.729

1414
CD1
TYR
179
6.036
67.041
11.100

1415
CD2
TYR
179
6.680
67.769
8.935

1416
CE1
TYR
179
6.896
67.958
11.665

1417
CE2
TYR
179
7.540
68.684
9.499

1418
CZ
TYR
179
7.642
68.784
10.864

1419
OH
TYR
179
8.526
69.736
11.418

1420
C
TYR
179
4.921
63.875
7.733

1421
O
TYR
179
3.903
63.975
7.049

1422
N
LYS
180
5.386
62.685
8.163

1423
CA
LYS
180
4.812
61.451
7.704

1424
CB
LYS
180
5.861
60.329
7.580

1425
CG
LYS
180
5.738
59.384
6.376

1426
CD
LYS
180
7.076
58.709
6.047

1427
CE
LYS
180
7.005
57.517
5.094

1428
NZ
LYS
180
8.379
56.995
4.915

1429
C
LYS
180
3.820
61.021
8.735

1430
O
LYS
180
3.618
61.689
9.754

1431
N
CYS
181
3.162
59.870
8.507

1432
CA
CYS
181
2.346
59.308
9.536

1433
CB
CYS
181
0.843
59.360
9.197

1434
SG
CYS
181
−0.043
57.809
9.575

1435
C
CYS
181
2.720
57.866
9.654

1436
O
CYS
181
2.945
57.203
8.644

1437
N
GLU
182
2.790
57.336
10.886

1438
CA
GLU
182
2.891
55.912
10.975

1439
CB
GLU
182
4.308
55.377
11.229

1440
CG
GLU
182
4.386
53.907
10.858

1441
CD
GLU
182
5.659
53.237
11.331

1442
OE1
GLU
182
6.334
53.721
12.284

1443
OE2
GLU
182
5.955
52.176
10.731

1444
C
GLU
182
2.051
55.444
12.124

1445
O
GLU
182
1.864
56.156
13.114

1446
N
THR
183
1.525
54.208
12.002

1447
CA
THR
183
0.887
53.575
13.108

1448
CB
THR
183
−0.512
53.168
12.820

1449
OG1
THR
183
−0.899
53.744
11.586

1450
CG2
THR
183
−1.421
53.660
13.956

1451
C
THR
183
1.661
52.335
13.345

1452
O
THR
183
2.630
52.053
12.643

1453
N
GLN
184
1.269
51.552
14.357

1454
CA
GLN
184
2.038
50.381
14.624

1455
CB
GLN
184
3.094
50.616
15.730

1456
CG
GLN
184
4.189
49.546
15.762

1457
CD
GLN
184
5.296
49.994
16.718

1458
OE1
GLN
184
6.125
49.192
17.148

1459
NE2
GLN
184
5.281
51.299
17.093

1460
C
GLN
184
1.081
49.339
15.093

1461
O
GLN
184
−0.125
49.446
14.883

1462
N
ASN
185
1.617
48.316
15.774

1463
CA
ASN
185
0.859
47.438
16.613

1464
CB
ASN
185
−0.430
46.880
15.937

1465
CG
ASN
185
−0.206
45.640
15.083

1466
OD1
ASN
185
−0.609
44.539
15.453

1467
ND2
ASN
185
0.414
45.820
13.887

1468
C
ASN
185
1.832
46.378
17.005

1469
O
ASN
185
3.002
46.550
16.662

1470
N
PRO
186
1.482
45.322
17.704

1471
CA
PRO
186
2.358
44.196
17.833

1472
CD
PRO
186
0.170
45.092
18.285

1473
CB
PRO
186
1.584
43.101
18.553

1474
CG
PRO
186
0.307
43.779
19.075

1475
C
PRO
186
2.700
43.847
16.431

1476
O
PRO
186
1.782
43.516
15.680

1477
N
VAL
187
3.993
43.984
16.080

1478
CA
VAL
187
4.389
44.547
14.820

1479
CB
VAL
187
5.820
44.304
14.443

1480
CG1
VAL
187
6.032
44.826
13.013

1481
CG2
VAL
187
6.738
44.955
15.493

1482
C
VAL
187
3.590
43.981
13.707

1483
O
VAL
187
3.662
42.784
13.432

1484
N
SER
188
2.854
44.861
13.003

1485
CA
SER
188
2.614
44.657
11.609

1486
CB
SER
188
1.493
43.646
11.299

1487
OG
SER
188
0.618
43.512
12.408

1488
C
SER
188
2.237
45.999
11.068

1489
O
SER
188
1.062
46.296
10.844

1490
N
ALA
189
3.261
46.861
10.886

1491
CA
ALA
189
3.070
48.267
10.707

1492
CB
ALA
189
4.239
49.094
11.276

1493
C
ALA
189
2.968
48.617
9.242

1494
O
ALA
189
3.192
47.786
8.363

1495
N
ARG
190
2.629
49.901
8.979

1496
CA
ARG
190
2.654
50.555
7.691

1497
CB
ARG
190
1.307
50.543
6.946

1498
CG
ARG
190
0.764
49.157
6.638

1499
CD
ARG
190
−0.450
49.154
5.718

1500
NE
ARG
190
−0.380
47.838
5.045

1501
CZ
ARG
190
−0.874
47.651
3.777

1502
NH1
ARG
190
−1.628
48.628
3.192

1503
NH2
ARG
190
−0.585
46.493
3.130

1504
C
ARG
190
2.900
51.997
7.990

1505
O
ARG
190
2.899
52.382
9.163

1506
N
ARG
191
3.091
52.845
6.954

1507
CA
ARG
191
3.151
54.272
7.164

1508
CB
ARG
191
4.536
54.895
6.907

1509
CG
ARG
191
5.613
54.501
7.923

1510
CD
ARG
191
6.942
54.141
7.260

1511
NE
ARG
191
7.996
54.055
8.316

1512
CZ
ARG
191
9.300
54.007
7.938

1513
NH1
ARG
191
9.662
54.003
6.626

1514
NH2
ARG
191
10.277
53.961
8.906

1515
C
ARG
191
2.177
54.925
6.211

1516
O
ARG
191
1.373
54.234
5.591

1517
N
SER
192
2.206
56.275
6.101

1518
CA
SER
192
1.243
56.968
5.281

1519
CB
SER
192
0.481
58.085
6.033

1520
OG
SER
192
1.388
59.092
6.454

1521
C
SER
192
1.947
57.592
4.117

1522
O
SER
192
2.862
57.004
3.543

1523
N
ASP
193
1.517
58.808
3.710

1524
CA
ASP
193
2.090
59.451
2.560

1525
CB
ASP
193
1.228
60.566
1.959

1526
CG
ASP
193
−0.220
60.249
2.277

1527
OD1
ASP
193
−0.821
59.463
1.500

1528
OD2
ASP
193
−0.750
60.772
3.292

1529
C
ASP
193
3.352
60.126
2.973

1530
O
ASP
193
4.069
59.694
3.872

1531
N
SER
194
3.627
61.239
2.275

1532
CA
SER
194
4.675
62.121
2.671

1533
CB
SER
194
6.048
61.728
2.090

1534
OG
SER
194
6.246
60.340
2.303

1535
C
SER
194
4.292
63.471
2.152

1536
O
SER
194
4.550
63.807
0.995

1537
N
VAL
195
3.638
64.265
3.020

1538
CA
VAL
195
3.203
65.589
2.681

1539
CB
VAL
195
2.030
66.040
3.500

1540
CG1
VAL
195
0.850
65.112
3.192

1541
CG2
VAL
195
2.412
65.993
4.989

1542
C
VAL
195
4.329
66.517
2.974

1543
O
VAL
195
4.919
66.494
4.050

1544
N
ILE
196
4.706
67.372
2.015

1545
CA
ILE
196
5.829
68.180
2.373

1546
CB
ILE
196
6.885
68.313
1.318

1547
CG2
ILE
196
6.217
68.752
0.006

1548
CG1
ILE
196
7.986
69.267
1.811

1549
CD1
ILE
196
8.954
69.688
0.720

1550
C
ILE
196
5.327
69.538
2.732

1551
O
ILE
196
4.324
70.020
2.202

1552
N
LEU
197
5.996
70.185
3.703

1553
CA
LEU
197
5.411
71.396
4.185

1554
CB
LEU
197
4.822
71.286
5.590

1555
CG
LEU
197
3.701
72.319
5.823

1556
CD2
LEU
197
3.522
72.601
7.319

1557
CD1
LEU
197
2.398
71.924
5.121

1558
C
LEU
197
6.450
72.451
4.247

1559
O
LEU
197
7.301
72.459
5.137

1560
N
ASN
198
6.371
73.407
3.307

1561
CA
ASN
198
7.287
74.493
3.373

1562
CB
ASN
198
7.899
74.895
2.041

1563
CG
ASN
198
8.708
73.708
1.548

1564
OD1
ASN
198
9.294
72.985
2.355

1565
ND2
ASN
198
8.757
73.503
0.207

1566
C
ASN
198
6.525
75.677
3.826

1567
O
ASN
198
5.534
76.070
3.212

1568
N
VAL
199
7.013
76.294
4.915

1569
CA
VAL
199
6.481
77.537
5.368

1570
CB
VAL
199
6.835
77.844
6.787

1571
CG1
VAL
199
8.363
77.994
6.868

1572
CG2
VAL
199
6.014
79.070
7.250

1573
C
VAL
199
7.134
78.588
4.536

1574
O
VAL
199
8.232
78.393
4.017

1575
N
LEU
200
6.457
79.751
4.424

1576
CA
LEU
200
7.033
80.994
4.007

1577
CB
LEU
200
6.575
81.548
2.649

1578
CG
LEU
200
6.797
83.077
2.543

1579
CD2
LEU
200
6.213
83.641
1.239

1580
CD1
LEU
200
8.271
83.436
2.734

1581
C
LEU
200
6.494
81.964
4.974

1582
O
LEU
200
5.281
82.109
5.127

1583
N
TYR
201
7.412
82.649
5.661

1584
CA
TYR
201
7.063
83.577
6.676

1585
CB
TYR
201
8.309
84.123
7.409

1586
CG
TYR
201
9.522
83.684
6.626

1587
CD1
TYR
201
10.072
84.480
5.643

1588
CD2
TYR
201
10.119
82.459
6.860

1589
CE1
TYR
201
11.174
84.083
4.923

1590
CE2
TYR
201
11.228
82.059
6.138

1591
CZ
TYR
201
11.771
82.864
5.160

1592
OH
TYR
201
12.905
82.456
4.421

1593
C
TYR
201
6.423
84.694
5.955

1594
O
TYR
201
6.317
84.674
4.730

1595
N
GLY
202
5.999
85.721
6.716

1596
CA
GLY
202
5.666
87.004
6.174

1597
C
GLY
202
6.259
87.999
7.119

1598
O
GLY
202
5.629
88.401
8.101

1599
N
PRO
203
7.486
88.391
6.839

1600
CA
PRO
203
8.295
89.066
7.826

1601
CD
PRO
203
8.254
87.749
5.805

1602
CB
PRO
203
9.754
88.849
7.427

1603
CG
PRO
203
9.719
87.815
6.297

1604
C
PRO
203
7.997
90.541
7.906

1605
O
PRO
203
7.018
91.043
7.304

1606
OXT
PRO
203
8.804
91.221
8.590

[0138]

7

TABLE 4

Full coordinate set of domains N and A1 of human CEACAM1

(homology model)(1587 atoms, 203 amino acids)

ANum
AType
RType
RNum
X
Y
Z

1
N
GLN
1
7.745
28.820
40.481

2
CA
GLN
1
7.968
27.374
40.321

3
CB
GLN
1
6.951
26.588
41.158

4
CG
GLN
1
6.002
27.513
41.923

5
CD
GLN
1
4.805
26.718
42.405

6
OE1
GLN
1
4.676
25.534
42.096

7
NE2
GLN
1
3.900
27.386
43.176

8
C
GLN
1
7.803
26.950
38.910

9
O
GLN
1
6.852
26.235
38.607

10
N
LEU
2
8.763
27.375
38.060

11
CA
LEU
2
9.146
26.719
36.849

12
CB
LEU
2
10.105
25.557
37.169

13
CG
LEU
2
10.544
24.703
35.971

14
CD2
LEU
2
10.819
23.253
36.406

15
CD1
LEU
2
11.709
25.366
35.222

16
C
LEU
2
7.948
26.174
36.134

17
O
LEU
2
7.665
24.983
36.228

18
N
THR
3
7.204
27.009
35.390

19
CA
THR
3
6.354
26.364
34.436

20
CB
THR
3
4.901
26.252
34.790

21
OG1
THR
3
4.380
27.522
35.127

22
CG2
THR
3
4.750
25.257
35.938

23
C
THR
3
6.358
27.122
33.173

24
O
THR
3
7.377
27.626
32.695

25
N
THR
4
5.151
27.150
32.592

26
CA
THR
4
4.942
27.242
31.185

27
CB
THR
4
3.474
27.108
30.845

28
OG1
THR
4
3.248
26.953
29.453

29
CG2
THR
4
2.752
28.355
31.384

30
C
THR
4
5.417
28.566
30.701

31
O
THR
4
6.008
29.370
31.421

32
N
GLU
5
5.159
28.791
29.416

33
CA
GLU
5
5.330
30.049
28.792

34
CB
GLU
5
6.781
30.215
28.258

35
CG
GLU
5
7.079
31.549
27.586

36
CD
GLU
5
7.457
31.212
26.156

37
OE1
GLU
5
7.953
30.071
25.963

38
OE2
GLU
5
7.281
32.062
25.244

39
C
GLU
5
4.342
29.985
27.675

40
O
GLU
5
3.367
29.235
27.737

41
N
SER
6
4.554
30.766
26.613

42
CA
SER
6
3.800
30.517
25.431

43
CB
SER
6
2.280
30.724
25.559

44
OG
SER
6
1.673
30.516
24.293

45
C
SER
6
4.309
31.460
24.422

46
O
SER
6
4.771
32.549
24.740

47
N
MET
7
4.266
31.031
23.159

48
CA
MET
7
4.925
31.763
22.128

49
CB
MET
7
6.394
31.288
21.997

50
CG
MET
7
7.179
31.842
20.810

51
SD
MET
7
8.328
30.663
20.038

52
CE
MET
7
7.852
31.081
18.336

53
C
MET
7
4.186
31.445
20.866

54
O
MET
7
3.557
30.396
20.762

55
N
PRO
8
4.224
32.278
19.875

56
CA
PRO
8
4.909
33.534
19.906

57
CD
PRO
8
3.959
31.792
18.536

58
CB
PRO
8
5.135
33.929
18.443

59
CG
PRO
8
4.824
32.660
17.621

60
C
PRO
8
4.066
34.517
20.649

61
O
PRO
8
2.882
34.616
20.340

62
N
PHE
9
4.627
35.266
21.617

63
CA
PHE
9
3.779
36.245
22.231

64
CB
PHE
9
4.411
37.010
23.396

65
CG
PHE
9
5.861
36.691
23.383

66
CD1
PHE
9
6.754
37.498
22.713

67
CD2
PHE
9
6.308
35.568
24.038

68
CE1
PHE
9
8.092
37.189
22.695

69
CE2
PHE
9
7.645
35.256
24.023

70
CZ
PHE
9
8.531
36.067
23.357

71
C
PHE
9
3.440
37.247
21.200

72
O
PHE
9
4.258
37.576
20.350

73
N
ASN
10
2.201
37.752
21.257

74
CA
ASN
10
1.689
38.607
20.248

75
CB
ASN
10
2.618
39.784
19.929

76
CG
ASN
10
2.576
40.668
21.168

77
OD1
ASN
10
3.558
40.865
21.880

78
ND2
ASN
10
1.353
41.174
21.467

79
C
ASN
10
1.437
37.766
19.052

80
O
ASN
10
2.340
37.151
18.484

81
N
VAL
11
0.154
37.692
18.674

82
CA
VAL
11
−0.247
36.736
17.695

83
CB
VAL
11
−1.092
35.654
18.293

84
CG1
VAL
11
−0.845
34.359
17.507

85
CG2
VAL
11
−0.740
35.562
19.789

86
C
VAL
11
−1.059
37.471
16.691

87
O
VAL
11
−1.804
38.385
17.038

88
N
ALA
12
−0.934
37.089
15.410

89
CA
ALA
12
−1.721
37.744
14.412

90
CB
ALA
12
−0.983
37.913
13.081

91
C
ALA
12
−2.911
36.891
14.144

92
O
ALA
12
−3.074
35.821
14.719

93
N
GLU
13
−3.783
37.365
13.240

94
CA
GLU
13
−4.919
36.592
12.861

95
CB
GLU
13
−6.041
37.476
12.310

96
CG
GLU
13
−7.395
37.293
12.980

97
CD
GLU
13
−8.404
37.892
12.028

98
OE1
GLU
13
−9.298
38.637
12.512

99
OE2
GLU
13
−8.280
37.613
10.807

100
C
GLU
13
−4.472
35.715
11.735

101
O
GLU
13
−3.657
36.118
10.910

102
N
GLY
14
−5.001
34.480
11.664

103
CA
GLY
14
−4.637
33.601
10.588

104
C
GLY
14
−3.273
33.050
10.873

105
O
GLY
14
−2.674
32.367
10.041

106
N
LYS
15
−2.729
33.326
12.071

107
CA
LYS
15
−1.453
32.742
12.349

108
CB
LYS
15
−0.341
33.782
12.545

109
CG
LYS
15
−0.300
34.740
11.349

110
CD
LYS
15
0.971
35.585
11.223

111
CE
LYS
15
1.892
35.139
10.088

112
NZ
LYS
15
2.889
34.192
10.624

113
C
LYS
15
−1.604
31.914
13.582

114
O
LYS
15
−2.562
32.062
14.337

115
N
GLU
16
−0.654
30.980
13.784

116
CA
GLU
16
−0.793
30.008
14.822

117
CB
GLU
16
−0.099
28.662
14.531

118
CG
GLU
16
−0.817
27.763
13.526

119
CD
GLU
16
0.066
26.548
13.284

120
OE1
GLU
16
−0.479
25.412
13.252

121
OE2
GLU
16
1.301
26.743
13.127

122
C
GLU
16
−0.138
30.521
16.060

123
O
GLU
16
0.369
31.639
16.111

124
N
VAL
17
−0.165
29.654
17.091

125
CA
VAL
17
0.385
29.886
18.395

126
CB
VAL
17
−0.627
30.335
19.401

127
CG1
VAL
17
0.086
30.552
20.744

128
CG2
VAL
17
−1.377
31.568
18.873

129
C
VAL
17
0.785
28.550
18.887

130
O
VAL
17
0.121
27.557
18.600

131
N
LEU
18
1.871
28.471
19.673

132
CA
LEU
18
2.081
27.227
20.340

133
CB
LEU
18
3.385
26.488
19.986

134
CG
LEU
18
3.803
25.486
21.084

135
CD2
LEU
18
5.288
25.105
20.958

136
CD1
LEU
18
2.878
24.262
21.138

137
C
LEU
18
2.153
27.520
21.793

138
O
LEU
18
2.692
28.539
22.220

139
N
LEU
19
1.596
26.619
22.605

140
CA
LEU
19
1.671
26.891
23.998

141
CB
LEU
19
0.357
26.603
24.728

142
CG
LEU
19
−0.699
27.719
24.495

143
CD2
LEU
19
−0.657
28.261
23.052

144
CD1
LEU
19
−0.582
28.810
25.568

145
C
LEU
19
2.768
26.048
24.537

146
O
LEU
19
2.767
24.831
24.360

147
N
LEU
20
3.770
26.686
25.171

148
CA
LEU
20
4.972
25.975
25.479

149
CB
LEU
20
6.241
26.789
25.167

150
CG
LEU
20
7.476
25.958
24.757

151
CD2
LEU
20
8.768
26.791
24.823

152
CD1
LEU
20
7.290
25.316
23.372

153
C
LEU
20
4.984
25.709
26.937

154
O
LEU
20
5.152
26.632
27.732

155
N
VAL
21
4.848
24.432
27.335

156
CA
VAL
21
5.199
24.150
28.687

157
CB
VAL
21
4.536
22.938
29.273

158
CG1
VAL
21
5.379
22.415
30.449

159
CG2
VAL
21
3.106
23.324
29.691

160
C
VAL
21
6.654
23.881
28.641

161
O
VAL
21
7.147
23.341
27.657

162
N
HIS
22
7.382
24.273
29.699

163
CA
HIS
22
8.770
23.956
29.741

164
ND1
HIS
22
9.278
26.540
28.412

165
CG
HIS
22
9.501
26.347
29.754

166
CB
HIS
22
9.630
25.019
30.409

167
NE2
HIS
22
9.414
28.561
29.341

168
CD2
HIS
22
9.576
27.591
30.309

169
CE1
HIS
22
9.236
27.889
28.222

170
C
HIS
22
8.888
22.756
30.586

171
O
HIS
22
8.326
21.706
30.287

172
N
ASN
23
9.642
22.896
31.686

173
CA
ASN
23
9.947
21.761
32.494

174
CB
ASN
23
11.138
22.009
33.420

175
CG
ASN
23
12.294
22.403
32.521

176
OD1
ASN
23
12.300
23.480
31.930

177
ND2
ASN
23
13.299
21.498
32.399

178
C
ASN
23
8.768
21.449
33.346

179
O
ASN
23
8.108
22.340
33.878

180
N
LEU
24
8.504
20.143
33.510

181
CA
LEU
24
7.454
19.653
34.345

182
CB
LEU
24
7.252
20.402
35.675

183
CG
LEU
24
8.495
20.495
36.592

184
CD2
LEU
24
9.388
19.246
36.536

185
CD1
LEU
24
8.058
20.846
38.025

186
C
LEU
24
6.177
19.674
33.588

187
O
LEU
24
5.825
20.723
33.051

188
N
PRO
25
5.430
18.604
33.464

189
CA
PRO
25
5.905
17.250
33.603

190
CD
PRO
25
4.693
18.659
32.217

191
CB
PRO
25
6.472
16.966
32.217

192
CG
PRO
25
5.424
17.652
31.294

193
C
PRO
25
6.621
16.654
34.793

194
O
PRO
25
7.492
17.227
35.441

195
N
GLN
26
6.263
15.410
35.123

196
CA
GLN
26
7.054
14.783
36.126

197
CB
GLN
26
6.938
15.445
37.517

198
CG
GLN
26
8.258
15.403
38.292

199
CD
GLN
26
8.203
16.285
39.543

200
OE1
GLN
26
8.652
15.808
40.583

201
NE2
GLN
26
7.710
17.552
39.470

202
C
GLN
26
6.598
13.373
36.215

203
O
GLN
26
6.664
12.758
37.278

204
N
GLN
27
6.152
12.816
35.073

205
CA
GLN
27
5.761
11.442
35.082

206
CB
GLN
27
6.881
10.549
35.638

207
CG
GLN
27
6.712
9.051
35.410

208
CD
GLN
27
7.531
8.423
36.523

209
OE1
GLN
27
7.878
7.245
36.514

210
NE2
GLN
27
7.882
9.284
37.512

211
C
GLN
27
4.536
11.402
35.940

212
O
GLN
27
4.488
10.806
37.017

213
N
LEU
28
3.513
12.116
35.441

214
CA
LEU
28
2.258
12.361
36.082

215
CB
LEU
28
1.780
13.783
35.787

216
CG
LEU
28
3.010
14.651
35.434

217
CD2
LEU
28
3.853
14.914
36.689

218
CD1
LEU
28
2.669
15.931
34.666

219
C
LEU
28
1.279
11.381
35.528

220
O
LEU
28
1.554
10.182
35.482

221
N
PHE
29
0.089
11.848
35.107

222
CA
PHE
29
−0.888
10.851
34.786

223
CB
PHE
29
−1.817
10.508
35.964

224
CG
PHE
29
−2.827
9.519
35.499

225
CD1
PHE
29
−2.607
8.168
35.639

226
CD2
PHE
29
−4.020
9.916
34.928

227
CE1
PHE
29
−3.534
7.242
35.217

228
CE2
PHE
29
−4.946
8.987
34.504

229
CZ
PHE
29
−4.717
7.645
34.649

230
C
PHE
29
−1.768
11.357
33.690

231
O
PHE
29
−2.107
10.630
32.759

232
N
GLY
30
−2.217
12.614
33.797

233
CA
GLY
30
−3.261
13.008
32.917

234
C
GLY
30
−3.193
14.480
32.846

235
O
GLY
30
−3.083
15.190
33.842

236
N
TYR
31
−3.232
15.012
31.629

237
CA
TYR
31
−3.165
16.433
31.560

238
CB
TYR
31
−1.923
17.103
30.894

239
CG
TYR
31
−0.856
16.224
30.281

240
CD1
TYR
31
0.293
16.854
29.862

241
CD2
TYR
31
−0.926
14.855
30.081

242
CE1
TYR
31
1.325
16.147
29.287

243
CE2
TYR
31
0.090
14.140
29.516

244
CZ
TYR
31
1.219
14.785
29.115

245
OH
TYR
31
2.261
14.053
28.525

246
C
TYR
31
−4.372
16.873
30.829

247
O
TYR
31
−4.996
16.106
30.102

248
N
SER
32
−4.763
18.133
31.026

249
CA
SER
32
−5.893
18.618
30.311

250
CB
SER
32
−7.202
18.466
31.111

251
OG
SER
32
−8.331
18.854
30.345

252
C
SER
32
−5.632
20.067
30.086

253
O
SER
32
−5.185
20.781
30.984

254
N
TRP
33
−5.885
20.532
28.852

255
CA
TRP
33
−5.791
21.935
28.642

256
CB
TRP
33
−5.241
22.339
27.268

257
CG
TRP
33
−3.741
22.523
27.269

258
CD2
TRP
33
−3.062
23.685
27.791

259
CD1
TRP
33
−2.774
21.671
26.830

260
NE1
TRP
33
−1.529
22.203
27.077

261
CE2
TRP
33
−1.694
23.441
27.659

262
CE3
TRP
33
−3.538
24.848
28.336

263
CZ2
TRP
33
−0.772
24.359
28.087

264
CZ3
TRP
33
−2.602
25.774
28.754

265
CH2
TRP
33
−1.248
25.531
28.632

266
C
TRP
33
−7.149
22.500
28.762

267
O
TRP
33
−8.146
21.875
28.396

268
N
TYR
34
−7.216
23.722
29.302

269
CA
TYR
34
−8.503
24.278
29.528

270
CB
TYR
34
−8.780
24.470
31.020

271
CG
TYR
34
−9.040
23.109
31.570

272
CD1
TYR
34
−8.633
22.763
32.839

273
CD2
TYR
34
−9.706
22.184
30.794

274
CE1
TYR
34
−8.891
21.505
33.340

275
CE2
TYR
34
−9.967
20.932
31.284

276
CZ
TYR
34
−9.562
20.589
32.554

277
OH
TYR
34
−9.839
19.295
33.044

278
C
TYR
34
−8.561
25.590
28.829

279
O
TYR
34
−7.981
25.773
27.759

280
N
LYS
35
−9.317
26.534
29.416

281
CA
LYS
35
−9.519
27.763
28.727

282
CB
LYS
35
−10.371
27.602
27.454

283
CG
LYS
35
−10.539
28.909
26.676

284
CD
LYS
35
−11.440
28.787
25.445

285
CE
LYS
35
−11.134
29.852
24.396

286
NZ
LYS
35
−12.108
29.768
23.286

287
C
LYS
35
−10.272
28.664
29.640

288
O
LYS
35
−11.471
28.503
29.854

289
N
GLY
36
−9.586
29.673
30.190

290
CA
GLY
36
−10.333
30.733
30.788

291
C
GLY
36
−10.512
30.450
32.233

292
O
GLY
36
−11.530
30.820
32.811

293
N
GLU
37
−9.498
29.830
32.865

294
CA
GLU
37
−9.402
29.848
34.292

295
CB
GLU
37
−9.803
31.194
34.905

296
CG
GLU
37
−9.569
31.235
36.412

297
CD
GLU
37
−9.867
32.637
36.903

298
OE1
GLU
37
−9.509
32.952
38.069

299
OE2
GLU
37
−10.465
33.408
36.106

300
C
GLU
37
−10.295
28.812
34.876

301
O
GLU
37
−9.905
28.124
35.821

302
N
ARG
38
−11.517
28.705
34.341

303
CA
ARG
38
−12.503
27.833
34.883

304
CB
ARG
38
−13.774
27.771
34.027

305
CG
ARG
38
−14.960
27.211
34.811

306
CD
ARG
38
−16.255
27.138
34.006

307
NE
ARG
38
−17.321
27.741
34.863

308
CZ
ARG
38
−18.608
27.328
34.745

309
NH1
ARG
38
−19.561
27.764
35.626

310
NH2
ARG
38
−18.953
26.457
33.760

311
C
ARG
38
−11.889
26.488
34.908

312
O
ARG
38
−11.314
26.026
33.925

313
N
VAL
39
−11.941
25.845
36.075

314
CA
VAL
39
−11.127
24.692
36.224

315
CB
VAL
39
−10.681
24.558
37.642

316
CG1
VAL
39
−9.933
23.235
37.818

317
CG2
VAL
39
−9.822
25.793
37.966

318
C
VAL
39
−11.962
23.526
35.794

319
O
VAL
39
−11.494
22.389
35.702

320
N
ASP
40
−13.248
23.818
35.486

321
CA
ASP
40
−14.144
22.841
34.937

322
CB
ASP
40
−15.531
23.423
34.546

323
CG
ASP
40
−16.689
22.750
35.284

324
OD1
ASP
40
−17.851
23.117
34.954

325
OD2
ASP
40
−16.440
21.882
36.165

326
C
ASP
40
−13.556
22.348
33.656

327
O
ASP
40
−12.579
22.882
33.130

328
N
GLY
41
−14.193
21.296
33.118

329
CA
GLY
41
−14.005
20.893
31.756

330
C
GLY
41
−15.379
20.862
31.156

331
O
GLY
41
−15.678
20.034
30.291

332
N
ASN
42
−16.237
21.794
31.628

333
CA
ASN
42
−17.506
22.135
31.037

334
CB
ASN
42
−17.861
23.591
31.403

335
CG
ASN
42
−19.327
23.892
31.153

336
OD1
ASN
42
−19.717
24.366
30.085

337
ND2
ASN
42
−20.165
23.645
32.190

338
C
ASN
42
−17.233
22.109
29.577

339
O
ASN
42
−17.913
21.452
28.787

340
N
ARG
43
−16.140
22.809
29.243

341
CA
ARG
43
−15.380
22.564
28.070

342
CB
ARG
43
−15.021
23.859
27.323

343
CG
ARG
43
−16.237
24.524
26.690

344
CD
ARG
43
−17.056
23.501
25.915

345
NE
ARG
43
−18.490
23.736
26.208

346
CZ
ARG
43
−19.271
24.314
25.245

347
NH1
ARG
43
−20.623
24.307
25.374

348
NH2
ARG
43
−18.676
24.871
24.149

349
C
ARG
43
−14.097
21.978
28.558

350
O
ARG
43
−13.395
22.591
29.364

351
N
GLN
44
−13.759
20.764
28.081

352
CA
GLN
44
−12.443
20.260
28.326

353
CB
GLN
44
−12.412
18.912
29.067

354
CG
GLN
44
−10.989
18.427
29.356

355
CD
GLN
44
−11.059
17.023
29.951

356
OE1
GLN
44
−11.444
16.814
31.098

357
NE2
GLN
44
−10.661
16.032
29.122

358
C
GLN
44
−11.848
20.037
26.984

359
O
GLN
44
−12.378
19.277
26.171

360
N
ILE
45
−10.735
20.729
26.705

361
CA
ILE
45
−10.185
20.632
25.394

362
CB
ILE
45
−9.291
21.799
25.072

363
CG2
ILE
45
−9.572
22.220
23.620

364
CG1
ILE
45
−9.552
22.949
26.068

365
CD1
ILE
45
−10.590
23.962
25.577

366
C
ILE
45
−9.421
19.336
25.323

367
O
ILE
45
−9.943
18.344
24.819

368
N
VAL
46
−8.168
19.307
25.828

369
CA
VAL
46
−7.305
18.199
25.510

370
CB
VAL
46
−5.991
18.634
24.941

371
CG1
VAL
46
−5.196
17.427
24.414

372
CG2
VAL
46
−6.305
19.661
23.849

373
C
VAL
46
−6.992
17.420
26.747

374
O
VAL
46
−7.147
17.900
27.870

375
N
GLY
47
−6.514
16.171
26.551

376
CA
GLY
47
−6.037
15.364
27.630

377
C
GLY
47
−5.116
14.326
27.061

378
O
GLY
47
−5.461
13.149
26.966

379
N
TYR
48
−3.885
14.723
26.696

380
CA
TYR
48
−2.951
13.687
26.389

381
CB
TYR
48
−1.575
14.189
25.910

382
CG
TYR
48
−0.653
13.031
25.691

383
CD1
TYR
48
0.316
12.736
26.620

384
CD2
TYR
48
−0.718
12.246
24.560

385
CE1
TYR
48
1.184
11.683
26.437

386
CE2
TYR
48
0.150
11.189
24.371

387
CZ
TYR
48
1.105
10.896
25.310

388
OH
TYR
48
1.996
9.816
25.123

389
C
TYR
48
−2.811
12.986
27.692

390
O
TYR
48
−3.029
13.582
28.747

391
N
ALA
49
−2.523
11.679
27.627

392
CA
ALA
49
−2.635
10.824
28.761

393
CB
ALA
49
−3.418
9.550
28.414

394
C
ALA
49
−1.249
10.416
29.096

395
O
ALA
49
−0.438
10.170
28.207

396
N
ILE
50
−0.879
10.329
30.379

397
CA
ILE
50
0.376
9.667
30.389

398
CB
ILE
50
1.471
10.267
31.209

399
CG2
ILE
50
1.580
9.544
32.563

400
CG1
ILE
50
2.731
10.166
30.319

401
CD1
ILE
50
3.639
11.387
30.402

402
C
ILE
50
0.161
8.252
30.758

403
O
ILE
50
−0.922
7.858
31.180

404
N
GLY
51
1.206
7.432
30.541

405
CA
GLY
51
1.120
6.031
30.809

406
C
GLY
51
0.792
5.361
29.513

407
O
GLY
51
1.455
5.605
28.502

408
N
THR
52
−0.258
4.500
29.526

409
CA
THR
52
−0.807
4.056
28.280

410
CB
THR
52
−2.098
3.280
28.339

411
OG1
THR
52
−3.056
3.842
27.444

412
CG2
THR
52
−2.646
3.303
29.770

413
C
THR
52
−1.097
5.297
27.566

414
O
THR
52
−1.877
6.139
28.014

415
N
GLN
53
−0.392
5.463
26.451

416
CA
GLN
53
−0.440
6.751
25.887

417
CB
GLN
53
0.644
7.061
24.864

418
CG
GLN
53
2.063
6.841
25.358

419
CD
GLN
53
2.888
7.250
24.159

420
OE1
GLN
53
4.105
7.088
24.128

421
NE2
GLN
53
2.184
7.791
23.132

422
C
GLN
53
−1.683
6.811
25.120

423
O
GLN
53
−2.221
5.816
24.641

424
N
GLN
54
−2.153
8.041
24.990

425
CA
GLN
54
−3.278
8.289
24.183

426
CB
GLN
54
−4.511
7.472
24.608

427
CG
GLN
54
−5.606
7.348
23.547

428
CD
GLN
54
−6.643
6.386
24.116

429
OE1
GLN
54
−7.711
6.172
23.546

430
NE2
GLN
54
−6.321
5.794
25.296

431
C
GLN
54
−3.550
9.700
24.490

432
O
GLN
54
−3.053
10.233
25.479

433
N
ALA
55
−4.327
10.340
23.622

434
CA
ALA
55
−4.894
11.580
23.989

435
CB
ALA
55
−4.370
12.750
23.148

436
C
ALA
55
−6.313
11.363
23.677

437
O
ALA
55
−6.661
10.378
23.034

438
N
THR
56
−7.186
12.242
24.162

439
CA
THR
56
−8.550
11.885
24.010

440
CB
THR
56
−8.873
10.672
24.844

441
OG1
THR
56
−10.254
10.591
25.154

442
CG2
THR
56
−8.023
10.706
26.129

443
C
THR
56
−9.290
13.090
24.447

444
O
THR
56
−9.120
13.570
25.565

445
N
PRO
57
−10.044
13.675
23.564

446
CA
PRO
57
−10.420
15.036
23.724

447
CD
PRO
57
−10.492
13.080
22.319

448
CB
PRO
57
−11.029
15.490
22.409

449
CG
PRO
57
−10.995
14.262
21.460

450
C
PRO
57
−11.480
14.994
24.736

451
O
PRO
57
−11.971
13.910
25.043

452
N
GLY
58
−11.910
16.175
25.177

453
CA
GLY
58
−13.282
16.229
25.514

454
C
GLY
58
−13.985
16.846
24.360

455
O
GLY
58
−13.744
16.638
23.170

456
N
PRO
59
−14.884
17.624
24.839

457
CA
PRO
59
−16.089
17.881
24.116

458
CD
PRO
59
−15.093
17.523
26.270

459
CB
PRO
59
−17.218
17.796
25.150

460
CG
PRO
59
−16.592
17.292
26.460

461
C
PRO
59
−16.050
19.229
23.485

462
O
PRO
59
−17.024
19.598
22.832

463
N
ALA
60
−14.989
20.016
23.716

464
CA
ALA
60
−15.123
21.412
23.422

465
CB
ALA
60
−14.366
22.338
24.387

466
C
ALA
60
−14.587
21.677
22.054

467
O
ALA
60
−14.779
20.882
21.134

468
N
ASN
61
−13.926
22.838
21.871

469
CA
ASN
61
−13.568
23.153
20.528

470
CB
ASN
61
−13.429
24.641
20.200

471
CG
ASN
61
−14.192
24.798
18.894

472
OD1
ASN
61
−14.816
25.821
18.610

473
ND2
ASN
61
−14.167
23.715
18.067

474
C
ASN
61
−12.296
22.464
20.207

475
O
ASN
61
−11.276
22.613
20.882

476
N
SER
62
−12.373
21.645
19.147

477
CA
SER
62
−11.304
20.831
18.682

478
CB
SER
62
−11.782
19.416
18.336

479
OG
SER
62
−10.997
18.457
19.023

480
C
SER
62
−10.909
21.434
17.391

481
O
SER
62
−10.179
20.814
16.620

482
N
GLY
63
−11.444
22.648
17.143

483
CA
GLY
63
−11.533
23.269
15.858

484
C
GLY
63
−10.244
23.088
15.150

485
O
GLY
63
−10.153
22.353
14.165

486
N
ARG
64
−9.194
23.727
15.686

487
CA
ARG
64
−7.881
23.391
15.239

488
CB
ARG
64
−7.385
24.286
14.098

489
CG
ARG
64
−8.508
25.171
13.560

490
CD
ARG
64
−8.518
26.598
14.121

491
NE
ARG
64
−9.750
26.780
14.938

492
CZ
ARG
64
−9.643
26.996
16.301

493
NH1
ARG
64
−8.419
27.067
16.883

494
NH2
ARG
64
−10.772
27.132
17.047

495
C
ARG
64
−6.994
23.599
16.418

496
O
ARG
64
−6.603
24.726
16.714

497
N
GLU
65
−6.648
22.507
17.126

498
CA
GLU
65
−5.617
22.582
18.122

499
CB
GLU
65
−6.106
23.055
19.503

500
CG
GLU
65
−6.597
24.511
19.500

501
CD
GLU
65
−8.108
24.492
19.362

502
OE1
GLU
65
−8.664
23.428
18.984

503
OE2
GLU
65
−8.734
25.543
19.667

504
C
GLU
65
−5.060
21.198
18.239

505
O
GLU
65
−5.610
20.257
17.669

506
N
THR
66
−3.923
21.048
18.960

507
CA
THR
66
−3.216
19.804
19.076

508
CB
THR
66
−2.105
19.651
18.080

509
OG1
THR
66
−2.521
20.080
16.788

510
CG2
THR
66
−1.663
18.177
18.035

511
C
THR
66
−2.528
19.827
20.407

512
O
THR
66
−2.335
20.893
20.985

513
N
ILE
67
−2.112
18.655
20.930

514
CA
ILE
67
−1.356
18.719
22.147

515
CB
ILE
67
−2.043
18.118
23.342

516
CG2
ILE
67
−1.944
16.584
23.247

517
CG1
ILE
67
−1.455
18.697
24.634

518
CD1
ILE
67
−2.247
18.344
25.891

519
C
ILE
67
−0.069
17.986
21.962

520
O
ILE
67
0.040
17.062
21.156

521
N
TYR
68
0.955
18.396
22.736

522
CA
TYR
68
2.200
17.694
22.765

523
CB
TYR
68
3.443
18.590
22.780

524
CG
TYR
68
3.523
19.043
21.384

525
CD1
TYR
68
4.224
18.313
20.463

526
CD2
TYR
68
2.851
20.176
21.004

527
CE1
TYR
68
4.277
18.737
19.161

528
CE2
TYR
68
2.898
20.608
19.697

529
CZ
TYR
68
3.617
19.886
18.778

530
OH
TYR
68
3.662
20.322
17.433

531
C
TYR
68
2.253
16.944
24.038

532
O
TYR
68
1.792
17.386
25.090

533
N
PRO
69
2.882
15.824
23.933

534
CA
PRO
69
3.202
15.038
25.069

535
CD
PRO
69
2.915
15.073
22.691

536
CB
PRO
69
3.936
13.813
24.523

537
CG
PRO
69
3.431
13.670
23.074

538
C
PRO
69
4.007
15.829
26.057

539
O
PRO
69
3.949
15.496
27.237

540
N
ASN
70
4.768
16.861
25.644

541
CA
ASN
70
5.568
17.531
26.632

542
CB
ASN
70
6.819
18.229
26.068

543
CG
ASN
70
6.496
18.662
24.655

544
OD1
ASN
70
6.791
17.931
23.709

545
ND2
ASN
70
5.853
19.854
24.500

546
C
ASN
70
4.704
18.552
27.302

547
O
ASN
70
5.127
19.186
28.272

548
N
ALA
71
3.458
18.695
26.808

549
CA
ALA
71
2.406
19.425
27.463

550
CB
ALA
71
2.508
19.448
28.998

551
C
ALA
71
2.346
20.827
26.941

552
O
ALA
71
1.890
21.743
27.625

553
N
SER
72
2.773
21.000
25.672

554
CA
SER
72
2.498
22.150
24.864

555
CB
SER
72
3.436
22.277
23.644

556
OG
SER
72
4.602
23.045
23.915

557
C
SER
72
1.134
21.915
24.272

558
O
SER
72
0.683
20.773
24.207

559
N
LEU
73
0.452
22.994
23.813

560
CA
LEU
73
−0.827
22.852
23.165

561
CB
LEU
73
−2.016
23.261
24.057

562
CG
LEU
73
−3.399
23.049
23.403

563
CD2
LEU
73
−4.471
23.969
24.011

564
CD1
LEU
73
−3.781
21.557
23.396

565
C
LEU
73
−0.847
23.775
21.972

566
O
LEU
73
−1.087
24.977
22.105

567
N
LEU
74
−0.610
23.229
20.753

568
CA
LEU
74
−0.598
24.051
19.568

569
CB
LEU
74
−0.156
23.316
18.282

570
CG
LEU
74
−0.267
24.177
17.002

571
CD2
LEU
74
−0.138
23.340
15.718

572
CD1
LEU
74
0.748
25.327
17.020

573
C
LEU
74
−1.992
24.525
19.315

574
O
LEU
74
−2.935
23.734
19.335

575
N
ILE
75
−2.170
25.835
19.053

576
CA
ILE
75
−3.502
26.177
18.666

577
CB
ILE
75
−4.221
27.062
19.634

578
CG2
ILE
75
−3.274
28.196
20.064

579
CG1
ILE
75
−5.545
27.515
19.002

580
CD1
ILE
75
−6.379
28.415
19.905

581
C
ILE
75
−3.471
26.825
17.326

582
O
ILE
75
−2.878
27.885
17.129

583
N
GLN
76
−4.136
26.162
16.359

584
CA
GLN
76
−4.247
26.649
15.025

585
CB
GLN
76
−4.646
25.581
14.007

586
CG
GLN
76
−3.712
24.375
14.018

587
CD
GLN
76
−3.793
23.724
12.649

588
OE1
GLN
76
−4.801
23.892
11.968

589
NE2
GLN
76
−2.734
22.979
12.236

590
C
GLN
76
−5.330
27.655
15.023

591
O
GLN
76
−5.691
28.142
16.092

592
N
ASN
77
−5.828
27.970
13.806

593
CA
ASN
77
−6.387
29.227
13.370

594
CB
ASN
77
−7.479
29.103
12.273

595
CG
ASN
77
−7.018
28.322
11.026

596
OD1
ASN
77
−7.583
28.495
9.948

597
ND2
ASN
77
−6.007
27.427
11.144

598
C
ASN
77
−6.998
29.921
14.547

599
O
ASN
77
−8.032
29.494
15.056

600
N
VAL
78
−6.320
30.971
15.062

601
CA
VAL
78
−6.584
31.388
16.413

602
CB
VAL
78
−5.343
31.851
17.167

603
CG1
VAL
78
−4.099
31.157
16.600

604
CG2
VAL
78
−5.213
33.380
17.105

605
C
VAL
78
−7.574
32.510
16.381

606
O
VAL
78
−8.465
32.609
17.226

607
N
THR
79
−7.440
33.384
15.370

608
CA
THR
79
−8.198
34.592
15.248

609
CB
THR
79
−9.577
34.395
14.699

610
OG1
THR
79
−10.483
33.977
15.715

611
CG2
THR
79
−9.483
33.329
13.601

612
C
THR
79
−8.320
35.286
16.568

613
O
THR
79
−7.595
35.007
17.519

614
N
GLN
80
−9.249
36.262
16.615

615
CA
GLN
80
−9.376
37.212
17.684

616
CB
GLN
80
−9.973
38.543
17.223

617
CG
GLN
80
−11.491
38.579
17.400

618
CD
GLN
80
−11.834
39.953
17.929

619
OE1
GLN
80
−12.718
40.121
18.766

620
NE2
GLN
80
−11.093
40.979
17.432

621
C
GLN
80
−10.353
36.651
18.656

622
O
GLN
80
−10.398
37.032
19.826

623
N
ASN
81
−11.180
35.716
18.178

624
CA
ASN
81
−12.133
35.122
19.047

625
CB
ASN
81
−12.973
34.046
18.346

626
CG
ASN
81
−14.287
34.699
17.923

627
OD1
ASN
81
−15.084
34.153
17.159

628
ND2
ASN
81
−14.523
35.928
18.453

629
C
ASN
81
−11.359
34.475
20.138

630
O
ASN
81
−11.593
34.734
21.316

631
N
ASP
82
−10.404
33.604
19.767

632
CA
ASP
82
−9.833
32.726
20.737

633
CB
ASP
82
−9.205
31.481
20.100

634
CG
ASP
82
−10.386
30.651
19.647

635
OD1
ASP
82
−11.519
31.193
19.745

636
OD2
ASP
82
−10.191
29.477
19.230

637
C
ASP
82
−8.796
33.446
21.533

638
O
ASP
82
−8.042
32.820
22.273

639
N
THR
83
−8.749
34.787
21.448

640
CA
THR
83
−7.851
35.492
22.310

641
CB
THR
83
−7.897
36.982
22.138

642
OG1
THR
83
−6.609
37.535
22.336

643
CG2
THR
83
−8.890
37.562
23.163

644
C
THR
83
−8.266
35.179
23.709

645
O
THR
83
−9.352
34.649
23.933

646
N
GLY
84
−7.413
35.488
24.702

647
CA
GLY
84
−7.838
35.281
26.051

648
C
GLY
84
−6.994
34.236
26.684

649
O
GLY
84
−6.137
33.627
26.051

650
N
PHE
85
−7.231
34.030
27.992

651
CA
PHE
85
−6.397
33.238
28.854

652
CB
PHE
85
−6.517
33.701
30.318

653
CG
PHE
85
−6.046
32.659
31.298

654
CD1
PHE
85
−4.767
32.704
31.776

655
CD2
PHE
85
−6.900
31.689
31.741

656
CE1
PHE
85
−4.323
31.753
32.688

657
CE2
PHE
85
−6.471
30.734
32.647

658
CZ
PHE
85
−5.187
30.780
33.136

659
C
PHE
85
−6.876
31.828
28.765

660
O
PHE
85
−8.080
31.576
28.717

661
N
TYR
86
−5.926
30.871
28.763

662
CA
TYR
86
−6.273
29.500
28.973

663
CB
TYR
86
−5.940
28.538
27.802

664
CG
TYR
86
−6.581
28.958
26.506

665
CD1
TYR
86
−6.710
30.277
26.126

666
CD2
TYR
86
−7.044
27.984
25.643

667
CE1
TYR
86
−7.292
30.622
24.922

668
CE2
TYR
86
−7.626
28.318
24.440

669
CZ
TYR
86
−7.753
29.635
24.078

670
OH
TYR
86
−8.350
29.950
22.836

671
C
TYR
86
−5.426
29.078
30.120

672
O
TYR
86
−4.471
29.754
30.498

673
N
THR
87
−5.765
27.928
30.718

674
CA
THR
87
−4.995
27.432
31.810

675
CB
THR
87
−5.724
27.415
33.120

676
OG1
THR
87
−4.842
27.050
34.170

677
CG2
THR
87
−6.839
26.368
33.004

678
C
THR
87
−4.758
25.996
31.496

679
O
THR
87
−5.291
25.467
30.524

680
N
LEU
88
−3.955
25.326
32.328

681
CA
LEU
88
−3.808
23.925
32.086

682
CB
LEU
88
−2.394
23.538
31.660

683
CG
LEU
88
−2.248
22.027
31.439

684
CD2
LEU
88
−0.946
21.529
32.082

685
CD1
LEU
88
−2.419
21.666
29.955

686
C
LEU
88
−4.070
23.210
33.358

687
O
LEU
88
−3.830
23.751
34.435

688
N
GLN
89
−4.571
21.963
33.265

689
CA
GLN
89
−4.646
21.182
34.451

690
CB
GLN
89
−6.057
20.811
34.918

691
CG
GLN
89
−6.094
20.204
36.330

692
CD
GLN
89
−7.509
20.311
36.904

693
OE1
GLN
89
−7.734
20.967
37.921

694
NE2
GLN
89
−8.494
19.638
36.244

695
C
GLN
89
−3.927
19.906
34.180

696
O
GLN
89
−3.508
19.612
33.063

697
N
VAL
90
−3.700
19.147
35.263

698
CA
VAL
90
−2.942
17.928
35.255

699
CB
VAL
90
−1.454
18.140
35.160

700
CG1
VAL
90
−0.880
17.340
33.980

701
CG2
VAL
90
−1.164
19.659
35.117

702
C
VAL
90
−3.134
17.318
36.603

703
O
VAL
90
−2.750
17.912
37.607

704
N
ILE
91
−3.727
16.117
36.697

705
CA
ILE
91
−3.602
15.391
37.926

706
CB
ILE
91
−4.600
14.277
38.106

707
CG2
ILE
91
−5.118
14.244
39.570

708
CG1
ILE
91
−5.734
14.456
37.075

709
CD1
ILE
91
−5.569
13.686
35.757

710
C
ILE
91
−2.316
14.660
37.834

711
O
ILE
91
−1.698
14.548
36.779

712
N
LYS
92
−1.906
14.114
38.978

713
CA
LYS
92
−1.403
12.789
38.962

714
CB
LYS
92
0.108
12.622
39.171

715
CG
LYS
92
0.952
13.898
39.275

716
CD
LYS
92
2.360
13.651
39.827

717
CE
LYS
92
2.868
14.768
40.746

718
NZ
LYS
92
3.890
15.573
40.035

719
C
LYS
92
−2.082
12.159
40.106

720
O
LYS
92
−2.862
12.807
40.788

721
N
SER
93
−1.826
10.873
40.375

722
CA
SER
93
−2.558
10.409
41.503

723
CB
SER
93
−2.800
8.890
41.511

724
OG
SER
93
−4.065
8.626
42.092

725
C
SER
93
−1.763
10.774
42.706

726
O
SER
93
−1.221
9.889
43.378

727
N
ASP
94
−1.670
12.088
43.016

728
CA
ASP
94
−1.002
12.443
44.232

729
CB
ASP
94
0.428
11.908
44.302

730
CG
ASP
94
0.470
11.077
45.566

731
OD1
ASP
94
0.911
9.903
45.472

732
OD2
ASP
94
0.048
11.593
46.636

733
C
ASP
94
−0.906
13.930
44.439

734
O
ASP
94
−0.146
14.372
45.299

735
N
LEU
95
−1.672
14.748
43.696

736
CA
LEU
95
−1.844
16.121
44.074

737
CB
LEU
95
−0.557
16.914
44.387

738
CG
LEU
95
−0.663
17.839
45.627

739
CD2
LEU
95
−0.872
17.026
46.917

740
CD1
LEU
95
−1.704
18.954
45.420

741
C
LEU
95
−2.462
16.776
42.905

742
O
LEU
95
−2.208
16.409
41.760

743
N
VAL
96
−3.310
17.779
43.139

744
CA
VAL
96
−3.832
18.353
41.950

745
CB
VAL
96
−5.258
18.790
42.058

746
CG1
VAL
96
−5.717
19.213
40.658

747
CG2
VAL
96
−6.065
17.602
42.592

748
C
VAL
96
−2.962
19.512
41.614

749
O
VAL
96
−2.855
20.463
42.392

750
N
ASN
97
−2.306
19.451
40.436

751
CA
ASN
97
−1.519
20.565
40.045

752
CB
ASN
97
−0.066
20.210
39.747

753
CG
ASN
97
0.685
20.572
41.009

754
OD1
ASN
97
1.765
21.149
40.951

755
ND2
ASN
97
0.088
20.256
42.186

756
C
ASN
97
−2.155
21.136
38.842

757
O
ASN
97
−2.296
20.491
37.802

758
N
GLU
98
−2.579
22.391
38.977

759
CA
GLU
98
−3.261
23.033
37.913

760
CB
GLU
98
−4.363
23.984
38.422

761
CG
GLU
98
−5.405
24.351
37.366

762
CD
GLU
98
−6.060
25.664
37.772

763
OE1
GLU
98
−6.542
26.366
36.842

764
OE2
GLU
98
−6.112
25.973
38.995

765
C
GLU
98
−2.239
23.896
37.288

766
O
GLU
98
−1.894
23.738
36.119

767
N
GLU
99
−1.746
24.835
38.116

768
CA
GLU
99
−1.227
26.115
37.762

769
CB
GLU
99
−0.171
26.658
38.722

770
CG
GLU
99
0.776
27.531
37.911

771
CD
GLU
99
2.125
27.507
38.600

772
OE1
GLU
99
2.773
26.426
38.648

773
OE2
GLU
99
2.525
28.586
39.109

774
C
GLU
99
−0.555
26.094
36.432

775
O
GLU
99
0.298
25.250
36.149

776
N
ALA
100
−0.970
27.043
35.582

777
CA
ALA
100
−0.398
27.237
34.286

778
CB
ALA
100
−0.730
26.108
33.293

779
C
ALA
100
−1.073
28.479
33.797

780
O
ALA
100
−2.107
28.425
33.133

781
N
THR
101
−0.492
29.637
34.165

782
CA
THR
101
−1.033
30.933
33.868

783
CB
THR
101
−0.742
31.899
34.989

784
OG1
THR
101
−1.618
31.638
36.083

785
CG2
THR
101
−0.895
33.343
34.513

786
C
THR
101
−0.333
31.387
32.633

787
O
THR
101
0.750
30.903
32.328

788
N
GLY
102
−0.927
32.326
31.863

789
CA
GLY
102
−0.260
32.758
30.663

790
C
GLY
102
−1.298
33.092
29.642

791
O
GLY
102
−2.222
32.320
29.393

792
N
GLN
103
−1.160
34.281
29.033

793
CA
GLN
103
−2.188
34.753
28.162

794
CB
GLN
103
−2.897
36.006
28.728

795
CG
GLN
103
−4.028
36.564
27.861

796
CD
GLN
103
−4.570
37.772
28.604

797
OE1
GLN
103
−5.769
37.886
28.849

798
NE2
GLN
103
−3.645
38.698
28.991

799
C
GLN
103
−1.544
35.140
26.873

800
O
GLN
103
−0.319
35.159
26.743

801
N
PHE
104
−2.378
35.457
25.869

802
CA
PHE
104
−1.858
36.136
24.733

803
CB
PHE
104
−1.332
35.202
23.633

804
CG
PHE
104
−2.396
34.232
23.241

805
CD1
PHE
104
−2.448
32.999
23.840

806
CD2
PHE
104
−3.329
34.543
22.277

807
CE1
PHE
104
−3.412
32.086
23.488

808
CE2
PHE
104
−4.295
33.629
21.923

809
CZ
PHE
104
−4.342
32.399
22.528

810
C
PHE
104
−2.985
36.925
24.169

811
O
PHE
104
−4.122
36.815
24.619

812
N
HIS
105
−2.686
37.764
23.171

813
CA
HIS
105
−3.699
38.561
22.552

814
ND1
HIS
105
−4.316
40.623
24.898

815
CG
HIS
105
−3.250
40.546
24.028

816
CB
HIS
105
−3.382
40.064
22.622

817
NE2
HIS
105
−2.523
41.325
26.026

818
CD2
HIS
105
−2.166
40.982
24.733

819
CE1
HIS
105
−3.820
41.090
26.072

820
C
HIS
105
−3.724
38.181
21.116

821
O
HIS
105
−2.810
37.509
20.643

822
N
VAL
106
−4.769
38.609
20.372

823
CA
VAL
106
−4.764
38.447
18.941

824
CB
VAL
106
−6.036
37.862
18.404

825
CG1
VAL
106
−7.187
38.503
19.178

826
CG2
VAL
106
−6.108
38.088
16.879

827
C
VAL
106
−4.671
39.825
18.374

828
O
VAL
106
−5.184
40.761
18.991

829
N
TYR
107
−4.003
39.981
17.213

830
CA
TYR
107
−3.957
41.261
16.572

831
CB
TYR
107
−2.585
41.958
16.706

832
CG
TYR
107
−2.435
42.334
18.151

833
CD1
TYR
107
−1.993
41.432
19.094

834
CD2
TYR
107
−2.743
43.603
18.571

835
CE1
TYR
107
−1.856
41.796
20.418

836
CE2
TYR
107
−2.610
43.977
19.889

837
CZ
TYR
107
−2.174
43.062
20.824

838
OH
TYR
107
−2.036
43.448
22.175

839
C
TYR
107
−4.281
41.060
15.120

840
O
TYR
107
−3.576
40.372
14.384

841
N
PRO
108
−5.389
41.674
14.766

842
CA
PRO
108
−5.937
41.801
13.441

843
CD
PRO
108
−6.115
42.477
15.740

844
CB
PRO
108
−7.376
42.303
13.629

845
CG
PRO
108
−7.490
42.725
15.119

846
C
PRO
108
−5.109
42.808
12.699

847
O
PRO
108
−4.596
43.721
13.340

848
N
GLU
109
−4.936
42.681
11.367

849
CA
GLU
109
−3.861
43.397
10.720

850
CB
GLU
109
−3.556
42.913
9.293

851
CG
GLU
109
−3.518
41.402
9.189

852
CD
GLU
109
−4.941
40.951
8.923

853
OE1
GLU
109
−5.476
40.200
9.782

854
OE2
GLU
109
−5.503
41.339
7.863

855
C
GLU
109
−4.167
44.856
10.635

856
O
GLU
109
−5.104
45.337
11.260

857
N
LEU
110
−3.340
45.611
9.874

858
CA
LEU
110
−3.490
47.035
9.916

859
CB
LEU
110
−2.526
47.755
10.873

860
CG
LEU
110
−2.373
49.240
10.486

861
CD2
LEU
110
−0.896
49.678
10.437

862
CD1
LEU
110
−3.273
50.147
11.345

863
C
LEU
110
−3.265
47.664
8.572

864
O
LEU
110
−2.209
47.601
7.943

865
N
PRO
111
−4.315
48.348
8.227

866
CA
PRO
111
−4.434
49.224
7.094

867
CD
PRO
111
−5.570
48.141
8.927

868
CB
PRO
111
−5.711
50.020
7.342

869
CG
PRO
111
−6.550
49.151
8.299

870
C
PRO
111
−3.272
50.154
6.924

871
O
PRO
111
−2.423
50.215
7.809

872
N
LYS
112
−3.240
50.890
5.786

873
CA
LYS
112
−2.272
51.934
5.594

874
CB
LYS
112
−1.668
52.026
4.192

875
CG
LYS
112
−1.026
53.400
4.037

876
CD
LYS
112
−0.309
53.704
2.725

877
CE
LYS
112
0.036
55.198
2.670

878
NZ
LYS
112
1.278
55.437
1.902

879
C
LYS
112
−2.948
53.260
5.763

880
O
LYS
112
−3.903
53.592
5.064

881
N
PRO
113
−2.418
54.027
6.667

882
CA
PRO
113
−2.990
55.295
7.041

883
CD
PRO
113
−1.540
53.478
7.686

884
CB
PRO
113
−2.254
55.735
8.300

885
CG
PRO
113
−1.575
54.471
8.860

886
C
PRO
113
−2.886
56.333
5.971

887
O
PRO
113
−2.065
56.200
5.062

888
N
SER
114
−3.711
57.398
6.094

889
CA
SER
114
−3.767
58.464
5.136

890
CB
SER
114
−5.007
58.376
4.228

891
OG
SER
114
−5.128
59.529
3.411

892
C
SER
114
−3.885
59.748
5.903

893
O
SER
114
−4.893
59.986
6.568

894
N
ILE
115
−2.844
60.609
5.814

895
CA
ILE
115
−2.845
61.889
6.463

896
CB
ILE
115
−1.488
62.532
6.517

897
CG2
ILE
115
−1.249
63.215
5.158

898
CG1
ILE
115
−1.369
63.498
7.701

899
CD1
ILE
115
−0.502
64.726
7.409

900
C
ILE
115
−3.680
62.791
5.608

901
O
ILE
115
−4.188
62.369
4.573

902
N
SER
116
−3.818
64.066
6.026

903
CA
SER
116
−4.328
65.093
5.161

904
CB
SER
116
−5.780
64.885
4.680

905
OG
SER
116
−6.143
65.897
3.752

906
C
SER
116
−4.301
66.338
5.979

907
O
SER
116
−4.918
66.413
7.041

908
N
SER
117
−3.528
67.339
5.518

909
CA
SER
117
−3.331
68.524
6.288

910
CB
SER
117
−1.871
68.771
6.644

911
OG
SER
117
−1.734
69.985
7.368

912
C
SER
117
−3.721
69.674
5.436

913
O
SER
117
−3.764
69.572
4.212

914
N
ASN
118
−4.016
70.818
6.078

915
CA
ASN
118
−4.420
71.937
5.288

916
CB
ASN
118
−5.637
72.699
5.855

917
CG
ASN
118
−6.475
73.108
4.653

918
OD1
ASN
118
−7.671
73.360
4.774

919
ND2
ASN
118
−5.837
73.149
3.453

920
C
ASN
118
−3.281
72.893
5.189

921
O
ASN
118
−2.783
73.406
6.190

922
N
ASN
119
−2.858
73.160
3.939

923
CA
ASN
119
−2.045
74.283
3.578

924
CB
ASN
119
−2.503
75.589
4.238

925
CG
ASN
119
−2.412
76.691
3.189

926
OD1
ASN
119
−1.805
76.493
2.138

927
ND2
ASN
119
−3.009
77.871
3.495

928
C
ASN
119
−0.596
74.046
3.859

929
O
ASN
119
−0.161
74.012
5.006

930
N
SER
120
0.176
73.907
2.764

931
CA
SER
120
1.589
73.724
2.804

932
CB
SER
120
2.084
72.730
1.737

933
OG
SER
120
3.475
72.481
1.872

934
C
SER
120
2.223
75.046
2.548

935
O
SER
120
3.330
75.302
2.990

936
N
ASN
121
1.483
75.970
1.900

937
CA
ASN
121
1.851
77.362
1.905

938
CB
ASN
121
0.884
78.187
1.013

939
CG
ASN
121
1.478
78.373
−0.381

940
OD1
ASN
121
1.500
79.476
−0.927

941
ND2
ASN
121
1.944
77.245
−0.985

942
C
ASN
121
1.811
77.836
3.342

943
O
ASN
121
1.538
77.034
4.235

944
N
PRO
122
2.081
79.087
3.696

945
CA
PRO
122
2.123
79.438
5.097

946
CD
PRO
122
2.138
80.242
2.812

947
CB
PRO
122
2.563
80.901
5.158

948
CG
PRO
122
2.726
81.354
3.691

949
C
PRO
122
0.735
79.253
5.648

950
O
PRO
122
−0.186
79.337
4.843

951
N
VAL
123
0.489
78.951
6.950

952
CA
VAL
123
1.170
79.172
8.197

953
CB
VAL
123
1.289
77.929
9.016

954
CG1
VAL
123
−0.135
77.584
9.499

955
CG2
VAL
123
2.041
76.828
8.224

956
C
VAL
123
2.536
79.748
8.020

957
O
VAL
123
3.482
79.053
7.666

958
N
GLU
124
2.684
81.055
8.297

959
CA
GLU
124
4.022
81.545
8.327

960
CB
GLU
124
4.161
83.059
8.111

961
CG
GLU
124
3.373
83.609
6.929

962
CD
GLU
124
2.149
84.300
7.513

963
OE1
GLU
124
1.394
84.959
6.747

964
OE2
GLU
124
1.959
84.183
8.751

965
C
GLU
124
4.484
81.221
9.677

966
O
GLU
124
4.219
80.125
10.170

967
N
ASP
125
5.170
82.168
10.326

968
CA
ASP
125
5.497
81.926
11.688

969
CB
ASP
125
6.661
82.783
12.205

970
CG
ASP
125
7.953
82.041
11.905

971
OD1
ASP
125
9.013
82.506
12.400

972
OD2
ASP
125
7.901
80.989
11.217

973
C
ASP
125
4.286
82.265
12.488

974
O
ASP
125
3.669
83.307
12.280

975
N
LYS
126
3.947
81.372
13.437

976
CA
LYS
126
3.004
81.636
14.484

977
CB
LYS
126
3.008
83.115
14.913

978
CG
LYS
126
2.379
83.372
16.272

979
CD
LYS
126
1.476
84.604
16.267

980
CE
LYS
126
0.697
84.814
17.565

981
NZ
LYS
126
−0.112
86.049
17.460

982
C
LYS
126
1.626
81.234
14.041

983
O
LYS
126
0.647
81.899
14.376

984
N
ASP
127
1.501
80.124
13.282

985
CA
ASP
127
0.207
79.713
12.817

986
CB
ASP
127
0.025
79.924
11.312

987
CG
ASP
127
−0.213
81.426
11.077

988
OD1
ASP
127
−0.391
82.194
12.065

989
OD2
ASP
127
−0.231
81.835
9.891

990
C
ASP
127
0.068
78.259
13.142

991
O
ASP
127
0.572
77.813
14.169

992
N
ALA
128
−0.643
77.466
12.319

993
CA
ALA
128
−0.898
76.170
12.864

994
CB
ALA
128
−2.186
76.103
13.696

995
C
ALA
128
−1.040
75.169
11.773

996
O
ALA
128
−2.044
75.133
11.066

997
N
VAL
129
−0.051
74.275
11.634

998
CA
VAL
129
−0.375
73.098
10.902

999
CB
VAL
129
0.779
72.160
10.698

1000
CG1
VAL
129
0.833
71.779
9.208

1001
CG2
VAL
129
2.059
72.839
11.197

1002
C
VAL
129
−1.386
72.404
11.736

1003
O
VAL
129
−1.550
72.716
12.915

1004
N
ALA
130
−2.091
71.436
11.141

1005
CA
ALA
130
−2.805
70.497
11.938

1006
CB
ALA
130
−4.221
70.957
12.312

1007
C
ALA
130
−2.910
69.283
11.081

1008
O
ALA
130
−3.792
69.175
10.226

1009
N
PHE
131
−1.956
68.360
11.268

1010
CA
PHE
131
−1.829
67.238
10.398

1011
CB
PHE
131
−0.447
66.573
10.515

1012
CG
PHE
131
0.530
67.417
9.776

1013
CD1
PHE
131
0.126
68.151
8.694

1014
CD2
PHE
131
1.856
67.485
10.139

1015
CE1
PHE
131
0.991
68.941
7.979

1016
CE2
PHE
131
2.749
68.268
9.440

1017
CZ
PHE
131
2.312
69.000
8.360

1018
C
PHE
131
−2.827
66.245
10.846

1019
O
PHE
131
−2.722
65.707
11.947

1020
N
THR
132
−3.830
65.943
10.009

1021
CA
THR
132
−4.699
64.906
10.456

1022
CB
THR
132
−6.142
65.097
10.100

1023
OG1
THR
132
−6.642
66.275
10.711

1024
CG2
THR
132
−6.909
63.859
10.615

1025
C
THR
132
−4.246
63.636
9.821

1026
O
THR
132
−3.955
63.593
8.622

1027
N
CYS
133
−4.152
62.559
10.608

1028
CA
CYS
133
−3.922
61.266
10.036

1029
CB
CYS
133
−2.942
60.392
10.838

1030
SC
CYS
133
−2.951
58.665
10.271

1031
C
CYS
133
−5.241
60.594
10.093

1032
O
CYS
133
−6.033
60.825
11.006

1033
N
GLU
134
−5.520
59.744
9.092

1034
CA
GLU
134
−6.749
59.014
9.101

1035
CB
GLU
134
−7.682
59.319
7.908

1036
CG
GLU
134
−8.100
60.783
7.802

1037
CD
GLU
134
−9.098
60.900
6.674

1038
OE1
GLU
134
−10.190
61.482
6.905

1039
OE2
GLU
134
−8.773
60.422
5.555

1040
C
GLU
134
−6.450
57.549
9.050

1041
O
GLU
134
−5.434
57.077
8.537

1042
N
PRO
135
−7.380
56.864
9.660

1043
CA
PRO
135
−7.075
55.513
10.054

1044
CD
PRO
135
−7.905
57.600
10.790

1045
CB
PRO
135
−6.586
55.635
11.490

1046
CG
PRO
135
−7.099
57.022
11.968

1047
C
PRO
135
−8.362
54.736
10.005

1048
O
PRO
135
−9.427
55.331
10.160

1049
N
GLU
136
−8.346
53.407
9.800

1050
CA
GLU
136
−9.649
52.818
9.896

1051
CB
GLU
136
−10.376
52.575
8.548

1052
CG
GLU
136
−11.617
53.483
8.423

1053
CD
GLU
136
−12.565
53.099
7.278

1054
OE1
GLU
136
−12.914
53.996
6.461

1055
OE2
GLU
136
−12.983
51.914
7.221

1056
C
GLU
136
−9.553
51.505
10.596

1057
O
GLU
136
−10.222
50.558
10.188

1058
N
THR
137
−8.735
51.413
11.672

1059
CA
THR
137
−8.555
50.136
12.314

1060
CB
THR
137
−7.333
49.449
11.789

1061
OG1
THR
137
−6.803
48.563
12.762

1062
CG2
THR
137
−6.297
50.531
11.417

1063
C
THR
137
−8.423
50.285
13.813

1064
O
THR
137
−7.390
50.702
14.332

1065
N
GLN
138
−9.493
49.915
14.558

1066
CA
GLN
138
−9.538
50.128
15.980

1067
CB
GLN
138
−10.979
50.085
16.552

1068
CG
GLN
138
−11.079
49.776
18.050

1069
CD
GLN
138
−12.187
48.738
18.201

1070
OE1
GLN
138
−12.483
48.242
19.286

1071
NE2
GLN
138
−12.813
48.378
17.052

1072
C
GLN
138
−8.687
49.117
16.711

1073
O
GLN
138
−9.020
47.940
16.808

1074
N
ASP
139
−7.565
49.630
17.255

1075
CA
ASP
139
−6.583
49.099
18.178

1076
CB
ASP
139
−6.644
47.605
18.628

1077
CG
ASP
139
−5.732
47.470
19.878

1078
OD1
ASP
139
−6.194
46.962
20.936

1079
OD2
ASP
139
−4.546
47.884
19.787

1080
C
ASP
139
−5.271
49.394
17.542

1081
O
ASP
139
−5.055
49.099
16.368

1082
N
THR
140
−4.407
50.107
18.292

1083
CA
THR
140
−3.631
51.132
17.641

1084
CB
THR
140
−4.407
52.367
17.431

1085
OG1
THR
140
−4.937
52.755
18.684

1086
CG2
THR
140
−5.527
52.110
16.425

1087
C
THR
140
−2.571
51.650
18.555

1088
O
THR
140
−2.653
51.493
19.770

1089
N
THR
141
−1.561
52.368
18.002

1090
CA
THR
141
−0.618
53.006
18.881

1091
CB
THR
141
0.149
51.989
19.689

1092
OG1
THR
141
1.310
52.535
20.301

1093
CG2
THR
141
0.540
50.850
18.751

1094
C
THR
141
0.281
53.864
18.036

1095
O
THR
141
1.433
53.528
17.738

1096
N
TYR
142
−0.281
55.018
17.629

1097
CA
TYR
142
0.070
55.839
16.497

1098
CB
TYR
142
−1.127
56.763
16.224

1099
CG
TYR
142
−0.879
57.717
15.118

1100
CD1
TYR
142
−0.195
57.351
13.985

1101
CD2
TYR
142
−1.341
59.003
15.241

1102
CE1
TYR
142
0.018
58.246
12.960

1103
CE2
TYR
142
−1.136
59.901
14.224

1104
CZ
TYR
142
−0.453
59.530
13.091

1105
OH
TYR
142
−0.258
60.481
12.068

1106
C
TYR
142
1.264
56.679
16.841

1107
O
TYR
142
1.370
57.138
17.976

1108
N
LEU
143
2.184
56.912
15.871

1109
CA
LEU
143
3.279
57.807
16.130

1110
CB
LEU
143
4.672
57.151
15.999

1111
CG
LEU
143
5.150
56.408
17.261

1112
CD2
LEU
143
5.388
54.914
16.985

1113
CD1
LEU
143
4.196
56.660
18.435

1114
C
LEU
143
3.237
58.921
15.135

1115
O
LEU
143
2.578
58.819
14.095

1116
N
TRP
144
3.951
60.029
15.421

1117
CA
TRP
144
4.128
61.072
14.446

1118
CB
TRP
144
3.815
62.470
15.014

1119
CG
TRP
144
2.340
62.794
15.029

1120
CD2
TRP
144
1.644
63.221
13.846

1121
CD1
TRP
144
1.412
62.734
16.030

1122
NE1
TRP
144
0.170
63.065
15.536

1123
CE2
TRP
144
0.304
63.367
14.198

1124
CE3
TRP
144
2.088
63.455
12.580

1125
CZ2
TRP
144
−0.625
63.744
13.265

1126
CZ3
TRP
144
1.159
63.850
11.653

1127
CH2
TRP
144
−0.175
63.990
11.991

1128
C
TRP
144
5.575
61.022
14.049

1129
O
TRP
144
6.373
60.429
14.776

1130
N
TRP
145
5.968
61.609
12.894

1131
CA
TRP
145
7.367
61.580
12.543

1132
CB
TRP
145
7.841
60.250
11.889

1133
CG
TRP
145
7.369
58.918
12.469

1134
CD2
TRP
145
7.866
58.298
13.679

1135
CD1
TRP
145
6.458
58.042
11.947

1136
NE1
TRP
145
6.367
56.921
12.736

1137
CE2
TRP
145
7.224
57.062
13.808

1138
CE3
TRP
145
8.792
58.710
14.602

1139
CZ2
TRP
145
7.495
56.226
14.848

1140
CZ3
TRP
145
9.044
57.860
15.660

1141
CH2
TRP
145
8.416
56.639
15.781

1142
C
TRP
145
7.667
62.697
11.558

1143
O
TRP
145
6.796
63.125
10.796

1144
N
ILE
146
8.929
63.211
11.588

1145
CA
ILE
146
9.384
64.301
10.756

1146
CB
ILE
146
9.593
65.594
11.491

1147
CG2
ILE
146
10.050
65.253
12.910

1148
CG1
ILE
146
10.584
66.476
10.727

1149
CD1
ILE
146
11.308
67.487
11.605

1150
C
ILE
146
10.716
63.948
10.155

1151
O
ILE
146
11.567
63.339
10.806

1152
N
ASN
147
10.922
64.364
8.884

1153
CA
ASN
147
12.031
64.003
8.030

1154
CB
ASN
147
13.335
64.777
8.299

1155
CG
ASN
147
13.123
66.211
7.824

1156
OD1
ASN
147
13.176
66.513
6.634

1157
ND2
ASN
147
12.859
67.120
8.794

1158
C
ASN
147
12.289
62.538
8.137

1159
O
ASN
147
13.407
62.070
7.921

1160
N
ASN
148
11.233
61.769
8.445

1161
CA
ASN
148
11.361
60.351
8.515

1162
CB
ASN
148
11.800
59.755
7.161

1163
CG
ASN
148
11.819
58.235
7.206

1164
OD1
ASN
148
12.857
57.621
6.963

1165
ND2
ASN
148
10.658
57.612
7.550

1166
C
ASN
148
12.379
60.056
9.558

1167
O
ASN
148
13.111
59.077
9.468

1168
N
GLN
149
12.427
60.881
10.616

1169
CA
GLN
149
13.099
60.403
11.776

1170
CB
GLN
149
14.621
60.360
11.671

1171
CG
GLN
149
15.191
59.277
12.586

1172
CD
GLN
149
16.712
59.395
12.604

1173
OE1
GLN
149
17.255
60.477
12.385

1174
NE2
GLN
149
17.402
58.263
12.901

1175
C
GLN
149
12.753
61.240
12.962

1176
O
GLN
149
13.362
62.274
13.224

1177
N
SER
150
11.792
60.758
13.765

1178
CA
SER
150
11.660
61.156
15.136

1179
CB
SER
150
13.001
61.274
15.878

1180
OG
SER
150
13.394
59.986
16.315

1181
C
SER
150
10.968
62.457
15.261

1182
O
SER
150
11.252
63.385
14.510

1183
N
LEU
151
10.070
62.564
16.261

1184
CA
LEU
151
9.613
63.878
16.561

1185
CB
LEU
151
8.320
64.283
15.856

1186
CG
LEU
151
8.054
65.789
16.078

1187
CD2
LEU
151
6.858
66.324
15.282

1188
CD1
LEU
151
9.323
66.625
15.839

1189
C
LEU
151
9.377
64.000
18.028

1190
O
LEU
151
8.231
64.008
18.488

1191
N
PRO
152
10.461
64.195
18.733

1192
CA
PRO
152
10.451
65.338
19.586

1193
CD
PRO
152
11.704
64.227
17.974

1194
CB
PRO
152
10.911
66.441
18.667

1195
CG
PRO
152
12.000
65.728
17.830

1196
C
PRO
152
9.354
65.655
20.582

1197
O
PRO
152
9.629
65.554
21.780

1198
N
VAL
153
8.140
66.097
20.164

1199
CA
VAL
153
7.144
66.818
20.956

1200
CB
VAL
153
6.193
66.086
21.874

1201
CG1
VAL
153
5.605
67.152
22.830

1202
CG2
VAL
153
5.103
65.312
21.126

1203
C
VAL
153
7.778
67.785
21.894

1204
O
VAL
153
8.354
67.445
22.928

1205
N
SER
154
7.614
69.063
21.565

1206
CA
SER
154
8.202
70.059
22.390

1207
CB
SER
154
9.424
70.660
21.717

1208
OG
SER
154
9.461
70.231
20.363

1209
C
SER
154
7.141
71.088
22.471

1210
O
SER
154
6.263
71.053
21.611

1211
N
PRO
155
7.129
71.951
23.467

1212
CA
PRO
155
5.859
72.359
24.012

1213
CD
PRO
155
8.140
71.923
24.518

1214
CB
PRO
155
6.186
73.305
25.168

1215
CG
PRO
155
7.549
72.788
25.678

1216
C
PRO
155
4.847
72.870
23.044

1217
O
PRO
155
3.657
72.621
23.252

1218
N
ARG
156
5.241
73.546
21.960

1219
CA
ARG
156
4.234
74.145
21.126

1220
CB
ARG
156
4.768
75.000
19.970

1221
CG
ARG
156
6.278
75.067
19.905

1222
CD
ARG
156
6.766
75.606
18.569

1223
NE
ARG
156
7.413
74.490
17.802

1224
CZ
ARG
156
7.879
74.722
16.544

1225
NH1
ARG
156
7.598
75.914
15.921

1226
NH2
ARG
156
8.652
73.797
15.895

1227
C
ARG
156
3.391
73.108
20.468

1228
O
ARG
156
2.324
73.428
19.938

1229
N
LEU
157
3.826
71.839
20.457

1230
CA
LEU
157
2.977
70.955
19.718

1231
CB
LEU
157
3.629
69.616
19.301

1232
CG
LEU
157
4.773
69.785
18.283

1233
CD2
LEU
157
5.285
68.437
17.732

1234
CD1
LEU
157
5.906
70.640
18.868

1235
C
LEU
157
1.762
70.664
20.546

1236
O
LEU
157
1.756
70.892
21.755

1237
N
GLN
158
0.678
70.176
19.907

1238
CA
GLN
158
−0.417
69.590
20.628

1239
CB
GLN
158
−1.700
70.445
20.737

1240
CG
GLN
158
−2.746
69.805
21.654

1241
CD
GLN
158
−4.120
70.450
21.479

1242
OE1
GLN
158
−5.029
70.129
22.243

1243
NE2
GLN
158
−4.281
71.370
20.491

1244
C
GLN
158
−0.827
68.410
19.823

1245
O
GLN
158
−0.592
68.339
18.618

1246
N
LEU
159
−1.478
67.443
20.476

1247
CA
LEU
159
−2.092
66.411
19.711

1248
CB
LEU
159
−1.124
65.250
19.442

1249
CG
LEU
159
−0.095
65.059
20.572

1250
CD2
LEU
159
1.170
64.355
20.063

1251
CD1
LEU
159
−0.707
64.375
21.815

1252
C
LEU
159
−3.213
65.931
20.559

1253
O
LEU
159
−3.132
65.996
21.780

1254
N
SER
160
−4.319
65.453
19.962

1255
CA
SER
160
−5.327
64.916
20.827

1256
CB
SER
160
−6.367
65.955
21.304

1257
OG
SER
160
−6.954
66.625
20.200

1258
C
SER
160
−6.022
63.840
20.062

1259
O
SER
160
−5.645
63.527
18.937

1260
N
ASN
161
−7.065
63.252
20.665

1261
CA
ASN
161
−7.913
62.384
19.916

1262
CB
ASN
161
−8.480
63.062
18.660

1263
CG
ASN
161
−9.968
63.259
18.832

1264
OD1
ASN
161
−10.693
63.578
17.887

1265
ND2
ASN
161
−10.453
63.051
20.090

1266
C
ASN
161
−7.131
61.203
19.425

1267
O
ASN
161
−7.281
60.814
18.268

1268
N
GLY
162
−6.293
60.591
20.284

1269
CA
GLY
162
−5.693
59.323
19.982

1270
C
GLY
162
−4.555
59.525
19.025

1271
O
GLY
162
−4.356
58.736
18.104

1272
N
ASN
163
−3.786
60.612
19.239

1273
CA
ASN
163
−2.645
61.015
18.454

1274
CB
ASN
163
−1.567
59.946
18.220

1275
CG
ASN
163
−0.936
59.463
19.510

1276
OD1
ASN
163
−1.205
58.313
19.854

1277
ND2
ASN
163
−0.089
60.291
20.194

1278
C
ASN
163
−3.061
61.357
17.075

1279
O
ASN
163
−2.220
61.793
16.289

1280
N
ARG
164
−4.328
61.123
16.719

1281
CA
ARG
164
−4.671
61.193
15.337

1282
CB
ARG
164
−6.150
60.870
15.167

1283
CG
ARG
164
−6.575
60.616
13.738

1284
CD
ARG
164
−8.095
60.641
13.630

1285
NE
ARG
164
−8.445
61.816
12.814

1286
CZ
ARG
164
−9.480
61.697
11.942

1287
NH1
ARG
164
−9.850
62.747
11.170

1288
NH2
ARG
164
−10.144
60.511
11.868

1289
C
ARG
164
−4.429
62.602
14.907

1290
O
ARG
164
−3.640
62.875
14.005

1291
N
THR
165
−5.101
63.536
15.602

1292
CA
THR
165
−5.025
64.925
15.296

1293
CB
THR
165
−6.118
65.718
15.934

1294
OG1
THR
165
−6.042
65.578
17.343

1295
CG2
THR
165
−7.463
65.223
15.398

1296
C
THR
165
−3.775
65.456
15.893

1297
O
THR
165
−3.466
65.182
17.049

1298
N
LEU
166
−3.021
66.259
15.126

1299
CA
LEU
166
−1.930
66.979
15.714

1300
CB
LEU
166
−0.541
66.423
15.350

1301
CG
LEU
166
0.557
67.483
15.162

1302
CD2
LEU
166
1.615
67.004
14.162

1303
CD1
LEU
166
1.147
67.941
16.515

1304
C
LEU
166
−2.007
68.359
15.172

1305
O
LEU
166
−2.498
68.589
14.067

1306
N
THR
167
−1.552
69.339
15.968

1307
CA
THR
167
−1.668
70.677
15.477

1308
CB
THR
167
−2.855
71.391
16.041

1309
OG1
THR
167
−2.562
72.780
16.154

1310
CG2
THR
167
−3.169
70.815
17.430

1311
C
THR
167
−0.465
71.391
15.962

1312
O
THR
167
−0.181
71.396
17.158

1313
N
LEU
168
0.289
72.022
15.049

1314
CA
LEU
168
1.290
72.859
15.600

1315
CB
LEU
168
2.606
72.937
14.805

1316
CG
LEU
168
3.782
73.227
15.755

1317
CD2
LEU
168
5.131
73.221
15.017

1318
CD1
LEU
168
3.720
72.297
16.979

1319
C
LEU
168
0.723
74.225
15.676

1320
O
LEU
168
−0.260
74.543
14.991

1321
N
LEU
169
1.317
75.042
16.553

1322
CA
LEU
169
0.882
76.376
16.804

1323
CB
LEU
169
−0.632
76.460
17.083

1324
CG
LEU
169
−1.072
77.683
17.912

1325
CD2
LEU
169
−2.608
77.791
17.936

1326
CD1
LEU
169
−0.375
78.974
17.461

1327
C
LEU
169
1.623
76.775
18.025

1328
O
LEU
169
1.399
76.228
19.104

1329
N
SER
170
2.552
77.726
17.860

1330
CA
SER
170
2.780
78.205
16.538

1331
CB
SER
170
3.523
79.556
16.507

1332
OG
SER
170
4.895
79.374
16.206

1333
C
SER
170
3.625
77.173
15.866

1334
O
SER
170
3.979
76.150
16.452

1335
N
VAL
171
3.975
77.413
14.596

1336
CA
VAL
171
4.955
76.597
13.951

1337
CB
VAL
171
4.426
75.975
12.690

1338
CG1
VAL
171
4.238
77.095
11.648

1339
CG2
VAL
171
5.332
74.814
12.231

1340
C
VAL
171
6.053
77.555
13.620

1341
O
VAL
171
5.907
78.760
13.837

1342
N
THR
172
7.204
77.082
13.127

1343
CA
THR
172
8.229
78.059
12.932

1344
CB
THR
172
9.369
77.930
13.923

1345
OG1
THR
172
10.238
79.044
13.809

1346
CG2
THR
172
10.116
76.587
13.752

1347
C
THR
172
8.726
77.950
11.525

1348
O
THR
172
7.946
77.812
10.582

1349
N
ARG
173
10.055
78.037
11.351

1350
CA
ARG
173
10.712
77.906
10.090

1351
CB
ARG
173
11.891
78.869
10.037

1352
CG
ARG
173
12.246
79.290
11.463

1353
CD
ARG
173
13.280
80.396
11.594

1354
NE
ARG
173
14.249
79.943
12.637

1355
CZ
ARG
173
15.563
80.299
12.526

1356
NH1
ARG
173
15.944
81.135
11.512

1357
NH2
ARG
173
16.487
79.825
13.412

1358
C
ARG
173
11.300
76.529
10.069

1359
O
ARG
173
11.664
76.003
9.020

1360
N
ASN
174
11.435
75.925
11.265

1361
CA
ASN
174
12.241
74.748
11.421

1362
CB
ASN
174
12.724
74.557
12.864

1363
CG
ASN
174
13.733
73.424
12.886

1364
OD1
ASN
174
13.783
72.684
13.866

1365
ND2
ASN
174
14.514
73.254
11.780

1366
C
ASN
174
11.447
73.537
11.064

1367
O
ASN
174
11.954
72.418
11.058

1368
N
ASP
175
10.154
73.725
10.772

1369
CA
ASP
175
9.361
72.570
10.490

1370
CB
ASP
175
7.976
72.613
11.181

1371
CG
ASP
175
8.210
73.012
12.643

1372
OD1
ASP
175
8.634
74.179
12.858

1373
OD2
ASP
175
7.979
72.175
13.557

1374
C
ASP
175
9.220
72.534
9.002

1375
O
ASP
175
8.140
72.704
8.444

1376
N
THR
176
10.382
72.352
8.335

1377
CA
THR
176
10.522
72.428
6.910

1378
CB
THR
176
11.714
73.259
6.495

1379
OG1
THR
176
12.039
73.014
5.127

1380
CG2
THR
176
12.900
72.886
7.416

1381
C
THR
176
10.769
71.025
6.460

1382
O
THR
176
11.903
70.559
6.356

1383
N
GLY
177
9.684
70.284
6.206

1384
CA
GLY
177
9.890
68.928
5.832

1385
C
GLY
177
8.569
68.236
5.912

1386
O
GLY
177
7.613
68.622
6.587

1387
N
PRO
178
8.569
67.174
5.196

1388
CA
PRO
178
7.407
66.352
5.100

1389
CD
PRO
178
9.530
66.962
4.138

1390
CB
PRO
178
7.687
65.364
3.979

1391
CG
PRO
178
8.871
65.955
3.190

1392
C
PRO
178
7.170
65.663
6.399

1393
O
PRO
178
8.125
65.312
7.093

1394
N
TYR
179
5.893
65.439
6.744

1395
CA
TYR
179
5.615
64.802
7.988

1396
CB
TYR
179
4.871
65.704
8.979

1397
CG
TYR
179
5.887
66.576
9.640

1398
CD1
TYR
179
6.052
66.541
11.007

1399
CD2
TYR
179
6.677
67.435
8.900

1400
CE1
TYR
179
6.987
67.336
11.624

1401
CE2
TYR
179
7.609
68.230
9.512

1402
CZ
TYR
179
7.768
68.191
10.879

1403
OH
TYR
179
8.728
68.999
11.511

1404
C
TYR
179
4.736
63.637
7.705

1405
O
TYR
179
3.547
63.787
7.422

1406
N
GLU
180
5.336
62.436
7.776

1407
CA
GLU
180
4.658
61.203
7.559

1408
CB
GLU
180
5.624
60.064
7.207

1409
CG
GLU
180
4.982
58.850
6.546

1410
CD
GLU
180
6.055
58.282
5.622

1411
OE1
GLU
180
7.232
58.252
6.070

1412
OE2
GLU
180
5.738
57.899
4.463

1413
C
GLU
180
4.020
60.855
8.862

1414
O
GLU
180
4.252
61.509
9.876

1415
N
CYS
181
3.189
59.801
8.852

1416
CA
CYS
181
2.527
59.300
10.017

1417
CB
CYS
181
0.984
59.317
9.873

1418
SG
CYS
181
0.219
57.783
9.238

1419
C
CYS
181
3.008
57.894
10.154

1420
O
CYS
181
3.934
57.487
9.452

1421
N
GLU
182
2.414
57.108
11.071

1422
CA
GLU
182
2.772
55.724
11.127

1423
CB
GLU
182
4.246
55.464
11.503

1424
CG
GLU
182
5.015
54.612
10.480

1425
CD
GLU
182
5.648
53.403
11.166

1426
OE1
GLU
182
6.157
53.562
12.305

1427
OE2
GLU
182
5.643
52.295
10.564

1428
C
GLU
182
1.965
55.133
12.220

1429
O
GLU
182
2.258
55.353
13.391

1430
N
ILE
183
0.928
54.353
11.885

1431
CA
ILE
183
0.287
53.679
12.964

1432
CB
ILE
183
−1.111
53.259
12.650

1433
CG2
ILE
183
−1.782
52.867
13.969

1434
CG1
ILE
183
−1.832
54.401
11.909

1435
CD1
ILE
183
−3.267
54.629
12.377

1436
C
ILE
183
1.144
52.497
13.260

1437
O
ILE
183
2.151
52.286
12.587

1438
N
GLN
184
0.802
51.700
14.296

1439
CA
GLN
184
1.638
50.567
14.581

1440
CB
GLN
184
2.669
50.802
15.705

1441
CG
GLN
184
4.056
50.225
15.390

1442
CD
GLN
184
4.927
50.193
16.649

1443
OE1
GLN
184
5.396
49.137
17.072

1444
NE2
GLN
184
5.168
51.383
17.261

1445
C
GLN
184
0.741
49.476
15.063

1446
O
GLN
184
−0.396
49.344
14.614

1447
N
ASN
185
1.276
48.684
16.014

1448
CA
ASN
185
0.633
47.649
16.776

1449
CB
ASN
185
−0.604
47.002
16.082

1450
CG
ASN
185
−0.273
45.722
15.314

1451
OD1
ASN
185
−0.708
44.623
15.666

1452
ND2
ASN
185
0.493
45.873
14.205

1453
C
ASN
185
1.726
46.652
17.029

1454
O
ASN
185
2.874
46.979
16.734

1455
N
PRO
186
1.505
45.481
17.558

1456
CA
PRO
186
2.571
44.523
17.658

1457
CD
PRO
186
0.300
45.078
18.258

1458
CB
PRO
186
1.982
43.260
18.296

1459
CG
PRO
186
0.619
43.711
18.878

1460
C
PRO
186
3.065
44.285
16.270

1461
O
PRO
186
2.232
44.162
15.374

1462
N
VAL
187
4.407
44.251
16.091

1463
CA
VAL
187
5.150
44.369
14.864

1464
CB
VAL
187
6.318
43.418
14.763

1465
CG1
VAL
187
7.326
44.001
13.758

1466
CG2
VAL
187
6.881
43.129
16.166

1467
C
VAL
187
4.315
44.145
13.642

1468
O
VAL
187
4.443
43.107
12.987

1469
N
SER
188
3.459
45.116
13.273

1470
CA
SER
188
2.970
45.175
11.927

1471
CB
SER
188
1.711
44.342
11.669

1472
OG
SER
188
2.074
42.969
11.676

1473
C
SER
188
2.633
46.598
11.696

1474
O
SER
188
2.118
47.272
12.589

1475
N
ALA
189
2.965
47.116
10.500

1476
CA
ALA
189
2.863
48.535
10.358

1477
CB
ALA
189
4.180
49.263
10.665

1478
C
ALA
189
2.549
48.863
8.937

1479
O
ALA
189
2.902
48.122
8.020

1480
N
ASN
190
1.899
50.030
8.729

1481
CA
ASN
190
1.862
50.684
7.452

1482
CB
ASN
190
0.476
50.686
6.779

1483
CG
ASN
190
0.332
49.449
5.902

1484
OD1
ASN
190
−0.330
48.487
6.286

1485
ND2
ASN
190
0.992
49.463
4.715

1486
C
ASN
190
2.181
52.116
7.730

1487
O
ASN
190
1.663
52.693
8.686

1488
N
ARG
191
3.050
52.729
6.905

1489
CA
ARG
191
3.341
54.108
7.114

1490
CB
ARG
191
4.743
54.501
6.630

1491
CG
ARG
191
5.838
53.910
7.532

1492
CD
ARG
191
7.253
54.088
6.981

1493
NE
ARG
191
8.195
54.110
8.135

1494
CZ
ARG
191
9.463
54.588
7.965

1495
NH1
ARG
191
9.860
55.036
6.735

1496
NH2
ARG
191
10.328
54.630
9.002

1497
C
ARG
191
2.291
54.868
6.382

1498
O
ARG
191
1.161
54.394
6.291

1499
N
SER
192
2.632
56.080
5.869

1500
CA
SER
192
1.622
56.918
5.270

1501
CB
SER
192
0.941
57.867
6.252

1502
OG
SER
192
1.937
58.707
6.805

1503
C
SER
192
2.237
57.790
4.221

1504
O
SER
192
3.327
57.520
3.729

1505
N
ASP
193
1.503
58.867
3.851

1506
CA
ASP
193
1.844
59.687
2.729

1507
CB
ASP
193
0.617
60.136
1.928

1508
CG
ASP
193
−0.214
61.033
2.831

1509
OD1
ASP
193
−0.284
62.253
2.537

1510
OD2
ASP
193
−0.795
60.522
3.825

1511
C
ASP
193
2.568
60.911
3.194

1512
O
ASP
193
2.384
61.423
4.305

1513
N
PRO
194
3.442
61.342
2.326

1514
CA
PRO
194
4.645
61.952
2.807

1515
CD
PRO
194
3.655
60.565
1.122

1516
CB
PRO
194
5.798
61.242
2.093

1517
CG
PRO
194
5.148
60.213
1.137

1518
C
PRO
194
4.593
63.407
2.499

1519
O
PRO
194
5.478
63.909
1.817

1520
N
VAL
195
3.539
64.092
2.989

1521
CA
VAL
195
3.218
65.438
2.618

1522
CB
VAL
195
1.940
65.890
3.271

1523
CG1
VAL
195
0.839
64.901
2.911

1524
CG2
VAL
195
2.162
65.900
4.796

1525
C
VAL
195
4.330
66.337
3.070

1526
O
VAL
195
4.810
66.200
4.197

1527
N
THR
196
4.801
67.269
2.215

1528
CA
THR
196
5.909
68.104
2.619

1529
CB
THR
196
6.932
68.383
1.561

1530
OG1
THR
196
6.972
69.779
1.301

1531
CG2
THR
196
6.555
67.623
0.283

1532
C
THR
196
5.374
69.438
2.998

1533
O
THR
196
4.428
69.942
2.388

1534
N
LEU
197
5.976
70.066
4.022

1535
CA
LEU
197
5.496
71.369
4.332

1536
CB
LEU
197
4.846
71.506
5.710

1537
CG
LEU
197
4.012
72.792
5.784

1538
CD2
LEU
197
4.693
73.850
6.659

1539
CD1
LEU
197
2.563
72.498
6.188

1540
C
LEU
197
6.644
72.311
4.311

1541
O
LEU
197
7.580
72.197
5.103

1542
N
ASN
198
6.588
73.290
3.396

1543
CA
ASN
198
7.564
74.322
3.446

1544
CB
ASN
198
8.466
74.356
2.219

1545
CG
ASN
198
8.878
72.904
2.012

1546
OD1
ASN
198
9.507
72.312
2.888

1547
ND2
ASN
198
8.484
72.316
0.852

1548
C
ASN
198
6.821
75.601
3.534

1549
O
ASN
198
5.792
75.813
2.912

1550
N
VAL
199
7.333
76.495
4.374

1551
CA
VAL
199
6.557
77.613
4.778

1552
CB
VAL
199
6.840
77.858
6.242

1553
CG1
VAL
199
8.193
77.219
6.573

1554
CG2
VAL
199
6.813
79.351
6.565

1555
C
VAL
199
6.973
78.774
3.908

1556
O
VAL
199
7.990
78.707
3.214

1557
N
THR
200
6.185
79.870
3.900

1558
CA
THR
200
6.728
81.171
3.623

1559
CB
THR
200
6.094
81.916
2.481

1560
OG1
THR
200
6.227
81.169
1.276

1561
CG2
THR
200
6.776
83.288
2.348

1562
C
THR
200
6.337
81.976
4.804

1563
O
THR
200
5.256
81.771
5.355

1564
N
TYR
201
7.193
82.910
5.249

1565
CA
TYR
201
6.792
83.623
6.413

1566
CB
TYR
201
7.897
83.850
7.454

1567
CG
TYR
201
9.306
83.647
6.952

1568
CD1
TYR
201
9.758
84.189
5.769

1569
CD2
TYR
201
10.212
82.922
7.709

1570
CE1
TYR
201
11.054
83.995
5.352

1571
CE2
TYR
201
11.509
82.728
7.291

1572
CZ
TYR
201
11.937
83.265
6.108

1573
OH
TYR
201
13.266
83.069
5.669

1574
C
TYR
201
6.237
84.945
6.007

1575
O
TYR
201
6.022
85.205
4.824

1576
N
GLY
202
5.958
85.815
6.996

1577
CA
GLY
202
5.526
87.138
6.678

1578
C
GLY
202
6.519
88.088
7.275

1579
O
GLY
202
6.408
88.501
8.426

1580
N
PRO
203
7.540
88.402
6.524

1581
CA
PRO
203
8.742
88.910
7.125

1582
CD
PRO
203
7.826
87.571
5.373

1583
CB
PRO
203
9.927
88.292
6.401

1584
CG
PRO
203
9.325
87.222
5.468

1585
C
PRO
203
8.814
90.394
7.014

1586
O
PRO
203
7.777
91.011
6.660

1587
OXT
PRO
203
9.914
90.948
7.270

[0139]

8

TABLE 5

Full coordinate set of D1 of human CEACAM1a

(homology model)

ANum
AType
RType
RNum
X
Y
Z

1
N
GLN
1
7.864
28.910
40.421

2
CA
GLN
1
7.905
27.435
40.349

3
CB
GLN
1
6.753
26.828
41.151

4
CG
GLN
1
5.434
27.551
40.885

5
CD
GLN
1
4.357
26.911
41.737

6
OE1
GLN
1
4.478
25.734
42.076

7
NE2
GLN
1
3.289
27.681
42.089

8
C
GLN
1
7.774
26.958
38.948

9
O
GLN
1
6.836
26.227
38.632

10
N
LEU
2
8.764
27.359
38.125

11
CA
LEU
2
9.167
26.717
36.915

12
CB
LEU
2
10.129
25.553
37.221

13
CG
LEU
2
10.535
24.698
36.012

14
CD2
LEU
2
10.824
23.248
36.438

15
CD1
LEU
2
11.682
25.358
35.232

16
C
LEU
2
7.991
26.166
36.179

17
O
LEU
2
7.736
24.967
36.238

18
N
THR
3
7.241
26.998
35.441

19
CA
THR
3
6.453
26.341
34.443

20
CB
THR
3
4.973
26.259
34.701

21
OG1
THR
3
4.432
27.544
34.942

22
CG2
THR
3
4.743
25.336
35.894

23
C
THR
3
6.588
27.073
33.167

24
O
THR
3
7.667
27.522
32.778

25
N
THR
4
5.420
27.156
32.515

26
CA
THR
4
5.111
27.326
31.137

27
CB
THR
4
3.616
27.502
30.981

28
OG1
THR
4
3.185
27.173
29.674

29
CG2
THR
4
3.223
28.944
31.374

30
C
THR
4
5.773
28.512
30.539

31
O
THR
4
6.732
29.098
31.036

32
N
GLU
5
5.210
28.861
29.388

33
CA
GLU
5
5.379
30.103
28.756

34
CB
GLU
5
6.812
30.238
28.196

35
CG
GLU
5
7.107
31.576
27.539

36
CD
GLU
5
7.502
31.227
26.125

37
OE1
GLU
5
8.006
30.089
25.948

38
OE2
GLU
5
7.331
32.073
25.204

39
C
GLU
5
4.370
30.001
27.668

40
O
GLU
5
3.400
29.254
27.790

41
N
SER
6
4.565
30.735
26.572

42
CA
SER
6
3.788
30.481
25.404

43
CB
SER
6
2.282
30.723
25.535

44
OG
SER
6
1.659
30.546
24.275

45
C
SER
6
4.290
31.419
24.394

46
O
SER
6
4.782
32.496
24.709

47
N
MET
7
4.215
30.996
23.130

48
CA
MET
7
4.890
31.715
22.101

49
CB
MET
7
6.336
31.193
21.948

50
CG
MET
7
7.139
31.798
20.802

51
SD
MET
7
8.319
30.656
20.026

52
CE
MET
7
7.826
31.072
18.330

53
C
MET
7
4.138
31.429
20.842

54
O
MET
7
3.482
30.398
20.737

55
N
PRO
8
4.189
32.265
19.855

56
CA
PRO
8
4.884
33.515
19.894

57
CD
PRO
8
3.895
31.801
18.516

58
CB
PRO
8
5.090
33.925
18.433

59
CG
PRO
8
4.756
32.670
17.598

60
C
PRO
8
4.045
34.483
20.658

61
O
PRO
8
2.848
34.548
20.391

62
N
PHE
9
4.620
35.255
21.599

63
CA
PHE
9
3.770
36.228
22.220

64
CB
PHE
9
4.400
36.994
23.388

65
CG
PHE
9
5.847
36.673
23.378

66
CD1
PHE
9
6.745
37.489
22.727

67
CD2
PHE
9
6.287
35.541
24.022

68
CE1
PHE
9
8.083
37.176
22.710

69
CE2
PHE
9
7.622
35.226
24.008

70
CZ
PHE
9
8.516
36.047
23.364

71
C
PHE
9
3.426
37.232
21.189

72
O
PHE
9
4.245
37.567
20.341

73
N
ASN
10
2.185
37.730
21.242

74
CA
ASN
10
1.677
38.584
20.230

75
CB
ASN
10
2.602
39.764
19.931

76
CG
ASN
10
2.550
40.570
21.214

77
OD1
ASN
10
3.547
40.852
21.877

78
ND2
ASN
10
1.301
40.930
21.603

79
C
ASN
10
1.441
37.750
19.034

80
O
ASN
10
2.355
37.147
18.472

81
N
VAL
11
0.161
37.663
18.650

82
CA
VAL
11
−0.206
36.723
17.646

83
CB
VAL
11
−0.991
35.584
18.211

84
CG1
VAL
11
−1.030
34.470
17.161

85
CG2
VAL
11
−0.352
35.193
19.558

86
C
VAL
11
−1.051
37.448
16.661

87
O
VAL
11
−1.866
38.291
17.030

88
N
ALA
12
−0.868
37.137
15.370

89
CA
ALA
12
−1.622
37.830
14.377

90
CB
ALA
12
−0.875
37.972
13.044

91
C
ALA
12
−2.843
37.032
14.103

92
O
ALA
12
−3.216
36.145
14.868

93
N
GLU
13
−3.500
37.353
12.978

94
CA
GLU
13
−4.686
36.658
12.606

95
CB
GLU
13
−5.779
37.609
12.095

96
CG
GLU
13
−7.169
36.986
12.079

97
CD
GLU
13
−8.148
38.066
11.674

98
OE1
GLU
13
−8.617
38.806
12.570

99
OE2
GLU
13
−8.432
38.156
10.444

100
C
GLU
13
−4.316
35.742
11.488

101
O
GLU
13
−3.530
36.101
10.613

102
N
GLY
14
−4.870
34.517
11.494

103
CA
GLY
14
−4.533
33.571
10.470

104
C
GLY
14
−3.205
32.986
10.822

105
O
GLY
14
−2.596
32.257
10.036

106
N
LYS
15
−2.707
33.286
12.029

107
CA
LYS
15
−1.453
32.689
12.359

108
CB
LYS
15
−0.349
33.726
12.590

109
CG
LYS
15
−0.292
34.675
11.389

110
CD
LYS
15
0.965
35.540
11.278

111
CE
LYS
15
1.879
35.141
10.120

112
NZ
LYS
15
2.884
34.185
10.621

113
C
LYS
15
−1.661
31.854
13.575

114
O
LYS
15
−2.580
32.073
14.362

115
N
GLU
16
−0.802
30.831
13.721

116
CA
GLU
16
−0.926
29.897
14.790

117
CB
GLU
16
−0.251
28.537
14.518

118
CG
GLU
16
−0.977
27.604
13.550

119
CD
GLU
16
−0.103
26.370
13.360

120
OE1
GLU
16
−0.591
25.244
13.655

121
OE2
GLU
16
1.065
26.539
12.922

122
C
GLU
16
−0.175
30.451
15.949

123
O
GLU
16
0.317
31.576
15.925

124
N
VAL
17
−0.075
29.616
16.999

125
CA
VAL
17
0.741
29.857
18.148

126
CB
VAL
17
0.029
30.570
19.253

127
CG1
VAL
17
0.911
31.725
19.758

128
CG2
VAL
17
−1.369
30.976
18.751

129
C
VAL
17
1.022
28.498
18.678

130
O
VAL
17
0.383
27.518
18.292

131
N
LEU
18
1.994
28.395
19.595

132
CA
LEU
18
2.164
27.154
20.279

133
CB
LEU
18
3.505
26.441
20.019

134
CG
LEU
18
3.850
25.424
21.125

135
CD2
LEU
18
5.320
24.977
21.043

136
CD1
LEU
18
2.880
24.239
21.133

137
C
LEU
18
2.153
27.470
21.729

138
O
LEU
18
2.567
28.543
22.164

139
N
LEU
19
1.669
26.538
22.544

140
CA
LEU
19
1.728
26.881
23.921

141
CB
LEU
19
0.394
26.658
24.638

142
CG
LEU
19
−0.596
27.812
24.336

143
CD2
LEU
19
−0.441
28.370
22.911

144
CD1
LEU
19
−0.515
28.889
25.420

145
C
LEU
19
2.807
26.039
24.486

146
O
LEU
19
2.816
24.823
24.273

147
N
LEU
20
3.782
26.676
25.164

148
CA
LEU
20
4.987
25.975
25.493

149
CB
LEU
20
6.257
26.774
25.149

150
CG
LEU
20
7.502
25.954
24.741

151
CD2
LEU
20
8.778
26.814
24.806

152
CD1
LEU
20
7.325
25.298
23.361

153
C
LEU
20
5.005
25.775
26.962

154
O
LEU
20
5.196
26.733
27.710

155
N
VAL
21
4.849
24.522
27.421

156
CA
VAL
21
5.225
24.294
28.779

157
CB
VAL
21
4.501
23.163
29.456

158
CG1
VAL
21
5.442
22.475
30.460

159
CG2
VAL
21
3.238
23.732
30.128

160
C
VAL
21
6.659
23.936
28.702

161
O
VAL
21
7.094
23.345
27.718

162
N
HIS
22
7.440
24.321
29.724

163
CA
HIS
22
8.823
23.981
29.717

164
ND1
HIS
22
9.299
26.554
28.400

165
CG
HIS
22
9.553
26.362
29.736

166
CB
HIS
22
9.708
25.030
30.376

167
NE2
HIS
22
9.413
28.575
29.329

168
CD2
HIS
22
9.615
27.608
30.293

169
CE1
HIS
22
9.225
27.902
28.213

170
C
HIS
22
8.950
22.776
30.545

171
O
HIS
22
8.376
21.730
30.252

172
N
ASN
23
9.726
22.917
31.629

173
CA
ASN
23
9.999
21.795
32.469

174
CB
ASN
23
11.184
22.041
33.404

175
CG
ASN
23
12.345
22.422
32.510

176
OD1
ASN
23
12.358
23.495
31.910

177
ND2
ASN
23
13.342
21.506
32.397

178
C
ASN
23
8.798
21.519
33.309

179
O
ASN
23
8.119
22.429
33.783

180
N
LEU
24
8.533
20.220
33.520

181
CA
LEU
24
7.437
19.792
34.321

182
CB
LEU
24
7.257
20.563
35.639

183
CG
LEU
24
8.459
20.481
36.608

184
CD2
LEU
24
9.128
19.098
36.619

185
CD1
LEU
24
8.029
20.931
38.015

186
C
LEU
24
6.180
19.899
33.533

187
O
LEU
24
5.892
20.985
33.036

188
N
PRO
25
5.385
18.869
33.334

189
CA
PRO
25
5.765
17.486
33.483

190
CD
PRO
25
4.755
18.983
32.033

191
CB
PRO
25
6.453
17.210
32.152

192
CG
PRO
25
5.522
17.960
31.154

193
C
PRO
25
6.355
16.855
34.722

194
O
PRO
25
6.991
17.492
35.556

195
N
GLN
26
6.121
15.540
34.878

196
CA
GLN
26
6.673
14.829
35.990

197
CB
GLN
26
6.524
15.517
37.362

198
CG
GLN
26
7.565
15.034
38.374

199
CD
GLN
26
7.638
15.999
39.545

200
OE1
GLN
26
8.010
15.552
40.627

201
NE2
GLN
26
7.269
17.297
39.361

202
C
GLN
26
5.880
13.591
36.126

203
O
GLN
26
5.004
13.565
36.990

204
N
GLN
27
6.199
12.575
35.283

205
CA
GLN
27
5.738
11.207
35.329

206
CB
GLN
27
6.639
10.313
36.200

207
CG
GLN
27
7.082
8.995
35.562

208
CD
GLN
27
7.740
8.199
36.684

209
OE1
GLN
27
8.019
7.003
36.595

210
NE2
GLN
27
8.019
8.921
37.796

211
C
GLN
27
4.369
11.184
35.907

212
O
GLN
27
4.138
10.639
36.986

213
N
LEU
28
3.446
11.879
35.222

214
CA
LEU
28
2.207
12.259
35.819

215
CB
LEU
28
1.595
13.501
35.178

216
CG
LEU
28
2.209
14.829
35.660

217
CD2
LEU
28
1.667
15.253
37.044

218
CD1
LEU
28
2.040
15.902
34.579

219
C
LEU
28
1.235
11.156
35.616

220
O
LEU
28
1.476
10.003
35.978

221
N
PHE
29
0.076
11.517
35.050

222
CA
PHE
29
−0.946
10.546
34.866

223
CB
PHE
29
−1.819
10.352
36.113

224
CG
PHE
29
−2.929
9.502
35.647

225
CD1
PHE
29
−2.770
8.146
35.488

226
CD2
PHE
29
−4.149
10.063
35.354

227
CE1
PHE
29
−3.816
7.373
35.037

228
CE2
PHE
29
−5.193
9.289
34.902

229
CZ
PHE
29
−5.034
7.937
34.751

230
C
PHE
29
−1.842
11.097
33.810

231
O
PHE
29
−2.267
10.395
32.893

232
N
GLY
30
−2.157
12.397
33.926

233
CA
GLY
30
−3.108
12.964
33.035

234
C
GLY
30
−2.823
14.417
32.951

235
O
GLY
30
−2.343
15.042
33.899

236
N
TYR
31
−3.109
14.990
31.769

237
CA
TYR
31
−2.948
16.399
31.563

238
CB
TYR
31
−1.879
16.853
30.536

239
CG
TYR
31
−0.785
15.892
30.141

240
CDI
TYR
31
0.114
16.363
29.218

241
CD2
TYR
31
−0.616
14.590
30.578

242
CE1
TYR
31
1.170
15.607
28.781

243
CE2
TYR
31
0.429
13.817
30.153

244
CZ
TYR
31
1.304
14.317
29.228

245
OH
TYR
31
2.374
13.527
28.779

246
C
TYR
31
−4.246
16.838
30.972

247
O
TYR
31
−4.993
16.012
30.454

248
N
SER
32
−4.566
18.144
31.017

249
CA
SER
32
−5.727
18.548
30.281

250
CB
SER
32
−7.049
18.081
30.909

251
OG
SER
32
−8.157
18.657
30.240

252
C
SER
32
−5.755
20.038
30.208

253
O
SER
32
−5.827
20.731
31.222

254
N
TRP
33
−5.704
20.543
28.965

255
CA
TRP
33
−5.728
21.934
28.654

256
CB
TRP
33
−5.426
22.186
27.174

257
CG
TRP
33
−3.994
22.565
27.034

258
CD2
TRP
33
−3.532
23.884
26.685

259
CD1
TRP
33
−2.897
21.810
27.279

260
NE1
TRP
33
−1.763
22.570
27.138

261
CE2
TRP
33
−2.140
23.838
26.781

262
CE3
TRP
33
−4.207
25.020
26.335

263
CZ2
TRP
33
−1.390
24.952
26.526

264
CZ3
TRP
33
−3.449
26.139
26.070

265
CH2
TRP
33
−2.074
26.091
26.167

266
C
TRP
33
−7.091
22.467
28.882

267
O
TRP
33
−8.072
21.890
28.419

268
N
TYR
34
−7.213
23.612
29.572

269
CA
TYR
34
−8.535
24.143
29.605

270
CB
TYR
34
−9.078
24.365
31.014

271
CG
TYR
34
−9.277
23.022
31.635

272
CD1
TYR
34
−8.355
22.560
32.548

273
CD2
TYR
34
−10.358
22.221
31.325

274
CE1
TYR
34
−8.519
21.335
33.154

275
CE2
TYR
34
−10.511
21.001
31.937

276
CZ
TYR
34
−9.592
20.542
32.850

277
OH
TYR
34
−9.748
19.291
33.481

278
C
TYR
34
−8.539
25.445
28.888

279
O
TYR
34
−7.941
25.591
27.823

280
N
LYS
35
−9.271
26.420
29.453

281
CA
LYS
35
−9.443
27.644
28.748

282
CB
LYS
35
−10.250
27.484
27.450

283
CG
LYS
35
−10.468
28.818
26.736

284
CD
LYS
35
−11.374
28.723
25.508

285
CE
LYS
35
−11.104
29.833
24.497

286
NZ
LYS
35
−12.067
29.747
23.377

287
C
LYS
35
−10.221
28.566
29.618

288
O
LYS
35
−11.430
28.425
29.782

289
N
GLY
36
−9.545
29.571
30.188

290
CA
GLY
36
−10.307
30.640
30.746

291
C
GLY
36
−10.464
30.414
32.206

292
O
GLY
36
−11.476
30.805
32.776

293
N
GLU
37
−9.441
29.820
32.849

294
CA
GLU
37
−9.358
29.835
34.276

295
CB
GLU
37
−9.751
31.189
34.878

296
CG
GLU
37
−9.537
31.227
36.391

297
CD
GLU
37
−9.866
32.621
36.886

298
OE1
GLU
37
−9.523
32.930
38.062

299
OE2
GLU
37
−10.466
33.388
36.095

300
C
GLU
37
−10.260
28.798
34.845

301
O
GLU
37
−9.885
28.108
35.792

302
N
ARG
38
−11.476
28.685
34.289

303
CA
ARG
38
−12.476
27.817
34.819

304
CB
ARG
38
−13.715
27.734
33.930

305
CG
ARG
38
−14.958
27.259
34.682

306
CD
ARG
38
−16.263
27.630
33.973

307
NE
ARG
38
−17.327
27.672
35.021

308
CZ
ARG
38
−18.516
27.052
34.820

309
NH1
ARG
38
−19.463
27.008
35.806

310
NH2
ARG
38
−18.765
26.449
33.622

311
C
ARG
38
−11.872
26.467
34.897

312
O
ARG
38
−11.333
25.948
33.923

313
N
VAL
39
−11.882
25.888
36.100

314
CA
VAL
39
−11.120
24.701
36.271

315
CB
VAL
39
−10.699
24.551
37.692

316
CG1
VAL
39
−9.955
23.230
37.882

317
CG2
VAL
39
−9.817
25.764
38.024

318
C
VAL
39
−11.985
23.564
35.839

319
O
VAL
39
−11.559
22.408
35.824

320
N
ASP
40
−13.234
23.896
35.446

321
CA
ASP
40
−14.169
22.938
34.931

322
CB
ASP
40
−15.544
23.568
34.582

323
CG
ASP
40
−16.715
22.854
35.263

324
OD1
ASP
40
−17.870
23.228
34.931

325
OD2
ASP
40
−16.475
21.952
36.115

326
C
ASP
40
−13.627
22.404
33.646

327
O
ASP
40
−12.705
22.948
33.038

328
N
GLY
41
−14.234
21.295
33.193

329
CA
GLY
41
−14.027
20.807
31.864

330
C
GLY
41
−15.369
20.822
31.213

331
O
GLY
41
−15.604
20.069
30.263

332
N
ASN
42
−16.274
21.686
31.746

333
CA
ASN
42
−17.482
22.111
31.081

334
CB
ASN
42
−17.890
23.507
31.578

335
CG
ASN
42
−19.322
23.849
31.191

336
OD1
ASN
42
−19.600
24.338
30.100

337
ND2
ASN
42
−20.261
23.621
32.147

338
C
ASN
42
−17.057
22.257
29.663

339
O
ASN
42
−17.528
21.564
28.759

340
N
ARG
43
−16.022
23.093
29.504

341
CA
ARG
43
−15.131
22.973
28.409

342
CB
ARG
43
−14.937
24.311
27.668

343
CG
ARG
43
−16.017
24.489
26.605

344
CD
ARG
43
−16.642
23.129
26.298

345
NE
ARG
43
−17.709
23.312
25.290

346
CZ
ARG
43
−18.952
22.811
25.558

347
NH1
ARG
43
−19.891
22.784
24.578

348
NH2
ARG
43
−19.223
22.316
26.802

349
C
ARG
43
−13.813
22.513
28.969

350
O
ARG
43
−12.994
23.317
29.415

351
N
GLN
44
−13.594
21.177
28.946

352
CA
GLN
44
−12.271
20.637
29.087

353
CB
GLN
44
−12.243
19.210
29.676

354
CG
GLN
44
−10.918
18.467
29.447

355
CD
GLN
44
−10.916
17.123
30.179

356
OE1
GLN
44
−11.231
17.025
31.365

357
NE2
GLN
44
−10.551
16.049
29.436

358
C
GLN
44
−11.743
20.550
27.695

359
O
GLN
44
−12.522
20.495
26.743

360
N
ILE
45
−10.411
20.568
27.512

361
CA
ILE
45
−9.980
20.694
26.151

362
CB
ILE
45
−9.246
21.989
25.891

363
CG2
ILE
45
−9.076
22.147
24.372

364
CG1
ILE
45
−10.019
23.175
26.515

365
CD1
ILE
45
−10.808
24.010
25.500

366
C
ILE
45
−9.138
19.504
25.767

367
O
ILE
45
−9.641
18.593
25.117

368
N
VAL
46
−7.840
19.462
26.143

369
CA
VAL
46
−6.992
18.393
25.668

370
CB
VAL
46
−5.594
18.872
25.311

371
CG1
VAL
46
−4.592
17.731
25.039

372
CG2
VAL
46
−5.768
19.765
24.079

373
C
VAL
46
−6.962
17.335
26.729

374
O
VAL
46
−7.408
17.567
27.854

375
N
GLY
47
−6.447
16.130
26.390

376
CA
GLY
47
−6.256
15.083
27.349

377
C
GLY
47
−5.195
14.151
26.843

378
O
GLY
47
−5.408
12.942
26.782

379
N
TYR
48
−4.000
14.678
26.500

380
CA
TYR
48
−2.917
13.746
26.434

381
CB
TYR
48
−1.531
14.310
26.042

382
CG
TYR
48
−0.622
13.147
25.751

383
CD1
TYR
48
0.323
12.732
26.663

384
CD2
TYR
48
−0.694
12.460
24.563

385
CE1
TYR
48
1.156
11.669
26.392

386
CE2
TYR
48
0.131
11.397
24.281

387
CZ
TYR
48
1.053
10.986
25.202

388
OH
TYR
48
1.901
9.897
24.924

389
C
TYR
48
−2.840
13.221
27.824

390
O
TYR
48
−3.098
13.941
28.788

391
N
ALA
49
−2.567
11.917
27.937

392
CA
ALA
49
−2.597
11.247
29.188

393
CB
ALA
49
−3.492
9.982
29.140

394
C
ALA
49
−1.203
10.792
29.376

395
O
ALA
49
−0.412
10.810
28.434

396
N
ILE
50
−0.814
10.372
30.585

397
CA
ILE
50
0.504
9.811
30.495

398
CB
ILE
50
1.517
10.327
31.511

399
CG2
ILE
50
2.410
9.159
31.969

400
CG1
ILE
50
2.308
11.475
30.856

401
CD1
ILE
50
3.793
11.480
31.193

402
C
ILE
50
0.332
8.337
30.609

403
O
ILE
50
−0.025
7.817
31.665

404
N
GLY
51
0.586
7.637
29.476

405
CA
GLY
51
0.297
6.232
29.393

406
C
GLY
51
−0.504
6.047
28.152

407
O
GLY
51
−0.185
6.714
27.171

408
N
THR
52
−1.523
5.147
28.200

409
CA
THR
52
−2.381
4.973
27.085

410
CB
THR
52
−3.635
4.167
27.336

411
OG1
THR
52
−4.810
4.863
26.951

412
CG2
THR
52
−3.760
3.813
28.806

413
C
THR
52
−2.779
6.302
26.621

414
O
THR
52
−3.542
7.031
27.248

415
N
GLN
53
−2.190
6.667
25.463

416
CA
GLN
53
−3.009
7.112
24.409

417
CB
GLN
53
−4.423
6.548
24.578

418
CG
GLN
53
−5.048
5.889
23.362

419
CD
GLN
53
−6.524
6.039
23.665

420
OE1
GLN
53
−7.042
7.143
23.518

421
NE2
GLN
53
−7.203
4.942
24.100

422
C
GLN
53
−3.072
8.574
24.470

423
O
GLN
53
−2.479
9.198
25.349

424
N
GLN
54
−3.819
9.214
23.551

425
CA
GLN
54
−4.156
10.521
23.975

426
CB
GLN
54
−3.252
11.642
23.403

427
CG
GLN
54
−3.871
12.793
22.614

428
CD
GLN
54
−3.905
12.285
21.192

429
OE1
GLN
54
−3.098
12.626
20.326

430
NE2
GLN
54
−4.883
11.374
20.961

431
C
GLN
54
−5.601
10.693
23.713

432
O
GLN
54
−6.296
9.749
23.322

433
N
ALA
55
−6.150
11.877
24.008

434
CA
ALA
55
−7.527
11.778
24.293

435
CB
ALA
55
−7.792
11.764
25.802

436
C
ALA
55
−8.217
12.955
23.720

437
O
ALA
55
−7.598
13.875
23.178

438
N
THR
56
−9.560
12.958
23.823

439
CA
THR
56
−10.167
14.130
23.308

440
CB
THR
56
−10.183
14.184
21.820

441
OG1
THR
56
−10.707
15.437
21.408

442
CG2
THR
56
−11.049
13.030
21.273

443
C
THR
56
−11.576
14.286
23.787

444
O
THR
56
−12.456
13.440
23.640

445
N
PRO
57
−11.721
15.443
24.365

446
CA
PRO
57
−12.957
15.888
24.950

447
CD
PRO
57
−10.565
15.854
25.144

448
CB
PRO
57
−12.611
16.580
26.261

449
CG
PRO
57
−11.140
16.223
26.521

450
C
PRO
57
−13.739
16.844
24.112

451
O
PRO
57
−13.824
16.689
22.893

452
N
GLY
58
−14.324
17.848
24.798

453
CA
GLY
58
−15.723
18.198
24.742

454
C
GLY
58
−16.049
19.198
23.669

455
O
GLY
58
−17.098
19.057
23.036

456
N
PRO
59
−15.284
20.228
23.404

457
CA
PRO
59
−15.832
21.294
22.633

458
CD
PRO
59
−14.141
20.654
24.194

459
CB
PRO
59
−15.133
22.578
23.069

460
CG
PRO
59
−14.139
22.182
24.173

461
C
PRO
59
−15.508
21.064
21.206

462
O
PRO
59
−15.815
20.009
20.655

463
N
ALA
60
−14.861
22.080
20.609

464
CA
ALA
60
−14.428
22.067
19.250

465
CB
ALA
60
−14.415
23.471
18.628

466
C
ALA
60
−13.021
21.586
19.235

467
O
ALA
60
−12.244
21.861
20.146

468
N
ASN
61
−12.644
20.869
18.164

469
CA
ASN
61
−11.253
20.599
17.925

470
CB
ASN
61
−10.939
19.086
17.858

471
CG
ASN
61
−9.497
18.768
18.254

472
OD1
ASN
61
−9.153
17.589
18.324

473
ND2
ASN
61
−8.641
19.792
18.499

474
C
ASN
61
−10.974
21.179
16.580

475
O
ASN
61
−10.469
20.497
15.689

476
N
SER
62
−11.327
22.463
16.386

477
CA
SER
62
−11.251
22.990
15.058

478
CB
SER
62
−11.807
24.411
14.932

479
OG
SER
62
−13.209
24.341
14.753

480
C
SER
62
−9.814
23.054
14.720

481
O
SER
62
−9.406
22.870
13.574

482
N
GLY
63
−8.991
23.332
15.732

483
CA
GLY
63
−7.618
23.518
15.427

484
C
GLY
63
−6.936
23.862
16.694

485
O
GLY
63
−6.701
25.021
17.027

486
N
ARG
64
−6.619
22.796
17.430

487
CA
ARG
64
−5.777
22.827
18.571

488
CB
ARG
64
−6.569
22.796
19.899

489
CG
ARG
64
−7.288
24.107
20.232

490
CD
ARG
64
−8.778
24.128
19.890

491
NE
ARG
64
−9.200
25.559
19.923

492
CZ
ARG
64
−9.728
26.090
21.066

493
NH1
ARG
64
−10.073
27.415
21.086

494
NH2
ARG
64
−9.917
25.310
22.171

495
C
ARG
64
−5.039
21.550
18.429

496
O
ARG
64
−5.392
20.716
17.593

497
N
GLU
65
−3.987
21.361
19.217

498
CA
GLU
65
−3.408
20.062
19.192

499
CB
GLU
65
−2.457
19.826
18.018

500
CG
GLU
65
−2.927
18.721
17.072

501
CD
GLU
65
−2.859
19.306
15.683

502
OE1
GLU
65
−2.116
18.744
14.828

503
OE2
GLU
65
−3.527
20.348
15.474

504
C
GLU
65
−2.565
19.997
20.389

505
O
GLU
65
−2.089
21.020
20.869

506
N
THR
66
−2.346
18.799
20.920

507
CA
THR
66
−1.521
18.856
22.070

508
CB
THR
66
−2.105
18.180
23.279

509
OG1
THR
66
−1.538
18.690
24.467

510
CG2
THR
66
−1.837
16.672
23.183

511
C
THR
66
−0.231
18.209
21.721

512
O
THR
66
0.038
17.883
20.562

513
N
ILE
67
0.621
18.013
22.733

514
CA
ILE
67
1.763
17.181
22.520

515
CB
ILE
67
2.915
17.871
21.858

516
CG2
ILE
67
3.484
18.900
22.853

517
CG1
ILE
67
3.946
16.833
21.377

518
CD1
ILE
67
5.037
17.448
20.501

519
C
ILE
67
2.233
16.752
23.863

520
O
ILE
67
1.867
17.356
24.868

521
N
TYR
68
3.073
15.694
23.878

522
CA
TYR
68
3.688
15.102
25.034

523
CB
TYR
68
4.947
14.266
24.647

524
CG
TYR
68
5.363
13.318
25.725

525
CD1
TYR
68
4.425
12.517
26.336

526
CD2
TYR
68
6.686
13.209
26.112

527
CE1
TYR
68
4.804
11.631
27.319

528
CE2
TYR
68
7.056
12.323
27.092

529
CZ
TYR
68
6.120
11.526
27.705

530
OH
TYR
68
6.513
10.615
28.705

531
C
TYR
68
4.038
16.178
26.029

532
O
TYR
68
3.550
16.140
27.158

533
N
PRO
69
4.845
17.157
25.683

534
CA
PRO
69
5.436
18.039
26.660

535
CD
PRO
69
5.568
17.173
24.418

536
CB
PRO
69
6.493
18.851
25.914

537
CG
PRO
69
6.805
18.051
24.638

538
C
PRO
69
4.450
18.900
27.391

539
O
PRO
69
4.886
19.739
28.175

540
N
ASN
70
3.131
18.727
27.175

541
CA
ASN
70
2.173
19.562
27.845

542
CB
ASN
70
2.411
19.695
29.355

543
CG
ASN
70
1.216
20.433
29.947

544
OD1
ASN
70
1.329
21.120
30.963

545
ND2
ASN
70
0.032
20.262
29.302

546
C
ASN
70
2.291
20.913
27.232

547
O
ASN
70
2.230
21.945
27.901

548
N
ALA
71
2.478
20.914
25.908

549
CA
ALA
71
2.411
22.096
25.118

550
CB
ALA
71
3.577
22.194
24.105

551
C
ALA
71
1.136
21.929
24.362

552
O
ALA
71
0.758
20.806
24.031

553
N
SER
72
0.397
23.020
24.103

554
CA
SER
72
−0.759
22.808
23.287

555
CB
SER
72
−2.104
23.047
23.968

556
OG
SER
72
−3.068
23.427
23.000

557
C
SER
72
−0.681
23.757
22.152

558
O
SER
72
−0.636
24.975
22.336

559
N
LEU
73
−0.663
23.206
20.934

560
CA
LEU
73
−0.619
24.034
19.778

561
CB
LEU
73
−0.302
23.273
18.485

562
CG
LEU
73
0.180
24.196
17.349

563
CD2
LEU
73
−0.603
23.914
16.058

564
CD1
LEU
73
1.704
24.109
17.167

565
C
LEU
73
−1.973
24.628
19.624

566
O
LEU
73
−2.900
24.322
20.371

567
N
LEU
74
−2.101
25.533
18.646

568
CA
LEU
74
−3.345
26.199
18.447

569
CB
LEU
74
−3.459
27.536
19.199

570
CG
LEU
74
−4.850
27.823
19.824

571
CD2
LEU
74
−4.926
27.285
21.258

572
CD1
LEU
74
−5.997
27.327
18.932

573
C
LEU
74
−3.366
26.527
17.004

574
O
LEU
74
−2.447
27.169
16.498

575
N
ILE
75
−4.402
26.085
16.280

576
CA
ILE
75
−4.410
26.523
14.926

577
CB
ILE
75
−5.033
25.576
13.940

578
CG2
ILE
75
−6.560
25.787
13.924

579
CG1
ILE
75
−4.371
25.786
12.569

580
CD1
ILE
75
−5.283
25.535
11.370

581
C
ILE
75
−5.209
27.774
14.920

582
O
ILE
75
−5.634
28.219
15.986

583
N
GLN
76
−5.408
28.330
13.700

584
CA
GLN
76
−6.311
29.379
13.310

585
CB
GLN
76
−7.406
28.875
12.367

586
CG
GLN
76
−6.821
28.596
10.985

587
CD
GLN
76
−7.923
28.169
10.039

588
OE1
GLN
76
−7.629
27.449
9.087

589
NE2
GLN
76
−9.191
28.592
10.298

590
C
GLN
76
−6.893
30.066
14.492

591
O
GLN
76
−8.057
29.899
14.851

592
N
ASN
77
−6.021
30.859
15.134

593
CA
ASN
77
−6.337
31.584
16.314

594
CB
ASN
77
−5.184
32.526
16.704

595
CG
ASN
77
−5.119
32.678
18.220

596
OD1
ASN
77
−4.232
33.356
18.739

597
ND2
ASN
77
−6.059
32.025
18.950

598
C
ASN
77
−7.545
32.403
16.002

599
O
ASN
77
−8.675
31.980
16.235

600
N
VAL
78
−7.315
33.611
15.450

601
CA
VAL
78
−8.355
34.583
15.265

602
CB
VAL
78
−9.623
34.016
14.667

603
CG1
VAL
78
−10.475
35.153
14.066

604
CG2
VAL
78
−9.226
32.975
13.609

605
C
VAL
78
−8.582
35.198
16.612

606
O
VAL
78
−7.768
35.005
17.511

607
N
THR
79
−9.652
35.996
16.782

608
CA
THR
79
−9.706
36.891
17.903

609
CB
THR
79
−10.289
38.205
17.499

610
OG1
THR
79
−10.382
39.062
18.620

611
CG2
THR
79
−11.681
37.963
16.897

612
C
THR
79
−10.580
36.309
18.960

613
O
THR
79
−10.677
36.823
20.073

614
N
GLN
80
−11.246
35.210
18.606

615
CA
GLN
80
−12.325
34.683
19.364

616
CB
GLN
80
−13.210
33.867
18.421

617
CG
GLN
80
−13.740
34.777
17.308

618
CD
GLN
80
−14.815
35.642
17.953

619
OE1
GLN
80
−14.729
36.866
18.055

620
NE2
GLN
80
−15.882
34.950
18.432

621
C
GLN
80
−11.754
33.838
20.457

622
O
GLN
80
−12.408
33.580
21.467

623
N
ASN
81
−10.493
33.401
20.273

624
CA
ASN
81
−9.845
32.514
21.195

625
CB
ASN
81
−9.062
31.416
20.476

626
CG
ASN
81
−10.139
30.699
19.692

627
OD1
ASN
81
−11.288
30.716
20.126

628
ND2
ASN
81
−9.784
30.076
18.540

629
C
ASN
81
−8.888
33.313
22.000

630
O
ASN
81
−8.101
32.778
22.778

631
N
ASP
82
−8.968
34.644
21.836

632
CA
ASP
82
−8.188
35.547
22.620

633
CB
ASP
82
−8.377
37.004
22.186

634
CG
ASP
82
−7.340
37.818
22.921

635
OD1
ASP
82
−7.545
39.054
23.060

636
OD2
ASP
82
−6.320
37.221
23.353

637
C
ASP
82
−8.618
35.414
24.044

638
O
ASP
82
−9.805
35.230
24.308

639
N
THR
83
−7.631
35.499
24.967

640
CA
THR
83
−7.744
35.293
26.390

641
CB
THR
83
−9.121
35.035
26.931

642
OG1
THR
83
−9.126
35.158
28.348

643
CG2
THR
83
−9.552
33.618
26.534

644
C
THR
83
−6.930
34.089
26.723

645
O
THR
83
−6.469
33.378
25.832

646
N
GLY
84
−6.701
33.852
28.031

647
CA
GLY
84
−5.658
32.941
28.418

648
C
GLY
84
−6.249
31.613
28.750

649
O
GLY
84
−7.366
31.524
29.253

650
N
PHE
85
−5.479
30.539
28.478

651
CA
PHE
85
−5.972
29.202
28.621

652
CB
PHE
85
−5.604
28.296
27.427

653
CG
PHE
85
−6.219
28.832
26.167

654
CD1
PHE
85
−5.787
30.011
25.592

655
CD2
PHE
85
−7.246
28.150
25.546

656
CE1
PHE
85
−6.360
30.488
24.431

657
CE2
PHE
85
−7.824
28.618
24.387

658
CZ
PHE
85
−7.382
29.794
23.826

659
C
PHE
85
−5.407
28.626
29.891

660
O
PHE
85
−5.385
29.278
30.935

661
N
TYR
86
−4.969
27.353
29.843

662
CA
TYR
86
−4.667
26.675
31.075

663
CB
TYR
86
−5.923
26.733
31.984

664
CG
TYR
86
−6.011
25.980
33.293

665
CD1
TYR
86
−5.095
26.014
34.332

666
CD2
TYR
86
−7.149
25.235
33.478

667
CE1
TYR
86
−5.326
25.310
35.501

668
CE2
TYR
86
−7.407
24.534
34.632

669
CZ
TYR
86
−6.480
24.563
35.639

670
OH
TYR
86
−6.739
23.847
36.821

671
C
TYR
86
−4.286
25.273
30.709

672
O
TYR
86
−4.093
24.950
29.535

673
N
THR
87
−4.144
24.422
31.742

674
CA
THR
87
−4.055
23.003
31.594

675
CB
THR
87
−2.937
22.504
30.693

676
OG1
THR
87
−2.910
21.082
30.685

677
CG2
THR
87
−1.579
23.062
31.154

678
C
THR
87
−3.852
22.466
32.974

679
O
THR
87
−2.848
22.730
33.637

680
N
LEU
88
−4.869
21.729
33.434

681
CA
LEU
88
−4.907
21.063
34.699

682
CB
LEU
88
−6.356
20.641
34.985

683
CG
LEU
88
−6.629
19.766
36.207

684
CD2
LEU
88
−8.135
19.446
36.308

685
CD1
LEU
88
−6.050
20.422
37.460

686
C
LEU
88
−4.079
19.843
34.501

687
O
LEU
88
−3.939
19.408
33.364

688
N
GLN
89
−3.480
19.273
35.568

689
CA
GLN
89
−2.630
18.146
35.309

690
CB
GLN
89
−1.151
18.547
35.126

691
CG
GLN
89
−0.868
19.538
33.992

692
CD
GLN
89
0.327
20.378
34.436

693
OE1
GLN
89
0.234
21.601
34.534

694
NE2
GLN
89
1.469
19.701
34.727

695
C
GLN
89
−2.659
17.232
36.494

696
O
GLN
89
−2.131
17.577
37.551

697
N
VAL
90
−3.253
16.028
36.340

698
CA
VAL
90
−3.227
15.103
37.440

699
CB
VAL
90
−4.376
14.140
37.482

700
CG1
VAL
90
−3.865
12.873
38.190

701
CG2
VAL
90
−5.609
14.815
38.136

702
C
VAL
90
−2.000
14.226
37.378

703
O
VAL
90
−1.648
13.660
36.340

704
N
ILE
91
−1.334
14.078
38.546

705
CA
ILE
91
−0.921
12.803
39.054

706
CB
ILE
91
0.524
12.692
39.453

707
CG2
ILE
91
0.881
13.877
40.366

708
CG1
ILE
91
0.728
11.322
40.136

709
CD1
ILE
91
2.185
10.938
40.406

710
C
ILE
91
−1.699
12.629
40.314

711
O
ILE
91
−1.933
13.584
41.052

712
N
LYS
92
−2.115
11.386
40.586

713
CA
LYS
92
−3.063
11.114
41.614

714
CB
LYS
92
−3.683
9.719
41.503

715
CG
LYS
92
−5.151
9.735
41.922

716
CD
LYS
92
−5.717
11.156
42.035

717
CE
LYS
92
−6.775
11.299
43.126

718
NZ
LYS
92
−8.109
10.930
42.598

719
C
LYS
92
−2.421
11.199
42.957

720
O
LYS
92
−2.962
10.693
43.940

721
N
SER
93
−1.258
11.852
43.057

722
CA
SER
93
−0.679
12.046
44.352

723
CB
SER
93
0.859
12.047
44.311

724
OG
SER
93
1.383
11.900
45.622

725
C
SER
93
−1.132
13.380
44.846

726
O
SER
93
−1.555
13.539
45.990

727
N
ASP
94
−1.051
14.382
43.956

728
CA
ASP
94
−1.608
15.672
44.224

729
CB
ASP
94
−0.575
16.691
44.750

730
CG
ASP
94
−1.205
17.706
45.703

731
OD1
ASP
94
−0.405
18.455
46.332

732
OD2
ASP
94
−2.456
17.765
45.819

733
C
ASP
94
−2.040
16.165
42.887

734
O
ASP
94
−1.349
15.980
41.883

735
N
LEU
95
−3.207
16.821
42.832

736
CA
LEU
95
−3.465
17.564
41.640

737
CB
LEU
95
−4.956
17.698
41.272

738
CG
LEU
95
−5.228
18.471
39.972

739
CD2
LEU
95
−6.660
19.026
39.965

740
CD1
LEU
95
−4.919
17.617
38.727

741
C
LEU
95
−2.931
18.932
41.906

742
O
LEU
95
−3.032
19.430
43.025

743
N
VAL
96
−2.328
19.566
40.887

744
CA
VAL
96
−1.663
20.827
41.038

745
CB
VAL
96
−0.249
20.733
40.543

746
CG1
VAL
96
0.601
21.885
41.093

747
CG2
VAL
96
0.293
19.354
40.967

748
C
VAL
96
−2.427
21.778
40.179

749
O
VAL
96
−3.188
21.344
39.315

750
N
ASN
97
−2.294
23.100
40.401

751
CA
ASN
97
−3.127
23.981
39.626

752
CB
ASN
97
−3.747
25.163
40.423

753
CG
ASN
97
−5.012
25.706
39.736

754
OD1
ASN
97
−5.823
25.001
39.139

755
ND2
ASN
97
−5.217
27.052
39.840

756
C
ASN
97
−2.275
24.543
38.526

757
O
ASN
97
−2.143
23.926
37.469

758
N
GLU
98
−1.699
25.737
38.785

759
CA
GLU
98
−1.191
26.735
37.874

760
CB
GLU
98
−0.032
27.517
38.483

761
CG
GLU
98
1.287
27.449
37.715

762
CD
GLU
98
2.376
27.584
38.770

763
OE1
GLU
98
2.544
26.608
39.542

764
OE2
GLU
98
3.029
28.663
38.841

765
C
GLU
98
−0.728
26.203
36.554

766
O
GLU
98
−0.161
25.113
36.461

767
N
GLU
99
−0.927
27.000
35.470

768
CA
GLU
99
−0.181
28.221
35.246

769
CB
GLU
99
1.008
27.997
34.285

770
CG
GLU
99
0.769
28.478
32.847

771
CD
GLU
99
0.534
27.310
31.874

772
OE1
GLU
99
0.403
27.603
30.646

773
OE2
GLU
99
0.520
26.130
32.315

774
C
GLU
99
−1.113
29.184
34.536

775
O
GLU
99
−2.228
28.828
34.180

776
N
ALA
100
−0.689
30.434
34.241

777
CA
ALA
100
−1.506
31.134
33.279

778
CB
ALA
100
−2.228
32.374
33.847

779
C
ALA
100
−0.664
31.611
32.124

780
O
ALA
100
0.328
32.307
32.331

781
N
THR
101
−1.048
31.277
30.872

782
CA
THR
101
−0.412
31.900
29.731

783
CB
THR
101
−0.463
31.121
28.446

784
OG1
THR
101
−1.307
29.998
28.566

785
CG2
THR
101
0.974
30.686
28.147

786
C
THR
101
−1.164
33.152
29.494

787
O
THR
101
−1.616
33.761
30.452

788
N
GLY
102
−1.319
33.601
28.238

789
CA
GLY
102
−2.072
34.817
28.094

790
C
GLY
102
−1.556
35.545
26.912

791
O
GLY
102
−0.669
36.395
27.010

792
N
GLN
103
−2.133
35.207
25.753

793
CA
GLN
103
−1.797
35.855
24.530

794
CB
GLN
103
−1.573
34.860
23.381

795
CG
GLN
103
−2.554
33.681
23.462

796
CD
GLN
103
−2.287
32.707
22.322

797
OE1
GLN
103
−2.285
31.492
22.519

798
NE2
GLN
103
−2.009
33.259
21.109

799
C
GLN
103
−2.999
36.649
24.165

800
O
GLN
103
−4.132
36.267
24.461

801
N
PHE
104
−2.773
37.790
23.493

802
CA
PHE
104
−3.886
38.397
22.840

803
CB
PHE
104
−3.930
39.950
22.813

804
CG
PHE
104
−3.357
40.565
24.038

805
CD1
PHE
104
−3.696
40.119
25.298

806
CD2
PHE
104
−2.454
41.593
23.899

807
CE1
PHE
104
−3.159
40.719
26.402

808
CE2
PHE
104
−1.915
42.198
25.000

809
CZ
PHE
104
−2.256
41.752
26.261

810
C
PHE
104
−3.764
38.012
21.397

811
O
PHE
104
−2.999
37.126
21.014

812
N
HIS
105
−4.542
38.716
20.566

813
CA
HIS
105
−4.634
38.545
19.149

814
ND1
HIS
105
−6.199
37.389
16.330

815
CG
HIS
105
−6.527
38.187
17.392

816
CB
HIS
105
−6.034
37.991
18.798

817
NE2
HIS
105
−7.632
38.891
15.559

818
CD2
HIS
105
−7.405
39.116
16.902

819
CE1
HIS
105
−6.881
37.846
15.250

820
C
HIS
105
−4.523
39.952
18.635

821
O
HIS
105
−4.762
40.890
19.391

822
N
VAL
106
−4.153
40.173
17.358

823
CA
VAL
106
−4.310
41.516
16.872

824
CB
VAL
106
−3.017
42.258
16.614

825
CG1
VAL
106
−2.979
43.510
17.505

826
CG2
VAL
106
−1.826
41.317
16.876

827
C
VAL
106
−5.103
41.439
15.602

828
O
VAL
106
−5.483
40.356
15.159

829
N
TYR
107
−5.392
42.613
14.997

830
CA
TYR
107
−6.085
42.655
13.730

831
CB
TYR
107
−7.458
43.370
13.780

832
CG
TYR
107
−8.654
42.515
14.127

833
CD1
TYR
107
−9.279
42.628
15.352

834
CD2
TYR
107
−9.203
41.622
13.229

835
CE1
TYR
107
−10.390
41.874
15.659

836
CE2
TYR
107
−10.317
40.865
13.537

837
CZ
TYR
107
−10.930
40.985
14.762

838
OH
TYR
107
−12.075
40.231
15.113

839
C
TYR
107
−5.239
43.461
12.772

840
O
TYR
107
−4.918
44.628
12.998

280
N
LYS
35
−9.271
26.420
29.453

281
CA
LYS
35
−9.443
27.644
28.748

282
CB
LYS
35
−10.250
27.484
27.450

283
CG
LYS
35
−10.468
28.818
26.736

284
CD
LYS
35
−11.374
28.723
25.508

285
CE
LYS
35
−11.104
29.833
24.497

286
NZ
LYS
35
−12.067
29.747
23.377

287
C
LYS
35
−10.221
28.566
29.618

288
O
LYS
35
−11.430
28.425
29.782

289
N
GLY
36
−9.545
29.571
30.188

290
CA
GLY
36
−10.307
30.640
30.746

291
C
GLY
36
−10.464
30.414
32.206

292
O
GLY
36
−11.476
30.805
32.776

293
N
GLU
37
−9.441
29.820
32.849

294
CA
GLU
37
−9.358
29.835
34.276

295
CB
GLU
37
−9.751
31.189
34.878

296
CG
GLU
37
−9.537
31.227
36.391

297
CD
GLU
37
−9.866
32.621
36.886

298
OE1
GLU
37
−9.523
32.930
38.062

299
OE2
GLU
37
−10.466
33.388
36.095

300
C
GLU
37
−10.260
28.798
34.845

301
O
GLU
37
−9.885
28.108
35.792

302
N
ARG
38
−11.476
28.685
34.289

303
CA
ARG
38
−12.476
27.817
34.819

304
CB
ARG
38
−13.715
27.734
33.930

305
CG
ARG
38
−14.958
27.259
34.682

306
CD
ARG
38
−16.263
27.630
33.973

307
NE
ARG
38
−17.327
27.672
35.021

308
CZ
ARG
38
−18.516
27.052
34.820

309
NH1
ARG
38
−19.463
27.008
35.806

310
NH2
ARG
38
−18.765
26.449
33.622

311
C
ARG
38
−11.872
26.467
34.897

312
O
ARG
38
−11.333
25.948
33.923

313
N
VAL
39
−11.882
25.888
36.100

314
CA
VAL
39
−11.120
24.701
36.271

315
CB
VAL
39
−10.699
24.551
37.692

316
CG1
VAL
39
−9.955
23.230
37.882

317
CG2
VAL
39
−9.817
25.764
38.024

318
C
VAL
39
−11.985
23.564
35.839

319
O
VAL
39
−11.559
22.408
35.824

320
N
ASP
40
−13.234
23.896
35.446

321
CA
ASP
40
−14.169
22.938
34.931

322
CB
ASP
40
−15.544
23.568
34.582

323
CG
ASP
40
−16.715
22.854
35.263

324
OD1
ASP
40
−17.870
23.228
34.931

325
OD2
ASP
40
−16.475
21.952
36.115

326
C
ASP
40
−13.627
22.404
33.646

327
O
ASP
40
−12.705
22.948
33.038

328
N
GLY
41
−14.234
21.295
33.193

329
CA
GLY
41
−14.027
20.807
31.864

330
C
GLY
41
−15.369
20.822
31.213

331
O
GLY
41
−15.604
20.069
30.263

332
N
ASN
42
−16.274
21.686
31.746

333
CA
ASN
42
−17.482
22.111
31.081

334
CB
ASN
42
−17.890
23.507
31.578

335
CG
ASN
42
−19.322
23.849
31.191

336
OD1
ASN
42
−19.600
24.338
30.100

337
ND2
ASN
42
−20.261
23.621
32.147

338
C
ASN
42
−17.057
22.257
29.663

339
O
ASN
42
−17.528
21.564
28.759

340
N
ARG
43
−16.022
23.093
29.504

341
CA
ARG
43
−15.131
22.973
28.409

342
CB
ARG
43
−14.937
24.311
27.668

343
CG
ARG
43
−16.017
24.489
26.605

344
CD
ARG
43
−16.642
23.129
26.298

345
NE
ARG
43
−17.709
23.312
25.290

346
CZ
ARG
43
−18.952
22.811
25.558

347
NH1
ARG
43
−19.891
22.784
24.578

348
NH2
ARG
43
−19.223
22.316
26.802

349
C
ARG
43
−13.813
22.513
28.969

350
O
ARG
43
−12.994
23.317
29.415

351
N
GLN
44
−13.594
21.177
28.946

352
CA
GLN
44
−12.271
20.637
29.087

353
CB
GLN
44
−12.243
19.210
29.676

354
CG
GLN
44
−10.918
18.467
29.447

355
CD
GLN
44
−10.916
17.123
30.179

356
OE1
GLN
44
−11.231
17.025
31.365

357
NE2
GLN
44
−10.551
16.049
29.436

358
C
GLN
44
−11.743
20.550
27.695

359
O
GLN
44
−12.522
20.495
26.743

360
N
ILE
45
−10.411
20.568
27.512

361
CA
ILE
45
−9.980
20.694
26.151

362
CB
ILE
45
−9.246
21.989
25.891

363
CG2
ILE
45
−9.076
22.147
24.372

364
CG1
ILE
45
−10.019
23.175
26.515

365
CD1
ILE
45
−10.808
24.010
25.500

366
C
ILE
45
−9.138
19.504
25.767

367
O
ILE
45
−9.641
18.593
25.117

[0140]

9

TABLE 6

Full coordinate set of D1D4 of murine CEACAM 1a

(1691 atoms, 419 amino acids)

ANum
AType
RType
RNum
X
Y
Z

1
CB
GLU
1
8.347
25.351
44.432

2
CG
GLU
1
8.491
26.847
44.172

3
CD
GLU
1
7.393
27.687
44.808

4
OE1
GLU
1
6.242
27.209
44.909

5
OE2
GLU
1
7.687
28.837
45.205

6
C
GLU
1
8.465
24.539
42.087

7
O
GLU
1
9.059
24.281
41.031

8
N
GLU
1
10.588
24.923
43.469

9
CA
GLU
1
9.160
24.496
43.450

10
N
VAL
2
7.179
24.881
42.172

11
CA
VAL
2
6.233
24.989
41.065

12
CB
VAL
2
4.813
24.688
41.547

13
CG1
VAL
2
4.629
25.287
42.941

14
CG2
VAL
2
3.785
25.270
40.576

15
C
VAL
2
6.200
26.366
40.441

16
O
VAL
2
5.758
27.343
41.041

17
N
THR
3
6.636
26.426
39.204

18
CA
THR
3
6.658
27.675
38.508

19
CB
THR
3
8.095
28.045
38.222

20
OG1
THR
3
8.949
27.140
38.935

21
CG2
THR
3
8.383
29.469
38.663

22
C
THR
3
5.895
27.422
37.235

23
O
THR
3
6.092
26.400
36.582

24
N
ILE
4
4.999
28.331
36.895

25
CA
ILE
4
4.235
28.161
35.683

26
CB
ILE
4
2.788
27.774
36.016

27
CG2
ILE
4
2.255
28.682
37.113

28
CG1
ILE
4
1.944
27.777
34.745

29
CD1
ILE
4
0.536
27.360
34.992

30
C
ILE
4
4.303
29.461
34.901

31
O
ILE
4
3.821
30.498
35.350

32
N
GLU
5
4.950
29.403
33.744

33
CA
GLU
5
5.097
30.575
32.901

34
CB
GLU
5
6.589
30.833
32.640

35
CG
GLU
5
7.031
30.993
31.193

36
CD
GLU
5
8.540
30.866
31.052

37
OE1
GLU
5
9.192
30.421
32.023

38
OE2
GLU
5
9.077
31.209
29.979

39
C
GLU
5
4.335
30.288
31.626

40
O
GLU
5
4.099
29.132
31.295

41
N
ALA
6
3.918
31.329
30.924

42
CA
ALA
6
3.174
31.127
29.692

43
CB
ALA
6
1.851
31.847
29.759

44
C
ALA
6
3.965
31.639
28.525

45
O
ALA
6
4.288
32.815
28.468

46
N
VAL
7
4.300
30.761
27.597

47
CA
VAL
7
5.030
31.229
26.451

48
CB
VAL
7
6.371
30.504
26.262

49
CG1
VAL
7
6.414
29.788
24.920

50
CG2
VAL
7
7.491
31.529
26.340

51
C
VAL
7
4.171
31.098
25.212

52
O
VAL
7
3.697
30.015
24.875

53
N
PRO
8
3.941
32.223
24.550

54
CD
PRO
8
3.211
32.399
23.274

55
CA
PRO
8
4.500
33.495
25.032

56
CB
PRO
8
4.661
34.304
23.772

57
CG
PRO
8
3.500
33.848
22.905

58
C
PRO
8
3.597
34.213
26.032

59
O
PRO
8
2.377
34.204
25.880

60
N
PRO
9
4.171
34.811
27.091

61
CD
PRO
9
5.577
34.914
27.531

62
CA
PRO
9
3.238
35.508
27.985

63
CB
PRO
9
4.110
35.967
29.158

64
CG
PRO
9
5.523
35.886
28.680

65
C
PRO
9
2.793
36.657
27.096

66
O
PRO
9
3.617
37.175
26.354

67
N
GLN
10
1.526
37.054
27.133

68
CA
GLN
10
1.067
38.125
26.240

69
CB
GLN
10
2.076
39.271
26.173

70
CG
GLN
10
2.047
40.196
27.357

71
CD
GLN
10
0.984
41.248
27.217

72
OE1
GLN
10
0.337
41.351
26.182

73
NE2
GLN
10
0.793
42.038
28.261

74
C
GLN
10
0.947
37.522
24.842

75
O
GLN
10
1.844
37.670
24.014

76
N
VAL
11
−0.167
36.848
24.586

77
CA
VAL
11
−0.404
36.200
23.303

78
CB
VAL
11
−1.173
34.894
23.483

79
CG1
VAL
11
−0.833
33.945
22.346

80
CG2
VAL
11
−0.846
34.296
24.836

81
C
VAL
11
−1.182
37.047
22.318

82
O
VAL
11
−1.867
38.000
22.689

83
N
ALA
12
−1.095
36.670
21.054

84
CA
ALA
12
−1.798
37.401
20.023

85
CB
ALA
12
−0.834
37.785
18.922

86
C
ALA
12
−2.949
36.601
19.452

87
O
ALA
12
−2.870
35.381
19.323

88
N
GLU
13
−4.022
37.305
19.120

89
CA
GLU
13
−5.192
36.679
18.536

90
CB
GLU
13
−6.052
37.740
17.872

91
CG
GLU
13
−7.463
37.313
17.606

92
CD
GLU
13
−8.372
38.499
17.432

93
OE1
GLU
13
−8.551
39.240
18.420

94
OE2
GLU
13
−8.897
38.695
16.314

95
C
GLU
13
−4.731
35.668
17.492

96
O
GLU
13
−3.635
35.792
16.949

97
N
ASP
14
−5.572
34.676
17.219

98
CA
ASP
14
−5.279
33.620
16.249

99
CB
ASP
14
−5.937
33.983
14.876

100
CG
ASP
14
−4.963
34.497
13.809

101
OD1
ASP
14
−3.842
34.947
14.127

102
OD2
ASP
14
−5.353
34.454
12.616

103
C
ASP
14
−3.798
33.197
16.170

104
O
ASP
14
−3.233
32.969
15.099

105
N
ASN
15
−3.201
33.071
17.358

106
CA
ASN
15
−1.810
32.644
17.551

107
CB
ASN
15
−0.900
33.855
17.809

108
CG
ASN
15
0.010
34.167
16.630

109
OD1
ASN
15
0.013
33.451
15.625

110
ND2
ASN
15
0.789
35.240
16.751

111
C
ASN
15
−1.814
31.701
18.764

112
O
ASN
15
−2.762
31.714
19.541

113
N
ASN
16
−0.761
30.905
18.938

114
CA
ASN
16
−0.701
29.934
20.039

115
CB
ASN
16
−0.026
28.662
19.543

116
CG
ASN
16
−1.010
27.649
19.041

117
OD1
ASN
16
−0.823
26.448
19.222

118
ND2
ASN
16
−2.070
28.123
18.397

119
C
ASN
16
−0.035
30.323
21.361

120
O
ASN
16
0.634
31.354
21.468

121
N
VAL
17
−0.221
29.464
22.366

122
CA
VAL
17
0.372
29.673
23.689

123
CB
VAL
17
−0.469
30.539
24.612

124
CG1
VAL
17
0.446
31.468
25.389

125
CG2
VAL
17
−1.529
31.270
23.838

126
C
VAL
17
0.565
28.405
24.476

127
O
VAL
17
−0.238
27.479
24.396

128
N
LEU
18
1.615
28.394
25.284

129
CA
LEU
18
1.907
27.239
26.105

130
CB
LEU
18
3.256
26.639
25.728

131
CG
LEU
18
3.664
25.462
26.615

132
CD1
LEU
18
2.587
24.377
26.567

133
CD2
LEU
18
5.004
24.923
26.150

134
C
LEU
18
1.920
27.605
27.578

135
O
LEU
18
2.420
28.667
27.969

136
N
LEU
19
1.365
26.707
28.384

137
CA
LEU
19
1.293
26.885
29.821

138
CB
LEU
19
−0.034
26.356
30.352

139
CG
LEU
19
−1.218
27.289
30.109

140
CD1
LEU
19
−1.038
28.521
30.964

141
CD2
LEU
19
−1.310
27.670
28.633

142
C
LEU
19
2.430
26.090
30.407

143
O
LEU
19
2.277
24.913
30.732

144
N
LEU
20
3.576
26.743
30.538

145
CA
LEU
20
4.756
26.092
31.066

146
CB
LEU
20
5.994
26.949
30.840

147
CG
LEU
20
7.285
26.135
30.760

148
CD1
LEU
20
7.046
24.860
29.958

149
CD2
LEU
20
8.370
26.972
30.110

150
C
LEU
20
4.664
25.741
32.532

151
O
LEU
20
4.201
26.531
33.358

152
N
VAL
21
5.143
24.545
32.843

153
CA
VAL
21
5.131
24.032
34.197

154
CB
VAL
21
4.215
22.807
34.262

155
CG1
VAL
21
4.143
22.277
35.672

156
CG2
VAL
21
2.837
23.194
33.746

157
C
VAL
21
6.550
23.652
34.609

158
O
VAL
21
7.019
22.563
34.273

159
N
HIS
22
7.248
24.548
35.315

160
CA
HIS
22
8.615
24.246
35.754

161
CB
HIS
22
9.429
25.470
36.169

162
CG
HIS
22
9.337
26.638
35.258

163
CD2
HIS
22
9.297
27.973
35.521

164
ND1
HIS
22
9.338
26.530
33.883

165
CE1
HIS
22
9.303
27.749
33.343

166
NE2
HIS
22
9.278
28.623
34.332

167
C
HIS
22
8.581
23.389
36.987

168
O
HIS
22
7.645
23.455
37.780

169
N
ASN
23
9.663
22.644
37.168

170
CA
ASN
23
9.832
21.756
38.301

171
CB
ASN
23
10.762
22.404
39.323

172
CG
ASN
23
12.229
22.142
39.004

173
OD1
ASN
23
12.804
22.758
38.102

174
ND2
ASN
23
12.837
21.213
39.735

175
C
ASN
23
8.501
21.354
38.907

176
O
ASN
23
8.031
21.908
39.890

177
N
LEU
24
7.904
20.381
38.239

178
CA
LEU
24
6.631
19.790
38.584

179
CB
LEU
24
5.977
19.303
37.296

180
CG
LEU
24
4.585
18.694
37.312

181
CD1
LEU
24
4.553
17.596
36.268

182
CD2
LEU
24
4.245
18.155
38.689

183
C
LEU
24
6.988
18.623
39.495

184
O
LEU
24
7.369
17.553
39.032

185
N
PRO
25
6.831
18.803
40.810

186
CD
PRO
25
6.303
20.027
41.439

187
CA
PRO
25
7.161
17.763
41.789

188
CB
PRO
25
6.678
18.324
43.132

189
CG
PRO
25
6.281
19.712
42.899

190
C
PRO
25
6.712
16.318
41.610

191
O
PRO
25
5.702
16.016
40.972

192
N
LEU
26
7.527
15.460
42.222

193
CA
LEU
26
7.415
14.005
42.289

194
CB
LEU
26
7.511
13.593
43.763

195
CG
LEU
26
8.598
14.457
44.418

196
CD1
LEU
26
8.490
14.369
45.926

197
CD2
LEU
26
9.975
14.002
43.929

198
C
LEU
26
6.196
13.410
41.616

199
O
LEU
26
5.082
13.900
41.792

200
N
ALA
27
6.411
12.327
40.872

201
CA
ALA
27
5.331
11.732
40.102

202
CB
ALA
27
5.877
10.697
39.156

203
C
ALA
27
4.058
11.234
40.766

204
O
ALA
27
3.851
10.052
41.080

205
N
LEU
28
3.200
12.237
40.878

206
CA
LEU
28
1.860
12.234
41.415

207
CB
LEU
28
1.237
13.596
41.128

208
CG
LEU
28
1.996
14.804
41.662

209
CD1
LEU
28
2.580
15.664
40.545

210
CD2
LEU
28
1.021
15.591
42.491

211
C
LEU
28
0.959
11.190
40.812

212
O
LEU
28
1.379
10.331
40.046

213
N
GLY
29
−0.308
11.310
41.177

214
CA
GLY
29
−1.317
10.428
40.657

215
C
GLY
29
−1.736
11.032
39.335

216
O
GLY
29
−1.990
10.302
38.391

217
N
ALA
30
−1.787
12.359
39.251

218
CA
ALA
30
−2.187
13.008
38.006

219
CB
ALA
30
−3.485
12.396
37.505

220
C
ALA
30
−2.362
14.513
38.143

221
O
ALA
30
−2.423
15.041
39.254

222
N
PHE
31
−2.440
15.201
37.005

223
CA
PHE
31
−2.649
16.644
37.015

224
CB
PHE
31
−1.470
17.426
36.397

225
CG
PHE
31
−0.526
16.600
35.553

226
CD1
PHE
31
0.742
16.273
36.031

227
CD2
PHE
31
−0.859
16.233
34.254

228
CE1
PHE
31
1.661
15.592
35.227

229
CE2
PHE
31
0.058
15.553
33.448

230
CZ
PHE
31
1.317
15.236
33.933

231
C
PHE
31
−3.934
17.038
36.295

232
O
PHE
31
−4.458
16.291
35.463

233
N
ALA
32
−4.432
18.223
36.627

234
CA
ALA
32
−5.655
18.742
36.040

235
CB
ALA
32
−6.795
18.588
37.024

236
C
ALA
32
−5.478
20.206
35.675

237
O
ALA
32
−4.962
20.996
36.475

238
N
TRP
33
−5.914
20.565
34.472

239
CA
TRP
33
−5.793
21.939
33.999

240
CB
TRP
33
−5.123
21.975
32.617

241
CG
TRP
33
−3.705
22.467
32.635

242
CD2
TRP
33
−3.220
23.693
33.188

243
CE2
TRP
33
−1.838
23.739
32.974

244
CE3
TRP
33
−3.851
24.749
33.863

245
CD1
TRP
33
−2.609
21.840
32.111

246
NE1
TRP
33
−1.481
22.595
32.312

247
CZ2
TRP
33
−1.052
24.805
33.396

248
CZ3
TRP
33
−3.069
25.810
34.278

249
CH2
TRP
33
−1.688
25.829
34.048

250
C
TRP
33
−7.160
22.596
33.916

251
O
TRP
33
−7.976
22.253
33.062

252
N
TYR
34
−7.403
23.544
34.812

253
CA
TYR
34
−8.671
24.258
34.843

254
CB
TYR
34
−9.268
24.213
36.251

255
CG
TYR
34
−9.481
22.817
36.781

256
CD1
TYR
34
−8.738
22.340
37.856

257
CE1
TYR
34
−8.926
21.048
38.351

258
CD2
TYR
34
−10.423
21.969
36.209

259
CE2
TYR
34
−10.620
20.678
36.695

260
CZ
TYR
34
−9.866
20.224
37.766

261
OH
TYR
34
−10.041
18.948
38.253

262
C
TYR
34
−8.531
25.711
34.401

263
O
TYR
34
−7.433
26.272
34.359

264
N
LYS
35
−9.666
26.313
34.082

265
CA
LYS
35
−9.714
27.692
33.635

266
CB
LYS
35
−10.484
27.750
32.307

267
CG
LYS
35
−10.801
29.140
31.738

268
CD
LYS
35
−11.408
29.009
30.325

269
CE
LYS
35
−11.841
30.347
29.722

270
NZ
LYS
35
−12.528
30.158
28.405

271
C
LYS
35
−10.412
28.539
34.692

272
O
LYS
35
−11.465
28.161
35.194

273
N
GLY
36
−9.800
29.656
35.067

274
CA
GLY
36
−10.439
30.553
36.013

275
C
GLY
36
−10.360
30.443
37.525

276
O
GLY
36
−11.214
31.020
38.198

277
N
ASN
37
−9.385
29.730
38.082

278
CA
ASN
37
−9.277
29.656
39.544

279
CB
ASN
37
−9.365
31.100
40.114

280
CG
ASN
37
−9.477
31.164
41.641

281
OD1
ASN
37
−10.210
30.393
42.258

282
ND2
ASN
37
−8.770
32.120
42.251

283
C
ASN
37
−10.311
28.710
40.190

284
O
ASN
37
−10.123
28.267
41.322

285
N
THR
38
−11.391
28.380
39.484

286
CA
THR
38
−12.386
27.470
40.055

287
CB
THR
38
−13.700
27.427
39.235

288
OG1
THR
38
−13.450
27.862
37.895

289
CG2
THR
38
−14.762
28.307
39.873

290
C
THR
38
−11.839
26.046
40.086

291
O
THR
38
−11.673
25.421
39.040

292
N
THR
39
−11.557
25.536
41.282

293
CA
THR
39
−11.052
24.170
41.439

294
CB
THR
39
−10.387
23.980
42.832

295
OG1
THR
39
−10.417
22.598
43.203

296
CG2
THR
39
−11.115
24.796
43.891

297
C
THR
39
−12.252
23.233
41.305

298
O
THR
39
−12.347
22.204
41.970

299
N
ALA
40
−13.164
23.603
40.413

300
CA
ALA
40
−14.382
22.841
40.199

301
CB
ALA
40
−15.580
23.771
40.320

302
C
ALA
40
−14.476
22.058
38.895

303
O
ALA
40
−14.212
22.578
37.809

304
N
ILE
41
−14.885
20.799
39.027

305
CA
ILE
41
−15.070
19.895
37.898

306
CB
ILE
41
−15.826
18.634
38.337

307
CG2
ILE
41
−15.263
17.415
37.631

308
CG1
ILE
41
−15.727
18.477
39.856

309
CD1
ILE
41
−17.058
18.210
40.531

310
C
ILE
41
−15.897
20.607
36.837

311
O
ILE
41
−15.950
20.193
35.677

312
N
ASP
42
−16.558
21.675
37.268

313
CA
ASP
42
−17.380
22.496
36.401

314
CB
ASP
42
−17.748
23.795
37.127

315
CG
ASP
42
−18.993
24.455
36.566

316
OD1
ASP
42
−18.907
25.110
35.506

317
OD2
ASP
42
−20.064
24.324
37.194

318
C
ASP
42
−16.540
22.825
35.182

319
O
ASP
42
−17.032
22.831
34.053

320
N
LYS
43
−15.257
23.071
35.430

321
CA
LYS
43
−14.335
23.446
34.372

322
CB
LYS
43
−13.943
24.914
34.554

323
CG
LYS
43
−15.024
25.780
35.195

324
CD
LYS
43
−15.987
26.329
34.143

325
CE
LYS
43
−16.654
27.625
34.597

326
NZ
LYS
43
−17.005
28.511
33.447

327
C
LYS
43
−13.066
22.607
34.257

328
O
LYS
43
−11.965
23.130
34.423

329
N
GLU
44
−13.205
21.319
33.959

330
CA
GLU
44
−12.030
20.466
33.812

331
CB
GLU
44
−12.250
19.092
34.441

332
CG
GLU
44
−11.089
18.143
34.173

333
CD
GLU
44
−11.047
16.967
35.126

334
OE1
GLU
44
−10.883
17.186
36.346

335
OE2
GLU
44
−11.174
15.819
34.648

336
C
GLU
44
−11.701
20.275
32.347

337
O
GLU
44
−12.521
19.755
31.591

338
N
ILE
45
−10.501
20.688
31.949

339
CA
ILE
45
−10.088
20.545
30.562

340
CB
ILE
45
−9.347
21.766
30.035

341
CG2
ILE
45
−9.435
21.761
28.517

342
CG1
ILE
45
−9.902
23.040
30.678

343
CD1
ILE
45
−9.672
24.296
29.865

344
C
ILE
45
−9.194
19.372
30.284

345
O
ILE
45
−9.182
18.856
29.167

346
N
ALA
46
−8.428
18.959
31.284

347
CA
ALA
46
−7.530
17.841
31.084

348
CB
ALA
46
−6.381
18.267
30.189

349
C
ALA
46
−6.987
17.248
32.368

350
O
ALA
46
−6.720
17.959
33.343

351
N
ARG
47
−6.822
15.928
32.342

352
CA
ARG
47
−6.298
15.178
33.470

353
CB
ARG
47
−7.441
14.575
34.280

354
CG
ARG
47
−7.015
13.641
35.408

355
CD
ARG
47
−8.247
13.002
36.050

356
NE
ARG
47
−9.462
13.361
35.316

357
CZ
ARG
47
−10.486
12.542
35.095

358
NH1
ARG
47
−10.455
11.297
35.554

359
NH2
ARG
47
−11.537
12.966
34.401

360
C
ARG
47
−5.416
14.070
32.927

361
O
ARG
47
−5.896
13.124
32.308

362
N
PHE
48
−4.115
14.206
33.135

363
CA
PHE
48
−3.178
13.199
32.672

364
CB
PHE
48
−1.966
13.856
32.018

365
CG
PHE
48
−0.848
12.904
31.696

366
CD1
PHE
48
−0.055
12.372
32.705

367
CD2
PHE
48
−0.573
12.561
30.376

368
CE1
PHE
48
1.001
11.520
32.404

369
CE2
PHE
48
0.483
11.709
30.063

370
CZ
PHE
48
1.270
11.186
31.079

371
C
PHE
48
−2.774
12.448
33.917

372
O
PHE
48
−2.696
13.029
34.993

373
N
VAL
49
−2.508
11.160
33.764

374
CA
VAL
49
−2.160
10.329
34.900

375
CB
VAL
49
−3.265
9.311
35.153

376
CG1
VAL
49
−3.390
9.011
36.624

377
CG2
VAL
49
−4.551
9.854
34.625

378
C
VAL
49
−0.856
9.574
34.750

379
O
VAL
49
−0.704
8.745
33.855

380
N
PRO
50
0.111
9.865
35.630

381
CD
PRO
50
0.015
10.900
36.670

382
CA
PRO
50
1.419
9.203
35.602

383
CB
PRO
50
2.161
9.771
36.819

384
CG
PRO
50
1.248
10.723
37.473

385
C
PRO
50
1.315
7.685
35.687

386
O
PRO
50
1.290
6.986
34.674

387
N
ASN
51
1.251
7.201
36.920

388
CA
ASN
51
1.177
5.784
37.218

389
CB
ASN
51
0.438
5.604
38.552

390
CG
ASN
51
1.266
6.105
39.734

391
OD1
ASN
51
1.184
5.572
40.838

392
ND2
ASN
51
2.076
7.130
39.494

393
C
ASN
51
0.616
4.887
36.104

394
O
ASN
51
0.984
3.721
36.014

395
N
SER
52
−0.246
5.423
35.246

396
CA
SER
52
−0.778
4.642
34.135

397
CB
SER
52
−2.043
3.901
34.562

398
OG
SER
52
−1.712
2.728
35.285

399
C
SER
52
−1.073
5.519
32.922

400
O
SER
52
−2.207
5.576
32.451

401
N
ASN
53
−0.036
6.186
32.422

402
CA
ASN
53
−0.128
7.086
31.269

403
CB
ASN
53
1.077
6.875
30.345

404
CG
ASN
53
2.395
7.181
31.022

405
OD1
ASN
53
2.483
7.205
32.250

406
ND2
ASN
53
3.431
7.415
30.222

407
C
ASN
53
−1.406
7.005
30.438

408
O
ASN
53
−1.634
6.019
29.740

409
N
MET
54
−2.231
8.050
30.517

410
CA
MET
54
−3.478
8.111
29.758

411
CB
MET
54
−4.467
7.044
30.230

412
CG
MET
54
−5.813
7.131
29.521

413
SD
MET
54
−6.220
5.675
28.533

414
CE
MET
54
−5.644
6.180
26.893

415
C
MET
54
−4.150
9.477
29.811

416
O
MET
54
−4.214
10.128
30.849

417
N
ASN
55
−4.693
9.867
28.670

418
CA
ASN
55
−5.333
11.153
28.482

419
CB
ASN
55
−5.062
11.624
27.084

420
CG
ASN
55
−3.754
12.281
26.945

421
OD1
ASN
55
−2.716
11.750
27.330

422
ND2
ASN
55
−3.811
13.449
26.331

423
C
ASN
55
−6.827
11.271
28.638

424
O
ASN
55
−7.544
11.059
27.660

425
N
PHE
56
−7.333
11.609
29.814

426
CA
PHE
56
−8.772
11.808
29.866

427
CB
PHE
56
−9.470
11.056
31.007

428
CG
PHE
56
−8.568
10.201
31.837

429
CD1
PHE
56
−8.232
10.608
33.119

430
CD2
PHE
56
−8.191
8.930
31.413

431
CE1
PHE
56
−7.514
9.782
33.962

432
CE2
PHE
56
−7.467
8.090
32.254

433
CZ
PHE
56
−7.145
8.511
33.537

434
C
PHE
56
−9.048
13.307
29.994

435
O
PHE
56
−8.365
14.019
30.734

436
N
THR
57
−10.044
13.779
29.255

437
CA
THR
57
−10.412
15.190
29.262

438
CB
THR
57
−10.724
15.685
27.827

439
OG1
THR
57
−11.685
16.745
27.881

440
CG2
THR
57
−11.284
14.551
26.976

441
C
THR
57
−11.628
15.451
30.145

442
O
THR
57
−12.355
14.528
30.505

443
N
GLY
58
−11.837
16.716
30.498

444
CA
GLY
58
−12.979
17.076
31.318

445
C
GLY
58
−14.024
17.768
30.464

446
O
GLY
58
−13.890
17.812
29.241

447
N
GLN
59
−15.063
18.306
31.095

448
CA
GLN
59
−16.126
19.003
30.367

449
CB
GLN
59
−17.274
19.346
31.321

450
CG
GLN
59
−18.574
19.794
30.654

451
CD
GLN
59
−19.669
20.101
31.668

452
OE1
GLN
59
−20.534
20.949
31.435

453
NE2
GLN
59
−19.635
19.410
32.802

454
C
GLN
59
−15.540
20.283
29.787

455
O
GLN
59
−16.156
21.347
29.840

456
N
ALA
60
−14.346
20.175
29.220

457
CA
ALA
60
−13.690
21.341
28.672

458
CB
ALA
60
−12.475
21.627
29.453

459
C
ALA
60
−13.348
21.342
27.200

460
O
ALA
60
−12.564
20.527
26.710

461
N
TYR
61
−13.968
22.301
26.526

462
CA
TYR
61
−13.803
22.587
25.112

463
CB
TYR
61
−13.246
23.997
24.990

464
CG
TYR
61
−14.189
25.004
24.392

465
CD1
TYR
61
−15.560
24.760
24.312

466
CE1
TYR
61
−16.411
25.672
23.693

467
CD2
TYR
61
−13.697
26.190
23.853

468
CE2
TYR
61
−14.534
27.102
23.236

469
CZ
TYR
61
−15.887
26.841
23.156

470
OH
TYR
61
−16.702
27.733
22.501

471
C
TYR
61
−12.929
21.638
24.298

472
O
TYR
61
−13.379
21.077
23.298

473
N
SER
62
−11.676
21.494
24.724

474
CA
SER
62
−10.689
20.641
24.059

475
CB
SER
62
−10.853
19.176
24.482

476
OG
SER
62
−9.943
18.348
23.777

477
C
SER
62
−10.753
20.739
22.543

478
O
SER
62
−10.514
19.758
21.833

479
N
GLY
63
−11.090
21.925
22.047

480
CA
GLY
63
−11.150
22.108
20.613

481
C
GLY
63
−9.750
22.428
20.129

482
O
GLY
63
−9.412
22.215
18.961

483
N
ARG
64
−8.930
22.934
21.049

484
CA
ARG
64
−7.557
23.312
20.739

485
CB
ARG
64
−7.547
24.615
19.928

486
CG
ARG
64
−8.931
25.215
19.668

487
CD
ARG
64
−9.043
26.645
20.154

488
NE
ARG
64
−10.064
26.812
21.187

489
CZ
ARG
64
−9.907
27.584
22.252

490
NH1
ARG
64
−8.777
28.244
22.406

491
NH2
ARG
64
−10.870
27.697
23.151

492
C
ARG
64
−6.714
23.494
22.002

493
O
ARG
64
−6.246
24.596
22.294

494
N
GLU
65
−6.513
22.414
22.747

495
CA
GLU
65
−5.725
22.480
23.967

496
CB
GLU
65
−6.643
22.759
25.148

497
CG
GLU
65
−7.522
23.967
24.930

498
CD
GLU
65
−8.697
24.018
25.868

499
OE1
GLU
65
−8.509
23.683
27.052

500
OE2
GLU
65
−9.803
24.396
25.419

501
C
GLU
65
−5.013
21.164
24.179

502
O
GLU
65
−5.523
20.124
23.780

503
N
ILE
66
−3.834
21.193
24.793

504
CA
ILE
66
−3.115
19.951
25.041

505
CB
ILE
66
−2.154
19.590
23.888

506
CG2
ILE
66
−1.256
18.436
24.301

507
CG1
ILE
66
−2.950
19.134
22.669

508
CD1
ILE
66
−2.694
19.958
21.438

509
C
ILE
66
−2.319
19.934
26.326

510
O
ILE
66
−1.628
20.893
26.661

511
N
ILE
67
−2.425
18.814
27.032

512
CA
ILE
67
−1.716
18.602
28.290

513
CB
ILE
67
−2.591
17.830
29.294

514
CG2
ILE
67
−3.229
16.634
28.601

515
CG1
ILE
67
−1.741
17.351
30.474

516
CD1
ILE
67
−2.005
18.096
31.756

517
C
ILE
67
−0.493
17.754
27.970

518
O
ILE
67
−0.505
17.009
26.995

519
N
TYR
68
0.555
17.853
28.783

520
CA
TYR
68
1.769
17.078
28.539

521
CB
TYR
68
2.909
18.004
28.107

522
CG
TYR
68
2.798
18.568
26.705

523
CD1
TYR
68
3.893
18.553
25.849

524
CE1
TYR
68
3.815
19.086
24.564

525
CD2
TYR
68
1.611
19.136
26.240

526
CE2
TYR
68
1.526
19.672
24.952

527
CZ
TYR
68
2.635
19.642
24.119

528
OH
TYR
68
2.568
20.147
22.837

529
C
TYR
68
2.215
16.287
29.766

530
O
TYR
68
1.713
16.488
30.873

531
N
SER
69
3.172
15.389
29.560

532
CA
SER
69
3.699
14.562
30.639

533
CB
SER
69
4.622
13.480
30.074

534
OG
SER
69
4.604
13.482
28.651

535
C
SER
69
4.463
15.423
31.636

536
O
SER
69
4.517
15.103
32.819

537
N
ASN
70
5.074
16.504
31.159

538
CA
ASN
70
5.790
17.389
32.066

539
CB
ASN
70
6.799
18.303
31.328

540
CG
ASN
70
6.299
18.812
29.968

541
OD1
ASN
70
5.725
18.070
29.168

542
ND2
ASN
70
6.533
20.106
29.746

543
C
ASN
70
4.693
18.193
32.730

544
O
ASN
70
4.946
19.064
33.557

545
N
GLY
71
3.462
17.850
32.355

546
CA
GLY
71
2.278
18.489
32.893

547
C
GLY
71
2.073
19.899
32.395

548
O
GLY
71
1.924
20.815
33.185

549
N
SER
72
2.047
20.089
31.085

550
CA
SER
72
1.866
21.435
30.561

551
CB
SER
72
3.192
21.960
30.016

552
OG
SER
72
4.205
21.846
31.006

553
C
SER
72
0.780
21.521
29.505

554
O
SER
72
0.353
20.506
28.943

555
N
LEU
73
0.343
22.743
29.228

556
CA
LEU
73
−0.734
22.932
28.280

557
CB
LEU
73
−1.995
23.325
29.034

558
CG
LEU
73
−3.271
23.043
28.264

559
CD1
LEU
73
−3.946
21.849
28.889

560
CD2
LEU
73
−4.180
24.258
28.297

561
C
LEU
73
−0.511
23.933
27.170

562
O
LEU
73
−0.264
25.111
27.416

563
N
LEU
74
−0.591
23.461
25.936

564
CA
LEU
74
−0.451
24.373
24.825

565
CB
LEU
74
0.073
23.688
23.567

566
CG
LEU
74
−0.431
24.436
22.322

567
CD1
LEU
74
0.567
25.518
21.915

568
CD2
LEU
74
−0.676
23.460
21.200

569
C
LEU
74
−1.873
24.799
24.577

570
O
LEU
74
−2.809
24.071
24.889

571
N
PHE
75
−2.032
25.977
24.010

572
CA
PHE
75
−3.342
26.483
23.715

573
CB
PHE
75
−3.705
27.583
24.691

574
CG
PHE
75
−5.127
27.546
25.125

575
CD1
PHE
75
−5.468
27.075
26.388

576
CD2
PHE
75
−6.130
27.997
24.282

577
CE1
PHE
75
−6.797
27.054
26.806

578
CE2
PHE
75
−7.457
27.981
24.692

579
CZ
PHE
75
−7.794
27.511
25.953

580
C
PHE
75
−3.268
27.039
22.326

581
O
PHE
75
−2.542
28.002
22.067

582
N
GLN
76
−3.994
26.408
21.420

583
CA
GLN
76
−4.009
26.870
20.051

584
CB
GLN
76
−4.394
25.732
19.113

585
CG
GLN
76
−3.531
24.494
19.293

586
CD
GLN
76
−3.334
23.718
18.003

587
OE1
GLN
76
−4.292
23.205
17.423

588
NE2
GLN
76
−2.087
23.626
17.548

589
C
GLN
76
−5.034
27.976
19.992

590
O
GLN
76
−5.705
28.245
20.986

591
N
MET
77
−5.140
28.613
18.832

592
CA
MET
77
−6.080
29.707
18.608

593
CB
MET
77
−7.145
29.286
17.595

594
CG
MET
77
−6.633
28.383
16.482

595
SD
MET
77
−6.639
29.130
14.817

596
CE
MET
77
−7.657
30.610
15.055

597
C
MET
77
−6.773
30.221
19.863

598
O
MET
77
−7.887
29.802
20.178

599
N
ILE
78
−6.111
31.124
20.576

600
CA
ILE
78
−6.680
31.708
21.783

601
CB
ILE
78
−5.582
32.205
22.733

602
CG2
ILE
78
−6.197
32.999
23.862

603
CG1
ILE
78
−4.806
31.018
23.299

604
CD1
ILE
78
−4.040
30.244
22.264

605
C
ILE
78
−7.512
32.890
21.319

606
O
ILE
78
−7.301
33.407
20.221

607
N
THR
79
−8.461
33.320
22.136

608
CA
THR
79
−9.294
34.446
21.751

609
CB
THR
79
−10.574
33.963
21.053

610
OG1
THR
79
−10.232
32.985
20.063

611
CG2
THR
79
−11.281
35.125
20.377

612
C
THR
79
−9.659
35.251
22.976

613
O
THR
79
−9.661
34.722
24.078

614
N
MET
80
−9.952
36.533
22.783

615
CA
MET
80
−10.316
37.406
23.894

616
CB
MET
80
−11.196
38.560
23.388

617
CG
MET
80
−12.687
38.424
23.712

618
SD
MET
80
−13.329
39.702
24.832

619
CE
MET
80
−15.010
39.079
25.146

620
C
MET
80
−11.053
36.621
24.981

621
O
MET
80
−10.823
36.814
26.176

622
N
LYS
81
−11.925
35.722
24.544

623
CA
LYS
81
−12.720
34.894
25.438

624
CB
LYS
81
−13.783
34.160
24.615

625
CG
LYS
81
−13.960
34.719
23.198

626
CD
LYS
81
−15.418
35.052
22.893

627
CE
LYS
81
−15.582
36.480
22.381

628
NZ
LYS
81
−15.515
36.570
20.894

629
C
LYS
81
−11.865
33.896
26.226

630
O
LYS
81
−12.236
33.467
27.322

631
N
ASP
82
−10.718
33.537
25.657

632
CA
ASP
82
−9.780
32.596
26.266

633
CB
ASP
82
−8.926
31.940
25.179

634
CG
ASP
82
−9.392
30.545
24.823

635
OD1
ASP
82
−9.979
29.857
25.689

636
OD2
ASP
82
−9.163
30.138
23.669

637
C
ASP
82
−8.860
33.323
27.241

638
O
ASP
82
−8.117
32.700
27.997

639
N
MET
83
−8.905
34.648
27.204

640
CA
MET
83
−8.069
35.466
28.069

641
CB
MET
83
−8.285
36.942
27.751

642
CG
MET
83
−7.197
37.860
28.276

643
SD
MET
83
−7.281
39.481
27.485

644
CE
MET
83
−5.863
40.299
28.215

645
C
MET
83
−8.365
35.222
29.536

646
O
MET
83
−9.458
34.785
29.894

647
N
GLY
84
−7.390
35.518
30.387

648
CA
GLY
84
−7.587
35.323
31.809

649
C
GLY
84
−6.655
34.328
32.474

650
O
GLY
84
−5.683
33.862
31.883

651
N
VAL
85
−6.968
33.995
33.722

652
CA
VAL
85
−6.159
33.070
34.507

653
CB
VAL
85
−6.239
33.402
36.001

654
CG1
VAL
85
−7.606
33.982
36.314

655
CG2
VAL
85
−5.987
32.148
36.834

656
C
VAL
85
−6.575
31.622
34.346

657
O
VAL
85
−7.743
31.312
34.139

658
N
TYR
86
−5.598
30.737
34.463

659
CA
TYR
86
−5.851
29.322
34.355

660
CB
TYR
86
−5.271
28.794
33.049

661
CG
TYR
86
−6.112
29.205
31.868

662
CD1
TYR
86
−6.041
30.502
31.350

663
CE1
TYR
86
−6.862
30.904
30.286

664
CD2
TYR
86
−7.018
28.316
31.297

665
CE2
TYR
86
−7.840
28.704
30.236

666
CZ
TYR
86
−7.760
29.999
29.735

667
OH
TYR
86
−8.581
30.378
28.693

668
C
TYR
86
−5.200
28.666
35.553

669
O
TYR
86
−4.266
29.218
36.147

670
N
THR
87
−5.714
27.500
35.926

671
CA
THR
87
−5.170
26.789
37.069

672
CB
THR
87
−6.009
27.039
38.331

673
OG1
THR
87
−5.844
28.399
38.751

674
CG2
THR
87
−5.554
26.118
39.460

675
C
THR
87
−5.013
25.300
36.881

676
O
THR
87
−5.866
24.616
36.298

677
N
LEU
88
−3.903
24.803
37.394

678
CA
LEU
88
−3.598
23.407
37.298

679
CB
LEU
88
−2.232
23.230
36.657

680
CG
LEU
88
−1.572
21.890
36.945

681
CD1
LEU
88
−1.341
21.179
35.628

682
CD2
LEU
88
−0.277
22.094
37.694

683
C
LEU
88
−3.580
22.837
38.708

684
O
LEU
88
−3.158
23.497
39.656

685
N
ASP
89
−4.062
21.614
38.844

686
CA
ASP
89
−4.060
20.980
40.135

687
CB
ASP
89
−5.466
20.835
40.688

688
CG
ASP
89
−5.466
20.533
42.165

689
OD1
ASP
89
−4.427
20.041
42.660

690
OD2
ASP
89
−6.488
20.789
42.834

691
C
ASP
89
−3.453
19.632
39.935

692
O
ASP
89
−3.650
18.992
38.911

693
N
MET
90
−2.702
19.207
40.927

694
CA
MET
90
−2.048
17.931
40.860

695
CB
MET
90
−0.553
18.149
40.672

696
CG
MET
90
−0.253
19.287
39.713

697
SD
MET
90
0.923
20.491
40.358

698
CE
MET
90
0.184
20.923
41.913

699
C
MET
90
−2.336
17.175
42.139

700
O
MET
90
−2.652
17.772
43.173

701
N
THR
91
−2.233
15.855
42.068

702
CA
THR
91
−2.503
15.044
43.233

703
CB
THR
91
−4.001
14.788
43.385

704
OG1
THR
91
−4.720
16.011
43.182

705
CG2
THR
91
−4.299
14.236
44.763

706
C
THR
91
−1.812
13.703
43.203

707
O
THR
91
−1.657
13.083
42.153

708
N
ASP
92
−1.403
13.281
44.388

709
CA
ASP
92
−0.748
12.007
44.630

710
CB
ASP
92
0.771
12.185
44.762

711
CG
ASP
92
1.160
13.487
45.458

712
OD1
ASP
92
0.492
14.516
45.230

713
OD2
ASP
92
2.145
13.484
46.231

714
C
ASP
92
−1.362
11.729
45.983

715
O
ASP
92
−1.165
12.519
46.904

716
N
GLU
93
−2.117
10.648
46.138

717
CA
GLU
93
−2.715
10.477
47.445

718
CB
GLU
93
−3.787
9.392
47.470

719
CG
GLU
93
−5.063
9.947
48.095

720
CD
GLU
93
−5.284
11.409
47.734

721
OE1
GLU
93
−5.873
11.649
46.660

722
OE2
GLU
93
−4.869
12.308
48.506

723
C
GLU
93
−1.739
10.328
48.587

724
O
GLU
93
−1.086
9.308
48.813

725
N
ASN
94
−1.679
11.448
49.279

726
CA
ASN
94
−0.867
11.736
50.428

727
CB
ASN
94
0.596
11.367
50.190

728
CG
ASN
94
1.175
10.538
51.323

729
OD1
ASN
94
1.955
9.614
51.099

730
ND2
ASN
94
0.787
10.865
52.552

731
C
ASN
94
−1.088
13.240
50.351

732
O
ASN
94
−1.137
13.922
51.369

733
N
TYR
95
−1.254
13.735
49.117

734
CA
TYR
95
−1.535
15.149
48.875

735
CB
TYR
95
−0.432
16.035
49.444

736
CG
TYR
95
−1.058
17.151
50.234

737
CD1
TYR
95
−1.341
16.986
51.589

738
CE1
TYR
95
−2.060
17.944
52.301

739
CD2
TYR
95
−1.500
18.317
49.606

740
CE2
TYR
95
−2.222
19.285
50.309

741
CZ
TYR
95
−2.501
19.088
51.657

742
OH
TYR
95
−3.241
20.012
52.365

743
C
TYR
95
−1.869
15.658
47.471

744
O
TYR
95
−1.303
15.222
46.469

745
N
ARG
96
−2.805
16.608
47.437

746
CA
ARG
96
−3.268
17.267
46.215

747
CB
ARG
96
−4.786
17.055
46.035

748
CG
ARG
96
−5.568
18.250
45.450

749
CD
ARG
96
−7.080
17.966
45.305

750
NE
ARG
96
−7.913
19.110
45.708

751
CZ
ARG
96
−9.219
19.244
45.454

752
NH1
ARG
96
−9.879
18.308
44.789

753
NH2
ARG
96
−9.872
20.323
45.871

754
C
ARG
96
−2.971
18.763
46.373

755
O
ARG
96
−3.512
19.414
47.271

756
N
ARG
97
−2.106
19.307
45.520

757
CA
ARG
97
−1.767
20.725
45.593

758
CB
ARG
97
−0.250
20.898
45.679

759
CG
ARG
97
0.379
20.138
46.842

760
CD
ARG
97
1.906
20.212
46.837

761
NE
ARG
97
2.509
19.298
47.813

762
CZ
ARG
97
3.820
19.154
48.011

763
NH1
ARG
97
4.691
19.866
47.304

764
NH2
ARG
97
4.268
18.293
48.919

765
C
ARG
97
−2.312
21.434
44.363

766
O
ARG
97
−2.285
20.883
43.267

767
N
THR
98
−2.812
22.651
44.546

768
CA
THR
98
−3.380
23.427
43.447

769
CB
THR
98
−4.580
24.260
43.926

770
OG1
THR
98
−4.894
23.912
45.281

771
CG2
THR
98
−5.788
24.008
43.047

772
C
THR
98
−2.367
24.385
42.842

773
O
THR
98
−1.990
24.260
41.678

774
N
GLN
99
−1.958
25.353
43.657

775
CA
GLN
99
−0.981
26.385
43.307

776
CB
GLN
99
0.299
26.147
44.098

777
CG
GLN
99
0.738
27.327
44.937

778
CD
GLN
99
1.912
26.989
45.826

779
OE1
GLN
99
1.737
26.564
46.969

780
NE2
GLN
99
3.123
27.174
45.307

781
C
GLN
99
−0.621
26.568
41.823

782
O
GLN
99
0.538
26.459
41.440

783
N
ALA
100
−1.613
26.873
40.999

784
CA
ALA
100
−1.371
27.063
39.579

785
CB
ALA
100
−2.021
25.951
38.804

786
C
ALA
100
−1.848
28.418
39.064

787
O
ALA
100
−2.544
28.510
38.053

788
N
THR
101
−1.474
29.476
39.767

789
CA
THR
101
−1.841
30.809
39.329

790
CB
THR
101
−1.397
31.885
40.343

791
OG1
THR
101
−1.676
31.437
41.676

792
CG2
THR
101
−2.117
33.206
40.073

793
C
THR
101
−1.091
31.053
38.023

794
O
THR
101
0.124
30.872
37.960

795
N
VAL
102
−1.812
31.433
36.977

796
CA
VAL
102
−1.175
31.722
35.703

797
CB
VAL
102
−0.558
30.461
35.071

798
CG1
VAL
102
−0.975
30.300
33.624

799
CG2
VAL
102
0.929
30.588
35.126

800
C
VAL
102
−2.132
32.395
34.745

801
O
VAL
102
−3.043
31.785
34.183

802
N
ARG
103
−1.909
33.688
34.588

803
CA
ARG
103
−2.728
34.516
33.732

804
CB
ARG
103
−3.262
35.699
34.540

805
CG
ARG
103
−4.510
36.351
33.987

806
CD
ARG
103
−4.706
37.744
34.579

807
NE
ARG
103
−4.847
37.722
36.034

808
CZ
ARG
103
−3.836
37.858
36.889

809
NH1
ARG
103
−2.599
38.027
36.440

810
NH2
ARG
103
−4.061
37.829
38.198

811
C
ARG
103
−1.860
35.025
32.605

812
O
ARG
103
−0.659
35.210
32.771

813
N
PHE
104
−2.468
35.237
31.451

814
CA
PHE
104
−1.741
35.761
30.313

815
CB
PHE
104
−1.299
34.631
29.377

816
CG
PHE
104
−2.419
33.754
28.903

817
CD1
PHE
104
−2.868
32.694
29.679

818
CD2
PHE
104
−3.009
33.973
27.661

819
CE1
PHE
104
−3.897
31.866
29.227

820
CE2
PHE
104
−4.039
33.152
27.200

821
CZ
PHE
104
−4.483
32.095
27.982

822
C
PHE
104
−2.690
36.721
29.615

823
O
PHE
104
−3.855
36.831
30.012

824
N
HIS
105
−2.207
37.422
28.592

825
CA
HIS
105
−3.054
38.380
27.886

826
CB
HIS
105
−2.582
39.800
28.195

827
CG
HIS
105
−2.648
40.141
29.652

828
CD2
HIS
105
−1.687
40.228
30.594

829
ND1
HIS
105
−3.846
40.374
30.301

830
CE1
HIS
105
−3.608
40.587
31.584

831
NE2
HIS
105
−2.308
40.504
31.790

832
C
HIS
105
−3.137
38.168
26.383

833
O
HIS
105
−2.169
37.781
25.745

834
N
VAL
106
−4.315
38.415
25.828

835
CA
VAL
106
−4.535
38.259
24.403

836
CB
VAL
106
−5.904
37.613
24.108

837
CG1
VAL
106
−6.899
38.676
23.601

838
CG2
VAL
106
−5.742
36.513
23.081

839
C
VAL
106
−4.525
39.639
23.795

840
O
VAL
106
−4.763
40.628
24.491

841
N
HIS
107
−4.277
39.714
22.495

842
CA
HIS
107
−4.258
41.010
21.861

843
CB
HIS
107
−2.872
41.615
21.992

844
CG
HIS
107
−2.593
42.128
23.369

845
CD2
HIS
107
−1.745
41.685
24.324

846
ND1
HIS
107
−3.259
43.201
23.909

847
CE1
HIS
107
−2.835
43.408
25.141

848
NE2
HIS
107
−1.910
42.498
25.420

849
C
HIS
107
−4.728
41.083
20.430

850
O
HIS
107
−4.486
40.196
19.610

851
N
GLN
108
−5.431
42.168
20.160

852
CA
GLN
108
−5.955
42.437
18.847

853
CB
GLN
108
−7.164
43.360
18.963

854
CG
GLN
108
−8.474
42.627
19.142

855
CD
GLN
108
−8.962
42.030
17.843

856
OE1
GLN
108
−8.387
42.272
16.782

857
NE2
GLN
108
−10.029
41.247
17.916

858
C
GLN
108
−4.831
43.139
18.101

859
O
GLN
108
−4.343
44.185
18.535

860
N
PRO
109
−4.386
42.560
16.978

861
CD
PRO
109
−4.875
41.320
16.360

862
CA
PRO
109
−3.306
43.178
16.199

863
CB
PRO
109
−3.215
42.308
14.943

864
CG
PRO
109
−4.490
41.503
14.924

865
C
PRO
109
−3.713
44.608
15.878

866
O
PRO
109
−4.867
44.857
15.541

867
N
VAL
110
−2.780
45.548
15.984

868
CA
VAL
110
−3.114
46.943
15.722

869
CB
VAL
110
−2.045
47.897
16.247

870
CG1
VAL
110
−2.639
49.286
16.358

871
CG2
VAL
110
−1.540
47.428
17.594

872
C
VAL
110
−3.338
47.294
14.267

873
O
VAL
110
−2.988
46.535
13.361

874
N
THR
111
−3.931
48.461
14.059

875
CA
THR
111
−4.199
48.960
12.725

876
CB
THR
111
−5.689
49.231
12.527

877
OG1
THR
111
−6.093
50.311
13.380

878
CG2
THR
111
−6.500
47.991
12.861

879
C
THR
111
−3.445
50.267
12.591

880
O
THR
111
−3.029
50.851
13.588

881
N
GLN
112
−3.273
50.730
11.362

882
CA
GLN
112
−2.559
51.975
11.125

883
CB
GLN
112
−2.098
52.039
9.669

884
CG
GLN
112
−1.694
53.423
9.200

885
CD
GLN
112
−0.199
53.553
8.982

886
OE1
GLN
112
0.531
52.560
8.973

887
NE2
GLN
112
0.267
54.785
8.806

888
C
GLN
112
−3.445
53.173
11.442

889
O
GLN
112
−4.640
53.165
11.148

890
N
PRO
113
−2.867
54.221
12.058

891
CD
PRO
113
−1.455
54.321
12.473

892
CA
PRO
113
−3.610
55.432
12.413

893
CB
PRO
113
−2.844
55.967
13.611

894
CG
PRO
113
−1.417
55.599
13.302

895
C
PRO
113
−3.607
56.427
11.257

896
O
PRO
113
−3.727
56.043
10.094

897
N
PHE
114
−3.457
57.703
11.590

898
CA
PHE
114
−3.423
58.757
10.592

899
CB
PHE
114
−4.466
58.466
9.497

900
CG
PHE
114
−5.324
59.638
9.115

901
CD1
PHE
114
−4.851
60.614
8.243

902
CD2
PHE
114
−6.628
59.737
9.588

903
CE1
PHE
114
−5.670
61.671
7.841

904
CE2
PHE
114
−7.453
60.787
9.192

905
CZ
PHE
114
−6.972
61.756
8.318

906
C
PHE
114
−3.651
60.109
11.256

907
O
PHE
114
−4.723
60.389
11.800

908
N
LEU
115
−2.606
60.931
11.232

909
CA
LEU
115
−2.666
62.260
11.814

910
CB
LEU
115
−1.281
62.902
11.877

911
CG
LEU
115
−0.231
62.475
12.896

912
CD1
LEU
115
0.631
61.390
12.301

913
CD2
LEU
115
0.627
63.669
13.265

914
C
LEU
115
−3.543
63.152
10.971

915
O
LEU
115
−3.850
62.861
9.819

916
N
GLN
116
−3.931
64.258
11.571

917
CA
GLN
116
−4.739
65.259
10.919

918
CB
GLN
116
−6.222
65.080
11.256

919
CG
GLN
116
−7.053
64.427
10.158

920
CD
GLN
116
−8.557
64.573
10.380

921
OE1
GLN
116
−9.003
65.410
11.167

922
NE2
GLN
116
−9.342
63.756
9.683

923
C
GLN
116
−4.205
66.491
11.609

924
O
GLN
116
−4.123
66.537
12.835

925
N
VAL
117
−3.771
67.465
10.836

926
CA
VAL
117
−3.276
68.682
11.434

927
CB
VAL
117
−1.747
68.800
11.382

928
CG1
VAL
117
−1.312
69.991
12.219

929
CG2
VAL
117
−1.108
67.525
11.895

930
C
VAL
117
−3.876
69.762
10.587

931
O
VAL
117
−4.031
69.605
9.374

932
N
THR
118
−4.232
70.862
11.221

933
CA
THR
118
−4.812
71.941
10.474

934
CB
THR
118
−6.134
72.390
11.121

935
OG1
THR
118
−7.222
71.789
10.401

936
CG2
THR
118
−6.280
73.897
11.088

937
C
THR
118
−3.795
73.058
10.384

938
O
THR
118
−3.464
73.706
11.376

939
N
ASN
119
−3.279
73.227
9.170

940
CA
ASN
119
−2.294
74.241
8.841

941
CB
ASN
119
−2.647
75.564
9.526

942
CG
ASN
119
−2.671
76.723
8.555

943
OD1
ASN
119
−1.677
76.979
7.879

944
ND2
ASN
119
−3.793
77.430
8.469

945
C
ASN
119
−0.852
73.852
9.151

946
O
ASN
119
−0.349
74.083
10.245

947
N
THR
120
−0.196
73.248
8.169

948
CA
THR
120
1.194
72.853
8.299

949
CB
THR
120
1.691
72.163
7.005

950
OG1
THR
120
1.575
70.745
7.153

951
CG2
THR
120
3.149
72.523
6.702

952
C
THR
120
1.963
74.149
8.509

953
O
THR
120
3.063
74.156
9.058

954
N
THR
121
1.356
75.244
8.065

955
CA
THR
121
1.950
76.571
8.168

956
CB
THR
121
1.528
77.456
6.977

957
OG1
THR
121
2.182
77.002
5.786

958
CG2
THR
121
1.891
78.913
7.238

959
C
THR
121
1.524
77.271
9.448

960
O
THR
121
0.351
77.611
9.612

961
N
VAL
122
2.468
77.488
10.358

962
CA
VAL
122
2.134
78.173
11.597

963
CB
VAL
122
1.882
77.209
12.763

964
CG1
VAL
122
1.059
77.925
13.808

965
CG2
VAL
122
1.130
75.983
12.284

966
C
VAL
122
3.140
79.211
12.061

967
O
VAL
122
4.320
79.173
11.720

968
N
LYS
123
2.620
80.132
12.865

969
CA
LYS
123
3.353
81.255
13.431

970
CB
LYS
123
2.402
82.437
13.595

971
CG
LYS
123
2.306
83.368
12.408

972
CD
LYS
123
1.550
84.633
12.797

973
CE
LYS
123
1.006
85.355
11.576

974
NZ
LYS
123
0.424
86.679
11.933

975
C
LYS
123
3.988
80.974
14.785

976
O
LYS
123
3.411
80.287
15.627

977
N
GLU
124
5.173
81.538
14.992

978
CA
GLU
124
5.875
81.378
16.256

979
CB
GLU
124
7.205
82.134
16.222

980
CG
GLU
124
8.357
81.399
16.889

981
CD
GLU
124
9.689
82.114
16.720

982
OE1
GLU
124
9.768
83.316
17.053

983
OE2
GLU
124
10.657
81.472
16.258

984
C
GLU
124
4.981
81.956
17.342

985
O
GLU
124
4.536
83.098
17.237

986
N
LEU
125
4.708
81.157
18.369

987
CA
LEU
125
3.867
81.578
19.484

988
CB
LEU
125
4.249
82.997
19.931

989
CG
LEU
125
5.726
83.142
20.327

990
CDI
LEU
125
6.027
84.581
20.704

991
CD2
LEU
125
6.034
82.212
21.492

992
C
LEU
125
2.376
81.486
19.167

993
O
LEU
125
1.563
82.237
19.705

994
N
ASP
126
2.036
80.553
18.284

995
CA
ASP
126
0.651
80.312
17.897

996
CB
ASP
126
0.483
80.481
16.382

997
CG
ASP
126
0.073
81.893
15.990

998
CD1
ASP
126
0.000
82.767
16.880

999
CD2
ASP
126
−0.179
82.127
14.788

1000
C
ASP
126
0.316
78.880
18.321

1001
O
ASP
126
0.966
78.339
19.210

1002
N
SER
127
−0.665
78.252
17.686

1003
CA
SER
127
−1.024
76.895
18.075

1004
CB
SER
127
−2.416
76.884
18.696

1005
CG
SER
127
−3.383
76.445
17.753

1006
C
SER
127
−0.995
75.869
16.958

1007
O
SER
127
−1.060
76.210
15.779

1008
N
VAL
128
−0.897
74.606
17.353

1009
CA
VAL
128
−0.905
73.479
16.428

1010
CB
VAL
128
0.509
73.034
16.013

1011
CG1
VAL
128
0.411
71.890
15.016

1012
CG2
VAL
128
1.264
74.191
15.398

1013
C
VAL
128
−1.530
72.365
17.236

1014
O
VAL
128
−1.502
72.410
18.461

1015
N
THR
129
−2.098
71.370
16.573

1016
CA
THR
129
−2.709
70.283
17.311

1017
CB
THR
129
−4.133
70.650
17.778

1018
CG1
THR
129
−4.050
71.546
18.890

1019
CG2
THR
129
−4.888
69.416
18.221

1020
C
THR
129
−2.765
69.008
16.507

1021
O
THR
129
−3.714
68.757
15.766

1022
N
LEU
130
−1.734
68.200
16.650

1023
CA
LEU
130
−1.720
66.949
15.938

1024
CB
LEU
130
−0.330
66.339
15.974

1025
CG
LEU
130
0.784
67.312
15.609

1026
CD1
LEU
130
1.823
66.570
14.814

1027
CD2
LEU
130
0.236
68.475
14.800

1028
C
LEU
130
−2.696
66.068
16.657

1029
O
LEU
130
−2.770
66.091
17.893

1030
N
THR
131
−3.460
65.308
15.892

1031
CA
THR
131
−4.428
64.408
16.469

1032
CB
THR
131
−5.846
64.904
16.231

1033
OG1
THR
131
−5.850
66.338
16.256

1034
CG2
THR
131
−6.772
64.379
17.316

1035
C
THR
131
−4.194
63.108
15.754

1036
O
THR
131
−4.226
63.052
14.534

1037
N
CYS
132
−3.927
62.063
16.517

1038
CA
CYS
132
−3.645
60.763
15.936

1039
C
CYS
132
−4.906
59.925
15.849

1040
O
CYS
132
−5.303
59.271
16.809

1041
CB
CYS
132
−2.585
60.062
16.780

1042
SG
CYS
132
−2.117
58.412
16.196

1043
N
LEU
133
−5.524
59.952
14.676

1044
CA
LEU
133
−6.757
59.223
14.437

1045
CB
LEU
133
−7.383
59.673
13.120

1046
CG
LEU
133
−8.722
60.397
13.275

1047
CD1
LEU
133
−8.549
61.858
12.898

1048
CD2
LEU
133
−9.777
59.736
12.401

1049
C
LEU
133
−6.579
57.724
14.413

1050
O
LEU
133
−5.799
57.192
13.625

1051
N
SER
134
−7.309
57.045
15.290

1052
CA
SER
134
−7.253
55.596
15.342

1053
CB
SER
134
−6.187
55.099
16.316

1054
OG
SER
134
−6.175
53.675
16.335

1055
C
SER
134
−8.575
54.994
15.746

1056
O
SER
134
−9.367
55.589
16.478

1057
N
ASN
135
−8.799
53.793
15.245

1058
CA
ASN
135
−9.999
53.047
15.539

1059
CB
ASN
135
−10.863
52.909
14.292

1060
CG
ASN
135
−11.860
54.039
14.163

1061
OD1
ASN
135
−12.186
54.480
13.058

1062
ND2
ASN
135
−12.351
54.521
15.302

1063
C
ASN
135
−9.442
51.720
15.970

1064
O
ASN
135
−9.131
50.848
15.161

1065
N
ASP
136
−9.277
51.612
17.274

1066
CA
ASP
136
−8.728
50.438
17.919

1067
CB
ASP
136
−7.239
50.272
17.601

1068
CG
ASP
136
−6.976
49.531
16.319

1069
OD1
ASP
136
−6.087
49.988
15.572

1070
OD2
ASP
136
−7.632
48.497
16.067

1071
C
ASP
136
−8.798
50.906
19.341

1072
O
ASP
136
−8.333
52.007
19.635

1073
N
ILE
137
−9.386
50.138
20.237

1074
CA
ILE
137
−9.351
50.637
21.583

1075
CB
ILE
137
−10.713
51.109
22.078

1076
CG2
ILE
137
−10.604
51.547
23.539

1077
CG1
ILE
137
−11.122
52.328
21.244

1078
CD1
ILE
137
−12.322
53.083
21.763

1079
C
ILE
137
−8.682
49.658
22.511

1080
O
ILE
137
−9.017
48.475
22.593

1081
N
GLY
138
−7.687
50.222
23.177

1082
CA
GLY
138
−6.805
49.532
24.088

1083
C
GLY
138
−5.566
50.112
23.436

1084
O
GLY
138
−4.908
49.446
22.635

1085
N
ALA
139
−5.269
51.371
23.757

1086
CA
ALA
139
−4.157
52.075
23.133

1087
CB
ALA
139
−4.697
53.336
22.471

1088
C
ALA
139
−2.903
52.432
23.920

1089
O
ALA
139
−2.887
52.490
25.153

1090
N
ASN
140
−1.853
52.682
23.143

1091
CA
ASN
140
−0.540
53.090
23.628

1092
CB
ASN
140
0.376
51.888
23.874

1093
CG
ASN
140
1.696
52.291
24.505

1094
OD1
ASN
140
1.818
53.384
25.065

1095
ND2
ASN
140
2.693
51.411
24.418

1096
C
ASN
140
0.028
53.939
22.499

1097
O
ASN
140
0.842
53.480
21.696

1098
N
ILE
141
−0.436
55.177
22.427

1099
CA
ILE
141
0.014
56.084
21.395

1100
CB
ILE
141
−1.028
57.178
21.141

1101
CG2
ILE
141
−0.363
58.390
20.520

1102
CG1
ILE
141
−2.136
56.646
20.232

1103
CD1
ILE
141
−3.309
57.605
20.069

1104
C
ILE
141
1.308
56.735
21.835

1105
O
ILE
141
1.489
57.027
23.014

1106
N
GLN
142
2.207
56.953
20.881

1107
CA
GLN
142
3.489
57.592
21.156

1108
CB
GLN
142
4.615
56.558
21.158

1109
CG
GLN
142
5.328
56.473
22.491

1110
CD
GLN
142
6.569
55.613
22.445

1111
OE1
GLN
142
7.498
55.879
21.678

1112
NE2
GLN
142
6.598
54.574
23.275

1113
C
GLN
142
3.758
58.663
20.103

1114
O
GLN
142
3.555
58.435
18.914

1115
N
TRP
143
4.224
59.828
20.536

1116
CA
TRP
143
4.470
60.916
19.607

1117
CB
TRP
143
3.949
62.213
20.217

1118
CG
TRP
143
2.460
62.318
20.138

1119
CD2
TRP
143
1.676
62.566
18.961

1120
CE2
TRP
143
0.321
62.601
19.356

1121
CE3
TRP
143
1.998
62.763
17.609

1122
CD1
TRP
143
1.568
62.211
21.170

1123
NE1
TRP
143
0.280
62.382
20.709

1124
CZ2
TRP
143
−0.724
62.827
18.444

1125
CZ3
TRP
143
0.957
62.988
16.701

1126
CH2
TRP
143
−0.386
63.016
17.125

1127
C
TRP
143
5.911
61.083
19.152

1128
O
TRP
143
6.811
61.354
19.945

1129
N
LEU
144
6.114
60.934
17.850

1130
CA
LEU
144
7.439
61.063
17.266

1131
CB
LEU
144
7.713
59.897
16.316

1132
CG
LEU
144
7.556
58.477
16.855

1133
CD1
LEU
144
7.691
58.465
18.373

1134
CD2
LEU
144
6.207
57.938
16.426

1135
C
LEU
144
7.642
62.370
16.514

1136
O
LEU
144
6.752
62.854
15.812

1137
N
PHE
145
8.838
62.926
16.670

1138
CA
PHE
145
9.226
64.168
16.023

1139
CB
PHE
145
9.501
65.239
17.087

1140
CG
PHE
145
9.914
66.584
16.534

1141
CD1
PHE
145
10.309
66.729
15.211

1142
CD2
PHE
145
9.917
67.708
17.355

1143
CE1
PHE
145
10.703
67.964
14.716

1144
CE2
PHE
145
10.311
68.953
16.864

1145
CZ
PHE
145
10.704
69.078
15.541

1146
C
PHE
145
10.500
63.837
15.258

1147
O
PHE
145
11.448
63.305
15.830

1148
N
ASN
146
10.514
64.138
13.966

1149
CA
ASN
146
11.679
63.871
13.131

1150
CB
ASN
146
12.812
64.833
13.480

1151
CG
ASN
146
12.594
66.209
12.900

1152
OD1
ASN
146
11.788
66.388
11.985

1153
ND2
ASN
146
13.308
67.197
13.432

1154
C
ASN
146
12.176
62.441
13.252

1155
O
ASN
146
13.376
62.185
13.158

1156
N
SER
147
11.244
61.517
13.463

1157
CA
SER
147
11.558
60.095
13.583

1158
CB
SER
147
12.364
59.632
12.365

1159
OG
SER
147
12.420
60.637
11.367

1160
C
SER
147
12.286
59.695
14.868

1161
O
SER
147
13.100
58.773
14.883

1162
N
GLN
148
11.988
60.399
15.948

1163
CA
GLN
148
12.581
60.103
17.236

1164
CB
GLN
148
13.917
60.816
17.395

1165
CG
GLN
148
15.095
59.868
17.356

1166
CD
GLN
148
16.418
60.587
17.467

1167
OE1
GLN
148
16.492
61.802
17.289

1168
NE2
GLN
148
17.475
59.841
17.762

1169
C
GLN
148
11.589
60.583
18.270

1170
O
GLN
148
10.670
61.336
17.955

1171
N
SER
149
11.766
60.147
19.505

1172
CA
SER
149
10.845
60.512
20.565

1173
CB
SER
149
11.248
59.776
21.838

1174
OG
SER
149
11.763
58.493
21.516

1175
C
SER
149
10.708
62.007
20.839

1176
O
SER
149
11.694
62.692
21.110

1177
N
LEU
150
9.474
62.502
20.750

1178
CA
LEU
150
9.181
63.909
21.017

1179
CB
LEU
150
7.720
64.216
20.666

1180
CG
LEU
150
7.193
65.654
20.753

1181
CD1
LEU
150
8.300
66.632
21.125

1182
CD2
LEU
150
6.604
66.024
19.414

1183
C
LEU
150
9.398
64.045
22.523

1184
O
LEU
150
8.656
63.448
23.300

1185
N
GLN
151
10.394
64.823
22.949

1186
CA
GLN
151
10.659
64.916
24.383

1187
CB
GLN
151
11.816
65.862
24.709

1188
CG
GLN
151
12.402
65.520
26.091

1189
CD
GLN
151
13.150
66.658
26.756

1190
OE1
GLN
151
13.451
67.675
26.131

1191
NE2
GLN
151
13.461
66.486
28.037

1192
C
GLN
151
9.496
65.275
25.278

1193
O
GLN
151
9.531
64.984
26.476

1194
N
LEU
152
8.470
65.902
24.717

1195
CA
LEU
152
7.314
66.266
25.522

1196
CB
LEU
152
6.735
65.023
26.196

1197
CG
LEU
152
5.671
64.257
25.416

1198
CD1
LEU
152
6.143
62.840
25.090

1199
CD2
LEU
152
4.411
64.221
26.252

1200
C
LEU
152
7.766
67.258
26.582

1201
O
LEU
152
8.580
66.935
27.449

1202
N
THR
153
7.232
68.470
26.518

1203
CA
THR
153
7.624
69.497
27.468

1204
CB
THR
153
8.691
70.399
26.854

1205
OG1
THR
153
8.067
71.578
26.333

1206
CG2
THR
153
9.418
69.665
25.727

1207
C
THR
153
6.479
70.371
27.986

1208
O
THR
153
5.306
70.042
27.820

1209
N
GLU
154
6.841
71.493
28.604

1210
CA
GLU
154
5.886
72.427
29.199

1211
CB
GLU
154
6.654
73.480
30.006

1212
CG
GLU
154
5.982
74.846
30.076

1213
CD
GLU
154
6.956
75.961
30.427

1214
OE1
GLU
154
7.347
76.063
31.613

1215
OE2
GLU
154
7.327
76.735
29.516

1216
C
GLU
154
4.902
73.129
28.257

1217
O
GLU
154
3.706
73.217
28.553

1218
N
ARG
155
5.401
73.643
27.138

1219
CA
ARG
155
4.545
74.346
26.188

1220
CB
ARG
155
5.397
75.213
25.255

1221
CG
ARG
155
5.844
74.515
23.977

1222
CD
ARG
155
7.111
75.149
23.420

1223
NE
ARG
155
7.954
74.184
22.716

1224
CZ
ARG
155
8.419
74.361
21.485

1225
NH1
ARG
155
8.110
75.461
20.815

1226
NH2
ARG
155
9.189
73.439
20.923

1227
C
ARG
155
3.658
73.412
25.368

1228
O
ARG
155
2.913
73.859
24.499

1229
N
MET
156
3.744
72.114
25.634

1230
CA
MET
156
2.920
71.147
24.922

1231
CB
MET
156
3.751
69.939
24.494

1232
CG
MET
156
5.212
70.243
24.260

1233
SD
MET
156
5.998
68.984
23.234

1234
CE
MET
156
7.453
69.872
22.674

1235
C
MET
156
1.787
70.698
25.838

1236
O
MET
156
1.860
70.866
27.054

1237
N
THR
157
0.743
70.130
25.246

1238
CA
THR
157
−0.422
69.670
25.992

1239
CB
THR
157
−1.486
70.768
26.107

1240
OG1
THR
157
−0.956
71.881
26.836

1241
CG2
THR
157
−2.726
70.232
26.804

1242
C
THR
157
−1.063
68.546
25.220

1243
O
THR
157
−1.376
68.717
24.043

1244
N
LEU
158
−1.273
67.402
25.856

1245
CA
LEU
158
−1.908
66.321
25.130

1246
CB
LEU
158
−0.852
65.402
24.537

1247
CG
LEU
158
0.097
64.741
25.509

1248
CD1
LEU
158
−0.326
63.307
25.688

1249
CD2
LEU
158
1.497
64.800
24.958

1250
C
LEU
158
−2.908
65.541
25.959

1251
O
LEU
158
−2.641
65.184
27.100

1252
N
SER
159
−4.065
65.279
25.359

1253
CA
SER
159
−5.132
64.575
26.043

1254
CB
SER
159
−6.209
65.570
26.443

1255
OG
SER
159
−6.853
66.060
25.283

1256
C
SER
159
−5.787
63.433
25.286

1257
O
SER
159
−5.202
62.853
24.375

1258
N
GLN
160
−7.039
63.172
25.664

1259
CA
GLN
160
−7.834
62.080
25.131

1260
CB
GLN
160
−8.685
62.520
23.947

1261
CG
GLN
160
−10.139
62.644
24.420

1262
CD
GLN
160
−10.994
63.577
23.594

1263
OE1
GLN
160
−10.635
63.951
22.473

1264
NE2
GLN
160
−12.144
63.958
24.146

1265
C
GLN
160
−6.862
60.971
24.809

1266
O
GLN
160
−6.550
60.652
23.668

1267
N
ASN
161
−6.364
60.435
25.915

1268
CA
ASN
161
−5.387
59.375
25.978

1269
CB
ASN
161
−6.082
58.021
25.966

1270
CG
ASN
161
−6.462
57.569
27.362

1271
OD1
ASN
161
−7.482
56.908
27.564

1272
ND2
ASN
161
−5.636
57.932
28.341

1273
C
ASN
161
−4.353
59.476
24.896

1274
O
ASN
161
−4.311
58.667
23.983

1275
N
ASN
162
−3.517
60.499
25.017

1276
CA
ASN
162
−2.441
60.750
24.069

1277
CB
ASN
162
−1.438
59.590
24.114

1278
CG
ASN
162
−0.559
59.621
25.344

1279
OD1
ASN
162
−0.539
60.594
26.090

1280
ND2
ASN
162
0.183
58.543
25.558

1281
C
ASN
162
−2.891
60.969
22.614

1282
O
ASN
162
−2.053
61.185
21.739

1283
N
SER
163
−4.196
60.921
22.350

1284
CA
SER
163
−4.695
61.095
20.986

1285
CB
SER
163
−6.208
60.892
20.925

1286
OG
SER
163
−6.539
59.620
20.402

1287
C
SER
163
−4.387
62.463
20.432

1288
O
SER
163
−3.653
62.605
19.465

1289
N
ILE
164
−4.966
63.473
21.056

1290
CA
ILE
164
−4.785
64.846
20.622

1291
CB
ILE
164
−6.029
65.666
20.968

1292
CG2
ILE
164
−6.030
66.958
20.176

1293
CG1
ILE
164
−7.279
64.813
20.712

1294
CD1
ILE
164
−8.599
65.559
20.823

1295
C
ILE
164
−3.566
65.502
21.252

1296
O
ILE
164
−3.420
65.516
22.470

1297
N
LEU
165
−2.694
66.050
20.419

1298
CA
LEU
165
−1.500
66.709
20.912

1299
CB
LEU
165
−0.256
66.037
20.346

1300
CG
LEU
165
0.980
66.933
20.245

1301
CD1
LEU
165
1.169
67.741
21.529

1302
CD2
LEU
165
2.193
66.057
19.991

1303
C
LEU
165
−1.540
68.163
20.478

1304
O
LEU
165
−1.692
68.459
19.290

1305
N
ARG
166
−1.373
69.064
21.444

1306
CA
ARG
166
−1.420
70.496
21.178

1307
CB
ARG
166
−2.688
71.081
21.810

1308
CG
ARG
166
−2.621
72.557
22.164

1309
CD
ARG
166
−4.021
73.114
22.446

1310
NE
ARG
166
−4.466
72.851
23.817

1311
CZ
ARG
166
−5.741
72.717
24.186

1312
NH1
ARG
166
−6.712
72.804
23.284

1313
NH2
ARG
166
−6.048
72.481
25.456

1314
C
ARG
166
−0.197
71.254
21.675

1315
O
ARG
166
0.006
71.408
22.874

1316
N
ILE
167
0.609
71.732
20.738

1317
CA
ILE
167
1.802
72.489
21.069

1318
CB
ILE
167
2.904
72.257
20.045

1319
CG2
ILE
167
4.048
73.224
20.294

1320
CG1
ILE
167
3.366
70.799
20.118

1321
CD1
ILE
167
3.852
70.228
18.792

1322
C
ILE
167
1.426
73.952
21.037

1323
O
ILE
167
0.783
74.413
20.089

1324
N
ASP
168
1.836
74.682
22.069

1325
CA
ASP
168
1.534
76.102
22.179

1326
CB
ASP
168
0.011
76.281
22.245

1327
CG
ASP
168
−0.406
77.633
22.778

1328
OD1
ASP
168
0.157
78.081
23.799

1329
OD2
ASP
168
−1.311
78.246
22.175

1330
C
ASP
168
2.177
76.676
23.442

1331
O
ASP
168
1.923
76.196
24.547

1332
N
PRO
169
3.028
77.710
23.301

1333
CD
PRO
169
3.701
78.273
24.480

1334
CA
PRO
169
3.412
78.434
22.082

1335
CB
PRO
169
4.070
79.694
22.625

1336
CG
PRO
169
4.699
79.233
23.880

1337
C
PRO
169
4.383
77.652
21.201

1338
O
PRO
169
5.289
76.989
21.704

1339
N
ILE
170
4.200
77.737
19.886

1340
CA
ILE
170
5.091
77.035
18.979

1341
CB
ILE
170
4.441
76.816
17.612

1342
CG2
ILE
170
3.976
75.374
17.482

1343
CG1
ILE
170
3.279
77.789
17.443

1344
CD1
ILE
170
2.248
77.323
16.473

1345
C
ILE
170
6.349
77.869
18.798

1346
O
ILE
170
6.329
79.086
18.990

1347
N
LYS
171
7.444
77.211
18.441

1348
CA
LYS
171
8.713
77.895
18.228

1349
CB
LYS
171
9.517
77.941
19.533

1350
CG
LYS
171
10.508
76.802
19.735

1351
CD
LYS
171
10.927
76.707
21.200

1352
CE
LYS
171
12.407
76.390
21.343

1353
NZ
LYS
171
13.244
77.619
21.403

1354
C
LYS
171
9.485
77.172
17.136

1355
O
LYS
171
9.442
75.942
17.050

1356
N
ARG
172
10.189
77.936
16.306

1357
CA
ARG
172
10.934
77.361
15.198

1358
CB
ARG
172
12.032
78.314
14.713

1359
CG
ARG
172
12.759
79.107
15.786

1360
CD
ARG
172
13.763
80.063
15.135

1361
NE
ARG
172
14.959
80.279
15.947

1362
CZ
ARG
172
15.943
81.113
15.623

1363
NH1
ARG
172
15.877
81.816
14.496

1364
NH2
ARG
172
16.993
81.249
16.426

1365
C
ARG
172
11.527
75.994
15.490

1366
O
ARG
172
11.560
75.143
14.607

1367
N
GLU
173
11.989
75.773
16.719

1368
CA
GLU
173
12.564
74.478
17.077

1369
CB
GLU
173
12.691
74.334
18.601

1370
CG
GLU
173
13.323
73.012
19.051

1371
CD
GLU
173
13.568
72.938
20.551

1372
OE1
GLU
173
12.746
73.481
21.323

1373
OE2
GLU
173
14.584
72.331
20.956

1374
C
GLU
173
11.638
73.397
16.535

1375
O
GLU
173
12.091
72.371
16.020

1376
N
ASP
174
10.339
73.660
16.637

1377
CA
ASP
174
9.310
72.744
16.174

1378
CB
ASP
174
7.945
73.248
16.618

1379
CG
ASP
174
7.884
73.497
18.103

1380
OD1
ASP
174
7.729
74.670
18.500

1381
OD2
ASP
174
7.995
72.518
18.873

1382
C
ASP
174
9.316
72.553
14.661

1383
O
ASP
174
8.407
71.941
14.106

1384
N
ALA
175
10.339
73.081
13.997

1385
CA
ALA
175
10.470
72.948
12.552

1386
CB
ALA
175
11.540
73.900
12.034

1387
C
ALA
175
10.859
71.513
12.233

1388
O
ALA
175
12.046
71.176
12.229

1389
N
GLY
176
9.860
70.673
11.974

1390
CA
GLY
176
10.121
69.277
11.662

1391
C
GLY
176
8.874
68.493
11.282

1392
O
GLY
176
7.785
69.061
11.203

1393
N
GLU
177
9.026
67.190
11.045

1394
CA
GLU
177
7.899
66.340
10.663

1395
CB
GLU
177
8.264
65.482
9.443

1396
CG
GLU
177
9.615
64.773
9.528

1397
CD
GLU
177
9.855
63.828
8.358

1398
OE1
GLU
177
9.770
62.594
8.555

1399
OE2
GLU
177
10.129
64.320
7.241

1400
C
GLU
177
7.442
65.449
11.819

1401
O
GLU
177
8.195
64.618
12.329

1402
N
TYR
178
6.190
65.623
12.217

1403
CA
TYR
178
5.637
64.882
13.336

1404
CB
TYR
178
4.768
65.822
14.172

1405
CG
TYR
178
5.526
67.022
14.730

1406
CD1
TYR
178
5.133
67.625
15.919

1407
CE1
TYR
178
5.844
68.698
16.453

1408
CD2
TYR
178
6.655
67.535
14.084

1409
CE2
TYR
178
7.368
68.607
14.611

1410
CZ
TYR
178
6.958
69.182
15.796

1411
OH
TYR
178
7.672
70.227
16.339

1412
C
TYR
178
4.858
63.649
12.913

1413
O
TYR
178
4.119
63.659
11.928

1414
N
GLN
179
5.026
62.585
13.688

1415
CA
GLN
179
4.394
61.299
13.409

1416
CB
GLN
179
5.441
60.371
12.787

1417
CG
GLN
179
4.926
59.259
11.903

1418
CD
GLN
179
6.046
58.634
11.083

1419
OE1
GLN
179
6.387
57.467
11.257

1420
NE2
GLN
179
6.628
59.417
10.189

1421
C
GLN
179
3.853
60.662
14.689

1422
O
GLN
179
4.525
60.665
15.724

1423
N
CYS
180
2.642
60.116
14.620

1424
CA
CYS
180
2.051
59.460
15.778

1425
C
CYS
180
2.236
57.959
15.597

1426
O
CYS
180
2.267
57.468
14.472

1427
CB
CYS
180
0.568
59.819
15.907

1428
SG
CYS
180
−0.533
58.739
14.967

1429
N
GLU
181
2.382
57.235
16.703

1430
CA
GLU
181
2.587
55.789
16.649

1431
CB
GLU
181
4.067
55.465
16.818

1432
CG
GLU
181
4.350
54.006
17.128

1433
CD
GLU
181
5.835
53.725
17.242

1434
OE1
GLU
181
6.532
54.499
17.932

1435
OE2
GLU
181
6.309
52.736
16.639

1436
C
GLU
181
1.791
55.018
17.691

1437
O
GLU
181
1.810
55.349
18.879

1438
N
ILE
182
1.110
53.974
17.231

1439
CA
ILE
182
0.294
53.141
18.099

1440
CB
ILE
182
−0.994
52.683
17.391

1441
CG2
ILE
182
−1.620
51.545
18.166

1442
CG1
ILE
182
−1.999
53.830
17.301

1443
CD1
ILE
182
−3.384
53.384
16.842

1444
C
ILE
182
1.038
51.886
18.528

1445
O
ILE
182
1.702
51.245
17.714

1446
N
SER
183
0.912
51.541
19.808

1447
CA
SER
183
1.535
50.346
20.359

1448
CB
SER
183
2.515
50.710
21.480

1449
OG
SER
183
2.933
52.062
21.383

1450
C
SER
183
0.440
49.430
20.896

1451
O
SER
183
−0.691
49.849
21.122

1452
N
ASN
184
0.809
48.177
21.088

1453
CA
ASN
184
−0.033
47.080
21.577

1454
CB
ASN
184
−0.421
46.229
20.360

1455
CG
ASN
184
−1.611
45.318
20.594

1456
OD1
ASN
184
−1.458
44.113
20.810

1457
ND2
ASN
184
−2.806
45.880
20.508

1458
C
ASN
184
1.171
46.459
22.226

1459
O
ASN
184
2.143
47.174
22.463

1460
N
PRO
185
1.103
45.201
22.682

1461
CD
PRO
185
0.255
44.039
22.962

1462
CA
PRO
185
2.467
44.997
23.142

1463
CB
PRO
185
2.403
43.689
23.928

1464
CG
PRO
185
0.939
43.454
24.169

1465
C
PRO
185
3.056
44.823
21.727

1466
O
PRO
185
2.369
44.356
20.813

1467
N
VAL
186
4.290
45.259
21.548

1468
CA
VAL
186
4.997
45.228
20.277

1469
CB
VAL
186
6.459
44.866
20.580

1470
CG1
VAL
186
7.336
45.068
19.361

1471
CG2
VAL
186
6.944
45.777
21.719

1472
C
VAL
186
4.426
44.464
19.058

1473
O
VAL
186
4.903
43.395
18.659

1474
N
SER
187
3.397
45.096
18.488

1475
CA
SER
187
2.633
44.712
17.294

1476
CB
SER
187
1.408
43.872
17.660

1477
OG
SER
187
1.662
42.485
17.534

1478
C
SER
187
2.172
46.120
16.923

1479
O
SER
187
0.999
46.463
17.052

1480
N
VAL
188
3.121
46.935
16.481

1481
CA
VAL
188
2.869
48.337
16.180

1482
CB
VAL
188
4.024
49.165
16.722

1483
CG1
VAL
188
3.780
49.508
18.179

1484
CG2
VAL
188
5.312
48.367
16.589

1485
C
VAL
188
2.657
48.746
14.735

1486
O
VAL
188
2.845
47.956
13.819

1487
N
ARG
189
2.270
50.005
14.553

1488
CA
ARG
189
2.046
50.590
13.235

1489
CB
ARG
189
0.689
50.161
12.672

1490
CG
ARG
189
0.730
48.784
12.041

1491
CD
ARG
189
−0.167
48.650
10.828

1492
NE
ARG
189
−0.505
47.248
10.598

1493
CZ
ARG
189
−1.608
46.826
9.990

1494
NH1
ARG
189
−2.491
47.701
9.525

1495
NH2
ARG
189
−1.826
45.525
9.846

1496
C
ARG
189
2.118
52.109
13.353

1497
O
ARG
189
1.350
52.721
14.099

1498
N
ARG
190
3.053
52.709
12.620

1499
CA
ARG
190
3.254
54.155
12.646

1500
CB
ARG
190
4.685
54.490
12.218

1501
CG
ARG
190
5.757
53.710
12.980

1502
CD
ARG
190
7.160
54.199
12.633

1503
NE
ARG
190
8.150
53.848
13.652

1504
CZ
ARG
190
9.397
54.317
13.683

1505
NH1
ARG
190
9.826
55.146
12.741

1506
NH2
ARG
190
10.227
53.943
14.651

1507
C
ARG
190
2.264
54.889
11.756

1508
O
ARG
190
1.606
54.289
10.919

1509
N
SER
191
2.167
56.196
11.944

1510
CA
SER
191
1.246
57.011
11.168

1511
CB
SER
191
0.706
58.132
12.037

1512
OG
SER
191
1.788
58.879
12.565

1513
C
SER
191
1.967
57.616
9.979

1514
O
SER
191
3.117
57.271
9.707

1515
N
ASN
192
1.286
58.523
9.277

1516
CA
ASN
192
1.864
59.195
8.118

1517
CB
ASN
192
0.854
60.116
7.402

1518
CG
ASN
192
−0.575
59.983
7.918

1519
OD1
ASN
192
−1.419
60.832
7.627

1520
ND2
ASN
192
−0.857
58.928
8.672

1521
C
ASN
192
3.041
60.027
8.612

1522
O
ASN
192
3.726
59.632
9.549

1523
N
SER
193
3.275
61.186
8.009

1524
CA
SER
193
4.403
62.004
8.433

1525
CB
SER
193
5.637
61.641
7.603

1526
OG
SER
193
6.457
60.688
8.255

1527
C
SER
193
4.153
63.497
8.314

1528
O
SER
193
4.996
64.218
7.789

1529
N
ILE
194
3.016
63.975
8.802

1530
CA
ILE
194
2.726
65.401
8.699

1531
CB
ILE
194
1.601
65.832
9.657

1532
CG2
ILE
194
1.812
67.272
10.111

1533
CG1
ILE
194
0.261
65.769
8.929

1534
CD1
ILE
194
−0.547
64.518
9.213

1535
C
ILE
194
3.957
66.242
8.997

1536
O
ILE
194
4.530
66.169
10.084

1537
N
LYS
195
4.372
67.028
8.015

1538
CA
LYS
195
5.520
67.887
8.200

1539
CB
LYS
195
6.298
68.048
6.899

1540
CG
LYS
195
7.683
68.627
7.083

1541
CD
LYS
195
8.725
67.751
6.400

1542
CE
LYS
195
9.479
68.524
5.328

1543
NZ
LYS
195
9.757
69.919
5.768

1544
C
LYS
195
4.949
69.216
8.615

1545
O
LYS
195
3.903
69.632
8.130

1546
N
LEU
196
5.619
69.879
9.534

1547
CA
LEU
196
5.116
71.148
9.965

1548
CB
LEU
196
4.595
71.096
11.396

1549
CG
LEU
196
3.220
71.740
11.531

1550
CD1
LEU
196
2.161
70.672
11.305

1551
CD2
LEU
196
3.070
72.376
12.901

1552
C
LEU
196
6.164
72.183
9.878

1553
O
LEU
196
7.228
72.072
10.500

1554
N
ASP
197
5.898
73.178
9.059

1555
CA
ASP
197
6.837
74.229
9.021

1556
CB
ASP
197
7.709
74.165
7.787

1557
CG
ASP
197
8.895
73.228
8.028

1558
OD1
ASP
197
9.252
73.021
9.215

1559
OD2
ASP
197
9.458
72.713
7.054

1560
C
ASP
197
6.273
75.555
9.384

1561
O
ASP
197
5.109
75.907
9.210

1562
N
ILE
198
7.220
76.250
9.960

1563
CA
ILE
198
7.038
77.458
10.603

1564
CB
ILE
198
7.825
77.209
11.864

1565
CG2
ILE
198
7.563
78.212
12.916

1566
CG1
ILE
198
7.724
75.715
12.220

1567
CD1
ILE
198
7.332
75.402
13.587

1568
C
ILE
198
7.399
78.768
10.077

1569
O
ILE
198
8.531
79.018
9.594

1570
N
ILE
199
6.432
79.670
10.121

1571
CA
ILE
199
6.860
80.919
9.867

1572
CB
ILE
199
6.413
81.508
8.557

1573
CG2
ILE
199
7.302
82.734
8.216

1574
CG1
ILE
199
6.593
80.448
7.458

1575
CD1
ILE
199
7.976
80.448
6.836

1576
C
ILE
199
6.456
81.727
11.001

1577
O
ILE
199
5.422
81.545
11.660

1578
N
PHE
200
7.234
82.727
11.168

1579
CA
PHE
200
7.084
83.578
12.230

1580
CB
PHE
200
8.459
83.630
12.866

1581
CG
PHE
200
9.604
83.348
11.902

1582
CD1
PHE
200
10.400
84.395
11.482

1583
CD2
PHE
200
9.830
82.079
11.360

1584
CE1
PHE
200
11.394
84.220
10.540

1585
CE2
PHE
200
10.842
81.888
10.396

1586
CZ
PHE
200
11.621
82.969
9.989

1587
C
PHE
200
6.534
84.873
11.715

1588
O
PHE
200
6.814
85.256
10.577

1589
N
ASP
201
5.740
85.535
12.552

1590
CA
ASP
201
5.155
86.767
12.139

1591
CB
ASP
201
3.892
87.051
12.951

1592
CG
ASP
201
2.858
87.774
12.141

1593
OD1
ASP
201
2.902
87.651
10.902

1594
OD2
ASP
201
2.010
88.465
12.737

1595
C
ASP
201
6.087
87.950
12.118

1596
O
ASP
201
6.272
88.541
11.054

1597
N
PRO
202
6.687
88.326
13.264

1598
CD
PRO
202
6.585
87.855
14.653

1599
CA
PRO
202
7.577
89.491
13.127

1600
CB
PRO
202
7.868
89.922
14.573

1601
CG
PRO
202
7.024
89.062
15.456

1602
C
PRO
202
8.890
89.293
12.335

1603
O
PRO
202
9.194
88.217
11.844

1604
N
SER
203
9.650
90.380
12.225

1605
CA
SER
203
10.953
90.378
11.527

1606
CB
SER
203
10.734
90.705
10.057

1607
OG
SER
203
11.645
90.034
9.214

1608
C
SER
203
11.923
91.387
12.150

1609
O
SER
203
11.472
92.453
12.608

1610
OT
SER
203
13.127
91.080
12.183

1611
C1
NAG
337
−9.469
33.186
42.953

1612
C2
NAG
337
−8.576
34.420
43.270

1613
N2
NAG
337
−7.690
34.719
42.148

1614
C7
NAG
337
−6.368
34.889
42.274

1615
O7
NAG
337
−5.755
34.788
43.335

1616
C8
NAG
337
−5.619
35.210
40.989

1617
C3
NAG
337
−7.800
34.291
44.601

1618
O3
NAG
337
−7.298
35.563
44.985

1619
C4
NAG
337
−8.703
33.767
45.709

1620
O4
NAG
337
−7.958
33.573
46.905

1621
C5
NAG
337
−9.300
32.455
45.239

1622
O5
NAG
337
−10.171
32.702
44.114

1623
C6
NAG
337
−10.115
31.763
46.313

1624
O6
NAG
337
−9.595
30.471
46.594

1625
C1
NAG
355
−4.287
13.449
24.968

1626
C2
NAG
355
−4.296
14.880
24.417

1627
N2
NAG
355
−5.400
15.604
25.013

1628
C7
NAG
355
−5.298
16.912
25.215

1629
O7
NAG
355
−4.280
17.541
24.943

1630
C8
NAG
355
−6.507
17.605
25.825

1631
C3
NAG
355
−4.464
14.904
22.887

1632
O3
NAG
355
−4.235
16.218
22.400

1633
C4
NAG
355
−3.494
13.925
22.223

1634
O4
NAG
355
−3.669
13.927
20.814

1635
C5
NAG
355
−3.783
12.549
22.796

1636
O5
NAG
355
−3.459
12.560
24.196

1637
C6
NAG
355
−2.985
11.426
22.155

1638
O6
NAG
355
−3.099
10.223
22.904

1639
C1
NAG
370
6.875
20.681
28.445

1640
C2
NAG
370
8.262
21.265
28.392

1641
N2
NAG
370
8.681
21.759
29.689

1642
C7
NAG
370
9.976
21.812
29.982

1643
O7
NAG
370
10.850
21.497
29.175

1644
C8
NAG
370
10.344
22.309
31.367

1645
C3
NAG
370
8.191
22.354
27.338

1646
O3
NAG
370
9.470
22.953
27.184

1647
C4
NAG
370
7.718
21.741
25.991

1648
O4
NAG
370
7.191
22.783
25.156

1649
C5
NAG
370
6.617
20.651
26.078

1650
O5
NAG
370
6.692
19.853
27.296

1651
C6
NAG
370
6.739
19.703
24.903

1652
O6
NAG
370
6.222
20.290
23.714

1653
C1
NAG
371
7.907
23.026
24.005

1654
C2
NAG
371
7.150
23.963
23.089

1655
N2
NAG
371
5.717
23.735
22.982

1656
C7
NAG
371
5.172
22.761
22.258

1657
O7
NAG
371
5.822
21.934
21.619

1658
C8
NAG
371
3.646
22.729
22.275

1659
C3
NAG
371
7.904
23.921
21.782

1660
O3
NAG
371
7.174
24.587
20.756

1661
C4
NAG
371
9.179
24.679
22.101

1662
O4
NAG
371
10.034
24.722
20.972

1663
C5
NAG
371
9.963
24.103
23.299

1664
O5
NAG
371
9.119
23.677
24.394

1665
C6
NAG
371
10.846
25.160
23.903

1666
O6
NAG
371
11.950
25.428
23.072

1667
C1
MAN
372
10.464
25.992
20.679

1668
C2
MAN
372
12.019
26.016
20.807

1669
O2
MAN
372
12.611
24.881
20.198

1670
C3
MAN
372
12.612
27.284
20.168

1671
O3
MAN
372
14.023
27.153
20.050

1672
C4
MAN
372
12.025
27.564
18.780

1673
O4
MAN
372
12.409
28.867
18.345

1674
C5
MAN
372
10.503
27.484
18.806

1675
O5
MAN
372
10.091
26.245
19.350

1676
C6
MAN
372
9.983
27.420
17.396

1677
O6
MAN
372
10.129
26.089
16.855

1678
C1
NAG
419
−3.760
78.706
7.779

1679
C2
NAG
419
−4.885
78.830
6.751

1680
N2
NAG
419
−4.899
77.687
5.857

1681
C7
NAG
419
−5.923
76.838
5.874

1682
O7
NAG
419
−6.881
76.962
6.636

1683
C8
NAG
419
−5.855
75.676
4.897

1684
C3
NAG
419
−4.660
80.124
5.960

1685
O3
NAG
419
−5.734
80.323
5.049

1686
C4
NAG
419
−4.554
81.334
6.909

1687
O4
NAG
419
−4.151
82.483
6.172

1688
C5
NAG
419
−3.546
81.075
8.051

1689
O5
NAG
419
−3.815
79.806
8.695

1690
C6
NAG
419
−3.619
82.140
9.131

1691
O6
NAG
419
−2.839
83.275
8.790

[0141]

10

TABLE 7

Coordinate set of the CC′ loop of D1 of murine CEACAM1a

(partial sequence of #5, corresponding to amino acid

positions 35 through 45 (atoms positions 26 through 343)

ANum
AType
RType
RNum
X
Y
Z

264
N
LYS
35
−9.666
26.313
34.082

265
CA
LYS
35
−9.714
27.692
33.635

266
CB
LYS
35
−10.484
27.750
32.307

267
CG
LYS
35
−10.801
29.140
31.738

268
CD
LYS
35
−11.408
29.009
30.325

269
CE
LYS
35
−11.841
30.347
29.722

270
NZ
LYS
35
−12.528
30.158
28.405

271
C
LYS
35
−10.412
28.539
34.692

272
O
LYS
35
−11.465
28.161
35.194

273
N
GLY
36
−9.800
29.656
35.067

274
CA
GLY
36
−10.439
30.553
36.013

275
C
GLY
36
−10.360
30.443
37.525

276
O
GLY
36
−11.214
31.020
38.198

277
N
ASN
37
−9.385
29.730
38.082

278
CA
ASN
37
−9.277
29.656
39.544

279
GB
ASN
37
−9.365
31.100
40.114

280
CG
ASN
37
−9.477
31.164
41.641

281
OD1
ASN
37
−10.210
30.393
42.258

282
ND2
ASN
37
−8.770
32.120
42.251

283
C
ASN
37
−10.311
28.710
40.190

284
O
ASN
37
−10.123
28.267
41.322

285
N
THR
38
−11.391
28.380
39.484

286
CA
THR
38
−12.386
27.470
40.055

287
CB
THR
38
−13.700
27.427
39.235

288
OG1
THR
38
−13.450
27.862
37.895

289
CG2
THR
38
−14.762
28.307
39.873

290
C
THR
38
−11.839
26.046
40.086

291
O
THR
38
−11.673
25.421
39.040

292
N
THR
39
−11.557
25.536
41.282

293
CA
THR
39
−11.052
24.170
41.439

294
CB
THR
39
−10.387
23.980
42.832

295
OG1
THR
39
−10.417
22.598
43.203

296
CG2
THR
39
−11.115
24.796
43.891

297
C
THR
39
−12.252
23.233
41.305

298
O
THR
39
−12.347
22.204
41.970

299
N
ALA
40
−13.164
23.603
40.413

300
CA
ALA
40
−14.382
22.841
40.199

301
CB
ALA
40
−15.580
23.771
40.320

302
C
ALA
40
−14.476
22.058
38.895

344
C
ILE
45
−9.194
19.372
30.284

345
O
ILE
45
−9.182
18.856
29.167

303
O
ALA
40
−14.212
22.578
37.809

304
N
ILE
41
−14.885
20.799
39.027

305
CA
ILE
41
−15.070
19.895
37.898

306
GB
ILE
41
−15.826
18.634
38.337

307
CG2
ILE
41
−15.263
17.415
37.631

308
CG1
ILE
41
−15.727
18.477
39.856

309
CD1
ILE
41
−17.058
18.210
40.531

310
C
ILE
41
−15.897
20.607
36.837

311
O
ILE
41
−15.950
20.193
35.677

312
N
ASP
42
−16.558
21.675
37.268

313
CA
ASP
42
−17.380
22.496
36.401

314
CB
ASP
42
−17.748
23.795
37.127

315
CG
ASP
42
−18.993
24.455
36.566

316
OD1
ASP
42
−18.907
25.110
35.506

317
OD2
ASP
42
−20.064
24.324
37.194

318
C
ASP
42
−16.540
22.825
35.182

319
O
ASP
42
−17.032
22.831
34.053

320
N
LYS
43
−15.257
23.071
35.430

321
CA
LYS
43
−14.335
23.446
34.372

322
CB
LYS
43
−13.943
24.914
34.554

323
CG
LYS
43
−15.024
25.780
35.195

324
CD
LYS
43
−15.987
26.329
34.143

325
CE
LYS
43
−16.654
27.625
34.597

326
NZ
LYS
43
−17.005
28.511
33.447

327
C
LYS
43
−13.066
22.607
34.257

328
O
LYS
43
−11.965
23.130
34.423

329
N
GLU
44
−13.205
21.319
33.959

330
CA
GLU
44
−12.030
20.466
33.812

331
CB
GLU
44
−12.250
19.092
34.441

332
CG
GLU
44
−11.089
18.143
34.173

333
CD
GLU
44
−11.047
16.967
35.126

334
OE1
GLU
44
−10.883
17.186
36.346

335
OE2
GLU
44
−11.174
15.819
34.648

336
C
GLU
44
−11.701
20.275
32.347

337
O
GLU
44
−12.521
19.755
31.591

338
N
ILE
45
−10.501
20.688
31.949

339
CA
ILE
45
−10.088
20.545
30.562

340
CB
ILE
45
−9.347
21.766
30.035

341
CG2
ILE
45
−9.435
21.761
28.517

342
CG1
ILE
45
−9.902
23.040
30.678

343
CD1
ILE
45
−9.672
24.296
29.865

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	Number	Date	Country
Parent	10118471	Apr 2002	US
Child	10138176	May 2002	US

Carcinoembryonic antigen cell adhesion molecule 1 (CEACAM1) structure and uses thereof in drug identification and screening

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