Title of Invention: AAV CAPSID PROTEINS FOR NUCLEIC ACID TRANSFER Abstract: Recombinant adeno-associated viral (AAV) capsid proteins are provided. Methods for generating the recombinant adeno-associated viral capsid proteins and a library from which the capsids are selected are also provided. Detailed Description: CROSS REFERENCE TO RELATED APPLICATIONS This application is a continuation application of U.S. application Ser. No. 15/829,639, filed Dec. 1, 2017, now allowed; which is a divisional application of U.S. application Ser. No. 14/853,552, filed Sep. 14, 2015, now U.S. Pat. No. 9,856,469; which is a divisional application of U.S. application Ser. No. 13/594,773, filed Aug. 24, 2012, now U.S. Pat. No. 9,169,299; which claims priority under 35 U.S.C. § 119(e) to U.S. Provisional Application No. 61/526,688, filed Aug. 24, 2011 and to U.S. Provisional Application No. 61/545,488, filed Oct. 10, 2011, the entire contents of each is hereby incorporated by reference. STATEMENT REGARDING FEDERALLY SPONSORED RESEARCH This invention was made with Government support under contract HL092096 awarded by the National Institutes of Health. The Government has certain rights in this invention. REFERENCE TO SEQUENCE LISTING The present disclosure includes a sequence listing which is being submitted electronically in the form of a text file, created Apr. 22, 2021 and named “091511-0642_Sequence_Listing_1.txt” (263,014 bytes), the contents of which are incorporated herein by reference in their entirety. INTRODUCTION The subject matter described herein relates to in vitro and in vivo selection of sequences from a library of sequences encoding recombinant adeno-associated viral (AAV) viral capsid proteins and to methods of generating the libraries. The subject matter also relates to nucleotide sequences isolated from the libraries and to the AAV capsid proteins encoded by these sequences, and their usefulness as capsid proteins in recombinant AAV vectors for various nucleic acid transfer applications. The subject matter also relates to plasmids and viruses comprising the identified sequences, which preferably provide a high transduction efficiency and a low level of neutralization by the human immune system. BACKGROUND Multiple recombinant gene transfer vectors based on different types of viruses have been developed and tested in clinical trials in recent years. Gene transfer vectors based on adeno-associated virus (AAV), i.e., AAV vectors, have become favored vectors because of characteristics such as an ability to transduce different types of dividing and non-dividing cells of different tissues and the ability to establish stable, long-term transgene expression. While vectors based on other viruses, such as adenoviruses and retroviruses may possess certain desirable characteristics, the use of other vectors has been associated with toxicity or some human diseases. These side effects have not been detected with gene transfer vectors based on AAV (Manno et al., Nature Medicine, 12(3):342 (2006)). Additionally, the technology to produce and purify AAV vectors without undue effort has been developed. At least eleven AAV serotypes have been identified, cloned, sequenced, and converted into vectors, and at least 100 new AAV variants have been isolated from non-primates, primates and humans. However, the majority of preclinical data to date involving AAV vectors has been generated with vectors based on the human AAV-2 serotype, considered the AAV prototype. There are several disadvantages to the currently used AAV-2 vectors. For example, a number of clinically relevant cell types and tissues are not efficiently transduced with these vectors. Also, a large percentage of the human population is immune to AAV-2 due to prior exposure to wildtype AAV-2 virus. It has been estimated that up to 96% of humans are seropositive for AAV-2, and up to 67% of the seropositive individuals carry neutralizing anti-AAV-2 antibodies which could eliminate or greatly reduce transduction by AAV-2 vectors. Moreover, AAV-2 has been reported to cause a cell mediated immune response in patients when given systemically (Manno et al., Nature Medicine, 12(3):342 (2006)). Methods of overcoming the limitations of AAV-2 vectors have been proposed. For example, randomly mutagenizing the nucleotide sequence encoding the AAV-2 capsid by error-prone PCR has been proposed as a method of generating AAV-2 mutants that are able to escape the neutralizing antibodies that affect wildtype AAV-2. However, it is expected that it will be difficult to generate significantly improved AAV-2 variants with single random point mutations, as the naturally occurring serotypes have, at most, only about 85% homology in the capsid nucleotide sequence. Methods of using a mixture of AAV serotype constructs for AAV vectors have also been developed. The resulting chimeric vectors possess capsid proteins from different serotypes, and ideally, have properties of the different serotypes used. However, the ratio of the different capsid proteins is different from vector to vector and cannot be consistently controlled or reproduced (due to lack of genetic templates), which is unacceptable for clinical use and not satisfactory for experimental use. A third approach at modifying the AAV-2 capsid are peptide insertion libraries, in which randomized oligonucleotides encoding up to 7 amino acids are incorporated into a defined location within the AAV-2 capsid. The display of these peptides on the AAV-2 capsid surface can then be exploited to re-target the particles to cells or tissues that are otherwise refractory to infection with the wildtype AAV-2 virus. However, because knowledge of the atomic capsid structure is a prerequisite for this type of AAV modification, this method is generally restricted to AAV serotype 2. Moreover, peptide insertion libraries typically cannot address the issues of AAV particle immunogenicity or transduction efficiency. Thus, a need remains for new AAV vectors and a method of generating new AAV vectors. In particular, there is a need for AAV based vectors that can be used efficiently with a variety of cell types and tissues, and that do not react with a pre-existing anti-AAV human immunity that could neutralize or inactivate the vectors. Also needed are vectors that transduce different cell types in vivo and in vitro and that offer a more restricted biodistribution or a more promiscuous biodistribution, depending on the intended use. In particular, there remains a need for vectors capable of transducing a variety of cells types, such as hematopoietic stem cells or embryonic stem cells, as well as having desirable properties. A recombinant AAV vector known as “AAV-DJ” has been reported and described in U.S. patent application Ser. No. 12/538,791, published as US 20100047174, which is incorporated by reference herein, in its entirety. The foregoing examples of the related art and limitations related therewith are intended to be illustrative and not exclusive. Other limitations of the related art will become apparent to those of skill in the art upon a reading of the specification and a study of the drawings. BRIEF SUMMARY The following aspects and embodiments thereof described and illustrated below are meant to be exemplary and illustrative, not limiting in scope. In one aspect, recombinant capsid proteins and methods for generating recombinant capsid proteins are provided. The capsid proteins include regions or domains that are derived from different serotypes of AAV. The AAV serotypes may be human or non-human. Recombinant AAV comprising the capsid proteins and plasmids encoding the capsid proteins are also provided. In one aspect, a capsid protein comprises a first amino acid sequence similar or identical to a contiguous sequence of amino acids from a first AAV serotype, and a second amino acid sequence similar or identical to a contiguous sequence of amino acids from at least a second AAV serotype. In one embodiment, the capsid protein additionally comprises a sequence of amino acid residues similar or identical to a contiguous sequence of amino acids from a third AAV serotype. In another embodiment, the sequences of amino acids in the first sequence, in the second sequence, and in the third or further sequence, are each a contiguous sequence of amino acids from the first AAV serotype, the second AAV serotype, the third and/or further AAV serotypes. In another embodiment, the contiguous sequence of amino acids forms a conserved set of amino acid residues, the conserved set having at least about 70% sequence identity, at least about 75% sequence identity, at least about 80% sequence identity, at least about 85% sequence identity, at least about 90% sequence identity, at least about 95% sequence identity, at least about 96% sequence identity, at least about 97% sequence identity, at least about 98% sequence identity, or at least about 99% sequence identity with the AAV serotype from a contiguous sequence in its respective AAV serotype. In some aspects, a capsid protein is encoded by a nucleotide sequence selected from the group of sequences consisting of SEQ ID NOs: 1-28, or a sequence having at least 95% sequence identity thereto. In one embodiment, the capsid protein comprises an amino acid sequence encoded by the nucleotide sequence identified by SEQ ID NO: 1. In one embodiment, the capsid protein comprises an amino acid sequence encoded by the nucleotide sequence identified by SEQ ID NO: 2. In one embodiment, the capsid protein comprises an amino acid sequence encoded by the nucleotide sequence identified by SEQ ID NO: 3. In one embodiment, the capsid protein comprises an amino acid sequence encoded by the nucleotide sequence identified by SEQ ID NO: 4. In one embodiment, the capsid protein comprises an amino acid sequence encoded by the nucleotide sequence identified by SEQ ID NO: 5. In one embodiment, the capsid protein comprises an amino acid sequence encoded by the nucleotide sequence identified by SEQ ID NO: 6. In one embodiment, the capsid protein comprises an amino acid sequence encoded by the nucleotide sequence identified by SEQ ID NO: 7. In one embodiment, the capsid protein comprises an amino acid sequence encoded by the nucleotide sequence identified by SEQ ID NO: 8. In one embodiment, the capsid protein comprises an amino acid sequence encoded by the nucleotide sequence identified by SEQ ID NO: 9. In one embodiment, the capsid protein comprises an amino acid sequence encoded by the nucleotide sequence identified by SEQ ID NO: 10. In one embodiment, the capsid protein comprises an amino acid sequence encoded by the nucleotide sequence identified by SEQ ID NO: 11. In one embodiment, the capsid protein comprises an amino acid sequence encoded by the nucleotide sequence identified by SEQ ID NO: 12. In one embodiment, the capsid protein comprises an amino acid sequence encoded by the nucleotide sequence identified by SEQ ID NO: 13. In one embodiment, the capsid protein comprises an amino acid sequence encoded by the nucleotide sequence identified by SEQ ID NO: 14. In one embodiment, the capsid protein comprises an amino acid sequence encoded by the nucleotide sequence identified by SEQ ID NO: 15. In one embodiment, the capsid protein comprises an amino acid sequence encoded by the nucleotide sequence identified by SEQ ID NO: 16. In one embodiment, the capsid protein comprises an amino acid sequence encoded by the nucleotide sequence identified by SEQ ID NO: 17. In one embodiment, the capsid protein comprises an amino acid sequence encoded by the nucleotide sequence identified by SEQ ID NO: 18. In one embodiment, the capsid protein comprises an amino acid sequence encoded by the nucleotide sequence identified by SEQ ID NO: 19. In one embodiment, the capsid protein comprises an amino acid sequence encoded by the nucleotide sequence identified by SEQ ID NO: 20. In one embodiment, the capsid protein comprises an amino acid sequence encoded by the nucleotide sequence identified by SEQ ID NO: 21. In one embodiment, the capsid protein comprises an amino acid sequence encoded by the nucleotide sequence identified by SEQ ID NO: 22. In one embodiment, the capsid protein comprises an amino acid sequence encoded by the nucleotide sequence identified by SEQ ID NO: 23. In one embodiment, the capsid protein comprises an amino acid sequence encoded by the nucleotide sequence identified by SEQ ID NO: 24. In one embodiment, the capsid protein comprises an amino acid sequence encoded by the nucleotide sequence identified by SEQ ID NO: 25. In one embodiment, the capsid protein comprises an amino acid sequence encoded by the nucleotide sequence identified by SEQ ID NO: 26. In one embodiment, the capsid protein comprises an amino acid sequence encoded by the nucleotide sequence identified by SEQ ID NO: 27. In one embodiment, the capsid protein comprises an amino acid sequence encoded by the nucleotide sequence identified by SEQ ID NO: 28. A viral particle comprising a capsid protein sequence as described above, is contemplated in some embodiments. Disclosed herein is a genus of viral particles comprising the capsid proteins encoded by the nucleotide sequences identified by SEQ ID NOs: 1-28 of the sequence listing, or a sequence having at least 95% sequence identity to said sequences. Also disclosed is a plasmid comprising the nucleotide sequence selected from the group of sequences consisting of SEQ ID NOs: 1-28, or a sequence having at least 95% sequence identity thereto. Also disclosed is a recombinant AAV vector (rAAV), comprising a capsid protein having an amino acid sequence encoded by a nucleotide sequence selected from the group of sequences consisting of SEQ ID NOs: 1-28, or a sequence having at least 95% sequence identity thereto. In one aspect, a method of expressing a gene of interest in a mammal is provided. The present disclosure also provides a method of transfer of a nucleic acid of interest into a mammal, comprising introducing a recombinant AAV vector into a mammal, the recombinant AAV vector encoding a gene of interest which is encapsidated into a capsid protein encoded by a nucleotide sequence selected from the group of sequences consisting of SEQ ID NOs: 1-28, or a sequence having at least 95% sequence identity thereto. In still another aspect, a method of generating a library of recombinant AAV plasmids is disclosed, the method comprising: isolating AAV capsid nucleotide sequences from two or more serotypes of AAV; digesting the AAV capsid nucleotide sequences into fragments; reassembling the fragments using PCR to form PCR products; and cloning the re-assembled PCR products into plasmids to generate a library of recombinant AAV plasmids. The present disclosure also provides a method of generating a library of recombinant AAV plasmids, comprising (a) isolating AAV capsid nucleotide sequences from two or more serotypes of AAV; (b) digesting the AAV capsid nucleotide sequences into fragments; (c) reassembling the fragments using PCR to form PCR products; and (d) cloning the re-assembled PCR products into a wildtype viral genome to generate a library of recombinant AAV vectors (rAAVs). In another embodiment, the method comprises transfecting cells with the plasmids to produce a viral library, preferably an AAV viral library. In some aspects, the method further comprises (e) infecting cells in vitro with the rAAVs; (f) passaging the selected rAAVs in cells in vitro in the presence of a stringent condition and identifying an rAAV capsid that survives said passaging; and, optionally, (g) repeating (b) through (f) one or more times. In some aspects, the method further comprises (h) infecting a laboratory mammal in vivo with the selected rAAVs; (i) passaging the selected rAAVs in a laboratory mammal in vivo able to infect and propagate in said laboratory mammal and identifying an rAAV capsid that survives said passaging; and, optionally, (j) repeating (h) and (i) one or more times. Adenovirus has a broad host range, i.e., it can infect many human and other mammalian cell lines or primary cells, including replicative as well as non-replicative cells. Some lymphoid cell lines may be more resistant to Adenovirus infection, and thus may need high quantities of viruses to achieve sufficient infection levels. Cell types that may be used in the methods disclosed herein include, but are not limited to, CHO cells, monocytes, dendritic cells (DCs), freshly isolated human blood myeloid DCs, plasmacytoid DCs and monocyte-derived DCs, Langerhans cells and dermal DCs, Human T cell leukemia DND-41 cells, p53-deficient cancer cells, tumor cells retaining wild-type p53, tumor cells of unknown p53 status, adenocarcinomic human alveolar basal epithelial cells, also known as “A549 cells,” human KB cells, Madin Darby Bovine Kidney (MDBK) cells, Mouse Embryonic Fibroblasts (MEF cells), human pulmonary artery endothelial cells (hPAEC), NIH-3T3 cells, Huh-7.5 cells, Hep G2 cells, HEp-2 cells, HeLa cells, Dempsey cells, human embryonic kidney 293 cells (also known as “HEK 293” or “293 cells”), fetal rhesus monkey kidney (FRhK-4) cells, rat hepatoma H4TG cells, LMH chicken hepatoma epithelial cells, primary human hepatocytes and primary human keratinocytes. In some aspects, the rAAV is used to infect 293 cells. In some aspects, the rAAV is used to infect hPAEC cells. In some aspects, the rAAV is used to infect Huh-7.5 cells. In some embodiments a helper Adenovirus is used. In some embodiments, humanized FRG mice are transfected with an AAV in vitro selected library. In some embodiments, non-humanized FRG mice are transfected with an AAV in vitro selected library. In some embodiments, the method additionally includes, after the transfecting, passaging the viral library in a selected cell type in the presence of a stringent condition, and selecting AAV capsids that survive the passaging. Passaging can be for several or multiple passages, for example from between 2-5 or 2-10 passages. In some embodiments, the method additionally includes, after transfecting an animal model, passaging the AAV library through additional animal models, for subsequent selection of particular AAV isolates. In one embodiment, a stringent condition comprises the presence of human immune globulin. In another aspect, a library prepared according to the methods described above is disclosed. In one embodiment the library is comprised of plasmids of shuffled full-length capsid genes and in another embodiment the library is comprised of viral particles obtained by transfecting all or a portion of the plasmid library into a selected cell, optionally in combination with an adenoviral helper plasmid. The new, selected AAV capsid proteins described herein are useful for ex vivo or in vivo gene transfer, gene therapy, and genome editing applications, for example. A library prepared according to these methods is also provided. In addition to the exemplary aspects and embodiments described above, further aspects and embodiments will become apparent by reference to the drawings and by study of the following descriptions. BRIEF DESCRIPTION OF THE FIGURES FIG. 1 is a schematic showing a process for generating a recombinant AAV library; FIG. 2 is a flow chart summarizing a method of generating a library of AAV capsids using AAV shuffle library selection; FIG. 3 shows rounds 1 and 2 of AAV shuffle library selection in vitro; FIG. 4 shows rounds 2 and 3 of AAV shuffle library selection in vitro; FIG. 5 shows rounds 3 and 4 of AAV shuffle library selection in vitro; FIG. 6 compares the proportion of clones in the library to the proportion in each round of selection in vitro; FIG. 7 compares portions of several AAV serotypes and a recombinant AAV capsid protein in the library (AAV-PAEC); FIG. 8: compares amino acid substitutions in two rAAVs; FIG. 9: shows various views of a predicted 3-D structure of AAV-PAEC; FIG. 10: illustrates an experimental design of a process used to screen an AAV shuffle library in vivo; FIG. 11: illustrates an actual experiment used to screen an AAV shuffle library in vivo; FIG. 12: shows PCR amplified isolates from the AAV shuffle library screen in vivo; FIG. 13: compares the proportions of individual clones in the library to the proportion of individual clones in the selection from rounds 1 and 4 of in vivo; FIG. 14: shows amino acid substitutions in one selected rAAV (AAV-LK01); FIG. 15: shows various views of a predicted structure of AAV-LK01; FIG. 16: compares residues implicated in heparin binding in AAV-2 to residues in new rAAVs; FIG. 17: compares several AAV serotypes to several rAAV capsid proteins isolated using in vivo selection; FIG. 18: shows amino acid substitutions in one selected rAAV (AAV-LK02); FIG. 19: shows various views of a predicted structure of AAV-LK02; FIG. 20: shows amino acid substitutions in one selected rAAV (AAV-LK03); FIGS. 21 and 22: compare the relationship of selected rAAVs to wildtype AAVs on the DNA level and amino acid level, respectively; FIGS. 23A and 23B: show the Dot Blot titers of the rAAVs as compared to wildtype AAVs; FIGS. 24A and 24B: compare the transduction titers of the rAAVs to wildtype AAVs in Huh7.5 cells; FIGS. 25A, 25B and 25C: compare transduction efficiency per AAV vector genome (vg) of the rAAVs to wildtype AAVs in Huh7.5 cells; FIG. 26: compares transduction efficiency of rAAVs to wildtype AAVs in 293 cells; FIG. 27: compares transduction efficiency of rAAVs to wildtype AAVs in NIH3T3 cells; FIG. 28: compares transduction efficiency of selected rAAV isolates to wildtype AAVs in MEF cells; FIG. 29: shows the Dot Blot titers of certain rAAV isolates as compared to wildtype AAVs; FIG. 30: illustrates the neutralizing effects of hepatocyte growth factor on some AAVs and rAAV isolates. FIG. 31: shows the transduction efficiency of primary human hepatocytes by selected wildtype AAVs and rAAV isolates; FIG. 32: compares the expression levels of recombinant human factor IX (FIX) in immunocompetent C57/BL6 mice injected with various FIX-expressing AAVs; FIG. 33: compares the ability of selected rAAV isolates and wildtype AAVs to avoid neutralization by human immune globulin (IVIG); FIG. 34: compares transduction efficiency of certain rAAV isolates to wildtype AAVs in 293 cells; FIG. 35: compares transduction efficiency of certain rAAV isolates to wildtype AAVs in Huh 7.5 cells; FIG. 36: compares transduction efficiency of certain rAAV isolates to wildtype AAVs in PAEC cells; FIG. 37: compares transduction efficiency of certain rAAV isolates to wildtype AAVs in primary human keratinocytes; FIG. 38: compares transduction efficiency of certain rAAV isolates to wildtype AAVs in DND-41 cells; FIG. 39: compares transduction efficiency of particular rAAV isolates to wildtype AAVs in DND-41 cells; FIG. 40: compares transduction efficiency of certain rAAV isolates to wildtype AAVs in 3T3 cells; FIG. 41: compares transduction efficiency of certain rAAV isolates to wildtype AAVs in HeLa cells; FIG. 42: compares transduction efficiency of certain rAAV isolates to wildtype AAVs in MEF cells; FIG. 43: compares transduction efficiency of certain rAAV isolates to wildtype AAVs in H4TG cells; FIG. 44: compares transduction efficiency of certain rAAV isolates to wildtype AAVs in LMH cells; FIG. 45: compares transduction efficiency of certain rAAV isolates to wildtype AAVs in FRhK-4 cells; FIG. 46: compares the transduction of various cell lines by several wild type and recombinant AAV serotypes; FIG. 47: shows relatedness of wildtype AAVs to rAAVs isolates obtained by selection on human PAEC cells on the DNA level and amino acid level; and FIG. 48: shows the titer and transduction efficiency of rAAVs isolates obtained by selection on human PAEC cells as compared to wildtype AAVs. BRIEF DESCRIPTION OF THE SEQUENCES SEQ ID NO:1 is a nucleotide sequence encoding a novel recombinant AAV capsid protein, referred to herein as AAV-PAEC. SEQ ID NO:2 is a nucleotide sequence encoding a novel recombinant AAV capsid protein, referred to herein as AAV-LK01. SEQ ID NO:3 is a nucleotide sequence encoding a novel recombinant AAV capsid protein, referred to herein as AAV-LK02. SEQ ID NO:4 is a nucleotide sequence encoding a novel recombinant AAV capsid protein, referred to herein as AAV-LK03. SEQ ID NO:5 is a nucleotide sequence encoding a novel recombinant AAV capsid protein, referred to herein as AAV-LK04. SEQ ID NO:6 is a nucleotide sequence encoding a novel recombinant AAV capsid protein, referred to herein as AAV-LK05. SEQ ID NO:7 is a nucleotide sequence encoding a novel recombinant AAV capsid protein, referred to herein as AAV-LK06. SEQ ID NO:8 is a nucleotide sequence encoding a novel recombinant AAV capsid protein, referred to herein as AAV-LK07. SEQ ID NO:9 is a nucleotide sequence encoding a novel recombinant AAV capsid protein, referred to herein as AAV-LK08. SEQ ID NO:10 is a nucleotide sequence encoding a novel recombinant AAV capsid protein, referred to herein as AAV-LK09. SEQ ID NO:11 is a nucleotide sequence encoding a novel recombinant AAV capsid protein, referred to herein as AAV-LK10. SEQ ID NO:12 is a nucleotide sequence encoding a novel recombinant AAV capsid protein, referred to herein as AAV-LK11. SEQ ID NO:13 is a nucleotide sequence encoding a novel recombinant AAV capsid protein, referred to herein as AAV-LK12. SEQ ID NO:14 is a nucleotide sequence encoding a novel recombinant AAV capsid protein, referred to herein as AAV-LK13. SEQ ID NO:15 is a nucleotide sequence encoding a novel recombinant AAV capsid protein, referred to herein as AAV-LK14. SEQ ID NO:16 is a nucleotide sequence encoding a novel recombinant AAV capsid protein, referred to herein as AAV-LK15. SEQ ID NO:17 is a nucleotide sequence encoding a novel recombinant AAV capsid protein, referred to herein as AAV-LK16. SEQ ID NO:18 is a nucleotide sequence encoding a novel recombinant AAV capsid protein, referred to herein as AAV-LK17. SEQ ID NO:19 is a nucleotide sequence encoding a novel recombinant AAV capsid protein, referred to herein as AAV-LK18. SEQ ID NO:20 is a nucleotide sequence encoding a novel recombinant AAV capsid protein, referred to herein as AAV-LK19. SEQ ID NO:21 is a nucleotide sequence encoding a novel recombinant AAV capsid protein, referred to herein as AAV-PAEC2. SEQ ID NO:22 is a nucleotide sequence encoding a novel recombinant AAV capsid protein, referred to herein as AAV-PAEC4. SEQ ID NO:23 is a nucleotide sequence encoding a novel recombinant AAV capsid protein, referred to herein as AAV-PAEC6. SEQ ID NO:24 is a nucleotide sequence encoding a novel recombinant AAV capsid protein, referred to herein as AAV-PAEC7. SEQ ID NO:25 is a nucleotide sequence encoding a novel recombinant AAV capsid protein, referred to herein as AAV-PAEC8. SEQ ID NO:26 is a nucleotide sequence encoding a novel recombinant AAV capsid protein, referred to herein as AAV-PAEC11. SEQ ID NO:27 is a nucleotide sequence encoding a novel recombinant AAV capsid protein, referred to herein as AAV-PAEC12. SEQ ID NO:28 is a nucleotide sequence encoding a novel recombinant AAV capsid protein, referred to herein as AAV-PAEC13. SEQ ID NO:29 is an amino acid sequence encoded by SEQ ID NO: 2 (AAV-LK01). SEQ ID NO:30 is an amino acid sequence encoded by SEQ ID NO: 3 (AAV-LK02). SEQ ID NO:31 is an amino acid sequence encoded by SEQ ID NO: 4 (AAV-LK03). SEQ ID NO:32 is an amino acid sequence encoded by SEQ ID NO: 5 (AAV-LK04). SEQ ID NO:33 is an amino acid sequence encoded by SEQ ID NO: 6 (AAV-LK05). SEQ ID NO:34 is an amino acid sequence encoded by SEQ ID NO: 7 (AAV-LK06). SEQ ID NO:35 is an amino acid sequence encoded by SEQ ID NO: 8 (AAV-LK07). SEQ ID NO:36 is an amino acid sequence encoded by SEQ ID NO: 9 (AAV-LK08). SEQ ID NO:37 is an amino acid sequence encoded by SEQ ID NO: 10 (AAV-LK09). SEQ ID NO:38 is an amino acid sequence encoded by SEQ ID NO: 11 (AAV-LK10). SEQ ID NO:39 is an amino acid sequence encoded by SEQ ID NO: 12 (AAV-LK11). SEQ ID NO:40 is an amino acid sequence encoded by SEQ ID NO: 13 (AAV-LK12). SEQ ID NO:41 is an amino acid sequence encoded by SEQ ID NO: 14 (AAV-LK13). SEQ ID NO:42 is an amino acid sequence encoded by SEQ ID NO: 15 (AAV-LK14). SEQ ID NO:43 is an amino acid sequence encoded by SEQ ID NO: 16 (AAV-LK15). SEQ ID NO:44 is an amino acid sequence encoded by SEQ ID NO: 17 (AAV-LK16). SEQ ID NO:45 is an amino acid sequence encoded by SEQ ID NO: 18 (AAV-LK17). SEQ ID NO:46 is an amino acid sequence encoded by SEQ ID NO: 19 (AAV-LK18). SEQ ID NO:47 is an amino acid sequence encoded by SEQ ID NO: 20 (AAV-LK19). SEQ ID NO:48 is an amino acid sequence encoded by SEQ ID NO: 1 (PAEC). SEQ ID NO:49 is an amino acid sequence encoded by SEQ ID NO: 28 (PAEC-13). SEQ ID NO:50 is an amino acid sequence encoded by SEQ ID NO: 25 (PAEC-8). SEQ ID NO:51 is an amino acid sequence encoded by SEQ ID NO: 27 (PAEC-12). SEQ ID NO:52 is an amino acid sequence encoded by SEQ ID NO: 23 (PAEC-6). SEQ ID NO:53 is an amino acid sequence encoded by SEQ ID NO: 24 (PAEC-7). SEQ ID NO:54 is an amino acid sequence encoded by SEQ ID NO: 26 (PAEC-11). SEQ ID NO:55 is an amino acid sequence encoded by SEQ ID NO: 22 (PAEC-4). SEQ ID NO:56 is an amino acid sequence encoded by SEQ ID NO: 21 (PAEC-2). It is to be understood that each of the nucleotide sequences disclosed herein can be translated to predict an amino acid sequence representing a rAAV capsid protein. DETAILED DESCRIPTION Several embodiments of the present disclosure are described in detail hereinafter. These embodiments may take many different forms and should not be construed as limited to those embodiments explicitly set forth herein. Rather, these embodiments are provided so that this disclosure will be thorough and complete, and will fully convey the scope of the present disclosure to those skilled in the art. I. Definitions Where a range of values is provided, it is understood that each intervening value, to the tenth of the unit of the lower limit unless the context clearly dictates otherwise, between the upper and lower limits of that range is also specifically disclosed. Each smaller range between any stated value or intervening value in a stated range and any other stated or intervening value in that stated range is encompassed within the invention. The upper and lower limits of these smaller ranges may independently be included or excluded in the range, and each range where either, neither or both limits are included in the smaller ranges is also encompassed within the invention, subject to any specifically excluded limit in the stated range. Where the stated range includes one or both of the limits, ranges excluding either or both of those included limits are also included in the invention. Unless defined otherwise, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention belongs. Although any methods and materials similar or equivalent to those described herein can be used in the practice or testing of the present invention, some potential and preferred methods and materials are now described. It must be noted that as used herein and in the appended claims, the singular forms “a”, “an”, and “the” include plural referents unless the context clearly dictates otherwise. Thus, for example, reference to “a protein” includes more than one protein, and reference to “a compound” includes more than one compound. In describing and claiming the present invention, the following terminology will be used in accordance with the definitions set out below. A polynucleotide is typically composed of a specific sequence of four nucleotide bases: adenine (A); cytosine (C); guanine (G); and thymine (T) (uracil (U) for thymine (T) when the polynucleotide is RNA). Unless specifically delineated, the abbreviated nucleotides may be either ribonucleosides or 2′-deoxyribonucleosides. The nucleosides may be specified as being either ribonucleosides or 2′-deoxyribonucleosides on an individual basis or on an aggregate basis. When specified on an individual basis, the one-letter abbreviation is preceded by either a “d” or an “r,” where “d” indicates the nucleoside is a 2′-deoxyribonucleoside and “r” indicates the nucleoside is a ribonucleoside. For example, “dA” designates 2′-deoxyriboadenosine and “rA” designates riboadenosine. When specified on an aggregate basis, the particular nucleic acid or polynucleotide is identified as being either an RNA molecule or a DNA molecule. Nucleotides are abbreviated by adding a “p” to represent each phosphate, as well as whether the phosphates are attached to the 3′-position or the 5′-position of the sugar. Thus, 5′-nucleotides are abbreviated as “pN” and 3′-nucleotides are abbreviated as “Np,” where “N” represents A, G, C, T or U. When nucleic acid sequences are presented as a string of one-letter abbreviations, the sequences are presented in the 5′→3′ direction in accordance with common convention, and the phosphates are not indicated. Thus, the term polynucleotide sequence is the alphabetical representation of a polynucleotide molecule. This alphabetical representation can be input into databases in a computer having a central processing unit and used for bioinformatics applications such as functional genomics and homology searching. An “isolated polynucleotide” molecule is a nucleic acid molecule separate and discrete from the whole organism with which the molecule is found in nature; or a nucleic acid molecule devoid, in whole or part, of sequences normally associated with it in nature; or a sequence, as it exists in nature, but having heterologous sequences in association therewith. Techniques for determining nucleic acid and amino acid “sequence identity” also are known in the art. Typically, such techniques include determining the nucleotide sequence of the mRNA for a gene and/or determining the amino acid sequence encoded thereby, and comparing these sequences to a second nucleotide or amino acid sequence. In general, “identity” refers to an exact nucleotide-to-nucleotide or amino acid-to-amino acid correspondence of two polynucleotides or polypeptide sequences, respectively. Two or more sequences (polynucleotide or amino acid) can be compared by determining their “percent identity.” The percent identity of two sequences, whether nucleic acid or amino acid sequences, is the number of exact matches between two aligned sequences divided by the length of the shorter sequences and multiplied by 100. Percent identity may also be determined, for example, by comparing sequence information using the advanced BLAST computer program, including version 2.2.9, available from the National Institutes of Health. The BLAST program is based on the alignment method of Karlin and Altschul. Proc. Natl. Acad. Sci. USA 87:2264-2268 (1990) and as discussed in Altschul, et al., J. Mol. Biol. 215:403-410 (1990); Karlin And Altschul, Proc. Natl. Acad. Sci. USA 90:5873-5877 (1993); and Altschul et al., Nucleic Acids Res. 25:3389-3402 (1997). Briefly, the BLAST program defines identity as the number of identical aligned symbols (i.e., nucleotides or amino acids), divided by the total number of symbols in the shorter of the two sequences. The program may be used to determine percent identity over the entire length of the proteins being compared. Default parameters are provided to optimize searches with short query sequences in, for example, blastp with the program. The program also allows use of an SEG filter to mask-off segments of the query sequences as determined by the SEG program of Wootton and Federhen, Computers and Chemistry 17:149-163 (1993). Ranges of desired degrees of sequence identity are approximately 80% to 100% and integer values therebetween. Typically, the percent identities between a disclosed sequence and a claimed sequence are at least 80%, at least 85%, at least 90%, at least 95%, or at least 98%. Alternatively, the degree of sequence similarity between polynucleotides can be determined by hybridization of polynucleotides under conditions that form stable duplexes between homologous regions, followed by digestion with single-stranded-specific nuclease(s), and size determination of the digested fragments. Two DNA, or two polypeptide sequences are “substantially homologous” to each other when the sequences exhibit at least about 80-85%, preferably 85-90%, more preferably 90-95%, and most preferably 98-100% sequence identity to the reference sequence over a defined length of the molecules, as determined using the methods above. As used herein, substantially homologous also refers to sequences showing complete identity to the specified DNA or polypeptide sequence. DNA sequences that are substantially homologous can be identified in a Southern hybridization experiment under, for example, stringent conditions, as defined for that particular system. Defining appropriate hybridization conditions is within the skill of the art. In mammalian host cells, a number of viral based expression systems may be utilized. In cases where an adenovirus is used as an expression vector, a coding sequence may be ligated to an adenovirus transcription/translation control complex, e.g., the late promoter and tripartite leader sequence. This chimeric gene may then be inserted in the adenovirus genome by in vitro or in vivo recombination. Insertion in a non-essential region of the viral genome (e.g., region E1 or E3) will result in a recombinant virus that is viable and capable of expressing peptide in infected hosts. (e.g., see Logan & Shenk, 1984, Proc. Natl. Acad. Sci. USA 81:3655-3659). Alternatively, the vaccinia 7.5 K promoter may be used, (see, e.g., Mackett et al., 1982, Proc. Natl. Acad. Sci. USA 79:7415-7419; Mackett et al., 1984, J. Virol. 49:857-864; Panicali et al., 1982, Proc. Natl. Acad. Sci. USA 79:4927-4931). In the present disclosure, a recombinant AAV vector library is provided. While wild type AAVs (on which the library is based) can replicate in cells, the in vitro- and in vivo-selected isolates of the present disclosure are non-replicating and non-infectious. In other words, the viruses in the library contain only the Rep and Cap genes from wild type viruses, and do not contain any other reporter sequences such as GFP. After selection of the virus of interest according to the methods set forth herein, the recombinant Cap genes from the new isolates are cloned into plasmids for expressing the recombinant Cap proteins and packaging and production of non-replicating, non-infective vectors (a process also known as “vectorizing”). II. Chimeric AAV Capsid Capsid proteins with regions or domains or individual amino acids that are derived from two or more different serotypes of AAV are described herein. A capsid protein can have a first region that is derived from or having high levels of sequence similarity or identity to a first AAV serotype or known recombinant AAV capsid protein (e.g., AAV-DJ), a second region similarly derived from or having high levels of sequence similarity or identity to a second AAV serotype or known recombinant AAV capsid protein, as well as third, fourth, fifth, six, seventh and eighth regions, etc. derived from or having high levels of sequence similarity or identity to another AAV serotype or known recombinant AAV capsid protein. The AAV serotypes may be human AAV serotypes or non-human AAV serotypes, such as bovine, avian, and caprine AAV serotypes. In particular, non-primate mammalian AAV serotypes, such as AAV sequences from rodents (e.g., mice, rats, rabbits, and hamsters) and carnivores (e.g., dogs, cats, and raccoons), may be used. By including individual amino acids or regions from multiple AAV serotypes in one capsid protein, capsid proteins that have multiple desired properties that are separately derived from the multiple AAV serotypes may be obtained. In one embodiment, a capsid protein, referred to herein as “AAV-DJ”, that has an amino acid sequence comprising a first region that is derived from a first AAV serotype (AAV-2), a second region that is derived from a second AAV serotype (AAV-8), and a third region that is derived from a third AAV serotype (AAV-9), is provided. The AAV-DJ capsid protein was identified from a library of capsid proteins, using a method described below, as well as in U.S. patent application Ser. No. 12/538,791, published as US Patent Publication No. 20100047174, incorporated by reference herein, in its entirety. It will be appreciated that the AAV-DJ protein is merely exemplary of the beneficial capsid proteins that can be obtained from a library generated according to the teachings herein, where the beneficial capsid proteins preferably have multiple desired properties that are derived from multiple AAV serotypes. AAV-DJ has four mismatches to the two T cell epitopes in AAV-2 which have recently been identified as being involved in an anti-AAV cytotoxic T lymphocyte (CTL) response in humans. Thus, recombinant AAV vectors that include the AAV-DJ capsid protein or a derivative thereof are likely less immunogenic in humans than AAV-2 vectors that include the AAV-2 capsid. Studies were conducted to confirm that infectious viral particles can be formed with AAV-DJ as the capsid. In a first study, the AAV-DJ nucleotide sequence was inserted into an AAV helper plasmid that also expresses the AAV-2 rep gene. 293 kidney cells were then co-transfected with the AAV helper plasmid and an adenoviral helper plasmid, as well as a gfp-expressing vector plasmid. For comparison, two different versions of an AAV-2 helper were used (designated AAV-2 “old” and AAV-2 “new”) which differ in the expression levels of viral proteins. Three days after the co-transfection, Western blotting (with 303.9 (Rep) and B1 (capsid protein)) of the 293 cell extracts revealed the presence of presence of Rep and capsid proteins at levels comparable to those found in cells co-transfected with plasmids expressing the AAV-2, AAV-8, or AAV-9 capsid proteins. In another study, particle infectivity and ability to avoid neutralization by human immune globulin (IVIG) of AAV-DJ clone was compared to wildtypes AAV-2, AAV-8, and AAV-9. Two different versions of an AAV-2 helper were used (designated AAV-2 old and AAV-2 new) which differ in the expression levels of viral proteins. Recombinant AAVs with either the AAV-DJ, AAV-2, AAV-8, or AAV-9 capsids were produced by triple transfecting cells with a plasmid encoding gfp flanked by AAV inverted terminal repeats (ITRs), a plasmid encoding adenoviral helper genes, and a plasmid encoding the AAV-2 Rep gene and either the AAV-DJ, AAV-2, AAV-8, or AAV-9 capsid protein, and then freeze-thaw lysing the cells. Each virus-containing lysate was then neutralized using a high dose (1:1 volume) of two different batches of human immune globulin (IVIG1 and IVIG2) (293 cells); (Huh-7 cells)), or three decreasingly lower doses (1:2 (high), 1:10 (med), and 1:25 (low) antiserum/virus) of the two different batches of human immune globulin (IVIG1 and IVIG2), or a monoclonal A20 antibody (293 cells), or a polyclonal anti-AAV-8 serum (“A8”). A20 is a monoclonal antibody that was raised against assembled AAV-2 capsids and anti-AAV-8 is a polyclonal rabbit serum raised against assembled AAV-8 capsids. Lysates treated with PBS were used as a control. The virus-containing lysates were neutralized by incubating the lysates with the human immune globulin or antibody for a period of time (one hour at room temperature (20-25° C.)) and then infecting cells in the presence of helper adenovirus. The remaining activity of the viruses after the neutralization period was determined by titrating gfp expression units on the cells. In the absence of IVIG1, IVIG2, and A20, the AAV-DJ virus was at least as infectious on 293 cells as AAV-2 and several fold more infectious than AAV-2 on Huh-7 cells. It was demonstrated that the AAV-DJ virus and AAV-8 were able to partially escape neutralization by IVIG, while AAV-2 was not. AAV-9 had intermediate IVIG results relative to AAV-DJ/AAV-8 and AAV-2, and was neutralized at high IVIG doses. AAV-2 was neutralized by the A20 antibody, but the A20 antibody did not significantly affect AAV-DJ, AAV-8, or AAV-9. The polyclonal anti-AAV-8 antiserum neutralized all four capsids at high or medium doses, whereas AAV-2 and AAV-DJ partially escaped neutralization at the low dose. In summary, it was previously found that the AAV-DJ virus was more infectious to Huh-7 cells than the previously known most efficient AAV on Huh-7 cells (AAV-2), even in the presence of high concentrations of human immune globulin. Also, the AAV-DJ virus was found to have improved resistance to neutralization by human immune globulin relative to AAV-2. Such resistance is reasonable, given that the AAV-DJ capsid was selected from a library partially based on its ability to produce virus that resist neutralization by human immune globulin. However, the improved resistance of the AAV-DJ virus to the A20 antibody was surprising and unexpected, because (i) it was not part of the selection scheme described below that was used to isolate AAV-DJ; and (ii) AAV-DJ shares substantial identity to AAV-2, which is neutralized by the A20 antibody. In yet another study using human melanoma cell, in vitro infectivity of gfp-expressing vectors from the AAV-DJ capsid gene was compared to the in vitro infectivity of eight commonly used wildtype AAVs, AAV-1, AAV-2, AAV-3, AAV-4, AAV-5, AAV-6, AAV-8, or AAV-9. The melanoma cells were infected with 2×109 recombinant AAV particles of each serotype and gfp expression was visualized three days later. The results were quantitated, expressed as gfp expression in IU/mL, from virus titration on the melanoma cells (in 96-well plates) and the AAV-DJ vector was superior to the wildtype vectors, and, notably, substantially better than AAV-2. A number of cell lines were infected with ten-fold serial dilutions of each serotype, or AAV-DJ or the DJ heparin mutant DJ/8, discussed below, expressing a gfp reporter gene. Vector preparations were normalized to contain 2×109 total (vector DNA-containing) particles per mL prior to infection. Three days later, gfp-expressing cells were counted and infectious titers determined, taking into account the dilution factor. AAV-DJ vectors showed the highest infectivity on many cell lines, and ratios of total to infectious particles were frequently far below 500, highlighting the extreme efficiency of AAV-DJ in vitro, and suggesting its particular usefulness for ex vivo gene transfer applications. Vectors prepared with the AAV-DJ capsid were also tested in vivo for expression of a gene of interest. In a first study, recombinant human factor IX (FIX)-expressing AAVs with either the AAV-DJ, AAV-2, AAV-8, or AAV-9 capsids were produced by a triple transfection technique. Doses of 5×1010, 2×1011, and 1×1012 (low, medium, and high, respectively) recombinant viral particles were injected peripherally into immunocompetent mice (C57/BL6) and plasma hFIX was monitored for up to four months after injection. The FIX protein plasma levels were quantified by ELISA. FIX levels over 1% are considered therapeutic in hemophilics. The AAV-8,-9 or -DJ vectors exceeded the 100% level already at the lowest dose. A dose-dependent expression from the AAV-DJ capsid at levels equivalent to AAV-8 and -9, the two naturally identified AAVs reported in liver, was observed. The three viruses readily outperformed the AAV-2 prototype at any dose and expressed over 100% of normal hFIX levels from intravenous injection of 5×1010 particles, whereas AAV-2 expression was over 100% of normal hFIX levels only at a dose of 1×1012. In another study, recombinant human alpha-1-antitrypsin (hAAT)-expressing AAVs were prepared, from the AAV-DJ, AAV-2, AAV-8, or AAV-9 capsids. The hAAT gene was under an RSV promoter. Mice (C57/BL6) were injected via tail vein infusions of 2×1011 particles and plasma levels of hAAT were determined via specific ELISA 3, 7, and 14 days after injection. AAV-8, AAV-9, and AAV-DJ expressed efficiently and equally outperformed the vector with an AAV-2 capsid. In another in vivo study, liver transduction in the presence of human serum was quantified, to assess the ability of AAV-DJ to evade neutralization in vivo. Mice were passively immunized with 4 or 20 mg IVIG prior to infusion of hFIX-expressing AAV-2,-8,-9, or -DJ. Plasma hFIX levels for each AAV serotype were expressed as percent corresponding virus level in control mice treated with phosphate-buffered saline rather than IVIG as a function of time post infusion. AAV-2 expression was completely abolished, however transduction with AAV-DJ,-8 or -9 was inhibited in a dose-dependent manner, with AAV-DJ showing intermediate resistance at the high, and efficient evasion (similar to AAV-8 and AAV-9) at the low IVIG dose. These results were confirmed with a second independent IVIG batch from another vendor (Carimune 12%, Behring AG, data not shown). In another study, the feasibility to repeatedly administer the different viruses to mice was assessed, to evaluate capsid cross-neutralization. No gene expression upon re-infusion of any of the capsids into animals already treated with the same serotype was observed. However, AAV-8 and -9 also efficiently blocked each other, substantiating previous data (Gao, G. et al., J. Virol., 78:6381-6388 (2004)). This result might argue against the use of vectors based on these wildtypes in re-administration protocols, albeit they could be combined with AAV-2. In contrast, primary infusion of AAV-DJ allowed subsequent expression (up to 18%) from AAV-2,-8 or -9, likely due to the fact that AAV-DJ only shares a limited number of epitopes with each wildtype virus. In the reverse experiment, AAV-DJ vectors were inhibited in animals immunized with AAV-8 or -9, while giving detectable expression in AAV-2-treated mice. This implied a stronger or broader immune response from primary infusion of serotypes 8 or 9. AAV-DJ was more resistant to the corresponding mouse sera in culture. Less cross-reactivity between AAV-8 and -9 was noted. AAV-DJ, as well as other recombinant protein capsids identified in the library discussed below, retained a heparin binding domain (HBD) from the AAV-2 parent. This domain functions in binding to the primary AAV-2 receptor heparin sulfate proteoglycan (Summerford, C. et al., J. Virol., 72:1438-1445 (1998)). To investigate the role of the AAV-DJ HBD, two crucial arginine residues (Kern, A. et al., J. Virol., 77:11072-11081 (2003)) were mutated to the respective residues in AAV-8 or -9, and are referred to herein as AAV-DJ/8 and AAV-DJ/9. gfp expression was reduced by several orders of magnitude, and was as low as that observed with serotypes AAV-8 or AAV-9. The infectivity drop was shown to correlate with a reduced binding to cells. A titration of infectious particles on 293 kidney cells illustrated the role of the HBD for infection in culture, as seen by the reduction in infectivity in the HBD mutants AAV-DJ/8 and AAV-DJ/9. Additional mutants were prepared and tested, and are identified herein as AAV-2/8 (HBD negative), AAV-8/2 (HBD positive), and AAV-9/2 (HBD positive). Cell binding assays confirmed the role of the HBD for attachment to cultured cells, where the drop in binding with the mutants correlated with the transduction data. The HBD-positive AAV-8 and AAV-9 mutants bound several fold more efficiently than AAV-2 on HeLa cells but transduced less efficiently. Thus, cell attachment alone cannot explain the unusual infectivity of AAV-DJ. Instead, a synergistic effect from sharing beneficial properties from AAV-DJ parents is contemplated, resulting in enhancement of multiple steps in AAV-DJ transduction. The HBD also was shown to influence biodistribution,
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